UniProt_ID,UniProt_accession,Method,Kingdom,Length_aa,SwissProt_description,Prediction,judge_run1,judge_run2,judge_run3,judge_run4,judge_run5,judge_majority,reference_GO,extracted_GO_run1,extracted_GO_run2,extracted_GO_run3,extracted_GO_run4,extracted_GO_run5,wang_run1,wang_run2,wang_run3,wang_run4,wang_run5,n_nonempty_runs,wang_mean_nonempty,p_JAY,Retained
ENG1_RHIMI,A0A023I7E1,ESM2Text,Eukaryota,796,"Cleaves internal linkages in 1,3-beta-glucan.","Extracellular mannan synthase that plays an important role in cell wall degradation. Degrades a wide variety of substrates including aryl-beta-D-mannoside, carboxymethyl-beta-D-glucopyranoside, cellooligosaccharides, spore-forming spore amides and spore-forming spore-substituted cellooligosaccharides.",No,No,No,No,Maybe,not-Yes,GO:0052861; GO:0042973,GO:0004553,GO:0004553; GO:0015923,GO:0004567,GO:0004553,,0.7278,0.7042,0.5221,0.7278,,4,0.6705,0.3762,no
ENG1_RHIMI,A0A023I7E1,Prot2Text,Eukaryota,796,"Cleaves internal linkages in 1,3-beta-glucan.","Exo-alpha-L-arabinofuranosidase that specifically hydrolyzes the disaccharide cellobiose. Involved in the degradation of cellobiose. Hydrolyzes the disaccharide cellobiose and glucose. Cells may utilize cellobiose as a source of carbon, nitrogen and sulfur for growth.",No,No,No,No,No,not-Yes,GO:0052861; GO:0042973,GO:0004553,GO:0008422,GO:0004553,GO:0008422; GO:0046556,GO:0008422,0.7278,0.766,0.7278,0.7551,0.766,5,0.7485,0.3762,no
ENG1_RHIMI,A0A023I7E1,ProtT3,Eukaryota,796,"Cleaves internal linkages in 1,3-beta-glucan.",Secreted. Belongs to the glycosyl hydrolase 74 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0052861; GO:0042973,GO:0016798,GO:0016798,GO:0016798,GO:0004553,GO:0016798,0.626,0.626,0.626,0.7278,0.626,5,0.6464,0.3762,no
ENG1_RHIMI,A0A023I7E1,ProtTale,Eukaryota,796,"Cleaves internal linkages in 1,3-beta-glucan.","Cleaves internal bonds in 1,3-beta-D-glucosidic linkages in xyloglucan, a biopolymer found in the cell walls of plant cells, thereby releasing smaller oligosaccharides.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0052861; GO:0042973,GO:0042973,GO:0042973; GO:0004553,GO:0033940; GO:0004553,GO:0016162,GO:0033940; GO:0016798,0.8258,0.8769,0.682,0.6096,0.6056,5,0.72,0.3762,no
ENG1_RHIMI,A0A023I7E1,Protein2Text,Eukaryota,796,"Cleaves internal linkages in 1,3-beta-glucan.","The molecular function of this protein is not explicitly stated in the provided information. However, based on its name, it is likely that it is a beta-glucosidase, which is an enzyme that breaks down complex carbohydrates into simpler sugars. More specifically, it may be involved in the hydrolysis of complex glucosides, such as those found in plant cell walls, into glucose and other simple sugars.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0052861; GO:0042973,GO:0008422,GO:0008422,GO:0008422,GO:0008422,GO:0008422,0.766,0.766,0.766,0.766,0.766,5,0.766,0.3762,no
ENG1_RHIMI,A0A023I7E1,Reference,Eukaryota,796,"Cleaves internal linkages in 1,3-beta-glucan.","Cleaves internal linkages in 1,3-beta-glucan.",,,,,,,GO:0052861; GO:0042973,GO:0042973,GO:0042973,GO:0042973,GO:0042973,GO:0042973,0.8258,0.8258,0.8258,0.8258,0.8258,5,0.8258,0.3762,no
ARSI_BACX0,A0A059WI14,ESM2Text,Bacteria,161,"Nonheme iron-dependent dioxygenase that can break carbon- arsenic bonds, playing a role in the detoxification of environmental organoarsenical compounds. Catalyzes the oxygen-dependent demethylation of highly toxic methylarsonous acid (MAs(III)) to arsenite, which can then be exported out of the cell. Can also cleave the C-As bond in several trivalent aromatic arsenicals, including roxarsone (III), nitarsone (III) and (4-aminophenyl)arsonous acid. Organoarsenical degradation by this enzyme is proposed to have a significant impact on the arsenic biogeocycle that maintains a balance between organic and inorganic species.",Metallothioneins have a high content of cysteine residues that bind to FAD and coenzyme A.,No,No,No,No,No,not-Yes,GO:0051213; GO:0046872,,,,GO:0046872,,,,,0.7088,,1,0.7088,0.2874,no
ARSI_BACX0,A0A059WI14,Prot2Text,Bacteria,161,"Nonheme iron-dependent dioxygenase that can break carbon- arsenic bonds, playing a role in the detoxification of environmental organoarsenical compounds. Catalyzes the oxygen-dependent demethylation of highly toxic methylarsonous acid (MAs(III)) to arsenite, which can then be exported out of the cell. Can also cleave the C-As bond in several trivalent aromatic arsenicals, including roxarsone (III), nitarsone (III) and (4-aminophenyl)arsonous acid. Organoarsenical degradation by this enzyme is proposed to have a significant impact on the arsenic biogeocycle that maintains a balance between organic and inorganic species.",Metallothiol transferase which confers resistance to fosfomycin by catalyzing the addition of a thiol cofactor to fosfomycin. L-cysteine is probably the physiological thiol donor.,No,No,No,No,No,not-Yes,GO:0051213; GO:0046872,GO:0016740,,GO:0008728,GO:0016740,GO:0008906,0.3731,,0.2193,0.3731,0.196,4,0.2904,0.2874,no
ARSI_BACX0,A0A059WI14,ProtT3,Bacteria,161,"Nonheme iron-dependent dioxygenase that can break carbon- arsenic bonds, playing a role in the detoxification of environmental organoarsenical compounds. Catalyzes the oxygen-dependent demethylation of highly toxic methylarsonous acid (MAs(III)) to arsenite, which can then be exported out of the cell. Can also cleave the C-As bond in several trivalent aromatic arsenicals, including roxarsone (III), nitarsone (III) and (4-aminophenyl)arsonous acid. Organoarsenical degradation by this enzyme is proposed to have a significant impact on the arsenic biogeocycle that maintains a balance between organic and inorganic species.",To M.tuberculosis Rv1008c,Vague,Vague,Vague,Vague,No,not-Yes,GO:0051213; GO:0046872,,,,,,,,,,,0,,0.2874,no
ARSI_BACX0,A0A059WI14,ProtTale,Bacteria,161,"Nonheme iron-dependent dioxygenase that can break carbon- arsenic bonds, playing a role in the detoxification of environmental organoarsenical compounds. Catalyzes the oxygen-dependent demethylation of highly toxic methylarsonous acid (MAs(III)) to arsenite, which can then be exported out of the cell. Can also cleave the C-As bond in several trivalent aromatic arsenicals, including roxarsone (III), nitarsone (III) and (4-aminophenyl)arsonous acid. Organoarsenical degradation by this enzyme is proposed to have a significant impact on the arsenic biogeocycle that maintains a balance between organic and inorganic species.",Involved in the degradation of sulfonamides.,No,No,No,No,No,not-Yes,GO:0051213; GO:0046872,,,,,,,,,,,0,,0.2874,no
ARSI_BACX0,A0A059WI14,Protein2Text,Bacteria,161,"Nonheme iron-dependent dioxygenase that can break carbon- arsenic bonds, playing a role in the detoxification of environmental organoarsenical compounds. Catalyzes the oxygen-dependent demethylation of highly toxic methylarsonous acid (MAs(III)) to arsenite, which can then be exported out of the cell. Can also cleave the C-As bond in several trivalent aromatic arsenicals, including roxarsone (III), nitarsone (III) and (4-aminophenyl)arsonous acid. Organoarsenical degradation by this enzyme is proposed to have a significant impact on the arsenic biogeocycle that maintains a balance between organic and inorganic species.","The molecular function of this protein is unknown. However, it is likely involved in the detoxification of heavy metals, as it is a metallochaperone. Metallochaperones are proteins that bind to heavy metals and help to transport them within the cell, reducing their toxicity and facilitating their excretion. This protein is specifically involved in the transport of arsenic and other heavy metals, and is likely to play a role in protecting the cell from the toxic effects of these metals.",No,No,No,Vague,Maybe,not-Yes,GO:0051213; GO:0046872,,,,,GO:0046870,,,,,0.5476,1,0.5476,0.2874,no
ARSI_BACX0,A0A059WI14,Reference,Bacteria,161,"Nonheme iron-dependent dioxygenase that can break carbon- arsenic bonds, playing a role in the detoxification of environmental organoarsenical compounds. Catalyzes the oxygen-dependent demethylation of highly toxic methylarsonous acid (MAs(III)) to arsenite, which can then be exported out of the cell. Can also cleave the C-As bond in several trivalent aromatic arsenicals, including roxarsone (III), nitarsone (III) and (4-aminophenyl)arsonous acid. Organoarsenical degradation by this enzyme is proposed to have a significant impact on the arsenic biogeocycle that maintains a balance between organic and inorganic species.","Nonheme iron-dependent dioxygenase that can break carbon- arsenic bonds, playing a role in the detoxification of environmental organoarsenical compounds. Catalyzes the oxygen-dependent demethylation of highly toxic methylarsonous acid (MAs(III)) to arsenite, which can then be exported out of the cell. Can also cleave the C-As bond in several trivalent aromatic arsenicals, including roxarsone (III), nitarsone (III) and (4-aminophenyl)arsonous acid. Organoarsenical degradation by this enzyme is proposed to have a significant impact on the arsenic biogeocycle that maintains a balance between organic and inorganic species.",,,,,,,GO:0051213; GO:0046872,GO:0016702; GO:0046872,GO:0016702; GO:0046872,GO:0051213,GO:0051213,GO:0051213; GO:0005506,0.8735,0.8735,0.7088,0.7088,0.8854,5,0.81,0.2874,no
PGMA1_PHLG1,A0A0C3RR82,ESM2Text,Eukaryota,556,"Fusion protein of the methyltransferase pgiM1 and 12 type II borosin core peptides; part of the gene cluster that mediates the biosynthesis of a type II borosin, a highly methylated cyclic peptide with potent biological activities. Type II borosins derive from the C-terminus of the fusion protein, and it is the same protein that methylates its own C-terminus using S-adenosyl methionine (SAM). The C-terminus is subsequently cleaved off and macrocyclized by a prolyloligopeptidase to give the final product.","Impartic protease that probably acts as a co-chaperone, enhancing the proteolytic activity of the proteasome in the presence of abscisic acid, zinc or iron. May play a role in differentiation and proliferation of keratinocytes.",No,No,No,No,No,not-Yes,GO:0008168,GO:0008233,GO:0004190,,GO:0004190,,0.2915,0.1984,,0.1984,,3,0.2294,0.4122,no
PGMA1_PHLG1,A0A0C3RR82,Prot2Text,Eukaryota,556,"Fusion protein of the methyltransferase pgiM1 and 12 type II borosin core peptides; part of the gene cluster that mediates the biosynthesis of a type II borosin, a highly methylated cyclic peptide with potent biological activities. Type II borosins derive from the C-terminus of the fusion protein, and it is the same protein that methylates its own C-terminus using S-adenosyl methionine (SAM). The C-terminus is subsequently cleaved off and macrocyclized by a prolyloligopeptidase to give the final product.",Tubulin-folding protein; involved in the second step of the tubulin folding pathway.,No,No,No,No,No,not-Yes,GO:0008168,,,,GO:0005524,,,,,0.0633,,1,0.0633,0.4122,no
PGMA1_PHLG1,A0A0C3RR82,ProtT3,Eukaryota,556,"Fusion protein of the methyltransferase pgiM1 and 12 type II borosin core peptides; part of the gene cluster that mediates the biosynthesis of a type II borosin, a highly methylated cyclic peptide with potent biological activities. Type II borosins derive from the C-terminus of the fusion protein, and it is the same protein that methylates its own C-terminus using S-adenosyl methionine (SAM). The C-terminus is subsequently cleaved off and macrocyclized by a prolyloligopeptidase to give the final product.","Involved in the catabolism of methenyl-H(4)MPT (5-formyl- H(4)MPT). Catalyzes the conversion of 5-formyl-H(4)MPT to 5,10- methenyltetrahydromethanopterin. Belongs to the MCH family",No,No,No,No,No,not-Yes,GO:0008168,GO:0030269,GO:0018537,GO:0030272,GO:0018537,GO:0018537,0.4983,0.2742,0.2353,0.2742,0.2742,5,0.3112,0.4122,no
PGMA1_PHLG1,A0A0C3RR82,ProtTale,Eukaryota,556,"Fusion protein of the methyltransferase pgiM1 and 12 type II borosin core peptides; part of the gene cluster that mediates the biosynthesis of a type II borosin, a highly methylated cyclic peptide with potent biological activities. Type II borosins derive from the C-terminus of the fusion protein, and it is the same protein that methylates its own C-terminus using S-adenosyl methionine (SAM). The C-terminus is subsequently cleaved off and macrocyclized by a prolyloligopeptidase to give the final product.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS). SQS1 is composed of a 2,8- dioxobicyclo[6.1.0]nonan-9-ene (bicyclic diketone) core connected to a polyketide synthase (PKS) product. The SQS1 gene cluster is only required for the production of",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0008168,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.4122,no
PGMA1_PHLG1,A0A0C3RR82,Protein2Text,Eukaryota,556,"Fusion protein of the methyltransferase pgiM1 and 12 type II borosin core peptides; part of the gene cluster that mediates the biosynthesis of a type II borosin, a highly methylated cyclic peptide with potent biological activities. Type II borosins derive from the C-terminus of the fusion protein, and it is the same protein that methylates its own C-terminus using S-adenosyl methionine (SAM). The C-terminus is subsequently cleaved off and macrocyclized by a prolyloligopeptidase to give the final product.","The molecular function of this protein is not specified in the provided information. However, it is a prenyltransferase, which suggests that it may be involved in the transfer of a prenyl group to a protein or other molecule. Prenyltransferases are enzymes that catalyze the transfer of a prenyl group, such as farnesyl or geranylgeranyl, from a donor molecule to an acceptor molecule, typically a protein. This modification is important for the proper functioning of many proteins and is involved in a variety of cellular processes, including signal transduction, protein transport, and protein-protein interactions.",No,No,No,No,No,not-Yes,GO:0008168,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,0.4645,0.4645,0.4645,0.4645,0.4645,5,0.4645,0.4122,no
PGMA1_PHLG1,A0A0C3RR82,Reference,Eukaryota,556,"Fusion protein of the methyltransferase pgiM1 and 12 type II borosin core peptides; part of the gene cluster that mediates the biosynthesis of a type II borosin, a highly methylated cyclic peptide with potent biological activities. Type II borosins derive from the C-terminus of the fusion protein, and it is the same protein that methylates its own C-terminus using S-adenosyl methionine (SAM). The C-terminus is subsequently cleaved off and macrocyclized by a prolyloligopeptidase to give the final product.","Fusion protein of the methyltransferase pgiM1 and 12 type II borosin core peptides; part of the gene cluster that mediates the biosynthesis of a type II borosin, a highly methylated cyclic peptide with potent biological activities. Type II borosins derive from the C-terminus of the fusion protein, and it is the same protein that methylates its own C-terminus using S-adenosyl methionine (SAM). The C-terminus is subsequently cleaved off and macrocyclized by a prolyloligopeptidase to give the final product.",,,,,,,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168; GO:0008757,1.0,1.0,1.0,1.0,0.9527,5,0.9905,0.4122,no
DAO_UNKP,A0A0E3JXD9,ESM2Text,Bacteria,357,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.,"Catalyzes the oxidative demethylation of sarcosine to yield glycine, hydrogen peroxide and 5,10-methylenetetrahydrofolate.",No,No,No,Maybe,Maybe,not-Yes,GO:0003884,GO:0003884,GO:0003884,GO:0003884,GO:0003884,GO:0003884,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4036,no
DAO_UNKP,A0A0E3JXD9,Prot2Text,Bacteria,357,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.,Catalyzes the oxidative demethylation of sarcosine.,No,No,No,Maybe,Maybe,not-Yes,GO:0003884,GO:0003884,GO:0003884,GO:0033779,GO:0003884,GO:0003884,1.0,1.0,0.0,1.0,1.0,5,0.8,0.4036,no
DAO_UNKP,A0A0E3JXD9,ProtT3,Bacteria,357,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.,Belongs to the FAD-dependent oxidoreductase 2 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0003884,GO:0033734,GO:0033734,GO:0033734; GO:0016641,GO:0033734,GO:0003863,0.2943,0.2943,0.6007,0.2943,0.2943,5,0.3556,0.4036,no
DAO_UNKP,A0A0E3JXD9,ProtTale,Bacteria,357,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.,"Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac- AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.",No,No,No,No,No,not-Yes,GO:0003884,GO:0016407; GO:0005524,GO:0005524; GO:0016410,GO:0016407; GO:0005524,GO:0016407; GO:0005524,GO:0005524; GO:0140101,0.1323,0.1323,0.1323,0.1323,0.1543,5,0.1367,0.4036,no
DAO_UNKP,A0A0E3JXD9,Protein2Text,Bacteria,357,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.,This protein is an oxidoreductase.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0003884,GO:0016491,GO:0016491,,GO:0016491,GO:0016491,0.5381,0.5381,,0.5381,0.5381,4,0.5381,0.4036,no
DAO_UNKP,A0A0E3JXD9,Reference,Bacteria,357,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.,,,,,,,GO:0003884,GO:0003884,GO:0003884,GO:0003884,GO:0033971,GO:0033734,1.0,1.0,1.0,0.1737,0.2943,5,0.6936,0.4036,no
TACT3_SALT1,A0A0F6B5X4,ESM2Text,Bacteria,175,"Toxic component of a type II toxin-antitoxin (TA) system. Acetylates tRNA and inhibits translation. Acetylates only Gly-tRNA on all 3 Gly- tRNA(Gly) isoacceptors in situ. In vitro acetylates mainly Ile/Leu and Gly. Overexpression during the lag phase of a tacA3-tacT3 deletion strain leads to a 150-fold increase in persister cells in the presence of cefotaxime and a non-growth state in the absence of antibiotic. Persister cell formation and the growth defect are neutralized by cognate antitoxin TacA3, but not by TacA1 or TacA2. Plays a role in persister cell formation.","Controls the night/day rhythm of melatonin production. Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin.",No,No,No,No,No,not-Yes,GO:0016747; GO:0000049,GO:0004059; GO:0016407,GO:0004059,GO:0004062,GO:0004059,GO:0004059,0.6109,0.4404,0.3006,0.4404,0.4404,5,0.4465,0.3247,no
TACT3_SALT1,A0A0F6B5X4,Prot2Text,Bacteria,175,"Toxic component of a type II toxin-antitoxin (TA) system. Acetylates tRNA and inhibits translation. Acetylates only Gly-tRNA on all 3 Gly- tRNA(Gly) isoacceptors in situ. In vitro acetylates mainly Ile/Leu and Gly. Overexpression during the lag phase of a tacA3-tacT3 deletion strain leads to a 150-fold increase in persister cells in the presence of cefotaxime and a non-growth state in the absence of antibiotic. Persister cell formation and the growth defect are neutralized by cognate antitoxin TacA3, but not by TacA1 or TacA2. Plays a role in persister cell formation.",Detoxification of puromycin.,No,Vague,No,No,No,not-Yes,GO:0016747; GO:0000049,,,,,,,,,,,0,,0.3247,no
TACT3_SALT1,A0A0F6B5X4,ProtT3,Bacteria,175,"Toxic component of a type II toxin-antitoxin (TA) system. Acetylates tRNA and inhibits translation. Acetylates only Gly-tRNA on all 3 Gly- tRNA(Gly) isoacceptors in situ. In vitro acetylates mainly Ile/Leu and Gly. Overexpression during the lag phase of a tacA3-tacT3 deletion strain leads to a 150-fold increase in persister cells in the presence of cefotaxime and a non-growth state in the absence of antibiotic. Persister cell formation and the growth defect are neutralized by cognate antitoxin TacA3, but not by TacA1 or TacA2. Plays a role in persister cell formation.",Belongs to the acyltransferase 3 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016747; GO:0000049,GO:0016747,GO:0016747,GO:0016746,GO:0016747,GO:0016747,0.7073,0.7073,0.6097,0.7073,0.7073,5,0.6878,0.3247,no
TACT3_SALT1,A0A0F6B5X4,ProtTale,Bacteria,175,"Toxic component of a type II toxin-antitoxin (TA) system. Acetylates tRNA and inhibits translation. Acetylates only Gly-tRNA on all 3 Gly- tRNA(Gly) isoacceptors in situ. In vitro acetylates mainly Ile/Leu and Gly. Overexpression during the lag phase of a tacA3-tacT3 deletion strain leads to a 150-fold increase in persister cells in the presence of cefotaxime and a non-growth state in the absence of antibiotic. Persister cell formation and the growth defect are neutralized by cognate antitoxin TacA3, but not by TacA1 or TacA2. Plays a role in persister cell formation.",Toxic component of a type II toxin-antitoxin (TA) system. Acts as a DNA-dependent endonuclease.,No,No,No,No,Maybe,not-Yes,GO:0016747; GO:0000049,GO:0004519,GO:0004519,GO:0004520,GO:0004519,GO:0004520,0.2234,0.2234,0.1592,0.2234,0.1592,5,0.1977,0.3247,no
TACT3_SALT1,A0A0F6B5X4,Protein2Text,Bacteria,175,"Toxic component of a type II toxin-antitoxin (TA) system. Acetylates tRNA and inhibits translation. Acetylates only Gly-tRNA on all 3 Gly- tRNA(Gly) isoacceptors in situ. In vitro acetylates mainly Ile/Leu and Gly. Overexpression during the lag phase of a tacA3-tacT3 deletion strain leads to a 150-fold increase in persister cells in the presence of cefotaxime and a non-growth state in the absence of antibiotic. Persister cell formation and the growth defect are neutralized by cognate antitoxin TacA3, but not by TacA1 or TacA2. Plays a role in persister cell formation.","The molecular function of this protein is not explicitly stated in the provided information. However, based on its name and the context in which it is mentioned, it is likely that this protein is involved in a process related to DNA or RNA, possibly as a methyltransferase or a topoisomerase. Further research would be necessary to determine its specific molecular function.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0016747; GO:0000049,,,,,,,,,,,0,,0.3247,no
TACT3_SALT1,A0A0F6B5X4,Reference,Bacteria,175,"Toxic component of a type II toxin-antitoxin (TA) system. Acetylates tRNA and inhibits translation. Acetylates only Gly-tRNA on all 3 Gly- tRNA(Gly) isoacceptors in situ. In vitro acetylates mainly Ile/Leu and Gly. Overexpression during the lag phase of a tacA3-tacT3 deletion strain leads to a 150-fold increase in persister cells in the presence of cefotaxime and a non-growth state in the absence of antibiotic. Persister cell formation and the growth defect are neutralized by cognate antitoxin TacA3, but not by TacA1 or TacA2. Plays a role in persister cell formation.","Toxic component of a type II toxin-antitoxin (TA) system. Acetylates tRNA and inhibits translation. Acetylates only Gly-tRNA on all 3 Gly- tRNA(Gly) isoacceptors in situ. In vitro acetylates mainly Ile/Leu and Gly. Overexpression during the lag phase of a tacA3-tacT3 deletion strain leads to a 150-fold increase in persister cells in the presence of cefotaxime and a non-growth state in the absence of antibiotic. Persister cell formation and the growth defect are neutralized by cognate antitoxin TacA3, but not by TacA1 or TacA2. Plays a role in persister cell formation.",,,,,,,GO:0016747; GO:0000049,GO:0016746,GO:0016746,GO:0016746,GO:0016407,GO:0016407,0.6097,0.6097,0.6097,0.607,0.607,5,0.6086,0.3247,no
NAMPT_XANC8,A0A0H2X5R2,ESM2Text,Bacteria,468,"Catalyzes the condensation of nicotinamide with 5- phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. Plays an important role in the biosynthesis of NAD via the nicotinamide (NAM) salvage pathway. Is also capable of hydrolyzing ATP and shows ATP-dependent autophosphorylation activity.","Catalyzes the formation of N(5)-acetylcytidine (ac(5)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(5)C34.",No,No,No,No,No,not-Yes,GO:0047280,GO:0016407; GO:0005524,GO:0016407; GO:0005524,GO:0016407,GO:0016407,GO:0008080,0.2443,0.2443,0.3386,0.3386,0.2664,5,0.2864,0.3296,no
NAMPT_XANC8,A0A0H2X5R2,Prot2Text,Bacteria,468,"Catalyzes the condensation of nicotinamide with 5- phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. Plays an important role in the biosynthesis of NAD via the nicotinamide (NAM) salvage pathway. Is also capable of hydrolyzing ATP and shows ATP-dependent autophosphorylation activity.",Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP.,Maybe,Maybe,Maybe,Yes,Maybe,not-Yes,GO:0047280,GO:0004516,GO:0004516,GO:0004516,GO:0004516,GO:0004516,0.2353,0.2353,0.2353,0.2353,0.2353,5,0.2353,0.3296,no
NAMPT_XANC8,A0A0H2X5R2,ProtT3,Bacteria,468,"Catalyzes the condensation of nicotinamide with 5- phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. Plays an important role in the biosynthesis of NAD via the nicotinamide (NAM) salvage pathway. Is also capable of hydrolyzing ATP and shows ATP-dependent autophosphorylation activity.","Catalyzes the synthesis of NAD from nicotinic acid, ATP and 5-phosphoribose 1- diphosphate. Belongs to the NAPRTase family",Maybe,Maybe,Maybe,Yes,Yes,not-Yes,GO:0047280,GO:0004516,GO:0004516,GO:0004516; GO:0005524,GO:0004516,GO:0004516,0.2353,0.2353,0.1754,0.2353,0.2353,5,0.2233,0.3296,no
NAMPT_XANC8,A0A0H2X5R2,ProtTale,Bacteria,468,"Catalyzes the condensation of nicotinamide with 5- phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. Plays an important role in the biosynthesis of NAD via the nicotinamide (NAM) salvage pathway. Is also capable of hydrolyzing ATP and shows ATP-dependent autophosphorylation activity.",Catalyzes the NADPH-dependent reduction of 5-hydroxyuridine (ho5U) to 5-hydroxy- 2'-deoxyuridine (ho28U) at position 34 in tRNAs.,No,No,No,No,No,not-Yes,GO:0047280,GO:0016491,GO:0016491,GO:0016491; GO:0050661,GO:0016491,GO:0016491; GO:0050661,0.3552,0.3552,0.2603,0.3552,0.2603,5,0.3172,0.3296,no
NAMPT_XANC8,A0A0H2X5R2,Protein2Text,Bacteria,468,"Catalyzes the condensation of nicotinamide with 5- phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. Plays an important role in the biosynthesis of NAD via the nicotinamide (NAM) salvage pathway. Is also capable of hydrolyzing ATP and shows ATP-dependent autophosphorylation activity.","This protein is a part of the biosynthesis of NAD+, a crucial molecule for energy metabolism. More specifically, it is involved in the biosynthesis of NAD+ from nicotinamide mononucleotide (NMN) and ATP.",No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0047280,GO:0004515,GO:0004515,,GO:0004515,GO:0004515,0.2943,0.2943,,0.2943,0.2943,4,0.2943,0.3296,no
NAMPT_XANC8,A0A0H2X5R2,Reference,Bacteria,468,"Catalyzes the condensation of nicotinamide with 5- phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. Plays an important role in the biosynthesis of NAD via the nicotinamide (NAM) salvage pathway. Is also capable of hydrolyzing ATP and shows ATP-dependent autophosphorylation activity.","Catalyzes the condensation of nicotinamide with 5- phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. Plays an important role in the biosynthesis of NAD via the nicotinamide (NAM) salvage pathway. Is also capable of hydrolyzing ATP and shows ATP-dependent autophosphorylation activity.",,,,,,,GO:0047280,GO:0047280; GO:0016887; GO:0005524,GO:0047280; GO:0016887; GO:0005524,GO:0047280; GO:0016887,GO:0047280; GO:0016887; GO:0005524,GO:0047280; GO:0005524; GO:0016301,0.5563,0.5563,0.7232,0.5563,0.6135,5,0.6011,0.3296,no
HMPK_ACIB6,A0A0J9X285,ESM2Text,Bacteria,255,"Catalyzes the phosphorylation of hydroxymethylpyrimidine (HMP) to hydroxymethylpyrimidine phosphate (HMP-P). Unlike other HMPKs, it cannot catalyze the phosphorylation of HMP-P to generate the diphosphate HMP-PP. Shows no activity with pyridoxal, pyridoxamine or pyridoxine. Does not show phosphatase activity.","Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0008902; GO:0008972,GO:0016301,GO:0008902; GO:0008972,GO:0008972,GO:0008972,GO:0008972,0.5939,0.8105,0.6629,0.6629,0.6629,5,0.6786,0.3517,no
HMPK_ACIB6,A0A0J9X285,Prot2Text,Bacteria,255,"Catalyzes the phosphorylation of hydroxymethylpyrimidine (HMP) to hydroxymethylpyrimidine phosphate (HMP-P). Unlike other HMPKs, it cannot catalyze the phosphorylation of HMP-P to generate the diphosphate HMP-PP. Shows no activity with pyridoxal, pyridoxamine or pyridoxine. Does not show phosphatase activity.","Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0008902; GO:0008972,GO:0008972,GO:0008972,GO:0008972,GO:0008972,GO:0008972,0.6629,0.6629,0.6629,0.6629,0.6629,5,0.6629,0.3517,no
HMPK_ACIB6,A0A0J9X285,ProtT3,Bacteria,255,"Catalyzes the phosphorylation of hydroxymethylpyrimidine (HMP) to hydroxymethylpyrimidine phosphate (HMP-P). Unlike other HMPKs, it cannot catalyze the phosphorylation of HMP-P to generate the diphosphate HMP-PP. Shows no activity with pyridoxal, pyridoxamine or pyridoxine. Does not show phosphatase activity.","Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. Belongs to the ThiD family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0008902; GO:0008972,GO:0008972,GO:0008902,GO:0008902; GO:0005524,GO:0008972; GO:0008902,GO:0008902,0.6629,0.6629,0.9198,0.8105,0.6629,5,0.7438,0.3517,no
HMPK_ACIB6,A0A0J9X285,ProtTale,Bacteria,255,"Catalyzes the phosphorylation of hydroxymethylpyrimidine (HMP) to hydroxymethylpyrimidine phosphate (HMP-P). Unlike other HMPKs, it cannot catalyze the phosphorylation of HMP-P to generate the diphosphate HMP-PP. Shows no activity with pyridoxal, pyridoxamine or pyridoxine. Does not show phosphatase activity.","Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0008902; GO:0008972,GO:0008972; GO:0005524,GO:0008972; GO:0005524,GO:0008972; GO:0005524,GO:0008972; GO:0005524,GO:0008972; GO:0016301,0.9198,0.9198,0.9198,0.9198,0.7209,5,0.88,0.3517,no
HMPK_ACIB6,A0A0J9X285,Protein2Text,Bacteria,255,"Catalyzes the phosphorylation of hydroxymethylpyrimidine (HMP) to hydroxymethylpyrimidine phosphate (HMP-P). Unlike other HMPKs, it cannot catalyze the phosphorylation of HMP-P to generate the diphosphate HMP-PP. Shows no activity with pyridoxal, pyridoxamine or pyridoxine. Does not show phosphatase activity.","The molecular function of this protein is a transferase, specifically a kinase. It is involved in the transfer of a phosphate group to a molecule. In the case of the protein identified as a potential target for a specific compound, it is likely involved in the phosphorylation of a nucleotide, specifically a purine or pyrimidine base, as part of the purine salvage pathway.",Maybe,Vague,Vague,Maybe,Maybe,not-Yes,GO:0005524; GO:0008902; GO:0008972,GO:0016301,GO:0016301,,GO:0016301,GO:0016301,0.5939,0.5939,,0.5939,0.5939,4,0.5939,0.3517,no
HMPK_ACIB6,A0A0J9X285,Reference,Bacteria,255,"Catalyzes the phosphorylation of hydroxymethylpyrimidine (HMP) to hydroxymethylpyrimidine phosphate (HMP-P). Unlike other HMPKs, it cannot catalyze the phosphorylation of HMP-P to generate the diphosphate HMP-PP. Shows no activity with pyridoxal, pyridoxamine or pyridoxine. Does not show phosphatase activity.","Catalyzes the phosphorylation of hydroxymethylpyrimidine (HMP) to hydroxymethylpyrimidine phosphate (HMP-P). Unlike other HMPKs, it cannot catalyze the phosphorylation of HMP-P to generate the diphosphate HMP-PP. Shows no activity with pyridoxal, pyridoxamine or pyridoxine. Does not show phosphatase activity.",,,,,,,GO:0005524; GO:0008902; GO:0008972,GO:0008902,GO:0008902,GO:0008902,GO:0016301; GO:0005524,GO:0008902; GO:0005524,0.6629,0.6629,0.6629,0.8624,0.9198,5,0.7542,0.3517,no
AMDH_STRVG,A0A0L8M630,ESM2Text,Bacteria,360,"Catalyzes the reversible oxidative deaminations of a broad range of amines, amino alcohols and amino acids. Catalyzes the reversible dehydrogenation of serinol in the presence of NAD(+) to give dihydroxyacetone, ammonium ion and NADH, while NADP(+) shows a slight activity. Is also able to produce 2-amino-1-propanol and aspartate by the reductive amination of the corresponding keto alcohol (hydroxyacetone) and keto acid (oxaloacetate) in the presence of ammonium ions and NADH, and that of acetophenone from phenylethylamine by the oxidative deamination in the presence of NAD(+).","Catalyzes the NAD(P)(+)-dependent oxidative decarboxylation of D-erythritol to D-xylulose. Can also use the non-physiological substrate D-arabinose as substrate. Can use both NAD(+) and NADP(+) as electron acceptor, with a marked preference for NAD(+). Is involved in the anaerobic D-xylose utilization pathway.",No,Maybe,No,Maybe,No,not-Yes,GO:0008839,GO:0016616; GO:0051287,GO:0016491; GO:0070403; GO:0070404,GO:0016616,GO:0016614,GO:0016616,0.2892,0.3325,0.3987,0.482,0.3987,5,0.3802,0.1925,no
AMDH_STRVG,A0A0L8M630,Prot2Text,Bacteria,360,"Catalyzes the reversible oxidative deaminations of a broad range of amines, amino alcohols and amino acids. Catalyzes the reversible dehydrogenation of serinol in the presence of NAD(+) to give dihydroxyacetone, ammonium ion and NADH, while NADP(+) shows a slight activity. Is also able to produce 2-amino-1-propanol and aspartate by the reductive amination of the corresponding keto alcohol (hydroxyacetone) and keto acid (oxaloacetate) in the presence of ammonium ions and NADH, and that of acetophenone from phenylethylamine by the oxidative deamination in the presence of NAD(+).","Reduces the physiological low-potential two-electron acceptor coenzyme F420, and the artificial one-electron acceptor methylviologen.",No,No,No,No,No,not-Yes,GO:0008839,GO:0016491,GO:0043738,GO:0016491,GO:0016491,GO:0050454,0.6019,0.3987,0.6019,0.6019,0.3386,5,0.5086,0.1925,no
AMDH_STRVG,A0A0L8M630,ProtT3,Bacteria,360,"Catalyzes the reversible oxidative deaminations of a broad range of amines, amino alcohols and amino acids. Catalyzes the reversible dehydrogenation of serinol in the presence of NAD(+) to give dihydroxyacetone, ammonium ion and NADH, while NADP(+) shows a slight activity. Is also able to produce 2-amino-1-propanol and aspartate by the reductive amination of the corresponding keto alcohol (hydroxyacetone) and keto acid (oxaloacetate) in the presence of ammonium ions and NADH, and that of acetophenone from phenylethylamine by the oxidative deamination in the presence of NAD(+).",Catalyzes the conversion of N(5)-(2-aminoethyl)-L-ornithine to N(5)-(2-aminoethyl)-D-ornithine. Belongs to the N(5)-(2-aminoethyl)-L-ornithine N(6)-lyase family,No,No,No,No,No,not-Yes,GO:0008839,GO:0016853,GO:0016853,GO:0016853,GO:0016855,GO:0016855,0.3552,0.3552,0.3552,0.2353,0.2353,5,0.3072,0.1925,no
AMDH_STRVG,A0A0L8M630,ProtTale,Bacteria,360,"Catalyzes the reversible oxidative deaminations of a broad range of amines, amino alcohols and amino acids. Catalyzes the reversible dehydrogenation of serinol in the presence of NAD(+) to give dihydroxyacetone, ammonium ion and NADH, while NADP(+) shows a slight activity. Is also able to produce 2-amino-1-propanol and aspartate by the reductive amination of the corresponding keto alcohol (hydroxyacetone) and keto acid (oxaloacetate) in the presence of ammonium ions and NADH, and that of acetophenone from phenylethylamine by the oxidative deamination in the presence of NAD(+).","Catalyzes the NAD(+)-dependent oxidation of L-threonine to (R)-4-hydroxy-L,D-threonine. Involved in the degradation pathway of L-threonine to glycine, which allows E.coli to grow on L-threonine as the sole carbon source. Is also able to catalyze the reverse reaction.",No,No,No,No,No,not-Yes,GO:0008839,GO:0016616,GO:0016616,GO:0008743; GO:0051287,GO:0016491; GO:0003824,GO:0008743,0.3987,0.3987,0.2492,0.5553,0.3386,5,0.3881,0.1925,no
AMDH_STRVG,A0A0L8M630,Protein2Text,Bacteria,360,"Catalyzes the reversible oxidative deaminations of a broad range of amines, amino alcohols and amino acids. Catalyzes the reversible dehydrogenation of serinol in the presence of NAD(+) to give dihydroxyacetone, ammonium ion and NADH, while NADP(+) shows a slight activity. Is also able to produce 2-amino-1-propanol and aspartate by the reductive amination of the corresponding keto alcohol (hydroxyacetone) and keto acid (oxaloacetate) in the presence of ammonium ions and NADH, and that of acetophenone from phenylethylamine by the oxidative deamination in the presence of NAD(+).",The molecular function of this protein is an oxidoreductase.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008839,GO:0016491,GO:0016491,,GO:0016491,GO:0016491,0.6019,0.6019,,0.6019,0.6019,4,0.6019,0.1925,no
AMDH_STRVG,A0A0L8M630,Reference,Bacteria,360,"Catalyzes the reversible oxidative deaminations of a broad range of amines, amino alcohols and amino acids. Catalyzes the reversible dehydrogenation of serinol in the presence of NAD(+) to give dihydroxyacetone, ammonium ion and NADH, while NADP(+) shows a slight activity. Is also able to produce 2-amino-1-propanol and aspartate by the reductive amination of the corresponding keto alcohol (hydroxyacetone) and keto acid (oxaloacetate) in the presence of ammonium ions and NADH, and that of acetophenone from phenylethylamine by the oxidative deamination in the presence of NAD(+).","Catalyzes the reversible oxidative deaminations of a broad range of amines, amino alcohols and amino acids. Catalyzes the reversible dehydrogenation of serinol in the presence of NAD(+) to give dihydroxyacetone, ammonium ion and NADH, while NADP(+) shows a slight activity. Is also able to produce 2-amino-1-propanol and aspartate by the reductive amination of the corresponding keto alcohol (hydroxyacetone) and keto acid (oxaloacetate) in the presence of ammonium ions and NADH, and that of acetophenone from phenylethylamine by the oxidative deamination in the presence of NAD(+).",,,,,,,GO:0008839,GO:0016639; GO:0051287,GO:0016639; GO:0051287,GO:0016639,GO:0016639,GO:0016639,0.2892,0.2892,0.3987,0.3987,0.3987,5,0.3549,0.1925,no
GQQA_KOMEU,A0A0M0ELU2,ESM2Text,Bacteria,281,"Multifunctional enzyme that acts on N-acyl-homoserine lactones (AHLs), beta-lactam antibiotics and shows prephenate dehydratase activity. Acts as an acylase on AHL and hydrolyzes the amide bond of the acyl side-chain of AHL molecules, releasing homoserine lactone (HSL) and the fatty acid. Can use different 3-oxo-acyl homoserine lactones, such as 3-oxo-decanoyl homoserine lactone, which is the preferred substrate, 3-oxo-octanoyl homoserine lactone, 3-oxo-hexanoyl homoserine lactone and 3-oxo-dodecanoyl homoserine lactone. It can also degrade various beta-lactam antibiotics, including penicillin G, amoxicillin and ampicillin, but not cefotaxime. In addition, it can complement a phenylalanine auxotrophic E.coli mutant, which carries a kanamycin gene inserted into pheA, suggesting that GqqA can also function as a prephenate dehydratase. Involved in bacterial quorum quenching (QQ) and cellulose biofilm formation.",Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.,No,No,No,No,No,not-Yes,GO:0016787; GO:0004664,GO:0004399; GO:0051287,GO:0004399,GO:0004399,GO:0004399,GO:0004399,0.2592,0.3034,0.3034,0.3034,0.3034,5,0.2946,0.1549,no
GQQA_KOMEU,A0A0M0ELU2,Prot2Text,Bacteria,281,"Multifunctional enzyme that acts on N-acyl-homoserine lactones (AHLs), beta-lactam antibiotics and shows prephenate dehydratase activity. Acts as an acylase on AHL and hydrolyzes the amide bond of the acyl side-chain of AHL molecules, releasing homoserine lactone (HSL) and the fatty acid. Can use different 3-oxo-acyl homoserine lactones, such as 3-oxo-decanoyl homoserine lactone, which is the preferred substrate, 3-oxo-octanoyl homoserine lactone, 3-oxo-hexanoyl homoserine lactone and 3-oxo-dodecanoyl homoserine lactone. It can also degrade various beta-lactam antibiotics, including penicillin G, amoxicillin and ampicillin, but not cefotaxime. In addition, it can complement a phenylalanine auxotrophic E.coli mutant, which carries a kanamycin gene inserted into pheA, suggesting that GqqA can also function as a prephenate dehydratase. Involved in bacterial quorum quenching (QQ) and cellulose biofilm formation.",Catalyzes the conversion of 4-hydroxybenzoate (4-HB) to 2-oxo-4-hydroxybenzoate (2-oxo-4-HBA) in the aflatoxin biosynthesis pathway.,No,No,No,No,No,not-Yes,GO:0016787; GO:0004664,GO:0016491,,GO:0016491,GO:0016491,,0.5119,,0.5119,0.5119,,3,0.5119,0.1549,no
GQQA_KOMEU,A0A0M0ELU2,ProtT3,Bacteria,281,"Multifunctional enzyme that acts on N-acyl-homoserine lactones (AHLs), beta-lactam antibiotics and shows prephenate dehydratase activity. Acts as an acylase on AHL and hydrolyzes the amide bond of the acyl side-chain of AHL molecules, releasing homoserine lactone (HSL) and the fatty acid. Can use different 3-oxo-acyl homoserine lactones, such as 3-oxo-decanoyl homoserine lactone, which is the preferred substrate, 3-oxo-octanoyl homoserine lactone, 3-oxo-hexanoyl homoserine lactone and 3-oxo-dodecanoyl homoserine lactone. It can also degrade various beta-lactam antibiotics, including penicillin G, amoxicillin and ampicillin, but not cefotaxime. In addition, it can complement a phenylalanine auxotrophic E.coli mutant, which carries a kanamycin gene inserted into pheA, suggesting that GqqA can also function as a prephenate dehydratase. Involved in bacterial quorum quenching (QQ) and cellulose biofilm formation.",Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation of prephenate to phenylpyruvate. Cytoplasm. Belongs to the phenylpyruvate decarboxylase family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787; GO:0004664,GO:0004106; GO:0008738,GO:0004106; GO:0004664,GO:0004106; GO:0004664,GO:0004106; GO:0008738,GO:0004106; GO:0004664,0.377,0.7035,0.7035,0.377,0.7035,5,0.5729,0.1549,no
GQQA_KOMEU,A0A0M0ELU2,ProtTale,Bacteria,281,"Multifunctional enzyme that acts on N-acyl-homoserine lactones (AHLs), beta-lactam antibiotics and shows prephenate dehydratase activity. Acts as an acylase on AHL and hydrolyzes the amide bond of the acyl side-chain of AHL molecules, releasing homoserine lactone (HSL) and the fatty acid. Can use different 3-oxo-acyl homoserine lactones, such as 3-oxo-decanoyl homoserine lactone, which is the preferred substrate, 3-oxo-octanoyl homoserine lactone, 3-oxo-hexanoyl homoserine lactone and 3-oxo-dodecanoyl homoserine lactone. It can also degrade various beta-lactam antibiotics, including penicillin G, amoxicillin and ampicillin, but not cefotaxime. In addition, it can complement a phenylalanine auxotrophic E.coli mutant, which carries a kanamycin gene inserted into pheA, suggesting that GqqA can also function as a prephenate dehydratase. Involved in bacterial quorum quenching (QQ) and cellulose biofilm formation.",Catalyzes the condensation of isopentenyl diphosphate (IPP) with Mg-ATP to produce isoprenyl diphosphate (IPP).,No,No,No,No,No,not-Yes,GO:0016787; GO:0004664,GO:0016301,GO:0016740,,GO:0016740,,0.3498,0.5119,,0.5119,,3,0.4579,0.1549,no
GQQA_KOMEU,A0A0M0ELU2,Protein2Text,Bacteria,281,"Multifunctional enzyme that acts on N-acyl-homoserine lactones (AHLs), beta-lactam antibiotics and shows prephenate dehydratase activity. Acts as an acylase on AHL and hydrolyzes the amide bond of the acyl side-chain of AHL molecules, releasing homoserine lactone (HSL) and the fatty acid. Can use different 3-oxo-acyl homoserine lactones, such as 3-oxo-decanoyl homoserine lactone, which is the preferred substrate, 3-oxo-octanoyl homoserine lactone, 3-oxo-hexanoyl homoserine lactone and 3-oxo-dodecanoyl homoserine lactone. It can also degrade various beta-lactam antibiotics, including penicillin G, amoxicillin and ampicillin, but not cefotaxime. In addition, it can complement a phenylalanine auxotrophic E.coli mutant, which carries a kanamycin gene inserted into pheA, suggesting that GqqA can also function as a prephenate dehydratase. Involved in bacterial quorum quenching (QQ) and cellulose biofilm formation.","This protein is an enzyme, specifically a lyase, which catalyzes the D-amino acid decarboxylation reaction.",No,No,No,No,No,not-Yes,GO:0016787; GO:0004664,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.4043,0.4043,0.4043,0.4043,0.4043,5,0.4043,0.1549,no
GQQA_KOMEU,A0A0M0ELU2,Reference,Bacteria,281,"Multifunctional enzyme that acts on N-acyl-homoserine lactones (AHLs), beta-lactam antibiotics and shows prephenate dehydratase activity. Acts as an acylase on AHL and hydrolyzes the amide bond of the acyl side-chain of AHL molecules, releasing homoserine lactone (HSL) and the fatty acid. Can use different 3-oxo-acyl homoserine lactones, such as 3-oxo-decanoyl homoserine lactone, which is the preferred substrate, 3-oxo-octanoyl homoserine lactone, 3-oxo-hexanoyl homoserine lactone and 3-oxo-dodecanoyl homoserine lactone. It can also degrade various beta-lactam antibiotics, including penicillin G, amoxicillin and ampicillin, but not cefotaxime. In addition, it can complement a phenylalanine auxotrophic E.coli mutant, which carries a kanamycin gene inserted into pheA, suggesting that GqqA can also function as a prephenate dehydratase. Involved in bacterial quorum quenching (QQ) and cellulose biofilm formation.","Multifunctional enzyme that acts on N-acyl-homoserine lactones (AHLs), beta-lactam antibiotics and shows prephenate dehydratase activity. Acts as an acylase on AHL and hydrolyzes the amide bond of the acyl side-chain of AHL molecules, releasing homoserine lactone (HSL) and the fatty acid. Can use different 3-oxo-acyl homoserine lactones, such as 3-oxo-decanoyl homoserine lactone, which is the preferred substrate, 3-oxo-octanoyl homoserine lactone, 3-oxo-hexanoyl homoserine lactone and 3-oxo-dodecanoyl homoserine lactone. It can also degrade various beta-lactam antibiotics, including penicillin G, amoxicillin and ampicillin, but not cefotaxime. In addition, it can complement a phenylalanine auxotrophic E.coli mutant, which carries a kanamycin gene inserted into pheA, suggesting that GqqA can also function as a prephenate dehydratase. Involved in bacterial quorum quenching (QQ) and cellulose biofilm formation.",,,,,,,GO:0016787; GO:0004664,GO:0008800; GO:0004664,GO:0008800; GO:0004664,GO:0008800; GO:0004664,GO:0008800; GO:0004664; GO:0016811,GO:0008800; GO:0004664,0.801,0.801,0.801,0.7963,0.801,5,0.8001,0.1549,no
UBP48_DANRE,A0A0R4IB93,ESM2Text,Eukaryota,1047,Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins.,"Ubiquitin-protein ligase involved in the regulation of several biological processes including cell growth, differentiation, apoptosis, and DNA damage response. Mediates ubiquitination of CDC25C. Is an important regulator of the duration of cell proliferation by controlling the stability of CDKN1B. Functions in the ubiquitin-mediated proteasomal degradation of TFDP1.",No,No,No,No,Maybe,not-Yes,GO:0004843; GO:0004197,GO:0004842,GO:0004842,GO:0004842,GO:0004842,GO:0061630,0.2775,0.2775,0.2775,0.2775,0.2283,5,0.2677,0.6648,yes
UBP48_DANRE,A0A0R4IB93,Prot2Text,Eukaryota,1047,Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins.,Ubiquitin carboxylase (CC) that mediates deubiquitination of target proteins. Acts as an important regulator of autophagy by mediating deubiquitination of ATG8 family proteins (bacterionylation factor I and ubiquitin ligase). Deubiquitinates the glyceraldehyde-3-phosphate dehydrogenase GUT2 and regulates its activity. Probably acts as a regulator of autophagy by mediating deubiquitination of GUT2 inhibitor alpha-factor MYC. Also mediates deubiquitination of GUT2 inhibitor of beta-oxidation pathway.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004843; GO:0004197,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,0.8672,0.8672,0.8672,0.8672,0.8672,5,0.8672,0.6648,yes
UBP48_DANRE,A0A0R4IB93,ProtT3,Eukaryota,1047,Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins.,Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Nucleus. Belongs to the peptidase C19 family. USP18 subfamily,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004843; GO:0004197,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,0.8672,0.8672,0.8672,0.8672,0.8672,5,0.8672,0.6648,yes
UBP48_DANRE,A0A0R4IB93,ProtTale,Eukaryota,1047,Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins.,Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004843; GO:0004197,GO:0036459,GO:0036459; GO:0008233,GO:0101005,GO:0036459; GO:0008233,GO:0004843; GO:0008233,0.8672,0.8515,0.7187,0.8515,0.8515,5,0.8281,0.6648,yes
UBP48_DANRE,A0A0R4IB93,Protein2Text,Eukaryota,1047,Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins.,"This protein is a deubiquitinase, which means it is involved in the removal of ubiquitin from other proteins. Specifically, it is a ubiquitin-specific protease (USP) that plays a role in regulating protein stability and function by reversing ubiquitination, a process that marks proteins for degradation.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004843; GO:0004197,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,0.8672,0.8672,0.8672,0.8672,0.8672,5,0.8672,0.6648,yes
UBP48_DANRE,A0A0R4IB93,Reference,Eukaryota,1047,Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins.,Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins.,,,,,,,GO:0004843; GO:0004197,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0036459; GO:0004843,0.8672,0.8672,0.8672,0.8672,0.9004,5,0.8738,0.6648,yes
MCR2_ECOLX,A0A1C3NEV1,ESM2Text,Bacteria,538,Probably catalyzes the addition of a phosphoethanolamine moiety to lipid A. Phosphoethanolamine modification of lipid A confers polymyxin resistance. Confers resistance to polymyxin-type antibiotics such as colistin.,Controls the biosynthesis of the nonessential phospholipid phosphatidylcholine; it transfers the phospholipid to the position 2 of diacylglycerol (DAG) producing phosphatidylcholine (PtdCho).,No,No,No,No,Maybe,not-Yes,GO:0046872; GO:0016776,GO:0004142,GO:0004142,GO:0004142,GO:0004142,GO:0004142,0.3788,0.3788,0.3788,0.3788,0.3788,5,0.3788,0.3497,no
MCR2_ECOLX,A0A1C3NEV1,Prot2Text,Bacteria,538,Probably catalyzes the addition of a phosphoethanolamine moiety to lipid A. Phosphoethanolamine modification of lipid A confers polymyxin resistance. Confers resistance to polymyxin-type antibiotics such as colistin.,"Exoglucosyltransferase involved in glycosylation steps of the biosynthesis of phospholipids. Transfers a glucosyl group from UDP-Glc to the non-reducing end of the glucosyl moiety, forming a phosphoglycerolipid. Can also use diacylglycerol (DAG) as a sugar donor and the physiological acceptor of the diacylglycerol moiety; the physiological acceptor is unknown.",No,No,No,No,No,not-Yes,GO:0046872; GO:0016776,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0046527,0.4132,0.4132,0.4132,0.4132,0.2954,5,0.3896,0.3497,no
MCR2_ECOLX,A0A1C3NEV1,ProtT3,Bacteria,538,Probably catalyzes the addition of a phosphoethanolamine moiety to lipid A. Phosphoethanolamine modification of lipid A confers polymyxin resistance. Confers resistance to polymyxin-type antibiotics such as colistin.,Catalyzes the addition of a phosphoethanolamine moiety to lipid A. Cell inner membrane; Multi-pass membrane protein. Belongs to the phosphoethanolamine transferase family. LpxE subfamily,Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0016776,GO:0016772,GO:0016772,GO:0016780,GO:0016780,GO:0016740,0.6032,0.6032,0.5032,0.5032,0.5125,5,0.5451,0.3497,no
MCR2_ECOLX,A0A1C3NEV1,ProtTale,Bacteria,538,Probably catalyzes the addition of a phosphoethanolamine moiety to lipid A. Phosphoethanolamine modification of lipid A confers polymyxin resistance. Confers resistance to polymyxin-type antibiotics such as colistin.,Catalyzes the addition of a phosphoethanolamine moiety to the lipid A. The phosphoethanolamine modification is required for resistance to polymyxin.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0016776,GO:0016740,GO:0016740,GO:0016740,GO:0016740,GO:0016740,0.5125,0.5125,0.5125,0.5125,0.5125,5,0.5125,0.3497,no
MCR2_ECOLX,A0A1C3NEV1,Protein2Text,Bacteria,538,Probably catalyzes the addition of a phosphoethanolamine moiety to lipid A. Phosphoethanolamine modification of lipid A confers polymyxin resistance. Confers resistance to polymyxin-type antibiotics such as colistin.,"This protein is involved in the molecular function of lipid metabolism.

Specifically, it is a translocase enzyme that plays a role in the transport of lipids across the cell membrane.

More specifically, it is involved in the transfer of lipids from the inner membrane to the outer membrane, which is an important process for the maintenance of cellular homeostasis and the proper functioning of cellular processes.

It is also involved in the transfer of lipids to the outer membrane, which is important for the maintenance of membrane integrity and the proper functioning of cellular processes.

In addition, it is involved in the transfer of lipids to other cellular components, such as the cell wall and the extracellular matrix, which is important for the maintenance of cellular structure and function.

Overall, this protein plays a critical role in the maintenance of cellular homeostasis and the proper functioning of cellular processes, and its dysfunction has been implicated in various diseases, including atherosclerosis and Alzheimer's disease.

In the context of the provided text, this protein is involved in the transport of lipids, which is an important process for the maintenance of cellular homeostasis and the proper functioning of cellular processes. The protein is also involved in the transfer of lipids to the outer membrane, which is important for the maintenance of membrane integrity and the proper functioning of cellular processes. 

The exact function of this protein is to facilitate the transfer of lipids across the cell membrane, which is an important process for the maintenance of cellular homeostasis and the proper functioning of cellular processes. 

This protein is involved in the transfer of lipids from the inner membrane to the outer membrane, which is an important process for the maintenance of membrane integrity and the proper functioning of cellular processes. 

This protein is also involved in the transfer of lipids to other cellular components, such as the cell wall and the extracellular matrix, which is important for the maintenance of cellular structure and function. 

This protein plays a critical role in the maintenance of cellular homeostasis and the proper functioning of cellular processes, and its dysfunction has been implicated in various diseases, including atherosclerosis and Alzheimer's disease. 

In the context of the provided text, the protein is involved in the transport of lipids, which is an important process for the maintenance of cellular homeostasis and the proper functioning of cellular processes. 

The protein is involved in the transfer of lipids to the outer membrane, which is important for the maintenance of membrane integrity and the proper functioning of cellular processes. 

The protein is also involved in the transfer",No,Vague,Vague,Vague,Maybe,not-Yes,GO:0046872; GO:0016776,,,,,GO:0005548,,,,,0.1395,1,0.1395,0.3497,no
MCR2_ECOLX,A0A1C3NEV1,Reference,Bacteria,538,Probably catalyzes the addition of a phosphoethanolamine moiety to lipid A. Phosphoethanolamine modification of lipid A confers polymyxin resistance. Confers resistance to polymyxin-type antibiotics such as colistin.,Probably catalyzes the addition of a phosphoethanolamine moiety to lipid A. Phosphoethanolamine modification of lipid A confers polymyxin resistance. Confers resistance to polymyxin-type antibiotics such as colistin.,,,,,,,GO:0046872; GO:0016776,GO:0016740,GO:0016740,GO:0016740,GO:0016780,GO:0016740,0.5125,0.5125,0.5125,0.5032,0.5125,5,0.5106,0.3497,no
PIGK_MONRU,A0A1C8AX29,ESM2Text,Eukaryota,2014,"Fatty acid synthase subunit beta; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants. PigJ and pigK form the two subunits of a dedicated fungal fatty acid synthase (FAS) that produces the side chain fatty acyl moiety of MonAzPs, a beta-keto fatty acid. The chain length control of the pigJ-pigK FAS is somewhat flexible as MonAzPs features either a beta-ketooctanoic or a beta-ketodecanoic acid moiety. The beta-ketoacyl-ACP probably serves as the substrate for the acetyltransferase pigD that directly transfers the fatty acyl chain to the C-4 alcohol of the pyran ring. The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4-hydroxy-2- oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially involved in the biosynthesis of orange and red pigments via desaturation of C6(7).","Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0019171; GO:0004313; GO:0004314; GO:0004318; GO:0004312; GO:0016297; GO:0004321; GO:0031409,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.4893,0.4893,0.4893,0.4893,0.4893,5,0.4893,0.1585,no
PIGK_MONRU,A0A1C8AX29,Prot2Text,Eukaryota,2014,"Fatty acid synthase subunit beta; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants. PigJ and pigK form the two subunits of a dedicated fungal fatty acid synthase (FAS) that produces the side chain fatty acyl moiety of MonAzPs, a beta-keto fatty acid. The chain length control of the pigJ-pigK FAS is somewhat flexible as MonAzPs features either a beta-ketooctanoic or a beta-ketodecanoic acid moiety. The beta-ketoacyl-ACP probably serves as the substrate for the acetyltransferase pigD that directly transfers the fatty acyl chain to the C-4 alcohol of the pyran ring. The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4-hydroxy-2- oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially involved in the biosynthesis of orange and red pigments via desaturation of C6(7).","Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0019171; GO:0004313; GO:0004314; GO:0004318; GO:0004312; GO:0016297; GO:0004321; GO:0031409,GO:0004312; GO:0004314; GO:0004319; GO:0004317,GO:0004312,GO:0004312,GO:0004312; GO:0004314; GO:0004316; GO:0004317; GO:0004320,GO:0004312,0.5884,0.4893,0.4893,0.5727,0.4893,5,0.5258,0.1585,no
PIGK_MONRU,A0A1C8AX29,ProtT3,Eukaryota,2014,"Fatty acid synthase subunit beta; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants. PigJ and pigK form the two subunits of a dedicated fungal fatty acid synthase (FAS) that produces the side chain fatty acyl moiety of MonAzPs, a beta-keto fatty acid. The chain length control of the pigJ-pigK FAS is somewhat flexible as MonAzPs features either a beta-ketooctanoic or a beta-ketodecanoic acid moiety. The beta-ketoacyl-ACP probably serves as the substrate for the acetyltransferase pigD that directly transfers the fatty acyl chain to the C-4 alcohol of the pyran ring. The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4-hydroxy-2- oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially involved in the biosynthesis of orange and red pigments via desaturation of C6(7).",Involved in fatty acid metabolism. Peroxisome. Belongs to the enoyl-CoA hydratase/isomerase family,Maybe,No,Maybe,No,Maybe,not-Yes,GO:0019171; GO:0004313; GO:0004314; GO:0004318; GO:0004312; GO:0016297; GO:0004321; GO:0031409,GO:0004300,GO:0004300,GO:0004300,GO:0004300,GO:0004300,0.2942,0.2942,0.2942,0.2942,0.2942,5,0.2942,0.1585,no
PIGK_MONRU,A0A1C8AX29,ProtTale,Eukaryota,2014,"Fatty acid synthase subunit beta; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants. PigJ and pigK form the two subunits of a dedicated fungal fatty acid synthase (FAS) that produces the side chain fatty acyl moiety of MonAzPs, a beta-keto fatty acid. The chain length control of the pigJ-pigK FAS is somewhat flexible as MonAzPs features either a beta-ketooctanoic or a beta-ketodecanoic acid moiety. The beta-ketoacyl-ACP probably serves as the substrate for the acetyltransferase pigD that directly transfers the fatty acyl chain to the C-4 alcohol of the pyran ring. The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4-hydroxy-2- oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially involved in the biosynthesis of orange and red pigments via desaturation of C6(7).","Fatty acid synthase beta subunit; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS). SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms. These initial steps feature the priming of an unusual benzoic acid starter unit",Yes,Yes,Yes,Yes,Yes,Yes,GO:0019171; GO:0004313; GO:0004314; GO:0004318; GO:0004312; GO:0016297; GO:0004321; GO:0031409,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.4893,0.4893,0.4893,0.4893,0.4893,5,0.4893,0.1585,no
PIGK_MONRU,A0A1C8AX29,Protein2Text,Eukaryota,2014,"Fatty acid synthase subunit beta; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants. PigJ and pigK form the two subunits of a dedicated fungal fatty acid synthase (FAS) that produces the side chain fatty acyl moiety of MonAzPs, a beta-keto fatty acid. The chain length control of the pigJ-pigK FAS is somewhat flexible as MonAzPs features either a beta-ketooctanoic or a beta-ketodecanoic acid moiety. The beta-ketoacyl-ACP probably serves as the substrate for the acetyltransferase pigD that directly transfers the fatty acyl chain to the C-4 alcohol of the pyran ring. The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4-hydroxy-2- oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially involved in the biosynthesis of orange and red pigments via desaturation of C6(7).","The molecular function of this protein is not explicitly stated in the provided information. However, based on the fact that it is involved in a process related to cellular metabolism, it is likely that it plays a role in catalyzing a specific biochemical reaction. The protein is probably a type of enzyme, and its function would involve facilitating a chemical reaction that converts one molecule into another. If you have more information about the protein or its context, I may be able to provide a more specific answer.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0019171; GO:0004313; GO:0004314; GO:0004318; GO:0004312; GO:0016297; GO:0004321; GO:0031409,,,,,,,,,,,0,,0.1585,no
PIGK_MONRU,A0A1C8AX29,Reference,Eukaryota,2014,"Fatty acid synthase subunit beta; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants. PigJ and pigK form the two subunits of a dedicated fungal fatty acid synthase (FAS) that produces the side chain fatty acyl moiety of MonAzPs, a beta-keto fatty acid. The chain length control of the pigJ-pigK FAS is somewhat flexible as MonAzPs features either a beta-ketooctanoic or a beta-ketodecanoic acid moiety. The beta-ketoacyl-ACP probably serves as the substrate for the acetyltransferase pigD that directly transfers the fatty acyl chain to the C-4 alcohol of the pyran ring. The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4-hydroxy-2- oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially involved in the biosynthesis of orange and red pigments via desaturation of C6(7).","Fatty acid synthase subunit beta; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants. PigJ and pigK form the two subunits of a dedicated fungal fatty acid synthase (FAS) that produces the side chain fatty acyl moiety of MonAzPs, a beta-keto fatty acid. The chain length control of the pigJ-pigK FAS is somewhat flexible as MonAzPs features either a beta-ketooctanoic or a beta-ketodecanoic acid moiety. The beta-ketoacyl-ACP probably serves as the substrate for the acetyltransferase pigD that directly transfers the fatty acyl chain to the C-4 alcohol of the pyran ring. The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4-hydroxy-2- oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially involved in the biosynthesis of orange and red pigments via desaturation of C6(7).",,,,,,,GO:0019171; GO:0004313; GO:0004314; GO:0004318; GO:0004312; GO:0016297; GO:0004321; GO:0031409,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.4893,0.4893,0.4893,0.4893,0.4893,5,0.4893,0.1585,no
PIGJ_MONRU,A0A1D5AG16,ESM2Text,Eukaryota,1842,"Fatty acid synthase alpha subunit; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants. PigJ and pigK form the two subunits of a dedicated fungal fatty acid synthase (FAS) that produces the side chain fatty acyl moiety of MonAzPs, a beta-keto fatty acid. The chain length control of the pigJ-pigK FAS is somewhat flexible as MonAzPs features either a beta-ketooctanoic or a beta-ketodecanoic acid moiety. The beta-ketoacyl-ACP probably serves as the substrate for the acetyltransferase pigD that directly transfers the fatty acyl chain to the C-4 alcohol of the pyran ring. The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4-hydroxy-2- oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially involved in the biosynthesis of orange and red pigments via desaturation of C6(7).","Fatty acid synthase subunit alpha; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcsC",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004316; GO:0004315; GO:0004312; GO:0004321; GO:0008897; GO:0000287; GO:0031409,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.517,0.517,0.517,0.517,0.517,5,0.517,0.2132,no
PIGJ_MONRU,A0A1D5AG16,Prot2Text,Eukaryota,1842,"Fatty acid synthase alpha subunit; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants. PigJ and pigK form the two subunits of a dedicated fungal fatty acid synthase (FAS) that produces the side chain fatty acyl moiety of MonAzPs, a beta-keto fatty acid. The chain length control of the pigJ-pigK FAS is somewhat flexible as MonAzPs features either a beta-ketooctanoic or a beta-ketodecanoic acid moiety. The beta-ketoacyl-ACP probably serves as the substrate for the acetyltransferase pigD that directly transfers the fatty acyl chain to the C-4 alcohol of the pyran ring. The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4-hydroxy-2- oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially involved in the biosynthesis of orange and red pigments via desaturation of C6(7).","Fatty acid synthase alpha subunit; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004316; GO:0004315; GO:0004312; GO:0004321; GO:0008897; GO:0000287; GO:0031409,GO:0004312,GO:0004312,GO:0004312,GO:0004312; GO:0016874,GO:0004312,0.517,0.517,0.517,0.5368,0.517,5,0.521,0.2132,no
PIGJ_MONRU,A0A1D5AG16,ProtT3,Eukaryota,1842,"Fatty acid synthase alpha subunit; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants. PigJ and pigK form the two subunits of a dedicated fungal fatty acid synthase (FAS) that produces the side chain fatty acyl moiety of MonAzPs, a beta-keto fatty acid. The chain length control of the pigJ-pigK FAS is somewhat flexible as MonAzPs features either a beta-ketooctanoic or a beta-ketodecanoic acid moiety. The beta-ketoacyl-ACP probably serves as the substrate for the acetyltransferase pigD that directly transfers the fatty acyl chain to the C-4 alcohol of the pyran ring. The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4-hydroxy-2- oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially involved in the biosynthesis of orange and red pigments via desaturation of C6(7).",11-beta-hydroxysteroid reductase involved in the biosynthesis of brassinosteroids (BRs). Catalyzes the NADPH-dependent reduction of 11-deoxophytodienoic acid (11-DODA) to 11-deoxophytodienoic acid alcohol (11-DODA-OH) (By similarity). Endoplasmic reticulum. Belongs to the short-chain dehydrogenases/reductases (SDR) family,No,No,No,No,No,not-Yes,GO:0004316; GO:0004315; GO:0004312; GO:0004321; GO:0008897; GO:0000287; GO:0031409,GO:0016616,GO:0016229; GO:0016616,GO:0016491; GO:0050661,GO:0016229,GO:0016616,0.3627,0.4033,0.3754,0.2994,0.3627,5,0.3607,0.2132,no
PIGJ_MONRU,A0A1D5AG16,ProtTale,Eukaryota,1842,"Fatty acid synthase alpha subunit; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants. PigJ and pigK form the two subunits of a dedicated fungal fatty acid synthase (FAS) that produces the side chain fatty acyl moiety of MonAzPs, a beta-keto fatty acid. The chain length control of the pigJ-pigK FAS is somewhat flexible as MonAzPs features either a beta-ketooctanoic or a beta-ketodecanoic acid moiety. The beta-ketoacyl-ACP probably serves as the substrate for the acetyltransferase pigD that directly transfers the fatty acyl chain to the C-4 alcohol of the pyran ring. The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4-hydroxy-2- oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially involved in the biosynthesis of orange and red pigments via desaturation of C6(7).","Fatty acid synthase alpha subunit; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3- hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (A",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004316; GO:0004315; GO:0004312; GO:0004321; GO:0008897; GO:0000287; GO:0031409,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.517,0.517,0.517,0.517,0.517,5,0.517,0.2132,no
PIGJ_MONRU,A0A1D5AG16,Protein2Text,Eukaryota,1842,"Fatty acid synthase alpha subunit; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants. PigJ and pigK form the two subunits of a dedicated fungal fatty acid synthase (FAS) that produces the side chain fatty acyl moiety of MonAzPs, a beta-keto fatty acid. The chain length control of the pigJ-pigK FAS is somewhat flexible as MonAzPs features either a beta-ketooctanoic or a beta-ketodecanoic acid moiety. The beta-ketoacyl-ACP probably serves as the substrate for the acetyltransferase pigD that directly transfers the fatty acyl chain to the C-4 alcohol of the pyran ring. The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4-hydroxy-2- oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially involved in the biosynthesis of orange and red pigments via desaturation of C6(7).","This protein is a subunit of succinate dehydrogenase, which is a mitochondrial enzyme that catalyzes the conversion of succinate to fumarate during the citric acid cycle. This subunit is involved in the transfer of electrons from succinate to ubiquinone (coenzyme Q).",No,No,No,No,No,not-Yes,GO:0004316; GO:0004315; GO:0004312; GO:0004321; GO:0008897; GO:0000287; GO:0031409,GO:0016627,GO:0008177; GO:0016627,GO:0008177,GO:0008177,GO:0000104; GO:0016627,0.2994,0.3001,0.1898,0.1898,0.3105,5,0.2579,0.2132,no
PIGJ_MONRU,A0A1D5AG16,Reference,Eukaryota,1842,"Fatty acid synthase alpha subunit; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants. PigJ and pigK form the two subunits of a dedicated fungal fatty acid synthase (FAS) that produces the side chain fatty acyl moiety of MonAzPs, a beta-keto fatty acid. The chain length control of the pigJ-pigK FAS is somewhat flexible as MonAzPs features either a beta-ketooctanoic or a beta-ketodecanoic acid moiety. The beta-ketoacyl-ACP probably serves as the substrate for the acetyltransferase pigD that directly transfers the fatty acyl chain to the C-4 alcohol of the pyran ring. The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4-hydroxy-2- oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially involved in the biosynthesis of orange and red pigments via desaturation of C6(7).","Fatty acid synthase alpha subunit; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants. PigJ and pigK form the two subunits of a dedicated fungal fatty acid synthase (FAS) that produces the side chain fatty acyl moiety of MonAzPs, a beta-keto fatty acid. The chain length control of the pigJ-pigK FAS is somewhat flexible as MonAzPs features either a beta-ketooctanoic or a beta-ketodecanoic acid moiety. The beta-ketoacyl-ACP probably serves as the substrate for the acetyltransferase pigD that directly transfers the fatty acyl chain to the C-4 alcohol of the pyran ring. The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4-hydroxy-2- oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially involved in the biosynthesis of orange and red pigments via desaturation of C6(7).",,,,,,,GO:0004316; GO:0004315; GO:0004312; GO:0004321; GO:0008897; GO:0000287; GO:0031409,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.517,0.517,0.517,0.517,0.517,5,0.517,0.2132,no
VPS34_CANAL,A0A1D8PDV7,ESM2Text,Eukaryota,1020,"Multifunctional phosphatidylinositol 3-kinase involved in acidification of vacuoles, pH-dependent cell growth, and autophagocytosis. Plays an important role in protein transport and virulence. Component of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). Finally, it might also be involved in ethanol tolerance and cell wall integrity.",(Microbial infection) Phosphorylates the host serine/threonine protein kinase PAK1 on a specific serine residue to generate PAK1-phosphoinositide (PIP).,No,No,Maybe,No,No,not-Yes,GO:0016303; GO:0005524; GO:0004672,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.6048,0.6048,0.6048,0.6048,0.6048,5,0.6048,0.5434,yes
VPS34_CANAL,A0A1D8PDV7,Prot2Text,Eukaryota,1020,"Multifunctional phosphatidylinositol 3-kinase involved in acidification of vacuoles, pH-dependent cell growth, and autophagocytosis. Plays an important role in protein transport and virulence. Component of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). Finally, it might also be involved in ethanol tolerance and cell wall integrity.",(Microbial infection) Required for vacuolar sorting and polarized sorting of a subset of S.typhimurium-containing vacuolar proteins.,Vague,Vague,Vague,No,No,not-Yes,GO:0016303; GO:0005524; GO:0004672,,,,,,,,,,,0,,0.5434,yes
VPS34_CANAL,A0A1D8PDV7,ProtT3,Eukaryota,1020,"Multifunctional phosphatidylinositol 3-kinase involved in acidification of vacuoles, pH-dependent cell growth, and autophagocytosis. Plays an important role in protein transport and virulence. Component of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). Finally, it might also be involved in ethanol tolerance and cell wall integrity.","Catalytic subunit of the PI3K complex that mediates synthesis of phosphatidylinositol 3-phosphate (PtdIns(3)P) which is a precursor of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), two signaling lipids that regulate a variety of cellular processes. Belongs to the PI3/PI4-kinase family. Type III PI3K subfamily",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0016303; GO:0005524; GO:0004672,GO:0035004,GO:0016303,GO:0046934; GO:0005524,GO:0035004,GO:0052731,0.0,0.6633,0.8432,0.0,0.1352,5,0.3283,0.5434,yes
VPS34_CANAL,A0A1D8PDV7,ProtTale,Eukaryota,1020,"Multifunctional phosphatidylinositol 3-kinase involved in acidification of vacuoles, pH-dependent cell growth, and autophagocytosis. Plays an important role in protein transport and virulence. Component of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). Finally, it might also be involved in ethanol tolerance and cell wall integrity.","Phosphatidylinositol 3-phosphate kinase that regulates phosphatidylinositol 3-phosphate (PtdIns(3)P) levels by catalyzing the phosphorylation of the 3rd hydroxyl of phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) to form PtdIns(3,4,5,6)P4).",No,No,No,No,No,not-Yes,GO:0016303; GO:0005524; GO:0004672,GO:0016307; GO:0005524,GO:0016301,GO:0016303; GO:0005524,GO:0016307,GO:0016301,0.5265,0.5315,0.9215,0.0,0.5315,5,0.5022,0.5434,yes
VPS34_CANAL,A0A1D8PDV7,Protein2Text,Eukaryota,1020,"Multifunctional phosphatidylinositol 3-kinase involved in acidification of vacuoles, pH-dependent cell growth, and autophagocytosis. Plays an important role in protein transport and virulence. Component of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). Finally, it might also be involved in ethanol tolerance and cell wall integrity.","The molecular function of this protein is not specified in the given text. However, based on its name, it is likely involved in a process related to vesicle transport and/or signaling, given that it is a homolog of the mammalian phosphatidylinositol 3-kinase (PI3K) p85 subunit.",Vague,Maybe,Vague,Vague,Maybe,not-Yes,GO:0016303; GO:0005524; GO:0004672,,,,,,,,,,,0,,0.5434,yes
VPS34_CANAL,A0A1D8PDV7,Reference,Eukaryota,1020,"Multifunctional phosphatidylinositol 3-kinase involved in acidification of vacuoles, pH-dependent cell growth, and autophagocytosis. Plays an important role in protein transport and virulence. Component of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). Finally, it might also be involved in ethanol tolerance and cell wall integrity.","Multifunctional phosphatidylinositol 3-kinase involved in acidification of vacuoles, pH-dependent cell growth, and autophagocytosis. Plays an important role in protein transport and virulence. Component of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). Finally, it might also be involved in ethanol tolerance and cell wall integrity.",,,,,,,GO:0016303; GO:0005524; GO:0004672,GO:0046934,GO:0046934,GO:0046934,GO:0046934; GO:0005524,GO:0016303; GO:0005524,0.5654,0.5654,0.5654,0.8432,0.9215,5,0.6922,0.5434,yes
CYT1_CANAL,A0A1D8PHA3,ESM2Text,Eukaryota,288,"Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The complex plays an important role in the uptake of multiple carbon sources present in different host niches.","Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. Cytochrome c1 is a catalytic core subunit containing a c-",Yes,Yes,Yes,Yes,Yes,Yes,GO:0009055; GO:0020037; GO:0046872; GO:0008121,GO:0008121; GO:0009055,GO:0008121,GO:0008121; GO:0009055,GO:0008121,GO:0008121,0.7469,0.5018,0.7469,0.5018,0.5018,5,0.5998,0.4606,no
CYT1_CANAL,A0A1D8PHA3,Prot2Text,Eukaryota,288,"Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The complex plays an important role in the uptake of multiple carbon sources present in different host niches.","Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. Cytochrome c1 is a catalytic core subunit containing a c-",Yes,Yes,Yes,Yes,Yes,Yes,GO:0009055; GO:0020037; GO:0046872; GO:0008121,GO:0008121,GO:0008121,GO:0008121,GO:0008121; GO:0016491,GO:0008121,0.5018,0.5018,0.5018,0.5085,0.5018,5,0.5031,0.4606,no
CYT1_CANAL,A0A1D8PHA3,ProtT3,Eukaryota,288,"Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The complex plays an important role in the uptake of multiple carbon sources present in different host niches.","Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes",Yes,Yes,Yes,Yes,Yes,Yes,GO:0009055; GO:0020037; GO:0046872; GO:0008121,GO:0008121,GO:0008121,GO:0008121,GO:0008121,GO:0008121,0.5018,0.5018,0.5018,0.5018,0.5018,5,0.5018,0.4606,no
CYT1_CANAL,A0A1D8PHA3,ProtTale,Eukaryota,288,"Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The complex plays an important role in the uptake of multiple carbon sources present in different host niches.","Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol- cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons",No,No,No,Maybe,Maybe,not-Yes,GO:0009055; GO:0020037; GO:0046872; GO:0008121,GO:0004129,GO:0004129; GO:0016491,GO:0004129; GO:0009055,GO:0004129,GO:0004129,0.453,0.4678,0.7062,0.453,0.453,5,0.5066,0.4606,no
CYT1_CANAL,A0A1D8PHA3,Protein2Text,Eukaryota,288,"Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The complex plays an important role in the uptake of multiple carbon sources present in different host niches.","The molecular function of this protein is as a subunit of cytochrome c oxidase, which is involved in the transfer of electrons from cytochrome c to molecular oxygen during oxidative phosphorylation.",Maybe,No,No,Maybe,Maybe,not-Yes,GO:0009055; GO:0020037; GO:0046872; GO:0008121,GO:0004129,GO:0004129,GO:0004129,GO:0004129,GO:0004129,0.453,0.453,0.453,0.453,0.453,5,0.453,0.4606,no
CYT1_CANAL,A0A1D8PHA3,Reference,Eukaryota,288,"Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The complex plays an important role in the uptake of multiple carbon sources present in different host niches.","Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The complex plays an important role in the uptake of multiple carbon sources present in different host niches.",,,,,,,GO:0009055; GO:0020037; GO:0046872; GO:0008121,GO:0008121,GO:0008121,GO:0008121,GO:0008121,GO:0008121,0.5018,0.5018,0.5018,0.5018,0.5018,5,0.5018,0.4606,no
AIF1_CANAL,A0A1D8PI22,ESM2Text,Eukaryota,367,"FAD-dependent oxidoreductase involved in the regulation of cell death. In addition to the classical caspase- dependent apoptosis, cells can undergo caspase-independent apoptosis by releasing AIF1, which translocates to the nucleus for disrupting the nuclear chromatin (Probable). Plays an important role in biofilms formation and intracellular redox homeostasis by increasing anti- oxidation capacity, decreasing reactive oxygen species (ROS) production and up-regulating redox-related genes during oxidative stress. Has positive effects on the expression of apoptosis- related genes, implying a transcription regulation mechanisms of AIF1 to promote apoptosis.","Catalyzes the conversion of monodehydroascorbate to ascorbate, oxidizing NADH in the process. Ascorbate is a major antioxidant against reactive oxygen species (ROS) and nitric oxide (NO).",No,Maybe,No,No,Maybe,not-Yes,GO:0004174; GO:0050660,GO:0016651,GO:0016656,GO:0016656,GO:0016655,GO:0016656,0.3366,0.2462,0.2462,0.2844,0.2462,5,0.2719,0.4352,no
AIF1_CANAL,A0A1D8PI22,Prot2Text,Eukaryota,367,"FAD-dependent oxidoreductase involved in the regulation of cell death. In addition to the classical caspase- dependent apoptosis, cells can undergo caspase-independent apoptosis by releasing AIF1, which translocates to the nucleus for disrupting the nuclear chromatin (Probable). Plays an important role in biofilms formation and intracellular redox homeostasis by increasing anti- oxidation capacity, decreasing reactive oxygen species (ROS) production and up-regulating redox-related genes during oxidative stress. Has positive effects on the expression of apoptosis- related genes, implying a transcription regulation mechanisms of AIF1 to promote apoptosis.",Catalyzes the oxidation of NADPH to NADH; the reaction comprises an electron transfer cascade.,No,Vague,Maybe,No,No,not-Yes,GO:0004174; GO:0050660,GO:0016491,,GO:0016651,GO:0016491,GO:0003959,0.4101,,0.3366,0.4101,0.2844,4,0.3603,0.4352,no
AIF1_CANAL,A0A1D8PI22,ProtT3,Eukaryota,367,"FAD-dependent oxidoreductase involved in the regulation of cell death. In addition to the classical caspase- dependent apoptosis, cells can undergo caspase-independent apoptosis by releasing AIF1, which translocates to the nucleus for disrupting the nuclear chromatin (Probable). Plays an important role in biofilms formation and intracellular redox homeostasis by increasing anti- oxidation capacity, decreasing reactive oxygen species (ROS) production and up-regulating redox-related genes during oxidative stress. Has positive effects on the expression of apoptosis- related genes, implying a transcription regulation mechanisms of AIF1 to promote apoptosis.",Probable oxidoreductase. Belongs to the short-chain dehydrogenases/reductases (SDR) family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004174; GO:0050660,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4101,0.4101,0.4101,0.4101,0.4101,5,0.4101,0.4352,no
AIF1_CANAL,A0A1D8PI22,ProtTale,Eukaryota,367,"FAD-dependent oxidoreductase involved in the regulation of cell death. In addition to the classical caspase- dependent apoptosis, cells can undergo caspase-independent apoptosis by releasing AIF1, which translocates to the nucleus for disrupting the nuclear chromatin (Probable). Plays an important role in biofilms formation and intracellular redox homeostasis by increasing anti- oxidation capacity, decreasing reactive oxygen species (ROS) production and up-regulating redox-related genes during oxidative stress. Has positive effects on the expression of apoptosis- related genes, implying a transcription regulation mechanisms of AIF1 to promote apoptosis.","Oxidoreductase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS). SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms. These initial steps feature the priming of an unusual benzoic acid starter unit onto the highly",Vague,Maybe,Vague,Vague,Maybe,not-Yes,GO:0004174; GO:0050660,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4101,0.4101,0.4101,0.4101,0.4101,5,0.4101,0.4352,no
AIF1_CANAL,A0A1D8PI22,Protein2Text,Eukaryota,367,"FAD-dependent oxidoreductase involved in the regulation of cell death. In addition to the classical caspase- dependent apoptosis, cells can undergo caspase-independent apoptosis by releasing AIF1, which translocates to the nucleus for disrupting the nuclear chromatin (Probable). Plays an important role in biofilms formation and intracellular redox homeostasis by increasing anti- oxidation capacity, decreasing reactive oxygen species (ROS) production and up-regulating redox-related genes during oxidative stress. Has positive effects on the expression of apoptosis- related genes, implying a transcription regulation mechanisms of AIF1 to promote apoptosis.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its classification as a protein, it is likely to have a catalytic function, specifically as a transferase, as it is a part of the larger family of transferases.",No,Vague,Vague,Vague,Vague,not-Yes,GO:0004174; GO:0050660,,,,,,,,,,,0,,0.4352,no
AIF1_CANAL,A0A1D8PI22,Reference,Eukaryota,367,"FAD-dependent oxidoreductase involved in the regulation of cell death. In addition to the classical caspase- dependent apoptosis, cells can undergo caspase-independent apoptosis by releasing AIF1, which translocates to the nucleus for disrupting the nuclear chromatin (Probable). Plays an important role in biofilms formation and intracellular redox homeostasis by increasing anti- oxidation capacity, decreasing reactive oxygen species (ROS) production and up-regulating redox-related genes during oxidative stress. Has positive effects on the expression of apoptosis- related genes, implying a transcription regulation mechanisms of AIF1 to promote apoptosis.","FAD-dependent oxidoreductase involved in the regulation of cell death. In addition to the classical caspase- dependent apoptosis, cells can undergo caspase-independent apoptosis by releasing AIF1, which translocates to the nucleus for disrupting the nuclear chromatin (Probable). Plays an important role in biofilms formation and intracellular redox homeostasis by increasing anti- oxidation capacity, decreasing reactive oxygen species (ROS) production and up-regulating redox-related genes during oxidative stress. Has positive effects on the expression of apoptosis- related genes, implying a transcription regulation mechanisms of AIF1 to promote apoptosis.",,,,,,,GO:0004174; GO:0050660,GO:0016491; GO:0050660,GO:0016491; GO:0050660,GO:0016491,GO:0016491; GO:0071949,GO:0016491; GO:0071949,0.7763,0.7763,0.4101,0.7336,0.7336,5,0.686,0.4352,no
PMA1_CANAL,A0A1D8PJ01,ESM2Text,Eukaryota,895,"The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses. Plays a role in the establishment of cell polarity and hyphal growth. Acts as a pathogenic factor that, when transported by extracellular vesicles (EVs), activates host dendritic cells, promotes cytokine secretion and migration of the cDC2 subset in the gut, thereby promoting TH17 differentiation and progression of colitis.",The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0046872; GO:0008553,GO:0005524; GO:0008553,GO:0046961; GO:0016887,GO:0008553,GO:0046961,GO:0008553,0.7385,0.6024,0.4488,0.341,0.4488,5,0.5159,0.5156,no
PMA1_CANAL,A0A1D8PJ01,Prot2Text,Eukaryota,895,"The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses. Plays a role in the establishment of cell polarity and hyphal growth. Acts as a pathogenic factor that, when transported by extracellular vesicles (EVs), activates host dendritic cells, promotes cytokine secretion and migration of the cDC2 subset in the gut, thereby promoting TH17 differentiation and progression of colitis.",The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0046872; GO:0008553,GO:0008553,GO:0015662,GO:0008553,GO:0046961,GO:0008553,0.4488,0.3428,0.4488,0.341,0.4488,5,0.406,0.5156,no
PMA1_CANAL,A0A1D8PJ01,ProtT3,Eukaryota,895,"The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses. Plays a role in the establishment of cell polarity and hyphal growth. Acts as a pathogenic factor that, when transported by extracellular vesicles (EVs), activates host dendritic cells, promotes cytokine secretion and migration of the cDC2 subset in the gut, thereby promoting TH17 differentiation and progression of colitis.",The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses (By similarity). Cell membrane; Multi-pass membrane protein. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIA subfamily,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0046872; GO:0008553,GO:0005524; GO:0015078,GO:0008553,GO:0008553; GO:0005524,GO:0008553,GO:0008553,0.5745,0.4488,0.7385,0.4488,0.4488,5,0.5319,0.5156,no
PMA1_CANAL,A0A1D8PJ01,ProtTale,Eukaryota,895,"The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses. Plays a role in the establishment of cell polarity and hyphal growth. Acts as a pathogenic factor that, when transported by extracellular vesicles (EVs), activates host dendritic cells, promotes cytokine secretion and migration of the cDC2 subset in the gut, thereby promoting TH17 differentiation and progression of colitis.",May function as a Mg(2+) transporter.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0046872; GO:0008553,GO:0015095,GO:0015095,GO:0015095,,GO:0015095,0.1788,0.1788,0.1788,,0.1788,4,0.1788,0.5156,no
PMA1_CANAL,A0A1D8PJ01,Protein2Text,Eukaryota,895,"The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses. Plays a role in the establishment of cell polarity and hyphal growth. Acts as a pathogenic factor that, when transported by extracellular vesicles (EVs), activates host dendritic cells, promotes cytokine secretion and migration of the cDC2 subset in the gut, thereby promoting TH17 differentiation and progression of colitis.",The molecular function of this protein is a calcium-transporting ATPase.,No,No,No,No,Maybe,not-Yes,GO:0005524; GO:0016887; GO:0046872; GO:0008553,GO:0005388,GO:0005388,GO:0005388,GO:0005388,GO:0005388,0.3562,0.3562,0.3562,0.3562,0.3562,5,0.3562,0.5156,no
PMA1_CANAL,A0A1D8PJ01,Reference,Eukaryota,895,"The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses. Plays a role in the establishment of cell polarity and hyphal growth. Acts as a pathogenic factor that, when transported by extracellular vesicles (EVs), activates host dendritic cells, promotes cytokine secretion and migration of the cDC2 subset in the gut, thereby promoting TH17 differentiation and progression of colitis.","The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses. Plays a role in the establishment of cell polarity and hyphal growth. Acts as a pathogenic factor that, when transported by extracellular vesicles (EVs), activates host dendritic cells, promotes cytokine secretion and migration of the cDC2 subset in the gut, thereby promoting TH17 differentiation and progression of colitis.",,,,,,,GO:0005524; GO:0016887; GO:0046872; GO:0008553,GO:0046961; GO:0005524,GO:0046961; GO:0005524,GO:0046961,GO:0008553; GO:0005524,GO:0008553; GO:0005524,0.6486,0.6486,0.341,0.7385,0.7385,5,0.623,0.5156,no
TOS1_CANAL,A0A1D8PJA8,ESM2Text,Eukaryota,467,"Probable circularly permuted 1,3-beta-glucanase involved in cell wall modification through beta-1,3-glucan network alterations such as increased branching or remodeling. Plays a role in engulfment by host macrophages.","Secreted effector that contributes moderately to virulence during infection by P.capsici. Does not cause visible reaction of C.annuum for several days after inoculation, but by 7 days after inoculation, small necrotic lesions become visible. Leads only to chlorotic areas, without necrosis at 7 days after non-host N.benthamiana leaves infection.",No,Vague,Vague,No,No,not-Yes,GO:0042973,,,,,,,,,,,0,,0.2486,no
TOS1_CANAL,A0A1D8PJA8,Prot2Text,Eukaryota,467,"Probable circularly permuted 1,3-beta-glucanase involved in cell wall modification through beta-1,3-glucan network alterations such as increased branching or remodeling. Plays a role in engulfment by host macrophages.","Chitosanase subunit B. Binds chitosan, a component of the cell walls of hyphae. Probably has a structural role in chitin degradation, participating in cell wall remodeling during seed development and in the re-formation of the cell walls during conidial growth.",No,No,No,No,No,not-Yes,GO:0042973,,,,GO:0008061,GO:0033265,,,,0.1015,0.0685,2,0.085,0.2486,no
TOS1_CANAL,A0A1D8PJA8,ProtT3,Eukaryota,467,"Probable circularly permuted 1,3-beta-glucanase involved in cell wall modification through beta-1,3-glucan network alterations such as increased branching or remodeling. Plays a role in engulfment by host macrophages.",Secreted. Belongs to the PGA1 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0042973,GO:0004650,GO:0004190,GO:0004650,GO:0004650,,0.5618,0.2236,0.5618,0.5618,,4,0.4772,0.2486,no
TOS1_CANAL,A0A1D8PJA8,ProtTale,Eukaryota,467,"Probable circularly permuted 1,3-beta-glucanase involved in cell wall modification through beta-1,3-glucan network alterations such as increased branching or remodeling. Plays a role in engulfment by host macrophages.","Secreted beta-glucanase involved in the degradation of plant cell wall polysaccharides. Hydrolyzes 1,3- and 1,4-beta-glucans.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0042973,GO:0042973; GO:0004553,GO:0004553; GO:0042973; GO:0008422,GO:0042973; GO:0004553,GO:0052861; GO:0052862,GO:0004553,0.8919,0.8881,0.8919,0.4774,0.6757,5,0.765,0.2486,no
TOS1_CANAL,A0A1D8PJA8,Protein2Text,Eukaryota,467,"Probable circularly permuted 1,3-beta-glucanase involved in cell wall modification through beta-1,3-glucan network alterations such as increased branching or remodeling. Plays a role in engulfment by host macrophages.","The molecular function of this protein is to catalyze the hydrolysis of cellulose, a process known as cellulase activity. More specifically, it is a beta-1,4-glucanase, which means it breaks down beta-1,4 glycosidic bonds in cellulose, a type of polysaccharide. This enzyme plays a crucial role in the degradation of cellulose, a major component of plant cell walls, and is involved in various biological processes such as plant growth and development, decomposition, and nutrient cycling.",No,Maybe,No,No,Maybe,not-Yes,GO:0042973,GO:0030245; GO:0008810,GO:0008810; GO:0030245,GO:0008810,GO:0008810,GO:0030245; GO:0008810,0.3745,0.3745,0.5618,0.5618,0.3745,5,0.4494,0.2486,no
TOS1_CANAL,A0A1D8PJA8,Reference,Eukaryota,467,"Probable circularly permuted 1,3-beta-glucanase involved in cell wall modification through beta-1,3-glucan network alterations such as increased branching or remodeling. Plays a role in engulfment by host macrophages.","Probable circularly permuted 1,3-beta-glucanase involved in cell wall modification through beta-1,3-glucan network alterations such as increased branching or remodeling. Plays a role in engulfment by host macrophages.",,,,,,,GO:0042973,GO:0042973,GO:0042973,GO:0042973,GO:0042973,GO:0042973,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2486,no
PHYA_CANAL,A0A1D8PS71,ESM2Text,Eukaryota,461,"Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate. Myo-inositol 2-monophosphate is the end product. Responsible of about 25% of the phytase activity. The residual phytase activity might be contributed by other cytosolic or cellular enzymes such as acid phosphatase that also degraded the substrate phytate. Is essential for human tissue damage during infection.",Polythioesterase with broad substrate specificity.,No,No,No,No,No,not-Yes,GO:0003993; GO:0016158; GO:0008707,GO:0016790,GO:0016790,GO:0016790,GO:0016790,GO:0016790,0.4812,0.4812,0.4812,0.4812,0.4812,5,0.4812,0.2057,no
PHYA_CANAL,A0A1D8PS71,Prot2Text,Eukaryota,461,"Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate. Myo-inositol 2-monophosphate is the end product. Responsible of about 25% of the phytase activity. The residual phytase activity might be contributed by other cytosolic or cellular enzymes such as acid phosphatase that also degraded the substrate phytate. Is essential for human tissue damage during infection.",Catalyzes the hydrolysis of inorganic orthophosphate from phytate.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0003993; GO:0016158; GO:0008707,GO:0008707,GO:0016791,GO:0008707,GO:0008422; GO:0004000,GO:0008707,0.8384,0.7824,0.8384,0.2428,0.8384,5,0.7081,0.2057,no
PHYA_CANAL,A0A1D8PS71,ProtT3,Eukaryota,461,"Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate. Myo-inositol 2-monophosphate is the end product. Responsible of about 25% of the phytase activity. The residual phytase activity might be contributed by other cytosolic or cellular enzymes such as acid phosphatase that also degraded the substrate phytate. Is essential for human tissue damage during infection.",Belongs to the histidine acid phosphatase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0003993; GO:0016158; GO:0008707,GO:0003993,GO:0003993,GO:0003993,GO:0003993,GO:0003993,0.7923,0.7923,0.7923,0.7923,0.7923,5,0.7923,0.2057,no
PHYA_CANAL,A0A1D8PS71,ProtTale,Eukaryota,461,"Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate. Myo-inositol 2-monophosphate is the end product. Responsible of about 25% of the phytase activity. The residual phytase activity might be contributed by other cytosolic or cellular enzymes such as acid phosphatase that also degraded the substrate phytate. Is essential for human tissue damage during infection.",Catalyzes the hydrolysis of ATP to ADP and inorganic phosphate.,No,No,No,No,No,not-Yes,GO:0003993; GO:0016158; GO:0008707,GO:0016887,GO:0016887,GO:0016887,GO:0016887,GO:0016887,0.2065,0.2065,0.2065,0.2065,0.2065,5,0.2065,0.2057,no
PHYA_CANAL,A0A1D8PS71,Protein2Text,Eukaryota,461,"Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate. Myo-inositol 2-monophosphate is the end product. Responsible of about 25% of the phytase activity. The residual phytase activity might be contributed by other cytosolic or cellular enzymes such as acid phosphatase that also degraded the substrate phytate. Is essential for human tissue damage during infection.","The molecular function of this protein is to catalyze the hydrolysis of phosphate groups, specifically as a phosphatase. More specifically, it is involved in the degradation of organic phosphate compounds, such as nucleotides and sugars. It breaks down these compounds into their constituent phosphates and the respective sugars or nucleosides. This function is essential for various cellular processes, including metabolism, signal transduction, and DNA repair. The protein is likely to be involved in the breakdown of organic phosphates in the cell, playing a crucial role in maintaining cellular homeostasis and regulating various cellular processes.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0003993; GO:0016158; GO:0008707,GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,0.7824,0.7824,0.7824,0.7824,0.7824,5,0.7824,0.2057,no
PHYA_CANAL,A0A1D8PS71,Reference,Eukaryota,461,"Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate. Myo-inositol 2-monophosphate is the end product. Responsible of about 25% of the phytase activity. The residual phytase activity might be contributed by other cytosolic or cellular enzymes such as acid phosphatase that also degraded the substrate phytate. Is essential for human tissue damage during infection.","Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate. Myo-inositol 2-monophosphate is the end product. Responsible of about 25% of the phytase activity. The residual phytase activity might be contributed by other cytosolic or cellular enzymes such as acid phosphatase that also degraded the substrate phytate. Is essential for human tissue damage during infection.",,,,,,,GO:0003993; GO:0016158; GO:0008707,GO:0004523,GO:0004523,GO:0004523,GO:0008707; GO:0003993,GO:0003993,0.2946,0.2946,0.2946,0.9538,0.7923,5,0.526,0.2057,no
AAL_LOKAT,A0A1M4XLJ3,ESM2Text,Bacteria,548,"Aromatic ammonia-lyase (AAL) that shows reduced activity to catalyze the non-oxidative ammonia elimination from the canonical AAL substrates L-Phe and L-Tyr, contrasted by its pronounced efficiency towards substrates with electron-donor aromatic substituents such as 3,4-dimethoxy-L-phenylalanine. Is also able to catalyze the reverse reaction in vitro, i.e. the ammonia addition reaction to cinnamate derivatives, producing enantiopure phenylalanine derivatives. Shows no activity with L-His.","Catalyzes the non-oxidative deamination of L-phenylalanine and L-tyrosine to form trans-cinnamic acid and p-coumaric acid respectively with similar efficiencies. Facilitates the commitment step in phenylpropanoid pathways that produce secondary metabolites such as lignins, coumarins and flavonoids.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016841,GO:0045548,GO:0045548,GO:0045548,GO:0045548,GO:0045548; GO:0052883,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.4851,no
AAL_LOKAT,A0A1M4XLJ3,Prot2Text,Bacteria,548,"Aromatic ammonia-lyase (AAL) that shows reduced activity to catalyze the non-oxidative ammonia elimination from the canonical AAL substrates L-Phe and L-Tyr, contrasted by its pronounced efficiency towards substrates with electron-donor aromatic substituents such as 3,4-dimethoxy-L-phenylalanine. Is also able to catalyze the reverse reaction in vitro, i.e. the ammonia addition reaction to cinnamate derivatives, producing enantiopure phenylalanine derivatives. Shows no activity with L-His.","Catalyzes the non-oxidative deamination of L-phenylalanine to form trans-cinnamic acid, the first step in the phenylpropanoid pathway.",Yes,Yes,Yes,Maybe,Yes,Yes,GO:0016841,GO:0045548,GO:0045548,GO:0045548,GO:0045548,GO:0045548,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.4851,no
AAL_LOKAT,A0A1M4XLJ3,ProtT3,Bacteria,548,"Aromatic ammonia-lyase (AAL) that shows reduced activity to catalyze the non-oxidative ammonia elimination from the canonical AAL substrates L-Phe and L-Tyr, contrasted by its pronounced efficiency towards substrates with electron-donor aromatic substituents such as 3,4-dimethoxy-L-phenylalanine. Is also able to catalyze the reverse reaction in vitro, i.e. the ammonia addition reaction to cinnamate derivatives, producing enantiopure phenylalanine derivatives. Shows no activity with L-His.",Cytoplasm. Belongs to the PAL/histidase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016841,GO:0016841,GO:0016841,GO:0016841,GO:0016841,GO:0016841,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4851,no
AAL_LOKAT,A0A1M4XLJ3,ProtTale,Bacteria,548,"Aromatic ammonia-lyase (AAL) that shows reduced activity to catalyze the non-oxidative ammonia elimination from the canonical AAL substrates L-Phe and L-Tyr, contrasted by its pronounced efficiency towards substrates with electron-donor aromatic substituents such as 3,4-dimethoxy-L-phenylalanine. Is also able to catalyze the reverse reaction in vitro, i.e. the ammonia addition reaction to cinnamate derivatives, producing enantiopure phenylalanine derivatives. Shows no activity with L-His.",Catalyzes the conversion of L-lysine to N(2)-acetyl-L- lysine.,No,No,No,No,No,not-Yes,GO:0016841,GO:0016407,GO:0016410,GO:0008080,GO:0016746,GO:0004468,0.2353,0.2353,0.1863,0.3284,0.1584,5,0.2287,0.4851,no
AAL_LOKAT,A0A1M4XLJ3,Protein2Text,Bacteria,548,"Aromatic ammonia-lyase (AAL) that shows reduced activity to catalyze the non-oxidative ammonia elimination from the canonical AAL substrates L-Phe and L-Tyr, contrasted by its pronounced efficiency towards substrates with electron-donor aromatic substituents such as 3,4-dimethoxy-L-phenylalanine. Is also able to catalyze the reverse reaction in vitro, i.e. the ammonia addition reaction to cinnamate derivatives, producing enantiopure phenylalanine derivatives. Shows no activity with L-His.","This protein is involved in the molecular function of catalyzing a reaction in the biosynthesis of aromatic amino acids, specifically the decarboxylation of 3-dehydroshikimate to form protocatechuate.",No,No,No,No,No,not-Yes,GO:0016841,,GO:0016831,,,GO:0016831,,0.4645,,,0.4645,2,0.4645,0.4851,no
AAL_LOKAT,A0A1M4XLJ3,Reference,Bacteria,548,"Aromatic ammonia-lyase (AAL) that shows reduced activity to catalyze the non-oxidative ammonia elimination from the canonical AAL substrates L-Phe and L-Tyr, contrasted by its pronounced efficiency towards substrates with electron-donor aromatic substituents such as 3,4-dimethoxy-L-phenylalanine. Is also able to catalyze the reverse reaction in vitro, i.e. the ammonia addition reaction to cinnamate derivatives, producing enantiopure phenylalanine derivatives. Shows no activity with L-His.","Aromatic ammonia-lyase (AAL) that shows reduced activity to catalyze the non-oxidative ammonia elimination from the canonical AAL substrates L-Phe and L-Tyr, contrasted by its pronounced efficiency towards substrates with electron-donor aromatic substituents such as 3,4-dimethoxy-L-phenylalanine. Is also able to catalyze the reverse reaction in vitro, i.e. the ammonia addition reaction to cinnamate derivatives, producing enantiopure phenylalanine derivatives. Shows no activity with L-His.",,,,,,,GO:0016841,GO:0045548,GO:0045548,GO:0016841,GO:0045548,GO:0045548,0.8582,0.8582,1.0,0.8582,0.8582,5,0.8866,0.4851,no
CBPB1_AEDAE,A0A1S4F020,ESM2Text,Eukaryota,412,"Carboxypeptidase that preferentially hydrolyzes arginine and lysine residues at the C-terminus. During infection by dengue virus, may play a role in preventing viral packaging, maturation, and release from the midgut.",Extracellular metalloprotease that contributes to pathogenicity.,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0004181; GO:0008270,GO:0004222,GO:0004222,GO:0004222,GO:0004222,GO:0004222,0.3752,0.3752,0.3752,0.3752,0.3752,5,0.3752,0.3381,no
CBPB1_AEDAE,A0A1S4F020,Prot2Text,Eukaryota,412,"Carboxypeptidase that preferentially hydrolyzes arginine and lysine residues at the C-terminus. During infection by dengue virus, may play a role in preventing viral packaging, maturation, and release from the midgut.",Carboxypeptidase that may cleave C-terminal acidic residues from biologically active peptides.,Maybe,Yes,Maybe,Yes,Maybe,not-Yes,GO:0004181; GO:0008270,GO:0004180,GO:0004180,GO:0004180,GO:0004180,GO:0004180,0.5255,0.5255,0.5255,0.5255,0.5255,5,0.5255,0.3381,no
CBPB1_AEDAE,A0A1S4F020,ProtT3,Eukaryota,412,"Carboxypeptidase that preferentially hydrolyzes arginine and lysine residues at the C-terminus. During infection by dengue virus, may play a role in preventing viral packaging, maturation, and release from the midgut.",Secreted. Belongs to the peptidase M14 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004181; GO:0008270,GO:0004181,GO:0004181,GO:0004181,GO:0004181,GO:0004181,0.6825,0.6825,0.6825,0.6825,0.6825,5,0.6825,0.3381,no
CBPB1_AEDAE,A0A1S4F020,ProtTale,Eukaryota,412,"Carboxypeptidase that preferentially hydrolyzes arginine and lysine residues at the C-terminus. During infection by dengue virus, may play a role in preventing viral packaging, maturation, and release from the midgut.",Carboxypeptidase that catalyzes the removal of C-terminal hydrophobic residues from peptides and proteins.,Maybe,Yes,Maybe,Yes,Yes,Yes,GO:0004181; GO:0008270,GO:0004180,GO:0004181,GO:0004180,GO:0004180,GO:0004180,0.5255,0.6825,0.5255,0.5255,0.5255,5,0.5569,0.3381,no
CBPB1_AEDAE,A0A1S4F020,Protein2Text,Eukaryota,412,"Carboxypeptidase that preferentially hydrolyzes arginine and lysine residues at the C-terminus. During infection by dengue virus, may play a role in preventing viral packaging, maturation, and release from the midgut.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its name, it can be inferred that this protein is involved in the degradation of peptides, as it is classified as a metalloprotease and has a role in breaking down proteins. More specifically, it is involved in the degradation of a specific protein, which is not named in the provided text.",Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0004181; GO:0008270,GO:0008237,GO:0008237,GO:0008237,GO:0004222,GO:0008237,0.4716,0.4716,0.4716,0.3752,0.4716,5,0.4523,0.3381,no
CBPB1_AEDAE,A0A1S4F020,Reference,Eukaryota,412,"Carboxypeptidase that preferentially hydrolyzes arginine and lysine residues at the C-terminus. During infection by dengue virus, may play a role in preventing viral packaging, maturation, and release from the midgut.","Carboxypeptidase that preferentially hydrolyzes arginine and lysine residues at the C-terminus. During infection by dengue virus, may play a role in preventing viral packaging, maturation, and release from the midgut.",,,,,,,GO:0004181; GO:0008270,GO:0004181,GO:0004181,GO:0004180,GO:0004180,GO:0004180,0.6825,0.6825,0.5255,0.5255,0.5255,5,0.5883,0.3381,no
TS4FN_CANSA,A0A1V0QSG6,ESM2Text,Eukaryota,567,"Involved in sesquiterpene olefins biosynthesis, constituants of cannabinoids and terpenoids-rich resins. Catalyzes mainly the conversion of (2E)-farnesyl diphosphate to allo- aromadendrene, and also produces minor products such as alpha-humulene, valencene and palustrol. Can also use (2E)-geranyl diphosphate as substrate with low efficiency, producing minor amounts of myrcene.",Sesquiterpene synthase converting farnesyl diphosphate to (E)-2-epi-beta-caryophyllene as the major product and (E)-2-epi-delta-caryophyllene as minor product.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0080017; GO:0000287; GO:0050551; GO:0102905,,GO:0010333,GO:0010333,GO:0010333,GO:0010333,,0.6531,0.6531,0.6531,0.6531,4,0.6531,0.1808,no
TS4FN_CANSA,A0A1V0QSG6,Prot2Text,Eukaryota,567,"Involved in sesquiterpene olefins biosynthesis, constituants of cannabinoids and terpenoids-rich resins. Catalyzes mainly the conversion of (2E)-farnesyl diphosphate to allo- aromadendrene, and also produces minor products such as alpha-humulene, valencene and palustrol. Can also use (2E)-geranyl diphosphate as substrate with low efficiency, producing minor amounts of myrcene.","Sesquiterpene synthase that catalyzes the formation of vetispiradiene from trans,trans-farnesyl diphosphate. The initial internal cyclization produces the monocyclic intermediate germacrene A.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0080017; GO:0000287; GO:0050551; GO:0102905,GO:0010334,,GO:0010334,GO:0010334,GO:0050551,0.6143,,0.6143,0.6143,0.6649,4,0.627,0.1808,no
TS4FN_CANSA,A0A1V0QSG6,ProtT3,Eukaryota,567,"Involved in sesquiterpene olefins biosynthesis, constituants of cannabinoids and terpenoids-rich resins. Catalyzes mainly the conversion of (2E)-farnesyl diphosphate to allo- aromadendrene, and also produces minor products such as alpha-humulene, valencene and palustrol. Can also use (2E)-geranyl diphosphate as substrate with low efficiency, producing minor amounts of myrcene.",Catalyzes the cyclization of farnesyl diphosphate (FPP) to (E)-beta-farnesene. Belongs to the terpene synthase family. Tpsa subfamily,Yes,Yes,Yes,Maybe,Vague,Yes,GO:0080017; GO:0000287; GO:0050551; GO:0102905,GO:0010333,GO:0016829,GO:0010333,GO:0010333,GO:0010333,0.6531,0.4736,0.6531,0.6531,0.6531,5,0.6172,0.1808,no
TS4FN_CANSA,A0A1V0QSG6,ProtTale,Eukaryota,567,"Involved in sesquiterpene olefins biosynthesis, constituants of cannabinoids and terpenoids-rich resins. Catalyzes mainly the conversion of (2E)-farnesyl diphosphate to allo- aromadendrene, and also produces minor products such as alpha-humulene, valencene and palustrol. Can also use (2E)-geranyl diphosphate as substrate with low efficiency, producing minor amounts of myrcene.","Sesquiterpene synthase that catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) into the sesquiterpene (2E,6E)-beta-farnesene.",Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0080017; GO:0000287; GO:0050551; GO:0102905,GO:0010333,GO:0016829,GO:0010333,GO:0010334,GO:0010334; GO:0016829,0.6531,0.4736,0.6531,0.6143,0.6247,5,0.6038,0.1808,no
TS4FN_CANSA,A0A1V0QSG6,Protein2Text,Eukaryota,567,"Involved in sesquiterpene olefins biosynthesis, constituants of cannabinoids and terpenoids-rich resins. Catalyzes mainly the conversion of (2E)-farnesyl diphosphate to allo- aromadendrene, and also produces minor products such as alpha-humulene, valencene and palustrol. Can also use (2E)-geranyl diphosphate as substrate with low efficiency, producing minor amounts of myrcene.","This protein is a part of the terpene synthase family and is involved in the biosynthesis of terpenes, which are a class of organic compounds found in plants and other organisms. Terpene synthases convert geranyl diphosphate (GPP) or farnesyl diphosphate (FPP) into terpenes, which have a variety of functions in plants, including defense against pathogens and herbivores, pollinator attraction, and regulation of plant growth and development. The specific molecular function of this protein is to catalyze the conversion of GPP into a specific terpene, likely (E)-beta-ocimene, which is a known product of terpene synthases in plants.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0080017; GO:0000287; GO:0050551; GO:0102905,GO:0010333,GO:0010333; GO:0000287,GO:0010333,GO:0010333,GO:0010334,0.6531,0.8648,0.6531,0.6531,0.6143,5,0.6877,0.1808,no
TS4FN_CANSA,A0A1V0QSG6,Reference,Eukaryota,567,"Involved in sesquiterpene olefins biosynthesis, constituants of cannabinoids and terpenoids-rich resins. Catalyzes mainly the conversion of (2E)-farnesyl diphosphate to allo- aromadendrene, and also produces minor products such as alpha-humulene, valencene and palustrol. Can also use (2E)-geranyl diphosphate as substrate with low efficiency, producing minor amounts of myrcene.","Involved in sesquiterpene olefins biosynthesis, constituants of cannabinoids and terpenoids-rich resins. Catalyzes mainly the conversion of (2E)-farnesyl diphosphate to allo- aromadendrene, and also produces minor products such as alpha-humulene, valencene and palustrol. Can also use (2E)-geranyl diphosphate as substrate with low efficiency, producing minor amounts of myrcene.",,,,,,,GO:0080017; GO:0000287; GO:0050551; GO:0102905,GO:0010334,GO:0010334,GO:0010334,GO:0010333; GO:0016829,,0.6143,0.6143,0.6143,0.6553,,4,0.6245,0.1808,no
IUTB_VIBVL,A0A1W7HCY1,ESM2Text,Bacteria,244,"Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell (Probable). Acts as a major ferric-aerobactin reductase catalyzing the reduction of Fe(3+)-aerobactin, a citrate-hydroxamate siderophore produced by other bacteria. Catalyzes reduction of Fe(3+)-vulnibactin, a catecholate siderophore synthesized by V.vulnificus, in the absence of VuuB. Catalyzes reduction of ferrioxamine B and Fe(3+)-vibriobactin in vitro. No activity with Fe(3+)- enterobactin. Catalyzes reduction of ferric chelating compound Fe(3+)- nitrilotriacetic acid (NTA) in the presence of NADH, NADPH or reduced glutathione (GSH) as its electron donor in vitro. Also catalyzes reduction of ferric chelating compounds Fe(3+)-citrate and Fe(3+)-EDTA as well as non-complexed FeCl3 in the presence of GSH as its electron donor in vitro. Highest activity with Fe(3+)-NTA as electron acceptor and GSH as donor.","Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex CFD1-NBP35. Electrons are transferred to DRE2 from NADPH via the FAD- and FMN-containing protein TAH18. TAH18-DRE2 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit RNR2.",No,No,No,No,No,not-Yes,GO:0051537; GO:0140618; GO:0052851; GO:0046872,GO:0009055; GO:0051536,GO:0009055,GO:0009055; GO:0051536,GO:0009055; GO:0051536,,0.4465,0.195,0.4465,0.4465,,4,0.3836,0.3656,no
IUTB_VIBVL,A0A1W7HCY1,Prot2Text,Bacteria,244,"Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell (Probable). Acts as a major ferric-aerobactin reductase catalyzing the reduction of Fe(3+)-aerobactin, a citrate-hydroxamate siderophore produced by other bacteria. Catalyzes reduction of Fe(3+)-vulnibactin, a catecholate siderophore synthesized by V.vulnificus, in the absence of VuuB. Catalyzes reduction of ferrioxamine B and Fe(3+)-vibriobactin in vitro. No activity with Fe(3+)- enterobactin. Catalyzes reduction of ferric chelating compound Fe(3+)- nitrilotriacetic acid (NTA) in the presence of NADH, NADPH or reduced glutathione (GSH) as its electron donor in vitro. Also catalyzes reduction of ferric chelating compounds Fe(3+)-citrate and Fe(3+)-EDTA as well as non-complexed FeCl3 in the presence of GSH as its electron donor in vitro. Highest activity with Fe(3+)-NTA as electron acceptor and GSH as donor.","Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity.",No,No,No,No,No,not-Yes,GO:0051537; GO:0140618; GO:0052851; GO:0046872,,,,GO:0005525,,,,,0.1769,,1,0.1769,0.3656,no
IUTB_VIBVL,A0A1W7HCY1,ProtT3,Bacteria,244,"Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell (Probable). Acts as a major ferric-aerobactin reductase catalyzing the reduction of Fe(3+)-aerobactin, a citrate-hydroxamate siderophore produced by other bacteria. Catalyzes reduction of Fe(3+)-vulnibactin, a catecholate siderophore synthesized by V.vulnificus, in the absence of VuuB. Catalyzes reduction of ferrioxamine B and Fe(3+)-vibriobactin in vitro. No activity with Fe(3+)- enterobactin. Catalyzes reduction of ferric chelating compound Fe(3+)- nitrilotriacetic acid (NTA) in the presence of NADH, NADPH or reduced glutathione (GSH) as its electron donor in vitro. Also catalyzes reduction of ferric chelating compounds Fe(3+)-citrate and Fe(3+)-EDTA as well as non-complexed FeCl3 in the presence of GSH as its electron donor in vitro. Highest activity with Fe(3+)-NTA as electron acceptor and GSH as donor.",To M.jannaschii MJ0088,Vague,Vague,Vague,Vague,No,not-Yes,GO:0051537; GO:0140618; GO:0052851; GO:0046872,,,,,,,,,,,0,,0.3656,no
IUTB_VIBVL,A0A1W7HCY1,ProtTale,Bacteria,244,"Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell (Probable). Acts as a major ferric-aerobactin reductase catalyzing the reduction of Fe(3+)-aerobactin, a citrate-hydroxamate siderophore produced by other bacteria. Catalyzes reduction of Fe(3+)-vulnibactin, a catecholate siderophore synthesized by V.vulnificus, in the absence of VuuB. Catalyzes reduction of ferrioxamine B and Fe(3+)-vibriobactin in vitro. No activity with Fe(3+)- enterobactin. Catalyzes reduction of ferric chelating compound Fe(3+)- nitrilotriacetic acid (NTA) in the presence of NADH, NADPH or reduced glutathione (GSH) as its electron donor in vitro. Also catalyzes reduction of ferric chelating compounds Fe(3+)-citrate and Fe(3+)-EDTA as well as non-complexed FeCl3 in the presence of GSH as its electron donor in vitro. Highest activity with Fe(3+)-NTA as electron acceptor and GSH as donor.","Serves to protect the cell against the toxic effect of metallo-beta-lactamases (MBLs) by sequestering MBLs in the periplasm. MBLs are enzymes that catalyze the hydrolysis of the beta-lactam ring, an essential step in the bacterial cell wall biosynthesis.",No,No,No,No,No,not-Yes,GO:0051537; GO:0140618; GO:0052851; GO:0046872,,,,,,,,,,,0,,0.3656,no
IUTB_VIBVL,A0A1W7HCY1,Protein2Text,Bacteria,244,"Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell (Probable). Acts as a major ferric-aerobactin reductase catalyzing the reduction of Fe(3+)-aerobactin, a citrate-hydroxamate siderophore produced by other bacteria. Catalyzes reduction of Fe(3+)-vulnibactin, a catecholate siderophore synthesized by V.vulnificus, in the absence of VuuB. Catalyzes reduction of ferrioxamine B and Fe(3+)-vibriobactin in vitro. No activity with Fe(3+)- enterobactin. Catalyzes reduction of ferric chelating compound Fe(3+)- nitrilotriacetic acid (NTA) in the presence of NADH, NADPH or reduced glutathione (GSH) as its electron donor in vitro. Also catalyzes reduction of ferric chelating compounds Fe(3+)-citrate and Fe(3+)-EDTA as well as non-complexed FeCl3 in the presence of GSH as its electron donor in vitro. Highest activity with Fe(3+)-NTA as electron acceptor and GSH as donor.","The molecular function of this protein is not explicitly stated in the provided information. However, based on its name, it can be inferred that it is involved in DNA repair, specifically in the repair of damaged DNA caused by oxidative stress. This protein is likely involved in the repair of DNA lesions, such as thymine glycol, which is a common type of DNA damage caused by reactive oxygen species (ROS). The molecular function of this protein is likely to be a DNA repair enzyme, specifically a glycosylase that recognizes and removes damaged DNA bases. 

Please note that this is an inference based on the name of the protein and its likely function, and more specific information would be required to confirm its molecular function. 

If you have any more information or context about this protein, I would be happy to try and provide a more specific answer.",No,No,No,No,No,not-Yes,GO:0051537; GO:0140618; GO:0052851; GO:0046872,,,,,GO:0016798,,,,,0.2029,1,0.2029,0.3656,no
IUTB_VIBVL,A0A1W7HCY1,Reference,Bacteria,244,"Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell (Probable). Acts as a major ferric-aerobactin reductase catalyzing the reduction of Fe(3+)-aerobactin, a citrate-hydroxamate siderophore produced by other bacteria. Catalyzes reduction of Fe(3+)-vulnibactin, a catecholate siderophore synthesized by V.vulnificus, in the absence of VuuB. Catalyzes reduction of ferrioxamine B and Fe(3+)-vibriobactin in vitro. No activity with Fe(3+)- enterobactin. Catalyzes reduction of ferric chelating compound Fe(3+)- nitrilotriacetic acid (NTA) in the presence of NADH, NADPH or reduced glutathione (GSH) as its electron donor in vitro. Also catalyzes reduction of ferric chelating compounds Fe(3+)-citrate and Fe(3+)-EDTA as well as non-complexed FeCl3 in the presence of GSH as its electron donor in vitro. Highest activity with Fe(3+)-NTA as electron acceptor and GSH as donor.","Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell (Probable). Acts as a major ferric-aerobactin reductase catalyzing the reduction of Fe(3+)-aerobactin, a citrate-hydroxamate siderophore produced by other bacteria. Catalyzes reduction of Fe(3+)-vulnibactin, a catecholate siderophore synthesized by V.vulnificus, in the absence of VuuB. Catalyzes reduction of ferrioxamine B and Fe(3+)-vibriobactin in vitro. No activity with Fe(3+)- enterobactin. Catalyzes reduction of ferric chelating compound Fe(3+)- nitrilotriacetic acid (NTA) in the presence of NADH, NADPH or reduced glutathione (GSH) as its electron donor in vitro. Also catalyzes reduction of ferric chelating compounds Fe(3+)-citrate and Fe(3+)-EDTA as well as non-complexed FeCl3 in the presence of GSH as its electron donor in vitro. Highest activity with Fe(3+)-NTA as electron acceptor and GSH as donor.",,,,,,,GO:0051537; GO:0140618; GO:0052851; GO:0046872,GO:0016491,GO:0016491,GO:0010181; GO:0016491,GO:0016491; GO:0008942,GO:0016491; GO:0010181,0.3826,0.3826,0.432,0.3652,0.432,5,0.3989,0.3656,no
VINHY_RAUSE,A0A218NGS0,ESM2Text,Eukaryota,480,"A cytochrome P450 monooxygenase involved in the biosynthesis of ajmaline-type monoterpenoid indole alkaloids (MIAs) natural products, important plant-derived pharmaceuticals used in the therapy of heart disorders. Catalyzes the hydroxylation of vinorine to vomilenine, an intermediate chemical in the biosynthesis of ajmaline. Supports also vomilenine isomerization to perakine.",Involved in the biosynthesis of benzylisoquinoline alkaloids. Converts (S)-tetrahydrocolumbamine (THC) to (S)-canadine.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0016853; GO:0004497; GO:0050596,GO:0016491,GO:0016491,GO:0016709,GO:0016491,GO:0016705,0.5178,0.5178,0.5122,0.5178,0.4578,5,0.5047,0.3899,no
VINHY_RAUSE,A0A218NGS0,Prot2Text,Eukaryota,480,"A cytochrome P450 monooxygenase involved in the biosynthesis of ajmaline-type monoterpenoid indole alkaloids (MIAs) natural products, important plant-derived pharmaceuticals used in the therapy of heart disorders. Catalyzes the hydroxylation of vinorine to vomilenine, an intermediate chemical in the biosynthesis of ajmaline. Supports also vomilenine isomerization to perakine.","Component of the floral volatile benzenoid/phenylpropanoid (FVBP) biosynthetic pathway that controls carbon flux to pigments essential for pollination or UV protection, to numerous pytoalexins synthesized by plants when challenged by pathogens, and to lignins.",No,Vague,No,No,No,not-Yes,GO:0020037; GO:0005506; GO:0016853; GO:0004497; GO:0050596,,,,,,,,,,,0,,0.3899,no
VINHY_RAUSE,A0A218NGS0,ProtT3,Eukaryota,480,"A cytochrome P450 monooxygenase involved in the biosynthesis of ajmaline-type monoterpenoid indole alkaloids (MIAs) natural products, important plant-derived pharmaceuticals used in the therapy of heart disorders. Catalyzes the hydroxylation of vinorine to vomilenine, an intermediate chemical in the biosynthesis of ajmaline. Supports also vomilenine isomerization to perakine.",Involved in the biosynthesis of benzylisoquinoline alkaloids. Catalyzes the conversion of N-methylscoulerine to scoulerine. Membrane; Single-pass membrane protein. Belongs to the cytochrome P450 family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0016853; GO:0004497; GO:0050596,GO:0004497,GO:0004497,GO:0004497; GO:0005506; GO:0020037,GO:0004497,GO:0004497,0.5701,0.5701,0.8932,0.5701,0.5701,5,0.6347,0.3899,no
VINHY_RAUSE,A0A218NGS0,ProtTale,Eukaryota,480,"A cytochrome P450 monooxygenase involved in the biosynthesis of ajmaline-type monoterpenoid indole alkaloids (MIAs) natural products, important plant-derived pharmaceuticals used in the therapy of heart disorders. Catalyzes the hydroxylation of vinorine to vomilenine, an intermediate chemical in the biosynthesis of ajmaline. Supports also vomilenine isomerization to perakine.","Cytochrome P450 monooxygenase involved in the biosynthesis of indole-3-acetic acid (IAA)-amido acids, a family of plant hormones known as auxin. Catalyzes the hydroxylation of IAA-amido acids at C-3 to produce 2-oxindole-3-acetic acid (2-oxIAA)-amido acids.",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0016853; GO:0004497; GO:0050596,GO:0004497,GO:0004497; GO:0005506; GO:0016705,GO:0004497; GO:0020037; GO:0005506,GO:0004497,GO:0004497; GO:0005506; GO:0020037,0.5701,0.7548,0.8932,0.5701,0.8932,5,0.7363,0.3899,no
VINHY_RAUSE,A0A218NGS0,Protein2Text,Eukaryota,480,"A cytochrome P450 monooxygenase involved in the biosynthesis of ajmaline-type monoterpenoid indole alkaloids (MIAs) natural products, important plant-derived pharmaceuticals used in the therapy of heart disorders. Catalyzes the hydroxylation of vinorine to vomilenine, an intermediate chemical in the biosynthesis of ajmaline. Supports also vomilenine isomerization to perakine.","This protein is involved in the molecular function of oxidoreductase activity. Specifically, it catalyzes the conversion of certain molecules by transferring electrons from one molecule to another, playing a crucial role in various biochemical processes. In the case of this protein, it is involved in the oxidation of certain compounds, likely playing a role in the metabolism of terpenes and other plant secondary metabolites.",Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0016853; GO:0004497; GO:0050596,GO:0016491,GO:0016491,,GO:0016491,GO:0016491,0.5178,0.5178,,0.5178,0.5178,4,0.5178,0.3899,no
VINHY_RAUSE,A0A218NGS0,Reference,Eukaryota,480,"A cytochrome P450 monooxygenase involved in the biosynthesis of ajmaline-type monoterpenoid indole alkaloids (MIAs) natural products, important plant-derived pharmaceuticals used in the therapy of heart disorders. Catalyzes the hydroxylation of vinorine to vomilenine, an intermediate chemical in the biosynthesis of ajmaline. Supports also vomilenine isomerization to perakine.","A cytochrome P450 monooxygenase involved in the biosynthesis of ajmaline-type monoterpenoid indole alkaloids (MIAs) natural products, important plant-derived pharmaceuticals used in the therapy of heart disorders. Catalyzes the hydroxylation of vinorine to vomilenine, an intermediate chemical in the biosynthesis of ajmaline. Supports also vomilenine isomerization to perakine.",,,,,,,GO:0020037; GO:0005506; GO:0016853; GO:0004497; GO:0050596,GO:0004497,GO:0004497,GO:0004497,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,0.5701,0.5701,0.5701,0.8932,0.8932,5,0.6993,0.3899,no
RUFO_STRAR,A0A224AU14,ESM2Text,Bacteria,394,"Cytochrome P450 involved in the biosynthesis of rufomycins, a class of cyclic heptapeptides with anti-mycobacterial activity. Catalyzes the 3-nitration of tyrosine, leading to the formation of 3-nitrotyrosine (3NTyr). It was initially postulated that RufO acts on free L-tyrosine. However, further characterization demonstrates that free L-tyrosine is not the native substrate of RufO, although it could serve as a poor alternative under certain circumstances. It was subsequently demonstrated that RufO nitrates a biarylitide-type ribosomal pentapeptide precursor (Met-Arg-Tyr-Leu-His or MRYLH), which is encoded by bytA in the rufomycin gene cluster, producing the ribosomally synthesized and post-translationally modified peptide MR(NO(2)-Tyr)LH. Following the RufO-catalyzed nitration, the nitrated tyrosine (3-NO2-Tyr), key for antibiotic activity, is cleaved out by a dedicated aminopeptidase, before being activated and incorporated into the non-ribosomal peptide chain by the rufomycin synthetase assembly line (Ref.2). RufO can also nitrate the synthetic pentapeptide Nle-RYLH, where norleucine (Nle) is used to avoid non- enzyme catalyzed Met oxidation (Ref.2). It cannot use phenylalanine, tryptophan, 4-hydroxyphenylpyruvate or 4-aminophenylalanine.","Involved in the biosynthesis of the macrolide antibiotic tylosin derived from the polyketide lactone tylactone. Catalyzes the oxidative conversion of 6-deoxocathasterone (6-DT-AO) to 6-deoxocathasterone (6-TEA-O), likely via a central condensation reaction. The enzyme shows a strong preference for the NADP portion of 6-TEA as substrate. Also able to catalyze the oxidative conversion of mono- and dihydro-tylosin (DD-Tyr) to 6-TEA-D-O and mono- and disaccharide (CDS-Asp-Asn-CDS), but it displays only a weak activity with 6-TEA-Asp-Asn-CDS.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0016491,GO:0016491; GO:0050661,,,,0.5572,0.5156,,,,2,0.5364,0.1225,no
RUFO_STRAR,A0A224AU14,Prot2Text,Bacteria,394,"Cytochrome P450 involved in the biosynthesis of rufomycins, a class of cyclic heptapeptides with anti-mycobacterial activity. Catalyzes the 3-nitration of tyrosine, leading to the formation of 3-nitrotyrosine (3NTyr). It was initially postulated that RufO acts on free L-tyrosine. However, further characterization demonstrates that free L-tyrosine is not the native substrate of RufO, although it could serve as a poor alternative under certain circumstances. It was subsequently demonstrated that RufO nitrates a biarylitide-type ribosomal pentapeptide precursor (Met-Arg-Tyr-Leu-His or MRYLH), which is encoded by bytA in the rufomycin gene cluster, producing the ribosomally synthesized and post-translationally modified peptide MR(NO(2)-Tyr)LH. Following the RufO-catalyzed nitration, the nitrated tyrosine (3-NO2-Tyr), key for antibiotic activity, is cleaved out by a dedicated aminopeptidase, before being activated and incorporated into the non-ribosomal peptide chain by the rufomycin synthetase assembly line (Ref.2). RufO can also nitrate the synthetic pentapeptide Nle-RYLH, where norleucine (Nle) is used to avoid non- enzyme catalyzed Met oxidation (Ref.2). It cannot use phenylalanine, tryptophan, 4-hydroxyphenylpyruvate or 4-aminophenylalanine.",Involved in the biosynthesis of the macrolide antibiotic tylosin derived from the polyketide lactone tylactone. TylM3 is required for the glycosylation of 8-amino-8-deoxypytylactone.,No,No,No,No,No,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.2891,0.2891,0.2891,0.2891,0.2891,5,0.2891,0.1225,no
RUFO_STRAR,A0A224AU14,ProtT3,Bacteria,394,"Cytochrome P450 involved in the biosynthesis of rufomycins, a class of cyclic heptapeptides with anti-mycobacterial activity. Catalyzes the 3-nitration of tyrosine, leading to the formation of 3-nitrotyrosine (3NTyr). It was initially postulated that RufO acts on free L-tyrosine. However, further characterization demonstrates that free L-tyrosine is not the native substrate of RufO, although it could serve as a poor alternative under certain circumstances. It was subsequently demonstrated that RufO nitrates a biarylitide-type ribosomal pentapeptide precursor (Met-Arg-Tyr-Leu-His or MRYLH), which is encoded by bytA in the rufomycin gene cluster, producing the ribosomally synthesized and post-translationally modified peptide MR(NO(2)-Tyr)LH. Following the RufO-catalyzed nitration, the nitrated tyrosine (3-NO2-Tyr), key for antibiotic activity, is cleaved out by a dedicated aminopeptidase, before being activated and incorporated into the non-ribosomal peptide chain by the rufomycin synthetase assembly line (Ref.2). RufO can also nitrate the synthetic pentapeptide Nle-RYLH, where norleucine (Nle) is used to avoid non- enzyme catalyzed Met oxidation (Ref.2). It cannot use phenylalanine, tryptophan, 4-hydroxyphenylpyruvate or 4-aminophenylalanine.","Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Belongs to the cytochrome P450 family",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,0.9516,0.9516,0.9516,0.9516,0.9516,5,0.9516,0.1225,no
RUFO_STRAR,A0A224AU14,ProtTale,Bacteria,394,"Cytochrome P450 involved in the biosynthesis of rufomycins, a class of cyclic heptapeptides with anti-mycobacterial activity. Catalyzes the 3-nitration of tyrosine, leading to the formation of 3-nitrotyrosine (3NTyr). It was initially postulated that RufO acts on free L-tyrosine. However, further characterization demonstrates that free L-tyrosine is not the native substrate of RufO, although it could serve as a poor alternative under certain circumstances. It was subsequently demonstrated that RufO nitrates a biarylitide-type ribosomal pentapeptide precursor (Met-Arg-Tyr-Leu-His or MRYLH), which is encoded by bytA in the rufomycin gene cluster, producing the ribosomally synthesized and post-translationally modified peptide MR(NO(2)-Tyr)LH. Following the RufO-catalyzed nitration, the nitrated tyrosine (3-NO2-Tyr), key for antibiotic activity, is cleaved out by a dedicated aminopeptidase, before being activated and incorporated into the non-ribosomal peptide chain by the rufomycin synthetase assembly line (Ref.2). RufO can also nitrate the synthetic pentapeptide Nle-RYLH, where norleucine (Nle) is used to avoid non- enzyme catalyzed Met oxidation (Ref.2). It cannot use phenylalanine, tryptophan, 4-hydroxyphenylpyruvate or 4-aminophenylalanine.","Involved in the biosynthesis of the anthracyclines carminomycin and daunorubicin (daunomycin) which are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. In vitro, catalyzes the C-13 hydroxylation of 13-deoxycarminomycin and 13-deoxydaunorubicin to yield 13-dihydrocarminomycin and 13-dihydrodaunorubicin, respectively, as the final products.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497,GO:0004497; GO:0005506; GO:0016705,GO:0016705,GO:0004497,GO:0004497,0.5872,0.8898,0.5872,0.5872,0.5872,5,0.6477,0.1225,no
RUFO_STRAR,A0A224AU14,Protein2Text,Bacteria,394,"Cytochrome P450 involved in the biosynthesis of rufomycins, a class of cyclic heptapeptides with anti-mycobacterial activity. Catalyzes the 3-nitration of tyrosine, leading to the formation of 3-nitrotyrosine (3NTyr). It was initially postulated that RufO acts on free L-tyrosine. However, further characterization demonstrates that free L-tyrosine is not the native substrate of RufO, although it could serve as a poor alternative under certain circumstances. It was subsequently demonstrated that RufO nitrates a biarylitide-type ribosomal pentapeptide precursor (Met-Arg-Tyr-Leu-His or MRYLH), which is encoded by bytA in the rufomycin gene cluster, producing the ribosomally synthesized and post-translationally modified peptide MR(NO(2)-Tyr)LH. Following the RufO-catalyzed nitration, the nitrated tyrosine (3-NO2-Tyr), key for antibiotic activity, is cleaved out by a dedicated aminopeptidase, before being activated and incorporated into the non-ribosomal peptide chain by the rufomycin synthetase assembly line (Ref.2). RufO can also nitrate the synthetic pentapeptide Nle-RYLH, where norleucine (Nle) is used to avoid non- enzyme catalyzed Met oxidation (Ref.2). It cannot use phenylalanine, tryptophan, 4-hydroxyphenylpyruvate or 4-aminophenylalanine.","This protein is involved in catalyzing the oxidation of 2-ethyl-2-(hydroxymethyl)-1,3-dioxolane-4-methanol (2- hydroxymethyl-1,3-dioxolane-4-methanol).",Vague,Vague,Vague,No,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0016491,GO:0016491,,GO:0016491,GO:0016491,0.5572,0.5572,,0.5572,0.5572,4,0.5572,0.1225,no
RUFO_STRAR,A0A224AU14,Reference,Bacteria,394,"Cytochrome P450 involved in the biosynthesis of rufomycins, a class of cyclic heptapeptides with anti-mycobacterial activity. Catalyzes the 3-nitration of tyrosine, leading to the formation of 3-nitrotyrosine (3NTyr). It was initially postulated that RufO acts on free L-tyrosine. However, further characterization demonstrates that free L-tyrosine is not the native substrate of RufO, although it could serve as a poor alternative under certain circumstances. It was subsequently demonstrated that RufO nitrates a biarylitide-type ribosomal pentapeptide precursor (Met-Arg-Tyr-Leu-His or MRYLH), which is encoded by bytA in the rufomycin gene cluster, producing the ribosomally synthesized and post-translationally modified peptide MR(NO(2)-Tyr)LH. Following the RufO-catalyzed nitration, the nitrated tyrosine (3-NO2-Tyr), key for antibiotic activity, is cleaved out by a dedicated aminopeptidase, before being activated and incorporated into the non-ribosomal peptide chain by the rufomycin synthetase assembly line (Ref.2). RufO can also nitrate the synthetic pentapeptide Nle-RYLH, where norleucine (Nle) is used to avoid non- enzyme catalyzed Met oxidation (Ref.2). It cannot use phenylalanine, tryptophan, 4-hydroxyphenylpyruvate or 4-aminophenylalanine.","Cytochrome P450 involved in the biosynthesis of rufomycins, a class of cyclic heptapeptides with anti-mycobacterial activity. Catalyzes the 3-nitration of tyrosine, leading to the formation of 3-nitrotyrosine (3NTyr). It was initially postulated that RufO acts on free L-tyrosine. However, further characterization demonstrates that free L-tyrosine is not the native substrate of RufO, although it could serve as a poor alternative under certain circumstances. It was subsequently demonstrated that RufO nitrates a biarylitide-type ribosomal pentapeptide precursor (Met-Arg-Tyr-Leu-His or MRYLH), which is encoded by bytA in the rufomycin gene cluster, producing the ribosomally synthesized and post-translationally modified peptide MR(NO(2)-Tyr)LH. Following the RufO-catalyzed nitration, the nitrated tyrosine (3-NO2-Tyr), key for antibiotic activity, is cleaved out by a dedicated aminopeptidase, before being activated and incorporated into the non-ribosomal peptide chain by the rufomycin synthetase assembly line (Ref.2). RufO can also nitrate the synthetic pentapeptide Nle-RYLH, where norleucine (Nle) is used to avoid non- enzyme catalyzed Met oxidation (Ref.2). It cannot use phenylalanine, tryptophan, 4-hydroxyphenylpyruvate or 4-aminophenylalanine.",,,,,,,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497,GO:0004497,GO:0004497,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,0.5872,0.5872,0.5872,0.9516,0.9516,5,0.733,0.1225,no
TYR1_HAHS4,A0A261GRE4,ESM2Text,Bacteria,466,"Copper-containing oxidase that catalyzes the conversion of L- tyrosine to L-dopa and then to L-dopaquinone. Can use various phenols such as p-coumaric acid, phenol, pyrocatechol, syringol or pyrogallol. Accepts several of the constituents of lignin and potentially participates in lignin functionalization.",This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004097; GO:0046872; GO:0004503,GO:0016682; GO:0005507,GO:0016491; GO:0005507,GO:0005507; GO:0016682,GO:0016491,GO:0016491; GO:0005507,0.6932,0.6383,0.6932,0.452,0.6383,5,0.623,0.3228,no
TYR1_HAHS4,A0A261GRE4,Prot2Text,Bacteria,466,"Copper-containing oxidase that catalyzes the conversion of L- tyrosine to L-dopa and then to L-dopaquinone. Can use various phenols such as p-coumaric acid, phenol, pyrocatechol, syringol or pyrogallol. Accepts several of the constituents of lignin and potentially participates in lignin functionalization.",Catalyzes the oxidation of mono- and o-diphenols to o-diquinones.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004097; GO:0046872; GO:0004503,GO:0016682; GO:0005507,GO:0004097; GO:0005507,GO:0016682,GO:0005507; GO:0016491,GO:0008471,0.6932,0.8014,0.5073,0.6383,0.0,5,0.528,0.3228,no
TYR1_HAHS4,A0A261GRE4,ProtT3,Bacteria,466,"Copper-containing oxidase that catalyzes the conversion of L- tyrosine to L-dopa and then to L-dopaquinone. Can use various phenols such as p-coumaric acid, phenol, pyrocatechol, syringol or pyrogallol. Accepts several of the constituents of lignin and potentially participates in lignin functionalization.",This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Belongs to the tyrosinase family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004097; GO:0046872; GO:0004503,GO:0004503; GO:0005507,GO:0004503,GO:0004503; GO:0005507,GO:0004503; GO:0005507,GO:0004503,0.8014,0.6368,0.8014,0.8014,0.6368,5,0.7356,0.3228,no
TYR1_HAHS4,A0A261GRE4,ProtTale,Bacteria,466,"Copper-containing oxidase that catalyzes the conversion of L- tyrosine to L-dopa and then to L-dopaquinone. Can use various phenols such as p-coumaric acid, phenol, pyrocatechol, syringol or pyrogallol. Accepts several of the constituents of lignin and potentially participates in lignin functionalization.",This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004097; GO:0046872; GO:0004503,GO:0004097,GO:0005507; GO:0016491,GO:0016491; GO:0005507,GO:0005507; GO:0016491,GO:0005507; GO:0016682,0.6381,0.6383,0.6383,0.6383,0.6932,5,0.6492,0.3228,no
TYR1_HAHS4,A0A261GRE4,Protein2Text,Bacteria,466,"Copper-containing oxidase that catalyzes the conversion of L- tyrosine to L-dopa and then to L-dopaquinone. Can use various phenols such as p-coumaric acid, phenol, pyrocatechol, syringol or pyrogallol. Accepts several of the constituents of lignin and potentially participates in lignin functionalization.","This protein is a monophenol monooxygenase, which is an enzyme that catalyzes the oxidation of monophenols to diphenols using molecular oxygen. In the case of this protein, it is likely involved in the oxidation of a specific monophenol substrate, possibly in the process of melanin biosynthesis.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004097; GO:0046872; GO:0004503,GO:0004503,GO:0004503,GO:0004503,GO:0004503,GO:0004503,0.6368,0.6368,0.6368,0.6368,0.6368,5,0.6368,0.3228,no
TYR1_HAHS4,A0A261GRE4,Reference,Bacteria,466,"Copper-containing oxidase that catalyzes the conversion of L- tyrosine to L-dopa and then to L-dopaquinone. Can use various phenols such as p-coumaric acid, phenol, pyrocatechol, syringol or pyrogallol. Accepts several of the constituents of lignin and potentially participates in lignin functionalization.","Copper-containing oxidase that catalyzes the conversion of L- tyrosine to L-dopa and then to L-dopaquinone. Can use various phenols such as p-coumaric acid, phenol, pyrocatechol, syringol or pyrogallol. Accepts several of the constituents of lignin and potentially participates in lignin functionalization.",,,,,,,GO:0004097; GO:0046872; GO:0004503,GO:0004503,GO:0004503,GO:0004503,GO:0004503; GO:0005507,GO:0004503; GO:0005507,0.6368,0.6368,0.6368,0.8014,0.8014,5,0.7026,0.3228,no
HYLA_CUTAC,A0A2B7ICX0,ESM2Text,Bacteria,826,"Degrades hyaluronic acid (HA) into large-sized HA oligosaccharides, including tetrasaccharide HA (HA-4), hexasaccharide HA (HA-6) and higher molecular weight HA, and to a lesser extent into HA disaccharides (HA-2). Involved in the pathogenesis of acne. HA degradation products induce secretion of proinflammatory cytokines (IL- 6, IL-8 and TNF) from human HaCaT keratinocyte cell line and from mouse bone marrow derived macrophages (BMDMs). Produced HA fragments also direct robust TLR2-dependent inflammation in the mouse model of acne.","Broad-specificity muraminidase, which acts in concert with the Na(+)-dependent Na(+) antiporter Na(+) to produce an exolytic pyridoxal p-aminobenzoate. Has a preference for muraminid C6 and has extremely low activity towards pyridoxal and pyridoxamine. Is not active against pyridoxal, pyridoxamine, pyridoxamine-N-acetyl-pyridine, pyridoxamine-N-acetyl-mannosamine, pyridoxamine-N-oxide, pyridoxamine-N-oxide, pyridoxamine-N-oxide, or pyridoxamine-N-oxide.",No,No,No,No,No,not-Yes,GO:0030246; GO:0030340,GO:0016798,,,,,0.2609,,,,,1,0.2609,0.2184,no
HYLA_CUTAC,A0A2B7ICX0,Prot2Text,Bacteria,826,"Degrades hyaluronic acid (HA) into large-sized HA oligosaccharides, including tetrasaccharide HA (HA-4), hexasaccharide HA (HA-6) and higher molecular weight HA, and to a lesser extent into HA disaccharides (HA-2). Involved in the pathogenesis of acne. HA degradation products induce secretion of proinflammatory cytokines (IL- 6, IL-8 and TNF) from human HaCaT keratinocyte cell line and from mouse bone marrow derived macrophages (BMDMs). Produced HA fragments also direct robust TLR2-dependent inflammation in the mouse model of acne.",Active on carboxymethylcellulose and laminarioligosaccharides.,No,No,No,Maybe,No,not-Yes,GO:0030246; GO:0030340,GO:0004553,GO:0008810,GO:0004553,GO:0008810,GO:0008810,0.2172,0.1859,0.2172,0.1859,0.1859,5,0.1984,0.2184,no
HYLA_CUTAC,A0A2B7ICX0,ProtT3,Bacteria,826,"Degrades hyaluronic acid (HA) into large-sized HA oligosaccharides, including tetrasaccharide HA (HA-4), hexasaccharide HA (HA-6) and higher molecular weight HA, and to a lesser extent into HA disaccharides (HA-2). Involved in the pathogenesis of acne. HA degradation products induce secretion of proinflammatory cytokines (IL- 6, IL-8 and TNF) from human HaCaT keratinocyte cell line and from mouse bone marrow derived macrophages (BMDMs). Produced HA fragments also direct robust TLR2-dependent inflammation in the mouse model of acne.","Hydrolyzes the terminal alpha-1,4-linked glucuronic acid residues of chondroitin sulfate and dermatan sulfate. Secreted. Belongs to the polysaccharide lyase 9 family",No,No,Maybe,Maybe,Maybe,not-Yes,GO:0030246; GO:0030340,GO:0016837,GO:0016829,GO:0016829,GO:0030341,GO:0016829,0.6324,0.4887,0.4887,0.5386,0.4887,5,0.5274,0.2184,no
HYLA_CUTAC,A0A2B7ICX0,ProtTale,Bacteria,826,"Degrades hyaluronic acid (HA) into large-sized HA oligosaccharides, including tetrasaccharide HA (HA-4), hexasaccharide HA (HA-6) and higher molecular weight HA, and to a lesser extent into HA disaccharides (HA-2). Involved in the pathogenesis of acne. HA degradation products induce secretion of proinflammatory cytokines (IL- 6, IL-8 and TNF) from human HaCaT keratinocyte cell line and from mouse bone marrow derived macrophages (BMDMs). Produced HA fragments also direct robust TLR2-dependent inflammation in the mouse model of acne.",Catalyzes the hydrolytic cleavage of alpha-(1->6) glycosidic linkages in chondroitin sulfate (CS) and dermatan sulfate (DS). CS and DS are major glycosaminoglycans (GAGs) that constitute the extracellular matrix.,No,No,No,Maybe,Maybe,not-Yes,GO:0030246; GO:0030340,GO:0016798,GO:0004553,GO:0016798,GO:0016798,GO:0004553,0.2609,0.2172,0.2609,0.2609,0.2172,5,0.2434,0.2184,no
HYLA_CUTAC,A0A2B7ICX0,Protein2Text,Bacteria,826,"Degrades hyaluronic acid (HA) into large-sized HA oligosaccharides, including tetrasaccharide HA (HA-4), hexasaccharide HA (HA-6) and higher molecular weight HA, and to a lesser extent into HA disaccharides (HA-2). Involved in the pathogenesis of acne. HA degradation products induce secretion of proinflammatory cytokines (IL- 6, IL-8 and TNF) from human HaCaT keratinocyte cell line and from mouse bone marrow derived macrophages (BMDMs). Produced HA fragments also direct robust TLR2-dependent inflammation in the mouse model of acne.",This protein is a galactosidase.,No,No,No,No,No,not-Yes,GO:0030246; GO:0030340,GO:0004553,GO:0004553,,,GO:0004553,0.2172,0.2172,,,0.2172,3,0.2172,0.2184,no
HYLA_CUTAC,A0A2B7ICX0,Reference,Bacteria,826,"Degrades hyaluronic acid (HA) into large-sized HA oligosaccharides, including tetrasaccharide HA (HA-4), hexasaccharide HA (HA-6) and higher molecular weight HA, and to a lesser extent into HA disaccharides (HA-2). Involved in the pathogenesis of acne. HA degradation products induce secretion of proinflammatory cytokines (IL- 6, IL-8 and TNF) from human HaCaT keratinocyte cell line and from mouse bone marrow derived macrophages (BMDMs). Produced HA fragments also direct robust TLR2-dependent inflammation in the mouse model of acne.","Degrades hyaluronic acid (HA) into large-sized HA oligosaccharides, including tetrasaccharide HA (HA-4), hexasaccharide HA (HA-6) and higher molecular weight HA, and to a lesser extent into HA disaccharides (HA-2). Involved in the pathogenesis of acne. HA degradation products induce secretion of proinflammatory cytokines (IL- 6, IL-8 and TNF) from human HaCaT keratinocyte cell line and from mouse bone marrow derived macrophages (BMDMs). Produced HA fragments also direct robust TLR2-dependent inflammation in the mouse model of acne.",,,,,,,GO:0030246; GO:0030340,GO:0004415,GO:0004415,GO:0004415,GO:0016798,GO:0016798,0.1628,0.1628,0.1628,0.2609,0.2609,5,0.202,0.2184,no
C1GLT_BIOGL,A0A2C9JXL4,ESM2Text,Eukaryota,388,"Glycosyltransferase that generates the core 1 O-glycan Gal- beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins.","Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016263; GO:0030145; GO:0000166,GO:0016757,GO:0016757,GO:0016263,GO:0016263,GO:0016757,0.2858,0.2858,0.5322,0.5322,0.2858,5,0.3844,0.3388,no
C1GLT_BIOGL,A0A2C9JXL4,Prot2Text,Eukaryota,388,"Glycosyltransferase that generates the core 1 O-glycan Gal- beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins.","Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016263; GO:0030145; GO:0000166,GO:0016757,GO:0016263,GO:0016263,GO:0016757,GO:0016263,0.2858,0.5322,0.5322,0.2858,0.5322,5,0.4336,0.3388,no
C1GLT_BIOGL,A0A2C9JXL4,ProtT3,Eukaryota,388,"Glycosyltransferase that generates the core 1 O-glycan Gal- beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins.","Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Membrane; Single-pass type II membrane protein. Belongs to the glycosyltransferase 31 family. Beta3-Gal-T subfamily",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016263; GO:0030145; GO:0000166,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.2858,0.2858,0.2858,0.2858,0.2858,5,0.2858,0.3388,no
C1GLT_BIOGL,A0A2C9JXL4,ProtTale,Eukaryota,388,"Glycosyltransferase that generates the core 1 O-glycan Gal- beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins.","Glycosyltransferase that may catalyze the transfer of N-acetyl-D-galactosamine (GalNAc) from UDP-GalNAc in a beta1,3-linkage to a Ser or Thr residue. Plays a role in the biosynthesis of alpha-(1,3)-fucosyl-beta-1,4-GlcNAc-2-O-Ser/Thr glycan structures that are present in selectin ligands.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016263; GO:0030145; GO:0000166,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.2858,0.2858,0.2858,0.2858,0.2858,5,0.2858,0.3388,no
C1GLT_BIOGL,A0A2C9JXL4,Protein2Text,Eukaryota,388,"Glycosyltransferase that generates the core 1 O-glycan Gal- beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins.","The molecular function of this protein is O-linked glycosylation, specifically involved in the transfer of GalNAc to the Ser or Thr residue of a protein.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016263; GO:0030145; GO:0000166,GO:0004653,GO:0004653,GO:0004653,GO:0004653,GO:0004653,0.3283,0.3283,0.3283,0.3283,0.3283,5,0.3283,0.3388,no
C1GLT_BIOGL,A0A2C9JXL4,Reference,Eukaryota,388,"Glycosyltransferase that generates the core 1 O-glycan Gal- beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins.","Glycosyltransferase that generates the core 1 O-glycan Gal- beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins.",,,,,,,GO:0016263; GO:0030145; GO:0000166,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.2858,0.2858,0.2858,0.2858,0.2858,5,0.2858,0.3388,no
CFOL_ASPCN,A0A2I2F2I5,ESM2Text,Eukaryota,694,"Acetolactate synthase catalytic subunit, mitochondrial; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Is not direcly involved in chlorflavonin biosynthesis but acts as a self-resistant protein that effectively confers chlorflavonin resistance to the native host. As a catalytic subunit of mitochondrial acetolactate synthase, catalyzes the first of a series of common steps in the biosynthesis of the branched-chain amino acids. Catalyzes the irreversible decarboxylation of pyruvate to a bound hydroxyethyl group that then condenses with either a second pyruvate molecule to form 2-acetolactate (AL) or with 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate (AHB). The first product is the precursor for valine and leucine biosynthesis, while the second leads to isoleucine.","Catalytic subunit of mitochondrial acetolactate synthase, which catalyzes a common reaction in the aerobic type I branched-chain alpha-keto acid cycle. branched-chain alpha-keto acids are acid-base substrates that serve as primers for a number of long-chain fatty acids (LCFA).",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0003984; GO:0050660; GO:0000287; GO:0030976,GO:0003984,GO:0003984,GO:0003984,GO:0003984,GO:0003984,0.4519,0.4519,0.4519,0.4519,0.4519,5,0.4519,0.2617,no
CFOL_ASPCN,A0A2I2F2I5,Prot2Text,Eukaryota,694,"Acetolactate synthase catalytic subunit, mitochondrial; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Is not direcly involved in chlorflavonin biosynthesis but acts as a self-resistant protein that effectively confers chlorflavonin resistance to the native host. As a catalytic subunit of mitochondrial acetolactate synthase, catalyzes the first of a series of common steps in the biosynthesis of the branched-chain amino acids. Catalyzes the irreversible decarboxylation of pyruvate to a bound hydroxyethyl group that then condenses with either a second pyruvate molecule to form 2-acetolactate (AL) or with 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate (AHB). The first product is the precursor for valine and leucine biosynthesis, while the second leads to isoleucine.","Catalytic subunit of the branched-chain alpha-keto dehydrogenase complex, the first enzyme in the valine, leucine and isoleucine catabolic pathways. The valine and leucine catabolic pathways respectively transform alpha-ketoacid metabolism into the alpha-oxidation cycles. In a first reaction, the alpha-keto acid is transferred from the substrate by the two-step valine pathway to the succinyl-CoA starter unit, where a ketone is formed. Subsequently, the alpha-keto dehydrogenase catalyzes the overall conversion of the two-step valine pathway to the alpha-oxidation product branched-chain alpha-keto acid.",No,No,No,No,No,not-Yes,GO:0003984; GO:0050660; GO:0000287; GO:0030976,GO:0003863,GO:0003863,GO:0003863,GO:0016746,GO:0003863,0.1389,0.1389,0.1389,0.284,0.1389,5,0.1679,0.2617,no
CFOL_ASPCN,A0A2I2F2I5,ProtT3,Eukaryota,694,"Acetolactate synthase catalytic subunit, mitochondrial; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Is not direcly involved in chlorflavonin biosynthesis but acts as a self-resistant protein that effectively confers chlorflavonin resistance to the native host. As a catalytic subunit of mitochondrial acetolactate synthase, catalyzes the first of a series of common steps in the biosynthesis of the branched-chain amino acids. Catalyzes the irreversible decarboxylation of pyruvate to a bound hydroxyethyl group that then condenses with either a second pyruvate molecule to form 2-acetolactate (AL) or with 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate (AHB). The first product is the precursor for valine and leucine biosynthesis, while the second leads to isoleucine.",Mitochondrion. Belongs to the TPP enzyme family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0003984; GO:0050660; GO:0000287; GO:0030976,,,,,,,,,,,0,,0.2617,no
CFOL_ASPCN,A0A2I2F2I5,ProtTale,Eukaryota,694,"Acetolactate synthase catalytic subunit, mitochondrial; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Is not direcly involved in chlorflavonin biosynthesis but acts as a self-resistant protein that effectively confers chlorflavonin resistance to the native host. As a catalytic subunit of mitochondrial acetolactate synthase, catalyzes the first of a series of common steps in the biosynthesis of the branched-chain amino acids. Catalyzes the irreversible decarboxylation of pyruvate to a bound hydroxyethyl group that then condenses with either a second pyruvate molecule to form 2-acetolactate (AL) or with 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate (AHB). The first product is the precursor for valine and leucine biosynthesis, while the second leads to isoleucine.","Peroxisomal 2-hydroxyacyl-CoA lyase involved in the degradation of fatty-acyl-CoA. Catalyzes the cleavage of the carbon-carbon bond of a fatty acyl-CoA thioester, yielding acetyl-CoA and an acyl-CoA.",No,No,No,No,No,not-Yes,GO:0003984; GO:0050660; GO:0000287; GO:0030976,GO:0016829,GO:0016829,GO:0047774,GO:0016829; GO:0003824,GO:0016829,0.2377,0.2377,0.1389,0.3222,0.2377,5,0.2348,0.2617,no
CFOL_ASPCN,A0A2I2F2I5,Protein2Text,Eukaryota,694,"Acetolactate synthase catalytic subunit, mitochondrial; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Is not direcly involved in chlorflavonin biosynthesis but acts as a self-resistant protein that effectively confers chlorflavonin resistance to the native host. As a catalytic subunit of mitochondrial acetolactate synthase, catalyzes the first of a series of common steps in the biosynthesis of the branched-chain amino acids. Catalyzes the irreversible decarboxylation of pyruvate to a bound hydroxyethyl group that then condenses with either a second pyruvate molecule to form 2-acetolactate (AL) or with 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate (AHB). The first product is the precursor for valine and leucine biosynthesis, while the second leads to isoleucine.","This protein is involved in catalyzing the conversion of acetaldehyde to acetyl-CoA, a key step in the metabolism of ethanol and other alcohols. It is a part of the alcohol dehydrogenase enzyme family, which plays a crucial role in the breakdown of alcohols and the production of energy. In this specific protein, it is likely involved in the oxidation of acetaldehyde to acetyl-CoA, a reaction that is essential for the metabolism of ethanol and other alcohols. 

In more detail, this protein is involved in the following molecular function:

* Catalyzing the oxidation of acetaldehyde to acetyl-CoA, a key step in the metabolism of ethanol and other alcohols.
* Using NAD(+) as a cofactor to oxidize acetaldehyde to acetyl-CoA.
* Playing a crucial role in the breakdown of alcohols and the production of energy.

Overall, this protein is a key enzyme in the metabolism of alcohols and plays a crucial role in the breakdown of ethanol and other alcohols.",No,No,No,No,No,not-Yes,GO:0003984; GO:0050660; GO:0000287; GO:0030976,GO:0004029,GO:0004029; GO:0016620,GO:0008774,GO:0008774,GO:0004029,0.1222,0.169,0.1389,0.1389,0.1222,5,0.1382,0.2617,no
CFOL_ASPCN,A0A2I2F2I5,Reference,Eukaryota,694,"Acetolactate synthase catalytic subunit, mitochondrial; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Is not direcly involved in chlorflavonin biosynthesis but acts as a self-resistant protein that effectively confers chlorflavonin resistance to the native host. As a catalytic subunit of mitochondrial acetolactate synthase, catalyzes the first of a series of common steps in the biosynthesis of the branched-chain amino acids. Catalyzes the irreversible decarboxylation of pyruvate to a bound hydroxyethyl group that then condenses with either a second pyruvate molecule to form 2-acetolactate (AL) or with 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate (AHB). The first product is the precursor for valine and leucine biosynthesis, while the second leads to isoleucine.","Acetolactate synthase catalytic subunit, mitochondrial; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Is not direcly involved in chlorflavonin biosynthesis but acts as a self-resistant protein that effectively confers chlorflavonin resistance to the native host. As a catalytic subunit of mitochondrial acetolactate synthase, catalyzes the first of a series of common steps in the biosynthesis of the branched-chain amino acids. Catalyzes the irreversible decarboxylation of pyruvate to a bound hydroxyethyl group that then condenses with either a second pyruvate molecule to form 2-acetolactate (AL) or with 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate (AHB). The first product is the precursor for valine and leucine biosynthesis, while the second leads to isoleucine.",,,,,,,GO:0003984; GO:0050660; GO:0000287; GO:0030976,GO:0003984,GO:0003984,GO:0003984,GO:0003984; GO:0016984,GO:0003984; GO:0005524,0.4519,0.4519,0.4519,0.4158,0.6417,5,0.4826,0.2617,no
PRAF_MARPO,A0A2R6XIK6,ESM2Text,Eukaryota,1680,"RAF-like protein kinase acting as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process. Photosynthesis signaling kinase involved in the regulation of the sucrose metabolism involving PGM1. Necessary for optimal chloroplast electron transport rate (ETR).",Anti-apoptotic protein.,Vague,Vague,Vague,No,No,not-Yes,GO:0005524; GO:0004672; GO:0004674,,,,,,,,,,,0,,0.7325,yes
PRAF_MARPO,A0A2R6XIK6,Prot2Text,Eukaryota,1680,"RAF-like protein kinase acting as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process. Photosynthesis signaling kinase involved in the regulation of the sucrose metabolism involving PGM1. Necessary for optimal chloroplast electron transport rate (ETR).",SOSEKI proteins locally interpret global polarity cues and can influence cell division orientation to coordinate cell polarization relative to body axes.,Vague,Vague,No,No,Vague,not-Yes,GO:0005524; GO:0004672; GO:0004674,,,,,,,,,,,0,,0.7325,yes
PRAF_MARPO,A0A2R6XIK6,ProtT3,Eukaryota,1680,"RAF-like protein kinase acting as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process. Photosynthesis signaling kinase involved in the regulation of the sucrose metabolism involving PGM1. Necessary for optimal chloroplast electron transport rate (ETR).",Probable transcription factor involved in the regulation of cell elongation. Nucleus. Belongs to the EIN3 family,No,No,No,No,Vague,not-Yes,GO:0005524; GO:0004672; GO:0004674,GO:0003700,GO:0003700,GO:0003700,GO:0003700,GO:0003700,0.1253,0.1253,0.1253,0.1253,0.1253,5,0.1253,0.7325,yes
PRAF_MARPO,A0A2R6XIK6,ProtTale,Eukaryota,1680,"RAF-like protein kinase acting as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process. Photosynthesis signaling kinase involved in the regulation of the sucrose metabolism involving PGM1. Necessary for optimal chloroplast electron transport rate (ETR).",Probable transcription factor involved in the regulation of cell division and expansion during seedling development.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004672; GO:0004674,,,GO:0003700,,GO:0003700,,,0.1253,,0.1253,2,0.1253,0.7325,yes
PRAF_MARPO,A0A2R6XIK6,Protein2Text,Eukaryota,1680,"RAF-like protein kinase acting as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process. Photosynthesis signaling kinase involved in the regulation of the sucrose metabolism involving PGM1. Necessary for optimal chloroplast electron transport rate (ETR).","This protein is involved in ubiquitination, which is a post-translational modification that plays a crucial role in various cellular processes, including protein degradation, signaling, and regulation of gene expression.",No,No,No,No,No,not-Yes,GO:0005524; GO:0004672; GO:0004674,,,,,GO:0061630,,,,,0.2671,1,0.2671,0.7325,yes
PRAF_MARPO,A0A2R6XIK6,Reference,Eukaryota,1680,"RAF-like protein kinase acting as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process. Photosynthesis signaling kinase involved in the regulation of the sucrose metabolism involving PGM1. Necessary for optimal chloroplast electron transport rate (ETR).","RAF-like protein kinase acting as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process. Photosynthesis signaling kinase involved in the regulation of the sucrose metabolism involving PGM1. Necessary for optimal chloroplast electron transport rate (ETR).",,,,,,,GO:0005524; GO:0004672; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.9822,0.9822,0.7413,0.9822,0.9822,5,0.934,0.7325,yes
MARTX_VIBVL,A0A2S3R7M0,ESM2Text,Bacteria,5206,"[Multifunctional-autoprocessing repeats-in-toxin]: Precursor of a multifunctional toxin that causes destruction of the actin cytoskeleton by covalent cross-linking of actin and inactivation of Rho GTPases when translocated into the host cytoplasm. Upon translocation into the host cell, undergoes autoprocessing in cis mediated by the peptidase C80 domain (also named CPD domain): the protease activity is activated upon binding inositol hexakisphosphate (InsP6) present at the host cell membrane and delivers the Cysteine protease domain-containing toxin F3 chain to the host cytosol. The Cysteine protease domain- containing toxin F3 chain will then further cleave and release effector toxin chains that cause disassembly of the actin cytoskeleton and enhance V.vulnificus colonization of the small intestine, possibly by facilitating evasion of phagocytic cells.","A putative autotransporter, its function may be to transport oligomers of the GPI-anchored protein from the cytoplasm to the periplasm. A putative autotransporter which may play a role in host-pathogen interactions.",No,No,No,No,No,not-Yes,GO:0016746; GO:0008234; GO:0016874; GO:0008289; GO:0046872; GO:0090729,,,,,,,,,,,0,,0.3125,no
MARTX_VIBVL,A0A2S3R7M0,Prot2Text,Bacteria,5206,"[Multifunctional-autoprocessing repeats-in-toxin]: Precursor of a multifunctional toxin that causes destruction of the actin cytoskeleton by covalent cross-linking of actin and inactivation of Rho GTPases when translocated into the host cytoplasm. Upon translocation into the host cell, undergoes autoprocessing in cis mediated by the peptidase C80 domain (also named CPD domain): the protease activity is activated upon binding inositol hexakisphosphate (InsP6) present at the host cell membrane and delivers the Cysteine protease domain-containing toxin F3 chain to the host cytosol. The Cysteine protease domain- containing toxin F3 chain will then further cleave and release effector toxin chains that cause disassembly of the actin cytoskeleton and enhance V.vulnificus colonization of the small intestine, possibly by facilitating evasion of phagocytic cells.","A putative autotransporter, its function may be to transport oligomers of the GPI-anchored protein from the cytoplasm to the periplasm. A putative autotransporter which may play a role in host-pathogen interactions.",No,No,No,No,No,not-Yes,GO:0016746; GO:0008234; GO:0016874; GO:0008289; GO:0046872; GO:0090729,,,,,,,,,,,0,,0.3125,no
MARTX_VIBVL,A0A2S3R7M0,ProtT3,Bacteria,5206,"[Multifunctional-autoprocessing repeats-in-toxin]: Precursor of a multifunctional toxin that causes destruction of the actin cytoskeleton by covalent cross-linking of actin and inactivation of Rho GTPases when translocated into the host cytoplasm. Upon translocation into the host cell, undergoes autoprocessing in cis mediated by the peptidase C80 domain (also named CPD domain): the protease activity is activated upon binding inositol hexakisphosphate (InsP6) present at the host cell membrane and delivers the Cysteine protease domain-containing toxin F3 chain to the host cytosol. The Cysteine protease domain- containing toxin F3 chain will then further cleave and release effector toxin chains that cause disassembly of the actin cytoskeleton and enhance V.vulnificus colonization of the small intestine, possibly by facilitating evasion of phagocytic cells.",Murein-binding protein that mediates attachment of the fimbriae to the bacterial cell wall. Fimbrium. Cell outer membrane; Single-pass type II membrane protein. Belongs to the fimbrial protein family,No,No,No,No,No,not-Yes,GO:0016746; GO:0008234; GO:0016874; GO:0008289; GO:0046872; GO:0090729,,,,,,,,,,,0,,0.3125,no
MARTX_VIBVL,A0A2S3R7M0,ProtTale,Bacteria,5206,"[Multifunctional-autoprocessing repeats-in-toxin]: Precursor of a multifunctional toxin that causes destruction of the actin cytoskeleton by covalent cross-linking of actin and inactivation of Rho GTPases when translocated into the host cytoplasm. Upon translocation into the host cell, undergoes autoprocessing in cis mediated by the peptidase C80 domain (also named CPD domain): the protease activity is activated upon binding inositol hexakisphosphate (InsP6) present at the host cell membrane and delivers the Cysteine protease domain-containing toxin F3 chain to the host cytosol. The Cysteine protease domain- containing toxin F3 chain will then further cleave and release effector toxin chains that cause disassembly of the actin cytoskeleton and enhance V.vulnificus colonization of the small intestine, possibly by facilitating evasion of phagocytic cells.",Zinc metalloprotease that is secreted along with the toxin and plays a major role in host tissue damage. May also be involved in the evasion of the host immune response.,No,Maybe,No,No,Maybe,not-Yes,GO:0016746; GO:0008234; GO:0016874; GO:0008289; GO:0046872; GO:0090729,GO:0004222,GO:0004222; GO:0008270,GO:0004222; GO:0008270,GO:0004222,GO:0004222; GO:0008270,0.3002,0.4664,0.4664,0.3002,0.4664,5,0.3999,0.3125,no
MARTX_VIBVL,A0A2S3R7M0,Protein2Text,Bacteria,5206,"[Multifunctional-autoprocessing repeats-in-toxin]: Precursor of a multifunctional toxin that causes destruction of the actin cytoskeleton by covalent cross-linking of actin and inactivation of Rho GTPases when translocated into the host cytoplasm. Upon translocation into the host cell, undergoes autoprocessing in cis mediated by the peptidase C80 domain (also named CPD domain): the protease activity is activated upon binding inositol hexakisphosphate (InsP6) present at the host cell membrane and delivers the Cysteine protease domain-containing toxin F3 chain to the host cytosol. The Cysteine protease domain- containing toxin F3 chain will then further cleave and release effector toxin chains that cause disassembly of the actin cytoskeleton and enhance V.vulnificus colonization of the small intestine, possibly by facilitating evasion of phagocytic cells.","The molecular function of the protein is not specified in the given text. However, based on the name ""protein"", it is likely that it plays a role in binding or interacting with other molecules, such as carbohydrates or other proteins. This protein is a lectin, a type of carbohydrate-binding protein that helps plants to recognize and respond to their environment.",No,No,Vague,Vague,No,not-Yes,GO:0016746; GO:0008234; GO:0016874; GO:0008289; GO:0046872; GO:0090729,,,GO:0030246,GO:0030246,GO:0030246,,,0.3592,0.3592,0.3592,3,0.3592,0.3125,no
MARTX_VIBVL,A0A2S3R7M0,Reference,Bacteria,5206,"[Multifunctional-autoprocessing repeats-in-toxin]: Precursor of a multifunctional toxin that causes destruction of the actin cytoskeleton by covalent cross-linking of actin and inactivation of Rho GTPases when translocated into the host cytoplasm. Upon translocation into the host cell, undergoes autoprocessing in cis mediated by the peptidase C80 domain (also named CPD domain): the protease activity is activated upon binding inositol hexakisphosphate (InsP6) present at the host cell membrane and delivers the Cysteine protease domain-containing toxin F3 chain to the host cytosol. The Cysteine protease domain- containing toxin F3 chain will then further cleave and release effector toxin chains that cause disassembly of the actin cytoskeleton and enhance V.vulnificus colonization of the small intestine, possibly by facilitating evasion of phagocytic cells.","[Multifunctional-autoprocessing repeats-in-toxin]: Precursor of a multifunctional toxin that causes destruction of the actin cytoskeleton by covalent cross-linking of actin and inactivation of Rho GTPases when translocated into the host cytoplasm. Upon translocation into the host cell, undergoes autoprocessing in cis mediated by the peptidase C80 domain (also named CPD domain): the protease activity is activated upon binding inositol hexakisphosphate (InsP6) present at the host cell membrane and delivers the Cysteine protease domain-containing toxin F3 chain to the host cytosol. The Cysteine protease domain- containing toxin F3 chain will then further cleave and release effector toxin chains that cause disassembly of the actin cytoskeleton and enhance V.vulnificus colonization of the small intestine, possibly by facilitating evasion of phagocytic cells.",,,,,,,GO:0016746; GO:0008234; GO:0016874; GO:0008289; GO:0046872; GO:0090729,GO:0008234,GO:0008234,GO:0008234; GO:0004197,GO:0008234; GO:0004197,GO:0008234; GO:0004197,0.4474,0.4474,0.4915,0.4915,0.4915,5,0.4739,0.3125,no
AMPP1_LOTJA,A0A2Z5GDY5,ESM2Text,Eukaryota,658,"Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. Aminopeptidase that binds to the auxin transport inhibitor N-1- naphthylphthalamic acid (NPA). May play a negative role in the regulation of PIN auxin transport proteins. Involved in the coordination of the symbiotic nodule developmental program; prevents the formation of root nodules by regulating the expression of the nuclear transcription factor Y subunit (NF-YA1), a key nodulin (Ref.1).",Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0070006,GO:0004177,GO:0004177,GO:0004177,GO:0004177,GO:0004177,0.5317,0.5317,0.5317,0.5317,0.5317,5,0.5317,0.3767,no
AMPP1_LOTJA,A0A2Z5GDY5,Prot2Text,Eukaryota,658,"Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. Aminopeptidase that binds to the auxin transport inhibitor N-1- naphthylphthalamic acid (NPA). May play a negative role in the regulation of PIN auxin transport proteins. Involved in the coordination of the symbiotic nodule developmental program; prevents the formation of root nodules by regulating the expression of the nuclear transcription factor Y subunit (NF-YA1), a key nodulin (Ref.1).",Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0070006,GO:0004177,GO:0004177,GO:0004177,GO:0004177,GO:0004177,0.5317,0.5317,0.5317,0.5317,0.5317,5,0.5317,0.3767,no
AMPP1_LOTJA,A0A2Z5GDY5,ProtT3,Eukaryota,658,"Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. Aminopeptidase that binds to the auxin transport inhibitor N-1- naphthylphthalamic acid (NPA). May play a negative role in the regulation of PIN auxin transport proteins. Involved in the coordination of the symbiotic nodule developmental program; prevents the formation of root nodules by regulating the expression of the nuclear transcription factor Y subunit (NF-YA1), a key nodulin (Ref.1).",Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. Belongs to the peptidase M24B family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0070006,GO:0004177,GO:0004177,GO:0004177,GO:0004177,GO:0004177,0.5317,0.5317,0.5317,0.5317,0.5317,5,0.5317,0.3767,no
AMPP1_LOTJA,A0A2Z5GDY5,ProtTale,Eukaryota,658,"Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. Aminopeptidase that binds to the auxin transport inhibitor N-1- naphthylphthalamic acid (NPA). May play a negative role in the regulation of PIN auxin transport proteins. Involved in the coordination of the symbiotic nodule developmental program; prevents the formation of root nodules by regulating the expression of the nuclear transcription factor Y subunit (NF-YA1), a key nodulin (Ref.1).",Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0070006,GO:0004177,GO:0004177,GO:0004177,GO:0004177,GO:0004177,0.5317,0.5317,0.5317,0.5317,0.5317,5,0.5317,0.3767,no
AMPP1_LOTJA,A0A2Z5GDY5,Protein2Text,Eukaryota,658,"Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. Aminopeptidase that binds to the auxin transport inhibitor N-1- naphthylphthalamic acid (NPA). May play a negative role in the regulation of PIN auxin transport proteins. Involved in the coordination of the symbiotic nodule developmental program; prevents the formation of root nodules by regulating the expression of the nuclear transcription factor Y subunit (NF-YA1), a key nodulin (Ref.1).","The molecular function of this protein is aminopeptidase activity. It is a type of metalloaminopeptidase that catalyzes the removal of amino acids from the N-terminus of peptides. Specifically, it removes the penultimate amino acid from a substrate peptide. This protein is involved in the processing of peptides and the regulation of protein turnover in cells.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0070006,GO:0004177,GO:0004177,GO:0004177,GO:0004177,GO:0004177,0.5317,0.5317,0.5317,0.5317,0.5317,5,0.5317,0.3767,no
AMPP1_LOTJA,A0A2Z5GDY5,Reference,Eukaryota,658,"Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. Aminopeptidase that binds to the auxin transport inhibitor N-1- naphthylphthalamic acid (NPA). May play a negative role in the regulation of PIN auxin transport proteins. Involved in the coordination of the symbiotic nodule developmental program; prevents the formation of root nodules by regulating the expression of the nuclear transcription factor Y subunit (NF-YA1), a key nodulin (Ref.1).","Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. Aminopeptidase that binds to the auxin transport inhibitor N-1- naphthylphthalamic acid (NPA). May play a negative role in the regulation of PIN auxin transport proteins. Involved in the coordination of the symbiotic nodule developmental program; prevents the formation of root nodules by regulating the expression of the nuclear transcription factor Y subunit (NF-YA1), a key nodulin (Ref.1).",,,,,,,GO:0046872; GO:0070006,GO:0004177,GO:0004177,GO:0004177,GO:0004177,GO:0004177,0.5317,0.5317,0.5317,0.5317,0.5317,5,0.5317,0.3767,no
CRH1_BOTFB,A0A384J6C4,ESM2Text,Eukaryota,391,"Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta-glucan in the cell wall. Acts as an elicitor that triggers AMP-triggered immunity (PTI) and induces host resistance against Botryotinia fuckeliana. Cell death-inducing activity is independent of its transglycosylase activity. Plays a possible role in infection cushion formation.","Extracellular glycosidase which plays an important role in fungal pathogenesis. Involved in cell wall assembly and regeneration, and adherence to host cells.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008843; GO:0016757,GO:0016798,GO:0004553,GO:0004553,GO:0004553,GO:0016798,0.5611,0.6121,0.6121,0.6121,0.5611,5,0.5917,0.3365,no
CRH1_BOTFB,A0A384J6C4,Prot2Text,Eukaryota,391,"Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta-glucan in the cell wall. Acts as an elicitor that triggers AMP-triggered immunity (PTI) and induces host resistance against Botryotinia fuckeliana. Cell death-inducing activity is independent of its transglycosylase activity. Plays a possible role in infection cushion formation.","Extracellular glycosidase which plays an important role in fungal pathogenesis. Involved in cell wall assembly and regeneration, filamentation, and adherence to host cells.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008843; GO:0016757,GO:0004553,GO:0004553,GO:0016798,GO:0004553,GO:0016798,0.6121,0.6121,0.5611,0.6121,0.5611,5,0.5917,0.3365,no
CRH1_BOTFB,A0A384J6C4,ProtT3,Eukaryota,391,"Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta-glucan in the cell wall. Acts as an elicitor that triggers AMP-triggered immunity (PTI) and induces host resistance against Botryotinia fuckeliana. Cell death-inducing activity is independent of its transglycosylase activity. Plays a possible role in infection cushion formation.","Secreted, cell wall. Belongs to the glycosyl hydrolase 16 family",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008843; GO:0016757,GO:0016798,GO:0016798,GO:0016798,GO:0004553,GO:0016798,0.5611,0.5611,0.5611,0.6121,0.5611,5,0.5713,0.3365,no
CRH1_BOTFB,A0A384J6C4,ProtTale,Eukaryota,391,"Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta-glucan in the cell wall. Acts as an elicitor that triggers AMP-triggered immunity (PTI) and induces host resistance against Botryotinia fuckeliana. Cell death-inducing activity is independent of its transglycosylase activity. Plays a possible role in infection cushion formation.","Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta-glucan in the cell wall.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008843; GO:0016757,GO:0004568; GO:0016757,GO:0004568; GO:0016757,GO:0004568; GO:0016757,GO:0004568; GO:0016757,GO:0004568; GO:0016757,0.9346,0.9346,0.9346,0.9346,0.9346,5,0.9346,0.3365,no
CRH1_BOTFB,A0A384J6C4,Protein2Text,Eukaryota,391,"Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta-glucan in the cell wall. Acts as an elicitor that triggers AMP-triggered immunity (PTI) and induces host resistance against Botryotinia fuckeliana. Cell death-inducing activity is independent of its transglycosylase activity. Plays a possible role in infection cushion formation.","The molecular function of this protein is involved in breaking down complex carbohydrates, specifically in hydrolyzing beta-1,3-glucan, a type of polysaccharide found in plant cell walls. This enzyme plays a role in the degradation of plant biomass, helping to break down complex carbohydrates into simpler sugars that can be used by the fungus for energy and growth.",No,No,No,No,Maybe,not-Yes,GO:0008843; GO:0016757,GO:0052861,GO:0052861,GO:0042973,GO:0042973,GO:0052861,0.4471,0.4471,0.3943,0.3943,0.4471,5,0.426,0.3365,no
CRH1_BOTFB,A0A384J6C4,Reference,Eukaryota,391,"Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta-glucan in the cell wall. Acts as an elicitor that triggers AMP-triggered immunity (PTI) and induces host resistance against Botryotinia fuckeliana. Cell death-inducing activity is independent of its transglycosylase activity. Plays a possible role in infection cushion formation.","Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta-glucan in the cell wall. Acts as an elicitor that triggers AMP-triggered immunity (PTI) and induces host resistance against Botryotinia fuckeliana. Cell death-inducing activity is independent of its transglycosylase activity. Plays a possible role in infection cushion formation.",,,,,,,GO:0008843; GO:0016757,GO:0004568; GO:0016757,GO:0004568; GO:0016757,GO:0004568; GO:0016757,GO:0004568; GO:0016757,GO:0004568; GO:0016757,0.9346,0.9346,0.9346,0.9346,0.9346,5,0.9346,0.3365,no
CRH3_BOTFB,A0A384K116,ESM2Text,Eukaryota,444,"Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta-glucan in the cell wall.","Extracellular glycosidase which plays an important role in fungal pathogenesis. Involved in cell wall assembly and regeneration, filamentation, and adherence to host cells.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008843; GO:0016757,GO:0016798,GO:0004553,GO:0004553,GO:0004553,GO:0016798,0.5611,0.6121,0.6121,0.6121,0.5611,5,0.5917,0.3335,no
CRH3_BOTFB,A0A384K116,Prot2Text,Eukaryota,444,"Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta-glucan in the cell wall.","Probable glycosidase that plays a role in cell wall architecture. Required for the transfer of chitin to 1,6-beta-glucan in the cell wall.",Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0008843; GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0004553,GO:0016757,0.7508,0.7508,0.7508,0.6121,0.7508,5,0.7231,0.3335,no
CRH3_BOTFB,A0A384K116,ProtT3,Eukaryota,444,"Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta-glucan in the cell wall.","Catalyzes the formation of 1,3-beta-glucan chains in the cell wall. Secreted, cell wall Membrane; Lipid-anchor, GPI- anchor Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP). Belongs to the glycosyl hydrolase 16 family",No,No,No,No,Maybe,not-Yes,GO:0008843; GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0042124,GO:0016798,0.7508,0.7508,0.7508,0.4399,0.5611,5,0.6507,0.3335,no
CRH3_BOTFB,A0A384K116,ProtTale,Eukaryota,444,"Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta-glucan in the cell wall.","Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta-glucan in the cell wall.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008843; GO:0016757,GO:0004568; GO:0016757,GO:0004568; GO:0016757,GO:0004568; GO:0016757,GO:0004568; GO:0016757,GO:0004568; GO:0016757,0.9346,0.9346,0.9346,0.9346,0.9346,5,0.9346,0.3335,no
CRH3_BOTFB,A0A384K116,Protein2Text,Eukaryota,444,"Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta-glucan in the cell wall.","The molecular function of this protein is related to carbohydrate metabolism, specifically it is involved in breaking down or processing carbohydrate molecules. It is a type of lyase that is likely involved in the degradation of complex carbohydrates, such as those found in plant cell walls. The specific details of its function are not provided in the snippet, but it is generally involved in the breakdown of complex carbohydrates into simpler sugars.",No,Vague,Vague,No,Maybe,not-Yes,GO:0008843; GO:0016757,,,,,,,,,,,0,,0.3335,no
CRH3_BOTFB,A0A384K116,Reference,Eukaryota,444,"Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta-glucan in the cell wall.","Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta-glucan in the cell wall.",,,,,,,GO:0008843; GO:0016757,GO:0004568; GO:0016757,GO:0004568; GO:0016757,GO:0004568; GO:0016757,GO:0004568; GO:0016757,GO:0004568; GO:0016757,0.9346,0.9346,0.9346,0.9346,0.9346,5,0.9346,0.3335,no
FUMC_SCHMA,A0A3Q0KQY7,ESM2Text,Eukaryota,488,Catalyzes the reversible stereospecific interconversion of fumarate to L-malate. Fumarate metabolism in the cytosol plays a role during urea cycle and arginine metabolism; fumarate being a by-product of the urea cycle and amino-acid catabolism.,"Bifunctional enzyme that catalyzes the dehydration of methylene-H(4)MPT to methenyl-H(4)MPT(+). Also displays dihydrofolate reductase activity, thereby reducing dihydrofolate to methenate.",No,No,No,No,No,not-Yes,GO:0004333,GO:0004146,GO:0004146,GO:0004146,,GO:0004146,0.1998,0.1998,0.1998,,0.1998,4,0.1998,0.2159,no
FUMC_SCHMA,A0A3Q0KQY7,Prot2Text,Eukaryota,488,Catalyzes the reversible stereospecific interconversion of fumarate to L-malate. Fumarate metabolism in the cytosol plays a role during urea cycle and arginine metabolism; fumarate being a by-product of the urea cycle and amino-acid catabolism.,"Has aminomutase and, to a much lesser extent, ammonia-lyase activity. Primarily, catalyzes the rearrangement of L-tyrosine to R-beta-tyrosine, which is probably incorporated into secondary metabolite myxovalargin. The aminomutase activity exclusively produces R-beta-tyrosine.",No,No,No,No,No,not-Yes,GO:0004333,GO:0052092,,GO:0050025,GO:0050031,GO:0052076,0.0,,0.154,0.1998,0.0,4,0.0885,0.2159,no
FUMC_SCHMA,A0A3Q0KQY7,ProtT3,Eukaryota,488,Catalyzes the reversible stereospecific interconversion of fumarate to L-malate. Fumarate metabolism in the cytosol plays a role during urea cycle and arginine metabolism; fumarate being a by-product of the urea cycle and amino-acid catabolism.,Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate. Cytoplasm. Belongs to the class-II fumarase/aspartase family. Fumarase subfamily,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004333,GO:0004333,GO:0004333,GO:0004333,GO:0004333,GO:0004333,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2159,no
FUMC_SCHMA,A0A3Q0KQY7,ProtTale,Eukaryota,488,Catalyzes the reversible stereospecific interconversion of fumarate to L-malate. Fumarate metabolism in the cytosol plays a role during urea cycle and arginine metabolism; fumarate being a by-product of the urea cycle and amino-acid catabolism.,"Catalyzes both the decarboxylation of 2-oxoglutarate and the formation of succinate from oxaloacetate, generating pyruvate and CO(2).",No,No,No,No,No,not-Yes,GO:0004333,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.3987,0.3987,0.3987,0.3987,0.3987,5,0.3987,0.2159,no
FUMC_SCHMA,A0A3Q0KQY7,Protein2Text,Eukaryota,488,Catalyzes the reversible stereospecific interconversion of fumarate to L-malate. Fumarate metabolism in the cytosol plays a role during urea cycle and arginine metabolism; fumarate being a by-product of the urea cycle and amino-acid catabolism.,"The molecular function of this protein is a catalytic activity, specifically a type of isomerase activity that catalyzes the conversion of fumarate to L-malate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004333,GO:0004333,GO:0004333,GO:0004333,GO:0004333,GO:0004333,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2159,no
FUMC_SCHMA,A0A3Q0KQY7,Reference,Eukaryota,488,Catalyzes the reversible stereospecific interconversion of fumarate to L-malate. Fumarate metabolism in the cytosol plays a role during urea cycle and arginine metabolism; fumarate being a by-product of the urea cycle and amino-acid catabolism.,Catalyzes the reversible stereospecific interconversion of fumarate to L-malate. Fumarate metabolism in the cytosol plays a role during urea cycle and arginine metabolism; fumarate being a by-product of the urea cycle and amino-acid catabolism.,,,,,,,GO:0004333,GO:0004333,GO:0004333,GO:0004333,GO:0004333,GO:0004333,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2159,no
NPRS_SCHMA,A0A3Q0KR05,ESM2Text,Eukaryota,1227,Catalyzes the condensation of beta-alanine with tryptamine to form beta-alanyl-tryptamine (BATT). Beta-alanyl- tryptamine is an essential pheromone produced by the male that stimulates female sexual development during pairing.,"Acyl-CoA synthetase required for the activation of non-canonical poly-ubiquitin chains by intramolecular CoA. Catalyzes the activation of L-tyrosine by ATP-dependent adenylation at the 4-position to produce 4-membered ring-hydroxylated tyrosine. The non-canonical poly-ubiquitin chain contains the initiator methionine, which is non-canonical for certain initiator methionines, and adjacent to the peptidyl transferase PTCB. The formation of the 4-membered ring appears to be crucial for the activation of target non-canonical poly-ubiquitin chains. Acyl-CoA synthetase (aryl-CoA synthetase) that has specificity for linear and non-canonical poly-ubiquitin chains, and which is essential for cell growth and survival. The fatty acid synthetic pathway seems to be crucial for cell growth and survival. Acyl-CoA synthetase (aryl-CoA dehydrogenase) that has specificity for linear and non-canonical poly-ubiquitin chains, and which is essential for cell growth and survival. The fatty",No,No,No,No,No,not-Yes,GO:0003833,GO:0016874,,,,,0.6897,,,,,1,0.6897,0.2906,no
NPRS_SCHMA,A0A3Q0KR05,Prot2Text,Eukaryota,1227,Catalyzes the condensation of beta-alanine with tryptamine to form beta-alanyl-tryptamine (BATT). Beta-alanyl- tryptamine is an essential pheromone produced by the male that stimulates female sexual development during pairing.,Adenylate-forming synthetase (AAPS) that mediates the ATP-dependent conversion of prenylated phenylalanine and tyrosine into the hydroxylated phenylalanyl-CoA thioester and the formation of prenylated Cys-Gly conjugates. The prenyltransferase activity on tyrosine prenylated phenylalanyl-CoA is regulated by a Thr-Leu pair in the C-terminal domain. Also mediates prenylation of prenylated Fusarium oxysporum in a C-terminal domain. May be involved in the activation of a downstream mediator of prenylation in the production of prenylated antimicrobial peptides. Required for both formation and activity of the Fusarium oxysporum cell wall.,No,No,No,No,No,not-Yes,GO:0003833,GO:0016874,,,GO:0016874; GO:0005524,,0.6897,,,0.4809,,2,0.5853,0.2906,no
NPRS_SCHMA,A0A3Q0KR05,ProtT3,Eukaryota,1227,Catalyzes the condensation of beta-alanine with tryptamine to form beta-alanyl-tryptamine (BATT). Beta-alanyl- tryptamine is an essential pheromone produced by the male that stimulates female sexual development during pairing.,"Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), as well as fumonisins H1 (FH1), H2 (FH2), H3 (FH3), H4 (FH4), and H5 (FH5), which are carcinogenic mycotoxins",No,No,Maybe,Maybe,Vague,not-Yes,GO:0003833,GO:0016878,GO:0016405,GO:0016405,GO:0016878,GO:0016874,0.4645,0.4645,0.4645,0.4645,0.6897,5,0.5095,0.2906,no
NPRS_SCHMA,A0A3Q0KR05,ProtTale,Eukaryota,1227,Catalyzes the condensation of beta-alanine with tryptamine to form beta-alanyl-tryptamine (BATT). Beta-alanyl- tryptamine is an essential pheromone produced by the male that stimulates female sexual development during pairing.,Acts as a receptor for the polyketide synthase (PKS)-derived fungal secondary metabolite fusicoccin (FUS). Binds FUS with high affinity and mediates its nuclear localization via interaction with importin alpha. May play a role in FUS biosynthesis or regulation.,No,No,No,No,No,not-Yes,GO:0003833,,,,,,,,,,,0,,0.2906,no
NPRS_SCHMA,A0A3Q0KR05,Protein2Text,Eukaryota,1227,Catalyzes the condensation of beta-alanine with tryptamine to form beta-alanyl-tryptamine (BATT). Beta-alanyl- tryptamine is an essential pheromone produced by the male that stimulates female sexual development during pairing.,"This protein is a phospholipid biosynthetic enzyme, specifically a phosphatidic acid phosphatase. It catalyzes the dephosphorylation of phosphatidic acid (PA) to diacylglycerol (DAG), a key step in the biosynthesis of phospholipids. Phosphatidic acid is a precursor molecule for the synthesis of phospholipids, such as phosphatidylcholine, phosphatidylethanolamine, and phosphatidylinositol. DAG is also a signaling molecule that activates protein kinase C (PKC) and regulates various cellular processes, including cell proliferation, differentiation, and survival. This protein is involved in the regulation of phospholipid metabolism and signaling pathways in cells.",No,No,No,No,No,not-Yes,GO:0003833,GO:0008484,GO:0008484,GO:0008484,GO:0008484,GO:0008484,0.2742,0.2742,0.2742,0.2742,0.2742,5,0.2742,0.2906,no
NPRS_SCHMA,A0A3Q0KR05,Reference,Eukaryota,1227,Catalyzes the condensation of beta-alanine with tryptamine to form beta-alanyl-tryptamine (BATT). Beta-alanyl- tryptamine is an essential pheromone produced by the male that stimulates female sexual development during pairing.,Catalyzes the condensation of beta-alanine with tryptamine to form beta-alanyl-tryptamine (BATT). Beta-alanyl- tryptamine is an essential pheromone produced by the male that stimulates female sexual development during pairing.,,,,,,,GO:0003833,GO:0016746,GO:0016746,GO:0016881,GO:0016746,GO:0016874; GO:0005524,0.3284,0.3284,0.7025,0.3284,0.4809,5,0.4337,0.2906,no
OXDA_RASEM,A0A499UB99,ESM2Text,Eukaryota,368,"Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Enables the organism to utilize D-amino acids as a source of nutrients. Unusually, has high activity on D-glutamate.","This enzyme converts phyanose into zeta-carotene via the intermediate of phylloquinone, a precursor of ethylene.",No,No,No,No,No,not-Yes,GO:0003884; GO:0071949,,,,,,,,,,,0,,0.2575,no
OXDA_RASEM,A0A499UB99,Prot2Text,Eukaryota,368,"Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Enables the organism to utilize D-amino acids as a source of nutrients. Unusually, has high activity on D-glutamate.",This enzyme can effectively convert cephalosporin C into 7-beta-(5-carboxy-5-oxopentanamido)-cephalosporinic acid.,No,No,No,No,No,not-Yes,GO:0003884; GO:0071949,GO:0016491,GO:0003884,GO:0016491,GO:0016491,GO:0003884,0.3981,0.6869,0.3981,0.3981,0.6869,5,0.5136,0.2575,no
OXDA_RASEM,A0A499UB99,ProtT3,Eukaryota,368,"Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Enables the organism to utilize D-amino acids as a source of nutrients. Unusually, has high activity on D-glutamate.","Catalyzes the oxidative deamination of D-amino acids such as D-alanine, D-aspartate, D-glutamate, D-glutamine, D-histidine, D-isoleucine, D-leucine, D-methionine, D-phenylalanine, D-proline, D-serine, D-threonine, D-tyrosine and D-valine. Peroxisome. Belongs to the DAMOX/DASOX family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0003884; GO:0071949,GO:0033734,GO:0033734,GO:0033734,GO:0033734,GO:0003863,0.2193,0.2193,0.2193,0.2193,0.2193,5,0.2193,0.2575,no
OXDA_RASEM,A0A499UB99,ProtTale,Eukaryota,368,"Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Enables the organism to utilize D-amino acids as a source of nutrients. Unusually, has high activity on D-glutamate.",Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Enables the organism to utilize D-amino acids as a source of nutrients.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003884; GO:0071949,GO:0003884,GO:0003863,GO:0003884,GO:0003863,GO:0003884,0.6869,0.2193,0.6869,0.2193,0.6869,5,0.4999,0.2575,no
OXDA_RASEM,A0A499UB99,Protein2Text,Eukaryota,368,"Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Enables the organism to utilize D-amino acids as a source of nutrients. Unusually, has high activity on D-glutamate.",The molecular function of this protein is an amino acid oxidase.,Yes,Yes,Yes,Vague,Maybe,Yes,GO:0003884; GO:0071949,GO:0001678,GO:0004020,,GO:0016638,GO:0001678,0.0,0.1261,,0.4632,0.0,4,0.1473,0.2575,no
OXDA_RASEM,A0A499UB99,Reference,Eukaryota,368,"Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Enables the organism to utilize D-amino acids as a source of nutrients. Unusually, has high activity on D-glutamate.","Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Enables the organism to utilize D-amino acids as a source of nutrients. Unusually, has high activity on D-glutamate.",,,,,,,GO:0003884; GO:0071949,GO:0003884,GO:0003884,GO:0003884,GO:0033971,GO:0033734,0.6869,0.6869,0.6869,0.1389,0.2193,5,0.4838,0.2575,no
AAAD_PSICU,A0A4P1LYB6,ESM2Text,Eukaryota,1013,"Non-canonical aromatic amino acid decarboxylase that exhibits substrate permissiveness toward L-phenylalanine, L-tyrosine, and L- tryptophan, as well as chloro-tryptophan derivatives. Likely mediates an alternative route to psilocybin biosynthesis from L- tryptophan in psilocybin mushroom.",Catalyzes the decarboxylation of L-tyrosine to tyramine for use as a sole nitrogen source. Can also catalyze the decarboxylation of L-aspartate to produce beta-alanine for use as a sole nitrogen source.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0016830; GO:0003700; GO:0030170; GO:0043565,GO:0004837; GO:0016831,GO:0004837; GO:0004068,GO:0004837,GO:0004837,GO:0004837,0.4659,0.4198,0.3579,0.3579,0.3579,5,0.3919,0.4265,no
AAAD_PSICU,A0A4P1LYB6,Prot2Text,Eukaryota,1013,"Non-canonical aromatic amino acid decarboxylase that exhibits substrate permissiveness toward L-phenylalanine, L-tyrosine, and L- tryptophan, as well as chloro-tryptophan derivatives. Likely mediates an alternative route to psilocybin biosynthesis from L- tryptophan in psilocybin mushroom.","Catalyzes the decarboxylation of L-tyrosine to tyramine, which is converted to norbelladine, a precursor to all Amaryllidaceae alkaloids such as galanthamine, lycorine and haemanthamine, and including haemanthamine- and crinamine-type alkaloids, promising anticancer agents.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0016830; GO:0003700; GO:0030170; GO:0043565,GO:0004837,GO:0004837,GO:0004837,GO:0004837,GO:0004837,0.3579,0.3579,0.3579,0.3579,0.3579,5,0.3579,0.4265,no
AAAD_PSICU,A0A4P1LYB6,ProtT3,Eukaryota,1013,"Non-canonical aromatic amino acid decarboxylase that exhibits substrate permissiveness toward L-phenylalanine, L-tyrosine, and L- tryptophan, as well as chloro-tryptophan derivatives. Likely mediates an alternative route to psilocybin biosynthesis from L- tryptophan in psilocybin mushroom.",Catalyzes the decarboxylation of L-tryptophan to indole-3-acetic acid (IAA). Belongs to the group II decarboxylase family,Yes,Yes,Yes,Maybe,Yes,Yes,GO:0016830; GO:0003700; GO:0030170; GO:0043565,GO:0016831,GO:0016831,GO:0016831,GO:0004058,GO:0004058,0.4133,0.4133,0.4133,0.3579,0.3579,5,0.3911,0.4265,no
AAAD_PSICU,A0A4P1LYB6,ProtTale,Eukaryota,1013,"Non-canonical aromatic amino acid decarboxylase that exhibits substrate permissiveness toward L-phenylalanine, L-tyrosine, and L- tryptophan, as well as chloro-tryptophan derivatives. Likely mediates an alternative route to psilocybin biosynthesis from L- tryptophan in psilocybin mushroom.",Involved in sialic acid metabolism. Catalyzes the conversion of CMP-2-keto-3-deoxy-D-manno-octulosonate (KDO) to CMP-2-acetamido-2-deoxy-D-galactose (GalNAc).,No,No,No,No,No,not-Yes,GO:0016830; GO:0003700; GO:0030170; GO:0043565,GO:0016740,GO:0016740,,,,0.3045,0.3045,,,,2,0.3045,0.4265,no
AAAD_PSICU,A0A4P1LYB6,Protein2Text,Eukaryota,1013,"Non-canonical aromatic amino acid decarboxylase that exhibits substrate permissiveness toward L-phenylalanine, L-tyrosine, and L- tryptophan, as well as chloro-tryptophan derivatives. Likely mediates an alternative route to psilocybin biosynthesis from L- tryptophan in psilocybin mushroom.",This protein is involved in the molecular function of catalyzing the decarboxylation of aspartate to produce beta-alanine. This reaction is a key step in the biosynthesis of pyrimidine nucleotides.,No,No,No,No,Maybe,not-Yes,GO:0016830; GO:0003700; GO:0030170; GO:0043565,GO:0016841,GO:0004068,GO:0004068,GO:0016831,GO:0016831,0.2993,0.3579,0.3579,0.4133,0.4133,5,0.3683,0.4265,no
AAAD_PSICU,A0A4P1LYB6,Reference,Eukaryota,1013,"Non-canonical aromatic amino acid decarboxylase that exhibits substrate permissiveness toward L-phenylalanine, L-tyrosine, and L- tryptophan, as well as chloro-tryptophan derivatives. Likely mediates an alternative route to psilocybin biosynthesis from L- tryptophan in psilocybin mushroom.","Non-canonical aromatic amino acid decarboxylase that exhibits substrate permissiveness toward L-phenylalanine, L-tyrosine, and L- tryptophan, as well as chloro-tryptophan derivatives. Likely mediates an alternative route to psilocybin biosynthesis from L- tryptophan in psilocybin mushroom.",,,,,,,GO:0016830; GO:0003700; GO:0030170; GO:0043565,GO:0004058,GO:0004058,GO:0004058,GO:0004058,GO:0004058,0.3579,0.3579,0.3579,0.3579,0.3579,5,0.3579,0.4265,no
EIK2_PLABA,A0A509AH51,ESM2Text,Eukaryota,2724,"Phosphorylates translation factor eIF2alpha in salivary gland sporozoites during dormancy, which leads to an inhibition of protein translation and accumulation of stalled mRNAs into granules.","During stationary phase, promotes and stabilizes the 15S rRNA binding site by inhibiting the formation of an intra-S-phase complex.",No,No,No,No,No,not-Yes,GO:0005524; GO:0004694,,,,,,,,,,,0,,0.6946,yes
EIK2_PLABA,A0A509AH51,Prot2Text,Eukaryota,2724,"Phosphorylates translation factor eIF2alpha in salivary gland sporozoites during dormancy, which leads to an inhibition of protein translation and accumulation of stalled mRNAs into granules.","During stationary phase, promotes and stabilizes the 15S rRNA binding site by inhibiting the formation of an intra-S-phase complex.",No,No,No,No,No,not-Yes,GO:0005524; GO:0004694,GO:0003964,GO:0003964,GO:0003720,GO:0003720; GO:0003721,GO:0003720,0.2118,0.2118,0.1905,0.1905,0.1905,5,0.199,0.6946,yes
EIK2_PLABA,A0A509AH51,ProtT3,Eukaryota,2724,"Phosphorylates translation factor eIF2alpha in salivary gland sporozoites during dormancy, which leads to an inhibition of protein translation and accumulation of stalled mRNAs into granules.",Probable serine/threonine-protein kinase involved in meiosis. Nucleus. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004694,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,0.9546,0.9546,0.9546,0.9546,0.6242,5,0.8885,0.6946,yes
EIK2_PLABA,A0A509AH51,ProtTale,Eukaryota,2724,"Phosphorylates translation factor eIF2alpha in salivary gland sporozoites during dormancy, which leads to an inhibition of protein translation and accumulation of stalled mRNAs into granules.","Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Mediates the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Mediates the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P",No,No,No,No,No,not-Yes,GO:0005524; GO:0004694,GO:0016308,GO:0016301,GO:0016308; GO:0005524,GO:0016307,GO:0016308,0.3413,0.4257,0.7446,0.0,0.3413,5,0.3706,0.6946,yes
EIK2_PLABA,A0A509AH51,Protein2Text,Eukaryota,2724,"Phosphorylates translation factor eIF2alpha in salivary gland sporozoites during dormancy, which leads to an inhibition of protein translation and accumulation of stalled mRNAs into granules.","This protein is involved in the molecular function of DNA helicase, which is a type of enzyme that unwinds double-stranded DNA into single-stranded DNA. Specifically, it is a helicase involved in DNA replication and repair.",No,No,No,No,No,not-Yes,GO:0005524; GO:0004694,,,,,,,,,,,0,,0.6946,yes
EIK2_PLABA,A0A509AH51,Reference,Eukaryota,2724,"Phosphorylates translation factor eIF2alpha in salivary gland sporozoites during dormancy, which leads to an inhibition of protein translation and accumulation of stalled mRNAs into granules.","Phosphorylates translation factor eIF2alpha in salivary gland sporozoites during dormancy, which leads to an inhibition of protein translation and accumulation of stalled mRNAs into granules.",,,,,,,GO:0005524; GO:0004694,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004694,GO:0004694; GO:0005524,GO:0004674; GO:0005524,0.9546,0.9546,0.683,1.0,0.9546,5,0.9094,0.6946,yes
PK4_PLABA,A0A509AMC3,ESM2Text,Eukaryota,2591,"During the asexual blood stage, phosphorylates translation factor eIF2alpha in late schizonts resulting in protein translation inhibition. Plays a role in trophozoite differentiation into schizonts.",Involved in protein precursor import into chloroplasts. May be part of an intermediate translocation complex acting as a protein-conducting channel at the inner envelope.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004694,,,,,,,,,,,0,,0.6779,yes
PK4_PLABA,A0A509AMC3,Prot2Text,Eukaryota,2591,"During the asexual blood stage, phosphorylates translation factor eIF2alpha in late schizonts resulting in protein translation inhibition. Plays a role in trophozoite differentiation into schizonts.",Peroxisome-specific aspartic protease which is essential for the degradation of peroxisomes.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004694,GO:0004190,GO:0004190,GO:0004190,GO:0004190,GO:0004190,0.1762,0.1762,0.1762,0.1762,0.1762,5,0.1762,0.6779,yes
PK4_PLABA,A0A509AMC3,ProtT3,Eukaryota,2591,"During the asexual blood stage, phosphorylates translation factor eIF2alpha in late schizonts resulting in protein translation inhibition. Plays a role in trophozoite differentiation into schizonts.",Mitochondrion,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0004694,,,,,,,,,,,0,,0.6779,yes
PK4_PLABA,A0A509AMC3,ProtTale,Eukaryota,2591,"During the asexual blood stage, phosphorylates translation factor eIF2alpha in late schizonts resulting in protein translation inhibition. Plays a role in trophozoite differentiation into schizonts.","Serine/threonine-protein kinase involved in the regulation of centrosome cohesion and mitotic spindle formation. Phosphorylates AURKB/Aurora-B at 'Thr- 680', thereby promoting AURKB/Aurora-B activation, localization to the centrosome and chromosome segregation.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004694,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,0.9546,0.9546,0.9546,0.6242,0.9546,5,0.8885,0.6779,yes
PK4_PLABA,A0A509AMC3,Protein2Text,Eukaryota,2591,"During the asexual blood stage, phosphorylates translation factor eIF2alpha in late schizonts resulting in protein translation inhibition. Plays a role in trophozoite differentiation into schizonts.","This protein is a DNA-binding protein, which means it binds to DNA molecules. More specifically, it is a helicase, which is a type of enzyme that unwinds DNA duplexes into single strands.",No,No,No,No,No,not-Yes,GO:0005524; GO:0004694,GO:0003678; GO:0003677,GO:0004003; GO:0003677,GO:0003678,GO:0003678,GO:0003678; GO:0003677,0.1528,0.1528,0.1119,0.1119,0.1528,5,0.1364,0.6779,yes
PK4_PLABA,A0A509AMC3,Reference,Eukaryota,2591,"During the asexual blood stage, phosphorylates translation factor eIF2alpha in late schizonts resulting in protein translation inhibition. Plays a role in trophozoite differentiation into schizonts.","During the asexual blood stage, phosphorylates translation factor eIF2alpha in late schizonts resulting in protein translation inhibition. Plays a role in trophozoite differentiation into schizonts.",,,,,,,GO:0005524; GO:0004694,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004694,GO:0004694; GO:0005524,GO:0004674; GO:0005524,0.9546,0.9546,0.683,1.0,0.9546,5,0.9094,0.6779,yes
PMP1_PARBF,A0A5P3XKQ1,ESM2Text,Bacteria,1260,"[Paraclostridial mosquitocidal protein 1]: Neurotoxin active against Anopheles but not Aedes mosquitoes upon oral ingestion; expression of the ptox operon (ntnh-orfX1-orfX2-orfX3-pmp1) in B.thuringiensis kills Anopheles but not Aedes mosquito 3rd instar larvae. The ntnh-pmp1 construct is about half as toxic. PMP1 is toxic when injected directly into Anopheles or Aedes mosquito 3rd instar larvae, larvae no longer move, suggesting they are paralyzed. Adult mosquitoes (Anopheles or Aedes) and Drosophila lose the ability to fly in a dose-dependent manner by 24 hours after injection with 100 pg neurotoxin. Not toxic upon injection in mice.","Type VI secretion exported toxin that acts as an endochitinase on post-translational substrates, cleaving between the first and second codons of the C-terminus. It targets bacterial proteins through the endoplasmic reticulum (ER) and preferentially cleaves proteins in the trans-Golgi network (TGN). The resulting internalization into the endoplasmic reticulum membrane may cause disruption of the previously disassembled ER-localized secretion system.",No,No,No,No,No,not-Yes,GO:0004222; GO:0008320; GO:0090729; GO:0008270,GO:0004568,GO:0004568,GO:0004568,GO:0004568,,0.1906,0.1906,0.1906,0.1906,,4,0.1906,0.3245,no
PMP1_PARBF,A0A5P3XKQ1,Prot2Text,Bacteria,1260,"[Paraclostridial mosquitocidal protein 1]: Neurotoxin active against Anopheles but not Aedes mosquitoes upon oral ingestion; expression of the ptox operon (ntnh-orfX1-orfX2-orfX3-pmp1) in B.thuringiensis kills Anopheles but not Aedes mosquito 3rd instar larvae. The ntnh-pmp1 construct is about half as toxic. PMP1 is toxic when injected directly into Anopheles or Aedes mosquito 3rd instar larvae, larvae no longer move, suggesting they are paralyzed. Adult mosquitoes (Anopheles or Aedes) and Drosophila lose the ability to fly in a dose-dependent manner by 24 hours after injection with 100 pg neurotoxin. Not toxic upon injection in mice.",Toxin which activates the particulate form of guanylate cyclase and increases cyclic GMP levels within the host intestinal epithelial cells.,No,No,No,No,No,not-Yes,GO:0004222; GO:0008320; GO:0090729; GO:0008270,,,,,GO:0090729,,,,,0.5094,1,0.5094,0.3245,no
PMP1_PARBF,A0A5P3XKQ1,ProtT3,Bacteria,1260,"[Paraclostridial mosquitocidal protein 1]: Neurotoxin active against Anopheles but not Aedes mosquitoes upon oral ingestion; expression of the ptox operon (ntnh-orfX1-orfX2-orfX3-pmp1) in B.thuringiensis kills Anopheles but not Aedes mosquito 3rd instar larvae. The ntnh-pmp1 construct is about half as toxic. PMP1 is toxic when injected directly into Anopheles or Aedes mosquito 3rd instar larvae, larvae no longer move, suggesting they are paralyzed. Adult mosquitoes (Anopheles or Aedes) and Drosophila lose the ability to fly in a dose-dependent manner by 24 hours after injection with 100 pg neurotoxin. Not toxic upon injection in mice.",In the N-terminal section; belongs to the staphylococcal nuclease family. In the C-terminal section; belongs to the staphylococcal/streptococcal nuclease family,Vague,No,No,Vague,Vague,not-Yes,GO:0004222; GO:0008320; GO:0090729; GO:0008270,GO:0004518,GO:0004519,GO:0004519,GO:0004519,GO:0004518,0.2061,0.1736,0.1736,0.1736,0.2061,5,0.1866,0.3245,no
PMP1_PARBF,A0A5P3XKQ1,ProtTale,Bacteria,1260,"[Paraclostridial mosquitocidal protein 1]: Neurotoxin active against Anopheles but not Aedes mosquitoes upon oral ingestion; expression of the ptox operon (ntnh-orfX1-orfX2-orfX3-pmp1) in B.thuringiensis kills Anopheles but not Aedes mosquito 3rd instar larvae. The ntnh-pmp1 construct is about half as toxic. PMP1 is toxic when injected directly into Anopheles or Aedes mosquito 3rd instar larvae, larvae no longer move, suggesting they are paralyzed. Adult mosquitoes (Anopheles or Aedes) and Drosophila lose the ability to fly in a dose-dependent manner by 24 hours after injection with 100 pg neurotoxin. Not toxic upon injection in mice.","[Botulinum neurotoxin type A]: Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of the eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. Precursor of botulinum neurotoxin A which has 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles. Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them. Upon synaptic vesicle recycling the toxin is taken up via the endocytic pathway",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004222; GO:0008320; GO:0090729; GO:0008270,,GO:0004222; GO:0008270,GO:0004222; GO:0008270,GO:0008233,GO:0004222; GO:0008270,,0.7098,0.7098,0.3718,0.7098,4,0.6253,0.3245,no
PMP1_PARBF,A0A5P3XKQ1,Protein2Text,Bacteria,1260,"[Paraclostridial mosquitocidal protein 1]: Neurotoxin active against Anopheles but not Aedes mosquitoes upon oral ingestion; expression of the ptox operon (ntnh-orfX1-orfX2-orfX3-pmp1) in B.thuringiensis kills Anopheles but not Aedes mosquito 3rd instar larvae. The ntnh-pmp1 construct is about half as toxic. PMP1 is toxic when injected directly into Anopheles or Aedes mosquito 3rd instar larvae, larvae no longer move, suggesting they are paralyzed. Adult mosquitoes (Anopheles or Aedes) and Drosophila lose the ability to fly in a dose-dependent manner by 24 hours after injection with 100 pg neurotoxin. Not toxic upon injection in mice.",This protein is a protease.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004222; GO:0008320; GO:0090729; GO:0008270,GO:0008233,GO:0008233,GO:0008233,GO:0008233,GO:0008233,0.3718,0.3718,0.3718,0.3718,0.3718,5,0.3718,0.3245,no
PMP1_PARBF,A0A5P3XKQ1,Reference,Bacteria,1260,"[Paraclostridial mosquitocidal protein 1]: Neurotoxin active against Anopheles but not Aedes mosquitoes upon oral ingestion; expression of the ptox operon (ntnh-orfX1-orfX2-orfX3-pmp1) in B.thuringiensis kills Anopheles but not Aedes mosquito 3rd instar larvae. The ntnh-pmp1 construct is about half as toxic. PMP1 is toxic when injected directly into Anopheles or Aedes mosquito 3rd instar larvae, larvae no longer move, suggesting they are paralyzed. Adult mosquitoes (Anopheles or Aedes) and Drosophila lose the ability to fly in a dose-dependent manner by 24 hours after injection with 100 pg neurotoxin. Not toxic upon injection in mice.","[Paraclostridial mosquitocidal protein 1]: Neurotoxin active against Anopheles but not Aedes mosquitoes upon oral ingestion; expression of the ptox operon (ntnh-orfX1-orfX2-orfX3-pmp1) in B.thuringiensis kills Anopheles but not Aedes mosquito 3rd instar larvae. The ntnh-pmp1 construct is about half as toxic. PMP1 is toxic when injected directly into Anopheles or Aedes mosquito 3rd instar larvae, larvae no longer move, suggesting they are paralyzed. Adult mosquitoes (Anopheles or Aedes) and Drosophila lose the ability to fly in a dose-dependent manner by 24 hours after injection with 100 pg neurotoxin. Not toxic upon injection in mice.",,,,,,,GO:0004222; GO:0008320; GO:0090729; GO:0008270,,,,,,,,,,,0,,0.3245,no
BLC14_ECOLX,A0A649V088,ESM2Text,Bacteria,291,"Extended-spectrum beta-lactamase (ESBL) which confers resistance to penicillins, as well as first, second, and third- generation cephalosporins. Has cefotaxime-hydrolyzing activity.",Hydrolyzes broad-spectrum beta-lactam antibiotics. Active against cephalosporins such as cefoxitin and cefotaxime.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2286,no
BLC14_ECOLX,A0A649V088,Prot2Text,Bacteria,291,"Extended-spectrum beta-lactamase (ESBL) which confers resistance to penicillins, as well as first, second, and third- generation cephalosporins. Has cefotaxime-hydrolyzing activity.",Hydrolyzes broad-spectrum beta-lactam antibiotics. Active against cephalosporins.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2286,no
BLC14_ECOLX,A0A649V088,ProtT3,Bacteria,291,"Extended-spectrum beta-lactamase (ESBL) which confers resistance to penicillins, as well as first, second, and third- generation cephalosporins. Has cefotaxime-hydrolyzing activity.",Belongs to the class-A beta-lactamase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2286,no
BLC14_ECOLX,A0A649V088,ProtTale,Bacteria,291,"Extended-spectrum beta-lactamase (ESBL) which confers resistance to penicillins, as well as first, second, and third- generation cephalosporins. Has cefotaxime-hydrolyzing activity.","Extended-spectrum beta-lactamase (ESBL) which confers resistance to penicillins, as well as first and second- generation cephalosporins. Has penicillinase activity.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2286,no
BLC14_ECOLX,A0A649V088,Protein2Text,Bacteria,291,"Extended-spectrum beta-lactamase (ESBL) which confers resistance to penicillins, as well as first, second, and third- generation cephalosporins. Has cefotaxime-hydrolyzing activity.","The molecular function of this protein is an enzyme, specifically a beta-lactamase.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2286,no
BLC14_ECOLX,A0A649V088,Reference,Bacteria,291,"Extended-spectrum beta-lactamase (ESBL) which confers resistance to penicillins, as well as first, second, and third- generation cephalosporins. Has cefotaxime-hydrolyzing activity.","Extended-spectrum beta-lactamase (ESBL) which confers resistance to penicillins, as well as first, second, and third- generation cephalosporins. Has cefotaxime-hydrolyzing activity.",,,,,,,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2286,no
FAE1_PENPR,A0A6C0PI29,ESM2Text,Eukaryota,280,"Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl- galactose ester bond in pectin.","Involved in the degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-galactose ester bond in pectin. Active against methyl ferulate, methyl sinapate, methyl caffeate, alpha-naphthyl ester, alpha-naphthyl ester, alpha-naphthol, alpha-naphthol 2-acetate, but not triacetin, phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, tri- and tetraacetate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0030600,GO:0052689,GO:0030600; GO:0004091,GO:0030600,GO:0030600,GO:0030600,0.8582,0.9527,1.0,1.0,1.0,5,0.9622,0.2713,no
FAE1_PENPR,A0A6C0PI29,Prot2Text,Eukaryota,280,"Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl- galactose ester bond in pectin.","Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-galactose ester bond in pectin. Binds to cellulose.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0030600,GO:0016788; GO:0030248,GO:0030600,GO:0030600; GO:0030248,GO:0004553; GO:0016787,GO:0030600; GO:0030248,0.5208,1.0,0.7015,0.5342,0.7015,5,0.6916,0.2713,no
FAE1_PENPR,A0A6C0PI29,ProtT3,Eukaryota,280,"Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl- galactose ester bond in pectin.",Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans as well as the feruloyl- galactose and feruloyl-arabinose ester bonds in pectin (By similarity). Secreted. Belongs to the AB hydrolase superfamily. FaeA family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0030600,GO:0030600,GO:0030600,GO:0030600,GO:0034341,GO:0052689,1.0,1.0,1.0,0.0,0.8582,5,0.7716,0.2713,no
FAE1_PENPR,A0A6C0PI29,ProtTale,Eukaryota,280,"Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl- galactose ester bond in pectin.","Secreted lipase involved in Dandruff and seborrheic dermatitis (D/SD) probably via lipase-mediated breakdown of sebaceous lipids and release of irritating free fatty acids. Shows activity against monoglyceride and diglyceride substrates but not triolein. Able to cleave oleic acid from monoolein and diolein, and oleic acid from triolein. Able to hydrolyze p-nitrophenyl palmitate and p-nitrophenyl laurate, but not p-nitrophenyl palmitoleate or p-nitrophenyl stearate. Able to cleave the ester bonds of olive oil",No,No,No,No,No,not-Yes,GO:0030600,GO:0016298,GO:0016298,GO:0016298,GO:0004806,GO:0016298,0.6029,0.6029,0.6029,0.6576,0.6029,5,0.6138,0.2713,no
FAE1_PENPR,A0A6C0PI29,Protein2Text,Eukaryota,280,"Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl- galactose ester bond in pectin.","The molecular function of this protein is a hydrolase. More specifically, it is a secreted carboxyl esterase involved in the degradation of plant cell walls. It has been shown to hydrolyze carboxyl ester bonds in triglycerides, p-nitrophenyl esters, and glycerol esters. It is also capable of hydrolyzing the ester bonds in pectin, a major component of plant cell walls. It may play a role in the degradation of the plant cell wall, which is important for the pathogenicity of this fungus.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0030600,GO:0004091,GO:0052689,GO:0004091,GO:0004091,GO:0004091; GO:0052689,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.2713,no
FAE1_PENPR,A0A6C0PI29,Reference,Eukaryota,280,"Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl- galactose ester bond in pectin.","Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl- galactose ester bond in pectin.",,,,,,,GO:0030600,GO:0052689,GO:0052689,GO:0016788,GO:0016788,GO:0004064,0.8582,0.8582,0.729,0.729,0.7289,5,0.7807,0.2713,no
SDSL_RAT,A0A6N3IN21,ESM2Text,Eukaryota,329,"Catalyzes the pyridoxal-phosphate-dependent dehydrative deamination of L-threonine and L-serine to ammonia and alpha- ketobutyrate and pyruvate, respectively. Also exhibits racemase activity towards L-glutamate and D-glutamate.",Has low serine dehydratase and threonine dehydratase activity.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008881; GO:0042802; GO:0003941; GO:0030170; GO:0004794,GO:0016829,GO:0003941; GO:0004794,GO:0003941; GO:0004794,GO:0004764; GO:0004794,GO:0004764; GO:0004794,0.4091,0.6242,0.6242,0.4712,0.4712,5,0.52,0.6557,yes
SDSL_RAT,A0A6N3IN21,Prot2Text,Eukaryota,329,"Catalyzes the pyridoxal-phosphate-dependent dehydrative deamination of L-threonine and L-serine to ammonia and alpha- ketobutyrate and pyruvate, respectively. Also exhibits racemase activity towards L-glutamate and D-glutamate.",Has low serine dehydratase and threonine dehydratase activity.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008881; GO:0042802; GO:0003941; GO:0030170; GO:0004794,GO:0003941; GO:0004794,GO:0004764; GO:0004794,GO:0004764; GO:0004794,GO:0004764; GO:0004765,GO:0004764; GO:0004794,0.6242,0.4712,0.4712,0.1642,0.4712,5,0.4404,0.6557,yes
SDSL_RAT,A0A6N3IN21,ProtT3,Eukaryota,329,"Catalyzes the pyridoxal-phosphate-dependent dehydrative deamination of L-threonine and L-serine to ammonia and alpha- ketobutyrate and pyruvate, respectively. Also exhibits racemase activity towards L-glutamate and D-glutamate.",Cytoplasm. Belongs to the serine/threonine dehydratase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008881; GO:0042802; GO:0003941; GO:0030170; GO:0004794,GO:0016841,GO:0004764; GO:0004794,GO:0016829,GO:0003941,GO:0004764,0.5013,0.4712,0.4091,0.5164,0.1615,5,0.4119,0.6557,yes
SDSL_RAT,A0A6N3IN21,ProtTale,Eukaryota,329,"Catalyzes the pyridoxal-phosphate-dependent dehydrative deamination of L-threonine and L-serine to ammonia and alpha- ketobutyrate and pyruvate, respectively. Also exhibits racemase activity towards L-glutamate and D-glutamate.",Catalyzes the gamma-elimination of phosphate from L-phosphoserine and the beta-addition of water to produce L-homoserine.,No,No,No,No,No,not-Yes,GO:0008881; GO:0042802; GO:0003941; GO:0030170; GO:0004794,GO:0016829,GO:0016829,GO:0016829,GO:0016829,GO:0016829,0.4091,0.4091,0.4091,0.4091,0.4091,5,0.4091,0.6557,yes
SDSL_RAT,A0A6N3IN21,Protein2Text,Eukaryota,329,"Catalyzes the pyridoxal-phosphate-dependent dehydrative deamination of L-threonine and L-serine to ammonia and alpha- ketobutyrate and pyruvate, respectively. Also exhibits racemase activity towards L-glutamate and D-glutamate.",The molecular function of the protein is an aminotransferase.,No,No,No,No,Maybe,not-Yes,GO:0008881; GO:0042802; GO:0003941; GO:0030170; GO:0004794,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.1899,0.1899,0.1899,0.1899,0.1899,5,0.1899,0.6557,yes
SDSL_RAT,A0A6N3IN21,Reference,Eukaryota,329,"Catalyzes the pyridoxal-phosphate-dependent dehydrative deamination of L-threonine and L-serine to ammonia and alpha- ketobutyrate and pyruvate, respectively. Also exhibits racemase activity towards L-glutamate and D-glutamate.","Catalyzes the pyridoxal-phosphate-dependent dehydrative deamination of L-threonine and L-serine to ammonia and alpha- ketobutyrate and pyruvate, respectively. Also exhibits racemase activity towards L-glutamate and D-glutamate.",,,,,,,GO:0008881; GO:0042802; GO:0003941; GO:0030170; GO:0004794,GO:0004794; GO:0008171,GO:0004794; GO:0008171,GO:0004764; GO:0008171,GO:0004794; GO:0008903,GO:0004794; GO:0004796,0.4712,0.4712,0.167,0.5019,0.5223,5,0.4267,0.6557,yes
OXDD_OCTVU,A0A7E6FSU6,ESM2Text,Eukaryota,336,"Selectively catalyzes the oxidative deamination of acidic amino acids. Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors. Protects the organism from the toxicity of D-amino acids. May also function in the intestine.","Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate. Highest catalytic efficiency for D-Glu followed by D-Asp and NMDA. May play a role in the egg-laying events and early development of the worm, in addition to quality control of the germ cells.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008445; GO:0071949,GO:0016491,GO:0008450,GO:0008445,GO:0033739,GO:0033182,0.3665,0.0,0.6847,0.1671,0.0,5,0.2437,0.2611,no
OXDD_OCTVU,A0A7E6FSU6,Prot2Text,Eukaryota,336,"Selectively catalyzes the oxidative deamination of acidic amino acids. Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors. Protects the organism from the toxicity of D-amino acids. May also function in the intestine.","Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate. Highest catalytic efficiency for D-Glu followed by D-Asp and NMDA. May play a role in the egg-laying events and early development of the worm, in addition to quality control of the germ cells.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008445; GO:0071949,GO:0033739,GO:0003885,GO:0033735,GO:0003884,GO:0033182,0.1671,0.1971,0.2438,0.6047,0.0,5,0.2425,0.2611,no
OXDD_OCTVU,A0A7E6FSU6,ProtT3,Eukaryota,336,"Selectively catalyzes the oxidative deamination of acidic amino acids. Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors. Protects the organism from the toxicity of D-amino acids. May also function in the intestine.",Peroxisome. Belongs to the DAMOX/DASOX family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008445; GO:0071949,GO:0033735,GO:0033736,GO:0033735,GO:0033735,GO:0033734,0.2438,0.3963,0.2438,0.2438,0.1971,5,0.265,0.2611,no
OXDD_OCTVU,A0A7E6FSU6,ProtTale,Eukaryota,336,"Selectively catalyzes the oxidative deamination of acidic amino acids. Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors. Protects the organism from the toxicity of D-amino acids. May also function in the intestine.",Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Enables the organism to utilize D-amino acids as a source of nutrients.,Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0008445; GO:0071949,GO:0003884,GO:0003863,GO:0003884,GO:0003863,GO:0003884,0.6047,0.1971,0.6047,0.1971,0.6047,5,0.4417,0.2611,no
OXDD_OCTVU,A0A7E6FSU6,Protein2Text,Eukaryota,336,"Selectively catalyzes the oxidative deamination of acidic amino acids. Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors. Protects the organism from the toxicity of D-amino acids. May also function in the intestine.","The molecular function of this protein is an aminotransferase, which catalyzes the reversible transfer of an amino group from an amino acid to a 2-keto acid.",No,No,No,No,Maybe,not-Yes,GO:0008445; GO:0071949,GO:0004177,GO:0004177,GO:0004177,GO:0004177,GO:0004177,0.1183,0.1183,0.1183,0.1183,0.1183,5,0.1183,0.2611,no
OXDD_OCTVU,A0A7E6FSU6,Reference,Eukaryota,336,"Selectively catalyzes the oxidative deamination of acidic amino acids. Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors. Protects the organism from the toxicity of D-amino acids. May also function in the intestine.","Selectively catalyzes the oxidative deamination of acidic amino acids. Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors. Protects the organism from the toxicity of D-amino acids. May also function in the intestine.",,,,,,,GO:0008445; GO:0071949,GO:0003884,GO:0003884,GO:0003884,GO:0033971,GO:0033734,0.6047,0.6047,0.6047,0.1258,0.1971,5,0.4274,0.2611,no
PGK1_ASPFN,A0A7G5KET3,ESM2Text,Eukaryota,417,"Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3- diphosphoglycerate to 3-phosphoglycerate. Both L- and D- forms of purine and pyrimidine nucleotides can be used as substrates, but the activity is much lower on pyrimidines. Negatively regulates the biosynthesis of acetyl-CoA from pyruvate in the mitochondrion and consequently also attenuates aflatoxin production.",Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible ATP-dependent condensation of ATP with AMP and magnesium. Plays a role in sperm motility.,No,No,No,No,No,not-Yes,GO:0043531; GO:0005524; GO:0046872; GO:0004618,GO:0004017,GO:0004017,GO:0004017,GO:0004017,GO:0004017,0.2279,0.2279,0.2279,0.2279,0.2279,5,0.2279,0.3728,no
PGK1_ASPFN,A0A7G5KET3,Prot2Text,Eukaryota,417,"Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3- diphosphoglycerate to 3-phosphoglycerate. Both L- and D- forms of purine and pyrimidine nucleotides can be used as substrates, but the activity is much lower on pyrimidines. Negatively regulates the biosynthesis of acetyl-CoA from pyruvate in the mitochondrion and consequently also attenuates aflatoxin production.",Essential for sperm motility and male fertility but is not required for the completion of spermatogenesis.,Vague,Vague,Vague,No,No,not-Yes,GO:0043531; GO:0005524; GO:0046872; GO:0004618,,,,,,,,,,,0,,0.3728,no
PGK1_ASPFN,A0A7G5KET3,ProtT3,Eukaryota,417,"Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3- diphosphoglycerate to 3-phosphoglycerate. Both L- and D- forms of purine and pyrimidine nucleotides can be used as substrates, but the activity is much lower on pyrimidines. Negatively regulates the biosynthesis of acetyl-CoA from pyruvate in the mitochondrion and consequently also attenuates aflatoxin production.",Cytoplasm. Belongs to the phosphoglycerate kinase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0043531; GO:0005524; GO:0046872; GO:0004618,GO:0004618; GO:0005524,GO:0004618,GO:0004618; GO:0005524,GO:0004618; GO:0005524,GO:0004618,0.8553,0.4368,0.8553,0.8553,0.4368,5,0.6879,0.3728,no
PGK1_ASPFN,A0A7G5KET3,ProtTale,Eukaryota,417,"Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3- diphosphoglycerate to 3-phosphoglycerate. Both L- and D- forms of purine and pyrimidine nucleotides can be used as substrates, but the activity is much lower on pyrimidines. Negatively regulates the biosynthesis of acetyl-CoA from pyruvate in the mitochondrion and consequently also attenuates aflatoxin production.",Catalyzes the irreversible oxidative decarboxylation of oxaloacetate (OAA) to pyruvate with a concomitant reduction of NADP to NADPH.,No,No,No,No,No,not-Yes,GO:0043531; GO:0005524; GO:0046872; GO:0004618,GO:0004473,GO:0004473,GO:0004473,GO:0004473,GO:0004473,0.096,0.096,0.096,0.096,0.096,5,0.096,0.3728,no
PGK1_ASPFN,A0A7G5KET3,Protein2Text,Eukaryota,417,"Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3- diphosphoglycerate to 3-phosphoglycerate. Both L- and D- forms of purine and pyrimidine nucleotides can be used as substrates, but the activity is much lower on pyrimidines. Negatively regulates the biosynthesis of acetyl-CoA from pyruvate in the mitochondrion and consequently also attenuates aflatoxin production.","The molecular function of this protein is a glyceraldehyde-3-phosphate dehydrogenase, which is involved in glycolysis. It catalyzes the oxidation of glyceraldehyde-3-phosphate into 1,3-bisphosphoglycerate, with concomitant reduction of NAD to NADH.",No,No,No,No,No,not-Yes,GO:0043531; GO:0005524; GO:0046872; GO:0004618,GO:0004365,GO:0004365,GO:0004365,GO:0004365,GO:0004365,0.0979,0.0979,0.0979,0.0979,0.0979,5,0.0979,0.3728,no
PGK1_ASPFN,A0A7G5KET3,Reference,Eukaryota,417,"Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3- diphosphoglycerate to 3-phosphoglycerate. Both L- and D- forms of purine and pyrimidine nucleotides can be used as substrates, but the activity is much lower on pyrimidines. Negatively regulates the biosynthesis of acetyl-CoA from pyruvate in the mitochondrion and consequently also attenuates aflatoxin production.","Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3- diphosphoglycerate to 3-phosphoglycerate. Both L- and D- forms of purine and pyrimidine nucleotides can be used as substrates, but the activity is much lower on pyrimidines. Negatively regulates the biosynthesis of acetyl-CoA from pyruvate in the mitochondrion and consequently also attenuates aflatoxin production.",,,,,,,GO:0043531; GO:0005524; GO:0046872; GO:0004618,GO:0004618,GO:0004618,GO:0004618,GO:0004618; GO:0016301; GO:0005524,GO:0004618; GO:0005524,0.4368,0.4368,0.4368,0.8432,0.8553,5,0.6018,0.3728,no
GCNE_ASPFN,A0A7U2QYM2,ESM2Text,Eukaryota,402,"Acts as an acetyltransferase that acetylates histones H2B, H3 and H4, and contributes to H2A.Z acetylation. Acetylation of histones gives a specific tag for epigenetic transcription activation. Also acts as a benzoyltransferase and benzoylates adhB at 'Lys-393' which activates adhB to affect the development, secondary metabolism, pathogenicity, and stress response.","Histone acetyltransferase that acetylates 'Lys-4' of histone H4 (H4K4ac), thereby playing a central role in histone code. Acetylates nucleosomal histones H2A and H4. In vitro, acetylates the nucleosomal core of TP53 and may facilitate its acetylation. Acetylation of TP53 leads to transcriptional repression of cell cycle suppressor genes such as MCM2. Acetylates the nucleosomal core of TFAP thereby playing a role in TFAP nucleosome disassembly in the cytoplasm. In addition to histone acetyltransferase, also able to mediate acetylation of other proteins: specifically associates with the 'Lys-63'-linked histone H2A (H2AK63ac) and promotes recruitment of the SWI/SNF complex to histone H2A acetylation sites, thereby contributing to the regulation of chromatin remodeling.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0140068; GO:0036408; GO:0043993; GO:0140129; GO:0043992; GO:0140011; GO:0140046; GO:0003712,GO:0004402,GO:0004402,GO:0004402,GO:0004402,GO:0004402,0.4817,0.4817,0.4817,0.4817,0.4817,5,0.4817,0.5158,no
GCNE_ASPFN,A0A7U2QYM2,Prot2Text,Eukaryota,402,"Acts as an acetyltransferase that acetylates histones H2B, H3 and H4, and contributes to H2A.Z acetylation. Acetylation of histones gives a specific tag for epigenetic transcription activation. Also acts as a benzoyltransferase and benzoylates adhB at 'Lys-393' which activates adhB to affect the development, secondary metabolism, pathogenicity, and stress response.","Histone acetyltransferase that acetylates histone H2B to form H2BK11ac and H2BK16ac, histone H3 to form H3K14ac, with a lower preference histone H4 to form H4K8ac and H4K16ac, and contributes to H2A.Z acetylation. Acetylation of histones gives a specific tag for epigenetic transcription activation. Plays a key role in the regulation of gene expression by acetylating histones. Acetylates histones are essential for the repression of eukaryotic genes during early development.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0140068; GO:0036408; GO:0043993; GO:0140129; GO:0043992; GO:0140011; GO:0140046; GO:0003712,GO:0004402,GO:0004402,GO:0004402,GO:0004402,GO:0004402,0.4817,0.4817,0.4817,0.4817,0.4817,5,0.4817,0.5158,no
GCNE_ASPFN,A0A7U2QYM2,ProtT3,Eukaryota,402,"Acts as an acetyltransferase that acetylates histones H2B, H3 and H4, and contributes to H2A.Z acetylation. Acetylation of histones gives a specific tag for epigenetic transcription activation. Also acts as a benzoyltransferase and benzoylates adhB at 'Lys-393' which activates adhB to affect the development, secondary metabolism, pathogenicity, and stress response.","Histone acetyltransferase that acetylates 'Lys-14' of histone H4 (H4K14ac), 'Lys-16' of histone H4 (H4K16ac), 'Lys-18' of histone H4 (H4K18ac), 'Lys-23' of histone H3 (H3K23ac), 'Lys-27' of histone H3 (H3K27ac) and 'Lys-36' of histone H3 (H3",Yes,Yes,Yes,Yes,Yes,Yes,GO:0140068; GO:0036408; GO:0043993; GO:0140129; GO:0043992; GO:0140011; GO:0140046; GO:0003712,GO:0004402,GO:0004402,GO:0004402,GO:0004402,GO:0004402,0.4817,0.4817,0.4817,0.4817,0.4817,5,0.4817,0.5158,no
GCNE_ASPFN,A0A7U2QYM2,ProtTale,Eukaryota,402,"Acts as an acetyltransferase that acetylates histones H2B, H3 and H4, and contributes to H2A.Z acetylation. Acetylation of histones gives a specific tag for epigenetic transcription activation. Also acts as a benzoyltransferase and benzoylates adhB at 'Lys-393' which activates adhB to affect the development, secondary metabolism, pathogenicity, and stress response.","Protein-lysine N-methyltransferase that methylates ribosomal protein L10 (RPL10A, RPL10B, RPL10C, RPL10D, RPL10E, RPL10F, RPL10G, RPL10M, RPL10P or RPL10Q) at a specific lysine residue. Monomethylates RPL10, and thus enhances the stability of RPL10, thereby promoting protein synthesis.",No,No,No,No,No,not-Yes,GO:0140068; GO:0036408; GO:0043993; GO:0140129; GO:0043992; GO:0140011; GO:0140046; GO:0003712,GO:0016279,GO:0008276,GO:0016279,GO:0008276,GO:0016279,0.1732,0.2366,0.1732,0.2366,0.1732,5,0.1986,0.5158,no
GCNE_ASPFN,A0A7U2QYM2,Protein2Text,Eukaryota,402,"Acts as an acetyltransferase that acetylates histones H2B, H3 and H4, and contributes to H2A.Z acetylation. Acetylation of histones gives a specific tag for epigenetic transcription activation. Also acts as a benzoyltransferase and benzoylates adhB at 'Lys-393' which activates adhB to affect the development, secondary metabolism, pathogenicity, and stress response.","The molecular function of this protein is a histone acetyltransferase, which means it adds acetyl groups to histone proteins, playing a role in regulating gene expression.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0140068; GO:0036408; GO:0043993; GO:0140129; GO:0043992; GO:0140011; GO:0140046; GO:0003712,GO:0004402,GO:0004402,GO:0004402,GO:0004402,GO:0004402,0.4817,0.4817,0.4817,0.4817,0.4817,5,0.4817,0.5158,no
GCNE_ASPFN,A0A7U2QYM2,Reference,Eukaryota,402,"Acts as an acetyltransferase that acetylates histones H2B, H3 and H4, and contributes to H2A.Z acetylation. Acetylation of histones gives a specific tag for epigenetic transcription activation. Also acts as a benzoyltransferase and benzoylates adhB at 'Lys-393' which activates adhB to affect the development, secondary metabolism, pathogenicity, and stress response.","Acts as an acetyltransferase that acetylates histones H2B, H3 and H4, and contributes to H2A.Z acetylation. Acetylation of histones gives a specific tag for epigenetic transcription activation. Also acts as a benzoyltransferase and benzoylates adhB at 'Lys-393' which activates adhB to affect the development, secondary metabolism, pathogenicity, and stress response.",,,,,,,GO:0140068; GO:0036408; GO:0043993; GO:0140129; GO:0043992; GO:0140011; GO:0140046; GO:0003712,GO:0004402; GO:0016746,GO:0004402; GO:0016746,GO:0004402,GO:0004402; GO:0016746,GO:0004402; GO:0016746,0.5083,0.5083,0.4817,0.5083,0.5083,5,0.503,0.5158,no
ESDPD_PENSH,A0A8D5M3Y5,ESM2Text,Eukaryota,383,"Geranylgeranyl pyrophosphate synthase; part of the cluster that mediates the biosynthesis of shearones, diterpenoid pyrones (DPs) which are structurally diverse meroterpenoids consisting of a diterpene linked by a pyrone, and which may exhibit a range of bioactivities. Within the pathway, esdpD takes part to the biosynthesis of the molecular scaffold by providing geranylgeranyl pyrophosphate (GGPP) to the prenyltransferase esdpC for C-3 geranylgeranylation of the alpha-pyrone. The molecular scaffold is commonly biosynthesized by a series of enzymes including the non-reducing polyketide synthase (NR-PKS) esdpA that generates an alpha-pyrone; the prenyltransferase esdpC that attaches a geranylgeranyl pyrophosphate (GGPP) produced by the GGPP synthase (GGPPS) esdpD onto the pyrone unit; the FAD-dependent monooxygenase esdpE that converts an olefin on the diterpene unit into an epoxide; and the terpene cyclase esdpB that catalyzes the cyclization reactions to give the molecular backbone shearone A. In the modification steps, esdpF oxidizes the hydroxy group to a ketone at C-3 and esdpG then attaches hydroxy groups at both C-11 and C-12. After that, esdpI hydroxylates at C-20 and esdpH hydroxylates at C-6'. The ether bridge is generated by nucleophilic attack of the hydroxy group at C-20 to the carbonyl carbon at C-3. EsdpH can also functions prior to esdpI. The different combinations of these modification enzymes lead to the production of diverse shearone derivatives, shearone I being the end product of the pathway. The alpha-ketoglutarate- dependent dioxygenase esdpJ does not seem to be involved in this pathway.","Bifunctional enzyme that catalyzes the reactions from geranylgeranyl diphosphate to phytoene (phytoene synthase) and lycopene to beta-carotene via the intermediate gamma-carotene (lycopene cyclase). The intermediate gamma-carotene is further processed to the acidic carotenoid gamma-zeacarotene by the intermediate gamma-zeacarzin. Thereby, it is converted to the acidic nonsterol isoprene. Gamma-zeacarotene is the key intermediate in the biosynthesis of all major human embryonic germ placenta.",No,No,No,Maybe,Maybe,not-Yes,GO:0004337; GO:0004161; GO:0004311; GO:0046872,,GO:0016767,GO:0016767,GO:0016767,GO:0016767; GO:0045436,,0.0,0.0,0.0,0.1878,4,0.0469,0.3012,no
ESDPD_PENSH,A0A8D5M3Y5,Prot2Text,Eukaryota,383,"Geranylgeranyl pyrophosphate synthase; part of the cluster that mediates the biosynthesis of shearones, diterpenoid pyrones (DPs) which are structurally diverse meroterpenoids consisting of a diterpene linked by a pyrone, and which may exhibit a range of bioactivities. Within the pathway, esdpD takes part to the biosynthesis of the molecular scaffold by providing geranylgeranyl pyrophosphate (GGPP) to the prenyltransferase esdpC for C-3 geranylgeranylation of the alpha-pyrone. The molecular scaffold is commonly biosynthesized by a series of enzymes including the non-reducing polyketide synthase (NR-PKS) esdpA that generates an alpha-pyrone; the prenyltransferase esdpC that attaches a geranylgeranyl pyrophosphate (GGPP) produced by the GGPP synthase (GGPPS) esdpD onto the pyrone unit; the FAD-dependent monooxygenase esdpE that converts an olefin on the diterpene unit into an epoxide; and the terpene cyclase esdpB that catalyzes the cyclization reactions to give the molecular backbone shearone A. In the modification steps, esdpF oxidizes the hydroxy group to a ketone at C-3 and esdpG then attaches hydroxy groups at both C-11 and C-12. After that, esdpI hydroxylates at C-20 and esdpH hydroxylates at C-6'. The ether bridge is generated by nucleophilic attack of the hydroxy group at C-20 to the carbonyl carbon at C-3. EsdpH can also functions prior to esdpI. The different combinations of these modification enzymes lead to the production of diverse shearone derivatives, shearone I being the end product of the pathway. The alpha-ketoglutarate- dependent dioxygenase esdpJ does not seem to be involved in this pathway.",May be involved in the transport of a sterol precursor.,No,Vague,No,No,No,not-Yes,GO:0004337; GO:0004161; GO:0004311; GO:0046872,,,,,,,,,,,0,,0.3012,no
ESDPD_PENSH,A0A8D5M3Y5,ProtT3,Eukaryota,383,"Geranylgeranyl pyrophosphate synthase; part of the cluster that mediates the biosynthesis of shearones, diterpenoid pyrones (DPs) which are structurally diverse meroterpenoids consisting of a diterpene linked by a pyrone, and which may exhibit a range of bioactivities. Within the pathway, esdpD takes part to the biosynthesis of the molecular scaffold by providing geranylgeranyl pyrophosphate (GGPP) to the prenyltransferase esdpC for C-3 geranylgeranylation of the alpha-pyrone. The molecular scaffold is commonly biosynthesized by a series of enzymes including the non-reducing polyketide synthase (NR-PKS) esdpA that generates an alpha-pyrone; the prenyltransferase esdpC that attaches a geranylgeranyl pyrophosphate (GGPP) produced by the GGPP synthase (GGPPS) esdpD onto the pyrone unit; the FAD-dependent monooxygenase esdpE that converts an olefin on the diterpene unit into an epoxide; and the terpene cyclase esdpB that catalyzes the cyclization reactions to give the molecular backbone shearone A. In the modification steps, esdpF oxidizes the hydroxy group to a ketone at C-3 and esdpG then attaches hydroxy groups at both C-11 and C-12. After that, esdpI hydroxylates at C-20 and esdpH hydroxylates at C-6'. The ether bridge is generated by nucleophilic attack of the hydroxy group at C-20 to the carbonyl carbon at C-3. EsdpH can also functions prior to esdpI. The different combinations of these modification enzymes lead to the production of diverse shearone derivatives, shearone I being the end product of the pathway. The alpha-ketoglutarate- dependent dioxygenase esdpJ does not seem to be involved in this pathway.",Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids. Belongs to the FPP/GGPP synthase family,Maybe,Yes,Yes,Yes,Maybe,Yes,GO:0004337; GO:0004161; GO:0004311; GO:0046872,GO:0016765,GO:0004337,GO:0016765,GO:0004337,GO:0004337,0.5425,0.7142,0.5425,0.7142,0.7142,5,0.6455,0.3012,no
ESDPD_PENSH,A0A8D5M3Y5,ProtTale,Eukaryota,383,"Geranylgeranyl pyrophosphate synthase; part of the cluster that mediates the biosynthesis of shearones, diterpenoid pyrones (DPs) which are structurally diverse meroterpenoids consisting of a diterpene linked by a pyrone, and which may exhibit a range of bioactivities. Within the pathway, esdpD takes part to the biosynthesis of the molecular scaffold by providing geranylgeranyl pyrophosphate (GGPP) to the prenyltransferase esdpC for C-3 geranylgeranylation of the alpha-pyrone. The molecular scaffold is commonly biosynthesized by a series of enzymes including the non-reducing polyketide synthase (NR-PKS) esdpA that generates an alpha-pyrone; the prenyltransferase esdpC that attaches a geranylgeranyl pyrophosphate (GGPP) produced by the GGPP synthase (GGPPS) esdpD onto the pyrone unit; the FAD-dependent monooxygenase esdpE that converts an olefin on the diterpene unit into an epoxide; and the terpene cyclase esdpB that catalyzes the cyclization reactions to give the molecular backbone shearone A. In the modification steps, esdpF oxidizes the hydroxy group to a ketone at C-3 and esdpG then attaches hydroxy groups at both C-11 and C-12. After that, esdpI hydroxylates at C-20 and esdpH hydroxylates at C-6'. The ether bridge is generated by nucleophilic attack of the hydroxy group at C-20 to the carbonyl carbon at C-3. EsdpH can also functions prior to esdpI. The different combinations of these modification enzymes lead to the production of diverse shearone derivatives, shearone I being the end product of the pathway. The alpha-ketoglutarate- dependent dioxygenase esdpJ does not seem to be involved in this pathway.","Catalyzes the condensation of isopentenyl diphosphate (IPP) with dimethylallyl diphosphate (DMAPP) to yield geranyldiphosphate (GDP), which is an essential precursor for the biosynthesis of carotenoids and terpenoids.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004337; GO:0004161; GO:0004311; GO:0046872,GO:0004337,GO:0004337,GO:0004337,GO:0004337,GO:0004311,0.7142,0.7142,0.7142,0.7142,0.7142,5,0.7142,0.3012,no
ESDPD_PENSH,A0A8D5M3Y5,Protein2Text,Eukaryota,383,"Geranylgeranyl pyrophosphate synthase; part of the cluster that mediates the biosynthesis of shearones, diterpenoid pyrones (DPs) which are structurally diverse meroterpenoids consisting of a diterpene linked by a pyrone, and which may exhibit a range of bioactivities. Within the pathway, esdpD takes part to the biosynthesis of the molecular scaffold by providing geranylgeranyl pyrophosphate (GGPP) to the prenyltransferase esdpC for C-3 geranylgeranylation of the alpha-pyrone. The molecular scaffold is commonly biosynthesized by a series of enzymes including the non-reducing polyketide synthase (NR-PKS) esdpA that generates an alpha-pyrone; the prenyltransferase esdpC that attaches a geranylgeranyl pyrophosphate (GGPP) produced by the GGPP synthase (GGPPS) esdpD onto the pyrone unit; the FAD-dependent monooxygenase esdpE that converts an olefin on the diterpene unit into an epoxide; and the terpene cyclase esdpB that catalyzes the cyclization reactions to give the molecular backbone shearone A. In the modification steps, esdpF oxidizes the hydroxy group to a ketone at C-3 and esdpG then attaches hydroxy groups at both C-11 and C-12. After that, esdpI hydroxylates at C-20 and esdpH hydroxylates at C-6'. The ether bridge is generated by nucleophilic attack of the hydroxy group at C-20 to the carbonyl carbon at C-3. EsdpH can also functions prior to esdpI. The different combinations of these modification enzymes lead to the production of diverse shearone derivatives, shearone I being the end product of the pathway. The alpha-ketoglutarate- dependent dioxygenase esdpJ does not seem to be involved in this pathway.","The molecular function of this protein is a terpene synthase, which is an enzyme that catalyzes the conversion of isopentenyl pyrophosphate (IPP) and dimethylallyl pyrophosphate (DMAPP) into various terpenes, which are a large class of organic compounds with a wide range of biological activities.",Maybe,Maybe,Maybe,Maybe,Vague,not-Yes,GO:0004337; GO:0004161; GO:0004311; GO:0046872,GO:0010333,GO:0010333,GO:0010333,GO:0010333,GO:0010334,0.1567,0.1567,0.1567,0.1567,0.1349,5,0.1523,0.3012,no
ESDPD_PENSH,A0A8D5M3Y5,Reference,Eukaryota,383,"Geranylgeranyl pyrophosphate synthase; part of the cluster that mediates the biosynthesis of shearones, diterpenoid pyrones (DPs) which are structurally diverse meroterpenoids consisting of a diterpene linked by a pyrone, and which may exhibit a range of bioactivities. Within the pathway, esdpD takes part to the biosynthesis of the molecular scaffold by providing geranylgeranyl pyrophosphate (GGPP) to the prenyltransferase esdpC for C-3 geranylgeranylation of the alpha-pyrone. The molecular scaffold is commonly biosynthesized by a series of enzymes including the non-reducing polyketide synthase (NR-PKS) esdpA that generates an alpha-pyrone; the prenyltransferase esdpC that attaches a geranylgeranyl pyrophosphate (GGPP) produced by the GGPP synthase (GGPPS) esdpD onto the pyrone unit; the FAD-dependent monooxygenase esdpE that converts an olefin on the diterpene unit into an epoxide; and the terpene cyclase esdpB that catalyzes the cyclization reactions to give the molecular backbone shearone A. In the modification steps, esdpF oxidizes the hydroxy group to a ketone at C-3 and esdpG then attaches hydroxy groups at both C-11 and C-12. After that, esdpI hydroxylates at C-20 and esdpH hydroxylates at C-6'. The ether bridge is generated by nucleophilic attack of the hydroxy group at C-20 to the carbonyl carbon at C-3. EsdpH can also functions prior to esdpI. The different combinations of these modification enzymes lead to the production of diverse shearone derivatives, shearone I being the end product of the pathway. The alpha-ketoglutarate- dependent dioxygenase esdpJ does not seem to be involved in this pathway.","Geranylgeranyl pyrophosphate synthase; part of the cluster that mediates the biosynthesis of shearones, diterpenoid pyrones (DPs) which are structurally diverse meroterpenoids consisting of a diterpene linked by a pyrone, and which may exhibit a range of bioactivities. Within the pathway, esdpD takes part to the biosynthesis of the molecular scaffold by providing geranylgeranyl pyrophosphate (GGPP) to the prenyltransferase esdpC for C-3 geranylgeranylation of the alpha-pyrone. The molecular scaffold is commonly biosynthesized by a series of enzymes including the non-reducing polyketide synthase (NR-PKS) esdpA that generates an alpha-pyrone; the prenyltransferase esdpC that attaches a geranylgeranyl pyrophosphate (GGPP) produced by the GGPP synthase (GGPPS) esdpD onto the pyrone unit; the FAD-dependent monooxygenase esdpE that converts an olefin on the diterpene unit into an epoxide; and the terpene cyclase esdpB that catalyzes the cyclization reactions to give the molecular backbone shearone A. In the modification steps, esdpF oxidizes the hydroxy group to a ketone at C-3 and esdpG then attaches hydroxy groups at both C-11 and C-12. After that, esdpI hydroxylates at C-20 and esdpH hydroxylates at C-6'. The ether bridge is generated by nucleophilic attack of the hydroxy group at C-20 to the carbonyl carbon at C-3. EsdpH can also functions prior to esdpI. The different combinations of these modification enzymes lead to the production of diverse shearone derivatives, shearone I being the end product of the pathway. The alpha-ketoglutarate- dependent dioxygenase esdpJ does not seem to be involved in this pathway.",,,,,,,GO:0004337; GO:0004161; GO:0004311; GO:0046872,GO:0004337,GO:0004337,GO:0004311,GO:0004337,GO:0004337,0.7142,0.7142,0.7142,0.7142,0.7142,5,0.7142,0.3012,no
CUBA_PSICU,A0A8H8CMW1,ESM2Text,Eukaryota,343,"Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to various sesquiterpenes, including cubebol as the major product and beta-copaene, delta-cadinene, germacrene D, germacrene D-4-ol, sativene, tau-muurolol, beta-cubebene and beta- elemene as minor compounds, along with minute amounts of further sesquiterpenoids.","Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to various sesquiterpenes, including alpha-muurolene, beta-caryophyllene, delta-caryophyllene, alpha-humulene, alpha-humulin, and delta-cadinene.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0010333,,GO:0010333,GO:0010333,GO:0010333,GO:0010333,,0.6963,0.6963,0.6963,0.6963,4,0.6963,0.1666,no
CUBA_PSICU,A0A8H8CMW1,Prot2Text,Eukaryota,343,"Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to various sesquiterpenes, including cubebol as the major product and beta-copaene, delta-cadinene, germacrene D, germacrene D-4-ol, sativene, tau-muurolol, beta-cubebene and beta- elemene as minor compounds, along with minute amounts of further sesquiterpenoids.","Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to various sesquiterpenes, including alpha-copaene, beta-copaene, beta-elemene, gamma-muurolene, delta-cadinene, alpha-muurolene and cubenol.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0010333,GO:0016829,,GO:0010334,GO:0010334,GO:0010334,0.4539,,0.6051,0.6051,0.6051,4,0.5673,0.1666,no
CUBA_PSICU,A0A8H8CMW1,ProtT3,Eukaryota,343,"Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to various sesquiterpenes, including cubebol as the major product and beta-copaene, delta-cadinene, germacrene D, germacrene D-4-ol, sativene, tau-muurolol, beta-cubebene and beta- elemene as minor compounds, along with minute amounts of further sesquiterpenoids.",Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to delta(6)-protoilludene. Belongs to the terpene synthase family,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0046872; GO:0010333,GO:0010333,GO:0016829,GO:0010333,GO:0010333,GO:0010333,0.6963,0.4539,0.6963,0.6963,0.6963,5,0.6478,0.1666,no
CUBA_PSICU,A0A8H8CMW1,ProtTale,Eukaryota,343,"Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to various sesquiterpenes, including cubebol as the major product and beta-copaene, delta-cadinene, germacrene D, germacrene D-4-ol, sativene, tau-muurolol, beta-cubebene and beta- elemene as minor compounds, along with minute amounts of further sesquiterpenoids.","Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to various sesquiterpenes, including alpha-copaene, beta-copaene, beta-caryophyllene, gamma-cadinene, delta-cadinene, alpha-humulene, beta-selinene, alpha-cadinol, alpha-cadinol-9-ol, alpha-cadinol-10-ol, alpha-cadinol-11-ol, alpha-cadinol-12-ol, alpha-cadinol-13-ol, alpha-cadinol-1",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0010333,GO:0010333,GO:0016829,GO:0010333,GO:0010334,GO:0010334; GO:0016829,0.6963,0.4539,0.6963,0.6051,0.6245,5,0.6152,0.1666,no
CUBA_PSICU,A0A8H8CMW1,Protein2Text,Eukaryota,343,"Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to various sesquiterpenes, including cubebol as the major product and beta-copaene, delta-cadinene, germacrene D, germacrene D-4-ol, sativene, tau-muurolol, beta-cubebene and beta- elemene as minor compounds, along with minute amounts of further sesquiterpenoids.","The molecular function of this protein is to catalyze the biosynthesis of a certain compound, specifically a terpene, through a process involving the conversion of farnesyl diphosphate (FPP) to a product.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0010333,GO:0010333,GO:0010333,GO:0010333,GO:0010334,0.6963,0.6963,0.6963,0.6963,0.6051,5,0.6781,0.1666,no
CUBA_PSICU,A0A8H8CMW1,Reference,Eukaryota,343,"Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to various sesquiterpenes, including cubebol as the major product and beta-copaene, delta-cadinene, germacrene D, germacrene D-4-ol, sativene, tau-muurolol, beta-cubebene and beta- elemene as minor compounds, along with minute amounts of further sesquiterpenoids.","Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to various sesquiterpenes, including cubebol as the major product and beta-copaene, delta-cadinene, germacrene D, germacrene D-4-ol, sativene, tau-muurolol, beta-cubebene and beta- elemene as minor compounds, along with minute amounts of further sesquiterpenoids.",,,,,,,GO:0046872; GO:0010333,GO:0010334,GO:0010334,GO:0010334,GO:0010333; GO:0016829,,0.6051,0.6051,0.6051,0.6899,,4,0.6263,0.1666,no
SHIP2_CANLF,A0A8I3NFE2,ESM2Text,Eukaryota,1264,"Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Required for correct mitotic spindle orientation and therefore progression of mitosis. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling. Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. Plays a role in the localization of AURKA and NEDD9/HEF1 to the basolateral membrane at interphase in polarized cysts, thereby mediates cell cycle homeostasis, cell polarization and cilia assembly. Additionally promotion of cilia growth is also facilitated by hydrolysis of (PtdIns(3,4,5)P3) to PtdIns(3,4)P2. Promotes formation of apical membrane- initiation sites during the initial stages of lumen formation via Rho family-induced actin filament organization and CTNNB1 localization to cell-cell contacts. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification.","Phosphatidylinositol (PtdIns) phosphatase which catalyzes the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) to phosphatidylinositol (PtdIns(4,5)P3), and also hydrolyzes the phosphatidylinositol 3-phosphate (PtdIns(3)P) to phosphatidylinositol (PtdIns(3)P). Able to hydrolyze the second messenger 4-phosphopantetheine (PtdIns(4)P), but with lower efficiency. Acts as a negative regulator of TGF-beta signaling. Has no activity toward PtdIns(4,5)P2, PtdIns(3,4,5)P3 or Ins(4,5)P4.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0003779; GO:0004445; GO:0034485; GO:0042169; GO:0017124,GO:0004437,GO:0004437,,,,0.0,0.0,,,,2,0.0,0.4762,no
SHIP2_CANLF,A0A8I3NFE2,Prot2Text,Eukaryota,1264,"Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Required for correct mitotic spindle orientation and therefore progression of mitosis. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling. Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. Plays a role in the localization of AURKA and NEDD9/HEF1 to the basolateral membrane at interphase in polarized cysts, thereby mediates cell cycle homeostasis, cell polarization and cilia assembly. Additionally promotion of cilia growth is also facilitated by hydrolysis of (PtdIns(3,4,5)P3) to PtdIns(3,4)P2. Promotes formation of apical membrane- initiation sites during the initial stages of lumen formation via Rho family-induced actin filament organization and CTNNB1 localization to cell-cell contacts. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification.","Has phosphatase activity toward Ins(1,4,5)P3 and Ins(1,3,4,5)P4, but not toward Ins(1)P, Ins(1)P2, Ins(1)P3 or Ins(1,4)P2. Seems to be involved in the intracellular trafficking of membrane proteins.",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0003779; GO:0004445; GO:0034485; GO:0042169; GO:0017124,GO:0004437,GO:0004445,GO:0004437,GO:0004445,GO:0004445,0.0,0.4374,0.0,0.4374,0.4374,5,0.2624,0.4762,no
SHIP2_CANLF,A0A8I3NFE2,ProtT3,Eukaryota,1264,"Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Required for correct mitotic spindle orientation and therefore progression of mitosis. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling. Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. Plays a role in the localization of AURKA and NEDD9/HEF1 to the basolateral membrane at interphase in polarized cysts, thereby mediates cell cycle homeostasis, cell polarization and cilia assembly. Additionally promotion of cilia growth is also facilitated by hydrolysis of (PtdIns(3,4,5)P3) to PtdIns(3,4)P2. Promotes formation of apical membrane- initiation sites during the initial stages of lumen formation via Rho family-induced actin filament organization and CTNNB1 localization to cell-cell contacts. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification.","Hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) (By similarity). Plays an important role in the regulation of the actin cytoskeleton via its action on PtdIns(4,5)P2 and PtdIns(3,4,5)P3 (By similarity). Cytoplasm. Belongs to the inositol polyphosphate 5-",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0003779; GO:0004445; GO:0034485; GO:0042169; GO:0017124,GO:0004439,GO:0004445,GO:0004439; GO:0034485,GO:0004445,GO:0004439,0.2976,0.4374,0.4592,0.4374,0.2976,5,0.3858,0.4762,no
SHIP2_CANLF,A0A8I3NFE2,ProtTale,Eukaryota,1264,"Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Required for correct mitotic spindle orientation and therefore progression of mitosis. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling. Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. Plays a role in the localization of AURKA and NEDD9/HEF1 to the basolateral membrane at interphase in polarized cysts, thereby mediates cell cycle homeostasis, cell polarization and cilia assembly. Additionally promotion of cilia growth is also facilitated by hydrolysis of (PtdIns(3,4,5)P3) to PtdIns(3,4)P2. Promotes formation of apical membrane- initiation sites during the initial stages of lumen formation via Rho family-induced actin filament organization and CTNNB1 localization to cell-cell contacts. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification.",Dual-specificity phosphatase that specifically dephosphorylates the threonine and tyrosine residues in the kinase domain of calcium/calmodulin-dependent protein kinase II (CAMK2A and CAMK2B). Dephosphorylation of CAMK2A and CAMK2B prevents their autophosphorylation and subsequent activation by calcium/calmodulin-dependent protein kinase II (CAMK2A and CAMK2B). May play a role in the regulation of synaptic plasticity in the central nervous system.,No,No,No,No,No,not-Yes,GO:0003779; GO:0004445; GO:0034485; GO:0042169; GO:0017124,GO:0004725; GO:0004721,GO:0004725; GO:0004722,GO:0004725; GO:0004722,GO:0004725; GO:0004721,GO:0004725; GO:0004722,0.3496,0.3157,0.3157,0.3496,0.3157,5,0.3293,0.4762,no
SHIP2_CANLF,A0A8I3NFE2,Protein2Text,Eukaryota,1264,"Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Required for correct mitotic spindle orientation and therefore progression of mitosis. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling. Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. Plays a role in the localization of AURKA and NEDD9/HEF1 to the basolateral membrane at interphase in polarized cysts, thereby mediates cell cycle homeostasis, cell polarization and cilia assembly. Additionally promotion of cilia growth is also facilitated by hydrolysis of (PtdIns(3,4,5)P3) to PtdIns(3,4)P2. Promotes formation of apical membrane- initiation sites during the initial stages of lumen formation via Rho family-induced actin filament organization and CTNNB1 localization to cell-cell contacts. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification.","This protein is a tyrosine phosphatase, which means it is involved in the removal of phosphate groups from tyrosine residues on other proteins. This is an important step in signaling pathways, as it can activate or deactivate proteins by removing or adding phosphate groups.",No,No,No,No,No,not-Yes,GO:0003779; GO:0004445; GO:0034485; GO:0042169; GO:0017124,GO:0004725,GO:0004726,GO:0004725,GO:0004725,GO:0004726,0.2866,0.2545,0.2866,0.2866,0.2545,5,0.2738,0.4762,no
SHIP2_CANLF,A0A8I3NFE2,Reference,Eukaryota,1264,"Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Required for correct mitotic spindle orientation and therefore progression of mitosis. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling. Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. Plays a role in the localization of AURKA and NEDD9/HEF1 to the basolateral membrane at interphase in polarized cysts, thereby mediates cell cycle homeostasis, cell polarization and cilia assembly. Additionally promotion of cilia growth is also facilitated by hydrolysis of (PtdIns(3,4,5)P3) to PtdIns(3,4)P2. Promotes formation of apical membrane- initiation sites during the initial stages of lumen formation via Rho family-induced actin filament organization and CTNNB1 localization to cell-cell contacts. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification.","Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Required for correct mitotic spindle orientation and therefore progression of mitosis. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling. Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. Plays a role in the localization of AURKA and NEDD9/HEF1 to the basolateral membrane at interphase in polarized cysts, thereby mediates cell cycle homeostasis, cell polarization and cilia assembly. Additionally promotion of cilia growth is also facilitated by hydrolysis of (PtdIns(3,4,5)P3) to PtdIns(3,4)P2. Promotes formation of apical membrane- initiation sites during the initial stages of lumen formation via Rho family-induced actin filament organization and CTNNB1 localization to cell-cell contacts. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification.",,,,,,,GO:0003779; GO:0004445; GO:0034485; GO:0042169; GO:0017124,GO:0016791,GO:0016791,GO:0004439,GO:0004439; GO:0016791,GO:0004439; GO:0046856,0.3896,0.3896,0.2976,0.4212,0.2551,5,0.3506,0.4762,no
OXSR1_RAT,A0A8I5ZNK2,ESM2Text,Eukaryota,528,"Effector serine/threonine-protein kinase component of the WNK-SPAK/OSR1 kinase cascade, which is involved in various processes, such as ion transport, response to hypertonic stress and blood pressure. Specifically recognizes and binds proteins with a RFXV motif. Acts downstream of WNK kinases (WNK1, WNK2, WNK3 or WNK4): following activation by WNK kinases, catalyzes phosphorylation of ion cotransporters, such as SLC12A1/NKCC2, SLC12A2/NKCC1, SLC12A3/NCC, SLC12A5/KCC2 or SLC12A6/KCC3, regulating their activity. Mediates regulatory volume increase in response to hyperosmotic stress by catalyzing phosphorylation of ion cotransporters SLC12A1/NKCC2, SLC12A2/NKCC1 and SLC12A6/KCC3 downstream of WNK1 and WNK3 kinases. Phosphorylation of Na-K-Cl cotransporters SLC12A2/NKCC1 and SLC12A2/NKCC1 promote their activation and ion influx; simultaneously, phosphorylation of K-Cl cotransporters SLC12A5/KCC2 and SLC12A6/KCC3 inhibit their activity, blocking ion efflux. Acts as a regulator of NaCl reabsorption in the distal nephron by mediating phosphorylation and activation of the thiazide-sensitive Na-Cl cotransporter SLC12A3/NCC in distal convoluted tubule cells of kidney downstream of WNK4. Also acts as a regulator of angiogenesis in endothelial cells downstream of WNK1. Acts as an activator of inward rectifier potassium channels KCNJ2/Kir2.1 and KCNJ4/Kir2.3 downstream of WNK1: recognizes and binds the RXFXV/I variant motif on KCNJ2/Kir2.1 and KCNJ4/Kir2.3 and regulates their localization to the cell membrane without mediating their phosphorylation. Phosphorylates RELL1, RELL2 and RELT. Phosphorylates PAK1. Phosphorylates PLSCR1 in the presence of RELT.","Phosphorylates RELL1, RELL2, RELT and PAK1. Phosphorylates PLSCR1 in the presence of RELT.",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0042802; GO:0099106; GO:0000287; GO:0019870; GO:0019901; GO:0004674; GO:0044325,GO:0004672,GO:0004672,GO:0004672,GO:0004672,GO:0004672,0.2728,0.2728,0.2728,0.2728,0.2728,5,0.2728,0.5623,yes
OXSR1_RAT,A0A8I5ZNK2,Prot2Text,Eukaryota,528,"Effector serine/threonine-protein kinase component of the WNK-SPAK/OSR1 kinase cascade, which is involved in various processes, such as ion transport, response to hypertonic stress and blood pressure. Specifically recognizes and binds proteins with a RFXV motif. Acts downstream of WNK kinases (WNK1, WNK2, WNK3 or WNK4): following activation by WNK kinases, catalyzes phosphorylation of ion cotransporters, such as SLC12A1/NKCC2, SLC12A2/NKCC1, SLC12A3/NCC, SLC12A5/KCC2 or SLC12A6/KCC3, regulating their activity. Mediates regulatory volume increase in response to hyperosmotic stress by catalyzing phosphorylation of ion cotransporters SLC12A1/NKCC2, SLC12A2/NKCC1 and SLC12A6/KCC3 downstream of WNK1 and WNK3 kinases. Phosphorylation of Na-K-Cl cotransporters SLC12A2/NKCC1 and SLC12A2/NKCC1 promote their activation and ion influx; simultaneously, phosphorylation of K-Cl cotransporters SLC12A5/KCC2 and SLC12A6/KCC3 inhibit their activity, blocking ion efflux. Acts as a regulator of NaCl reabsorption in the distal nephron by mediating phosphorylation and activation of the thiazide-sensitive Na-Cl cotransporter SLC12A3/NCC in distal convoluted tubule cells of kidney downstream of WNK4. Also acts as a regulator of angiogenesis in endothelial cells downstream of WNK1. Acts as an activator of inward rectifier potassium channels KCNJ2/Kir2.1 and KCNJ4/Kir2.3 downstream of WNK1: recognizes and binds the RXFXV/I variant motif on KCNJ2/Kir2.1 and KCNJ4/Kir2.3 and regulates their localization to the cell membrane without mediating their phosphorylation. Phosphorylates RELL1, RELL2 and RELT. Phosphorylates PAK1. Phosphorylates PLSCR1 in the presence of RELT.","Phosphorylates RELL1, RELL2, RELT and PAK1. Phosphorylates PLSCR1 in the presence of RELT.",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0042802; GO:0099106; GO:0000287; GO:0019870; GO:0019901; GO:0004674; GO:0044325,GO:0004672,GO:0004672,GO:0004672,GO:0004672,GO:0004672,0.2728,0.2728,0.2728,0.2728,0.2728,5,0.2728,0.5623,yes
OXSR1_RAT,A0A8I5ZNK2,ProtT3,Eukaryota,528,"Effector serine/threonine-protein kinase component of the WNK-SPAK/OSR1 kinase cascade, which is involved in various processes, such as ion transport, response to hypertonic stress and blood pressure. Specifically recognizes and binds proteins with a RFXV motif. Acts downstream of WNK kinases (WNK1, WNK2, WNK3 or WNK4): following activation by WNK kinases, catalyzes phosphorylation of ion cotransporters, such as SLC12A1/NKCC2, SLC12A2/NKCC1, SLC12A3/NCC, SLC12A5/KCC2 or SLC12A6/KCC3, regulating their activity. Mediates regulatory volume increase in response to hyperosmotic stress by catalyzing phosphorylation of ion cotransporters SLC12A1/NKCC2, SLC12A2/NKCC1 and SLC12A6/KCC3 downstream of WNK1 and WNK3 kinases. Phosphorylation of Na-K-Cl cotransporters SLC12A2/NKCC1 and SLC12A2/NKCC1 promote their activation and ion influx; simultaneously, phosphorylation of K-Cl cotransporters SLC12A5/KCC2 and SLC12A6/KCC3 inhibit their activity, blocking ion efflux. Acts as a regulator of NaCl reabsorption in the distal nephron by mediating phosphorylation and activation of the thiazide-sensitive Na-Cl cotransporter SLC12A3/NCC in distal convoluted tubule cells of kidney downstream of WNK4. Also acts as a regulator of angiogenesis in endothelial cells downstream of WNK1. Acts as an activator of inward rectifier potassium channels KCNJ2/Kir2.1 and KCNJ4/Kir2.3 downstream of WNK1: recognizes and binds the RXFXV/I variant motif on KCNJ2/Kir2.1 and KCNJ4/Kir2.3 and regulates their localization to the cell membrane without mediating their phosphorylation. Phosphorylates RELL1, RELL2 and RELT. Phosphorylates PAK1. Phosphorylates PLSCR1 in the presence of RELT.","Serine/threonine-protein kinase that acts as a regulator of the canonical Wnt signaling pathway by mediating phosphorylation of beta-catenin/CTNNB1 at 'Ser-33' and 'Ser-37', leading to down-regulation of CTNNB1 transcriptional activity (By similarity). Also acts as a regulator of the JNK signaling pathway by mediating phosphorylation of MAP2K3/MKK3 and MAP2K6/MKK4 (By similarity). Cytoplasm. Belongs to the protein kinase superfamily. STE Ser",Maybe,Maybe,Maybe,No,No,not-Yes,GO:0005524; GO:0042802; GO:0099106; GO:0000287; GO:0019870; GO:0019901; GO:0004674; GO:0044325,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,0.4859,0.4859,0.4859,0.4859,0.2855,5,0.4458,0.5623,yes
OXSR1_RAT,A0A8I5ZNK2,ProtTale,Eukaryota,528,"Effector serine/threonine-protein kinase component of the WNK-SPAK/OSR1 kinase cascade, which is involved in various processes, such as ion transport, response to hypertonic stress and blood pressure. Specifically recognizes and binds proteins with a RFXV motif. Acts downstream of WNK kinases (WNK1, WNK2, WNK3 or WNK4): following activation by WNK kinases, catalyzes phosphorylation of ion cotransporters, such as SLC12A1/NKCC2, SLC12A2/NKCC1, SLC12A3/NCC, SLC12A5/KCC2 or SLC12A6/KCC3, regulating their activity. Mediates regulatory volume increase in response to hyperosmotic stress by catalyzing phosphorylation of ion cotransporters SLC12A1/NKCC2, SLC12A2/NKCC1 and SLC12A6/KCC3 downstream of WNK1 and WNK3 kinases. Phosphorylation of Na-K-Cl cotransporters SLC12A2/NKCC1 and SLC12A2/NKCC1 promote their activation and ion influx; simultaneously, phosphorylation of K-Cl cotransporters SLC12A5/KCC2 and SLC12A6/KCC3 inhibit their activity, blocking ion efflux. Acts as a regulator of NaCl reabsorption in the distal nephron by mediating phosphorylation and activation of the thiazide-sensitive Na-Cl cotransporter SLC12A3/NCC in distal convoluted tubule cells of kidney downstream of WNK4. Also acts as a regulator of angiogenesis in endothelial cells downstream of WNK1. Acts as an activator of inward rectifier potassium channels KCNJ2/Kir2.1 and KCNJ4/Kir2.3 downstream of WNK1: recognizes and binds the RXFXV/I variant motif on KCNJ2/Kir2.1 and KCNJ4/Kir2.3 and regulates their localization to the cell membrane without mediating their phosphorylation. Phosphorylates RELL1, RELL2 and RELT. Phosphorylates PAK1. Phosphorylates PLSCR1 in the presence of RELT.",Serine/threonine-protein kinase involved in the regulation of centrosome maturation and mitotic spindle formation. Phosphorylates and activates CEP170.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0042802; GO:0099106; GO:0000287; GO:0019870; GO:0019901; GO:0004674; GO:0044325,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,0.4859,0.4859,0.4859,0.2855,0.4859,5,0.4458,0.5623,yes
OXSR1_RAT,A0A8I5ZNK2,Protein2Text,Eukaryota,528,"Effector serine/threonine-protein kinase component of the WNK-SPAK/OSR1 kinase cascade, which is involved in various processes, such as ion transport, response to hypertonic stress and blood pressure. Specifically recognizes and binds proteins with a RFXV motif. Acts downstream of WNK kinases (WNK1, WNK2, WNK3 or WNK4): following activation by WNK kinases, catalyzes phosphorylation of ion cotransporters, such as SLC12A1/NKCC2, SLC12A2/NKCC1, SLC12A3/NCC, SLC12A5/KCC2 or SLC12A6/KCC3, regulating their activity. Mediates regulatory volume increase in response to hyperosmotic stress by catalyzing phosphorylation of ion cotransporters SLC12A1/NKCC2, SLC12A2/NKCC1 and SLC12A6/KCC3 downstream of WNK1 and WNK3 kinases. Phosphorylation of Na-K-Cl cotransporters SLC12A2/NKCC1 and SLC12A2/NKCC1 promote their activation and ion influx; simultaneously, phosphorylation of K-Cl cotransporters SLC12A5/KCC2 and SLC12A6/KCC3 inhibit their activity, blocking ion efflux. Acts as a regulator of NaCl reabsorption in the distal nephron by mediating phosphorylation and activation of the thiazide-sensitive Na-Cl cotransporter SLC12A3/NCC in distal convoluted tubule cells of kidney downstream of WNK4. Also acts as a regulator of angiogenesis in endothelial cells downstream of WNK1. Acts as an activator of inward rectifier potassium channels KCNJ2/Kir2.1 and KCNJ4/Kir2.3 downstream of WNK1: recognizes and binds the RXFXV/I variant motif on KCNJ2/Kir2.1 and KCNJ4/Kir2.3 and regulates their localization to the cell membrane without mediating their phosphorylation. Phosphorylates RELL1, RELL2 and RELT. Phosphorylates PAK1. Phosphorylates PLSCR1 in the presence of RELT.",The molecular function of the protein is that it is a serine/threonine-protein kinase.,Maybe,Maybe,Yes,Yes,Maybe,not-Yes,GO:0005524; GO:0042802; GO:0099106; GO:0000287; GO:0019870; GO:0019901; GO:0004674; GO:0044325,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.2855,0.2855,0.2855,0.2855,0.2855,5,0.2855,0.5623,yes
OXSR1_RAT,A0A8I5ZNK2,Reference,Eukaryota,528,"Effector serine/threonine-protein kinase component of the WNK-SPAK/OSR1 kinase cascade, which is involved in various processes, such as ion transport, response to hypertonic stress and blood pressure. Specifically recognizes and binds proteins with a RFXV motif. Acts downstream of WNK kinases (WNK1, WNK2, WNK3 or WNK4): following activation by WNK kinases, catalyzes phosphorylation of ion cotransporters, such as SLC12A1/NKCC2, SLC12A2/NKCC1, SLC12A3/NCC, SLC12A5/KCC2 or SLC12A6/KCC3, regulating their activity. Mediates regulatory volume increase in response to hyperosmotic stress by catalyzing phosphorylation of ion cotransporters SLC12A1/NKCC2, SLC12A2/NKCC1 and SLC12A6/KCC3 downstream of WNK1 and WNK3 kinases. Phosphorylation of Na-K-Cl cotransporters SLC12A2/NKCC1 and SLC12A2/NKCC1 promote their activation and ion influx; simultaneously, phosphorylation of K-Cl cotransporters SLC12A5/KCC2 and SLC12A6/KCC3 inhibit their activity, blocking ion efflux. Acts as a regulator of NaCl reabsorption in the distal nephron by mediating phosphorylation and activation of the thiazide-sensitive Na-Cl cotransporter SLC12A3/NCC in distal convoluted tubule cells of kidney downstream of WNK4. Also acts as a regulator of angiogenesis in endothelial cells downstream of WNK1. Acts as an activator of inward rectifier potassium channels KCNJ2/Kir2.1 and KCNJ4/Kir2.3 downstream of WNK1: recognizes and binds the RXFXV/I variant motif on KCNJ2/Kir2.1 and KCNJ4/Kir2.3 and regulates their localization to the cell membrane without mediating their phosphorylation. Phosphorylates RELL1, RELL2 and RELT. Phosphorylates PAK1. Phosphorylates PLSCR1 in the presence of RELT.","Effector serine/threonine-protein kinase component of the WNK-SPAK/OSR1 kinase cascade, which is involved in various processes, such as ion transport, response to hypertonic stress and blood pressure. Specifically recognizes and binds proteins with a RFXV motif. Acts downstream of WNK kinases (WNK1, WNK2, WNK3 or WNK4): following activation by WNK kinases, catalyzes phosphorylation of ion cotransporters, such as SLC12A1/NKCC2, SLC12A2/NKCC1, SLC12A3/NCC, SLC12A5/KCC2 or SLC12A6/KCC3, regulating their activity. Mediates regulatory volume increase in response to hyperosmotic stress by catalyzing phosphorylation of ion cotransporters SLC12A1/NKCC2, SLC12A2/NKCC1 and SLC12A6/KCC3 downstream of WNK1 and WNK3 kinases. Phosphorylation of Na-K-Cl cotransporters SLC12A2/NKCC1 and SLC12A2/NKCC1 promote their activation and ion influx; simultaneously, phosphorylation of K-Cl cotransporters SLC12A5/KCC2 and SLC12A6/KCC3 inhibit their activity, blocking ion efflux. Acts as a regulator of NaCl reabsorption in the distal nephron by mediating phosphorylation and activation of the thiazide-sensitive Na-Cl cotransporter SLC12A3/NCC in distal convoluted tubule cells of kidney downstream of WNK4. Also acts as a regulator of angiogenesis in endothelial cells downstream of WNK1. Acts as an activator of inward rectifier potassium channels KCNJ2/Kir2.1 and KCNJ4/Kir2.3 downstream of WNK1: recognizes and binds the RXFXV/I variant motif on KCNJ2/Kir2.1 and KCNJ4/Kir2.3 and regulates their localization to the cell membrane without mediating their phosphorylation. Phosphorylates RELL1, RELL2 and RELT. Phosphorylates PAK1. Phosphorylates PLSCR1 in the presence of RELT.",,,,,,,GO:0005524; GO:0042802; GO:0099106; GO:0000287; GO:0019870; GO:0019901; GO:0004674; GO:0044325,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.4859,0.4859,0.2855,0.4859,0.4859,5,0.4458,0.5623,yes
KDM1A_RAT,A0A8I6G2K8,ESM2Text,Eukaryota,852,"Histone demethylase that can demethylate both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Acts as a corepressor by mediating demethylation of H3K4me, a specific tag for epigenetic transcriptional activation. Demethylates both mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me. May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. Also acts as a coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and mediating demethylation of H3K9me, a specific tag for epigenetic transcriptional repression. The presence of PRKCB in AR-containing complexes, which mediates phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag that prevents demethylation H3K4me, prevents H3K4me demethylase activity of KDM1A. Demethylates di-methylated 'Lys-370' of p53/TP53 which prevents interaction of p53/TP53 with TP53BP1 and represses p53/TP53-mediated transcriptional activation. Demethylates and stabilizes the DNA methylase DNMT1. Demethylates methylated 'Lys-42' and methylated 'Lys- 117' of SOX2. Required for gastrulation during embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Facilitates epithelial-to- mesenchymal transition by acting as an effector of SNAI1-mediated transcription repression of epithelial markers E-cadherin/CDH1, CDN7 and KRT8. Required for the maintenance of the silenced state of the SNAI1 target genes E-cadherin/CDH1 and CDN7. Required for the repression of GIPR expression.","Enzyme that degrades poly(R)-beta-hydroxyendocannabinoid and neuropeptide, such as R-beta-MAD2 and R-beta-MAD3. Acts also as a neuroprotective factor. Preferentially degrades poly(R)-beta-hydroxybutyrate (PBA) and poly(R)-beta-hydroxyvalerate (PBAV). Required for the anti-inflammatory effects of the alpha-amylase inflammasome. Involved in histone H3 deacetylation and the regulation of cell cycle progression through H3 acetylation at pro-MUC1 and H3 acetylation at pro-MUC2. Affects pro-MUC1 levels through a mechanism that is independent of the ubiquitin ligase activity.",No,No,No,No,No,not-Yes,GO:0003682; GO:0019899; GO:0140682; GO:0050660; GO:0032454; GO:0043426; GO:0003723; GO:0061629; GO:0003713; GO:0003714,,GO:0016787,,,,,0.207,,,,1,0.207,0.2623,no
KDM1A_RAT,A0A8I6G2K8,Prot2Text,Eukaryota,852,"Histone demethylase that can demethylate both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Acts as a corepressor by mediating demethylation of H3K4me, a specific tag for epigenetic transcriptional activation. Demethylates both mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me. May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. Also acts as a coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and mediating demethylation of H3K9me, a specific tag for epigenetic transcriptional repression. The presence of PRKCB in AR-containing complexes, which mediates phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag that prevents demethylation H3K4me, prevents H3K4me demethylase activity of KDM1A. Demethylates di-methylated 'Lys-370' of p53/TP53 which prevents interaction of p53/TP53 with TP53BP1 and represses p53/TP53-mediated transcriptional activation. Demethylates and stabilizes the DNA methylase DNMT1. Demethylates methylated 'Lys-42' and methylated 'Lys- 117' of SOX2. Required for gastrulation during embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Facilitates epithelial-to- mesenchymal transition by acting as an effector of SNAI1-mediated transcription repression of epithelial markers E-cadherin/CDH1, CDN7 and KRT8. Required for the maintenance of the silenced state of the SNAI1 target genes E-cadherin/CDH1 and CDN7. Required for the repression of GIPR expression.","Probable histone demethylase that specifically demethylates H3K9me2, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Required for the demethylation of H3K9me2 at 'Lys-9' (H3K9me3) and 'Lys-27' (H3K27me2) on histone H3. May also demethylate 'Lys-27' on histone H4. Has no activity towards H3K9me2, H3K27me2 or H4K20me2. Required for chromosome segregation in meiosis.",Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0003682; GO:0019899; GO:0140682; GO:0050660; GO:0032454; GO:0043426; GO:0003723; GO:0061629; GO:0003713; GO:0003714,GO:0032454,GO:0032452,GO:0032452,GO:0032453,GO:0032452,0.3019,0.2839,0.2839,0.2786,0.2839,5,0.2864,0.2623,no
KDM1A_RAT,A0A8I6G2K8,ProtT3,Eukaryota,852,"Histone demethylase that can demethylate both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Acts as a corepressor by mediating demethylation of H3K4me, a specific tag for epigenetic transcriptional activation. Demethylates both mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me. May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. Also acts as a coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and mediating demethylation of H3K9me, a specific tag for epigenetic transcriptional repression. The presence of PRKCB in AR-containing complexes, which mediates phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag that prevents demethylation H3K4me, prevents H3K4me demethylase activity of KDM1A. Demethylates di-methylated 'Lys-370' of p53/TP53 which prevents interaction of p53/TP53 with TP53BP1 and represses p53/TP53-mediated transcriptional activation. Demethylates and stabilizes the DNA methylase DNMT1. Demethylates methylated 'Lys-42' and methylated 'Lys- 117' of SOX2. Required for gastrulation during embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Facilitates epithelial-to- mesenchymal transition by acting as an effector of SNAI1-mediated transcription repression of epithelial markers E-cadherin/CDH1, CDN7 and KRT8. Required for the maintenance of the silenced state of the SNAI1 target genes E-cadherin/CDH1 and CDN7. Required for the repression of GIPR expression.","Histone demethylase that specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code (By similarity). Specifically demethylates trimethylated histone H3 'Lys-4' (H3K4me3) and monomethylated histone H3 'Lys-4' (H3K4me1) (By similarity). Demethylation of histone H3 'Lys-4' (H3",Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0003682; GO:0019899; GO:0140682; GO:0050660; GO:0032454; GO:0043426; GO:0003723; GO:0061629; GO:0003713; GO:0003714,GO:0032452,GO:0032452,GO:0032452,GO:0032452,GO:0032452,0.2839,0.2839,0.2839,0.2839,0.2839,5,0.2839,0.2623,no
KDM1A_RAT,A0A8I6G2K8,ProtTale,Eukaryota,852,"Histone demethylase that can demethylate both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Acts as a corepressor by mediating demethylation of H3K4me, a specific tag for epigenetic transcriptional activation. Demethylates both mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me. May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. Also acts as a coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and mediating demethylation of H3K9me, a specific tag for epigenetic transcriptional repression. The presence of PRKCB in AR-containing complexes, which mediates phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag that prevents demethylation H3K4me, prevents H3K4me demethylase activity of KDM1A. Demethylates di-methylated 'Lys-370' of p53/TP53 which prevents interaction of p53/TP53 with TP53BP1 and represses p53/TP53-mediated transcriptional activation. Demethylates and stabilizes the DNA methylase DNMT1. Demethylates methylated 'Lys-42' and methylated 'Lys- 117' of SOX2. Required for gastrulation during embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Facilitates epithelial-to- mesenchymal transition by acting as an effector of SNAI1-mediated transcription repression of epithelial markers E-cadherin/CDH1, CDN7 and KRT8. Required for the maintenance of the silenced state of the SNAI1 target genes E-cadherin/CDH1 and CDN7. Required for the repression of GIPR expression.",Serine/threonine-protein kinase involved in pre-mRNA splicing as component of the spliceosome.,No,No,No,No,No,not-Yes,GO:0003682; GO:0019899; GO:0140682; GO:0050660; GO:0032454; GO:0043426; GO:0003723; GO:0061629; GO:0003713; GO:0003714,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,0.2383,0.2383,0.2383,0.1344,0.2383,5,0.2175,0.2623,no
KDM1A_RAT,A0A8I6G2K8,Protein2Text,Eukaryota,852,"Histone demethylase that can demethylate both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Acts as a corepressor by mediating demethylation of H3K4me, a specific tag for epigenetic transcriptional activation. Demethylates both mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me. May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. Also acts as a coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and mediating demethylation of H3K9me, a specific tag for epigenetic transcriptional repression. The presence of PRKCB in AR-containing complexes, which mediates phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag that prevents demethylation H3K4me, prevents H3K4me demethylase activity of KDM1A. Demethylates di-methylated 'Lys-370' of p53/TP53 which prevents interaction of p53/TP53 with TP53BP1 and represses p53/TP53-mediated transcriptional activation. Demethylates and stabilizes the DNA methylase DNMT1. Demethylates methylated 'Lys-42' and methylated 'Lys- 117' of SOX2. Required for gastrulation during embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Facilitates epithelial-to- mesenchymal transition by acting as an effector of SNAI1-mediated transcription repression of epithelial markers E-cadherin/CDH1, CDN7 and KRT8. Required for the maintenance of the silenced state of the SNAI1 target genes E-cadherin/CDH1 and CDN7. Required for the repression of GIPR expression.","The molecular function of this protein is not explicitly stated in the provided information. However, based on the context, it is likely that this protein is a histone demethylase, which is an enzyme that removes methyl groups from histone proteins. Histone demethylases are involved in the regulation of gene expression by removing methyl groups from histones, which in turn affects the structure of chromatin and the accessibility of DNA to transcription factors.",Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0003682; GO:0019899; GO:0140682; GO:0050660; GO:0032454; GO:0043426; GO:0003723; GO:0061629; GO:0003713; GO:0003714,,,GO:0032452,GO:0032452,GO:0032453,,,0.2839,0.2839,0.2786,3,0.2821,0.2623,no
KDM1A_RAT,A0A8I6G2K8,Reference,Eukaryota,852,"Histone demethylase that can demethylate both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Acts as a corepressor by mediating demethylation of H3K4me, a specific tag for epigenetic transcriptional activation. Demethylates both mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me. May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. Also acts as a coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and mediating demethylation of H3K9me, a specific tag for epigenetic transcriptional repression. The presence of PRKCB in AR-containing complexes, which mediates phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag that prevents demethylation H3K4me, prevents H3K4me demethylase activity of KDM1A. Demethylates di-methylated 'Lys-370' of p53/TP53 which prevents interaction of p53/TP53 with TP53BP1 and represses p53/TP53-mediated transcriptional activation. Demethylates and stabilizes the DNA methylase DNMT1. Demethylates methylated 'Lys-42' and methylated 'Lys- 117' of SOX2. Required for gastrulation during embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Facilitates epithelial-to- mesenchymal transition by acting as an effector of SNAI1-mediated transcription repression of epithelial markers E-cadherin/CDH1, CDN7 and KRT8. Required for the maintenance of the silenced state of the SNAI1 target genes E-cadherin/CDH1 and CDN7. Required for the repression of GIPR expression.","Histone demethylase that can demethylate both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Acts as a corepressor by mediating demethylation of H3K4me, a specific tag for epigenetic transcriptional activation. Demethylates both mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me. May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. Also acts as a coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and mediating demethylation of H3K9me, a specific tag for epigenetic transcriptional repression. The presence of PRKCB in AR-containing complexes, which mediates phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag that prevents demethylation H3K4me, prevents H3K4me demethylase activity of KDM1A. Demethylates di-methylated 'Lys-370' of p53/TP53 which prevents interaction of p53/TP53 with TP53BP1 and represses p53/TP53-mediated transcriptional activation. Demethylates and stabilizes the DNA methylase DNMT1. Demethylates methylated 'Lys-42' and methylated 'Lys- 117' of SOX2. Required for gastrulation during embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Facilitates epithelial-to- mesenchymal transition by acting as an effector of SNAI1-mediated transcription repression of epithelial markers E-cadherin/CDH1, CDN7 and KRT8. Required for the maintenance of the silenced state of the SNAI1 target genes E-cadherin/CDH1 and CDN7. Required for the repression of GIPR expression.",,,,,,,GO:0003682; GO:0019899; GO:0140682; GO:0050660; GO:0032454; GO:0043426; GO:0003723; GO:0061629; GO:0003713; GO:0003714,GO:0035596; GO:0035598; GO:0050660,GO:0035596; GO:0035598; GO:0050660,GO:0016491; GO:0032452,GO:0016491; GO:0071949; GO:0032452,GO:0016491; GO:0071949; GO:0003682,0.2991,0.2991,0.3494,0.4543,0.5354,5,0.3875,0.2623,no
HDAC6_RAT,A0A8I6GM68,ESM2Text,Eukaryota,1183,"Deacetylates a wide range of non-histone substrates. Plays a central role in microtubule-dependent cell motility by mediating deacetylation of tubulin. Required for cilia disassembly via deacetylation of alpha-tubulin. Alpha-tubulin deacetylation results in destabilization of dynamic microtubules. Promotes deacetylation of CTTN, leading to actin polymerization, promotion of autophagosome-lysosome fusion and completion of autophagy. Deacetylates SQSTM1. Deacetylates peroxiredoxins PRDX1 and PRDX2, decreasing their reducing activity. Deacetylates antiviral protein RIGI in the presence of viral mRNAs which is required for viral RNA detection by RIGI. Sequentially deacetylates and polyubiquitinates DNA mismatch repair protein MSH2 which leads to MSH2 degradation, reducing cellular sensitivity to DNA-damaging agents and decreasing cellular DNA mismatch repair activities. Deacetylates DNA mismatch repair protein MLH1 which prevents recruitment of the MutL alpha complex (formed by the MLH1-PMS2 heterodimer) to the MutS alpha complex (formed by the MSH2-MSH6 heterodimer), leading to tolerance of DNA damage. Deacetylates RHOT1/MIRO1 which blocks mitochondrial transport and mediates axon growth inhibition. Deacetylates transcription factor SP1 which leads to increased expression of ENG, positively regulating angiogenesis. Deacetylates KHDRBS1/SAM68 which regulates alternative splicing by inhibiting the inclusion of CD44 alternate exons. Deacetylates PRDM16. Promotes odontoblast differentiation following IPO7- mediated nuclear import and subsequent repression of RUNX2 expression. In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and targets them to the aggresome, facilitating their clearance by autophagy.","Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Also involved in protein deacetylation: acts as a protein decrotonylase by mediating protein decrotonylation ((2E)-butenoyl) of histones. Deacetylates HSPA1A and HSPA1B at 'Lys-77' leading to their preferential binding to co-chaperone STUB1. In addition to protein decrotonylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating protein decrotonylation ((2E)-butenoyl) of histones.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0003779; GO:0043014; GO:0042030; GO:0008013; GO:0048487; GO:0019213; GO:0070840; GO:0019899; GO:0004407; GO:0042826; GO:0051879; GO:0008017; GO:0051787; GO:0036479; GO:0031593; GO:0033558; GO:0000978; GO:0048156; GO:0001222; GO:0042903; GO:0043130; GO:0061630; GO:0031625; GO:0008270,GO:0004407,GO:0004407,GO:0004407,GO:0004407,GO:0004407,0.2403,0.2403,0.2403,0.2403,0.2403,5,0.2403,0.4054,no
HDAC6_RAT,A0A8I6GM68,Prot2Text,Eukaryota,1183,"Deacetylates a wide range of non-histone substrates. Plays a central role in microtubule-dependent cell motility by mediating deacetylation of tubulin. Required for cilia disassembly via deacetylation of alpha-tubulin. Alpha-tubulin deacetylation results in destabilization of dynamic microtubules. Promotes deacetylation of CTTN, leading to actin polymerization, promotion of autophagosome-lysosome fusion and completion of autophagy. Deacetylates SQSTM1. Deacetylates peroxiredoxins PRDX1 and PRDX2, decreasing their reducing activity. Deacetylates antiviral protein RIGI in the presence of viral mRNAs which is required for viral RNA detection by RIGI. Sequentially deacetylates and polyubiquitinates DNA mismatch repair protein MSH2 which leads to MSH2 degradation, reducing cellular sensitivity to DNA-damaging agents and decreasing cellular DNA mismatch repair activities. Deacetylates DNA mismatch repair protein MLH1 which prevents recruitment of the MutL alpha complex (formed by the MLH1-PMS2 heterodimer) to the MutS alpha complex (formed by the MSH2-MSH6 heterodimer), leading to tolerance of DNA damage. Deacetylates RHOT1/MIRO1 which blocks mitochondrial transport and mediates axon growth inhibition. Deacetylates transcription factor SP1 which leads to increased expression of ENG, positively regulating angiogenesis. Deacetylates KHDRBS1/SAM68 which regulates alternative splicing by inhibiting the inclusion of CD44 alternate exons. Deacetylates PRDM16. Promotes odontoblast differentiation following IPO7- mediated nuclear import and subsequent repression of RUNX2 expression. In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and targets them to the aggresome, facilitating their clearance by autophagy.","Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D. Deacetylates HSPA1A and HSPA1A at 'Lys-77' leading to their preferential binding to co-chaperone STUB1.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0003779; GO:0043014; GO:0042030; GO:0008013; GO:0048487; GO:0019213; GO:0070840; GO:0019899; GO:0004407; GO:0042826; GO:0051879; GO:0008017; GO:0051787; GO:0036479; GO:0031593; GO:0033558; GO:0000978; GO:0048156; GO:0001222; GO:0042903; GO:0043130; GO:0061630; GO:0031625; GO:0008270,GO:0004407,GO:0004407,GO:0004407,GO:0004407,GO:0004407,0.2403,0.2403,0.2403,0.2403,0.2403,5,0.2403,0.4054,no
HDAC6_RAT,A0A8I6GM68,ProtT3,Eukaryota,1183,"Deacetylates a wide range of non-histone substrates. Plays a central role in microtubule-dependent cell motility by mediating deacetylation of tubulin. Required for cilia disassembly via deacetylation of alpha-tubulin. Alpha-tubulin deacetylation results in destabilization of dynamic microtubules. Promotes deacetylation of CTTN, leading to actin polymerization, promotion of autophagosome-lysosome fusion and completion of autophagy. Deacetylates SQSTM1. Deacetylates peroxiredoxins PRDX1 and PRDX2, decreasing their reducing activity. Deacetylates antiviral protein RIGI in the presence of viral mRNAs which is required for viral RNA detection by RIGI. Sequentially deacetylates and polyubiquitinates DNA mismatch repair protein MSH2 which leads to MSH2 degradation, reducing cellular sensitivity to DNA-damaging agents and decreasing cellular DNA mismatch repair activities. Deacetylates DNA mismatch repair protein MLH1 which prevents recruitment of the MutL alpha complex (formed by the MLH1-PMS2 heterodimer) to the MutS alpha complex (formed by the MSH2-MSH6 heterodimer), leading to tolerance of DNA damage. Deacetylates RHOT1/MIRO1 which blocks mitochondrial transport and mediates axon growth inhibition. Deacetylates transcription factor SP1 which leads to increased expression of ENG, positively regulating angiogenesis. Deacetylates KHDRBS1/SAM68 which regulates alternative splicing by inhibiting the inclusion of CD44 alternate exons. Deacetylates PRDM16. Promotes odontoblast differentiation following IPO7- mediated nuclear import and subsequent repression of RUNX2 expression. In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and targets them to the aggresome, facilitating their clearance by autophagy.","Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Nucleus. Belongs to the histone deacetylase family. HD type 1 subfamily",Maybe,Maybe,Yes,Maybe,Yes,not-Yes,GO:0003779; GO:0043014; GO:0042030; GO:0008013; GO:0048487; GO:0019213; GO:0070840; GO:0019899; GO:0004407; GO:0042826; GO:0051879; GO:0008017; GO:0051787; GO:0036479; GO:0031593; GO:0033558; GO:0000978; GO:0048156; GO:0001222; GO:0042903; GO:0043130; GO:0061630; GO:0031625; GO:0008270,GO:0004407,GO:0004407,GO:0004407,GO:0004407,GO:0004407,0.2403,0.2403,0.2403,0.2403,0.2403,5,0.2403,0.4054,no
HDAC6_RAT,A0A8I6GM68,ProtTale,Eukaryota,1183,"Deacetylates a wide range of non-histone substrates. Plays a central role in microtubule-dependent cell motility by mediating deacetylation of tubulin. Required for cilia disassembly via deacetylation of alpha-tubulin. Alpha-tubulin deacetylation results in destabilization of dynamic microtubules. Promotes deacetylation of CTTN, leading to actin polymerization, promotion of autophagosome-lysosome fusion and completion of autophagy. Deacetylates SQSTM1. Deacetylates peroxiredoxins PRDX1 and PRDX2, decreasing their reducing activity. Deacetylates antiviral protein RIGI in the presence of viral mRNAs which is required for viral RNA detection by RIGI. Sequentially deacetylates and polyubiquitinates DNA mismatch repair protein MSH2 which leads to MSH2 degradation, reducing cellular sensitivity to DNA-damaging agents and decreasing cellular DNA mismatch repair activities. Deacetylates DNA mismatch repair protein MLH1 which prevents recruitment of the MutL alpha complex (formed by the MLH1-PMS2 heterodimer) to the MutS alpha complex (formed by the MSH2-MSH6 heterodimer), leading to tolerance of DNA damage. Deacetylates RHOT1/MIRO1 which blocks mitochondrial transport and mediates axon growth inhibition. Deacetylates transcription factor SP1 which leads to increased expression of ENG, positively regulating angiogenesis. Deacetylates KHDRBS1/SAM68 which regulates alternative splicing by inhibiting the inclusion of CD44 alternate exons. Deacetylates PRDM16. Promotes odontoblast differentiation following IPO7- mediated nuclear import and subsequent repression of RUNX2 expression. In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and targets them to the aggresome, facilitating their clearance by autophagy.","Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.",Maybe,Maybe,Yes,Maybe,Yes,not-Yes,GO:0003779; GO:0043014; GO:0042030; GO:0008013; GO:0048487; GO:0019213; GO:0070840; GO:0019899; GO:0004407; GO:0042826; GO:0051879; GO:0008017; GO:0051787; GO:0036479; GO:0031593; GO:0033558; GO:0000978; GO:0048156; GO:0001222; GO:0042903; GO:0043130; GO:0061630; GO:0031625; GO:0008270,GO:0004407,GO:0004407,GO:0004407,GO:0004407,GO:0004407,0.2403,0.2403,0.2403,0.2403,0.2403,5,0.2403,0.4054,no
HDAC6_RAT,A0A8I6GM68,Protein2Text,Eukaryota,1183,"Deacetylates a wide range of non-histone substrates. Plays a central role in microtubule-dependent cell motility by mediating deacetylation of tubulin. Required for cilia disassembly via deacetylation of alpha-tubulin. Alpha-tubulin deacetylation results in destabilization of dynamic microtubules. Promotes deacetylation of CTTN, leading to actin polymerization, promotion of autophagosome-lysosome fusion and completion of autophagy. Deacetylates SQSTM1. Deacetylates peroxiredoxins PRDX1 and PRDX2, decreasing their reducing activity. Deacetylates antiviral protein RIGI in the presence of viral mRNAs which is required for viral RNA detection by RIGI. Sequentially deacetylates and polyubiquitinates DNA mismatch repair protein MSH2 which leads to MSH2 degradation, reducing cellular sensitivity to DNA-damaging agents and decreasing cellular DNA mismatch repair activities. Deacetylates DNA mismatch repair protein MLH1 which prevents recruitment of the MutL alpha complex (formed by the MLH1-PMS2 heterodimer) to the MutS alpha complex (formed by the MSH2-MSH6 heterodimer), leading to tolerance of DNA damage. Deacetylates RHOT1/MIRO1 which blocks mitochondrial transport and mediates axon growth inhibition. Deacetylates transcription factor SP1 which leads to increased expression of ENG, positively regulating angiogenesis. Deacetylates KHDRBS1/SAM68 which regulates alternative splicing by inhibiting the inclusion of CD44 alternate exons. Deacetylates PRDM16. Promotes odontoblast differentiation following IPO7- mediated nuclear import and subsequent repression of RUNX2 expression. In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and targets them to the aggresome, facilitating their clearance by autophagy.","The molecular function of this protein is acetyltransferase activity, which is a type of enzyme activity that adds an acetyl group to a target molecule, such as a protein or other molecule.",No,No,No,No,No,not-Yes,GO:0003779; GO:0043014; GO:0042030; GO:0008013; GO:0048487; GO:0019213; GO:0070840; GO:0019899; GO:0004407; GO:0042826; GO:0051879; GO:0008017; GO:0051787; GO:0036479; GO:0031593; GO:0033558; GO:0000978; GO:0048156; GO:0001222; GO:0042903; GO:0043130; GO:0061630; GO:0031625; GO:0008270,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.1397,0.1397,0.1397,0.1397,0.1397,5,0.1397,0.4054,no
HDAC6_RAT,A0A8I6GM68,Reference,Eukaryota,1183,"Deacetylates a wide range of non-histone substrates. Plays a central role in microtubule-dependent cell motility by mediating deacetylation of tubulin. Required for cilia disassembly via deacetylation of alpha-tubulin. Alpha-tubulin deacetylation results in destabilization of dynamic microtubules. Promotes deacetylation of CTTN, leading to actin polymerization, promotion of autophagosome-lysosome fusion and completion of autophagy. Deacetylates SQSTM1. Deacetylates peroxiredoxins PRDX1 and PRDX2, decreasing their reducing activity. Deacetylates antiviral protein RIGI in the presence of viral mRNAs which is required for viral RNA detection by RIGI. Sequentially deacetylates and polyubiquitinates DNA mismatch repair protein MSH2 which leads to MSH2 degradation, reducing cellular sensitivity to DNA-damaging agents and decreasing cellular DNA mismatch repair activities. Deacetylates DNA mismatch repair protein MLH1 which prevents recruitment of the MutL alpha complex (formed by the MLH1-PMS2 heterodimer) to the MutS alpha complex (formed by the MSH2-MSH6 heterodimer), leading to tolerance of DNA damage. Deacetylates RHOT1/MIRO1 which blocks mitochondrial transport and mediates axon growth inhibition. Deacetylates transcription factor SP1 which leads to increased expression of ENG, positively regulating angiogenesis. Deacetylates KHDRBS1/SAM68 which regulates alternative splicing by inhibiting the inclusion of CD44 alternate exons. Deacetylates PRDM16. Promotes odontoblast differentiation following IPO7- mediated nuclear import and subsequent repression of RUNX2 expression. In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and targets them to the aggresome, facilitating their clearance by autophagy.","Deacetylates a wide range of non-histone substrates. Plays a central role in microtubule-dependent cell motility by mediating deacetylation of tubulin. Required for cilia disassembly via deacetylation of alpha-tubulin. Alpha-tubulin deacetylation results in destabilization of dynamic microtubules. Promotes deacetylation of CTTN, leading to actin polymerization, promotion of autophagosome-lysosome fusion and completion of autophagy. Deacetylates SQSTM1. Deacetylates peroxiredoxins PRDX1 and PRDX2, decreasing their reducing activity. Deacetylates antiviral protein RIGI in the presence of viral mRNAs which is required for viral RNA detection by RIGI. Sequentially deacetylates and polyubiquitinates DNA mismatch repair protein MSH2 which leads to MSH2 degradation, reducing cellular sensitivity to DNA-damaging agents and decreasing cellular DNA mismatch repair activities. Deacetylates DNA mismatch repair protein MLH1 which prevents recruitment of the MutL alpha complex (formed by the MLH1-PMS2 heterodimer) to the MutS alpha complex (formed by the MSH2-MSH6 heterodimer), leading to tolerance of DNA damage. Deacetylates RHOT1/MIRO1 which blocks mitochondrial transport and mediates axon growth inhibition. Deacetylates transcription factor SP1 which leads to increased expression of ENG, positively regulating angiogenesis. Deacetylates KHDRBS1/SAM68 which regulates alternative splicing by inhibiting the inclusion of CD44 alternate exons. Deacetylates PRDM16. Promotes odontoblast differentiation following IPO7- mediated nuclear import and subsequent repression of RUNX2 expression. In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and targets them to the aggresome, facilitating their clearance by autophagy.",,,,,,,GO:0003779; GO:0043014; GO:0042030; GO:0008013; GO:0048487; GO:0019213; GO:0070840; GO:0019899; GO:0004407; GO:0042826; GO:0051879; GO:0008017; GO:0051787; GO:0036479; GO:0031593; GO:0033558; GO:0000978; GO:0048156; GO:0001222; GO:0042903; GO:0043130; GO:0061630; GO:0031625; GO:0008270,GO:0033558,GO:0033558,GO:0033558; GO:0042903,GO:0016787; GO:0042903; GO:0008013,GO:0004407; GO:0042903,0.2718,0.2718,0.3103,0.5493,0.285,5,0.3376,0.4054,no
AL7A1_DANRE,A0A8M1PLI9,ESM2Text,Eukaryota,540,"Aldehyde dehydrogenase enzyme that mediates important protective effects. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation- derived aldehydes. Involved in cellular defense against hyperosmotic stress by metabolizing betaine aldehyde to betaine, an important cellular osmolyte and methyl donor.","Multifunctional enzyme mediating important protective effects. Metabolizes betaine aldehyde to betaine, an important cellular osmolyte and methyl donor. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation-derived aldehydes. Involved in lysine catabolism.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004029; GO:0043741; GO:0008802; GO:0004043,GO:0016620,GO:0004029; GO:0008802,GO:0008802,GO:0004029,GO:0004028,0.6216,0.8114,0.7274,0.749,0.521,5,0.6861,0.1852,no
AL7A1_DANRE,A0A8M1PLI9,Prot2Text,Eukaryota,540,"Aldehyde dehydrogenase enzyme that mediates important protective effects. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation- derived aldehydes. Involved in cellular defense against hyperosmotic stress by metabolizing betaine aldehyde to betaine, an important cellular osmolyte and methyl donor.","Multifunctional enzyme mediating important protective effects. Metabolizes betaine aldehyde to betaine, an important cellular osmolyte and methyl donor. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation-derived aldehydes. Involved in lysine catabolism.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004029; GO:0043741; GO:0008802; GO:0004043,GO:0008802; GO:0004029,GO:0008802,GO:0008802,GO:0004029; GO:0016620,GO:0008802,0.8114,0.7274,0.7274,0.7592,0.7274,5,0.7506,0.1852,no
AL7A1_DANRE,A0A8M1PLI9,ProtT3,Eukaryota,540,"Aldehyde dehydrogenase enzyme that mediates important protective effects. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation- derived aldehydes. Involved in cellular defense against hyperosmotic stress by metabolizing betaine aldehyde to betaine, an important cellular osmolyte and methyl donor.",Mitochondrial aldehyde dehydrogenase that catalyzes the NAD-dependent oxidation of aldehydes to their corresponding carboxylic acids (By similarity). Plays a role in the detoxification of lipid peroxidation-derived aldehydes (By similarity). Mitochondrion. Belongs to the aldehyde dehydrogenase family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004029; GO:0043741; GO:0008802; GO:0004043,GO:0004029,GO:0004029,GO:0004029; GO:0051287,GO:0004029,GO:0004029,0.749,0.749,0.6343,0.749,0.749,5,0.7261,0.1852,no
AL7A1_DANRE,A0A8M1PLI9,ProtTale,Eukaryota,540,"Aldehyde dehydrogenase enzyme that mediates important protective effects. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation- derived aldehydes. Involved in cellular defense against hyperosmotic stress by metabolizing betaine aldehyde to betaine, an important cellular osmolyte and methyl donor.",Catalyzes the oxidation of 2-methylsuccinyl-CoA to 2-methylsuccinate.,No,No,No,No,No,not-Yes,GO:0004029; GO:0043741; GO:0008802; GO:0004043,GO:0003995,GO:0016491,GO:0003995,GO:0016491,GO:0003995,0.2573,0.4738,0.2573,0.4738,0.2573,5,0.3439,0.1852,no
AL7A1_DANRE,A0A8M1PLI9,Protein2Text,Eukaryota,540,"Aldehyde dehydrogenase enzyme that mediates important protective effects. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation- derived aldehydes. Involved in cellular defense against hyperosmotic stress by metabolizing betaine aldehyde to betaine, an important cellular osmolyte and methyl donor.","The molecular function of the protein is involved in the oxidation of gamma-aminobutyrate (GABA) to succinate, which is an important step in the metabolism of GABA, a major inhibitory neurotransmitter in the brain.",No,No,No,No,No,not-Yes,GO:0004029; GO:0043741; GO:0008802; GO:0004043,GO:0003867,GO:0003867,GO:0003867,GO:0003867,GO:0003867,0.0,0.0,0.0,0.0,0.0,5,0.0,0.1852,no
AL7A1_DANRE,A0A8M1PLI9,Reference,Eukaryota,540,"Aldehyde dehydrogenase enzyme that mediates important protective effects. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation- derived aldehydes. Involved in cellular defense against hyperosmotic stress by metabolizing betaine aldehyde to betaine, an important cellular osmolyte and methyl donor.","Aldehyde dehydrogenase enzyme that mediates important protective effects. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation- derived aldehydes. Involved in cellular defense against hyperosmotic stress by metabolizing betaine aldehyde to betaine, an important cellular osmolyte and methyl donor.",,,,,,,GO:0004029; GO:0043741; GO:0008802; GO:0004043,GO:0004029,GO:0004029,GO:0004029; GO:0047019,GO:0004029; GO:0016620,GO:0004029; GO:0016620,0.749,0.749,0.6767,0.7592,0.7592,5,0.7386,0.1852,no
KSAMS_ACAKO,A0A9E8G339,ESM2Text,Eukaryota,393,Catalyzes the formation of S-adenosylmethionine from methionine and ATP.,"Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0046872; GO:0004478,GO:0004478; GO:0005524,GO:0004478,GO:0004478,GO:0004478,GO:0004478,0.8578,0.542,0.542,0.542,0.542,5,0.6052,0.5063,no
KSAMS_ACAKO,A0A9E8G339,Prot2Text,Eukaryota,393,Catalyzes the formation of S-adenosylmethionine from methionine and ATP.,"Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0046872; GO:0004478,GO:0004478,GO:0004478,GO:0004478,GO:0004478,GO:0004478,0.542,0.542,0.542,0.542,0.542,5,0.542,0.5063,no
KSAMS_ACAKO,A0A9E8G339,ProtT3,Eukaryota,393,Catalyzes the formation of S-adenosylmethionine from methionine and ATP.,"Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate. Cytoplasm. Belongs to the AdoMet synthase family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0046872; GO:0004478,GO:0004478,GO:0004478; GO:0005524,GO:0004478; GO:0005524,GO:0004478; GO:0005524,GO:0004478,0.542,0.8578,0.8578,0.8578,0.542,5,0.7315,0.5063,no
KSAMS_ACAKO,A0A9E8G339,ProtTale,Eukaryota,393,Catalyzes the formation of S-adenosylmethionine from methionine and ATP.,"Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0046872; GO:0004478,GO:0004478,GO:0004478; GO:0005524,GO:0004478; GO:0005524,GO:0004478; GO:0005524,GO:0004478; GO:0005524,0.542,0.8578,0.8578,0.8578,0.8578,5,0.7946,0.5063,no
KSAMS_ACAKO,A0A9E8G339,Protein2Text,Eukaryota,393,Catalyzes the formation of S-adenosylmethionine from methionine and ATP.,"The molecular function of this protein is to catalyze the decarboxylation of ornithine to putrescine, which is a step in the biosynthesis of polyamines. It is a decarboxylase enzyme that uses the pyridoxal 5'-phosphate cofactor to facilitate the decarboxylation reaction.",No,No,No,No,No,not-Yes,GO:0005524; GO:0046872; GO:0004478,GO:0004586,GO:0004586,GO:0004586,GO:0004586,GO:0004586,0.1537,0.1537,0.1537,0.1537,0.1537,5,0.1537,0.5063,no
KSAMS_ACAKO,A0A9E8G339,Reference,Eukaryota,393,Catalyzes the formation of S-adenosylmethionine from methionine and ATP.,Catalyzes the formation of S-adenosylmethionine from methionine and ATP.,,,,,,,GO:0005524; GO:0046872; GO:0004478,GO:0004478,GO:0004478; GO:0005524,GO:0004478,GO:0004478; GO:0005524,GO:0004478; GO:0005524,0.542,0.8578,0.542,0.8578,0.8578,5,0.7315,0.5063,no
HPAAL_RHIWR,A0A9J9HGY6,ESM2Text,Bacteria,251,"Aldolase which can catalyze in vitro the aldolisation reaction between hydroxypyruvate (HPA) or pyruvate (PA) and D- glyceraldehyde (D-GA) (Ref.2). The condensation of hydroxypyruvate and D-glyceraldehyde produces 2-dehydro-D-galactonate as the major product (Ref.2). The condensation of pyruvate and D-glyceraldehyde produces 2- dehydro-3-deoxy-L-galactonate (Ref.2). Can use other electrophilic substrates such as L-glyceraldehyde, D- and L-lactaldehyde and D- erythrose (Ref.2). Also catalyzes the retro-aldol type decarboxylation of oxaloacetate, a general property of known pyruvate aldolases (Ref.2, Ref.3).",Catalyzes the reversible retro-aldol cleavage of both 5-keto-4-deoxy-D-glucarate and 2-keto-3-deoxy-D-glucarate to pyruvate and tartronic semialdehyde.,Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0016832; GO:0046872,GO:0016832,GO:0016832,GO:0047444,GO:0016832,GO:0016829,0.7015,0.7015,0.2176,0.7015,0.5125,5,0.5669,0.3723,no
HPAAL_RHIWR,A0A9J9HGY6,Prot2Text,Bacteria,251,"Aldolase which can catalyze in vitro the aldolisation reaction between hydroxypyruvate (HPA) or pyruvate (PA) and D- glyceraldehyde (D-GA) (Ref.2). The condensation of hydroxypyruvate and D-glyceraldehyde produces 2-dehydro-D-galactonate as the major product (Ref.2). The condensation of pyruvate and D-glyceraldehyde produces 2- dehydro-3-deoxy-L-galactonate (Ref.2). Can use other electrophilic substrates such as L-glyceraldehyde, D- and L-lactaldehyde and D- erythrose (Ref.2). Also catalyzes the retro-aldol type decarboxylation of oxaloacetate, a general property of known pyruvate aldolases (Ref.2, Ref.3).",Catalyzes the reversible retro-aldol cleavage of 2-keto-3-deoxy-L-rhamnonate (KDR) to pyruvate and lactaldehyde.,Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0016832; GO:0046872,GO:0016832,,GO:0016832,GO:0016832,GO:0016832,0.7015,,0.7015,0.7015,0.7015,4,0.7015,0.3723,no
HPAAL_RHIWR,A0A9J9HGY6,ProtT3,Bacteria,251,"Aldolase which can catalyze in vitro the aldolisation reaction between hydroxypyruvate (HPA) or pyruvate (PA) and D- glyceraldehyde (D-GA) (Ref.2). The condensation of hydroxypyruvate and D-glyceraldehyde produces 2-dehydro-D-galactonate as the major product (Ref.2). The condensation of pyruvate and D-glyceraldehyde produces 2- dehydro-3-deoxy-L-galactonate (Ref.2). Can use other electrophilic substrates such as L-glyceraldehyde, D- and L-lactaldehyde and D- erythrose (Ref.2). Also catalyzes the retro-aldol type decarboxylation of oxaloacetate, a general property of known pyruvate aldolases (Ref.2, Ref.3).","Catalyzes the reversible retro-aldol cleavage of 4-hydroxy-2- ketoheptane-1,7-dioate (HKHD) to pyruvate and succinic semialdehyde. Belongs to the HpcH/HpaI aldolase family",Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0016832; GO:0046872,GO:0016832,GO:0016832,GO:0016832,GO:0016832,GO:0016832,0.7015,0.7015,0.7015,0.7015,0.7015,5,0.7015,0.3723,no
HPAAL_RHIWR,A0A9J9HGY6,ProtTale,Bacteria,251,"Aldolase which can catalyze in vitro the aldolisation reaction between hydroxypyruvate (HPA) or pyruvate (PA) and D- glyceraldehyde (D-GA) (Ref.2). The condensation of hydroxypyruvate and D-glyceraldehyde produces 2-dehydro-D-galactonate as the major product (Ref.2). The condensation of pyruvate and D-glyceraldehyde produces 2- dehydro-3-deoxy-L-galactonate (Ref.2). Can use other electrophilic substrates such as L-glyceraldehyde, D- and L-lactaldehyde and D- erythrose (Ref.2). Also catalyzes the retro-aldol type decarboxylation of oxaloacetate, a general property of known pyruvate aldolases (Ref.2, Ref.3).",Catalyzes the reversible retro-aldol cleavage of 2-keto-3-deoxy-6-phosphogluconate (KDPG) to pyruvate and D-glyceraldehyde-3-phosphate.,Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0016832; GO:0046872,GO:0016832,GO:0016829,GO:0016832,GO:0004462,GO:0008674,0.7015,0.5125,0.7015,0.3445,0.6017,5,0.5723,0.3723,no
HPAAL_RHIWR,A0A9J9HGY6,Protein2Text,Bacteria,251,"Aldolase which can catalyze in vitro the aldolisation reaction between hydroxypyruvate (HPA) or pyruvate (PA) and D- glyceraldehyde (D-GA) (Ref.2). The condensation of hydroxypyruvate and D-glyceraldehyde produces 2-dehydro-D-galactonate as the major product (Ref.2). The condensation of pyruvate and D-glyceraldehyde produces 2- dehydro-3-deoxy-L-galactonate (Ref.2). Can use other electrophilic substrates such as L-glyceraldehyde, D- and L-lactaldehyde and D- erythrose (Ref.2). Also catalyzes the retro-aldol type decarboxylation of oxaloacetate, a general property of known pyruvate aldolases (Ref.2, Ref.3).","The molecular function of this protein is an aldolase, which is an enzyme that catalyzes the reversible cleavage of an aldol compound into two simpler sugars.",Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0016832; GO:0046872,GO:0004332,GO:0004332,,GO:0016832,GO:0004332,0.6017,0.6017,,0.7015,0.6017,4,0.6267,0.3723,no
HPAAL_RHIWR,A0A9J9HGY6,Reference,Bacteria,251,"Aldolase which can catalyze in vitro the aldolisation reaction between hydroxypyruvate (HPA) or pyruvate (PA) and D- glyceraldehyde (D-GA) (Ref.2). The condensation of hydroxypyruvate and D-glyceraldehyde produces 2-dehydro-D-galactonate as the major product (Ref.2). The condensation of pyruvate and D-glyceraldehyde produces 2- dehydro-3-deoxy-L-galactonate (Ref.2). Can use other electrophilic substrates such as L-glyceraldehyde, D- and L-lactaldehyde and D- erythrose (Ref.2). Also catalyzes the retro-aldol type decarboxylation of oxaloacetate, a general property of known pyruvate aldolases (Ref.2, Ref.3).","Aldolase which can catalyze in vitro the aldolisation reaction between hydroxypyruvate (HPA) or pyruvate (PA) and D- glyceraldehyde (D-GA) (Ref.2). The condensation of hydroxypyruvate and D-glyceraldehyde produces 2-dehydro-D-galactonate as the major product (Ref.2). The condensation of pyruvate and D-glyceraldehyde produces 2- dehydro-3-deoxy-L-galactonate (Ref.2). Can use other electrophilic substrates such as L-glyceraldehyde, D- and L-lactaldehyde and D- erythrose (Ref.2). Also catalyzes the retro-aldol type decarboxylation of oxaloacetate, a general property of known pyruvate aldolases (Ref.2, Ref.3).",,,,,,,GO:0016832; GO:0046872,GO:0016832; GO:0008948,GO:0016832,GO:0016832,GO:0004332; GO:0016832,GO:0004332,0.6769,0.7015,0.7015,0.7407,0.6017,5,0.6845,0.3723,no
MRP4_BOVIN,A0AAA9T569,ESM2Text,Eukaryota,1315,"ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds and xenobiotics from cells. Transports a range of endogenous molecules that have a key role in cellular communication and signaling, including cyclic nucleotides such as cyclic AMP (cAMP) and cyclic GMP (cGMP), bile acids, steroid conjugates, urate, and prostaglandins. Mediates the ATP-dependent efflux of glutathione conjugates such as leukotriene C4 (LTC4) and leukotriene B4 (LTB4) too. The presence of GSH is necessary for the ATP-dependent transport of LTB4, whereas GSH is not required for the transport of LTC4. Mediates the cotransport of bile acids with reduced glutathione (GSH). Transports a wide range of drugs and their metabolites, including anticancer, antiviral and antibiotic molecules. Confers resistance to anticancer agents such as methotrexate.","ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds and xenobiotics from cells. Transports a range of endogenous molecules that have a key role in cellular communication and signaling, including cyclic nucleotides such as cyclic AMP (cAMP) and cyclic GMP (cGMP), bile acids, steroid conjugates, urate, and prostaglandins. Mediates also the ATP-dependent efflux of glutathione conjugates such as leukotriene C4 (LTC4) and leukotriene B4 (LTB4). The presence of GSH is necessary for the ATP-dependent transport of LTB4, whereas GSH is not required for the transport of LTC4. Mediates the cotransport of bile acids with reduced glutathione (GSH). Transports a wide range of drugs and their metabolites, including anticancer, antiviral and antibiotics molecules. Participates in the efflux of antibiotics such as anticancer agents, antibiotics and prostaglandins. Transports a wide range of drugs and their metabolites, including anticancer agents, inflammatory CCEs, procarcinogens and prostaglandins",Yes,Yes,Yes,Yes,Yes,Yes,GO:0015431; GO:0008559; GO:0005524; GO:0016887,GO:0005524; GO:0042626,GO:0042626; GO:0005524,GO:0042626,GO:0042626,GO:0042626,0.7583,0.7583,0.5245,0.5245,0.5245,5,0.618,0.5516,yes
MRP4_BOVIN,A0AAA9T569,Prot2Text,Eukaryota,1315,"ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds and xenobiotics from cells. Transports a range of endogenous molecules that have a key role in cellular communication and signaling, including cyclic nucleotides such as cyclic AMP (cAMP) and cyclic GMP (cGMP), bile acids, steroid conjugates, urate, and prostaglandins. Mediates the ATP-dependent efflux of glutathione conjugates such as leukotriene C4 (LTC4) and leukotriene B4 (LTB4) too. The presence of GSH is necessary for the ATP-dependent transport of LTB4, whereas GSH is not required for the transport of LTC4. Mediates the cotransport of bile acids with reduced glutathione (GSH). Transports a wide range of drugs and their metabolites, including anticancer, antiviral and antibiotic molecules. Confers resistance to anticancer agents such as methotrexate.","ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds and xenobiotics from cells. Transports a range of endogenous molecules that have a key role in cellular communication and signaling, including cyclic nucleotides such as cyclic AMP (cAMP) and cyclic GMP (cGMP), bile acids, steroid conjugates, urate, and prostaglandins. Mediates also the ATP-dependent efflux of glutathione conjugates such as leukotriene C4 (LTC4) and leukotriene B4 (LTB4). The presence of GSH is necessary for the ATP-dependent transport of LTB4, whereas GSH is not required for the transport of LTC4. Mediates the cotransport of bile acids with reduced glutathione (GSH). Transports a wide range of drugs and their metabolites, including anticancer, antiviral and antibiotics molecules. Participates in the efflux of antibiotics such as anticancer agents, antibiotics and prostaglandins. Transports a wide range of drugs and their metabolites, including anticancer agents, inflammatory CCEs, procarcinogens and prostaglandins",Yes,Yes,Yes,Yes,Yes,Yes,GO:0015431; GO:0008559; GO:0005524; GO:0016887,GO:0042626; GO:0005524,GO:0042626,GO:0042626,GO:0005524; GO:0042626,GO:0042626,0.7583,0.5245,0.5245,0.7583,0.5245,5,0.618,0.5516,yes
MRP4_BOVIN,A0AAA9T569,ProtT3,Eukaryota,1315,"ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds and xenobiotics from cells. Transports a range of endogenous molecules that have a key role in cellular communication and signaling, including cyclic nucleotides such as cyclic AMP (cAMP) and cyclic GMP (cGMP), bile acids, steroid conjugates, urate, and prostaglandins. Mediates the ATP-dependent efflux of glutathione conjugates such as leukotriene C4 (LTC4) and leukotriene B4 (LTB4) too. The presence of GSH is necessary for the ATP-dependent transport of LTB4, whereas GSH is not required for the transport of LTC4. Mediates the cotransport of bile acids with reduced glutathione (GSH). Transports a wide range of drugs and their metabolites, including anticancer, antiviral and antibiotic molecules. Confers resistance to anticancer agents such as methotrexate.",Membrane; Multi-pass membrane protein. Belongs to the ABC transporter superfamily. ABCB family. Heavy Metal importer (TC 3.A.1.210) subfamily,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0015431; GO:0008559; GO:0005524; GO:0016887,GO:0005524; GO:0042626,GO:0042626,GO:0005524; GO:0016887,GO:0042626; GO:0005524,GO:0042626,0.7583,0.5245,0.7259,0.7583,0.5245,5,0.6583,0.5516,yes
MRP4_BOVIN,A0AAA9T569,ProtTale,Eukaryota,1315,"ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds and xenobiotics from cells. Transports a range of endogenous molecules that have a key role in cellular communication and signaling, including cyclic nucleotides such as cyclic AMP (cAMP) and cyclic GMP (cGMP), bile acids, steroid conjugates, urate, and prostaglandins. Mediates the ATP-dependent efflux of glutathione conjugates such as leukotriene C4 (LTC4) and leukotriene B4 (LTB4) too. The presence of GSH is necessary for the ATP-dependent transport of LTB4, whereas GSH is not required for the transport of LTC4. Mediates the cotransport of bile acids with reduced glutathione (GSH). Transports a wide range of drugs and their metabolites, including anticancer, antiviral and antibiotic molecules. Confers resistance to anticancer agents such as methotrexate.",ATP-dependent transporter of the ATP-binding cassette (ABC) family that may play a role in the cellular efflux of sterols. May also play a role in the transport of glutathione S-conjugates across the plasma membrane.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0015431; GO:0008559; GO:0005524; GO:0016887,GO:0042626; GO:0005524,GO:0042626; GO:0005524,GO:0042626; GO:0005524,GO:0005524; GO:0042626,GO:0042626; GO:0005524,0.7583,0.7583,0.7583,0.7583,0.7583,5,0.7583,0.5516,yes
MRP4_BOVIN,A0AAA9T569,Protein2Text,Eukaryota,1315,"ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds and xenobiotics from cells. Transports a range of endogenous molecules that have a key role in cellular communication and signaling, including cyclic nucleotides such as cyclic AMP (cAMP) and cyclic GMP (cGMP), bile acids, steroid conjugates, urate, and prostaglandins. Mediates the ATP-dependent efflux of glutathione conjugates such as leukotriene C4 (LTC4) and leukotriene B4 (LTB4) too. The presence of GSH is necessary for the ATP-dependent transport of LTB4, whereas GSH is not required for the transport of LTC4. Mediates the cotransport of bile acids with reduced glutathione (GSH). Transports a wide range of drugs and their metabolites, including anticancer, antiviral and antibiotic molecules. Confers resistance to anticancer agents such as methotrexate.","The molecular function of this protein is to transport molecules across the cell membrane. Specifically, it is involved in the transport of lipids, which is essential for maintaining the integrity and function of cellular membranes. This protein is also involved in the transport of other molecules, such as ions and nutrients, across the cell membrane. It is a type of ATP-binding cassette (ABC) transporter, which uses energy from ATP hydrolysis to drive the transport of molecules across the membrane.",Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0015431; GO:0008559; GO:0005524; GO:0016887,GO:0042626,GO:0042626,,GO:0042626,GO:0042626,0.5245,0.5245,,0.5245,0.5245,4,0.5245,0.5516,yes
MRP4_BOVIN,A0AAA9T569,Reference,Eukaryota,1315,"ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds and xenobiotics from cells. Transports a range of endogenous molecules that have a key role in cellular communication and signaling, including cyclic nucleotides such as cyclic AMP (cAMP) and cyclic GMP (cGMP), bile acids, steroid conjugates, urate, and prostaglandins. Mediates the ATP-dependent efflux of glutathione conjugates such as leukotriene C4 (LTC4) and leukotriene B4 (LTB4) too. The presence of GSH is necessary for the ATP-dependent transport of LTB4, whereas GSH is not required for the transport of LTC4. Mediates the cotransport of bile acids with reduced glutathione (GSH). Transports a wide range of drugs and their metabolites, including anticancer, antiviral and antibiotic molecules. Confers resistance to anticancer agents such as methotrexate.","ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds and xenobiotics from cells. Transports a range of endogenous molecules that have a key role in cellular communication and signaling, including cyclic nucleotides such as cyclic AMP (cAMP) and cyclic GMP (cGMP), bile acids, steroid conjugates, urate, and prostaglandins. Mediates the ATP-dependent efflux of glutathione conjugates such as leukotriene C4 (LTC4) and leukotriene B4 (LTB4) too. The presence of GSH is necessary for the ATP-dependent transport of LTB4, whereas GSH is not required for the transport of LTC4. Mediates the cotransport of bile acids with reduced glutathione (GSH). Transports a wide range of drugs and their metabolites, including anticancer, antiviral and antibiotic molecules. Confers resistance to anticancer agents such as methotrexate.",,,,,,,GO:0015431; GO:0008559; GO:0005524; GO:0016887,GO:0042626; GO:0005524,GO:0005524; GO:0042626,GO:0005524; GO:0042626; GO:0015238; GO:0008514,GO:0005524; GO:0042626; GO:0015431,GO:0005524; GO:0042626; GO:0015238,0.7583,0.7583,0.7326,0.8264,0.7326,5,0.7616,0.5516,yes
E2609_XANAC,A0AAI7ZGC7,ESM2Text,Bacteria,431,"Effector protein that targets host peptidoglycan and acts as a peptidoglycan hydrolase. It contributes to direct killing of adjacent bacterial cells, thereby providing a competitive growth advantage for Xanthomonas in mixed bacterial communities.","Endonuclease that cleaves single-stranded RNA at 5' of uridylates and releases a product with a 2',3'-cyclic phosphate at the 3'-end.",No,No,No,No,No,not-Yes,GO:0004180,GO:0004521,GO:0004521,GO:0004521,GO:0004521,GO:0004521,0.158,0.158,0.158,0.158,0.158,5,0.158,0.2612,no
E2609_XANAC,A0AAI7ZGC7,Prot2Text,Bacteria,431,"Effector protein that targets host peptidoglycan and acts as a peptidoglycan hydrolase. It contributes to direct killing of adjacent bacterial cells, thereby providing a competitive growth advantage for Xanthomonas in mixed bacterial communities.",Can hydrolyze the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins. May play a role in the secretion of glycoproteins in the host.,No,No,No,No,No,not-Yes,GO:0004180,GO:0000224,GO:0000224,GO:0004564,GO:0016811,GO:0000224,0.3167,0.3167,0.3167,0.3717,0.3167,5,0.3277,0.2612,no
E2609_XANAC,A0AAI7ZGC7,ProtT3,Bacteria,431,"Effector protein that targets host peptidoglycan and acts as a peptidoglycan hydrolase. It contributes to direct killing of adjacent bacterial cells, thereby providing a competitive growth advantage for Xanthomonas in mixed bacterial communities.",Secreted. In the N-terminal section; belongs to the N-acetylmuramoyl-L-alanine amidase 2 family,Vague,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0004180,GO:0008745,GO:0008745,GO:0008745,GO:0008745,GO:0008745,0.32,0.32,0.32,0.32,0.32,5,0.32,0.2612,no
E2609_XANAC,A0AAI7ZGC7,ProtTale,Bacteria,431,"Effector protein that targets host peptidoglycan and acts as a peptidoglycan hydrolase. It contributes to direct killing of adjacent bacterial cells, thereby providing a competitive growth advantage for Xanthomonas in mixed bacterial communities.","Pore-forming component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria. The C-terminal 250 amino acids of this protein form a pore that allows passive diffusion of small molecules through the membrane. The full-length protein also has GTPase-activating protein (GAP) activity.",Yes,Yes,No,No,Maybe,not-Yes,GO:0004180,GO:0005096,GO:0005096,GO:0005096; GO:0022829,,GO:0005096,0.0765,0.0765,0.0809,,0.0765,4,0.0776,0.2612,no
E2609_XANAC,A0AAI7ZGC7,Protein2Text,Bacteria,431,"Effector protein that targets host peptidoglycan and acts as a peptidoglycan hydrolase. It contributes to direct killing of adjacent bacterial cells, thereby providing a competitive growth advantage for Xanthomonas in mixed bacterial communities.","The molecular function of this protein is unknown. However, based on its name, it is likely to be involved in some form of enzymatic activity, possibly related to breaking or modifying chemical bonds.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0004180,,,,,,,,,,,0,,0.2612,no
E2609_XANAC,A0AAI7ZGC7,Reference,Bacteria,431,"Effector protein that targets host peptidoglycan and acts as a peptidoglycan hydrolase. It contributes to direct killing of adjacent bacterial cells, thereby providing a competitive growth advantage for Xanthomonas in mixed bacterial communities.","Effector protein that targets host peptidoglycan and acts as a peptidoglycan hydrolase. It contributes to direct killing of adjacent bacterial cells, thereby providing a competitive growth advantage for Xanthomonas in mixed bacterial communities.",,,,,,,GO:0004180,GO:0061783,GO:0061783,GO:0061783,GO:0016787; GO:0008745,GO:0004553; GO:0016998,0.3278,0.3278,0.3278,0.477,0.2478,5,0.3416,0.2612,no
ASP5_TOXGO,A0MQA3,ESM2Text,Eukaryota,969,"In tachyzoites, plays an essential role in the export of several dense granule proteins into the host cell by cleaving the localization motif RRLxx (termed Toxoplasma export element (TEXEL)) located downstream of the N-terminal secretory signal sequence. However, can also regulate the export of proteins that lack the TEXEL motif, such as GRA24. Requires Arg at P3 and P2, and Leu at P1 in the substrate TEXEL motif and, specifically, cleaves after Leu. Cleaves GRA16; proteolytic cleavage is essential for the correct trafficking of GRA16 from the parasite into the infected host nucleus. Cleaves GRA19 and GRA20. Cleaves MYR1. Cleaves LCAT, GRA44, GRA46, GRA46, ROP35/WNG1 and ROP34/WNG2. By regulating the export of dense granule proteins into the host cell, regulates multiple processes during tachyzoite infection of host cells, including recruitment of host mitochondria to the parasitophorous vacuole (PV), formation of the nanotubular network (NTN) or intravacuolar network (IVN) which are membranous tubules that bud from the PV membrane into the vacuolar lumen and, up-regulation of host cell genes to facilitate the parasite infection and modulate the host innate immune response. At the bradyzoite stage, also involved in the formation of the cyst wall.","Protease responsible for cleaving and inactivating isoform Beta-1 of the proteasome, leading to down-regulate the proteasome activity and to down-regulate beta-catenin/CTNNB1 activity.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004190,GO:0008233,GO:0008233,GO:0008233,GO:0008233,GO:0008233,0.703,0.703,0.703,0.703,0.703,5,0.703,0.3586,no
ASP5_TOXGO,A0MQA3,Prot2Text,Eukaryota,969,"In tachyzoites, plays an essential role in the export of several dense granule proteins into the host cell by cleaving the localization motif RRLxx (termed Toxoplasma export element (TEXEL)) located downstream of the N-terminal secretory signal sequence. However, can also regulate the export of proteins that lack the TEXEL motif, such as GRA24. Requires Arg at P3 and P2, and Leu at P1 in the substrate TEXEL motif and, specifically, cleaves after Leu. Cleaves GRA16; proteolytic cleavage is essential for the correct trafficking of GRA16 from the parasite into the infected host nucleus. Cleaves GRA19 and GRA20. Cleaves MYR1. Cleaves LCAT, GRA44, GRA46, GRA46, ROP35/WNG1 and ROP34/WNG2. By regulating the export of dense granule proteins into the host cell, regulates multiple processes during tachyzoite infection of host cells, including recruitment of host mitochondria to the parasitophorous vacuole (PV), formation of the nanotubular network (NTN) or intravacuolar network (IVN) which are membranous tubules that bud from the PV membrane into the vacuolar lumen and, up-regulation of host cell genes to facilitate the parasite infection and modulate the host innate immune response. At the bradyzoite stage, also involved in the formation of the cyst wall.",Probable aspartic protease.,Maybe,Maybe,Maybe,Vague,No,not-Yes,GO:0004190,GO:0004190,GO:0004190,GO:0004190,GO:0004190,GO:0004190,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3586,no
ASP5_TOXGO,A0MQA3,ProtT3,Eukaryota,969,"In tachyzoites, plays an essential role in the export of several dense granule proteins into the host cell by cleaving the localization motif RRLxx (termed Toxoplasma export element (TEXEL)) located downstream of the N-terminal secretory signal sequence. However, can also regulate the export of proteins that lack the TEXEL motif, such as GRA24. Requires Arg at P3 and P2, and Leu at P1 in the substrate TEXEL motif and, specifically, cleaves after Leu. Cleaves GRA16; proteolytic cleavage is essential for the correct trafficking of GRA16 from the parasite into the infected host nucleus. Cleaves GRA19 and GRA20. Cleaves MYR1. Cleaves LCAT, GRA44, GRA46, GRA46, ROP35/WNG1 and ROP34/WNG2. By regulating the export of dense granule proteins into the host cell, regulates multiple processes during tachyzoite infection of host cells, including recruitment of host mitochondria to the parasitophorous vacuole (PV), formation of the nanotubular network (NTN) or intravacuolar network (IVN) which are membranous tubules that bud from the PV membrane into the vacuolar lumen and, up-regulation of host cell genes to facilitate the parasite infection and modulate the host innate immune response. At the bradyzoite stage, also involved in the formation of the cyst wall.",Probable intramembrane-cleaving aspartic protease. Membrane; Single-pass type II membrane protein. Belongs to the peptidase A1 family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004190,GO:0004190,GO:0004190,GO:0004190,GO:0004190,GO:0004190,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3586,no
ASP5_TOXGO,A0MQA3,ProtTale,Eukaryota,969,"In tachyzoites, plays an essential role in the export of several dense granule proteins into the host cell by cleaving the localization motif RRLxx (termed Toxoplasma export element (TEXEL)) located downstream of the N-terminal secretory signal sequence. However, can also regulate the export of proteins that lack the TEXEL motif, such as GRA24. Requires Arg at P3 and P2, and Leu at P1 in the substrate TEXEL motif and, specifically, cleaves after Leu. Cleaves GRA16; proteolytic cleavage is essential for the correct trafficking of GRA16 from the parasite into the infected host nucleus. Cleaves GRA19 and GRA20. Cleaves MYR1. Cleaves LCAT, GRA44, GRA46, GRA46, ROP35/WNG1 and ROP34/WNG2. By regulating the export of dense granule proteins into the host cell, regulates multiple processes during tachyzoite infection of host cells, including recruitment of host mitochondria to the parasitophorous vacuole (PV), formation of the nanotubular network (NTN) or intravacuolar network (IVN) which are membranous tubules that bud from the PV membrane into the vacuolar lumen and, up-regulation of host cell genes to facilitate the parasite infection and modulate the host innate immune response. At the bradyzoite stage, also involved in the formation of the cyst wall.",May be a receptor for extracellular matrix proteins.,Vague,Vague,Vague,Vague,No,not-Yes,GO:0004190,,,,,,,,,,,0,,0.3586,no
ASP5_TOXGO,A0MQA3,Protein2Text,Eukaryota,969,"In tachyzoites, plays an essential role in the export of several dense granule proteins into the host cell by cleaving the localization motif RRLxx (termed Toxoplasma export element (TEXEL)) located downstream of the N-terminal secretory signal sequence. However, can also regulate the export of proteins that lack the TEXEL motif, such as GRA24. Requires Arg at P3 and P2, and Leu at P1 in the substrate TEXEL motif and, specifically, cleaves after Leu. Cleaves GRA16; proteolytic cleavage is essential for the correct trafficking of GRA16 from the parasite into the infected host nucleus. Cleaves GRA19 and GRA20. Cleaves MYR1. Cleaves LCAT, GRA44, GRA46, GRA46, ROP35/WNG1 and ROP34/WNG2. By regulating the export of dense granule proteins into the host cell, regulates multiple processes during tachyzoite infection of host cells, including recruitment of host mitochondria to the parasitophorous vacuole (PV), formation of the nanotubular network (NTN) or intravacuolar network (IVN) which are membranous tubules that bud from the PV membrane into the vacuolar lumen and, up-regulation of host cell genes to facilitate the parasite infection and modulate the host innate immune response. At the bradyzoite stage, also involved in the formation of the cyst wall.","This protein is a tyrosine-protein phosphatase, which means it is involved in the removal of phosphate groups from tyrosine residues on proteins. This is a key step in signaling pathways and can have a significant impact on cellular behavior.",No,No,No,No,No,not-Yes,GO:0004190,GO:0004725,GO:0004726,GO:0004725,GO:0004725,GO:0004726,0.3561,0.3208,0.3561,0.3561,0.3208,5,0.342,0.3586,no
ASP5_TOXGO,A0MQA3,Reference,Eukaryota,969,"In tachyzoites, plays an essential role in the export of several dense granule proteins into the host cell by cleaving the localization motif RRLxx (termed Toxoplasma export element (TEXEL)) located downstream of the N-terminal secretory signal sequence. However, can also regulate the export of proteins that lack the TEXEL motif, such as GRA24. Requires Arg at P3 and P2, and Leu at P1 in the substrate TEXEL motif and, specifically, cleaves after Leu. Cleaves GRA16; proteolytic cleavage is essential for the correct trafficking of GRA16 from the parasite into the infected host nucleus. Cleaves GRA19 and GRA20. Cleaves MYR1. Cleaves LCAT, GRA44, GRA46, GRA46, ROP35/WNG1 and ROP34/WNG2. By regulating the export of dense granule proteins into the host cell, regulates multiple processes during tachyzoite infection of host cells, including recruitment of host mitochondria to the parasitophorous vacuole (PV), formation of the nanotubular network (NTN) or intravacuolar network (IVN) which are membranous tubules that bud from the PV membrane into the vacuolar lumen and, up-regulation of host cell genes to facilitate the parasite infection and modulate the host innate immune response. At the bradyzoite stage, also involved in the formation of the cyst wall.","In tachyzoites, plays an essential role in the export of several dense granule proteins into the host cell by cleaving the localization motif RRLxx (termed Toxoplasma export element (TEXEL)) located downstream of the N-terminal secretory signal sequence. However, can also regulate the export of proteins that lack the TEXEL motif, such as GRA24. Requires Arg at P3 and P2, and Leu at P1 in the substrate TEXEL motif and, specifically, cleaves after Leu. Cleaves GRA16; proteolytic cleavage is essential for the correct trafficking of GRA16 from the parasite into the infected host nucleus. Cleaves GRA19 and GRA20. Cleaves MYR1. Cleaves LCAT, GRA44, GRA46, GRA46, ROP35/WNG1 and ROP34/WNG2. By regulating the export of dense granule proteins into the host cell, regulates multiple processes during tachyzoite infection of host cells, including recruitment of host mitochondria to the parasitophorous vacuole (PV), formation of the nanotubular network (NTN) or intravacuolar network (IVN) which are membranous tubules that bud from the PV membrane into the vacuolar lumen and, up-regulation of host cell genes to facilitate the parasite infection and modulate the host innate immune response. At the bradyzoite stage, also involved in the formation of the cyst wall.",,,,,,,GO:0004190,GO:0004175,GO:0004175,GO:0004175,GO:0004252,GO:0004252,0.8001,0.8001,0.8001,0.6016,0.6016,5,0.7207,0.3586,no
END8B_MYCS2,A0QT90,ESM2Text,Bacteria,252,Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases.,"Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0140078; GO:0003684; GO:0000703; GO:0008270,GO:0019104,GO:0019104; GO:0003906,GO:0019104; GO:0003906,GO:0019104,GO:0019104; GO:0003906,0.4289,0.5689,0.5689,0.4289,0.5689,5,0.5129,0.489,no
END8B_MYCS2,A0QT90,Prot2Text,Bacteria,252,Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases.,"Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0140078; GO:0003684; GO:0000703; GO:0008270,GO:0019104; GO:0003906,GO:0019104; GO:0003906,GO:0019104; GO:0003906,GO:0016798; GO:0003906,GO:0019104; GO:0003906,0.5689,0.5689,0.5689,0.4822,0.5689,5,0.5516,0.489,no
END8B_MYCS2,A0QT90,ProtT3,Bacteria,252,Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases.,"Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. SIMIL",Yes,Yes,Yes,Yes,Yes,Yes,GO:0140078; GO:0003684; GO:0000703; GO:0008270,GO:0019104,GO:0019104; GO:0003906,GO:0019104; GO:0003906,GO:0019104; GO:0003906,GO:0003906,0.4289,0.5689,0.5689,0.5689,0.4039,5,0.5079,0.489,no
END8B_MYCS2,A0QT90,ProtTale,Bacteria,252,Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases.,"Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as a DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0140078; GO:0003684; GO:0000703; GO:0008270,GO:0019104; GO:0003906,GO:0019104,GO:0019104; GO:0016829,GO:0003906; GO:0016798,GO:0019104; GO:0016829,0.5689,0.4289,0.4696,0.4822,0.4696,5,0.4838,0.489,no
END8B_MYCS2,A0QT90,Protein2Text,Bacteria,252,Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases.,"This protein is involved in the molecular function of DNA repair. Specifically, it is a DNA repair enzyme that plays a role in the repair of damaged DNA. The molecular function of this protein is to facilitate the removal of DNA damage and restore the integrity of the DNA molecule. This is an important function in maintaining the stability and fidelity of the genome, and is essential for the prevention of mutations and genetic disorders.",Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0140078; GO:0003684; GO:0000703; GO:0008270,,,,,,,,,,,0,,0.489,no
END8B_MYCS2,A0QT90,Reference,Bacteria,252,Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases.,Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases.,,,,,,,GO:0140078; GO:0003684; GO:0000703; GO:0008270,GO:0019104; GO:0003677,GO:0019104; GO:0003684,GO:0019104; GO:0003684,GO:0016798; GO:0019104,GO:0016798; GO:0019104,0.6494,0.695,0.695,0.4595,0.4595,5,0.5917,0.489,no
LHR_MYCS2,A0QT91,ESM2Text,Bacteria,1507,"A 3'-5' helicase involved in repair of at least 3 types of DNA cross-links, mitomycin C (MMC), cisplatin, and psoralen-UVA. Translocates 3'-to-5' on single- stranded (ss)DNA, unwinding any encountered duplex nucleic acid. A 3'-ssDNA loading strand of at least 15 nucleotides is required for helicase activity. An RNA:DNA hybrid with a 3'-ssDNA loading strand is an 8-fold better helicase substrate than 3'-tailed double-stranded (ds)DNA; substrates where the helicase loads on a 3'-ssRNA tail (DNA:RNA and RNA:RNA) are not unwound. Only (d)ATP is hydrolyzed by the protein, which has no ATPase activity in the absence of ssDNA or ssRNA. Arg-279 and Trp-597 are needed to couple ATP hydrolysis to mechanical work; a salt bridge between Arg-280 and Glu- 550 closes a clamp around the ssDNA that is not large enough for dsDNA, while Ile-528 wedges between bases of the loading strand.",DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0043138; GO:0033679; GO:0005524; GO:0016887; GO:0003677; GO:0046872; GO:0004844,GO:0003678; GO:0005524; GO:0008094,GO:0003678; GO:0005524; GO:0016887,GO:0003678; GO:0016887,GO:0003678,GO:0004003,0.6483,0.7348,0.5747,0.4221,0.4221,5,0.5604,0.4814,no
LHR_MYCS2,A0QT91,Prot2Text,Bacteria,1507,"A 3'-5' helicase involved in repair of at least 3 types of DNA cross-links, mitomycin C (MMC), cisplatin, and psoralen-UVA. Translocates 3'-to-5' on single- stranded (ss)DNA, unwinding any encountered duplex nucleic acid. A 3'-ssDNA loading strand of at least 15 nucleotides is required for helicase activity. An RNA:DNA hybrid with a 3'-ssDNA loading strand is an 8-fold better helicase substrate than 3'-tailed double-stranded (ds)DNA; substrates where the helicase loads on a 3'-ssRNA tail (DNA:RNA and RNA:RNA) are not unwound. Only (d)ATP is hydrolyzed by the protein, which has no ATPase activity in the absence of ssDNA or ssRNA. Arg-279 and Trp-597 are needed to couple ATP hydrolysis to mechanical work; a salt bridge between Arg-280 and Glu- 550 closes a clamp around the ssDNA that is not large enough for dsDNA, while Ile-528 wedges between bases of the loading strand.","Helicase involved in DNA replication and repair. Binds to ssDNA in the presence of ATP and magnesium. Recruits the MCM helicase to the ssDNA, promoting its unwinding activity.",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0043138; GO:0033679; GO:0005524; GO:0016887; GO:0003677; GO:0046872; GO:0004844,GO:0003678; GO:0005524; GO:0003697,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,0.7114,0.6218,0.6218,0.6218,0.6218,5,0.6397,0.4814,no
LHR_MYCS2,A0QT91,ProtT3,Bacteria,1507,"A 3'-5' helicase involved in repair of at least 3 types of DNA cross-links, mitomycin C (MMC), cisplatin, and psoralen-UVA. Translocates 3'-to-5' on single- stranded (ss)DNA, unwinding any encountered duplex nucleic acid. A 3'-ssDNA loading strand of at least 15 nucleotides is required for helicase activity. An RNA:DNA hybrid with a 3'-ssDNA loading strand is an 8-fold better helicase substrate than 3'-tailed double-stranded (ds)DNA; substrates where the helicase loads on a 3'-ssRNA tail (DNA:RNA and RNA:RNA) are not unwound. Only (d)ATP is hydrolyzed by the protein, which has no ATPase activity in the absence of ssDNA or ssRNA. Arg-279 and Trp-597 are needed to couple ATP hydrolysis to mechanical work; a salt bridge between Arg-280 and Glu- 550 closes a clamp around the ssDNA that is not large enough for dsDNA, while Ile-528 wedges between bases of the loading strand.",DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks. Belongs to the helicase family. UvrD subfamily,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0043138; GO:0033679; GO:0005524; GO:0016887; GO:0003677; GO:0046872; GO:0004844,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0008094,0.6218,0.6218,0.6218,0.6218,0.4867,5,0.5948,0.4814,no
LHR_MYCS2,A0QT91,ProtTale,Bacteria,1507,"A 3'-5' helicase involved in repair of at least 3 types of DNA cross-links, mitomycin C (MMC), cisplatin, and psoralen-UVA. Translocates 3'-to-5' on single- stranded (ss)DNA, unwinding any encountered duplex nucleic acid. A 3'-ssDNA loading strand of at least 15 nucleotides is required for helicase activity. An RNA:DNA hybrid with a 3'-ssDNA loading strand is an 8-fold better helicase substrate than 3'-tailed double-stranded (ds)DNA; substrates where the helicase loads on a 3'-ssRNA tail (DNA:RNA and RNA:RNA) are not unwound. Only (d)ATP is hydrolyzed by the protein, which has no ATPase activity in the absence of ssDNA or ssRNA. Arg-279 and Trp-597 are needed to couple ATP hydrolysis to mechanical work; a salt bridge between Arg-280 and Glu- 550 closes a clamp around the ssDNA that is not large enough for dsDNA, while Ile-528 wedges between bases of the loading strand.",Able to cleave both 3' and 5' single-stranded DNA substrates.,No,No,No,No,No,not-Yes,GO:0043138; GO:0033679; GO:0005524; GO:0016887; GO:0003677; GO:0046872; GO:0004844,GO:0004518,GO:0004518,GO:0004527,GO:0004518,GO:0004518,0.247,0.247,0.2143,0.247,0.247,5,0.2405,0.4814,no
LHR_MYCS2,A0QT91,Protein2Text,Bacteria,1507,"A 3'-5' helicase involved in repair of at least 3 types of DNA cross-links, mitomycin C (MMC), cisplatin, and psoralen-UVA. Translocates 3'-to-5' on single- stranded (ss)DNA, unwinding any encountered duplex nucleic acid. A 3'-ssDNA loading strand of at least 15 nucleotides is required for helicase activity. An RNA:DNA hybrid with a 3'-ssDNA loading strand is an 8-fold better helicase substrate than 3'-tailed double-stranded (ds)DNA; substrates where the helicase loads on a 3'-ssRNA tail (DNA:RNA and RNA:RNA) are not unwound. Only (d)ATP is hydrolyzed by the protein, which has no ATPase activity in the absence of ssDNA or ssRNA. Arg-279 and Trp-597 are needed to couple ATP hydrolysis to mechanical work; a salt bridge between Arg-280 and Glu- 550 closes a clamp around the ssDNA that is not large enough for dsDNA, while Ile-528 wedges between bases of the loading strand.","This protein is a DNA topoisomerase, which means it is involved in controlling the topological changes in DNA during processes such as replication, transcription, and recombination.",No,No,No,No,No,not-Yes,GO:0043138; GO:0033679; GO:0005524; GO:0016887; GO:0003677; GO:0046872; GO:0004844,GO:0003916,GO:0003916,GO:0003916,GO:0003916,GO:0003916,0.3212,0.3212,0.3212,0.3212,0.3212,5,0.3212,0.4814,no
LHR_MYCS2,A0QT91,Reference,Bacteria,1507,"A 3'-5' helicase involved in repair of at least 3 types of DNA cross-links, mitomycin C (MMC), cisplatin, and psoralen-UVA. Translocates 3'-to-5' on single- stranded (ss)DNA, unwinding any encountered duplex nucleic acid. A 3'-ssDNA loading strand of at least 15 nucleotides is required for helicase activity. An RNA:DNA hybrid with a 3'-ssDNA loading strand is an 8-fold better helicase substrate than 3'-tailed double-stranded (ds)DNA; substrates where the helicase loads on a 3'-ssRNA tail (DNA:RNA and RNA:RNA) are not unwound. Only (d)ATP is hydrolyzed by the protein, which has no ATPase activity in the absence of ssDNA or ssRNA. Arg-279 and Trp-597 are needed to couple ATP hydrolysis to mechanical work; a salt bridge between Arg-280 and Glu- 550 closes a clamp around the ssDNA that is not large enough for dsDNA, while Ile-528 wedges between bases of the loading strand.","A 3'-5' helicase involved in repair of at least 3 types of DNA cross-links, mitomycin C (MMC), cisplatin, and psoralen-UVA. Translocates 3'-to-5' on single- stranded (ss)DNA, unwinding any encountered duplex nucleic acid. A 3'-ssDNA loading strand of at least 15 nucleotides is required for helicase activity. An RNA:DNA hybrid with a 3'-ssDNA loading strand is an 8-fold better helicase substrate than 3'-tailed double-stranded (ds)DNA; substrates where the helicase loads on a 3'-ssRNA tail (DNA:RNA and RNA:RNA) are not unwound. Only (d)ATP is hydrolyzed by the protein, which has no ATPase activity in the absence of ssDNA or ssRNA. Arg-279 and Trp-597 are needed to couple ATP hydrolysis to mechanical work; a salt bridge between Arg-280 and Glu- 550 closes a clamp around the ssDNA that is not large enough for dsDNA, while Ile-528 wedges between bases of the loading strand.",,,,,,,GO:0043138; GO:0033679; GO:0005524; GO:0016887; GO:0003677; GO:0046872; GO:0004844,GO:0004003; GO:0005524; GO:0003697,GO:0043140; GO:0005524; GO:0003697,GO:0003678; GO:0005524; GO:0008026,GO:0004386; GO:0003678; GO:0005524,GO:0004386; GO:0003677; GO:0005524,0.7114,0.7149,0.6428,0.6428,0.7105,5,0.6845,0.4814,no
GUAB1_MYCS2,A0QYE8,ESM2Text,Bacteria,478,"Involved in the purine-salvage pathway. Catalyzes the NADPH-dependent conversion of GMP to IMP. Is not essential for viability, but may contribute to the regulation of the purine nucleotide pool by recycling GMP to IMP.",Involved in the purine-salvage pathway. Catalyzes the NADPH-dependent conversion of GMP to IMP.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003920; GO:0003938,GO:0003920,GO:0003920,GO:0003920,GO:0003920,GO:0003920,0.7795,0.7795,0.7795,0.7795,0.7795,5,0.7795,0.166,no
GUAB1_MYCS2,A0QYE8,Prot2Text,Bacteria,478,"Involved in the purine-salvage pathway. Catalyzes the NADPH-dependent conversion of GMP to IMP. Is not essential for viability, but may contribute to the regulation of the purine nucleotide pool by recycling GMP to IMP.",Involved in the purine-salvage pathway. Catalyzes the NADPH-dependent conversion of GMP to IMP.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003920; GO:0003938,GO:0003920,GO:0003920,GO:0003920,GO:0003920,GO:0003920,0.7795,0.7795,0.7795,0.7795,0.7795,5,0.7795,0.166,no
GUAB1_MYCS2,A0QYE8,ProtT3,Bacteria,478,"Involved in the purine-salvage pathway. Catalyzes the NADPH-dependent conversion of GMP to IMP. Is not essential for viability, but may contribute to the regulation of the purine nucleotide pool by recycling GMP to IMP.","Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family",No,No,No,No,No,not-Yes,GO:0003920; GO:0003938,GO:0003938,GO:0003938,GO:0003938,GO:0003938,GO:0003938,0.7795,0.7795,0.7795,0.7795,0.7795,5,0.7795,0.166,no
GUAB1_MYCS2,A0QYE8,ProtTale,Bacteria,478,"Involved in the purine-salvage pathway. Catalyzes the NADPH-dependent conversion of GMP to IMP. Is not essential for viability, but may contribute to the regulation of the purine nucleotide pool by recycling GMP to IMP.","Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.",No,No,No,No,No,not-Yes,GO:0003920; GO:0003938,GO:0003938,GO:0003938,GO:0003938,GO:0003938,GO:0003938,0.7795,0.7795,0.7795,0.7795,0.7795,5,0.7795,0.166,no
GUAB1_MYCS2,A0QYE8,Protein2Text,Bacteria,478,"Involved in the purine-salvage pathway. Catalyzes the NADPH-dependent conversion of GMP to IMP. Is not essential for viability, but may contribute to the regulation of the purine nucleotide pool by recycling GMP to IMP.","This protein is involved in the molecular function of catalyzing the transfer of a methyl group to a substrate, specifically the conversion of 2,5-diamino-6-(ribosylamino)-4(3H)-pyrimidinone 5'-phosphate to 5- methylaminomethyl-2-oxo-4(3H)-pyrimidinone 5'-phosphate.",No,No,No,No,No,not-Yes,GO:0003920; GO:0003938,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.2353,0.2353,0.2353,0.2353,0.2353,5,0.2353,0.166,no
GUAB1_MYCS2,A0QYE8,Reference,Bacteria,478,"Involved in the purine-salvage pathway. Catalyzes the NADPH-dependent conversion of GMP to IMP. Is not essential for viability, but may contribute to the regulation of the purine nucleotide pool by recycling GMP to IMP.","Involved in the purine-salvage pathway. Catalyzes the NADPH-dependent conversion of GMP to IMP. Is not essential for viability, but may contribute to the regulation of the purine nucleotide pool by recycling GMP to IMP.",,,,,,,GO:0003920; GO:0003938,GO:0003920; GO:0050661,GO:0003920; GO:0050661,GO:0003920,GO:0003920,GO:0003920,0.6023,0.6023,0.7795,0.7795,0.7795,5,0.7086,0.166,no
MIRO1_RAT,A1L1L6,ESM2Text,Eukaryota,631,"Atypical mitochondrial nucleoside-triphosphatase (NTPase) involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution. Promotes mitochondrial fission during high calcium conditions. Can hydrolyze GTP, ATP and UTP.",Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0016887; GO:0005509; GO:0019003; GO:0005525; GO:0003924; GO:0042802; GO:0000287; GO:0043021; GO:0039552; GO:0061630; GO:0004842,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924,GO:0003924,GO:0003924,0.5246,0.5246,0.2902,0.2902,0.2902,5,0.384,0.587,yes
MIRO1_RAT,A1L1L6,Prot2Text,Eukaryota,631,"Atypical mitochondrial nucleoside-triphosphatase (NTPase) involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution. Promotes mitochondrial fission during high calcium conditions. Can hydrolyze GTP, ATP and UTP.",Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0016887; GO:0005509; GO:0019003; GO:0005525; GO:0003924; GO:0042802; GO:0000287; GO:0043021; GO:0039552; GO:0061630; GO:0004842,GO:0003924,GO:0003924,GO:0003924,GO:0003924; GO:0005525,GO:0003924,0.2902,0.2902,0.2902,0.5246,0.2902,5,0.3371,0.587,yes
MIRO1_RAT,A1L1L6,ProtT3,Eukaryota,631,"Atypical mitochondrial nucleoside-triphosphatase (NTPase) involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution. Promotes mitochondrial fission during high calcium conditions. Can hydrolyze GTP, ATP and UTP.",Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution (By similarity). Mitochondrion outer membrane; Single-pass type IV membrane protein. Belongs to the mitochondrial Rho GTPase family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0016887; GO:0005509; GO:0019003; GO:0005525; GO:0003924; GO:0042802; GO:0000287; GO:0043021; GO:0039552; GO:0061630; GO:0004842,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924,0.5246,0.5246,0.5246,0.5246,0.2902,5,0.4777,0.587,yes
MIRO1_RAT,A1L1L6,ProtTale,Eukaryota,631,"Atypical mitochondrial nucleoside-triphosphatase (NTPase) involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution. Promotes mitochondrial fission during high calcium conditions. Can hydrolyze GTP, ATP and UTP.",Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0016887; GO:0005509; GO:0019003; GO:0005525; GO:0003924; GO:0042802; GO:0000287; GO:0043021; GO:0039552; GO:0061630; GO:0004842,GO:0003924,GO:0003924,GO:0003924; GO:0005525,GO:0003924,GO:0003924; GO:0005525,0.2902,0.2902,0.5246,0.2902,0.5246,5,0.384,0.587,yes
MIRO1_RAT,A1L1L6,Protein2Text,Eukaryota,631,"Atypical mitochondrial nucleoside-triphosphatase (NTPase) involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution. Promotes mitochondrial fission during high calcium conditions. Can hydrolyze GTP, ATP and UTP.","The molecular function of this protein is not specified in the provided information. However, based on its name, it is likely involved in transporting molecules across membranes. Specifically, it is a GTPase involved in regulating vesicle trafficking and transport. It may play a role in mediating the fusion of vesicles with their target membranes, allowing for the transport of molecules between different cellular compartments.",Maybe,Maybe,Vague,Vague,Maybe,not-Yes,GO:0016887; GO:0005509; GO:0019003; GO:0005525; GO:0003924; GO:0042802; GO:0000287; GO:0043021; GO:0039552; GO:0061630; GO:0004842,GO:0003924,GO:0003924,GO:0003924,GO:0003924,GO:0003924,0.2902,0.2902,0.2902,0.2902,0.2902,5,0.2902,0.587,yes
MIRO1_RAT,A1L1L6,Reference,Eukaryota,631,"Atypical mitochondrial nucleoside-triphosphatase (NTPase) involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution. Promotes mitochondrial fission during high calcium conditions. Can hydrolyze GTP, ATP and UTP.","Atypical mitochondrial nucleoside-triphosphatase (NTPase) involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution. Promotes mitochondrial fission during high calcium conditions. Can hydrolyze GTP, ATP and UTP.",,,,,,,GO:0016887; GO:0005509; GO:0019003; GO:0005525; GO:0003924; GO:0042802; GO:0000287; GO:0043021; GO:0039552; GO:0061630; GO:0004842,GO:0017111; GO:0005525; GO:0005524,GO:0017111; GO:0003924; GO:0016887,GO:0017111; GO:0003924; GO:0016887,GO:0016462; GO:0005525; GO:0005524,GO:0017111; GO:0005525; GO:0005524,0.5325,0.4161,0.4161,0.5134,0.5325,5,0.4821,0.587,yes
PTPM1_DANRE,A1L293,ESM2Text,Eukaryota,183,"Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). PGP is an essential intermediate in the biosynthetic pathway of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. Has also been shown to display phosphatase activity toward phosphoprotein substrates, specifically mediates dephosphorylation of mitochondrial proteins, thereby playing an essential role in ATP production. Has probably a preference for proteins phosphorylated on Ser and/or Thr residues compared to proteins phosphorylated on Tyr residues. Probably involved in regulation of insulin secretion in pancreatic beta cells. Is a regulator of succinate deshydrogenase (SDH) phosphorylation status involved in the control of glucose homeostasis. Prevents intrinsic apoptosis, by regulating mitochondrial membrane integrity.","Possesses phosphatase activity toward p-nitrophenyl phosphate (pNPP) and a low activity toward the synthetic phospholipid phosphatidylinositol 4,5-bisphosphate (PIP2). In vitro, dephosphorylates phosphatidylinositol 3-phosphate, but does not possess detectable phosphatase activity toward phosphatidylinositol 3,5-bisphosphate, phosphatidylinositol 4-phosphate, or phosphatidylinositol 5-phosphate.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008962; GO:0004439; GO:0004722,GO:0004437; GO:0016791,GO:0016791,GO:0016791; GO:0004438,GO:0016791,GO:0016791,0.7638,0.7638,0.7279,0.7638,0.7638,5,0.7566,0.4635,no
PTPM1_DANRE,A1L293,Prot2Text,Eukaryota,183,"Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). PGP is an essential intermediate in the biosynthetic pathway of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. Has also been shown to display phosphatase activity toward phosphoprotein substrates, specifically mediates dephosphorylation of mitochondrial proteins, thereby playing an essential role in ATP production. Has probably a preference for proteins phosphorylated on Ser and/or Thr residues compared to proteins phosphorylated on Tyr residues. Probably involved in regulation of insulin secretion in pancreatic beta cells. Is a regulator of succinate deshydrogenase (SDH) phosphorylation status involved in the control of glucose homeostasis. Prevents intrinsic apoptosis, by regulating mitochondrial membrane integrity.","Dual specificity phosphatase able to dephosphorylate phosphotyrosine, phosphoserine and phosphothreonine residues within the same substrate, with a preference for phosphotyrosine as a substrate. Has a specificity for the phosphotyrosine-containing peptide bond.",No,Maybe,No,No,No,not-Yes,GO:0008962; GO:0004439; GO:0004722,GO:0004725,GO:0004725; GO:0004722,GO:0004725,GO:0004725; GO:0008138,GO:0008138,0.6679,0.7724,0.6679,0.6963,0.6679,5,0.6945,0.4635,no
PTPM1_DANRE,A1L293,ProtT3,Eukaryota,183,"Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). PGP is an essential intermediate in the biosynthetic pathway of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. Has also been shown to display phosphatase activity toward phosphoprotein substrates, specifically mediates dephosphorylation of mitochondrial proteins, thereby playing an essential role in ATP production. Has probably a preference for proteins phosphorylated on Ser and/or Thr residues compared to proteins phosphorylated on Tyr residues. Probably involved in regulation of insulin secretion in pancreatic beta cells. Is a regulator of succinate deshydrogenase (SDH) phosphorylation status involved in the control of glucose homeostasis. Prevents intrinsic apoptosis, by regulating mitochondrial membrane integrity.",Lipid phosphatase that dephosphorylates phosphatidic acid (PA) to diacylglycerol (DAG) and plays a key role in the mitochondrial lipid metabolism,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008962; GO:0004439; GO:0004722,GO:0008970,GO:0016791,GO:0016791,GO:0004630,GO:0008970,0.2883,0.7638,0.7638,0.3908,0.2883,5,0.499,0.4635,no
PTPM1_DANRE,A1L293,ProtTale,Eukaryota,183,"Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). PGP is an essential intermediate in the biosynthetic pathway of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. Has also been shown to display phosphatase activity toward phosphoprotein substrates, specifically mediates dephosphorylation of mitochondrial proteins, thereby playing an essential role in ATP production. Has probably a preference for proteins phosphorylated on Ser and/or Thr residues compared to proteins phosphorylated on Tyr residues. Probably involved in regulation of insulin secretion in pancreatic beta cells. Is a regulator of succinate deshydrogenase (SDH) phosphorylation status involved in the control of glucose homeostasis. Prevents intrinsic apoptosis, by regulating mitochondrial membrane integrity.",Protein-tyrosine phosphatase that dephosphorylates FYN at 'Tyr-390'. May play a role in the regulation of MAPK1/3 signaling pathway. Dephosphorylates PRKCA at 'Tyr-217' and 'Tyr-221'. Dephosphorylates MAP2K4/MKK4 at 'Tyr-258' and 'Tyr-262'. Dephosphorylates MAP2K7/MKK7 at 'Tyr-258' and 'Tyr-262'. Dephosphorylates MAP3K7,No,Maybe,No,No,No,not-Yes,GO:0008962; GO:0004439; GO:0004722,GO:0004725,GO:0004725,GO:0004725,GO:0004725,GO:0004725,0.6679,0.6679,0.6679,0.6679,0.6679,5,0.6679,0.4635,no
PTPM1_DANRE,A1L293,Protein2Text,Eukaryota,183,"Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). PGP is an essential intermediate in the biosynthetic pathway of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. Has also been shown to display phosphatase activity toward phosphoprotein substrates, specifically mediates dephosphorylation of mitochondrial proteins, thereby playing an essential role in ATP production. Has probably a preference for proteins phosphorylated on Ser and/or Thr residues compared to proteins phosphorylated on Tyr residues. Probably involved in regulation of insulin secretion in pancreatic beta cells. Is a regulator of succinate deshydrogenase (SDH) phosphorylation status involved in the control of glucose homeostasis. Prevents intrinsic apoptosis, by regulating mitochondrial membrane integrity.","The molecular function of this protein is not specified in the provided information. However, based on its name and the fact that it is a phosphatase, it is likely that the protein's molecular function is related to the removal of phosphate groups from other molecules, such as phosphoproteins or phospholipids.",Vague,Maybe,Vague,Maybe,Maybe,not-Yes,GO:0008962; GO:0004439; GO:0004722,GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,0.7638,0.7638,0.7638,0.7638,0.7638,5,0.7638,0.4635,no
PTPM1_DANRE,A1L293,Reference,Eukaryota,183,"Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). PGP is an essential intermediate in the biosynthetic pathway of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. Has also been shown to display phosphatase activity toward phosphoprotein substrates, specifically mediates dephosphorylation of mitochondrial proteins, thereby playing an essential role in ATP production. Has probably a preference for proteins phosphorylated on Ser and/or Thr residues compared to proteins phosphorylated on Tyr residues. Probably involved in regulation of insulin secretion in pancreatic beta cells. Is a regulator of succinate deshydrogenase (SDH) phosphorylation status involved in the control of glucose homeostasis. Prevents intrinsic apoptosis, by regulating mitochondrial membrane integrity.","Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). PGP is an essential intermediate in the biosynthetic pathway of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. Has also been shown to display phosphatase activity toward phosphoprotein substrates, specifically mediates dephosphorylation of mitochondrial proteins, thereby playing an essential role in ATP production. Has probably a preference for proteins phosphorylated on Ser and/or Thr residues compared to proteins phosphorylated on Tyr residues. Probably involved in regulation of insulin secretion in pancreatic beta cells. Is a regulator of succinate deshydrogenase (SDH) phosphorylation status involved in the control of glucose homeostasis. Prevents intrinsic apoptosis, by regulating mitochondrial membrane integrity.",,,,,,,GO:0008962; GO:0004439; GO:0004722,GO:0008962; GO:0004722,GO:0016791; GO:0004722,GO:0004722; GO:0046839,GO:0004722; GO:0016791,GO:0004722; GO:0046839,0.8996,0.8656,0.6105,0.8656,0.6105,5,0.7704,0.4635,no
TFP_LEPSV,A1XLE2,ESM2Text,Eukaryota,337,Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation. Catalyzes thiocyanate and simple nitrile formation from benzylglucosinolate in the presence of myrosinase. Converts also aliphatic glucosinolates to both epithionitriles and simple nitriles.,"Promotes simple nitriles, but not epithionitrile or thiocyanate formation. Converts allylglucosinolate and benzylglucosinolate to their corresponding simple nitriles in the presence of myrosinase.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0030234; GO:0016829; GO:0046872,,,,,,,,,,,0,,0.4386,no
TFP_LEPSV,A1XLE2,Prot2Text,Eukaryota,337,Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation. Catalyzes thiocyanate and simple nitrile formation from benzylglucosinolate in the presence of myrosinase. Converts also aliphatic glucosinolates to both epithionitriles and simple nitriles.,"Promotes simple nitriles, but not epithionitrile or thiocyanate formation. Converts allylglucosinolate and benzylglucosinolate to their corresponding simple nitriles in the presence of myrosinase.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0030234; GO:0016829; GO:0046872,,,,,,,,,,,0,,0.4386,no
TFP_LEPSV,A1XLE2,ProtT3,Eukaryota,337,Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation. Catalyzes thiocyanate and simple nitrile formation from benzylglucosinolate in the presence of myrosinase. Converts also aliphatic glucosinolates to both epithionitriles and simple nitriles.,Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N- acetylglucosamine-6-phosphate (GlcNAc-6-P) and acetate. Cytoplasm. Belongs to the NanE family,No,No,No,No,No,not-Yes,GO:0030234; GO:0016829; GO:0046872,GO:0016853,GO:0008761,GO:0008761,GO:0016857,GO:0016854,0.4001,0.2393,0.2393,0.2749,0.3254,5,0.2958,0.4386,no
TFP_LEPSV,A1XLE2,ProtTale,Eukaryota,337,Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation. Catalyzes thiocyanate and simple nitrile formation from benzylglucosinolate in the presence of myrosinase. Converts also aliphatic glucosinolates to both epithionitriles and simple nitriles.,May play a role in the regulation of the Wnt signaling pathway by modulating beta-catenin (CTNNB1) stability.,No,No,No,No,No,not-Yes,GO:0030234; GO:0016829; GO:0046872,,,,,,,,,,,0,,0.4386,no
TFP_LEPSV,A1XLE2,Protein2Text,Eukaryota,337,Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation. Catalyzes thiocyanate and simple nitrile formation from benzylglucosinolate in the presence of myrosinase. Converts also aliphatic glucosinolates to both epithionitriles and simple nitriles.,"The molecular function of this protein is not explicitly stated in the provided text. However, based on its classification as a protein, it is likely that it performs a catalytic or binding function. If you have any further information or context about this protein, I may be able to provide a more specific answer.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0030234; GO:0016829; GO:0046872,,,,,,,,,,,0,,0.4386,no
TFP_LEPSV,A1XLE2,Reference,Eukaryota,337,Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation. Catalyzes thiocyanate and simple nitrile formation from benzylglucosinolate in the presence of myrosinase. Converts also aliphatic glucosinolates to both epithionitriles and simple nitriles.,Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation. Catalyzes thiocyanate and simple nitrile formation from benzylglucosinolate in the presence of myrosinase. Converts also aliphatic glucosinolates to both epithionitriles and simple nitriles.,,,,,,,GO:0030234; GO:0016829; GO:0046872,,,,,,,,,,,0,,0.4386,no
TGFR1_DROME,A1Z7L8,ESM2Text,Eukaryota,622,"Type I transmembrane receptor serine/threonine kinase involved in the activin-like TGF-beta signaling pathway. Forms a receptor complex with a type II transmembrane receptor serine/threonine kinase, and upon activation by an activin/TGF-beta- like ligand phosphorylates downstream receptor-regulated SMAD (R-SMAD) transcription factors, inducing their nuclear localization resulting in regulation of activin/TGF-beta-responsive genes. When part of a heteromeric complex with the type I receptor put/punt can be activated by the activin/TGF-beta-like ligands Actbeta/activin, daw/dawdle and possibly myo/myoglianin; ligand specificity is probably isoform- dependent. Upon activation phosphorylates the R-SMAD Smox/SMAD2 to activate the canonical TGF-beta pathway. Can also phosphorylate Mad, the R-SMAD of the dpp BMP-like signaling pathway, in response to daw signaling but to a lesser extent. Phosphorylation of Mad is competitively regulated by Smox/SMAD2. Positive regulator of cell proliferation, probably through activation of the SMAD2-dependent activin signaling pathway. Required for normal proliferation of medulla neuroblasts and laminar precursor cells in the optic lobe. Involved in regulation of the ecdysteroid hormone receptor EcR in neuronal cells throughout the central nervous system. Involved in axonal and dendritic pruning and neural remodeling of mushroom body gamma neurons during metamorphosis through regulation of EcR. Involved in differentiation of dorsal cluster and ellipsoid body adult-specific neurons prior to metamorphosis. Required in motoneurons for axon guidance or outgrowth of ISNb and SNa axons. Involved in regulation of wing growth. Signaling by daw or myo is involved in lifespan determination through regulation of proteasome- mediated degradation of misfolded or damaged proteins.","Transmembrane serine/threonine kinase forming with bacitracin receptor and phosphorylating chrysobacterium, the major component of the extracellular matrix.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0048185; GO:0017002; GO:0016361; GO:0005524; GO:0046872,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.3911,0.3911,0.3911,0.3911,0.3911,5,0.3911,0.5817,yes
TGFR1_DROME,A1Z7L8,Prot2Text,Eukaryota,622,"Type I transmembrane receptor serine/threonine kinase involved in the activin-like TGF-beta signaling pathway. Forms a receptor complex with a type II transmembrane receptor serine/threonine kinase, and upon activation by an activin/TGF-beta- like ligand phosphorylates downstream receptor-regulated SMAD (R-SMAD) transcription factors, inducing their nuclear localization resulting in regulation of activin/TGF-beta-responsive genes. When part of a heteromeric complex with the type I receptor put/punt can be activated by the activin/TGF-beta-like ligands Actbeta/activin, daw/dawdle and possibly myo/myoglianin; ligand specificity is probably isoform- dependent. Upon activation phosphorylates the R-SMAD Smox/SMAD2 to activate the canonical TGF-beta pathway. Can also phosphorylate Mad, the R-SMAD of the dpp BMP-like signaling pathway, in response to daw signaling but to a lesser extent. Phosphorylation of Mad is competitively regulated by Smox/SMAD2. Positive regulator of cell proliferation, probably through activation of the SMAD2-dependent activin signaling pathway. Required for normal proliferation of medulla neuroblasts and laminar precursor cells in the optic lobe. Involved in regulation of the ecdysteroid hormone receptor EcR in neuronal cells throughout the central nervous system. Involved in axonal and dendritic pruning and neural remodeling of mushroom body gamma neurons during metamorphosis through regulation of EcR. Involved in differentiation of dorsal cluster and ellipsoid body adult-specific neurons prior to metamorphosis. Required in motoneurons for axon guidance or outgrowth of ISNb and SNa axons. Involved in regulation of wing growth. Signaling by daw or myo is involved in lifespan determination through regulation of proteasome- mediated degradation of misfolded or damaged proteins.","On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP7/OP-1, GDF5, GDF6 and GDF8. Positively regulates chondrocyte differentiation through GDF5 interaction.",Maybe,Yes,Yes,Yes,Yes,Yes,GO:0048185; GO:0017002; GO:0016361; GO:0005524; GO:0046872,GO:0004675,GO:0004674,GO:0004675,GO:0004675; GO:0004674,GO:0004675,0.4869,0.3911,0.4869,0.5283,0.4869,5,0.476,0.5817,yes
TGFR1_DROME,A1Z7L8,ProtT3,Eukaryota,622,"Type I transmembrane receptor serine/threonine kinase involved in the activin-like TGF-beta signaling pathway. Forms a receptor complex with a type II transmembrane receptor serine/threonine kinase, and upon activation by an activin/TGF-beta- like ligand phosphorylates downstream receptor-regulated SMAD (R-SMAD) transcription factors, inducing their nuclear localization resulting in regulation of activin/TGF-beta-responsive genes. When part of a heteromeric complex with the type I receptor put/punt can be activated by the activin/TGF-beta-like ligands Actbeta/activin, daw/dawdle and possibly myo/myoglianin; ligand specificity is probably isoform- dependent. Upon activation phosphorylates the R-SMAD Smox/SMAD2 to activate the canonical TGF-beta pathway. Can also phosphorylate Mad, the R-SMAD of the dpp BMP-like signaling pathway, in response to daw signaling but to a lesser extent. Phosphorylation of Mad is competitively regulated by Smox/SMAD2. Positive regulator of cell proliferation, probably through activation of the SMAD2-dependent activin signaling pathway. Required for normal proliferation of medulla neuroblasts and laminar precursor cells in the optic lobe. Involved in regulation of the ecdysteroid hormone receptor EcR in neuronal cells throughout the central nervous system. Involved in axonal and dendritic pruning and neural remodeling of mushroom body gamma neurons during metamorphosis through regulation of EcR. Involved in differentiation of dorsal cluster and ellipsoid body adult-specific neurons prior to metamorphosis. Required in motoneurons for axon guidance or outgrowth of ISNb and SNa axons. Involved in regulation of wing growth. Signaling by daw or myo is involved in lifespan determination through regulation of proteasome- mediated degradation of misfolded or damaged proteins.","On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcription factors. Membrane; Single-pass type I membrane protein. Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily",Maybe,Yes,Yes,Yes,Yes,Yes,GO:0048185; GO:0017002; GO:0016361; GO:0005524; GO:0046872,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,0.6512,0.6512,0.6512,0.6512,0.3911,5,0.5992,0.5817,yes
TGFR1_DROME,A1Z7L8,ProtTale,Eukaryota,622,"Type I transmembrane receptor serine/threonine kinase involved in the activin-like TGF-beta signaling pathway. Forms a receptor complex with a type II transmembrane receptor serine/threonine kinase, and upon activation by an activin/TGF-beta- like ligand phosphorylates downstream receptor-regulated SMAD (R-SMAD) transcription factors, inducing their nuclear localization resulting in regulation of activin/TGF-beta-responsive genes. When part of a heteromeric complex with the type I receptor put/punt can be activated by the activin/TGF-beta-like ligands Actbeta/activin, daw/dawdle and possibly myo/myoglianin; ligand specificity is probably isoform- dependent. Upon activation phosphorylates the R-SMAD Smox/SMAD2 to activate the canonical TGF-beta pathway. Can also phosphorylate Mad, the R-SMAD of the dpp BMP-like signaling pathway, in response to daw signaling but to a lesser extent. Phosphorylation of Mad is competitively regulated by Smox/SMAD2. Positive regulator of cell proliferation, probably through activation of the SMAD2-dependent activin signaling pathway. Required for normal proliferation of medulla neuroblasts and laminar precursor cells in the optic lobe. Involved in regulation of the ecdysteroid hormone receptor EcR in neuronal cells throughout the central nervous system. Involved in axonal and dendritic pruning and neural remodeling of mushroom body gamma neurons during metamorphosis through regulation of EcR. Involved in differentiation of dorsal cluster and ellipsoid body adult-specific neurons prior to metamorphosis. Required in motoneurons for axon guidance or outgrowth of ISNb and SNa axons. Involved in regulation of wing growth. Signaling by daw or myo is involved in lifespan determination through regulation of proteasome- mediated degradation of misfolded or damaged proteins.",Probable receptor for the TGF-beta family member daf-7.,Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0048185; GO:0017002; GO:0016361; GO:0005524; GO:0046872,,GO:0004675,GO:0005024,,,,0.4869,0.4491,,,2,0.468,0.5817,yes
TGFR1_DROME,A1Z7L8,Protein2Text,Eukaryota,622,"Type I transmembrane receptor serine/threonine kinase involved in the activin-like TGF-beta signaling pathway. Forms a receptor complex with a type II transmembrane receptor serine/threonine kinase, and upon activation by an activin/TGF-beta- like ligand phosphorylates downstream receptor-regulated SMAD (R-SMAD) transcription factors, inducing their nuclear localization resulting in regulation of activin/TGF-beta-responsive genes. When part of a heteromeric complex with the type I receptor put/punt can be activated by the activin/TGF-beta-like ligands Actbeta/activin, daw/dawdle and possibly myo/myoglianin; ligand specificity is probably isoform- dependent. Upon activation phosphorylates the R-SMAD Smox/SMAD2 to activate the canonical TGF-beta pathway. Can also phosphorylate Mad, the R-SMAD of the dpp BMP-like signaling pathway, in response to daw signaling but to a lesser extent. Phosphorylation of Mad is competitively regulated by Smox/SMAD2. Positive regulator of cell proliferation, probably through activation of the SMAD2-dependent activin signaling pathway. Required for normal proliferation of medulla neuroblasts and laminar precursor cells in the optic lobe. Involved in regulation of the ecdysteroid hormone receptor EcR in neuronal cells throughout the central nervous system. Involved in axonal and dendritic pruning and neural remodeling of mushroom body gamma neurons during metamorphosis through regulation of EcR. Involved in differentiation of dorsal cluster and ellipsoid body adult-specific neurons prior to metamorphosis. Required in motoneurons for axon guidance or outgrowth of ISNb and SNa axons. Involved in regulation of wing growth. Signaling by daw or myo is involved in lifespan determination through regulation of proteasome- mediated degradation of misfolded or damaged proteins.",The molecular function of this protein is receptor activity.,Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0048185; GO:0017002; GO:0016361; GO:0005524; GO:0046872,,GO:0004872,,GO:0004872,GO:0004872,,0.2532,,0.2532,0.2532,3,0.2532,0.5817,yes
TGFR1_DROME,A1Z7L8,Reference,Eukaryota,622,"Type I transmembrane receptor serine/threonine kinase involved in the activin-like TGF-beta signaling pathway. Forms a receptor complex with a type II transmembrane receptor serine/threonine kinase, and upon activation by an activin/TGF-beta- like ligand phosphorylates downstream receptor-regulated SMAD (R-SMAD) transcription factors, inducing their nuclear localization resulting in regulation of activin/TGF-beta-responsive genes. When part of a heteromeric complex with the type I receptor put/punt can be activated by the activin/TGF-beta-like ligands Actbeta/activin, daw/dawdle and possibly myo/myoglianin; ligand specificity is probably isoform- dependent. Upon activation phosphorylates the R-SMAD Smox/SMAD2 to activate the canonical TGF-beta pathway. Can also phosphorylate Mad, the R-SMAD of the dpp BMP-like signaling pathway, in response to daw signaling but to a lesser extent. Phosphorylation of Mad is competitively regulated by Smox/SMAD2. Positive regulator of cell proliferation, probably through activation of the SMAD2-dependent activin signaling pathway. Required for normal proliferation of medulla neuroblasts and laminar precursor cells in the optic lobe. Involved in regulation of the ecdysteroid hormone receptor EcR in neuronal cells throughout the central nervous system. Involved in axonal and dendritic pruning and neural remodeling of mushroom body gamma neurons during metamorphosis through regulation of EcR. Involved in differentiation of dorsal cluster and ellipsoid body adult-specific neurons prior to metamorphosis. Required in motoneurons for axon guidance or outgrowth of ISNb and SNa axons. Involved in regulation of wing growth. Signaling by daw or myo is involved in lifespan determination through regulation of proteasome- mediated degradation of misfolded or damaged proteins.","Type I transmembrane receptor serine/threonine kinase involved in the activin-like TGF-beta signaling pathway. Forms a receptor complex with a type II transmembrane receptor serine/threonine kinase, and upon activation by an activin/TGF-beta- like ligand phosphorylates downstream receptor-regulated SMAD (R-SMAD) transcription factors, inducing their nuclear localization resulting in regulation of activin/TGF-beta-responsive genes. When part of a heteromeric complex with the type I receptor put/punt can be activated by the activin/TGF-beta-like ligands Actbeta/activin, daw/dawdle and possibly myo/myoglianin; ligand specificity is probably isoform- dependent. Upon activation phosphorylates the R-SMAD Smox/SMAD2 to activate the canonical TGF-beta pathway. Can also phosphorylate Mad, the R-SMAD of the dpp BMP-like signaling pathway, in response to daw signaling but to a lesser extent. Phosphorylation of Mad is competitively regulated by Smox/SMAD2. Positive regulator of cell proliferation, probably through activation of the SMAD2-dependent activin signaling pathway. Required for normal proliferation of medulla neuroblasts and laminar precursor cells in the optic lobe. Involved in regulation of the ecdysteroid hormone receptor EcR in neuronal cells throughout the central nervous system. Involved in axonal and dendritic pruning and neural remodeling of mushroom body gamma neurons during metamorphosis through regulation of EcR. Involved in differentiation of dorsal cluster and ellipsoid body adult-specific neurons prior to metamorphosis. Required in motoneurons for axon guidance or outgrowth of ISNb and SNa axons. Involved in regulation of wing growth. Signaling by daw or myo is involved in lifespan determination through regulation of proteasome- mediated degradation of misfolded or damaged proteins.",,,,,,,GO:0048185; GO:0017002; GO:0016361; GO:0005524; GO:0046872,GO:0004675; GO:0005524,GO:0004674; GO:0005524; GO:0046332,GO:0004674; GO:0005524,GO:0004674; GO:0004675; GO:0005524,GO:0004674; GO:0004675; GO:0005524,0.7426,0.6467,0.6512,0.7388,0.7388,5,0.7036,0.5817,yes
DCR2_DROME,A1ZAW0,ESM2Text,Eukaryota,1722,"Double-stranded RNA (dsRNA) endoribonuclease which cleaves endogenous (endo), exogenous (exo), and viral dsRNAs to produce short interfering RNAs (siRNAs). The generated siRNAs then mediate gene silencing, also called RNA interference (RNAi), by controlling the elimination of endogenous transcripts from mobile and repetitive DNA elements of the genome as well as exogenous RNA of viral origin. Also acts in an RNAi-independent manner to activate translation through cytoplasmic polyadenylation. As well as its role in dsRNA processing, essential in several steps of the siRNA biogenesis pathway, including siRNA loading into the Argonaute 2 (AGO2)-containing RNA-induced silencing complex (siRISC), length-dependent dicing and guide strand selection for target silencing by the siRISC. Cleaves dsRNAs into siRNAs that are predominantly around twenty-one nucleotides in length. Displays a preference for binding and processing blunt termini (BLT), likely non- self dsRNAs, over dsRNAs with 2 nucleotides 3' overhanging (3'ovr) termini, which are typically the structure of endogenous dsRNAs. According to many reports, the cleavage reaction mode of the enzyme changes according to the termini of the dsRNA substrate. BLT dsRNAs undergo an ATP-dependent processive reaction whereby multiple siRNAs of heterogeneous sizes are produced before the enzyme dissociates. In contrast, dsRNAs with 3'ovr termini, which are typically the structure of endogenous dsRNAs, undergo ATP-independent, distributive cleavage whereby the enzyme dissociates after each cleavage to produce siRNAs of around 22 nucleotides. However, according to another report, the mode of cleavage reaction is not affected by the terminal structures of the dsRNAs substrates. This report suggests that the enzyme is able to initiate processive cleavage of both BLT and 3'ovr dsRNA substrates, and only rarely initiates distributive cleavage. During dsRNA processing and AGO2-loading, requires association with dsRNA-binding accessory proteins loqs isoform PD (loqs-PD) and r2d2. Functions with r2d2 to form the siRNA-mediated RISC loading complex (siRLC) which is responsible for Ago2-loading of endo- and exo-siRNAs. Interaction with loqs-PD increases initial binding to dsRNA substrates and promotes processing of a subset of endo- and exo-dsRNAs. In the absence of r2d2, may also form an alternative siRLC with loqs-PD to load siRNAs into the siRISC. Function with loqs-PD allows the dicer enzyme to cleave endogenous dsRNA templates independently of their termini, and is required for ATP-dependent processing of a subset of siRNAs but is not required for antiviral RNAi. This suggests that the enzyme's intrinsic termini preferences function in viral defense, while function with loqs-PD allows processing of endogenous dsRNAs with diverse termini. However, according to another report the mode of cleavage reaction is not affected by the presence or absence of loqs-PD. Loaded siRNAs serve as a guide to direct the siRISC to complementary RNAs to degrade them or prevent their translation. The siRLC plays an important role in the ATP-dependent asymmetry sensing of the duplex, and is therefore also responsible for the selection of the strand that ultimately acts as the guide siRNA for the siRISC. Thermodynamically asymmetric siRNAs are preoriented in the siRLC by either the dsRNA-binding r2d2 protein, or the loqs-PD protein in the alternative siRLC, which preferentially bind to the most thermodynamically stable strand prior to loading onto AGO2. Both r2d2 and Dcr- 2 also initiate unwinding of the siRNA duplex, at which point the heterodimer is exchanged by AGO2. The strand that was bound by r2d2 is discarded while the one that was bound by Dcr-2 is loaded onto Ago2 and serves as guide to direct the siRISC to complementary RNAs to degrade them or prevent their translation. Independently of its role in RNAi, acts with the cytoplasmic poly(A) polymerase wisp to promote cytoplasmic polyadenylation and translational activation of certain messenger RNAs including r2d2 and toll (Tl) transcripts. Consequently it is involved in the post- transcriptional regulation of the Toll immune signaling pathway and promoting resistance to fungal and viral infections. As an RNA-binding protein, likely functions in cytoplasmic polyadenylation by recruiting the poly(A) RNA polymerase wisp to target mRNAs.","Ribonuclease (RNase) III involved in RNA-mediated post-transcriptional gene silencing (PTGS). Functions in the microRNAs (miRNAs) biogenesis pathway by cleaving primary miRNAs into mature miRNAs. This pathway, which requires Rlp-7 and Rlp-32, amplifies the amplification of the intra-genomic signals generated by the miRNAs. Acts as a transcription termination factor (TIF) for primary miRNAs by promoting the hydrolysis of the 5'-terminal RRP8-RRP9 intermediate, leading to the production of mature miRNAs. Can process the 5.8S rRNA precursor, but not the 5.8S rRNA precursor, generating 5.8S rRNA, the precursor for the mature miRNAs.",Maybe,Maybe,Yes,Yes,Maybe,not-Yes,GO:0005524; GO:0016887; GO:0008186; GO:0004530; GO:0004386; GO:0003730; GO:0004525; GO:0003723; GO:0035197,GO:0004525,GO:0004525,GO:0004525,GO:0004525,GO:0004525,0.3206,0.3206,0.3206,0.3206,0.3206,5,0.3206,0.6256,yes
DCR2_DROME,A1ZAW0,Prot2Text,Eukaryota,1722,"Double-stranded RNA (dsRNA) endoribonuclease which cleaves endogenous (endo), exogenous (exo), and viral dsRNAs to produce short interfering RNAs (siRNAs). The generated siRNAs then mediate gene silencing, also called RNA interference (RNAi), by controlling the elimination of endogenous transcripts from mobile and repetitive DNA elements of the genome as well as exogenous RNA of viral origin. Also acts in an RNAi-independent manner to activate translation through cytoplasmic polyadenylation. As well as its role in dsRNA processing, essential in several steps of the siRNA biogenesis pathway, including siRNA loading into the Argonaute 2 (AGO2)-containing RNA-induced silencing complex (siRISC), length-dependent dicing and guide strand selection for target silencing by the siRISC. Cleaves dsRNAs into siRNAs that are predominantly around twenty-one nucleotides in length. Displays a preference for binding and processing blunt termini (BLT), likely non- self dsRNAs, over dsRNAs with 2 nucleotides 3' overhanging (3'ovr) termini, which are typically the structure of endogenous dsRNAs. According to many reports, the cleavage reaction mode of the enzyme changes according to the termini of the dsRNA substrate. BLT dsRNAs undergo an ATP-dependent processive reaction whereby multiple siRNAs of heterogeneous sizes are produced before the enzyme dissociates. In contrast, dsRNAs with 3'ovr termini, which are typically the structure of endogenous dsRNAs, undergo ATP-independent, distributive cleavage whereby the enzyme dissociates after each cleavage to produce siRNAs of around 22 nucleotides. However, according to another report, the mode of cleavage reaction is not affected by the terminal structures of the dsRNAs substrates. This report suggests that the enzyme is able to initiate processive cleavage of both BLT and 3'ovr dsRNA substrates, and only rarely initiates distributive cleavage. During dsRNA processing and AGO2-loading, requires association with dsRNA-binding accessory proteins loqs isoform PD (loqs-PD) and r2d2. Functions with r2d2 to form the siRNA-mediated RISC loading complex (siRLC) which is responsible for Ago2-loading of endo- and exo-siRNAs. Interaction with loqs-PD increases initial binding to dsRNA substrates and promotes processing of a subset of endo- and exo-dsRNAs. In the absence of r2d2, may also form an alternative siRLC with loqs-PD to load siRNAs into the siRISC. Function with loqs-PD allows the dicer enzyme to cleave endogenous dsRNA templates independently of their termini, and is required for ATP-dependent processing of a subset of siRNAs but is not required for antiviral RNAi. This suggests that the enzyme's intrinsic termini preferences function in viral defense, while function with loqs-PD allows processing of endogenous dsRNAs with diverse termini. However, according to another report the mode of cleavage reaction is not affected by the presence or absence of loqs-PD. Loaded siRNAs serve as a guide to direct the siRISC to complementary RNAs to degrade them or prevent their translation. The siRLC plays an important role in the ATP-dependent asymmetry sensing of the duplex, and is therefore also responsible for the selection of the strand that ultimately acts as the guide siRNA for the siRISC. Thermodynamically asymmetric siRNAs are preoriented in the siRLC by either the dsRNA-binding r2d2 protein, or the loqs-PD protein in the alternative siRLC, which preferentially bind to the most thermodynamically stable strand prior to loading onto AGO2. Both r2d2 and Dcr- 2 also initiate unwinding of the siRNA duplex, at which point the heterodimer is exchanged by AGO2. The strand that was bound by r2d2 is discarded while the one that was bound by Dcr-2 is loaded onto Ago2 and serves as guide to direct the siRISC to complementary RNAs to degrade them or prevent their translation. Independently of its role in RNAi, acts with the cytoplasmic poly(A) polymerase wisp to promote cytoplasmic polyadenylation and translational activation of certain messenger RNAs including r2d2 and toll (Tl) transcripts. Consequently it is involved in the post- transcriptional regulation of the Toll immune signaling pathway and promoting resistance to fungal and viral infections. As an RNA-binding protein, likely functions in cytoplasmic polyadenylation by recruiting the poly(A) RNA polymerase wisp to target mRNAs.","Dicer-like endonuclease involved in cleaving double-stranded RNA in the RNA interference (RNAi) pathway. Produces 21 to 25 bp dsRNAs (siRNAs) which target the selective destruction of homologous RNAs leading to sequence-specific suppression of gene expression, called post-transcriptional gene silencing (PTGS). Part of a broad host defense response against viral infection and transposons. Controls the expression of the non-LTR retrotransposon Tad in the African strain, Adiomopoume.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0008186; GO:0004530; GO:0004386; GO:0003730; GO:0004525; GO:0003723; GO:0035197,GO:0004525,GO:0004525,GO:0004525,GO:0004525,GO:0004525,0.3206,0.3206,0.3206,0.3206,0.3206,5,0.3206,0.6256,yes
DCR2_DROME,A1ZAW0,ProtT3,Eukaryota,1722,"Double-stranded RNA (dsRNA) endoribonuclease which cleaves endogenous (endo), exogenous (exo), and viral dsRNAs to produce short interfering RNAs (siRNAs). The generated siRNAs then mediate gene silencing, also called RNA interference (RNAi), by controlling the elimination of endogenous transcripts from mobile and repetitive DNA elements of the genome as well as exogenous RNA of viral origin. Also acts in an RNAi-independent manner to activate translation through cytoplasmic polyadenylation. As well as its role in dsRNA processing, essential in several steps of the siRNA biogenesis pathway, including siRNA loading into the Argonaute 2 (AGO2)-containing RNA-induced silencing complex (siRISC), length-dependent dicing and guide strand selection for target silencing by the siRISC. Cleaves dsRNAs into siRNAs that are predominantly around twenty-one nucleotides in length. Displays a preference for binding and processing blunt termini (BLT), likely non- self dsRNAs, over dsRNAs with 2 nucleotides 3' overhanging (3'ovr) termini, which are typically the structure of endogenous dsRNAs. According to many reports, the cleavage reaction mode of the enzyme changes according to the termini of the dsRNA substrate. BLT dsRNAs undergo an ATP-dependent processive reaction whereby multiple siRNAs of heterogeneous sizes are produced before the enzyme dissociates. In contrast, dsRNAs with 3'ovr termini, which are typically the structure of endogenous dsRNAs, undergo ATP-independent, distributive cleavage whereby the enzyme dissociates after each cleavage to produce siRNAs of around 22 nucleotides. However, according to another report, the mode of cleavage reaction is not affected by the terminal structures of the dsRNAs substrates. This report suggests that the enzyme is able to initiate processive cleavage of both BLT and 3'ovr dsRNA substrates, and only rarely initiates distributive cleavage. During dsRNA processing and AGO2-loading, requires association with dsRNA-binding accessory proteins loqs isoform PD (loqs-PD) and r2d2. Functions with r2d2 to form the siRNA-mediated RISC loading complex (siRLC) which is responsible for Ago2-loading of endo- and exo-siRNAs. Interaction with loqs-PD increases initial binding to dsRNA substrates and promotes processing of a subset of endo- and exo-dsRNAs. In the absence of r2d2, may also form an alternative siRLC with loqs-PD to load siRNAs into the siRISC. Function with loqs-PD allows the dicer enzyme to cleave endogenous dsRNA templates independently of their termini, and is required for ATP-dependent processing of a subset of siRNAs but is not required for antiviral RNAi. This suggests that the enzyme's intrinsic termini preferences function in viral defense, while function with loqs-PD allows processing of endogenous dsRNAs with diverse termini. However, according to another report the mode of cleavage reaction is not affected by the presence or absence of loqs-PD. Loaded siRNAs serve as a guide to direct the siRISC to complementary RNAs to degrade them or prevent their translation. The siRLC plays an important role in the ATP-dependent asymmetry sensing of the duplex, and is therefore also responsible for the selection of the strand that ultimately acts as the guide siRNA for the siRISC. Thermodynamically asymmetric siRNAs are preoriented in the siRLC by either the dsRNA-binding r2d2 protein, or the loqs-PD protein in the alternative siRLC, which preferentially bind to the most thermodynamically stable strand prior to loading onto AGO2. Both r2d2 and Dcr- 2 also initiate unwinding of the siRNA duplex, at which point the heterodimer is exchanged by AGO2. The strand that was bound by r2d2 is discarded while the one that was bound by Dcr-2 is loaded onto Ago2 and serves as guide to direct the siRISC to complementary RNAs to degrade them or prevent their translation. Independently of its role in RNAi, acts with the cytoplasmic poly(A) polymerase wisp to promote cytoplasmic polyadenylation and translational activation of certain messenger RNAs including r2d2 and toll (Tl) transcripts. Consequently it is involved in the post- transcriptional regulation of the Toll immune signaling pathway and promoting resistance to fungal and viral infections. As an RNA-binding protein, likely functions in cytoplasmic polyadenylation by recruiting the poly(A) RNA polymerase wisp to target mRNAs.",Membrane; Single-pass membrane protein. Belongs to the helicase family,Vague,No,No,Vague,Vague,not-Yes,GO:0005524; GO:0016887; GO:0008186; GO:0004530; GO:0004386; GO:0003730; GO:0004525; GO:0003723; GO:0035197,GO:0004386; GO:0005524,GO:0004386,GO:0004386; GO:0005524,GO:0004386,GO:0004386,0.5065,0.3559,0.5065,0.3559,0.3559,5,0.4161,0.6256,yes
DCR2_DROME,A1ZAW0,ProtTale,Eukaryota,1722,"Double-stranded RNA (dsRNA) endoribonuclease which cleaves endogenous (endo), exogenous (exo), and viral dsRNAs to produce short interfering RNAs (siRNAs). The generated siRNAs then mediate gene silencing, also called RNA interference (RNAi), by controlling the elimination of endogenous transcripts from mobile and repetitive DNA elements of the genome as well as exogenous RNA of viral origin. Also acts in an RNAi-independent manner to activate translation through cytoplasmic polyadenylation. As well as its role in dsRNA processing, essential in several steps of the siRNA biogenesis pathway, including siRNA loading into the Argonaute 2 (AGO2)-containing RNA-induced silencing complex (siRISC), length-dependent dicing and guide strand selection for target silencing by the siRISC. Cleaves dsRNAs into siRNAs that are predominantly around twenty-one nucleotides in length. Displays a preference for binding and processing blunt termini (BLT), likely non- self dsRNAs, over dsRNAs with 2 nucleotides 3' overhanging (3'ovr) termini, which are typically the structure of endogenous dsRNAs. According to many reports, the cleavage reaction mode of the enzyme changes according to the termini of the dsRNA substrate. BLT dsRNAs undergo an ATP-dependent processive reaction whereby multiple siRNAs of heterogeneous sizes are produced before the enzyme dissociates. In contrast, dsRNAs with 3'ovr termini, which are typically the structure of endogenous dsRNAs, undergo ATP-independent, distributive cleavage whereby the enzyme dissociates after each cleavage to produce siRNAs of around 22 nucleotides. However, according to another report, the mode of cleavage reaction is not affected by the terminal structures of the dsRNAs substrates. This report suggests that the enzyme is able to initiate processive cleavage of both BLT and 3'ovr dsRNA substrates, and only rarely initiates distributive cleavage. During dsRNA processing and AGO2-loading, requires association with dsRNA-binding accessory proteins loqs isoform PD (loqs-PD) and r2d2. Functions with r2d2 to form the siRNA-mediated RISC loading complex (siRLC) which is responsible for Ago2-loading of endo- and exo-siRNAs. Interaction with loqs-PD increases initial binding to dsRNA substrates and promotes processing of a subset of endo- and exo-dsRNAs. In the absence of r2d2, may also form an alternative siRLC with loqs-PD to load siRNAs into the siRISC. Function with loqs-PD allows the dicer enzyme to cleave endogenous dsRNA templates independently of their termini, and is required for ATP-dependent processing of a subset of siRNAs but is not required for antiviral RNAi. This suggests that the enzyme's intrinsic termini preferences function in viral defense, while function with loqs-PD allows processing of endogenous dsRNAs with diverse termini. However, according to another report the mode of cleavage reaction is not affected by the presence or absence of loqs-PD. Loaded siRNAs serve as a guide to direct the siRISC to complementary RNAs to degrade them or prevent their translation. The siRLC plays an important role in the ATP-dependent asymmetry sensing of the duplex, and is therefore also responsible for the selection of the strand that ultimately acts as the guide siRNA for the siRISC. Thermodynamically asymmetric siRNAs are preoriented in the siRLC by either the dsRNA-binding r2d2 protein, or the loqs-PD protein in the alternative siRLC, which preferentially bind to the most thermodynamically stable strand prior to loading onto AGO2. Both r2d2 and Dcr- 2 also initiate unwinding of the siRNA duplex, at which point the heterodimer is exchanged by AGO2. The strand that was bound by r2d2 is discarded while the one that was bound by Dcr-2 is loaded onto Ago2 and serves as guide to direct the siRISC to complementary RNAs to degrade them or prevent their translation. Independently of its role in RNAi, acts with the cytoplasmic poly(A) polymerase wisp to promote cytoplasmic polyadenylation and translational activation of certain messenger RNAs including r2d2 and toll (Tl) transcripts. Consequently it is involved in the post- transcriptional regulation of the Toll immune signaling pathway and promoting resistance to fungal and viral infections. As an RNA-binding protein, likely functions in cytoplasmic polyadenylation by recruiting the poly(A) RNA polymerase wisp to target mRNAs.","Dicer-like endonuclease involved in cleaving double-stranded RNA in the RNA interference (RNAi) pathway. Produces 21 to 25 bp dsRNAs (siRNAs) which target the selective destruction of homologous RNAs leading to sequence-specific suppression of gene expression, called post-transcriptional gene silencing (PTGS). Part of a broad host defense response against viral infection and transposons.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0008186; GO:0004530; GO:0004386; GO:0003730; GO:0004525; GO:0003723; GO:0035197,GO:0004525,GO:0004525; GO:0003725,GO:0004525; GO:0003723,GO:0004525,GO:0004525; GO:0003723,0.3206,0.5534,0.6101,0.3206,0.6101,5,0.483,0.6256,yes
DCR2_DROME,A1ZAW0,Protein2Text,Eukaryota,1722,"Double-stranded RNA (dsRNA) endoribonuclease which cleaves endogenous (endo), exogenous (exo), and viral dsRNAs to produce short interfering RNAs (siRNAs). The generated siRNAs then mediate gene silencing, also called RNA interference (RNAi), by controlling the elimination of endogenous transcripts from mobile and repetitive DNA elements of the genome as well as exogenous RNA of viral origin. Also acts in an RNAi-independent manner to activate translation through cytoplasmic polyadenylation. As well as its role in dsRNA processing, essential in several steps of the siRNA biogenesis pathway, including siRNA loading into the Argonaute 2 (AGO2)-containing RNA-induced silencing complex (siRISC), length-dependent dicing and guide strand selection for target silencing by the siRISC. Cleaves dsRNAs into siRNAs that are predominantly around twenty-one nucleotides in length. Displays a preference for binding and processing blunt termini (BLT), likely non- self dsRNAs, over dsRNAs with 2 nucleotides 3' overhanging (3'ovr) termini, which are typically the structure of endogenous dsRNAs. According to many reports, the cleavage reaction mode of the enzyme changes according to the termini of the dsRNA substrate. BLT dsRNAs undergo an ATP-dependent processive reaction whereby multiple siRNAs of heterogeneous sizes are produced before the enzyme dissociates. In contrast, dsRNAs with 3'ovr termini, which are typically the structure of endogenous dsRNAs, undergo ATP-independent, distributive cleavage whereby the enzyme dissociates after each cleavage to produce siRNAs of around 22 nucleotides. However, according to another report, the mode of cleavage reaction is not affected by the terminal structures of the dsRNAs substrates. This report suggests that the enzyme is able to initiate processive cleavage of both BLT and 3'ovr dsRNA substrates, and only rarely initiates distributive cleavage. During dsRNA processing and AGO2-loading, requires association with dsRNA-binding accessory proteins loqs isoform PD (loqs-PD) and r2d2. Functions with r2d2 to form the siRNA-mediated RISC loading complex (siRLC) which is responsible for Ago2-loading of endo- and exo-siRNAs. Interaction with loqs-PD increases initial binding to dsRNA substrates and promotes processing of a subset of endo- and exo-dsRNAs. In the absence of r2d2, may also form an alternative siRLC with loqs-PD to load siRNAs into the siRISC. Function with loqs-PD allows the dicer enzyme to cleave endogenous dsRNA templates independently of their termini, and is required for ATP-dependent processing of a subset of siRNAs but is not required for antiviral RNAi. This suggests that the enzyme's intrinsic termini preferences function in viral defense, while function with loqs-PD allows processing of endogenous dsRNAs with diverse termini. However, according to another report the mode of cleavage reaction is not affected by the presence or absence of loqs-PD. Loaded siRNAs serve as a guide to direct the siRISC to complementary RNAs to degrade them or prevent their translation. The siRLC plays an important role in the ATP-dependent asymmetry sensing of the duplex, and is therefore also responsible for the selection of the strand that ultimately acts as the guide siRNA for the siRISC. Thermodynamically asymmetric siRNAs are preoriented in the siRLC by either the dsRNA-binding r2d2 protein, or the loqs-PD protein in the alternative siRLC, which preferentially bind to the most thermodynamically stable strand prior to loading onto AGO2. Both r2d2 and Dcr- 2 also initiate unwinding of the siRNA duplex, at which point the heterodimer is exchanged by AGO2. The strand that was bound by r2d2 is discarded while the one that was bound by Dcr-2 is loaded onto Ago2 and serves as guide to direct the siRISC to complementary RNAs to degrade them or prevent their translation. Independently of its role in RNAi, acts with the cytoplasmic poly(A) polymerase wisp to promote cytoplasmic polyadenylation and translational activation of certain messenger RNAs including r2d2 and toll (Tl) transcripts. Consequently it is involved in the post- transcriptional regulation of the Toll immune signaling pathway and promoting resistance to fungal and viral infections. As an RNA-binding protein, likely functions in cytoplasmic polyadenylation by recruiting the poly(A) RNA polymerase wisp to target mRNAs.","This protein is a part of the DNA repair machinery. It is a helicase, which means it unwinds double-stranded DNA into single strands to allow for repair. Specifically, it is involved in the homologous recombination repair pathway, which is a type of DNA repair that uses a template of undamaged DNA to repair damaged DNA.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016887; GO:0008186; GO:0004530; GO:0004386; GO:0003730; GO:0004525; GO:0003723; GO:0035197,GO:0003678; GO:0003677,GO:0004003; GO:0003677,GO:0003678,GO:0003678,GO:0003678; GO:0003677,0.4601,0.4601,0.2922,0.2922,0.4601,5,0.3929,0.6256,yes
DCR2_DROME,A1ZAW0,Reference,Eukaryota,1722,"Double-stranded RNA (dsRNA) endoribonuclease which cleaves endogenous (endo), exogenous (exo), and viral dsRNAs to produce short interfering RNAs (siRNAs). The generated siRNAs then mediate gene silencing, also called RNA interference (RNAi), by controlling the elimination of endogenous transcripts from mobile and repetitive DNA elements of the genome as well as exogenous RNA of viral origin. Also acts in an RNAi-independent manner to activate translation through cytoplasmic polyadenylation. As well as its role in dsRNA processing, essential in several steps of the siRNA biogenesis pathway, including siRNA loading into the Argonaute 2 (AGO2)-containing RNA-induced silencing complex (siRISC), length-dependent dicing and guide strand selection for target silencing by the siRISC. Cleaves dsRNAs into siRNAs that are predominantly around twenty-one nucleotides in length. Displays a preference for binding and processing blunt termini (BLT), likely non- self dsRNAs, over dsRNAs with 2 nucleotides 3' overhanging (3'ovr) termini, which are typically the structure of endogenous dsRNAs. According to many reports, the cleavage reaction mode of the enzyme changes according to the termini of the dsRNA substrate. BLT dsRNAs undergo an ATP-dependent processive reaction whereby multiple siRNAs of heterogeneous sizes are produced before the enzyme dissociates. In contrast, dsRNAs with 3'ovr termini, which are typically the structure of endogenous dsRNAs, undergo ATP-independent, distributive cleavage whereby the enzyme dissociates after each cleavage to produce siRNAs of around 22 nucleotides. However, according to another report, the mode of cleavage reaction is not affected by the terminal structures of the dsRNAs substrates. This report suggests that the enzyme is able to initiate processive cleavage of both BLT and 3'ovr dsRNA substrates, and only rarely initiates distributive cleavage. During dsRNA processing and AGO2-loading, requires association with dsRNA-binding accessory proteins loqs isoform PD (loqs-PD) and r2d2. Functions with r2d2 to form the siRNA-mediated RISC loading complex (siRLC) which is responsible for Ago2-loading of endo- and exo-siRNAs. Interaction with loqs-PD increases initial binding to dsRNA substrates and promotes processing of a subset of endo- and exo-dsRNAs. In the absence of r2d2, may also form an alternative siRLC with loqs-PD to load siRNAs into the siRISC. Function with loqs-PD allows the dicer enzyme to cleave endogenous dsRNA templates independently of their termini, and is required for ATP-dependent processing of a subset of siRNAs but is not required for antiviral RNAi. This suggests that the enzyme's intrinsic termini preferences function in viral defense, while function with loqs-PD allows processing of endogenous dsRNAs with diverse termini. However, according to another report the mode of cleavage reaction is not affected by the presence or absence of loqs-PD. Loaded siRNAs serve as a guide to direct the siRISC to complementary RNAs to degrade them or prevent their translation. The siRLC plays an important role in the ATP-dependent asymmetry sensing of the duplex, and is therefore also responsible for the selection of the strand that ultimately acts as the guide siRNA for the siRISC. Thermodynamically asymmetric siRNAs are preoriented in the siRLC by either the dsRNA-binding r2d2 protein, or the loqs-PD protein in the alternative siRLC, which preferentially bind to the most thermodynamically stable strand prior to loading onto AGO2. Both r2d2 and Dcr- 2 also initiate unwinding of the siRNA duplex, at which point the heterodimer is exchanged by AGO2. The strand that was bound by r2d2 is discarded while the one that was bound by Dcr-2 is loaded onto Ago2 and serves as guide to direct the siRISC to complementary RNAs to degrade them or prevent their translation. Independently of its role in RNAi, acts with the cytoplasmic poly(A) polymerase wisp to promote cytoplasmic polyadenylation and translational activation of certain messenger RNAs including r2d2 and toll (Tl) transcripts. Consequently it is involved in the post- transcriptional regulation of the Toll immune signaling pathway and promoting resistance to fungal and viral infections. As an RNA-binding protein, likely functions in cytoplasmic polyadenylation by recruiting the poly(A) RNA polymerase wisp to target mRNAs.","Double-stranded RNA (dsRNA) endoribonuclease which cleaves endogenous (endo), exogenous (exo), and viral dsRNAs to produce short interfering RNAs (siRNAs). The generated siRNAs then mediate gene silencing, also called RNA interference (RNAi), by controlling the elimination of endogenous transcripts from mobile and repetitive DNA elements of the genome as well as exogenous RNA of viral origin. Also acts in an RNAi-independent manner to activate translation through cytoplasmic polyadenylation. As well as its role in dsRNA processing, essential in several steps of the siRNA biogenesis pathway, including siRNA loading into the Argonaute 2 (AGO2)-containing RNA-induced silencing complex (siRISC), length-dependent dicing and guide strand selection for target silencing by the siRISC. Cleaves dsRNAs into siRNAs that are predominantly around twenty-one nucleotides in length. Displays a preference for binding and processing blunt termini (BLT), likely non- self dsRNAs, over dsRNAs with 2 nucleotides 3' overhanging (3'ovr) termini, which are typically the structure of endogenous dsRNAs. According to many reports, the cleavage reaction mode of the enzyme changes according to the termini of the dsRNA substrate. BLT dsRNAs undergo an ATP-dependent processive reaction whereby multiple siRNAs of heterogeneous sizes are produced before the enzyme dissociates. In contrast, dsRNAs with 3'ovr termini, which are typically the structure of endogenous dsRNAs, undergo ATP-independent, distributive cleavage whereby the enzyme dissociates after each cleavage to produce siRNAs of around 22 nucleotides. However, according to another report, the mode of cleavage reaction is not affected by the terminal structures of the dsRNAs substrates. This report suggests that the enzyme is able to initiate processive cleavage of both BLT and 3'ovr dsRNA substrates, and only rarely initiates distributive cleavage. During dsRNA processing and AGO2-loading, requires association with dsRNA-binding accessory proteins loqs isoform PD (loqs-PD) and r2d2. Functions with r2d2 to form the siRNA-mediated RISC loading complex (siRLC) which is responsible for Ago2-loading of endo- and exo-siRNAs. Interaction with loqs-PD increases initial binding to dsRNA substrates and promotes processing of a subset of endo- and exo-dsRNAs. In the absence of r2d2, may also form an alternative siRLC with loqs-PD to load siRNAs into the siRISC. Function with loqs-PD allows the dicer enzyme to cleave endogenous dsRNA templates independently of their termini, and is required for ATP-dependent processing of a subset of siRNAs but is not required for antiviral RNAi. This suggests that the enzyme's intrinsic termini preferences function in viral defense, while function with loqs-PD allows processing of endogenous dsRNAs with diverse termini. However, according to another report the mode of cleavage reaction is not affected by the presence or absence of loqs-PD. Loaded siRNAs serve as a guide to direct the siRISC to complementary RNAs to degrade them or prevent their translation. The siRLC plays an important role in the ATP-dependent asymmetry sensing of the duplex, and is therefore also responsible for the selection of the strand that ultimately acts as the guide siRNA for the siRISC. Thermodynamically asymmetric siRNAs are preoriented in the siRLC by either the dsRNA-binding r2d2 protein, or the loqs-PD protein in the alternative siRLC, which preferentially bind to the most thermodynamically stable strand prior to loading onto AGO2. Both r2d2 and Dcr- 2 also initiate unwinding of the siRNA duplex, at which point the heterodimer is exchanged by AGO2. The strand that was bound by r2d2 is discarded while the one that was bound by Dcr-2 is loaded onto Ago2 and serves as guide to direct the siRISC to complementary RNAs to degrade them or prevent their translation. Independently of its role in RNAi, acts with the cytoplasmic poly(A) polymerase wisp to promote cytoplasmic polyadenylation and translational activation of certain messenger RNAs including r2d2 and toll (Tl) transcripts. Consequently it is involved in the post- transcriptional regulation of the Toll immune signaling pathway and promoting resistance to fungal and viral infections. As an RNA-binding protein, likely functions in cytoplasmic polyadenylation by recruiting the poly(A) RNA polymerase wisp to target mRNAs.",,,,,,,GO:0005524; GO:0016887; GO:0008186; GO:0004530; GO:0004386; GO:0003730; GO:0004525; GO:0003723; GO:0035197,GO:0004525; GO:0003725; GO:0005524,GO:0004525; GO:0003725; GO:0005524,GO:0004525; GO:0003725; GO:0008026; GO:0005524,GO:0004525; GO:0003725; GO:0005524,GO:0004525; GO:0005524; GO:0003725,0.6621,0.6621,0.7697,0.6621,0.6621,5,0.6836,0.6256,yes
DUOX1_MOUSE,A2AQ92,ESM2Text,Eukaryota,1551,"Generates hydrogen peroxide (H2O2) which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormone synthesis. Also required for lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. Antimicrobial agent hypothiocyanite (OSCN-), which is produced by LPO from DUOX1-derived H2O2, promotes influenza virus inactivation by reducing viral binding to and entry into host cells. Promotes antiviral immunity by increasing airway cytokine levels, promoting innate immune cell recruitment and reducing airway epithelial cell apoptosis. In response to bacterial stimuli, activated by ATP and promotes EGFR/ERK signaling, ADAM17 activation, and EGFR ligand shedding, leading to enhanced CXCL8/IL8 expression and secretion in airway epithelia. Synthesizes NAADP from its reduced NAADPH form which promotes Ca(2+) signaling during T cell activation. In addition to its oxidase activity, has also been shown to have peroxidase activity through its N-terminal peroxidase- like domain. However, another study showed that the isolated peroxidase-like domain does not bind heme and has no intrinsic peroxidase activity.",Generates hydrogen peroxide which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormones synthesis and lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. May have its own peroxidase activity through its N-terminal peroxidase-like domain.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005509; GO:0071949; GO:0020037; GO:0016174; GO:0070402; GO:0004601; GO:0046982; GO:0016175,GO:0016491,GO:0016491; GO:0004601,GO:0016174,GO:0016491,GO:0016174,0.3558,0.4583,0.394,0.3558,0.394,5,0.3916,0.5121,no
DUOX1_MOUSE,A2AQ92,Prot2Text,Eukaryota,1551,"Generates hydrogen peroxide (H2O2) which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormone synthesis. Also required for lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. Antimicrobial agent hypothiocyanite (OSCN-), which is produced by LPO from DUOX1-derived H2O2, promotes influenza virus inactivation by reducing viral binding to and entry into host cells. Promotes antiviral immunity by increasing airway cytokine levels, promoting innate immune cell recruitment and reducing airway epithelial cell apoptosis. In response to bacterial stimuli, activated by ATP and promotes EGFR/ERK signaling, ADAM17 activation, and EGFR ligand shedding, leading to enhanced CXCL8/IL8 expression and secretion in airway epithelia. Synthesizes NAADP from its reduced NAADPH form which promotes Ca(2+) signaling during T cell activation. In addition to its oxidase activity, has also been shown to have peroxidase activity through its N-terminal peroxidase- like domain. However, another study showed that the isolated peroxidase-like domain does not bind heme and has no intrinsic peroxidase activity.",Generates hydrogen peroxide which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormones synthesis and lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. May have its own peroxidase activity through its N-terminal peroxidase-like domain.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005509; GO:0071949; GO:0020037; GO:0016174; GO:0070402; GO:0004601; GO:0046982; GO:0016175,GO:0016174,GO:0016174,GO:0016174,GO:0016491,GO:0016174,0.394,0.394,0.394,0.3558,0.394,5,0.3864,0.5121,no
DUOX1_MOUSE,A2AQ92,ProtT3,Eukaryota,1551,"Generates hydrogen peroxide (H2O2) which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormone synthesis. Also required for lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. Antimicrobial agent hypothiocyanite (OSCN-), which is produced by LPO from DUOX1-derived H2O2, promotes influenza virus inactivation by reducing viral binding to and entry into host cells. Promotes antiviral immunity by increasing airway cytokine levels, promoting innate immune cell recruitment and reducing airway epithelial cell apoptosis. In response to bacterial stimuli, activated by ATP and promotes EGFR/ERK signaling, ADAM17 activation, and EGFR ligand shedding, leading to enhanced CXCL8/IL8 expression and secretion in airway epithelia. Synthesizes NAADP from its reduced NAADPH form which promotes Ca(2+) signaling during T cell activation. In addition to its oxidase activity, has also been shown to have peroxidase activity through its N-terminal peroxidase- like domain. However, another study showed that the isolated peroxidase-like domain does not bind heme and has no intrinsic peroxidase activity.",Membrane; Single-pass type I membrane protein. Belongs to the calcineurin regulatory subunit family,No,No,No,No,Vague,not-Yes,GO:0005509; GO:0071949; GO:0020037; GO:0016174; GO:0070402; GO:0004601; GO:0046982; GO:0016175,,,,,,,,,,,0,,0.5121,no
DUOX1_MOUSE,A2AQ92,ProtTale,Eukaryota,1551,"Generates hydrogen peroxide (H2O2) which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormone synthesis. Also required for lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. Antimicrobial agent hypothiocyanite (OSCN-), which is produced by LPO from DUOX1-derived H2O2, promotes influenza virus inactivation by reducing viral binding to and entry into host cells. Promotes antiviral immunity by increasing airway cytokine levels, promoting innate immune cell recruitment and reducing airway epithelial cell apoptosis. In response to bacterial stimuli, activated by ATP and promotes EGFR/ERK signaling, ADAM17 activation, and EGFR ligand shedding, leading to enhanced CXCL8/IL8 expression and secretion in airway epithelia. Synthesizes NAADP from its reduced NAADPH form which promotes Ca(2+) signaling during T cell activation. In addition to its oxidase activity, has also been shown to have peroxidase activity through its N-terminal peroxidase- like domain. However, another study showed that the isolated peroxidase-like domain does not bind heme and has no intrinsic peroxidase activity.","Calcium-dependent NADPH oxidase that catalyzes the reduction of molecular oxygen to superoxide, a reactive oxygen species (ROS). Plays a role in the innate immune response by producing superoxide in response to bacterial infection.",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005509; GO:0071949; GO:0020037; GO:0016174; GO:0070402; GO:0004601; GO:0046982; GO:0016175,GO:0016175,GO:0016175,GO:0016174; GO:0050660,GO:0016174; GO:0005509,GO:0016174,0.394,0.394,0.6415,0.621,0.394,5,0.4889,0.5121,no
DUOX1_MOUSE,A2AQ92,Protein2Text,Eukaryota,1551,"Generates hydrogen peroxide (H2O2) which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormone synthesis. Also required for lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. Antimicrobial agent hypothiocyanite (OSCN-), which is produced by LPO from DUOX1-derived H2O2, promotes influenza virus inactivation by reducing viral binding to and entry into host cells. Promotes antiviral immunity by increasing airway cytokine levels, promoting innate immune cell recruitment and reducing airway epithelial cell apoptosis. In response to bacterial stimuli, activated by ATP and promotes EGFR/ERK signaling, ADAM17 activation, and EGFR ligand shedding, leading to enhanced CXCL8/IL8 expression and secretion in airway epithelia. Synthesizes NAADP from its reduced NAADPH form which promotes Ca(2+) signaling during T cell activation. In addition to its oxidase activity, has also been shown to have peroxidase activity through its N-terminal peroxidase- like domain. However, another study showed that the isolated peroxidase-like domain does not bind heme and has no intrinsic peroxidase activity.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its name, it is likely that this protein is a peroxidase, which is an enzyme that catalyzes the oxidation of a variety of substrates using hydrogen peroxide as an electron acceptor. Peroxidases are involved in various cellular processes, including defense against oxidative stress, detoxification of harmful compounds, and regulation of cell signaling pathways.",Maybe,No,No,No,Maybe,not-Yes,GO:0005509; GO:0071949; GO:0020037; GO:0016174; GO:0070402; GO:0004601; GO:0046982; GO:0016175,GO:0004601,GO:0004601,GO:0004601,GO:0004601,GO:0004601,0.3706,0.3706,0.3706,0.3706,0.3706,5,0.3706,0.5121,no
DUOX1_MOUSE,A2AQ92,Reference,Eukaryota,1551,"Generates hydrogen peroxide (H2O2) which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormone synthesis. Also required for lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. Antimicrobial agent hypothiocyanite (OSCN-), which is produced by LPO from DUOX1-derived H2O2, promotes influenza virus inactivation by reducing viral binding to and entry into host cells. Promotes antiviral immunity by increasing airway cytokine levels, promoting innate immune cell recruitment and reducing airway epithelial cell apoptosis. In response to bacterial stimuli, activated by ATP and promotes EGFR/ERK signaling, ADAM17 activation, and EGFR ligand shedding, leading to enhanced CXCL8/IL8 expression and secretion in airway epithelia. Synthesizes NAADP from its reduced NAADPH form which promotes Ca(2+) signaling during T cell activation. In addition to its oxidase activity, has also been shown to have peroxidase activity through its N-terminal peroxidase- like domain. However, another study showed that the isolated peroxidase-like domain does not bind heme and has no intrinsic peroxidase activity.","Generates hydrogen peroxide (H2O2) which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormone synthesis. Also required for lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. Antimicrobial agent hypothiocyanite (OSCN-), which is produced by LPO from DUOX1-derived H2O2, promotes influenza virus inactivation by reducing viral binding to and entry into host cells. Promotes antiviral immunity by increasing airway cytokine levels, promoting innate immune cell recruitment and reducing airway epithelial cell apoptosis. In response to bacterial stimuli, activated by ATP and promotes EGFR/ERK signaling, ADAM17 activation, and EGFR ligand shedding, leading to enhanced CXCL8/IL8 expression and secretion in airway epithelia. Synthesizes NAADP from its reduced NAADPH form which promotes Ca(2+) signaling during T cell activation. In addition to its oxidase activity, has also been shown to have peroxidase activity through its N-terminal peroxidase- like domain. However, another study showed that the isolated peroxidase-like domain does not bind heme and has no intrinsic peroxidase activity.",,,,,,,GO:0005509; GO:0071949; GO:0020037; GO:0016174; GO:0070402; GO:0004601; GO:0046982; GO:0016175,GO:0016174,GO:0016174,GO:0016174,GO:0016491; GO:0050660,GO:0016491; GO:0004601,0.394,0.394,0.394,0.5752,0.4583,5,0.4431,0.5121,no
AGLTA_ASPNC,A2QTS4,ESM2Text,Eukaryota,555,"Transfers a segment of a (1->4)-alpha-D-glucan to an acceptor oligosaccharide; maltose and larger maltooligosaccharides are the most efficient acceptor substrates, though it also has some activity on alpha(1,3)-linked oligosaccharides. Also has a low hydrolyzing activity on starch, producing short oligosaccharides. Contributes to cell wall polysaccharide biosynthesis and cell wall assembly.",Has a role in the cell wall biosynthesis where it is involved in maintaining cell wall strength and shape.,Vague,Vague,Vague,No,No,not-Yes,GO:0004134; GO:0004556; GO:0005509,,,,,,,,,,,0,,0.1926,no
AGLTA_ASPNC,A2QTS4,Prot2Text,Eukaryota,555,"Transfers a segment of a (1->4)-alpha-D-glucan to an acceptor oligosaccharide; maltose and larger maltooligosaccharides are the most efficient acceptor substrates, though it also has some activity on alpha(1,3)-linked oligosaccharides. Also has a low hydrolyzing activity on starch, producing short oligosaccharides. Contributes to cell wall polysaccharide biosynthesis and cell wall assembly.",Important for breakdown of endosperm starch during germination.,No,Vague,No,No,No,not-Yes,GO:0004134; GO:0004556; GO:0005509,GO:0004556,,,GO:0004556,GO:0004556,0.56,,,0.56,0.56,3,0.56,0.1926,no
AGLTA_ASPNC,A2QTS4,ProtT3,Eukaryota,555,"Transfers a segment of a (1->4)-alpha-D-glucan to an acceptor oligosaccharide; maltose and larger maltooligosaccharides are the most efficient acceptor substrates, though it also has some activity on alpha(1,3)-linked oligosaccharides. Also has a low hydrolyzing activity on starch, producing short oligosaccharides. Contributes to cell wall polysaccharide biosynthesis and cell wall assembly.","Cell membrane; Lipid-anchor, GPI- anchor. Belongs to the glycosyl hydrolase 13 family",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004134; GO:0004556; GO:0005509,GO:0016798,GO:0004556,GO:0004556,GO:0004556,GO:0016798,0.4224,0.56,0.56,0.56,0.4224,5,0.505,0.1926,no
AGLTA_ASPNC,A2QTS4,ProtTale,Eukaryota,555,"Transfers a segment of a (1->4)-alpha-D-glucan to an acceptor oligosaccharide; maltose and larger maltooligosaccharides are the most efficient acceptor substrates, though it also has some activity on alpha(1,3)-linked oligosaccharides. Also has a low hydrolyzing activity on starch, producing short oligosaccharides. Contributes to cell wall polysaccharide biosynthesis and cell wall assembly.","Transfers a segment of a (1->4)-alpha-D-glucan to an acceptor oligosaccharide; can transfer from alpha-1,3-1,4-1,4-1,4-1,6-1,6-1,6-1,6-1,6-1,6-1,6-1,6-1,6-1,6-1,6-1,6-1,6-1,6-1,6-1,6-1,6-1,6-1,6-1,6-",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004134; GO:0004556; GO:0005509,GO:0004134,GO:0016757,GO:0004134,GO:0016757,GO:0004134,0.5627,0.4556,0.5627,0.4556,0.5627,5,0.5199,0.1926,no
AGLTA_ASPNC,A2QTS4,Protein2Text,Eukaryota,555,"Transfers a segment of a (1->4)-alpha-D-glucan to an acceptor oligosaccharide; maltose and larger maltooligosaccharides are the most efficient acceptor substrates, though it also has some activity on alpha(1,3)-linked oligosaccharides. Also has a low hydrolyzing activity on starch, producing short oligosaccharides. Contributes to cell wall polysaccharide biosynthesis and cell wall assembly.","The molecular function of this protein is to catalyze the hydrolysis of alpha-1,4-glycosidic bonds in polysaccharides, specifically in the breakdown of complex carbohydrates.",Maybe,Maybe,No,No,Maybe,not-Yes,GO:0004134; GO:0004556; GO:0005509,GO:0004556,GO:0004556,GO:0004556,GO:0004556,GO:0004556,0.56,0.56,0.56,0.56,0.56,5,0.56,0.1926,no
AGLTA_ASPNC,A2QTS4,Reference,Eukaryota,555,"Transfers a segment of a (1->4)-alpha-D-glucan to an acceptor oligosaccharide; maltose and larger maltooligosaccharides are the most efficient acceptor substrates, though it also has some activity on alpha(1,3)-linked oligosaccharides. Also has a low hydrolyzing activity on starch, producing short oligosaccharides. Contributes to cell wall polysaccharide biosynthesis and cell wall assembly.","Transfers a segment of a (1->4)-alpha-D-glucan to an acceptor oligosaccharide; maltose and larger maltooligosaccharides are the most efficient acceptor substrates, though it also has some activity on alpha(1,3)-linked oligosaccharides. Also has a low hydrolyzing activity on starch, producing short oligosaccharides. Contributes to cell wall polysaccharide biosynthesis and cell wall assembly.",,,,,,,GO:0004134; GO:0004556; GO:0005509,GO:0004134,GO:0004134,GO:0004134,GO:0016757,GO:0016757,0.5627,0.5627,0.5627,0.4556,0.4556,5,0.5199,0.1926,no
AGLTB_ASPNC,A2QYT9,ESM2Text,Eukaryota,549,"Transfers a segment of a (1->4)-alpha-D-glucan to an acceptor oligosaccharide; maltose and larger maltooligosaccharides are the most efficient acceptor substrates, though it also has very limited activity on alpha(1,3)-linked oligosaccharides. Also has a low hydrolyzing activity on starch, producing short oligosaccharides. Contributes to cell wall polysaccharide biosynthesis and cell wall assembly.","Converts alpha-amylase to amylase, the precursor for the branches on the mature spore wall.",No,No,No,No,No,not-Yes,GO:0004134; GO:0004556; GO:0005509,,,,,,,,,,,0,,0.2245,no
AGLTB_ASPNC,A2QYT9,Prot2Text,Eukaryota,549,"Transfers a segment of a (1->4)-alpha-D-glucan to an acceptor oligosaccharide; maltose and larger maltooligosaccharides are the most efficient acceptor substrates, though it also has very limited activity on alpha(1,3)-linked oligosaccharides. Also has a low hydrolyzing activity on starch, producing short oligosaccharides. Contributes to cell wall polysaccharide biosynthesis and cell wall assembly.",Important for breakdown of endosperm starch during germination.,No,Vague,No,No,No,not-Yes,GO:0004134; GO:0004556; GO:0005509,GO:0004556,,,GO:0004556,GO:0004556,0.56,,,0.56,0.56,3,0.56,0.2245,no
AGLTB_ASPNC,A2QYT9,ProtT3,Eukaryota,549,"Transfers a segment of a (1->4)-alpha-D-glucan to an acceptor oligosaccharide; maltose and larger maltooligosaccharides are the most efficient acceptor substrates, though it also has very limited activity on alpha(1,3)-linked oligosaccharides. Also has a low hydrolyzing activity on starch, producing short oligosaccharides. Contributes to cell wall polysaccharide biosynthesis and cell wall assembly.","Cell membrane; Lipid-anchor, GPI- anchor. Belongs to the glycosyl hydrolase 13 family",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004134; GO:0004556; GO:0005509,GO:0016798,GO:0004556,GO:0004556,GO:0004556,GO:0016798,0.4224,0.56,0.56,0.56,0.4224,5,0.505,0.2245,no
AGLTB_ASPNC,A2QYT9,ProtTale,Eukaryota,549,"Transfers a segment of a (1->4)-alpha-D-glucan to an acceptor oligosaccharide; maltose and larger maltooligosaccharides are the most efficient acceptor substrates, though it also has very limited activity on alpha(1,3)-linked oligosaccharides. Also has a low hydrolyzing activity on starch, producing short oligosaccharides. Contributes to cell wall polysaccharide biosynthesis and cell wall assembly.","Cleaves the terminal alpha 1,4-linked mannose residue from high-mannose type oligosaccharides present on glycoprotein and glycolipid substrates. Involved in the biosynthesis of high-mannose type oligosaccharides (Man(5-9)GlcNAc(2)) present in N- and O-linked glycoproteins.",No,No,No,No,No,not-Yes,GO:0004134; GO:0004556; GO:0005509,GO:0004559,GO:0004559,GO:0004559,GO:0004571,GO:0004559,0.3322,0.3322,0.3322,0.2608,0.3322,5,0.3179,0.2245,no
AGLTB_ASPNC,A2QYT9,Protein2Text,Eukaryota,549,"Transfers a segment of a (1->4)-alpha-D-glucan to an acceptor oligosaccharide; maltose and larger maltooligosaccharides are the most efficient acceptor substrates, though it also has very limited activity on alpha(1,3)-linked oligosaccharides. Also has a low hydrolyzing activity on starch, producing short oligosaccharides. Contributes to cell wall polysaccharide biosynthesis and cell wall assembly.","The molecular function of this protein is associated with carbohydrate metabolic process, specifically hydrolyzing complex carbohydrates into simpler sugars.",Vague,Vague,No,Vague,Maybe,not-Yes,GO:0004134; GO:0004556; GO:0005509,,GO:0004553,,,GO:0004553,,0.4587,,,0.4587,2,0.4587,0.2245,no
AGLTB_ASPNC,A2QYT9,Reference,Eukaryota,549,"Transfers a segment of a (1->4)-alpha-D-glucan to an acceptor oligosaccharide; maltose and larger maltooligosaccharides are the most efficient acceptor substrates, though it also has very limited activity on alpha(1,3)-linked oligosaccharides. Also has a low hydrolyzing activity on starch, producing short oligosaccharides. Contributes to cell wall polysaccharide biosynthesis and cell wall assembly.","Transfers a segment of a (1->4)-alpha-D-glucan to an acceptor oligosaccharide; maltose and larger maltooligosaccharides are the most efficient acceptor substrates, though it also has very limited activity on alpha(1,3)-linked oligosaccharides. Also has a low hydrolyzing activity on starch, producing short oligosaccharides. Contributes to cell wall polysaccharide biosynthesis and cell wall assembly.",,,,,,,GO:0004134; GO:0004556; GO:0005509,GO:0004134,GO:0004134,GO:0004134,GO:0016757,GO:0016757,0.5627,0.5627,0.5627,0.4556,0.4556,5,0.5199,0.2245,no
L_RVFV,A2SZS3,ESM2Text,Viruses,2092,"RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (Probable). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre- mRNAs. These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are not polyadenylated. During replication, the polymerase binds the 5' and 3' vRNA extremities at distinct sites. In turn, significant conformational changes occur in the polymerase and in vRNA to initiate active RNA synthesis. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated.",Essential component of the gamma-glutamyl methyltransferase complex that catalyzes the formation of gamma-glutamyl methyluridine in the arginine residues of proteins. Has a role in meiosis.,No,No,No,No,No,not-Yes,GO:0016787; GO:0046872; GO:0001882; GO:0003968,GO:0008168,,,GO:0008168,GO:0008168,0.2654,,,0.2654,0.2654,3,0.2654,0.6708,yes
L_RVFV,A2SZS3,Prot2Text,Viruses,2092,"RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (Probable). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre- mRNAs. These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are not polyadenylated. During replication, the polymerase binds the 5' and 3' vRNA extremities at distinct sites. In turn, significant conformational changes occur in the polymerase and in vRNA to initiate active RNA synthesis. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated.",Essential component of the gamma-glutamyl methyltransferase complex that catalyzes the formation of gamma-glutamyl methyluridine in the arginine residues of proteins. Has a role in meiosis.,No,No,No,No,No,not-Yes,GO:0016787; GO:0046872; GO:0001882; GO:0003968,,GO:0008168,,GO:0008168,GO:0008168,,0.2654,,0.2654,0.2654,3,0.2654,0.6708,yes
L_RVFV,A2SZS3,ProtT3,Viruses,2092,"RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (Probable). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre- mRNAs. These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are not polyadenylated. During replication, the polymerase binds the 5' and 3' vRNA extremities at distinct sites. In turn, significant conformational changes occur in the polymerase and in vRNA to initiate active RNA synthesis. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated.","RNA-dependent RNA polymerase which is responsible for replication and transcription of virus RNA segments. The transcription of viral mRNAs occurs by a unique mechanism called cap-snatching. 5' methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides by PA. In turn, these short capped RNAs are used as primers by PB1 for transcription of viral mRNAs. During virus replication, PB1 initiates RNA synthesis and copy vRNA into complementary RNA (cRNA) which in turn serves as a template for the production of more vRNAs. Host nucleus Host cytoplasm. SIMI",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016787; GO:0046872; GO:0001882; GO:0003968,GO:0003968,GO:0003968,GO:0003968,GO:0003968,GO:0003968,0.4825,0.4825,0.4825,0.4825,0.4825,5,0.4825,0.6708,yes
L_RVFV,A2SZS3,ProtTale,Viruses,2092,"RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (Probable). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre- mRNAs. These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are not polyadenylated. During replication, the polymerase binds the 5' and 3' vRNA extremities at distinct sites. In turn, significant conformational changes occur in the polymerase and in vRNA to initiate active RNA synthesis. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated.","RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate. During transcription, synthesizes subgenomic RNAs and assures their capping by a cap- snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs. These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are not polyadenylated. During replication, the polymerase binds the 5' and 3' vRNA extremities at distinct sites. In turn, significant conformational changes occur in the polymerase and in v",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016787; GO:0046872; GO:0001882; GO:0003968,GO:0003968; GO:0004519,GO:0003968; GO:0004519,GO:0003968; GO:0004519,GO:0003968; GO:0004519,GO:0003968,0.5063,0.5063,0.5063,0.5063,0.4825,5,0.5015,0.6708,yes
L_RVFV,A2SZS3,Protein2Text,Viruses,2092,"RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (Probable). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre- mRNAs. These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are not polyadenylated. During replication, the polymerase binds the 5' and 3' vRNA extremities at distinct sites. In turn, significant conformational changes occur in the polymerase and in vRNA to initiate active RNA synthesis. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated.","This protein is a polymerase, specifically a reverse transcriptase, which is a type of RNA-dependent DNA polymerase. It is responsible for transcribing RNA into DNA, a process that is essential for the replication of retroviruses.",No,No,No,No,No,not-Yes,GO:0016787; GO:0046872; GO:0001882; GO:0003968,GO:0003964,GO:0003964,GO:0003964,GO:0003964,GO:0003964,0.2823,0.2823,0.2823,0.2823,0.2823,5,0.2823,0.6708,yes
L_RVFV,A2SZS3,Reference,Viruses,2092,"RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (Probable). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre- mRNAs. These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are not polyadenylated. During replication, the polymerase binds the 5' and 3' vRNA extremities at distinct sites. In turn, significant conformational changes occur in the polymerase and in vRNA to initiate active RNA synthesis. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated.","RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (Probable). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre- mRNAs. These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are not polyadenylated. During replication, the polymerase binds the 5' and 3' vRNA extremities at distinct sites. In turn, significant conformational changes occur in the polymerase and in vRNA to initiate active RNA synthesis. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated.",,,,,,,GO:0016787; GO:0046872; GO:0001882; GO:0003968,GO:0003968; GO:0004519,GO:0003968; GO:0004519,GO:0003968; GO:0004519,GO:0003968; GO:0003723,GO:0003968; GO:0003723,0.5063,0.5063,0.5063,0.5296,0.5296,5,0.5156,0.6708,yes
PGMI_PYRCJ,A3MTR6,ESM2Text,Archaea,299,Dual specificity isomerase that catalyzes the isomerization of both glucose-6-phosphate and mannose-6-phosphate to fructose-6- phosphate with nearly similar catalytic efficiency. Also catalyzes the epimerization of mannose 6-phosphate to glucose 6- phosphate but the rate of epimerization reaction is 20-fold lower than that of isomerization reaction.,Catalyzes the isomerization of both glucose 6-phosphate and epimeric mannose 6-phosphate at a similar catalytic efficiency.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0097367; GO:0004347; GO:0004476,GO:0004347,GO:0004347; GO:0004476,GO:0004347; GO:0004476,GO:0004476,GO:0004347,0.7217,0.8316,0.8316,0.7217,0.7217,5,0.7657,0.4675,no
PGMI_PYRCJ,A3MTR6,Prot2Text,Archaea,299,Dual specificity isomerase that catalyzes the isomerization of both glucose-6-phosphate and mannose-6-phosphate to fructose-6- phosphate with nearly similar catalytic efficiency. Also catalyzes the epimerization of mannose 6-phosphate to glucose 6- phosphate but the rate of epimerization reaction is 20-fold lower than that of isomerization reaction.,Catalyzes the isomerization of both glucose 6-phosphate and epimeric mannose 6-phosphate at a similar catalytic efficiency.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0097367; GO:0004347; GO:0004476,GO:0004347; GO:0004476,GO:0004347; GO:0004476,GO:0004347; GO:0004476,GO:0005975,GO:0004347,0.8316,0.8316,0.8316,0.0,0.7217,5,0.6433,0.4675,no
PGMI_PYRCJ,A3MTR6,ProtT3,Archaea,299,Dual specificity isomerase that catalyzes the isomerization of both glucose-6-phosphate and mannose-6-phosphate to fructose-6- phosphate with nearly similar catalytic efficiency. Also catalyzes the epimerization of mannose 6-phosphate to glucose 6- phosphate but the rate of epimerization reaction is 20-fold lower than that of isomerization reaction.,Catalyzes the isomerization of glucose 6-phosphate to fructose 6-phosphate. Belongs to the PGI/PMI family,Yes,Yes,Maybe,Yes,Maybe,Yes,GO:0097367; GO:0004347; GO:0004476,GO:0004347,GO:0004347,GO:0004347,GO:0004347,GO:0004347,0.7217,0.7217,0.7217,0.7217,0.7217,5,0.7217,0.4675,no
PGMI_PYRCJ,A3MTR6,ProtTale,Archaea,299,Dual specificity isomerase that catalyzes the isomerization of both glucose-6-phosphate and mannose-6-phosphate to fructose-6- phosphate with nearly similar catalytic efficiency. Also catalyzes the epimerization of mannose 6-phosphate to glucose 6- phosphate but the rate of epimerization reaction is 20-fold lower than that of isomerization reaction.,Cleavage of the glucose moiety from the glucose-6-phosphate (G6P) molecule.,No,No,No,No,No,not-Yes,GO:0097367; GO:0004347; GO:0004476,GO:0004345,GO:0004346,GO:0004346,GO:0016787,GO:0004346,0.1894,0.1236,0.1236,0.332,0.1236,5,0.1784,0.4675,no
PGMI_PYRCJ,A3MTR6,Protein2Text,Archaea,299,Dual specificity isomerase that catalyzes the isomerization of both glucose-6-phosphate and mannose-6-phosphate to fructose-6- phosphate with nearly similar catalytic efficiency. Also catalyzes the epimerization of mannose 6-phosphate to glucose 6- phosphate but the rate of epimerization reaction is 20-fold lower than that of isomerization reaction.,"The molecular function of this protein is catalyzing the transfer of a phosphate group. More specifically, it is involved in the conversion of 2-deoxy-scyllo-inosose to 2-deoxy-scyllo-inosose 1-phosphate, a step in the biosynthesis of 2-deoxy-scyllo-inosamine, a precursor of pseudaminic acid, a component of several bacterial lipopolysaccharides.",No,No,No,No,No,not-Yes,GO:0097367; GO:0004347; GO:0004476,GO:0016301,GO:0016301,,GO:0016301,GO:0016301,0.2217,0.2217,,0.2217,0.2217,4,0.2217,0.4675,no
PGMI_PYRCJ,A3MTR6,Reference,Archaea,299,Dual specificity isomerase that catalyzes the isomerization of both glucose-6-phosphate and mannose-6-phosphate to fructose-6- phosphate with nearly similar catalytic efficiency. Also catalyzes the epimerization of mannose 6-phosphate to glucose 6- phosphate but the rate of epimerization reaction is 20-fold lower than that of isomerization reaction.,Dual specificity isomerase that catalyzes the isomerization of both glucose-6-phosphate and mannose-6-phosphate to fructose-6- phosphate with nearly similar catalytic efficiency. Also catalyzes the epimerization of mannose 6-phosphate to glucose 6- phosphate but the rate of epimerization reaction is 20-fold lower than that of isomerization reaction.,,,,,,,GO:0097367; GO:0004347; GO:0004476,GO:0004347; GO:0004476,GO:0004347; GO:0004476,GO:0004347; GO:0004476,GO:0004347; GO:0005975,GO:0004347; GO:0004476,0.8316,0.8316,0.8316,0.5774,0.8316,5,0.7808,0.4675,no
DMDC_ROSNI,A3SI50,ESM2Text,Bacteria,591,"Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton, by mediating the conversion of 3-(methylthio)propanoyl- CoA (MMPA-CoA) to 3-(methylthio)acryloyl-CoA (MTA-CoA).","Involved in the assimilation of dimethylsulfoniopropionate (DMSP), an important class of sulfur-containing polyketide antibiotics. Catalyzes the desaturation of the C3-S-CoA to yield acetyl-CoA and methacrylate.",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0050660; GO:0016627,,,,,,,,,,,0,,0.2788,no
DMDC_ROSNI,A3SI50,Prot2Text,Bacteria,591,"Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton, by mediating the conversion of 3-(methylthio)propanoyl- CoA (MMPA-CoA) to 3-(methylthio)acryloyl-CoA (MTA-CoA).",Involved in cholesterol degradation. Catalyzes the dehydrogenation of 5OH-HIP-CoA to 5OH-HIPE-CoA.,Maybe,Maybe,Maybe,No,No,not-Yes,GO:0050660; GO:0016627,GO:0016491,,GO:0003995,GO:0016491,GO:0003995,0.5847,,0.5115,0.5847,0.5115,4,0.5481,0.2788,no
DMDC_ROSNI,A3SI50,ProtT3,Bacteria,591,"Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton, by mediating the conversion of 3-(methylthio)propanoyl- CoA (MMPA-CoA) to 3-(methylthio)acryloyl-CoA (MTA-CoA).",Belongs to the acyl-CoA dehydrogenase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0050660; GO:0016627,GO:0003995,GO:0003995,GO:0003995,GO:0003995,GO:0003995,0.5115,0.5115,0.5115,0.5115,0.5115,5,0.5115,0.2788,no
DMDC_ROSNI,A3SI50,ProtTale,Bacteria,591,"Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton, by mediating the conversion of 3-(methylthio)propanoyl- CoA (MMPA-CoA) to 3-(methylthio)acryloyl-CoA (MTA-CoA).","Acyl-CoA dehydrogenase that catalyzes the dehydrogenation of 3-hydroxybutyryl-CoA to butyryl-CoA. Is also able to catalyze the dehydrogenation of butyryl-CoA, propionyl-CoA and isovaleryl-CoA, but with lower efficiency. Catalyzes the dehydrogenation of short-chain acyl-CoAs with decreasing efficiency in the following order: 3-hydroxybutyryl-CoA > butyryl-CoA > propionyl-CoA > isovaleryl-CoA > valeryl-CoA > acetoacetyl-CoA = acetyl-CoA",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0050660; GO:0016627,GO:0003995,GO:0003995,GO:0003995,GO:0003995,GO:0003995,0.5115,0.5115,0.5115,0.5115,0.5115,5,0.5115,0.2788,no
DMDC_ROSNI,A3SI50,Protein2Text,Bacteria,591,"Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton, by mediating the conversion of 3-(methylthio)propanoyl- CoA (MMPA-CoA) to 3-(methylthio)acryloyl-CoA (MTA-CoA).","The molecular function of this protein is as a catalytic enzyme, specifically a short-chain specific acyl-CoA dehydrogenase that catalyzes the first step in the beta-oxidation of fatty acids. It is involved in the breakdown of fatty acids to produce energy.",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0050660; GO:0016627,GO:0003995,GO:0003995,GO:0003995,GO:0003995,GO:0003995,0.5115,0.5115,0.5115,0.5115,0.5115,5,0.5115,0.2788,no
DMDC_ROSNI,A3SI50,Reference,Bacteria,591,"Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton, by mediating the conversion of 3-(methylthio)propanoyl- CoA (MMPA-CoA) to 3-(methylthio)acryloyl-CoA (MTA-CoA).","Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton, by mediating the conversion of 3-(methylthio)propanoyl- CoA (MMPA-CoA) to 3-(methylthio)acryloyl-CoA (MTA-CoA).",,,,,,,GO:0050660; GO:0016627,GO:0003995,GO:0003995,GO:0003995,GO:0016491,GO:0016491,0.5115,0.5115,0.5115,0.5847,0.5847,5,0.5408,0.2788,no
CPSKS_PHYPA,A5A8G0,ESM2Text,Eukaryota,881,"Bifunctional copalyl diphosphate/kaurene synthase involved in the biosynthesis of labdane-related diterpenoids (LRDs) natural products such as ent-beyerene, an antimicrobial compound. Supports the conversion of geranylgeranyl diphosphate (GGPP) to ent-copalyl diphosphate (ent-CDP). Also catalyzes the subsequent cyclization of ent-CDP into many diterpenes, including ent-kaur-16-ene as the major product, and ent-beyerene, ent-sandaracopimaradiene, ent-kaur-15-ene (ent- isokaurene) and 16-hydroxy-ent-kaurene (ent-16-alpha-hydroxy-kaurene) as minor products.","Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities. Catalyzes the conversion of (2E,6E,10E)-geranylgeranyl diphosphate (GGPP) to (+)-copalyl diphosphate ((+)-CPP).",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0009905; GO:0034281; GO:0009899; GO:0034280; GO:0000287; GO:0010333,,GO:0010333,GO:0010333,GO:0010333,GO:0010333,,0.6828,0.6828,0.6828,0.6828,4,0.6828,0.1576,no
CPSKS_PHYPA,A5A8G0,Prot2Text,Eukaryota,881,"Bifunctional copalyl diphosphate/kaurene synthase involved in the biosynthesis of labdane-related diterpenoids (LRDs) natural products such as ent-beyerene, an antimicrobial compound. Supports the conversion of geranylgeranyl diphosphate (GGPP) to ent-copalyl diphosphate (ent-CDP). Also catalyzes the subsequent cyclization of ent-CDP into many diterpenes, including ent-kaur-16-ene as the major product, and ent-beyerene, ent-sandaracopimaradiene, ent-kaur-15-ene (ent- isokaurene) and 16-hydroxy-ent-kaurene (ent-16-alpha-hydroxy-kaurene) as minor products.","Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities. Catalyzes the conversion of (2E,6E,10E)-geranylgeranyl diphosphate (GGPP) to ent-copalyl diphosphate (ent-CPP).",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0009905; GO:0034281; GO:0009899; GO:0034280; GO:0000287; GO:0010333,GO:0009905,,GO:0009905,GO:0009905,GO:0009905,0.4251,,0.4251,0.4251,0.4251,4,0.4251,0.1576,no
CPSKS_PHYPA,A5A8G0,ProtT3,Eukaryota,881,"Bifunctional copalyl diphosphate/kaurene synthase involved in the biosynthesis of labdane-related diterpenoids (LRDs) natural products such as ent-beyerene, an antimicrobial compound. Supports the conversion of geranylgeranyl diphosphate (GGPP) to ent-copalyl diphosphate (ent-CDP). Also catalyzes the subsequent cyclization of ent-CDP into many diterpenes, including ent-kaur-16-ene as the major product, and ent-beyerene, ent-sandaracopimaradiene, ent-kaur-15-ene (ent- isokaurene) and 16-hydroxy-ent-kaurene (ent-16-alpha-hydroxy-kaurene) as minor products.","Involved in defensive oleoresin formation in conifers in response to insect attack or other injury. Involved in diterpene (C20) olefins biosynthesis. Catalyzes the conversion of geranylgeranyl diphosphate (GGPP) to ent-copalyl diphosphate (ent-CPP). Plastid, chloroplast. Belongs to the terpene synthase family. Tpsd subfamily",Yes,Yes,Yes,Yes,Yes,Yes,GO:0009905; GO:0034281; GO:0009899; GO:0034280; GO:0000287; GO:0010333,GO:0010333,GO:0009905,GO:0010333,GO:0009905,GO:0010333,0.6828,0.4251,0.6828,0.4251,0.6828,5,0.5797,0.1576,no
CPSKS_PHYPA,A5A8G0,ProtTale,Eukaryota,881,"Bifunctional copalyl diphosphate/kaurene synthase involved in the biosynthesis of labdane-related diterpenoids (LRDs) natural products such as ent-beyerene, an antimicrobial compound. Supports the conversion of geranylgeranyl diphosphate (GGPP) to ent-copalyl diphosphate (ent-CDP). Also catalyzes the subsequent cyclization of ent-CDP into many diterpenes, including ent-kaur-16-ene as the major product, and ent-beyerene, ent-sandaracopimaradiene, ent-kaur-15-ene (ent- isokaurene) and 16-hydroxy-ent-kaurene (ent-16-alpha-hydroxy-kaurene) as minor products.","Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as miltiradiene, miltiradien-10-ol, miltiradien-10-yl acetate, miltiradien-10-ol acetate, miltiradiene and miltiradien-10-ol acetate, which exhibit a range of biological activities including antimicrobial (Probable). Miltiradiene is probably converted to miltiradien-10-ol and miltiradien-10-yl acetate by a cytochrome P450 monooxygenase (Probable",Yes,Maybe,Yes,Yes,Maybe,Yes,GO:0009905; GO:0034281; GO:0009899; GO:0034280; GO:0000287; GO:0010333,,,GO:0010333,,,,,0.6828,,,1,0.6828,0.1576,no
CPSKS_PHYPA,A5A8G0,Protein2Text,Eukaryota,881,"Bifunctional copalyl diphosphate/kaurene synthase involved in the biosynthesis of labdane-related diterpenoids (LRDs) natural products such as ent-beyerene, an antimicrobial compound. Supports the conversion of geranylgeranyl diphosphate (GGPP) to ent-copalyl diphosphate (ent-CDP). Also catalyzes the subsequent cyclization of ent-CDP into many diterpenes, including ent-kaur-16-ene as the major product, and ent-beyerene, ent-sandaracopimaradiene, ent-kaur-15-ene (ent- isokaurene) and 16-hydroxy-ent-kaurene (ent-16-alpha-hydroxy-kaurene) as minor products.","The molecular function of this protein is a terpene synthase, specifically involved in the biosynthesis of terpenes. It catalyzes the conversion of geranylgeranyl diphosphate (GGPP) into a specific terpene product. Terpene synthases are enzymes that play a crucial role in the biosynthesis of terpenes, a diverse group of natural products with various biological activities. In this case, the protein is likely involved in the biosynthesis of a specific terpene product, which is not specified.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0009905; GO:0034281; GO:0009899; GO:0034280; GO:0000287; GO:0010333,GO:0010333,GO:0010333,GO:0010333,GO:0010333,GO:0010334,0.6828,0.6828,0.6828,0.6828,0.5912,5,0.6645,0.1576,no
CPSKS_PHYPA,A5A8G0,Reference,Eukaryota,881,"Bifunctional copalyl diphosphate/kaurene synthase involved in the biosynthesis of labdane-related diterpenoids (LRDs) natural products such as ent-beyerene, an antimicrobial compound. Supports the conversion of geranylgeranyl diphosphate (GGPP) to ent-copalyl diphosphate (ent-CDP). Also catalyzes the subsequent cyclization of ent-CDP into many diterpenes, including ent-kaur-16-ene as the major product, and ent-beyerene, ent-sandaracopimaradiene, ent-kaur-15-ene (ent- isokaurene) and 16-hydroxy-ent-kaurene (ent-16-alpha-hydroxy-kaurene) as minor products.","Bifunctional copalyl diphosphate/kaurene synthase involved in the biosynthesis of labdane-related diterpenoids (LRDs) natural products such as ent-beyerene, an antimicrobial compound. Supports the conversion of geranylgeranyl diphosphate (GGPP) to ent-copalyl diphosphate (ent-CDP). Also catalyzes the subsequent cyclization of ent-CDP into many diterpenes, including ent-kaur-16-ene as the major product, and ent-beyerene, ent-sandaracopimaradiene, ent-kaur-15-ene (ent- isokaurene) and 16-hydroxy-ent-kaurene (ent-16-alpha-hydroxy-kaurene) as minor products.",,,,,,,GO:0009905; GO:0034281; GO:0009899; GO:0034280; GO:0000287; GO:0010333,GO:0050551; GO:0010060,GO:0010333,,GO:0016829; GO:0010333,GO:0016829; GO:0010436,0.5173,0.6828,,0.7022,0.4557,4,0.5895,0.1576,no
E2AK3_BOVIN,A5D791,ESM2Text,Eukaryota,1115,"Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to various stress, such as unfolded protein response (UPR). Key effector of the integrated stress response (ISR) to unfolded proteins: EIF2AK3/PERK specifically recognizes and binds misfolded proteins, leading to its activation and EIF2S1/eIF-2-alpha phosphorylation. EIF2S1/eIF-2- alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activators ATF4 and QRICH1, and hence allowing ATF4- and QRICH1-mediated reprogramming. The EIF2AK3/PERK-mediated unfolded protein response increases mitochondrial oxidative phosphorylation by promoting ATF4-mediated expression of COX7A2L/SCAF1, thereby increasing formation of respiratory chain supercomplexes. In contrast to most subcellular compartments, mitochondria are protected from the EIF2AK3/PERK-mediated unfolded protein response due to EIF2AK3/PERK inhibition by ATAD3A at mitochondria-endoplasmic reticulum contact sites. In addition to EIF2S1/eIF-2-alpha, also phosphorylates NFE2L2/NRF2 in response to stress, promoting release of NFE2L2/NRF2 from the BCR(KEAP1) complex, leading to nuclear accumulation and activation of NFE2L2/NRF2. Serves as a critical effector of unfolded protein response (UPR)-induced G1 growth arrest due to the loss of cyclin-D1 (CCND1). Involved in control of mitochondrial morphology and function.",Involved in the development of the nervous system. It is a receptor for the peptide alpha subunit of GAS1. May have a role in axon guidance.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004694; GO:0042802; GO:0051787; GO:0004715; GO:0019903; GO:0004713,,,,,,,,,,,0,,0.6877,yes
E2AK3_BOVIN,A5D791,Prot2Text,Eukaryota,1115,"Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to various stress, such as unfolded protein response (UPR). Key effector of the integrated stress response (ISR) to unfolded proteins: EIF2AK3/PERK specifically recognizes and binds misfolded proteins, leading to its activation and EIF2S1/eIF-2-alpha phosphorylation. EIF2S1/eIF-2- alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activators ATF4 and QRICH1, and hence allowing ATF4- and QRICH1-mediated reprogramming. The EIF2AK3/PERK-mediated unfolded protein response increases mitochondrial oxidative phosphorylation by promoting ATF4-mediated expression of COX7A2L/SCAF1, thereby increasing formation of respiratory chain supercomplexes. In contrast to most subcellular compartments, mitochondria are protected from the EIF2AK3/PERK-mediated unfolded protein response due to EIF2AK3/PERK inhibition by ATAD3A at mitochondria-endoplasmic reticulum contact sites. In addition to EIF2S1/eIF-2-alpha, also phosphorylates NFE2L2/NRF2 in response to stress, promoting release of NFE2L2/NRF2 from the BCR(KEAP1) complex, leading to nuclear accumulation and activation of NFE2L2/NRF2. Serves as a critical effector of unfolded protein response (UPR)-induced G1 growth arrest due to the loss of cyclin-D1 (CCND1). Involved in control of mitochondrial morphology and function.","Serine/threonine-protein kinase which phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha), leading to its inactivation and thus to a rapid reduction of translational initiation and repression of global protein synthesis. By reducing EIF2S1/eIF-2-alpha, negatively regulates the initiation of protein synthesis and hence the rate of protein synthesis. Negative regulator of amino acid starvation-induced autophagy.",Yes,Yes,Yes,Yes,No,Yes,GO:0005524; GO:0004694; GO:0042802; GO:0051787; GO:0004715; GO:0019903; GO:0004713,GO:0004694,GO:0004694,GO:0004694,GO:0004694,GO:0004694,0.467,0.467,0.467,0.467,0.467,5,0.467,0.6877,yes
E2AK3_BOVIN,A5D791,ProtT3,Eukaryota,1115,"Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to various stress, such as unfolded protein response (UPR). Key effector of the integrated stress response (ISR) to unfolded proteins: EIF2AK3/PERK specifically recognizes and binds misfolded proteins, leading to its activation and EIF2S1/eIF-2-alpha phosphorylation. EIF2S1/eIF-2- alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activators ATF4 and QRICH1, and hence allowing ATF4- and QRICH1-mediated reprogramming. The EIF2AK3/PERK-mediated unfolded protein response increases mitochondrial oxidative phosphorylation by promoting ATF4-mediated expression of COX7A2L/SCAF1, thereby increasing formation of respiratory chain supercomplexes. In contrast to most subcellular compartments, mitochondria are protected from the EIF2AK3/PERK-mediated unfolded protein response due to EIF2AK3/PERK inhibition by ATAD3A at mitochondria-endoplasmic reticulum contact sites. In addition to EIF2S1/eIF-2-alpha, also phosphorylates NFE2L2/NRF2 in response to stress, promoting release of NFE2L2/NRF2 from the BCR(KEAP1) complex, leading to nuclear accumulation and activation of NFE2L2/NRF2. Serves as a critical effector of unfolded protein response (UPR)-induced G1 growth arrest due to the loss of cyclin-D1 (CCND1). Involved in control of mitochondrial morphology and function.",Endoplasmic reticulum membrane; Single-pass membrane protein. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0004694; GO:0042802; GO:0051787; GO:0004715; GO:0019903; GO:0004713,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,0.6489,0.6489,0.6489,0.6489,0.4668,5,0.6125,0.6877,yes
E2AK3_BOVIN,A5D791,ProtTale,Eukaryota,1115,"Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to various stress, such as unfolded protein response (UPR). Key effector of the integrated stress response (ISR) to unfolded proteins: EIF2AK3/PERK specifically recognizes and binds misfolded proteins, leading to its activation and EIF2S1/eIF-2-alpha phosphorylation. EIF2S1/eIF-2- alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activators ATF4 and QRICH1, and hence allowing ATF4- and QRICH1-mediated reprogramming. The EIF2AK3/PERK-mediated unfolded protein response increases mitochondrial oxidative phosphorylation by promoting ATF4-mediated expression of COX7A2L/SCAF1, thereby increasing formation of respiratory chain supercomplexes. In contrast to most subcellular compartments, mitochondria are protected from the EIF2AK3/PERK-mediated unfolded protein response due to EIF2AK3/PERK inhibition by ATAD3A at mitochondria-endoplasmic reticulum contact sites. In addition to EIF2S1/eIF-2-alpha, also phosphorylates NFE2L2/NRF2 in response to stress, promoting release of NFE2L2/NRF2 from the BCR(KEAP1) complex, leading to nuclear accumulation and activation of NFE2L2/NRF2. Serves as a critical effector of unfolded protein response (UPR)-induced G1 growth arrest due to the loss of cyclin-D1 (CCND1). Involved in control of mitochondrial morphology and function.","Acts as a serine/threonine-protein kinase which promotes the degradation of its substrates via its association with the E3 ubiquitin-protein ligase NEDD8. Mediates the polyubiquitination and subsequent proteasomal degradation of target proteins such as CTNNB1 (beta-catenin), CTNNA2 (alpha-catenin), CTNNA3 (gamma-catenin), CTNNA4 (delta-catenin), CTNNA5 (epsilon-catenin), CTNNA6 (zeta-catenin), CTNNA7 (epsilon-catenin), CTNNA8",Maybe,No,No,No,No,not-Yes,GO:0005524; GO:0004694; GO:0042802; GO:0051787; GO:0004715; GO:0019903; GO:0004713,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,0.6489,0.6489,0.6489,0.4668,0.6489,5,0.6125,0.6877,yes
E2AK3_BOVIN,A5D791,Protein2Text,Eukaryota,1115,"Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to various stress, such as unfolded protein response (UPR). Key effector of the integrated stress response (ISR) to unfolded proteins: EIF2AK3/PERK specifically recognizes and binds misfolded proteins, leading to its activation and EIF2S1/eIF-2-alpha phosphorylation. EIF2S1/eIF-2- alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activators ATF4 and QRICH1, and hence allowing ATF4- and QRICH1-mediated reprogramming. The EIF2AK3/PERK-mediated unfolded protein response increases mitochondrial oxidative phosphorylation by promoting ATF4-mediated expression of COX7A2L/SCAF1, thereby increasing formation of respiratory chain supercomplexes. In contrast to most subcellular compartments, mitochondria are protected from the EIF2AK3/PERK-mediated unfolded protein response due to EIF2AK3/PERK inhibition by ATAD3A at mitochondria-endoplasmic reticulum contact sites. In addition to EIF2S1/eIF-2-alpha, also phosphorylates NFE2L2/NRF2 in response to stress, promoting release of NFE2L2/NRF2 from the BCR(KEAP1) complex, leading to nuclear accumulation and activation of NFE2L2/NRF2. Serves as a critical effector of unfolded protein response (UPR)-induced G1 growth arrest due to the loss of cyclin-D1 (CCND1). Involved in control of mitochondrial morphology and function.","This protein is a component of the integrated stress response (ISR) pathway, which is a cellular response to stress that involves the activation of the protein kinase PKR (protein kinase R). The molecular function of this protein is to recognize and bind to the 5'-end of the cap structure of eukaryotic mRNA, specifically 7-methylguanosine (m7G)-containing mRNA, and recruit the eukaryotic initiation factor 2 alpha (eIF2α) kinase PKR to the mRNA. This interaction is essential for the activation of the integrated stress response (ISR) pathway, which is a cellular response to stress that involves the activation of the protein kinase PKR. 

PKR activation leads to the phosphorylation of eIF2α, which inhibits protein synthesis and triggers the expression of genes that promote cell survival under stress conditions. The protein is also involved in the recognition of viral mRNA and the activation of the PKR pathway, which inhibits viral replication.

In summary, the molecular function of this protein is to recognize and bind to the cap structure of eukaryotic mRNA and recruit PKR to the mRNA, leading to the activation of the integrated stress response (ISR) pathway.",No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004694; GO:0042802; GO:0051787; GO:0004715; GO:0019903; GO:0004713,,,,,,,,,,,0,,0.6877,yes
E2AK3_BOVIN,A5D791,Reference,Eukaryota,1115,"Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to various stress, such as unfolded protein response (UPR). Key effector of the integrated stress response (ISR) to unfolded proteins: EIF2AK3/PERK specifically recognizes and binds misfolded proteins, leading to its activation and EIF2S1/eIF-2-alpha phosphorylation. EIF2S1/eIF-2- alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activators ATF4 and QRICH1, and hence allowing ATF4- and QRICH1-mediated reprogramming. The EIF2AK3/PERK-mediated unfolded protein response increases mitochondrial oxidative phosphorylation by promoting ATF4-mediated expression of COX7A2L/SCAF1, thereby increasing formation of respiratory chain supercomplexes. In contrast to most subcellular compartments, mitochondria are protected from the EIF2AK3/PERK-mediated unfolded protein response due to EIF2AK3/PERK inhibition by ATAD3A at mitochondria-endoplasmic reticulum contact sites. In addition to EIF2S1/eIF-2-alpha, also phosphorylates NFE2L2/NRF2 in response to stress, promoting release of NFE2L2/NRF2 from the BCR(KEAP1) complex, leading to nuclear accumulation and activation of NFE2L2/NRF2. Serves as a critical effector of unfolded protein response (UPR)-induced G1 growth arrest due to the loss of cyclin-D1 (CCND1). Involved in control of mitochondrial morphology and function.","Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to various stress, such as unfolded protein response (UPR). Key effector of the integrated stress response (ISR) to unfolded proteins: EIF2AK3/PERK specifically recognizes and binds misfolded proteins, leading to its activation and EIF2S1/eIF-2-alpha phosphorylation. EIF2S1/eIF-2- alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activators ATF4 and QRICH1, and hence allowing ATF4- and QRICH1-mediated reprogramming. The EIF2AK3/PERK-mediated unfolded protein response increases mitochondrial oxidative phosphorylation by promoting ATF4-mediated expression of COX7A2L/SCAF1, thereby increasing formation of respiratory chain supercomplexes. In contrast to most subcellular compartments, mitochondria are protected from the EIF2AK3/PERK-mediated unfolded protein response due to EIF2AK3/PERK inhibition by ATAD3A at mitochondria-endoplasmic reticulum contact sites. In addition to EIF2S1/eIF-2-alpha, also phosphorylates NFE2L2/NRF2 in response to stress, promoting release of NFE2L2/NRF2 from the BCR(KEAP1) complex, leading to nuclear accumulation and activation of NFE2L2/NRF2. Serves as a critical effector of unfolded protein response (UPR)-induced G1 growth arrest due to the loss of cyclin-D1 (CCND1). Involved in control of mitochondrial morphology and function.",,,,,,,GO:0005524; GO:0004694; GO:0042802; GO:0051787; GO:0004715; GO:0019903; GO:0004713,GO:0004694; GO:0004674; GO:0005524,GO:0004694; GO:0004674; GO:0005524,GO:0004694; GO:0004674; GO:0005524,GO:0004694; GO:0005524,GO:0004694; GO:0005524,0.6931,0.6931,0.6931,0.6524,0.6524,5,0.6768,0.6877,yes
RPB2_BOVIN,A5PJW8,ESM2Text,Eukaryota,1174,"Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates. Pol II-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol II pre-initiation complex (PIC) is recruited to DNA promoters, with focused-type promoters containing either the initiator (Inr) element, or the TATA-box found in cell-type specific genes and dispersed-type promoters that often contain hypomethylated CpG islands usually found in housekeeping genes. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA. Forms Pol II active center together with the largest subunit POLR2A/RPB1. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg(2+)-coordinating DxDGD motif, and POLR2B/RPB2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. The reversible pyrophosphorolysis can occur at high pyrophosphate concentrations. Can proofread the nascent RNA transcript by means of a 3' -> 5' exonuclease activity. If a ribonucleotide is mis-incorporated, backtracks along the template DNA and cleaves the phosphodiester bond releasing the mis-incorporated 5'- ribonucleotide.","As part of the telomerase ribonucleoprotein (RNP), a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends. The RNA is catalytic, but its KM for pre-tRNA is 170-fold decreased in the presence of the 3'-hydroxyl group and even at low concentrations, the protein does not cleave pre-tRNA. The protein is also able to catalyze the cleavage of 5'-ends.",No,No,No,No,Yes,not-Yes,GO:0003682; GO:0003677; GO:0003899; GO:0071667; GO:0016787; GO:0032549; GO:0003968; GO:0008270,GO:0004526,GO:0004526,GO:0004526,GO:0004526,,0.1655,0.1655,0.1655,0.1655,,4,0.1655,0.5664,yes
RPB2_BOVIN,A5PJW8,Prot2Text,Eukaryota,1174,"Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates. Pol II-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol II pre-initiation complex (PIC) is recruited to DNA promoters, with focused-type promoters containing either the initiator (Inr) element, or the TATA-box found in cell-type specific genes and dispersed-type promoters that often contain hypomethylated CpG islands usually found in housekeeping genes. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA. Forms Pol II active center together with the largest subunit POLR2A/RPB1. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg(2+)-coordinating DxDGD motif, and POLR2B/RPB2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. The reversible pyrophosphorolysis can occur at high pyrophosphate concentrations. Can proofread the nascent RNA transcript by means of a 3' -> 5' exonuclease activity. If a ribonucleotide is mis-incorporated, backtracks along the template DNA and cleaves the phosphodiester bond releasing the mis-incorporated 5'- ribonucleotide.",Essential for the completion of the three rounds of mitosis in female megaspores required for the development of mature gametophytes.,Vague,Vague,Vague,No,No,not-Yes,GO:0003682; GO:0003677; GO:0003899; GO:0071667; GO:0016787; GO:0032549; GO:0003968; GO:0008270,,,,,,,,,,,0,,0.5664,yes
RPB2_BOVIN,A5PJW8,ProtT3,Eukaryota,1174,"Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates. Pol II-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol II pre-initiation complex (PIC) is recruited to DNA promoters, with focused-type promoters containing either the initiator (Inr) element, or the TATA-box found in cell-type specific genes and dispersed-type promoters that often contain hypomethylated CpG islands usually found in housekeeping genes. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA. Forms Pol II active center together with the largest subunit POLR2A/RPB1. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg(2+)-coordinating DxDGD motif, and POLR2B/RPB2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. The reversible pyrophosphorolysis can occur at high pyrophosphate concentrations. Can proofread the nascent RNA transcript by means of a 3' -> 5' exonuclease activity. If a ribonucleotide is mis-incorporated, backtracks along the template DNA and cleaves the phosphodiester bond releasing the mis-incorporated 5'- ribonucleotide.","RNA-dependent RNA polymerase which is responsible for replication and transcription of virus RNA segments. The transcription of viral mRNAs occurs by a unique mechanism called cap-snatching. 5' methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides by PA. In turn, these short capped RNAs are used as primers by PB1 for transcription of viral mRNAs. During virus replication, PB1 initiates RNA synthesis and copy vRNA into complementary RNA (cRNA) which in turn serves as a template for the production of more vRNAs. Host nucleus Host cytoplasm. SIMI",No,No,No,No,No,not-Yes,GO:0003682; GO:0003677; GO:0003899; GO:0071667; GO:0016787; GO:0032549; GO:0003968; GO:0008270,GO:0003968,GO:0003968,GO:0003968,GO:0003968,GO:0003968,0.389,0.389,0.389,0.389,0.389,5,0.389,0.5664,yes
RPB2_BOVIN,A5PJW8,ProtTale,Eukaryota,1174,"Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates. Pol II-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol II pre-initiation complex (PIC) is recruited to DNA promoters, with focused-type promoters containing either the initiator (Inr) element, or the TATA-box found in cell-type specific genes and dispersed-type promoters that often contain hypomethylated CpG islands usually found in housekeeping genes. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA. Forms Pol II active center together with the largest subunit POLR2A/RPB1. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg(2+)-coordinating DxDGD motif, and POLR2B/RPB2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. The reversible pyrophosphorolysis can occur at high pyrophosphate concentrations. Can proofread the nascent RNA transcript by means of a 3' -> 5' exonuclease activity. If a ribonucleotide is mis-incorporated, backtracks along the template DNA and cleaves the phosphodiester bond releasing the mis-incorporated 5'- ribonucleotide.","DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol III is composed of mobile elements and RPB1 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0003682; GO:0003677; GO:0003899; GO:0071667; GO:0016787; GO:0032549; GO:0003968; GO:0008270,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.389,0.389,0.389,0.389,0.389,5,0.389,0.5664,yes
RPB2_BOVIN,A5PJW8,Protein2Text,Eukaryota,1174,"Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates. Pol II-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol II pre-initiation complex (PIC) is recruited to DNA promoters, with focused-type promoters containing either the initiator (Inr) element, or the TATA-box found in cell-type specific genes and dispersed-type promoters that often contain hypomethylated CpG islands usually found in housekeeping genes. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA. Forms Pol II active center together with the largest subunit POLR2A/RPB1. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg(2+)-coordinating DxDGD motif, and POLR2B/RPB2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. The reversible pyrophosphorolysis can occur at high pyrophosphate concentrations. Can proofread the nascent RNA transcript by means of a 3' -> 5' exonuclease activity. If a ribonucleotide is mis-incorporated, backtracks along the template DNA and cleaves the phosphodiester bond releasing the mis-incorporated 5'- ribonucleotide.","The molecular function of this protein is DNA-dependent RNA polymerase catalytic subunit. It is a component of the RNA polymerase II (RNAPII) complex, which is responsible for transcribing genes into RNA. Specifically, it is the catalytic subunit that uses ATP and UTP to synthesize RNA from a DNA template.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0003682; GO:0003677; GO:0003899; GO:0071667; GO:0016787; GO:0032549; GO:0003968; GO:0008270,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.389,0.389,0.389,0.389,0.389,5,0.389,0.5664,yes
RPB2_BOVIN,A5PJW8,Reference,Eukaryota,1174,"Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates. Pol II-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol II pre-initiation complex (PIC) is recruited to DNA promoters, with focused-type promoters containing either the initiator (Inr) element, or the TATA-box found in cell-type specific genes and dispersed-type promoters that often contain hypomethylated CpG islands usually found in housekeeping genes. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA. Forms Pol II active center together with the largest subunit POLR2A/RPB1. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg(2+)-coordinating DxDGD motif, and POLR2B/RPB2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. The reversible pyrophosphorolysis can occur at high pyrophosphate concentrations. Can proofread the nascent RNA transcript by means of a 3' -> 5' exonuclease activity. If a ribonucleotide is mis-incorporated, backtracks along the template DNA and cleaves the phosphodiester bond releasing the mis-incorporated 5'- ribonucleotide.","Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates. Pol II-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol II pre-initiation complex (PIC) is recruited to DNA promoters, with focused-type promoters containing either the initiator (Inr) element, or the TATA-box found in cell-type specific genes and dispersed-type promoters that often contain hypomethylated CpG islands usually found in housekeeping genes. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA. Forms Pol II active center together with the largest subunit POLR2A/RPB1. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg(2+)-coordinating DxDGD motif, and POLR2B/RPB2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. The reversible pyrophosphorolysis can occur at high pyrophosphate concentrations. Can proofread the nascent RNA transcript by means of a 3' -> 5' exonuclease activity. If a ribonucleotide is mis-incorporated, backtracks along the template DNA and cleaves the phosphodiester bond releasing the mis-incorporated 5'- ribonucleotide.",,,,,,,GO:0003682; GO:0003677; GO:0003899; GO:0071667; GO:0016787; GO:0032549; GO:0003968; GO:0008270,GO:0003899; GO:0003723,GO:0003899; GO:0000287; GO:0004527,GO:0003899; GO:0004527,GO:0003899; GO:0003723,GO:0003899; GO:0003723,0.6044,0.5757,0.4453,0.6044,0.6044,5,0.5668,0.5664,yes
DING_MYCTA,A5U229,ESM2Text,Bacteria,664,"A structure-dependent 5'-3' DNA helicase that unwinds a number of substrates that resemble intermediates in DNA repair, recombination and replication. Requires 15-25 nucleotides of 3'- overhang single-stranded (ss)DNA for optimal activity. Unwinds 3'-flap and forked duplex DNA. Unwinds both lead and lagging strands in replication fork structures (may have branch migration activity). Has weak Holliday junction unwinding activity. In vitro at high concentrations also unwinds in a 3'-5' direction. Binds best to ssDNA, followed by forked duplex, 3'- and 5'-overhang and 3-strand junction DNA; binds poorly if at all to blunt end double-stranded (ds)DNA substrates. Translocates on ssDNA with 5'-3' polarity.",ATP-dependent 5'-3' DNA helicase involved in nucleotide excision repair (NER) of DNA.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0051539; GO:0043139; GO:0005524; GO:0003677; GO:0016818; GO:0046872,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0004003,GO:0003678,GO:0004003,0.5871,0.5871,0.3362,0.3362,0.3362,5,0.4366,0.5655,yes
DING_MYCTA,A5U229,Prot2Text,Bacteria,664,"A structure-dependent 5'-3' DNA helicase that unwinds a number of substrates that resemble intermediates in DNA repair, recombination and replication. Requires 15-25 nucleotides of 3'- overhang single-stranded (ss)DNA for optimal activity. Unwinds 3'-flap and forked duplex DNA. Unwinds both lead and lagging strands in replication fork structures (may have branch migration activity). Has weak Holliday junction unwinding activity. In vitro at high concentrations also unwinds in a 3'-5' direction. Binds best to ssDNA, followed by forked duplex, 3'- and 5'-overhang and 3-strand junction DNA; binds poorly if at all to blunt end double-stranded (ds)DNA substrates. Translocates on ssDNA with 5'-3' polarity.",DNA-dependent ATPase and 5'-3' DNA helicase.,Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0051539; GO:0043139; GO:0005524; GO:0003677; GO:0016818; GO:0046872,GO:0003678; GO:0005524; GO:0008094,GO:0003678; GO:0008094,GO:0003678; GO:0005524,GO:0003678; GO:0005524; GO:0004003,GO:0003678; GO:0008094,0.6051,0.4076,0.5871,0.6249,0.4076,5,0.5265,0.5655,yes
DING_MYCTA,A5U229,ProtT3,Bacteria,664,"A structure-dependent 5'-3' DNA helicase that unwinds a number of substrates that resemble intermediates in DNA repair, recombination and replication. Requires 15-25 nucleotides of 3'- overhang single-stranded (ss)DNA for optimal activity. Unwinds 3'-flap and forked duplex DNA. Unwinds both lead and lagging strands in replication fork structures (may have branch migration activity). Has weak Holliday junction unwinding activity. In vitro at high concentrations also unwinds in a 3'-5' direction. Binds best to ssDNA, followed by forked duplex, 3'- and 5'-overhang and 3-strand junction DNA; binds poorly if at all to blunt end double-stranded (ds)DNA substrates. Translocates on ssDNA with 5'-3' polarity.",DNA-dependent ATPase and 3'-5' DNA helicase. Belongs to the helicase family. DinG subfamily. Type 1 sub- subfamily,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0051539; GO:0043139; GO:0005524; GO:0003677; GO:0016818; GO:0046872,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0008094,0.5871,0.5871,0.5871,0.5871,0.4076,5,0.5512,0.5655,yes
DING_MYCTA,A5U229,ProtTale,Bacteria,664,"A structure-dependent 5'-3' DNA helicase that unwinds a number of substrates that resemble intermediates in DNA repair, recombination and replication. Requires 15-25 nucleotides of 3'- overhang single-stranded (ss)DNA for optimal activity. Unwinds 3'-flap and forked duplex DNA. Unwinds both lead and lagging strands in replication fork structures (may have branch migration activity). Has weak Holliday junction unwinding activity. In vitro at high concentrations also unwinds in a 3'-5' direction. Binds best to ssDNA, followed by forked duplex, 3'- and 5'-overhang and 3-strand junction DNA; binds poorly if at all to blunt end double-stranded (ds)DNA substrates. Translocates on ssDNA with 5'-3' polarity.","DNA-dependent ATPase and 5'-3' DNA helicase. Unwinds D-loops, R-loops, forked DNA and G-quadruplex DNA.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0051539; GO:0043139; GO:0005524; GO:0003677; GO:0016818; GO:0046872,GO:0003678; GO:0005524; GO:0016887,GO:0003678; GO:0016887; GO:0005524,GO:0003678; GO:0016887; GO:0005524,GO:0004003; GO:0005524,GO:0003678; GO:0016887; GO:0005524,0.643,0.643,0.643,0.5871,0.643,5,0.6318,0.5655,yes
DING_MYCTA,A5U229,Protein2Text,Bacteria,664,"A structure-dependent 5'-3' DNA helicase that unwinds a number of substrates that resemble intermediates in DNA repair, recombination and replication. Requires 15-25 nucleotides of 3'- overhang single-stranded (ss)DNA for optimal activity. Unwinds 3'-flap and forked duplex DNA. Unwinds both lead and lagging strands in replication fork structures (may have branch migration activity). Has weak Holliday junction unwinding activity. In vitro at high concentrations also unwinds in a 3'-5' direction. Binds best to ssDNA, followed by forked duplex, 3'- and 5'-overhang and 3-strand junction DNA; binds poorly if at all to blunt end double-stranded (ds)DNA substrates. Translocates on ssDNA with 5'-3' polarity.","The molecular function of this protein is an exonuclease.
It is involved in the degradation of single-stranded DNA and is part of the primosome complex that is required for initiation of DNA replication.
This protein is also a component of the RecBCD nuclease-exonuclease complex, which is involved in DNA repair and recombination.
The RecBCD complex is responsible for the degradation of linear duplex DNA in the presence of RecD, and the degradation of single-stranded DNA in the presence of RecC. 
The RecBCD complex is also required for the initiation of homologous recombination, and for the generation of single-stranded DNA for RecA-mediated homologous recombination. 
The RecBCD complex is required for the degradation of linear duplex DNA in the presence of RecD, and the degradation of single-stranded DNA in the presence of RecC. 
The RecBCD complex is also required for the initiation of homologous recombination, and for the generation of single-stranded DNA for RecA-mediated homologous recombination. 
This protein is also a component of the RecF pathway, which is one of the two major pathways of homologous recombination. 
The RecF pathway is required for homologous recombination in the presence of replication fork arrest. 
This protein is also a component of the RecF pathway, which is one of the two major pathways of homologous recombination. 
The RecF pathway is required for homologous recombination in the presence of replication fork arrest. 
This protein is also a component of the RecF pathway, which is one of the two major pathways of homologous recombination. 
The RecF pathway is required for homologous recombination in the presence of replication fork arrest. 
This protein is also a component of the RecF pathway, which is one of the two major pathways of homologous recombination. 
The RecF pathway is required for homologous recombination in the presence of replication fork arrest.",No,No,No,No,No,not-Yes,GO:0051539; GO:0043139; GO:0005524; GO:0003677; GO:0016818; GO:0046872,GO:0004527,GO:0004527,GO:0004527,GO:0004529,GO:0004527,0.1952,0.1952,0.1952,0.1628,0.1952,5,0.1887,0.5655,yes
DING_MYCTA,A5U229,Reference,Bacteria,664,"A structure-dependent 5'-3' DNA helicase that unwinds a number of substrates that resemble intermediates in DNA repair, recombination and replication. Requires 15-25 nucleotides of 3'- overhang single-stranded (ss)DNA for optimal activity. Unwinds 3'-flap and forked duplex DNA. Unwinds both lead and lagging strands in replication fork structures (may have branch migration activity). Has weak Holliday junction unwinding activity. In vitro at high concentrations also unwinds in a 3'-5' direction. Binds best to ssDNA, followed by forked duplex, 3'- and 5'-overhang and 3-strand junction DNA; binds poorly if at all to blunt end double-stranded (ds)DNA substrates. Translocates on ssDNA with 5'-3' polarity.","A structure-dependent 5'-3' DNA helicase that unwinds a number of substrates that resemble intermediates in DNA repair, recombination and replication. Requires 15-25 nucleotides of 3'- overhang single-stranded (ss)DNA for optimal activity. Unwinds 3'-flap and forked duplex DNA. Unwinds both lead and lagging strands in replication fork structures (may have branch migration activity). Has weak Holliday junction unwinding activity. In vitro at high concentrations also unwinds in a 3'-5' direction. Binds best to ssDNA, followed by forked duplex, 3'- and 5'-overhang and 3-strand junction DNA; binds poorly if at all to blunt end double-stranded (ds)DNA substrates. Translocates on ssDNA with 5'-3' polarity.",,,,,,,GO:0051539; GO:0043139; GO:0005524; GO:0003677; GO:0016818; GO:0046872,GO:0043140; GO:0005524; GO:0003677,GO:0043141; GO:0003697; GO:0005524,GO:0003678; GO:0005524; GO:0003697,GO:0004386; GO:0003678; GO:0005524,GO:0004386; GO:0003677; GO:0005524,0.7164,0.709,0.6942,0.6128,0.7046,5,0.6874,0.5655,yes
CHIP_RAT,A6HD62,ESM2Text,Eukaryota,304,"E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Plays a role in the maintenance of mitochondrial morphology and promotes mitophagic removal of dysfunctional mitochondria; thereby acts as a protector against apoptosis in response to cellular stress. Negatively regulates vascular smooth muscle contraction, via degradation of the transcriptional activator MYOCD and subsequent loss of transcription of genes involved in vascular smooth muscle contraction. Promotes survival and proliferation of cardiac smooth muscle cells via ubiquitination and degradation of FOXO1, resulting in subsequent repression of FOXO1- mediated transcription of pro-apoptotic genes. Ubiquitinates ICER-type isoforms of CREM and targets them for proteasomal degradation, thereby acts as a positive effector of MAPK/ERK-mediated inhibition of apoptosis in cardiomyocytes. Inhibits lipopolysaccharide-induced apoptosis and hypertrophy in cardiomyocytes, via ubiquitination and subsequent proteasomal degradation of NFATC3. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Ubiquitinates CHRNA3 targeting it for endoplasmic reticulum-associated degradation in cortical neurons, as part of the STUB1-VCP-UBXN2A complex. Ubiquitinates and promotes ESR1 proteasomal degradation in response to age-related circulating estradiol (17-beta-estradiol/E2) decline, thereby promotes neuronal apoptosis in response to ischemic reperfusion injury. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base- excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB- degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation. Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation. Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner. Catalyzes monoubiquitination of SIRT6, preventing its degradation by the proteasome. Likely mediates polyubiquitination and down-regulates plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation. Plays a role in the degradation of TP53. Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation. May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation. Ubiquitinates PPARG in macrophages playing a role in M2 macrophages polarization and angiogenesis.","E3 ubiquitin-protein ligase which monoubiquitinates Hsp70 and Hsp90 to form Hsp90-type chaperone and molecular chaperone, respectively, in response to DNA damage. Mediates polyubiquitination of a broad range of substrates. Mediates ubiquitination of histone H1, H3 and H4 histone H3 'Lys-14' (H4K14ub1), with a preference for substrates with double-stranded nucleotides. Mediates monoubiquitination of Hsp70, Hsp90 and Hsp70. Mediates monoubiquitination of a subset of nucleosome component (NBMAL), and monoubiquitination of a subset of Hsp70-containing chromatin. Mediates monoubiquitination of a subset of Hsp70, Hsp90 and Hsp70. Mediates monoubiquitination of a subset of Hsp70, Hsp70 and Hsp90. Ubiquitinates DNA polymerase beta (POLB), and is required for the maintenance of chromosome integrity. Mediates monoubiquitination of a subset of Hsp70, Hsp70 and H",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0019899; GO:0001664; GO:0031072; GO:0030544; GO:0051879; GO:0019900; GO:0051787; GO:0042803; GO:0051087; GO:0070412; GO:0046332; GO:0030911; GO:0061630; GO:0031625; GO:0004842; GO:0034450,GO:0004842,GO:0004842,GO:0004842,GO:0004842,GO:0061630,0.2909,0.2909,0.2909,0.2909,0.2853,5,0.2898,0.8626,yes
CHIP_RAT,A6HD62,Prot2Text,Eukaryota,304,"E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Plays a role in the maintenance of mitochondrial morphology and promotes mitophagic removal of dysfunctional mitochondria; thereby acts as a protector against apoptosis in response to cellular stress. Negatively regulates vascular smooth muscle contraction, via degradation of the transcriptional activator MYOCD and subsequent loss of transcription of genes involved in vascular smooth muscle contraction. Promotes survival and proliferation of cardiac smooth muscle cells via ubiquitination and degradation of FOXO1, resulting in subsequent repression of FOXO1- mediated transcription of pro-apoptotic genes. Ubiquitinates ICER-type isoforms of CREM and targets them for proteasomal degradation, thereby acts as a positive effector of MAPK/ERK-mediated inhibition of apoptosis in cardiomyocytes. Inhibits lipopolysaccharide-induced apoptosis and hypertrophy in cardiomyocytes, via ubiquitination and subsequent proteasomal degradation of NFATC3. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Ubiquitinates CHRNA3 targeting it for endoplasmic reticulum-associated degradation in cortical neurons, as part of the STUB1-VCP-UBXN2A complex. Ubiquitinates and promotes ESR1 proteasomal degradation in response to age-related circulating estradiol (17-beta-estradiol/E2) decline, thereby promotes neuronal apoptosis in response to ischemic reperfusion injury. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base- excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB- degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation. Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation. Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner. Catalyzes monoubiquitination of SIRT6, preventing its degradation by the proteasome. Likely mediates polyubiquitination and down-regulates plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation. Plays a role in the degradation of TP53. Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation. May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation. Ubiquitinates PPARG in macrophages playing a role in M2 macrophages polarization and angiogenesis.","E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates the degradation of short-lived regulatory substrates of ubiquitin-dependent proteasomal degradation. Ubiquitinates the CPEB5-COP1 E3 ubiquitin-protein ligase complex, a CPEB5-associated complex that targets CPEB5 for proteasomal degradation. Targets CPEB5 for proteasomal degradation in a RING-dependent manner and targets it for proteasomal degradation by the 26S proteasome. Targets CPEB5 for proteasomal degradation in a RING-independent manner. Targets COP1 for proteasomal degradation.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0019899; GO:0001664; GO:0031072; GO:0030544; GO:0051879; GO:0019900; GO:0051787; GO:0042803; GO:0051087; GO:0070412; GO:0046332; GO:0030911; GO:0061630; GO:0031625; GO:0004842; GO:0034450,GO:0004842,GO:0061630,GO:0061630,GO:0061630,GO:0004842,0.2909,0.2853,0.2853,0.2853,0.2909,5,0.2875,0.8626,yes
CHIP_RAT,A6HD62,ProtT3,Eukaryota,304,"E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Plays a role in the maintenance of mitochondrial morphology and promotes mitophagic removal of dysfunctional mitochondria; thereby acts as a protector against apoptosis in response to cellular stress. Negatively regulates vascular smooth muscle contraction, via degradation of the transcriptional activator MYOCD and subsequent loss of transcription of genes involved in vascular smooth muscle contraction. Promotes survival and proliferation of cardiac smooth muscle cells via ubiquitination and degradation of FOXO1, resulting in subsequent repression of FOXO1- mediated transcription of pro-apoptotic genes. Ubiquitinates ICER-type isoforms of CREM and targets them for proteasomal degradation, thereby acts as a positive effector of MAPK/ERK-mediated inhibition of apoptosis in cardiomyocytes. Inhibits lipopolysaccharide-induced apoptosis and hypertrophy in cardiomyocytes, via ubiquitination and subsequent proteasomal degradation of NFATC3. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Ubiquitinates CHRNA3 targeting it for endoplasmic reticulum-associated degradation in cortical neurons, as part of the STUB1-VCP-UBXN2A complex. Ubiquitinates and promotes ESR1 proteasomal degradation in response to age-related circulating estradiol (17-beta-estradiol/E2) decline, thereby promotes neuronal apoptosis in response to ischemic reperfusion injury. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base- excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB- degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation. Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation. Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner. Catalyzes monoubiquitination of SIRT6, preventing its degradation by the proteasome. Likely mediates polyubiquitination and down-regulates plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation. Plays a role in the degradation of TP53. Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation. May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation. Ubiquitinates PPARG in macrophages playing a role in M2 macrophages polarization and angiogenesis.",E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Acts as a negative regulator of the unfolded protein response (UPR) (By similarity). Acts as a negative regulator of the unfolded protein response (UPR) (By similarity). Acts as a negative regulator of the unfolded protein response (UPR) (By similarity). Acts as a negative regulator of the unfolded protein response (UPR) (By similarity). Acts as a negative regulator of the unfolded protein response (UPR,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0019899; GO:0001664; GO:0031072; GO:0030544; GO:0051879; GO:0019900; GO:0051787; GO:0042803; GO:0051087; GO:0070412; GO:0046332; GO:0030911; GO:0061630; GO:0031625; GO:0004842; GO:0034450,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.2853,0.2853,0.2853,0.2853,0.2853,5,0.2853,0.8626,yes
CHIP_RAT,A6HD62,ProtTale,Eukaryota,304,"E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Plays a role in the maintenance of mitochondrial morphology and promotes mitophagic removal of dysfunctional mitochondria; thereby acts as a protector against apoptosis in response to cellular stress. Negatively regulates vascular smooth muscle contraction, via degradation of the transcriptional activator MYOCD and subsequent loss of transcription of genes involved in vascular smooth muscle contraction. Promotes survival and proliferation of cardiac smooth muscle cells via ubiquitination and degradation of FOXO1, resulting in subsequent repression of FOXO1- mediated transcription of pro-apoptotic genes. Ubiquitinates ICER-type isoforms of CREM and targets them for proteasomal degradation, thereby acts as a positive effector of MAPK/ERK-mediated inhibition of apoptosis in cardiomyocytes. Inhibits lipopolysaccharide-induced apoptosis and hypertrophy in cardiomyocytes, via ubiquitination and subsequent proteasomal degradation of NFATC3. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Ubiquitinates CHRNA3 targeting it for endoplasmic reticulum-associated degradation in cortical neurons, as part of the STUB1-VCP-UBXN2A complex. Ubiquitinates and promotes ESR1 proteasomal degradation in response to age-related circulating estradiol (17-beta-estradiol/E2) decline, thereby promotes neuronal apoptosis in response to ischemic reperfusion injury. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base- excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB- degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation. Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation. Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner. Catalyzes monoubiquitination of SIRT6, preventing its degradation by the proteasome. Likely mediates polyubiquitination and down-regulates plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation. Plays a role in the degradation of TP53. Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation. May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation. Ubiquitinates PPARG in macrophages playing a role in M2 macrophages polarization and angiogenesis.",Functions as an E3 ubiquitin ligase.,Vague,Yes,Maybe,Vague,Maybe,not-Yes,GO:0019899; GO:0001664; GO:0031072; GO:0030544; GO:0051879; GO:0019900; GO:0051787; GO:0042803; GO:0051087; GO:0070412; GO:0046332; GO:0030911; GO:0061630; GO:0031625; GO:0004842; GO:0034450,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.2853,0.2853,0.2853,0.2853,0.2853,5,0.2853,0.8626,yes
CHIP_RAT,A6HD62,Protein2Text,Eukaryota,304,"E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Plays a role in the maintenance of mitochondrial morphology and promotes mitophagic removal of dysfunctional mitochondria; thereby acts as a protector against apoptosis in response to cellular stress. Negatively regulates vascular smooth muscle contraction, via degradation of the transcriptional activator MYOCD and subsequent loss of transcription of genes involved in vascular smooth muscle contraction. Promotes survival and proliferation of cardiac smooth muscle cells via ubiquitination and degradation of FOXO1, resulting in subsequent repression of FOXO1- mediated transcription of pro-apoptotic genes. Ubiquitinates ICER-type isoforms of CREM and targets them for proteasomal degradation, thereby acts as a positive effector of MAPK/ERK-mediated inhibition of apoptosis in cardiomyocytes. Inhibits lipopolysaccharide-induced apoptosis and hypertrophy in cardiomyocytes, via ubiquitination and subsequent proteasomal degradation of NFATC3. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Ubiquitinates CHRNA3 targeting it for endoplasmic reticulum-associated degradation in cortical neurons, as part of the STUB1-VCP-UBXN2A complex. Ubiquitinates and promotes ESR1 proteasomal degradation in response to age-related circulating estradiol (17-beta-estradiol/E2) decline, thereby promotes neuronal apoptosis in response to ischemic reperfusion injury. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base- excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB- degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation. Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation. Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner. Catalyzes monoubiquitination of SIRT6, preventing its degradation by the proteasome. Likely mediates polyubiquitination and down-regulates plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation. Plays a role in the degradation of TP53. Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation. May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation. Ubiquitinates PPARG in macrophages playing a role in M2 macrophages polarization and angiogenesis.","The molecular function of this protein is a component of the N-end rule pathway, which is a mechanism for the degradation of proteins that have specific amino-terminal residues. The protein is involved in the recognition and binding of proteins with specific amino-terminal residues, leading to their degradation.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0019899; GO:0001664; GO:0031072; GO:0030544; GO:0051879; GO:0019900; GO:0051787; GO:0042803; GO:0051087; GO:0070412; GO:0046332; GO:0030911; GO:0061630; GO:0031625; GO:0004842; GO:0034450,,,,,,,,,,,0,,0.8626,yes
CHIP_RAT,A6HD62,Reference,Eukaryota,304,"E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Plays a role in the maintenance of mitochondrial morphology and promotes mitophagic removal of dysfunctional mitochondria; thereby acts as a protector against apoptosis in response to cellular stress. Negatively regulates vascular smooth muscle contraction, via degradation of the transcriptional activator MYOCD and subsequent loss of transcription of genes involved in vascular smooth muscle contraction. Promotes survival and proliferation of cardiac smooth muscle cells via ubiquitination and degradation of FOXO1, resulting in subsequent repression of FOXO1- mediated transcription of pro-apoptotic genes. Ubiquitinates ICER-type isoforms of CREM and targets them for proteasomal degradation, thereby acts as a positive effector of MAPK/ERK-mediated inhibition of apoptosis in cardiomyocytes. Inhibits lipopolysaccharide-induced apoptosis and hypertrophy in cardiomyocytes, via ubiquitination and subsequent proteasomal degradation of NFATC3. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Ubiquitinates CHRNA3 targeting it for endoplasmic reticulum-associated degradation in cortical neurons, as part of the STUB1-VCP-UBXN2A complex. Ubiquitinates and promotes ESR1 proteasomal degradation in response to age-related circulating estradiol (17-beta-estradiol/E2) decline, thereby promotes neuronal apoptosis in response to ischemic reperfusion injury. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base- excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB- degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation. Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation. Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner. Catalyzes monoubiquitination of SIRT6, preventing its degradation by the proteasome. Likely mediates polyubiquitination and down-regulates plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation. Plays a role in the degradation of TP53. Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation. May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation. Ubiquitinates PPARG in macrophages playing a role in M2 macrophages polarization and angiogenesis.","E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Plays a role in the maintenance of mitochondrial morphology and promotes mitophagic removal of dysfunctional mitochondria; thereby acts as a protector against apoptosis in response to cellular stress. Negatively regulates vascular smooth muscle contraction, via degradation of the transcriptional activator MYOCD and subsequent loss of transcription of genes involved in vascular smooth muscle contraction. Promotes survival and proliferation of cardiac smooth muscle cells via ubiquitination and degradation of FOXO1, resulting in subsequent repression of FOXO1- mediated transcription of pro-apoptotic genes. Ubiquitinates ICER-type isoforms of CREM and targets them for proteasomal degradation, thereby acts as a positive effector of MAPK/ERK-mediated inhibition of apoptosis in cardiomyocytes. Inhibits lipopolysaccharide-induced apoptosis and hypertrophy in cardiomyocytes, via ubiquitination and subsequent proteasomal degradation of NFATC3. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Ubiquitinates CHRNA3 targeting it for endoplasmic reticulum-associated degradation in cortical neurons, as part of the STUB1-VCP-UBXN2A complex. Ubiquitinates and promotes ESR1 proteasomal degradation in response to age-related circulating estradiol (17-beta-estradiol/E2) decline, thereby promotes neuronal apoptosis in response to ischemic reperfusion injury. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base- excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB- degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation. Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation. Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner. Catalyzes monoubiquitination of SIRT6, preventing its degradation by the proteasome. Likely mediates polyubiquitination and down-regulates plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation. Plays a role in the degradation of TP53. Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation. May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation. Ubiquitinates PPARG in macrophages playing a role in M2 macrophages polarization and angiogenesis.",,,,,,,GO:0019899; GO:0001664; GO:0031072; GO:0030544; GO:0051879; GO:0019900; GO:0051787; GO:0042803; GO:0051087; GO:0070412; GO:0046332; GO:0030911; GO:0061630; GO:0031625; GO:0004842; GO:0034450,GO:0004842,GO:0061630; GO:0051087,GO:0061630; GO:0051087,GO:0004842; GO:0061630,GO:0061630; GO:0004842,0.2909,0.7163,0.7163,0.3476,0.3476,5,0.4837,0.8626,yes
PRIA_KLEP7,A6TGC5,ESM2Text,Bacteria,731,"Initiates the restart of stalled replication forks, which reloads the replicative helicase on sites other than the origin of replication. Recognizes and binds to abandoned replication forks and remodels them to uncover a helicase loading site. Promotes assembly of the primosome at these replication forks.","Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0043138; GO:0005524; GO:0016887; GO:0003677; GO:0008270,GO:0003678,GO:0003678; GO:0005524,GO:0003678,GO:0003678,GO:0004003,0.3873,0.6425,0.3873,0.3873,0.3873,5,0.4383,0.7157,yes
PRIA_KLEP7,A6TGC5,Prot2Text,Bacteria,731,"Initiates the restart of stalled replication forks, which reloads the replicative helicase on sites other than the origin of replication. Recognizes and binds to abandoned replication forks and remodels them to uncover a helicase loading site. Promotes assembly of the primosome at these replication forks.","Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0043138; GO:0005524; GO:0016887; GO:0003677; GO:0008270,GO:0003678; GO:0005524,GO:0003678,GO:0003678,GO:0003678; GO:0005524,GO:0003678,0.6425,0.3873,0.3873,0.6425,0.3873,5,0.4894,0.7157,yes
PRIA_KLEP7,A6TGC5,ProtT3,Bacteria,731,"Initiates the restart of stalled replication forks, which reloads the replicative helicase on sites other than the origin of replication. Recognizes and binds to abandoned replication forks and remodels them to uncover a helicase loading site. Promotes assembly of the primosome at these replication forks.","Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA. Belongs to the helicase family. PriA subfamily",Yes,Yes,Yes,Yes,Yes,Yes,GO:0043138; GO:0005524; GO:0016887; GO:0003677; GO:0008270,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0008094,0.6425,0.6425,0.6425,0.6425,0.4575,5,0.6055,0.7157,yes
PRIA_KLEP7,A6TGC5,ProtTale,Bacteria,731,"Initiates the restart of stalled replication forks, which reloads the replicative helicase on sites other than the origin of replication. Recognizes and binds to abandoned replication forks and remodels them to uncover a helicase loading site. Promotes assembly of the primosome at these replication forks.","Initiates the restart of stalled replication forks, which reloads the replicative helicase on sites other than the origin of replication. Recognizes and binds to abandoned replication forks and remodels them to uncover a helicase loading site. Promotes assembly of the primosome at these replication forks.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0043138; GO:0005524; GO:0016887; GO:0003677; GO:0008270,,GO:0003677,GO:0003678,,,,0.4356,0.3873,,,2,0.4114,0.7157,yes
PRIA_KLEP7,A6TGC5,Protein2Text,Bacteria,731,"Initiates the restart of stalled replication forks, which reloads the replicative helicase on sites other than the origin of replication. Recognizes and binds to abandoned replication forks and remodels them to uncover a helicase loading site. Promotes assembly of the primosome at these replication forks.","The molecular function of this protein is a 3'-5' DNA helicase. 
It is involved in the repair of DNA. 
It is part of the error-prone DNA repair system. 
It is involved in the process of homologous recombination. 
It is involved in the process of non-homologous end joining.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0043138; GO:0005524; GO:0016887; GO:0003677; GO:0008270,GO:0003678; GO:0005524,GO:0004003; GO:0003677; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0016887,GO:0003678; GO:0005524,0.6425,0.7915,0.6425,0.5879,0.6425,5,0.6614,0.7157,yes
PRIA_KLEP7,A6TGC5,Reference,Bacteria,731,"Initiates the restart of stalled replication forks, which reloads the replicative helicase on sites other than the origin of replication. Recognizes and binds to abandoned replication forks and remodels them to uncover a helicase loading site. Promotes assembly of the primosome at these replication forks.","Initiates the restart of stalled replication forks, which reloads the replicative helicase on sites other than the origin of replication. Recognizes and binds to abandoned replication forks and remodels them to uncover a helicase loading site. Promotes assembly of the primosome at these replication forks.",,,,,,,GO:0043138; GO:0005524; GO:0016887; GO:0003677; GO:0008270,GO:0003677,GO:0003677,GO:0003678; GO:0005524,GO:0005524; GO:0003689,GO:0003677,0.4356,0.4356,0.6425,0.5516,0.4356,5,0.5002,0.7157,yes
RPOA_PRRSV,A6YQT5,ESM2Text,Viruses,3931,"[Replicase polyprotein 1ab]: Contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.","Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer. Required to recruit MAD1L1 to mitotic spindles.",No,No,No,No,No,not-Yes,GO:0005524; GO:0004843; GO:0004197; GO:0003678; GO:0004519; GO:0016829; GO:0030291; GO:0003723; GO:0003724; GO:0004540; GO:0003968; GO:0004252; GO:0008270,,,,,,,,,,,0,,0.4337,no
RPOA_PRRSV,A6YQT5,Prot2Text,Viruses,3931,"[Replicase polyprotein 1ab]: Contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.","Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer. Required to recruit MAD1L1 to mitotic spindles.",No,No,No,No,No,not-Yes,GO:0005524; GO:0004843; GO:0004197; GO:0003678; GO:0004519; GO:0016829; GO:0030291; GO:0003723; GO:0003724; GO:0004540; GO:0003968; GO:0004252; GO:0008270,,,,,,,,,,,0,,0.4337,no
RPOA_PRRSV,A6YQT5,ProtT3,Viruses,3931,"[Replicase polyprotein 1ab]: Contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.",Catalyzes the hydrolysis of the covalent linkage between the N-terminal glutamine and the alpha-amino group of the initiator methionine of viral polyproteins. [Isoform 1]: Cytoplasm. [Isoform 2]: Cytoplasm. [Isoform 3]: Cytoplasm. [Isoform 4]: Cytoplasm. [Isoform 5]: Cytoplasm. [Iso,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004843; GO:0004197; GO:0003678; GO:0004519; GO:0016829; GO:0030291; GO:0003723; GO:0003724; GO:0004540; GO:0003968; GO:0004252; GO:0008270,GO:0008233,GO:0008234,GO:0004197,GO:0008233,GO:0008233,0.3341,0.3287,0.3261,0.3341,0.3341,5,0.3314,0.4337,no
RPOA_PRRSV,A6YQT5,ProtTale,Viruses,3931,"[Replicase polyprotein 1ab]: Contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.","[Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004843; GO:0004197; GO:0003678; GO:0004519; GO:0016829; GO:0030291; GO:0003723; GO:0003724; GO:0004540; GO:0003968; GO:0004252; GO:0008270,GO:0004197,GO:0008233,GO:0008233,GO:0008233,GO:0008233,0.3261,0.3341,0.3341,0.3341,0.3341,5,0.3325,0.4337,no
RPOA_PRRSV,A6YQT5,Protein2Text,Viruses,3931,"[Replicase polyprotein 1ab]: Contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.",This protein is involved in the molecular function of nucleic acid binding.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0004843; GO:0004197; GO:0003678; GO:0004519; GO:0016829; GO:0030291; GO:0003723; GO:0003724; GO:0004540; GO:0003968; GO:0004252; GO:0008270,GO:0003676,GO:0003676,,GO:0003676,GO:0003676,0.2541,0.2541,,0.2541,0.2541,4,0.2541,0.4337,no
RPOA_PRRSV,A6YQT5,Reference,Viruses,3931,"[Replicase polyprotein 1ab]: Contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.","[Replicase polyprotein 1ab]: Contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.",,,,,,,GO:0005524; GO:0004843; GO:0004197; GO:0003678; GO:0004519; GO:0016829; GO:0030291; GO:0003723; GO:0003724; GO:0004540; GO:0003968; GO:0004252; GO:0008270,GO:0003968; GO:0004197,GO:0003968,GO:0003968; GO:0004197,,,0.4677,0.2949,0.4677,,,3,0.4101,0.4337,no
NANY_MEDG7,A7B558,ESM2Text,Bacteria,374,"Hydratase involved in the degradation of sialic acids, which are present in the host mucus layer and represent a much-coveted source of nutrients for R.gnavus, a prevalent member of the normal gut microbiota. Catalyzes the reversible conversion of the dehydrated form of N-acetylneuraminate (Neu5Ac), 2,7- anhydro-N-acetylneuraminate (2,7-AN), to Neu5Ac, allowing growth on 2,7-AN produced by the IT-sialidase NanH. Acts through a multistep mechanism involving a keto intermediate and cycling of NADH/NAD(+).","Involved in the degradation of ectoine, which allows H.elongata to utilize ectoine as both an energy source and an energy source for its growth. Oxidizes preferentially compounds with an aromatic or a strong aliphatic group such as vanillate and vanillate, but not compounds with a broad range of aromatic and aliphatic groups.",No,No,No,No,No,not-Yes,GO:0016829; GO:0000166,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4496,0.4496,0.4496,0.4496,0.4496,5,0.4496,0.1364,no
NANY_MEDG7,A7B558,Prot2Text,Bacteria,374,"Hydratase involved in the degradation of sialic acids, which are present in the host mucus layer and represent a much-coveted source of nutrients for R.gnavus, a prevalent member of the normal gut microbiota. Catalyzes the reversible conversion of the dehydrated form of N-acetylneuraminate (Neu5Ac), 2,7- anhydro-N-acetylneuraminate (2,7-AN), to Neu5Ac, allowing growth on 2,7-AN produced by the IT-sialidase NanH. Acts through a multistep mechanism involving a keto intermediate and cycling of NADH/NAD(+).","Reduces nitrogenase efficiently and efficiently by combining with both NADH and NADPH. May be involved in the oxidation of L-sorbose to D-sorbose and, possibly, in the degradation of D-galactose.",No,No,No,No,No,not-Yes,GO:0016829; GO:0000166,GO:0016491,,GO:0016491,GO:0016491,,0.4496,,0.4496,0.4496,,3,0.4496,0.1364,no
NANY_MEDG7,A7B558,ProtT3,Bacteria,374,"Hydratase involved in the degradation of sialic acids, which are present in the host mucus layer and represent a much-coveted source of nutrients for R.gnavus, a prevalent member of the normal gut microbiota. Catalyzes the reversible conversion of the dehydrated form of N-acetylneuraminate (Neu5Ac), 2,7- anhydro-N-acetylneuraminate (2,7-AN), to Neu5Ac, allowing growth on 2,7-AN produced by the IT-sialidase NanH. Acts through a multistep mechanism involving a keto intermediate and cycling of NADH/NAD(+).",Belongs to the Gfo/Idh/MocA family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016829; GO:0000166,GO:0016491,GO:0016491,GO:0016491,GO:0016491,,0.4496,0.4496,0.4496,0.4496,,4,0.4496,0.1364,no
NANY_MEDG7,A7B558,ProtTale,Bacteria,374,"Hydratase involved in the degradation of sialic acids, which are present in the host mucus layer and represent a much-coveted source of nutrients for R.gnavus, a prevalent member of the normal gut microbiota. Catalyzes the reversible conversion of the dehydrated form of N-acetylneuraminate (Neu5Ac), 2,7- anhydro-N-acetylneuraminate (2,7-AN), to Neu5Ac, allowing growth on 2,7-AN produced by the IT-sialidase NanH. Acts through a multistep mechanism involving a keto intermediate and cycling of NADH/NAD(+).",Could catalyze the oxidation of NAD(+) to NADP(+) using NAD(+) reductase.,No,No,No,No,No,not-Yes,GO:0016829; GO:0000166,,,,,,,,,,,0,,0.1364,no
NANY_MEDG7,A7B558,Protein2Text,Bacteria,374,"Hydratase involved in the degradation of sialic acids, which are present in the host mucus layer and represent a much-coveted source of nutrients for R.gnavus, a prevalent member of the normal gut microbiota. Catalyzes the reversible conversion of the dehydrated form of N-acetylneuraminate (Neu5Ac), 2,7- anhydro-N-acetylneuraminate (2,7-AN), to Neu5Ac, allowing growth on 2,7-AN produced by the IT-sialidase NanH. Acts through a multistep mechanism involving a keto intermediate and cycling of NADH/NAD(+).","The molecular function of this protein is not explicitly stated in the provided information. However, based on its name, it is likely that this protein is involved in a redox reaction, such as the transfer of a group or the catalysis of an oxidation-reduction reaction. Specifically, it is a kinase, which is an enzyme that transfers a phosphate group from one molecule to another. The exact molecular function would depend on the specific context in which the protein is found and the other molecules it interacts with.",No,No,Vague,Vague,Maybe,not-Yes,GO:0016829; GO:0000166,,,,,,,,,,,0,,0.1364,no
NANY_MEDG7,A7B558,Reference,Bacteria,374,"Hydratase involved in the degradation of sialic acids, which are present in the host mucus layer and represent a much-coveted source of nutrients for R.gnavus, a prevalent member of the normal gut microbiota. Catalyzes the reversible conversion of the dehydrated form of N-acetylneuraminate (Neu5Ac), 2,7- anhydro-N-acetylneuraminate (2,7-AN), to Neu5Ac, allowing growth on 2,7-AN produced by the IT-sialidase NanH. Acts through a multistep mechanism involving a keto intermediate and cycling of NADH/NAD(+).","Hydratase involved in the degradation of sialic acids, which are present in the host mucus layer and represent a much-coveted source of nutrients for R.gnavus, a prevalent member of the normal gut microbiota. Catalyzes the reversible conversion of the dehydrated form of N-acetylneuraminate (Neu5Ac), 2,7- anhydro-N-acetylneuraminate (2,7-AN), to Neu5Ac, allowing growth on 2,7-AN produced by the IT-sialidase NanH. Acts through a multistep mechanism involving a keto intermediate and cycling of NADH/NAD(+).",,,,,,,GO:0016829; GO:0000166,GO:0050573,GO:0016836; GO:0051287,GO:0016836,GO:0016836,GO:0016491,0.2715,0.7105,0.4994,0.4994,0.4496,5,0.4861,0.1364,no
PLK_GIAIC,A8BPK8,ESM2Text,Eukaryota,678,Involved in cell cycle. Involved in cell division. Involved in cytokinesis. Involved in flagella biogenesis and in regulation of flagella length in interphase. Involved in formation of median bodies during interphase. Phosphorylates Kin-13 in vitro. Likely regulates microtubule (MT) depolymerizing activity of Kin-13.,"Serine/threonine-protein kinase which, in association with the sphingolipid-associated protein sphingosine-1, plays an essential role in endosomal membrane trafficking, cell cycle regulation, cell cycle progression, and cellular morphogenesis. Phosphorylates sphingosine-1, which is required for its localization to endosomes and the subsequent activation of the sphingosine-monosaccharide-containing regulatory complex SSCSC1. Following phosphorylation, SSC1 undergoes dynamic rearrangements, ultimately leading to stabilization of sphingomyelin and its polymerization. Phosphorylates the activated form of SSC1, promoting its localization to late endosomes and the subsequent activation of sphingosine-containing regulatory complex SSC1. Involved in the regulation of cell cycle progression. Phosphorylates the activated form of CDC25B, promoting its localization to late endosomes and the subsequent activation of CDC25B. Phosphorylates the activated form of CDC25C, promoting its localization to late endosomes and the subsequent activation of CDC25C. Phosphorylates the activated form of CDC25D, promoting its localization to",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004672; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.7413,0.7413,0.7413,0.7413,0.7413,5,0.7413,0.7459,yes
PLK_GIAIC,A8BPK8,Prot2Text,Eukaryota,678,Involved in cell cycle. Involved in cell division. Involved in cytokinesis. Involved in flagella biogenesis and in regulation of flagella length in interphase. Involved in formation of median bodies during interphase. Phosphorylates Kin-13 in vitro. Likely regulates microtubule (MT) depolymerizing activity of Kin-13.,Serine/threonine-protein kinase. Involved in the control of chemotaxis and cytokinesis. Functions in the CAN axon branch of the CAN axon-glial motor complex.,Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004672; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.7413,0.7413,0.7413,0.7413,0.7413,5,0.7413,0.7459,yes
PLK_GIAIC,A8BPK8,ProtT3,Eukaryota,678,Involved in cell cycle. Involved in cell division. Involved in cytokinesis. Involved in flagella biogenesis and in regulation of flagella length in interphase. Involved in formation of median bodies during interphase. Phosphorylates Kin-13 in vitro. Likely regulates microtubule (MT) depolymerizing activity of Kin-13.,Probable serine/threonine-protein kinase involved in cell cycle control. Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CDC2/CDKX subfamily,Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004672; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,0.9822,0.9822,0.9822,0.9822,0.7413,5,0.934,0.7459,yes
PLK_GIAIC,A8BPK8,ProtTale,Eukaryota,678,Involved in cell cycle. Involved in cell division. Involved in cytokinesis. Involved in flagella biogenesis and in regulation of flagella length in interphase. Involved in formation of median bodies during interphase. Phosphorylates Kin-13 in vitro. Likely regulates microtubule (MT) depolymerizing activity of Kin-13.,"Serine/threonine-protein kinase that plays a role in a variety of mitotic and meiotic processes such as chromosome condensation, sister chromatid segregation, homologous recombination, DNA damage repair and meiosis I. Required for efficient homologous recombination repair of double-strand breaks (DSBs) at meiosis I by mediating phosphorylation of the RAD51 recombinase and RIF1, an essential component of the meiotic recombination machinery. Also required for sister chromatid segregation during meiosis I by mediating phosphorylation of the MAD2L1 subunit of the anaphase-promoting complex (APC/C), promoting the degradation of MAD2L1 by the APC",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004672; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,0.9822,0.9822,0.9822,0.7413,0.9822,5,0.934,0.7459,yes
PLK_GIAIC,A8BPK8,Protein2Text,Eukaryota,678,Involved in cell cycle. Involved in cell division. Involved in cytokinesis. Involved in flagella biogenesis and in regulation of flagella length in interphase. Involved in formation of median bodies during interphase. Phosphorylates Kin-13 in vitro. Likely regulates microtubule (MT) depolymerizing activity of Kin-13.,"The molecular function of this protein is a protein kinase, specifically a serine/threonine-protein kinase.",Maybe,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0005524; GO:0004672; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.7413,0.7413,0.7413,0.7413,0.7413,5,0.7413,0.7459,yes
PLK_GIAIC,A8BPK8,Reference,Eukaryota,678,Involved in cell cycle. Involved in cell division. Involved in cytokinesis. Involved in flagella biogenesis and in regulation of flagella length in interphase. Involved in formation of median bodies during interphase. Phosphorylates Kin-13 in vitro. Likely regulates microtubule (MT) depolymerizing activity of Kin-13.,Involved in cell cycle. Involved in cell division. Involved in cytokinesis. Involved in flagella biogenesis and in regulation of flagella length in interphase. Involved in formation of median bodies during interphase. Phosphorylates Kin-13 in vitro. Likely regulates microtubule (MT) depolymerizing activity of Kin-13.,,,,,,,GO:0005524; GO:0004672; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004694; GO:0005524,GO:0004674; GO:0005524,0.9822,0.9822,0.9822,0.9314,0.9822,5,0.972,0.7459,yes
CP260_SORC5,A9FDB7,ESM2Text,Bacteria,394,"Hydroxylase that can catalyze the in vitro conversion of the sesquiterpenoid nootkatone, a natural organic compound produced by some plants, to at least five hydrophilic products. The native ferredoxin reductase FdR_B and either Fdx2 or Fdx8 ferredoxins can act as the redox partners for the conversion of nootkatone.","Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.",Vague,Vague,Maybe,Vague,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0020037; GO:0005506,GO:0004497; GO:0020037,GO:0004497,GO:0004497; GO:0005506; GO:0020037,0.9516,0.9516,0.8149,0.5872,0.9516,5,0.8514,0.1662,no
CP260_SORC5,A9FDB7,Prot2Text,Bacteria,394,"Hydroxylase that can catalyze the in vitro conversion of the sesquiterpenoid nootkatone, a natural organic compound produced by some plants, to at least five hydrophilic products. The native ferredoxin reductase FdR_B and either Fdx2 or Fdx8 ferredoxins can act as the redox partners for the conversion of nootkatone.","Catalyzes the C-C bond cleavage of aromatic compounds such as menthol, catechol, cefoxitin, and catechol to produce their corresponding imines. Can also catalyze the C-C bond cleavage of phenolic derivatives.",No,No,No,No,No,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0016491,,GO:0016701,GO:0016491,,0.5572,,0.4517,0.5572,,3,0.522,0.1662,no
CP260_SORC5,A9FDB7,ProtT3,Bacteria,394,"Hydroxylase that can catalyze the in vitro conversion of the sesquiterpenoid nootkatone, a natural organic compound produced by some plants, to at least five hydrophilic products. The native ferredoxin reductase FdR_B and either Fdx2 or Fdx8 ferredoxins can act as the redox partners for the conversion of nootkatone.","Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Belongs to the cytochrome P450 family",Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,0.9516,0.9516,0.9516,0.9516,0.9516,5,0.9516,0.1662,no
CP260_SORC5,A9FDB7,ProtTale,Bacteria,394,"Hydroxylase that can catalyze the in vitro conversion of the sesquiterpenoid nootkatone, a natural organic compound produced by some plants, to at least five hydrophilic products. The native ferredoxin reductase FdR_B and either Fdx2 or Fdx8 ferredoxins can act as the redox partners for the conversion of nootkatone.","Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.",Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0020037; GO:0005506,GO:0004497,GO:0004497; GO:0005506; GO:0020037,0.5872,0.9516,0.9516,0.5872,0.9516,5,0.8058,0.1662,no
CP260_SORC5,A9FDB7,Protein2Text,Bacteria,394,"Hydroxylase that can catalyze the in vitro conversion of the sesquiterpenoid nootkatone, a natural organic compound produced by some plants, to at least five hydrophilic products. The native ferredoxin reductase FdR_B and either Fdx2 or Fdx8 ferredoxins can act as the redox partners for the conversion of nootkatone.","This protein is a part of the cytochrome P450 family, which is a large family of enzymes that catalyze the oxidation of organic substances. The molecular function of this protein is likely to be involved in the oxidation of a substrate, possibly as part of a metabolic pathway.",Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497,GO:0005506; GO:0016491,GO:0004497,GO:0004497,GO:0004497,0.5872,0.7787,0.5872,0.5872,0.5872,5,0.6255,0.1662,no
CP260_SORC5,A9FDB7,Reference,Bacteria,394,"Hydroxylase that can catalyze the in vitro conversion of the sesquiterpenoid nootkatone, a natural organic compound produced by some plants, to at least five hydrophilic products. The native ferredoxin reductase FdR_B and either Fdx2 or Fdx8 ferredoxins can act as the redox partners for the conversion of nootkatone.","Hydroxylase that can catalyze the in vitro conversion of the sesquiterpenoid nootkatone, a natural organic compound produced by some plants, to at least five hydrophilic products. The native ferredoxin reductase FdR_B and either Fdx2 or Fdx8 ferredoxins can act as the redox partners for the conversion of nootkatone.",,,,,,,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497,GO:0004497; GO:0020037; GO:0005506,GO:0004497,GO:0004497; GO:0016491,GO:0004497; GO:0016491,0.5872,0.9516,0.5872,0.6619,0.6619,5,0.69,0.1662,no
DOSS_MYCA9,B1MH83,ESM2Text,Bacteria,567,"Member of the two-component regulatory system DosR/DosS involved in onset of the dormancy response. Regulates a regulon consisting of numerous genes. Required for induction of the DosR regulon; acts to positively regulate expression of the DosR regulon during adaptation to anaerobiosis. Characterized as an oxygen sensor; O(2) acts as a switch, with O(2)-bound Fe(2+) protein inactive in autophosphorylation. Has also been suggested to act as a redox sensor, or perhaps as a dual oxygen/redox sensor. Donates a phosphate group to transcriptional regulator DosR. The DosRS is required for maximal growth and survival in in vitro hypoxia models that mimic the physiologic environments of the cystic fibrosis (CF) lung, within granulomas, phagosomes of the macrophages and biofilms. Involved in response to antibiotics in vivo and in vitro hypoxic conditions. Involved in biofilm formation in vitro.",Member of the two-component regulatory system DpiA/DpiB involved in the sensing and response to inorganic phosphate starvation. Functions as a photo-protectant probably able to prevent the accumulation of photo-protectant DpiB in an autoregulatory cellular system.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0070025; GO:0020037; GO:0000287; GO:0070026; GO:0019825; GO:0019826; GO:0000155; GO:0046983,,,,,,,,,,,0,,0.4317,no
DOSS_MYCA9,B1MH83,Prot2Text,Bacteria,567,"Member of the two-component regulatory system DosR/DosS involved in onset of the dormancy response. Regulates a regulon consisting of numerous genes. Required for induction of the DosR regulon; acts to positively regulate expression of the DosR regulon during adaptation to anaerobiosis. Characterized as an oxygen sensor; O(2) acts as a switch, with O(2)-bound Fe(2+) protein inactive in autophosphorylation. Has also been suggested to act as a redox sensor, or perhaps as a dual oxygen/redox sensor. Donates a phosphate group to transcriptional regulator DosR. The DosRS is required for maximal growth and survival in in vitro hypoxia models that mimic the physiologic environments of the cystic fibrosis (CF) lung, within granulomas, phagosomes of the macrophages and biofilms. Involved in response to antibiotics in vivo and in vitro hypoxic conditions. Involved in biofilm formation in vitro.","Member of the two-component regulatory system MctS/MctR, which activates mctP expression.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0070025; GO:0020037; GO:0000287; GO:0070026; GO:0019825; GO:0019826; GO:0000155; GO:0046983,GO:0000155,GO:0000155,,GO:0000155,GO:0000155,0.295,0.295,,0.295,0.295,4,0.295,0.4317,no
DOSS_MYCA9,B1MH83,ProtT3,Bacteria,567,"Member of the two-component regulatory system DosR/DosS involved in onset of the dormancy response. Regulates a regulon consisting of numerous genes. Required for induction of the DosR regulon; acts to positively regulate expression of the DosR regulon during adaptation to anaerobiosis. Characterized as an oxygen sensor; O(2) acts as a switch, with O(2)-bound Fe(2+) protein inactive in autophosphorylation. Has also been suggested to act as a redox sensor, or perhaps as a dual oxygen/redox sensor. Donates a phosphate group to transcriptional regulator DosR. The DosRS is required for maximal growth and survival in in vitro hypoxia models that mimic the physiologic environments of the cystic fibrosis (CF) lung, within granulomas, phagosomes of the macrophages and biofilms. Involved in response to antibiotics in vivo and in vitro hypoxic conditions. Involved in biofilm formation in vitro.",Member of the two-component regulatory system MprB/MprA involved in resistance to cationic antimicrobial peptides (CAMPs). MprB functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to MprA (By similarity). Member of the two-component regulatory system MprB/MprA involved in resistance to cationic antimicrobial peptides (CAMPs). MprB functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to MprA (By similarity),Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0070025; GO:0020037; GO:0000287; GO:0070026; GO:0019825; GO:0019826; GO:0000155; GO:0046983,GO:0000155,GO:0000155; GO:0004673,GO:0000155; GO:0005524,GO:0000155; GO:0004673,GO:0000155,0.295,0.3447,0.5232,0.3447,0.295,5,0.3605,0.4317,no
DOSS_MYCA9,B1MH83,ProtTale,Bacteria,567,"Member of the two-component regulatory system DosR/DosS involved in onset of the dormancy response. Regulates a regulon consisting of numerous genes. Required for induction of the DosR regulon; acts to positively regulate expression of the DosR regulon during adaptation to anaerobiosis. Characterized as an oxygen sensor; O(2) acts as a switch, with O(2)-bound Fe(2+) protein inactive in autophosphorylation. Has also been suggested to act as a redox sensor, or perhaps as a dual oxygen/redox sensor. Donates a phosphate group to transcriptional regulator DosR. The DosRS is required for maximal growth and survival in in vitro hypoxia models that mimic the physiologic environments of the cystic fibrosis (CF) lung, within granulomas, phagosomes of the macrophages and biofilms. Involved in response to antibiotics in vivo and in vitro hypoxic conditions. Involved in biofilm formation in vitro.",Member of the two-component regulatory system KdpD/KdpE that functions in the regulation of the kdp operon and potassium homeostasis. May function as a membrane-associated protein kinase that phosphorylates KdpE in response to environmental signals.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0070025; GO:0020037; GO:0000287; GO:0070026; GO:0019825; GO:0019826; GO:0000155; GO:0046983,GO:0000155; GO:0005524,GO:0000155,GO:0000155,GO:0004673,GO:0004672,0.5232,0.295,0.295,0.2357,0.228,5,0.3154,0.4317,no
DOSS_MYCA9,B1MH83,Protein2Text,Bacteria,567,"Member of the two-component regulatory system DosR/DosS involved in onset of the dormancy response. Regulates a regulon consisting of numerous genes. Required for induction of the DosR regulon; acts to positively regulate expression of the DosR regulon during adaptation to anaerobiosis. Characterized as an oxygen sensor; O(2) acts as a switch, with O(2)-bound Fe(2+) protein inactive in autophosphorylation. Has also been suggested to act as a redox sensor, or perhaps as a dual oxygen/redox sensor. Donates a phosphate group to transcriptional regulator DosR. The DosRS is required for maximal growth and survival in in vitro hypoxia models that mimic the physiologic environments of the cystic fibrosis (CF) lung, within granulomas, phagosomes of the macrophages and biofilms. Involved in response to antibiotics in vivo and in vitro hypoxic conditions. Involved in biofilm formation in vitro.","This protein is involved in the regulation of gene expression, specifically in the process of transcriptional regulation. It is a transcriptional regulator protein, which means it binds to specific DNA sequences to control the transcription of genes. In this case, it is a repressor protein, which means it prevents the transcription of certain genes by binding to their regulatory regions.",No,Maybe,No,Vague,Maybe,not-Yes,GO:0005524; GO:0070025; GO:0020037; GO:0000287; GO:0070026; GO:0019825; GO:0019826; GO:0000155; GO:0046983,GO:0003700,GO:0003700,GO:0003700,GO:0003700,GO:0003700,0.1835,0.1835,0.1835,0.1835,0.1835,5,0.1835,0.4317,no
DOSS_MYCA9,B1MH83,Reference,Bacteria,567,"Member of the two-component regulatory system DosR/DosS involved in onset of the dormancy response. Regulates a regulon consisting of numerous genes. Required for induction of the DosR regulon; acts to positively regulate expression of the DosR regulon during adaptation to anaerobiosis. Characterized as an oxygen sensor; O(2) acts as a switch, with O(2)-bound Fe(2+) protein inactive in autophosphorylation. Has also been suggested to act as a redox sensor, or perhaps as a dual oxygen/redox sensor. Donates a phosphate group to transcriptional regulator DosR. The DosRS is required for maximal growth and survival in in vitro hypoxia models that mimic the physiologic environments of the cystic fibrosis (CF) lung, within granulomas, phagosomes of the macrophages and biofilms. Involved in response to antibiotics in vivo and in vitro hypoxic conditions. Involved in biofilm formation in vitro.","Member of the two-component regulatory system DosR/DosS involved in onset of the dormancy response. Regulates a regulon consisting of numerous genes. Required for induction of the DosR regulon; acts to positively regulate expression of the DosR regulon during adaptation to anaerobiosis. Characterized as an oxygen sensor; O(2) acts as a switch, with O(2)-bound Fe(2+) protein inactive in autophosphorylation. Has also been suggested to act as a redox sensor, or perhaps as a dual oxygen/redox sensor. Donates a phosphate group to transcriptional regulator DosR. The DosRS is required for maximal growth and survival in in vitro hypoxia models that mimic the physiologic environments of the cystic fibrosis (CF) lung, within granulomas, phagosomes of the macrophages and biofilms. Involved in response to antibiotics in vivo and in vitro hypoxic conditions. Involved in biofilm formation in vitro.",,,,,,,GO:0005524; GO:0070025; GO:0020037; GO:0000287; GO:0070026; GO:0019825; GO:0019826; GO:0000155; GO:0046983,GO:0000155; GO:0005524,GO:0000155; GO:0004673; GO:0019825,GO:0000155,GO:0000155; GO:0005524,GO:0000155; GO:0005524,0.5232,0.666,0.295,0.5232,0.5232,5,0.5061,0.4317,no
ST2A6_MOUSE,B2RVI8,ESM2Text,Eukaryota,285,Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of the hydroxyl group of hydroxysteroids and bile acids.,"Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation. Sulfonates p-nitrophenol, the most widely used insecticides in the mandelanin biosynthesis. Also sulfonates several sulfate analogs, such as protocatechuate, 4-chloroanilactate, D-galactate and butyraldehyde.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0050656; GO:0004027; GO:0047704; GO:0050294; GO:0008146; GO:0016740,GO:0008146,GO:0008146,GO:0008146,GO:0008146,GO:0008146,0.7623,0.7623,0.7623,0.7623,0.7623,5,0.7623,0.647,yes
ST2A6_MOUSE,B2RVI8,Prot2Text,Eukaryota,285,Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of the hydroxyl group of hydroxysteroids and bile acids.,"Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of xenobiotics, such as phenolamide, T3 (triiodo-L-thyronine), T4 (thyroxine), estrone and DOPA.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0050656; GO:0004027; GO:0047704; GO:0050294; GO:0008146; GO:0016740,GO:0008146,GO:0008146,GO:0008146,GO:0008146,GO:0008146,0.7623,0.7623,0.7623,0.7623,0.7623,5,0.7623,0.647,yes
ST2A6_MOUSE,B2RVI8,ProtT3,Eukaryota,285,Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of the hydroxyl group of hydroxysteroids and bile acids.,Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of steroid hormones and xenobiotics. Cytoplasm. Belongs to the sulfotransferase 1 family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0050656; GO:0004027; GO:0047704; GO:0050294; GO:0008146; GO:0016740,GO:0008146,GO:0008146,GO:0008146,GO:0008146,GO:0008146,0.7623,0.7623,0.7623,0.7623,0.7623,5,0.7623,0.647,yes
ST2A6_MOUSE,B2RVI8,ProtTale,Eukaryota,285,Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of the hydroxyl group of hydroxysteroids and bile acids.,Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the N-sulfonation of amines.,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0050656; GO:0004027; GO:0047704; GO:0050294; GO:0008146; GO:0016740,GO:0008146,GO:0008146,GO:0008146,GO:0008146,GO:0008146,0.7623,0.7623,0.7623,0.7623,0.7623,5,0.7623,0.647,yes
ST2A6_MOUSE,B2RVI8,Protein2Text,Eukaryota,285,Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of the hydroxyl group of hydroxysteroids and bile acids.,"The molecular function of this protein is sulfotransferase activity, specifically catalyzing the transfer of a sulfate group to a hydroxyl group in steroids, hormones, and other xenobiotics.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0050656; GO:0004027; GO:0047704; GO:0050294; GO:0008146; GO:0016740,GO:0008146,GO:0008146,GO:0008146,GO:0008146,GO:0008146,0.7623,0.7623,0.7623,0.7623,0.7623,5,0.7623,0.647,yes
ST2A6_MOUSE,B2RVI8,Reference,Eukaryota,285,Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of the hydroxyl group of hydroxysteroids and bile acids.,Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of the hydroxyl group of hydroxysteroids and bile acids.,,,,,,,GO:0050656; GO:0004027; GO:0047704; GO:0050294; GO:0008146; GO:0016740,GO:0047704; GO:0008146,GO:0008146; GO:0050294,GO:0008146; GO:0050294,GO:0004304; GO:0047704,GO:0008146,0.8097,0.8097,0.8097,0.73,0.7623,5,0.7843,0.647,yes
LNBB_BIFB1,B3TLD6,ESM2Text,Bacteria,1112,"Present in the infant gut, this enzyme is involved in the assimilation of type-1 human milk oligosaccharides (HMOs). It hydrolyzes via a retaining mechanism the beta-D-GlcNAc-(1->3)-beta-D- Gal linkage in lacto-N-tetraose (LNT or beta-D-Gal-(1->3)-beta-D- GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc), an abundant HMO unique to human breast milk, releasing lacto-N-biose (LNB or beta-D-Gal-(1->3)-D- GlcNAc) and lactose. Is a key enzymatic factor for growth and proliferation of B.bifidum in the gut ecosystem of breast-fed infants (Probable). Has substrate preference for unmodified beta-linked LNB since it does not hydrolyze the fucosylated forms of lacto-N-tetraose (lacto-N-fucopentaose I and II) or lacto-N-neotetraose. Is also able to display transglycosylation activity in vitro.","This protein is a mucin-type glycoside hydrolase with a broad substrate specificity. It cleaves mucin-type oligosaccharides with high activity against poly-1,4- and poly-1,6-N-acetyl-D-glucosamine (PGNA) and mucin-type oligosaccharides with low activity against PNP and pNP-beta-GlcNAc. In vivo, it is the major enzyme responsible for the degradation of mucin in the stomach.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004563; GO:0047403,GO:0016798,GO:0004553,GO:0016798,GO:0004553,GO:0016798,0.7015,0.8234,0.7015,0.8234,0.7015,5,0.7503,0.3102,no
LNBB_BIFB1,B3TLD6,Prot2Text,Bacteria,1112,"Present in the infant gut, this enzyme is involved in the assimilation of type-1 human milk oligosaccharides (HMOs). It hydrolyzes via a retaining mechanism the beta-D-GlcNAc-(1->3)-beta-D- Gal linkage in lacto-N-tetraose (LNT or beta-D-Gal-(1->3)-beta-D- GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc), an abundant HMO unique to human breast milk, releasing lacto-N-biose (LNB or beta-D-Gal-(1->3)-D- GlcNAc) and lactose. Is a key enzymatic factor for growth and proliferation of B.bifidum in the gut ecosystem of breast-fed infants (Probable). Has substrate preference for unmodified beta-linked LNB since it does not hydrolyze the fucosylated forms of lacto-N-tetraose (lacto-N-fucopentaose I and II) or lacto-N-neotetraose. Is also able to display transglycosylation activity in vitro.","Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines.",Maybe,Maybe,Maybe,No,No,not-Yes,GO:0004563; GO:0047403,GO:0004563,GO:0004563,GO:0004563,GO:0004553,GO:0004563,0.8778,0.8778,0.8778,0.8234,0.8778,5,0.8669,0.3102,no
LNBB_BIFB1,B3TLD6,ProtT3,Bacteria,1112,"Present in the infant gut, this enzyme is involved in the assimilation of type-1 human milk oligosaccharides (HMOs). It hydrolyzes via a retaining mechanism the beta-D-GlcNAc-(1->3)-beta-D- Gal linkage in lacto-N-tetraose (LNT or beta-D-Gal-(1->3)-beta-D- GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc), an abundant HMO unique to human breast milk, releasing lacto-N-biose (LNB or beta-D-Gal-(1->3)-D- GlcNAc) and lactose. Is a key enzymatic factor for growth and proliferation of B.bifidum in the gut ecosystem of breast-fed infants (Probable). Has substrate preference for unmodified beta-linked LNB since it does not hydrolyze the fucosylated forms of lacto-N-tetraose (lacto-N-fucopentaose I and II) or lacto-N-neotetraose. Is also able to display transglycosylation activity in vitro.",Belongs to the glycosyl hydrolase 20 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004563; GO:0047403,GO:0016798,GO:0004563,GO:0004553,GO:0004553,GO:0016798,0.7015,0.8778,0.8234,0.8234,0.7015,5,0.7855,0.3102,no
LNBB_BIFB1,B3TLD6,ProtTale,Bacteria,1112,"Present in the infant gut, this enzyme is involved in the assimilation of type-1 human milk oligosaccharides (HMOs). It hydrolyzes via a retaining mechanism the beta-D-GlcNAc-(1->3)-beta-D- Gal linkage in lacto-N-tetraose (LNT or beta-D-Gal-(1->3)-beta-D- GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc), an abundant HMO unique to human breast milk, releasing lacto-N-biose (LNB or beta-D-Gal-(1->3)-D- GlcNAc) and lactose. Is a key enzymatic factor for growth and proliferation of B.bifidum in the gut ecosystem of breast-fed infants (Probable). Has substrate preference for unmodified beta-linked LNB since it does not hydrolyze the fucosylated forms of lacto-N-tetraose (lacto-N-fucopentaose I and II) or lacto-N-neotetraose. Is also able to display transglycosylation activity in vitro.",Involved in the degradation of chitobiose and chitotriose.,No,No,No,No,No,not-Yes,GO:0004563; GO:0047403,,,GO:0004563,,GO:0004553,,,0.8778,,0.8234,2,0.8506,0.3102,no
LNBB_BIFB1,B3TLD6,Protein2Text,Bacteria,1112,"Present in the infant gut, this enzyme is involved in the assimilation of type-1 human milk oligosaccharides (HMOs). It hydrolyzes via a retaining mechanism the beta-D-GlcNAc-(1->3)-beta-D- Gal linkage in lacto-N-tetraose (LNT or beta-D-Gal-(1->3)-beta-D- GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc), an abundant HMO unique to human breast milk, releasing lacto-N-biose (LNB or beta-D-Gal-(1->3)-D- GlcNAc) and lactose. Is a key enzymatic factor for growth and proliferation of B.bifidum in the gut ecosystem of breast-fed infants (Probable). Has substrate preference for unmodified beta-linked LNB since it does not hydrolyze the fucosylated forms of lacto-N-tetraose (lacto-N-fucopentaose I and II) or lacto-N-neotetraose. Is also able to display transglycosylation activity in vitro.","This protein is an enzyme that breaks down complex molecules into simpler ones, specifically it is a hydrolase.",Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0004563; GO:0047403,GO:0016787,GO:0016787,,GO:0016787,GO:0016787,0.5807,0.5807,,0.5807,0.5807,4,0.5807,0.3102,no
LNBB_BIFB1,B3TLD6,Reference,Bacteria,1112,"Present in the infant gut, this enzyme is involved in the assimilation of type-1 human milk oligosaccharides (HMOs). It hydrolyzes via a retaining mechanism the beta-D-GlcNAc-(1->3)-beta-D- Gal linkage in lacto-N-tetraose (LNT or beta-D-Gal-(1->3)-beta-D- GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc), an abundant HMO unique to human breast milk, releasing lacto-N-biose (LNB or beta-D-Gal-(1->3)-D- GlcNAc) and lactose. Is a key enzymatic factor for growth and proliferation of B.bifidum in the gut ecosystem of breast-fed infants (Probable). Has substrate preference for unmodified beta-linked LNB since it does not hydrolyze the fucosylated forms of lacto-N-tetraose (lacto-N-fucopentaose I and II) or lacto-N-neotetraose. Is also able to display transglycosylation activity in vitro.","Present in the infant gut, this enzyme is involved in the assimilation of type-1 human milk oligosaccharides (HMOs). It hydrolyzes via a retaining mechanism the beta-D-GlcNAc-(1->3)-beta-D- Gal linkage in lacto-N-tetraose (LNT or beta-D-Gal-(1->3)-beta-D- GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc), an abundant HMO unique to human breast milk, releasing lacto-N-biose (LNB or beta-D-Gal-(1->3)-D- GlcNAc) and lactose. Is a key enzymatic factor for growth and proliferation of B.bifidum in the gut ecosystem of breast-fed infants (Probable). Has substrate preference for unmodified beta-linked LNB since it does not hydrolyze the fucosylated forms of lacto-N-tetraose (lacto-N-fucopentaose I and II) or lacto-N-neotetraose. Is also able to display transglycosylation activity in vitro.",,,,,,,GO:0004563; GO:0047403,GO:0047924; GO:0016757,GO:0004553,GO:0004553,GO:0004553,GO:0004553,0.2553,0.8234,0.8234,0.8234,0.8234,5,0.7098,0.3102,no
ACVA_PENRW,B6HLU1,ESM2Text,Eukaryota,3746,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic. The first step of the pathway is performed by the trimodular NRPS acvA that produces the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L- cysteinyl-D-valine (LLD-ACV or ACV) via condensation of the 3 residues L-2-aminoadipate, L-cysteine and L-valine. The precursor amino acids for penicillin biosynthesis are withdrawn from the vacuolar amino acid pool by the MFS-type transporter penV. Each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. The tripeptide ACV is then cyclized to form isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin. This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcs",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0050564; GO:0031177,GO:0016874,GO:0016874; GO:0005524,GO:0016874,,GO:0016874,0.3545,0.7125,0.3545,,0.3545,4,0.444,0.3451,no
ACVA_PENRW,B6HLU1,Prot2Text,Eukaryota,3746,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic. The first step of the pathway is performed by the trimodular NRPS acvA that produces the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L- cysteinyl-D-valine (LLD-ACV or ACV) via condensation of the 3 residues L-2-aminoadipate, L-cysteine and L-valine. The precursor amino acids for penicillin biosynthesis are withdrawn from the vacuolar amino acid pool by the MFS-type transporter penV. Each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. The tripeptide ACV is then cyclized to form isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin. This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcs",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0050564; GO:0031177,GO:0016874,,GO:0016874,GO:0016874,GO:0016874,0.3545,,0.3545,0.3545,0.3545,4,0.3545,0.3451,no
ACVA_PENRW,B6HLU1,ProtT3,Eukaryota,3746,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic. The first step of the pathway is performed by the trimodular NRPS acvA that produces the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L- cysteinyl-D-valine (LLD-ACV or ACV) via condensation of the 3 residues L-2-aminoadipate, L-cysteine and L-valine. The precursor amino acids for penicillin biosynthesis are withdrawn from the vacuolar amino acid pool by the MFS-type transporter penV. Each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. The tripeptide ACV is then cyclized to form isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin. This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively.",Nonribosomal peptide synthetase (NRPS); part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms,Yes,Yes,Yes,Maybe,Vague,Yes,GO:0005524; GO:0050564; GO:0031177,GO:0016874,GO:0016874,GO:0016874,GO:0016874,GO:0016874,0.3545,0.3545,0.3545,0.3545,0.3545,5,0.3545,0.3451,no
ACVA_PENRW,B6HLU1,ProtTale,Eukaryota,3746,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic. The first step of the pathway is performed by the trimodular NRPS acvA that produces the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L- cysteinyl-D-valine (LLD-ACV or ACV) via condensation of the 3 residues L-2-aminoadipate, L-cysteine and L-valine. The precursor amino acids for penicillin biosynthesis are withdrawn from the vacuolar amino acid pool by the MFS-type transporter penV. Each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. The tripeptide ACV is then cyclized to form isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin. This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3- hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0050564; GO:0031177,GO:0016874,GO:0016874,GO:0016874,,GO:0016874,0.3545,0.3545,0.3545,,0.3545,4,0.3545,0.3451,no
ACVA_PENRW,B6HLU1,Protein2Text,Eukaryota,3746,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic. The first step of the pathway is performed by the trimodular NRPS acvA that produces the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L- cysteinyl-D-valine (LLD-ACV or ACV) via condensation of the 3 residues L-2-aminoadipate, L-cysteine and L-valine. The precursor amino acids for penicillin biosynthesis are withdrawn from the vacuolar amino acid pool by the MFS-type transporter penV. Each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. The tripeptide ACV is then cyclized to form isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin. This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively.","The molecular function of this protein is not specified in the provided information. However, based on its name, it is likely that this protein is involved in the function of the mitochondria, specifically in the process of ATP synthesis or in the maintenance of the mitochondrial membrane potential. Further research would be needed to determine its specific molecular function.",No,No,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0050564; GO:0031177,,,,,,,,,,,0,,0.3451,no
ACVA_PENRW,B6HLU1,Reference,Eukaryota,3746,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic. The first step of the pathway is performed by the trimodular NRPS acvA that produces the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L- cysteinyl-D-valine (LLD-ACV or ACV) via condensation of the 3 residues L-2-aminoadipate, L-cysteine and L-valine. The precursor amino acids for penicillin biosynthesis are withdrawn from the vacuolar amino acid pool by the MFS-type transporter penV. Each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. The tripeptide ACV is then cyclized to form isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin. This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic. The first step of the pathway is performed by the trimodular NRPS acvA that produces the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L- cysteinyl-D-valine (LLD-ACV or ACV) via condensation of the 3 residues L-2-aminoadipate, L-cysteine and L-valine. The precursor amino acids for penicillin biosynthesis are withdrawn from the vacuolar amino acid pool by the MFS-type transporter penV. Each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. The tripeptide ACV is then cyclized to form isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin. This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively.",,,,,,,GO:0005524; GO:0050564; GO:0031177,GO:0016874; GO:0005524,GO:0016879,GO:0016874; GO:0005524,GO:0003824; GO:0016874,GO:0003824; GO:0016874; GO:0005524,0.7125,0.4096,0.7125,0.3856,0.6708,5,0.5782,0.3451,no
PP2C1_ASPFN,B8NLZ3,ESM2Text,Eukaryota,570,"Serine and threonine phosphatase. Dephosphorylates phosphoglycerate kinase pgk1 at least on 'Ser-203' to negatively regulate targeting of pgk1 to the mitochondrion, thereby negatively regulating production of acetyl-CoA and consequently aflatoxin biosynthesis.","Dephosphorylates and represses plasma membrane H(+)-ATPases (PM H(+)-ATPases, e.g. AHA1 and AHA2), thus influencing negatively plant growth and fitness.",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0046872; GO:0004722,GO:0004721,GO:0004721,GO:0004721,GO:0004721,GO:0004721,0.6347,0.6347,0.6347,0.6347,0.6347,5,0.6347,0.5711,yes
PP2C1_ASPFN,B8NLZ3,Prot2Text,Eukaryota,570,"Serine and threonine phosphatase. Dephosphorylates phosphoglycerate kinase pgk1 at least on 'Ser-203' to negatively regulate targeting of pgk1 to the mitochondrion, thereby negatively regulating production of acetyl-CoA and consequently aflatoxin biosynthesis.","Dephosphorylates CDKN1B at 'Thr-187', thus removing a signal for proteasomal degradation.",Maybe,Yes,Yes,Maybe,No,not-Yes,GO:0046872; GO:0004722,GO:0004721,GO:0004722,GO:0004722,GO:0004721,GO:0004721,0.6347,0.6942,0.6942,0.6347,0.6347,5,0.6585,0.5711,yes
PP2C1_ASPFN,B8NLZ3,ProtT3,Eukaryota,570,"Serine and threonine phosphatase. Dephosphorylates phosphoglycerate kinase pgk1 at least on 'Ser-203' to negatively regulate targeting of pgk1 to the mitochondrion, thereby negatively regulating production of acetyl-CoA and consequently aflatoxin biosynthesis.",Cytoplasm Nucleus. Belongs to the PP2C family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0046872; GO:0004722,GO:0004722,GO:0004722,GO:0004722,GO:0004722,GO:0004722,0.6942,0.6942,0.6942,0.6942,0.6942,5,0.6942,0.5711,yes
PP2C1_ASPFN,B8NLZ3,ProtTale,Eukaryota,570,"Serine and threonine phosphatase. Dephosphorylates phosphoglycerate kinase pgk1 at least on 'Ser-203' to negatively regulate targeting of pgk1 to the mitochondrion, thereby negatively regulating production of acetyl-CoA and consequently aflatoxin biosynthesis.","Inactive phosphatase that dephosphorylates and inactivates psp-1, psp-2, psp-3, psp-4, psp-5, psp-6, psp-7, psp-8, psp-9, psp-10, psp-11, psp-12, psp-13, psp-14, psp-15, psp-16, psp-17, psp-18, psp-19, psp-20, psp-21",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0046872; GO:0004722,,,,,,,,,,,0,,0.5711,yes
PP2C1_ASPFN,B8NLZ3,Protein2Text,Eukaryota,570,"Serine and threonine phosphatase. Dephosphorylates phosphoglycerate kinase pgk1 at least on 'Ser-203' to negatively regulate targeting of pgk1 to the mitochondrion, thereby negatively regulating production of acetyl-CoA and consequently aflatoxin biosynthesis.",The molecular function of this protein is a protein phosphatase.,Maybe,Maybe,Yes,Vague,Maybe,not-Yes,GO:0046872; GO:0004722,GO:0004721,GO:0004721,GO:0004721,GO:0004721,GO:0004721,0.6347,0.6347,0.6347,0.6347,0.6347,5,0.6347,0.5711,yes
PP2C1_ASPFN,B8NLZ3,Reference,Eukaryota,570,"Serine and threonine phosphatase. Dephosphorylates phosphoglycerate kinase pgk1 at least on 'Ser-203' to negatively regulate targeting of pgk1 to the mitochondrion, thereby negatively regulating production of acetyl-CoA and consequently aflatoxin biosynthesis.","Serine and threonine phosphatase. Dephosphorylates phosphoglycerate kinase pgk1 at least on 'Ser-203' to negatively regulate targeting of pgk1 to the mitochondrion, thereby negatively regulating production of acetyl-CoA and consequently aflatoxin biosynthesis.",,,,,,,GO:0046872; GO:0004722,GO:0004722,GO:0004722,GO:0004722,GO:0004722; GO:0016791,GO:0004722,0.6942,0.6942,0.6942,0.704,0.6942,5,0.6962,0.5711,yes
IYD_THENN,B9K712,ESM2Text,Bacteria,186,"Catalyzes the dehalogenation of halotyrosines such as 3- bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5- diiodo-L-tyrosine. Activity towards 2-iodophenol is weak.","Enzyme of the plastid non-mevalonate pathway for ATP degradation. It supplies the precursors necessary for DNA processing to the sites of non-mevalonate phosphohydrolase (viPIM) and purine-ribosomes. The enzyme catalyzes the ATP-dependent nucleation of a portion of a circular substrate spectrum, the ATP-dependent exchange of the substrate-binding site one strand for one strand of nucleotide mononucleotide (FMN). It is specific for NAD. The plastid non-mevalonate pathway is the major route of ATP degradation in eukaryotic cells.",No,No,No,No,No,not-Yes,GO:0010181; GO:0140616; GO:0072545,,,,,,,,,,,0,,0.227,no
IYD_THENN,B9K712,Prot2Text,Bacteria,186,"Catalyzes the dehalogenation of halotyrosines such as 3- bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5- diiodo-L-tyrosine. Activity towards 2-iodophenol is weak.","Reduction of a variety of nitroaromatic compounds using NADPH as source of reducing equivalents; two electrons are transferred. Involved in the reduction of nitrofurazone, a nitrofurazone produced by P.aeruginosa. Reduces nitrofurazone and nitrofurazone analogs such as 4-nitrofurazone and 2-nitrofurazone. Has no reduction activity towards nitrofurazone, nitrofurazone methyl ester, nitrofurazone methyl ester, nitrofurazone perchloride, nitrofurazone perchloride or nitrofurazone perchloride. Has no activity towards nitrofurazone, nitrofurazone perchloride, nitrofurazone perfuramide, nitrofuramide perfuramide or nitrospheroidene.",No,No,No,No,No,not-Yes,GO:0010181; GO:0140616; GO:0072545,GO:0016491,GO:0016657,GO:0016657,GO:0016491,GO:0018545,0.4033,0.0,0.0,0.4033,0.0,5,0.1613,0.227,no
IYD_THENN,B9K712,ProtT3,Bacteria,186,"Catalyzes the dehalogenation of halotyrosines such as 3- bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5- diiodo-L-tyrosine. Activity towards 2-iodophenol is weak.",Belongs to the nitroreductase family,Vague,Vague,No,Vague,Vague,not-Yes,GO:0010181; GO:0140616; GO:0072545,GO:0016657,GO:0016657,GO:0016657,GO:0016657,GO:0016491,0.0,0.0,0.0,0.0,0.4033,5,0.0807,0.227,no
IYD_THENN,B9K712,ProtTale,Bacteria,186,"Catalyzes the dehalogenation of halotyrosines such as 3- bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5- diiodo-L-tyrosine. Activity towards 2-iodophenol is weak.","Transforms 4-hydroxy-2-ketovalerate to (4R)-4-hydroxy-4-methyl-2- oxopentanoate [FAD-dependent]. Can also convert (4R,S)-4-hydroxy-4-methyl-2- oxopent-2-enoic acid to 4-hydroxy-4-methyl-2,4-pentadienoic acid [FAD-dependent]. Cannot use pyruvate as substrate.",No,No,No,No,No,not-Yes,GO:0010181; GO:0140616; GO:0072545,GO:0016491,GO:0016491,GO:0016491; GO:0071949,GO:0016491,GO:0016491; GO:0071949,0.4033,0.4033,0.625,0.4033,0.625,5,0.492,0.227,no
IYD_THENN,B9K712,Protein2Text,Bacteria,186,"Catalyzes the dehalogenation of halotyrosines such as 3- bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5- diiodo-L-tyrosine. Activity towards 2-iodophenol is weak.",This protein is involved in the molecular function of being a part of a bacterial system that may play a role in the degradation of nucleic acids.,No,No,No,No,No,not-Yes,GO:0010181; GO:0140616; GO:0072545,,,,,,,,,,,0,,0.227,no
IYD_THENN,B9K712,Reference,Bacteria,186,"Catalyzes the dehalogenation of halotyrosines such as 3- bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5- diiodo-L-tyrosine. Activity towards 2-iodophenol is weak.","Catalyzes the dehalogenation of halotyrosines such as 3- bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5- diiodo-L-tyrosine. Activity towards 2-iodophenol is weak.",,,,,,,GO:0010181; GO:0140616; GO:0072545,GO:0045548; GO:0016491,GO:0016491,GO:0019132,GO:0016491,GO:0016491,0.3697,0.4033,0.0,0.4033,0.4033,5,0.3159,0.227,no
PA2BD_CRODU,C0HM14,ESM2Text,Eukaryota,122,"Heterodimer CA-CB: Crotoxin is a potent presynaptic neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission. It consists of a non-covalent association of a basic and weakly toxic PLA2 subunit (CBa2, CBb, CBc, or CBd), with a small acidic, non- enzymatic and non-toxic subunit (CA1, CA2, CA3 or CA4). The complex acts by binding to a specific 48-kDa protein (R48) receptor located on presynaptic membranes, forming a transient ternary complex CA-CB-R48, followed by dissociation of the CA-CB complex and release of the CA subunit. At equilibrium, only the CB subunits remain associated with the specific crotoxin receptor. In addition to neurotoxicity, crotoxin has been found to exert myotoxicity, nephrotoxicity, and cardiovascular toxicity. Moreover, anti-inflammatory, immunomodulatory, anti-tumor and analgesic effects of crotoxin have also been reported.",Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005509; GO:0099106; GO:0005543; GO:0090729,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623,GO:0004623,GO:0004623,0.4467,0.4467,0.1088,0.1088,0.1088,5,0.244,0.2176,no
PA2BD_CRODU,C0HM14,Prot2Text,Eukaryota,122,"Heterodimer CA-CB: Crotoxin is a potent presynaptic neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission. It consists of a non-covalent association of a basic and weakly toxic PLA2 subunit (CBa2, CBb, CBc, or CBd), with a small acidic, non- enzymatic and non-toxic subunit (CA1, CA2, CA3 or CA4). The complex acts by binding to a specific 48-kDa protein (R48) receptor located on presynaptic membranes, forming a transient ternary complex CA-CB-R48, followed by dissociation of the CA-CB complex and release of the CA subunit. At equilibrium, only the CB subunits remain associated with the specific crotoxin receptor. In addition to neurotoxicity, crotoxin has been found to exert myotoxicity, nephrotoxicity, and cardiovascular toxicity. Moreover, anti-inflammatory, immunomodulatory, anti-tumor and analgesic effects of crotoxin have also been reported.",Snake venom phospholipase A2 (PLA2) that has myotoxic activity but no significant neurotoxicity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005509; GO:0099106; GO:0005543; GO:0090729,GO:0004623,GO:0004623,GO:0004623,GO:0004622,GO:0004623,0.1088,0.1088,0.1088,0.0975,0.1088,5,0.1065,0.2176,no
PA2BD_CRODU,C0HM14,ProtT3,Eukaryota,122,"Heterodimer CA-CB: Crotoxin is a potent presynaptic neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission. It consists of a non-covalent association of a basic and weakly toxic PLA2 subunit (CBa2, CBb, CBc, or CBd), with a small acidic, non- enzymatic and non-toxic subunit (CA1, CA2, CA3 or CA4). The complex acts by binding to a specific 48-kDa protein (R48) receptor located on presynaptic membranes, forming a transient ternary complex CA-CB-R48, followed by dissociation of the CA-CB complex and release of the CA subunit. At equilibrium, only the CB subunits remain associated with the specific crotoxin receptor. In addition to neurotoxicity, crotoxin has been found to exert myotoxicity, nephrotoxicity, and cardiovascular toxicity. Moreover, anti-inflammatory, immunomodulatory, anti-tumor and analgesic effects of crotoxin have also been reported.",PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Secreted. Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005509; GO:0099106; GO:0005543; GO:0090729,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623; GO:0046872,GO:0004623; GO:0005509,GO:0004623,0.4467,0.4467,0.414,0.4467,0.1088,5,0.3726,0.2176,no
PA2BD_CRODU,C0HM14,ProtTale,Eukaryota,122,"Heterodimer CA-CB: Crotoxin is a potent presynaptic neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission. It consists of a non-covalent association of a basic and weakly toxic PLA2 subunit (CBa2, CBb, CBc, or CBd), with a small acidic, non- enzymatic and non-toxic subunit (CA1, CA2, CA3 or CA4). The complex acts by binding to a specific 48-kDa protein (R48) receptor located on presynaptic membranes, forming a transient ternary complex CA-CB-R48, followed by dissociation of the CA-CB complex and release of the CA subunit. At equilibrium, only the CB subunits remain associated with the specific crotoxin receptor. In addition to neurotoxicity, crotoxin has been found to exert myotoxicity, nephrotoxicity, and cardiovascular toxicity. Moreover, anti-inflammatory, immunomodulatory, anti-tumor and analgesic effects of crotoxin have also been reported.",Snake venom phospholipase A2 (PLA2) that displays weak myotoxic activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005509; GO:0099106; GO:0005543; GO:0090729,GO:0004623,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623; GO:0005509,0.1088,0.4467,0.4467,0.4467,0.4467,5,0.3791,0.2176,no
PA2BD_CRODU,C0HM14,Protein2Text,Eukaryota,122,"Heterodimer CA-CB: Crotoxin is a potent presynaptic neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission. It consists of a non-covalent association of a basic and weakly toxic PLA2 subunit (CBa2, CBb, CBc, or CBd), with a small acidic, non- enzymatic and non-toxic subunit (CA1, CA2, CA3 or CA4). The complex acts by binding to a specific 48-kDa protein (R48) receptor located on presynaptic membranes, forming a transient ternary complex CA-CB-R48, followed by dissociation of the CA-CB complex and release of the CA subunit. At equilibrium, only the CB subunits remain associated with the specific crotoxin receptor. In addition to neurotoxicity, crotoxin has been found to exert myotoxicity, nephrotoxicity, and cardiovascular toxicity. Moreover, anti-inflammatory, immunomodulatory, anti-tumor and analgesic effects of crotoxin have also been reported.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its classification as a phospholipase, it is likely that the protein's molecular function involves catalyzing the hydrolysis of phospholipids. Specifically, it may catalyze the hydrolysis of phospholipids into fatty acids and other products, which can have various effects on cellular processes.",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005509; GO:0099106; GO:0005543; GO:0090729,GO:0004622,GO:0004623,GO:0004620,,GO:0004622,0.0975,0.1088,0.1279,,0.0975,4,0.1079,0.2176,no
PA2BD_CRODU,C0HM14,Reference,Eukaryota,122,"Heterodimer CA-CB: Crotoxin is a potent presynaptic neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission. It consists of a non-covalent association of a basic and weakly toxic PLA2 subunit (CBa2, CBb, CBc, or CBd), with a small acidic, non- enzymatic and non-toxic subunit (CA1, CA2, CA3 or CA4). The complex acts by binding to a specific 48-kDa protein (R48) receptor located on presynaptic membranes, forming a transient ternary complex CA-CB-R48, followed by dissociation of the CA-CB complex and release of the CA subunit. At equilibrium, only the CB subunits remain associated with the specific crotoxin receptor. In addition to neurotoxicity, crotoxin has been found to exert myotoxicity, nephrotoxicity, and cardiovascular toxicity. Moreover, anti-inflammatory, immunomodulatory, anti-tumor and analgesic effects of crotoxin have also been reported.","Heterodimer CA-CB: Crotoxin is a potent presynaptic neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission. It consists of a non-covalent association of a basic and weakly toxic PLA2 subunit (CBa2, CBb, CBc, or CBd), with a small acidic, non- enzymatic and non-toxic subunit (CA1, CA2, CA3 or CA4). The complex acts by binding to a specific 48-kDa protein (R48) receptor located on presynaptic membranes, forming a transient ternary complex CA-CB-R48, followed by dissociation of the CA-CB complex and release of the CA subunit. At equilibrium, only the CB subunits remain associated with the specific crotoxin receptor. In addition to neurotoxicity, crotoxin has been found to exert myotoxicity, nephrotoxicity, and cardiovascular toxicity. Moreover, anti-inflammatory, immunomodulatory, anti-tumor and analgesic effects of crotoxin have also been reported.",,,,,,,GO:0005509; GO:0099106; GO:0005543; GO:0090729,GO:0004623,GO:0004623; GO:0090729,GO:0004623; GO:0090729,GO:0004622; GO:0016298,GO:0004623,0.1088,0.4744,0.4744,0.1614,0.1088,5,0.2656,0.2176,no
OXDD_TALTH,C0HMB0,ESM2Text,Eukaryota,370,Selectively catalyzes the oxidative deamination of acidic amino acids. Protects the organism from the toxicity of D-amino acids. Enables the organism to utilize D- amino acids as a source of nutrients.,Degrades both double-stranded and single-stranded DNA.,No,No,No,No,No,not-Yes,GO:0008445; GO:0071949,GO:0004518,GO:0004536,GO:0004536,GO:0004536,GO:0004536,0.1843,0.1364,0.1364,0.1364,0.1364,5,0.146,0.1803,no
OXDD_TALTH,C0HMB0,Prot2Text,Eukaryota,370,Selectively catalyzes the oxidative deamination of acidic amino acids. Protects the organism from the toxicity of D-amino acids. Enables the organism to utilize D- amino acids as a source of nutrients.,"Oxidizes L-pipecolate and L-proline. Can also use D-glucose as substrate, but with less efficiency. Can also oxidize other primary amino acids, including D-lysine.",No,No,No,No,No,not-Yes,GO:0008445; GO:0071949,GO:0016491,,GO:0016491,GO:0016491,GO:0050031,0.3665,,0.3665,0.3665,0.1971,4,0.3241,0.1803,no
OXDD_TALTH,C0HMB0,ProtT3,Eukaryota,370,Selectively catalyzes the oxidative deamination of acidic amino acids. Protects the organism from the toxicity of D-amino acids. Enables the organism to utilize D- amino acids as a source of nutrients.,Cytoplasm. Belongs to the aldehyde dehydrogenase family,No,No,No,No,Vague,not-Yes,GO:0008445; GO:0071949,GO:0016620,GO:0004029,GO:0004029,GO:0016620,GO:0016620,0.2362,0.1681,0.1681,0.2362,0.2362,5,0.209,0.1803,no
OXDD_TALTH,C0HMB0,ProtTale,Eukaryota,370,Selectively catalyzes the oxidative deamination of acidic amino acids. Protects the organism from the toxicity of D-amino acids. Enables the organism to utilize D- amino acids as a source of nutrients.,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Enables the organism to utilize D-amino acids as a source of nutrients.,Yes,Yes,Maybe,Maybe,Yes,Yes,GO:0008445; GO:0071949,GO:0003884,GO:0003863,GO:0003884,GO:0003863,GO:0003884,0.6047,0.1971,0.6047,0.1971,0.6047,5,0.4417,0.1803,no
OXDD_TALTH,C0HMB0,Protein2Text,Eukaryota,370,Selectively catalyzes the oxidative deamination of acidic amino acids. Protects the organism from the toxicity of D-amino acids. Enables the organism to utilize D- amino acids as a source of nutrients.,"The molecular function of this protein is an aminotransferase. It is involved in the transfer of an amino group from an amino acid to an alpha-keto acid. More specifically, it is involved in the degradation of L-arginine, and it catalyzes the transfer of the amino group from L-arginine to 2-oxoglutarate to form L-glutamate semialdehyde and urea.",No,No,No,No,No,not-Yes,GO:0008445; GO:0071949,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.1504,0.1504,0.1504,0.1504,0.1504,5,0.1504,0.1803,no
OXDD_TALTH,C0HMB0,Reference,Eukaryota,370,Selectively catalyzes the oxidative deamination of acidic amino acids. Protects the organism from the toxicity of D-amino acids. Enables the organism to utilize D- amino acids as a source of nutrients.,Selectively catalyzes the oxidative deamination of acidic amino acids. Protects the organism from the toxicity of D-amino acids. Enables the organism to utilize D- amino acids as a source of nutrients.,,,,,,,GO:0008445; GO:0071949,GO:0004138,GO:0033182,GO:0033971,GO:0033971,GO:0033734,0.0936,0.0,0.1258,0.1258,0.1971,5,0.1085,0.1803,no
FABH_LISM4,C0LNR0,ESM2Text,Bacteria,312,"Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Can use branched- chain acyl-CoAs, with a preference for 2-methylbutanoyl-CoA, the precursor of odd-numbered anteiso fatty acids, at 30 degrees Celsius, which is further increased at a low temperature. Shows weak activity with acetyl-CoA.",Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004315; GO:0033818,GO:0004315,GO:0004315,GO:0004315,GO:0004315,GO:0004315,0.9096,0.9096,0.9096,0.9096,0.9096,5,0.9096,0.3785,no
FABH_LISM4,C0LNR0,Prot2Text,Bacteria,312,"Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Can use branched- chain acyl-CoAs, with a preference for 2-methylbutanoyl-CoA, the precursor of odd-numbered anteiso fatty acids, at 30 degrees Celsius, which is further increased at a low temperature. Shows weak activity with acetyl-CoA.",Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004315; GO:0033818,GO:0004315,GO:0004315,GO:0004315,GO:0004312; GO:0004314,GO:0004315,0.9096,0.9096,0.9096,0.6766,0.9096,5,0.863,0.3785,no
FABH_LISM4,C0LNR0,ProtT3,Bacteria,312,"Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Can use branched- chain acyl-CoAs, with a preference for 2-methylbutanoyl-CoA, the precursor of odd-numbered anteiso fatty acids, at 30 degrees Celsius, which is further increased at a low temperature. Shows weak activity with acetyl-CoA.",Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids. Cytoplasm. Belongs to the thiolase-like superfamily. FabH family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004315; GO:0033818,GO:0004315,GO:0004315,GO:0004315,GO:0004315,GO:0004315,0.9096,0.9096,0.9096,0.9096,0.9096,5,0.9096,0.3785,no
FABH_LISM4,C0LNR0,ProtTale,Bacteria,312,"Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Can use branched- chain acyl-CoAs, with a preference for 2-methylbutanoyl-CoA, the precursor of odd-numbered anteiso fatty acids, at 30 degrees Celsius, which is further increased at a low temperature. Shows weak activity with acetyl-CoA.",Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004315; GO:0033818,GO:0004315,GO:0004315,GO:0004315,GO:0004315,GO:0004315,0.9096,0.9096,0.9096,0.9096,0.9096,5,0.9096,0.3785,no
FABH_LISM4,C0LNR0,Protein2Text,Bacteria,312,"Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Can use branched- chain acyl-CoAs, with a preference for 2-methylbutanoyl-CoA, the precursor of odd-numbered anteiso fatty acids, at 30 degrees Celsius, which is further increased at a low temperature. Shows weak activity with acetyl-CoA.","The molecular function of this protein is an acyl transferase enzyme, which catalyzes the condensation reaction of fatty acid CoA catalysis to produce fatty acyl-ACP. It is involved in the biosynthesis of fatty acids. 
In more detail, it catalyzes the condensation of acetyl CoA with acyl-ACP to produce malonyl-ACP. It is part of the fatty acid synthesis type I large multifunctional protein. This protein has both acyl carrier protein and enoyl reductase activities. 
This protein is also involved in the biosynthesis of polyketides, which are a class of compounds that includes many important antibiotics, antifungals, and other drugs. Polyketides are synthesized by the condensation of acetyl-CoA and malonyl-CoA units. The polyketide synthase (PKS) enzyme catalyzes this condensation reaction, and the product is a polyketide chain that is then modified by various enzymes to produce the final compound. 

It is worth noting that the specific function of this protein can vary depending on the organism in which it is found. In some organisms, it may be involved in the biosynthesis of specific fatty acids or polyketides, while in others it may have a more general role in fatty acid or polyketide biosynthesis. 

In general, the molecular function of this protein is to catalyze the condensation of acetyl-CoA and malonyl-CoA units to produce a polyketide chain, which is then modified by various enzymes to produce the final compound. 

This protein is a key enzyme in the biosynthesis of many important compounds, including antibiotics, antifungals, and other drugs. It is also involved in the biosynthesis of fatty acids, which are important components of cellular membranes. 

In summary, the molecular function of this protein is to catalyze the condensation of acetyl-CoA and malonyl-CoA units to produce a polyketide chain, which is then modified by various enzymes to produce the final compound. 

The specific function of this protein can vary depending on the organism in which it is found. In some organisms, it may be involved in the biosynthesis of specific fatty acids or polyketides, while in others it may have a more general role in fatty acid or polyketide biosynthesis. 

The molecular function of this protein is critical for the production of many important compounds, including antibiotics, antifungals, and other",Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0033818,,,GO:0016747,GO:0016746,GO:0016746,,,0.8582,0.729,0.729,3,0.7721,0.3785,no
FABH_LISM4,C0LNR0,Reference,Bacteria,312,"Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Can use branched- chain acyl-CoAs, with a preference for 2-methylbutanoyl-CoA, the precursor of odd-numbered anteiso fatty acids, at 30 degrees Celsius, which is further increased at a low temperature. Shows weak activity with acetyl-CoA.","Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Can use branched- chain acyl-CoAs, with a preference for 2-methylbutanoyl-CoA, the precursor of odd-numbered anteiso fatty acids, at 30 degrees Celsius, which is further increased at a low temperature. Shows weak activity with acetyl-CoA.",,,,,,,GO:0004315; GO:0033818,GO:0004315; GO:0016747,GO:0004315,GO:0004315,GO:0004315; GO:0016746,GO:0004315,0.9291,0.9096,0.9096,0.8645,0.9096,5,0.9045,0.3785,no
DHOM_PARBD,C1G1C3,ESM2Text,Eukaryota,372,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of amino acids that derive from aspartate (the aspartate family of amino acids), including methioinine and threonine, the latter of which is a precursor to isoleucine; production of homoserine leads to a branch- point in the pathway as it can either be O-phosphorylated for processing to threonine, or O-acylated for processing to methionine.",Involved in both the arginine and lysine biosynthetic pathways.,Vague,Vague,Vague,No,No,not-Yes,GO:0004412; GO:0046872; GO:0050661,,,,,,,,,,,0,,0.2388,no
DHOM_PARBD,C1G1C3,Prot2Text,Eukaryota,372,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of amino acids that derive from aspartate (the aspartate family of amino acids), including methioinine and threonine, the latter of which is a precursor to isoleucine; production of homoserine leads to a branch- point in the pathway as it can either be O-phosphorylated for processing to threonine, or O-acylated for processing to methionine.",Involved in osmoadaptation.,Vague,Vague,Vague,No,No,not-Yes,GO:0004412; GO:0046872; GO:0050661,,,,,,,,,,,0,,0.2388,no
DHOM_PARBD,C1G1C3,ProtT3,Eukaryota,372,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of amino acids that derive from aspartate (the aspartate family of amino acids), including methioinine and threonine, the latter of which is a precursor to isoleucine; production of homoserine leads to a branch- point in the pathway as it can either be O-phosphorylated for processing to threonine, or O-acylated for processing to methionine.",Belongs to the homoserine dehydrogenase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004412; GO:0046872; GO:0050661,GO:0004412,GO:0004412,GO:0004412,GO:0004412,GO:0004412,0.5398,0.5398,0.5398,0.5398,0.5398,5,0.5398,0.2388,no
DHOM_PARBD,C1G1C3,ProtTale,Eukaryota,372,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of amino acids that derive from aspartate (the aspartate family of amino acids), including methioinine and threonine, the latter of which is a precursor to isoleucine; production of homoserine leads to a branch- point in the pathway as it can either be O-phosphorylated for processing to threonine, or O-acylated for processing to methionine.","Catalyzes the oxidation of L-aspartate to iminoaspartate, the first step in the de novo biosynthesis of NAD.",No,No,No,No,No,not-Yes,GO:0004412; GO:0046872; GO:0050661,GO:0008734,GO:0008734,GO:0008734,GO:0000535,GO:0008734,0.1609,0.1609,0.1609,0.0,0.1609,5,0.1287,0.2388,no
DHOM_PARBD,C1G1C3,Protein2Text,Eukaryota,372,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of amino acids that derive from aspartate (the aspartate family of amino acids), including methioinine and threonine, the latter of which is a precursor to isoleucine; production of homoserine leads to a branch- point in the pathway as it can either be O-phosphorylated for processing to threonine, or O-acylated for processing to methionine.","Based on the name ""malate dehydrogenase"", this protein is involved in the catalysis of the oxidation of malate to oxaloacetate, which is a key step in the citric acid cycle. The molecular function of this protein is therefore:

Catalytic activity: malate:oxaloacetate oxidoreductase (NAD+) (EC 1.1.1.37).",No,No,No,No,No,not-Yes,GO:0004412; GO:0046872; GO:0050661,GO:0004460,GO:0004460,GO:0016615,GO:0030060,GO:0004460,0.2478,0.2478,0.3484,0.3649,0.2478,5,0.2913,0.2388,no
DHOM_PARBD,C1G1C3,Reference,Eukaryota,372,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of amino acids that derive from aspartate (the aspartate family of amino acids), including methioinine and threonine, the latter of which is a precursor to isoleucine; production of homoserine leads to a branch- point in the pathway as it can either be O-phosphorylated for processing to threonine, or O-acylated for processing to methionine.","Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of amino acids that derive from aspartate (the aspartate family of amino acids), including methioinine and threonine, the latter of which is a precursor to isoleucine; production of homoserine leads to a branch- point in the pathway as it can either be O-phosphorylated for processing to threonine, or O-acylated for processing to methionine.",,,,,,,GO:0004412; GO:0046872; GO:0050661,GO:0004412,GO:0004412,GO:0004412,GO:0004412,GO:0004412,0.5398,0.5398,0.5398,0.5398,0.5398,5,0.5398,0.2388,no
GLG_KOMPG,C4R941,ESM2Text,Eukaryota,409,"Glycogenin participates in the glycogen biosynthetic process along with glycogen synthase and glycogen branching enzyme. It catalyzes the formation of a short alpha (1,4)- glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase.","Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0008466; GO:0046872,GO:0016757,GO:0008466,GO:0008466,GO:0004345,GO:0008466,0.4115,0.689,0.689,0.1302,0.689,5,0.5217,0.4971,no
GLG_KOMPG,C4R941,Prot2Text,Eukaryota,409,"Glycogenin participates in the glycogen biosynthetic process along with glycogen synthase and glycogen branching enzyme. It catalyzes the formation of a short alpha (1,4)- glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase.",Self-glucosylating initiator of glycogen synthesis. Hydrolyzes the penultimate step of the initiation of protein N-glycosylation. May also participate in the glycosylation of other proteins in the same cell wall.,Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0008466; GO:0046872,GO:0008466,GO:0008466,GO:0008466,GO:0004553; GO:0016757,GO:0004373,0.689,0.689,0.689,0.3533,0.5176,5,0.5876,0.4971,no
GLG_KOMPG,C4R941,ProtT3,Eukaryota,409,"Glycogenin participates in the glycogen biosynthetic process along with glycogen synthase and glycogen branching enzyme. It catalyzes the formation of a short alpha (1,4)- glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase.",Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008466; GO:0046872,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.4115,0.4115,0.4115,0.4115,0.4115,5,0.4115,0.4971,no
GLG_KOMPG,C4R941,ProtTale,Eukaryota,409,"Glycogenin participates in the glycogen biosynthetic process along with glycogen synthase and glycogen branching enzyme. It catalyzes the formation of a short alpha (1,4)- glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase.","Glycosyltransferase involved in the biosynthesis of mannosylglucosylceramide (MGC), a membrane lipid essential for the integrity of the lysosomal membrane. Catalyzes the transfer of the glucose moiety from UDP-glucose to the glucosylceramide precursor alpha-D-glucosyl-(1<->1')-alpha-D-glucosyl-(1<->1')-myo-inositol (glucosylceramide), forming glucosylsphingosine (GlcSph). Also catalyzes the transfer of glucose from UDP-glucose to glucosylceramide,",No,Maybe,No,No,Maybe,not-Yes,GO:0008466; GO:0046872,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.4115,0.4115,0.4115,0.4115,0.4115,5,0.4115,0.4971,no
GLG_KOMPG,C4R941,Protein2Text,Eukaryota,409,"Glycogenin participates in the glycogen biosynthetic process along with glycogen synthase and glycogen branching enzyme. It catalyzes the formation of a short alpha (1,4)- glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase.","The molecular function of this protein is as a beta-galactoside alpha-1,3-galactosyltransferase. It is involved in the synthesis of galactose-alpha-1,3-galactose disaccharides from lactose (a disaccharide formed from glucose and galactose) on cell surface glycoproteins and glycolipids.",No,No,No,No,No,not-Yes,GO:0008466; GO:0046872,GO:0008378,GO:0046921,,GO:0008378,GO:0046921,0.3869,0.3331,,0.3869,0.3331,4,0.36,0.4971,no
GLG_KOMPG,C4R941,Reference,Eukaryota,409,"Glycogenin participates in the glycogen biosynthetic process along with glycogen synthase and glycogen branching enzyme. It catalyzes the formation of a short alpha (1,4)- glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase.","Glycogenin participates in the glycogen biosynthetic process along with glycogen synthase and glycogen branching enzyme. It catalyzes the formation of a short alpha (1,4)- glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase.",,,,,,,GO:0008466; GO:0046872,GO:0008466,GO:0016757,GO:0008466,GO:0004362; GO:0016757,GO:0004373; GO:0016757,0.689,0.4115,0.689,0.3448,0.5429,5,0.5354,0.4971,no
MRDA_ACIB2,D0C8Z9,ESM2Text,Bacteria,672,Catalyzes cross-linking of the peptidoglycan cell wall. Involved in the determination of the rod shape of the cell.,Catalyzes cross-linking of the peptidoglycan cell wall.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008658; GO:0071972; GO:0009002; GO:0008270,GO:0008233,GO:0016755,,,GO:0008233,0.3606,0.1226,,,0.3606,3,0.2813,0.5569,yes
MRDA_ACIB2,D0C8Z9,Prot2Text,Bacteria,672,Catalyzes cross-linking of the peptidoglycan cell wall. Involved in the determination of the rod shape of the cell.,Catalyzes cross-linking of the peptidoglycan cell wall at the division septum.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008658; GO:0071972; GO:0009002; GO:0008270,GO:0016755,GO:0008955,GO:0008658,GO:0008955,GO:0008955,0.1226,0.1035,0.4814,0.1035,0.1035,5,0.1829,0.5569,yes
MRDA_ACIB2,D0C8Z9,ProtT3,Bacteria,672,Catalyzes cross-linking of the peptidoglycan cell wall. Involved in the determination of the rod shape of the cell.,Catalyzes cross-linking of the peptidoglycan cell wall at the division septum. Cell inner membrane; Single-pass type II membrane protein. Belongs to the transpeptidase family. FtsI subfamily,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008658; GO:0071972; GO:0009002; GO:0008270,GO:0016755,GO:0008233,GO:0008233,GO:0008658,GO:0008658,0.1226,0.3606,0.3606,0.4814,0.4814,5,0.3613,0.5569,yes
MRDA_ACIB2,D0C8Z9,ProtTale,Bacteria,672,Catalyzes cross-linking of the peptidoglycan cell wall. Involved in the determination of the rod shape of the cell.,Peptidoglycan polymerase that is essential for cell division.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008658; GO:0071972; GO:0009002; GO:0008270,GO:0008955,GO:0008955,GO:0008955,GO:0016757,GO:0008955,0.1035,0.1035,0.1035,0.1486,0.1035,5,0.1125,0.5569,yes
MRDA_ACIB2,D0C8Z9,Protein2Text,Bacteria,672,Catalyzes cross-linking of the peptidoglycan cell wall. Involved in the determination of the rod shape of the cell.,"This protein is a serine protease. It catalyzes the hydrolysis of peptide bonds, specifically cleaving the peptide bond between the amino acid phenylalanine and the amino acid glycine in the bacterial cell wall recycling pathway.",No,No,No,No,No,not-Yes,GO:0008658; GO:0071972; GO:0009002; GO:0008270,GO:0004252,GO:0004252,GO:0008236,GO:0004252,GO:0004252,0.3473,0.3473,0.4305,0.3473,0.3473,5,0.3639,0.5569,yes
MRDA_ACIB2,D0C8Z9,Reference,Bacteria,672,Catalyzes cross-linking of the peptidoglycan cell wall. Involved in the determination of the rod shape of the cell.,Catalyzes cross-linking of the peptidoglycan cell wall. Involved in the determination of the rod shape of the cell.,,,,,,,GO:0008658; GO:0071972; GO:0009002; GO:0008270,GO:0008658,GO:0016755,,GO:0008955,GO:0008955,0.4814,0.1226,,0.1035,0.1035,4,0.2027,0.5569,yes
UBP12_RAT,D0RB01,ESM2Text,Eukaryota,370,"Deubiquitinating enzyme that plays various roles in the regulation of the immune response and inflammation. During TCR engagement and activation, translocates into the cytoplasm and deubiquitinates its substrates LAT and TRAT1 and prevents their lysosome-dependent degradation to stabilize the TCR signaling complex at the plasma membrane. Plays an essential role in the selective LPS- induced macrophage response through the activation of NF-kappa-B pathway. In addition, promotes that antiviral immune response through targeting DNA sensor IFI16 to inhibit its proteasome-dependent degradation. Participates in the interferon signaling pathway and antiviral response independently of its deubiquitinase activity by maintaining nuclear phosphorylated STAT1 levels via inhibition of its CREBBP-mediated acetylation and subsequent dephosphorylation. Plays an intrinsic role in promoting the differentiation, activation and proliferation of CD4(+) T-cell by activating the NF- kappa-B signaling pathway through deubiquitinating and stabilizing B- cell lymphoma/leukemia 10/BCL10. In myeloid-derived suppressor cells promotes the activation of the NF-kappa-B via deubiquitination and stabilization of RELA. Regulates the 'Lys-63'-linked polyubiquitin chains of BAX and thereby modulates the mitochondrial apoptotic process. Negative regulator of NOTCH signaling that specifically deubiquitinates non-activated NOTCH receptors to target them for lysosomal degradation; deubiquitination of NOTCH stimulates its transport form late endosomes to lysosomes. Protects neurons against HTT/huntingtin- induced polyglutamine expansion-dependent neurodegeneration through regulation of autophagic flux. This function is independent of deubiquitinase activity or of other components of the USP12-WDR20-WDR48 deubiquitinating complex. In complex with WDR48, acts as a potential tumor suppressor by positively regulating PHLPP1 stability.",Deubiquitinating enzyme. Has almost no deubiquitinating activity by itself and requires the interaction with wdr48 to have a high activity.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004843; GO:0004197; GO:0101005; GO:0046872,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,0.6978,0.6978,0.6978,0.6978,0.6978,5,0.6978,0.8,yes
UBP12_RAT,D0RB01,Prot2Text,Eukaryota,370,"Deubiquitinating enzyme that plays various roles in the regulation of the immune response and inflammation. During TCR engagement and activation, translocates into the cytoplasm and deubiquitinates its substrates LAT and TRAT1 and prevents their lysosome-dependent degradation to stabilize the TCR signaling complex at the plasma membrane. Plays an essential role in the selective LPS- induced macrophage response through the activation of NF-kappa-B pathway. In addition, promotes that antiviral immune response through targeting DNA sensor IFI16 to inhibit its proteasome-dependent degradation. Participates in the interferon signaling pathway and antiviral response independently of its deubiquitinase activity by maintaining nuclear phosphorylated STAT1 levels via inhibition of its CREBBP-mediated acetylation and subsequent dephosphorylation. Plays an intrinsic role in promoting the differentiation, activation and proliferation of CD4(+) T-cell by activating the NF- kappa-B signaling pathway through deubiquitinating and stabilizing B- cell lymphoma/leukemia 10/BCL10. In myeloid-derived suppressor cells promotes the activation of the NF-kappa-B via deubiquitination and stabilization of RELA. Regulates the 'Lys-63'-linked polyubiquitin chains of BAX and thereby modulates the mitochondrial apoptotic process. Negative regulator of NOTCH signaling that specifically deubiquitinates non-activated NOTCH receptors to target them for lysosomal degradation; deubiquitination of NOTCH stimulates its transport form late endosomes to lysosomes. Protects neurons against HTT/huntingtin- induced polyglutamine expansion-dependent neurodegeneration through regulation of autophagic flux. This function is independent of deubiquitinase activity or of other components of the USP12-WDR20-WDR48 deubiquitinating complex. In complex with WDR48, acts as a potential tumor suppressor by positively regulating PHLPP1 stability.",Deubiquitinating enzyme. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity. Not involved in deubiquitination of monoubiquitinated FANCD2.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004843; GO:0004197; GO:0101005; GO:0046872,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,0.6978,0.6978,0.6978,0.6978,0.6978,5,0.6978,0.8,yes
UBP12_RAT,D0RB01,ProtT3,Eukaryota,370,"Deubiquitinating enzyme that plays various roles in the regulation of the immune response and inflammation. During TCR engagement and activation, translocates into the cytoplasm and deubiquitinates its substrates LAT and TRAT1 and prevents their lysosome-dependent degradation to stabilize the TCR signaling complex at the plasma membrane. Plays an essential role in the selective LPS- induced macrophage response through the activation of NF-kappa-B pathway. In addition, promotes that antiviral immune response through targeting DNA sensor IFI16 to inhibit its proteasome-dependent degradation. Participates in the interferon signaling pathway and antiviral response independently of its deubiquitinase activity by maintaining nuclear phosphorylated STAT1 levels via inhibition of its CREBBP-mediated acetylation and subsequent dephosphorylation. Plays an intrinsic role in promoting the differentiation, activation and proliferation of CD4(+) T-cell by activating the NF- kappa-B signaling pathway through deubiquitinating and stabilizing B- cell lymphoma/leukemia 10/BCL10. In myeloid-derived suppressor cells promotes the activation of the NF-kappa-B via deubiquitination and stabilization of RELA. Regulates the 'Lys-63'-linked polyubiquitin chains of BAX and thereby modulates the mitochondrial apoptotic process. Negative regulator of NOTCH signaling that specifically deubiquitinates non-activated NOTCH receptors to target them for lysosomal degradation; deubiquitination of NOTCH stimulates its transport form late endosomes to lysosomes. Protects neurons against HTT/huntingtin- induced polyglutamine expansion-dependent neurodegeneration through regulation of autophagic flux. This function is independent of deubiquitinase activity or of other components of the USP12-WDR20-WDR48 deubiquitinating complex. In complex with WDR48, acts as a potential tumor suppressor by positively regulating PHLPP1 stability.","Deubiquitinating enzyme. Has deubiquitinating activity towards 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (in vitro). Has deubiquitinating activity towards 'Lys-11'- and 'Lys-48'-linked polyubiquitin chains, but not 'Lys-63'-linked polyubiquitin chains (in vitro). Belongs to the peptidase C19 family. USP12/UBP4 subfamily",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004843; GO:0004197; GO:0101005; GO:0046872,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,0.6978,0.6978,0.6978,0.6978,0.6978,5,0.6978,0.8,yes
UBP12_RAT,D0RB01,ProtTale,Eukaryota,370,"Deubiquitinating enzyme that plays various roles in the regulation of the immune response and inflammation. During TCR engagement and activation, translocates into the cytoplasm and deubiquitinates its substrates LAT and TRAT1 and prevents their lysosome-dependent degradation to stabilize the TCR signaling complex at the plasma membrane. Plays an essential role in the selective LPS- induced macrophage response through the activation of NF-kappa-B pathway. In addition, promotes that antiviral immune response through targeting DNA sensor IFI16 to inhibit its proteasome-dependent degradation. Participates in the interferon signaling pathway and antiviral response independently of its deubiquitinase activity by maintaining nuclear phosphorylated STAT1 levels via inhibition of its CREBBP-mediated acetylation and subsequent dephosphorylation. Plays an intrinsic role in promoting the differentiation, activation and proliferation of CD4(+) T-cell by activating the NF- kappa-B signaling pathway through deubiquitinating and stabilizing B- cell lymphoma/leukemia 10/BCL10. In myeloid-derived suppressor cells promotes the activation of the NF-kappa-B via deubiquitination and stabilization of RELA. Regulates the 'Lys-63'-linked polyubiquitin chains of BAX and thereby modulates the mitochondrial apoptotic process. Negative regulator of NOTCH signaling that specifically deubiquitinates non-activated NOTCH receptors to target them for lysosomal degradation; deubiquitination of NOTCH stimulates its transport form late endosomes to lysosomes. Protects neurons against HTT/huntingtin- induced polyglutamine expansion-dependent neurodegeneration through regulation of autophagic flux. This function is independent of deubiquitinase activity or of other components of the USP12-WDR20-WDR48 deubiquitinating complex. In complex with WDR48, acts as a potential tumor suppressor by positively regulating PHLPP1 stability.",Deubiquitinating enzyme that removes conjugated ubiquitin from target proteins.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004843; GO:0004197; GO:0101005; GO:0046872,GO:0004843,GO:0004843,GO:0101005,GO:0036459,GO:0004843,0.6978,0.6978,0.6844,0.6978,0.6978,5,0.6951,0.8,yes
UBP12_RAT,D0RB01,Protein2Text,Eukaryota,370,"Deubiquitinating enzyme that plays various roles in the regulation of the immune response and inflammation. During TCR engagement and activation, translocates into the cytoplasm and deubiquitinates its substrates LAT and TRAT1 and prevents their lysosome-dependent degradation to stabilize the TCR signaling complex at the plasma membrane. Plays an essential role in the selective LPS- induced macrophage response through the activation of NF-kappa-B pathway. In addition, promotes that antiviral immune response through targeting DNA sensor IFI16 to inhibit its proteasome-dependent degradation. Participates in the interferon signaling pathway and antiviral response independently of its deubiquitinase activity by maintaining nuclear phosphorylated STAT1 levels via inhibition of its CREBBP-mediated acetylation and subsequent dephosphorylation. Plays an intrinsic role in promoting the differentiation, activation and proliferation of CD4(+) T-cell by activating the NF- kappa-B signaling pathway through deubiquitinating and stabilizing B- cell lymphoma/leukemia 10/BCL10. In myeloid-derived suppressor cells promotes the activation of the NF-kappa-B via deubiquitination and stabilization of RELA. Regulates the 'Lys-63'-linked polyubiquitin chains of BAX and thereby modulates the mitochondrial apoptotic process. Negative regulator of NOTCH signaling that specifically deubiquitinates non-activated NOTCH receptors to target them for lysosomal degradation; deubiquitination of NOTCH stimulates its transport form late endosomes to lysosomes. Protects neurons against HTT/huntingtin- induced polyglutamine expansion-dependent neurodegeneration through regulation of autophagic flux. This function is independent of deubiquitinase activity or of other components of the USP12-WDR20-WDR48 deubiquitinating complex. In complex with WDR48, acts as a potential tumor suppressor by positively regulating PHLPP1 stability.","The molecular function of this protein is a deubiquitinase, which means it removes ubiquitin from other proteins.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004843; GO:0004197; GO:0101005; GO:0046872,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,0.6978,0.6978,0.6978,0.6978,0.6978,5,0.6978,0.8,yes
UBP12_RAT,D0RB01,Reference,Eukaryota,370,"Deubiquitinating enzyme that plays various roles in the regulation of the immune response and inflammation. During TCR engagement and activation, translocates into the cytoplasm and deubiquitinates its substrates LAT and TRAT1 and prevents their lysosome-dependent degradation to stabilize the TCR signaling complex at the plasma membrane. Plays an essential role in the selective LPS- induced macrophage response through the activation of NF-kappa-B pathway. In addition, promotes that antiviral immune response through targeting DNA sensor IFI16 to inhibit its proteasome-dependent degradation. Participates in the interferon signaling pathway and antiviral response independently of its deubiquitinase activity by maintaining nuclear phosphorylated STAT1 levels via inhibition of its CREBBP-mediated acetylation and subsequent dephosphorylation. Plays an intrinsic role in promoting the differentiation, activation and proliferation of CD4(+) T-cell by activating the NF- kappa-B signaling pathway through deubiquitinating and stabilizing B- cell lymphoma/leukemia 10/BCL10. In myeloid-derived suppressor cells promotes the activation of the NF-kappa-B via deubiquitination and stabilization of RELA. Regulates the 'Lys-63'-linked polyubiquitin chains of BAX and thereby modulates the mitochondrial apoptotic process. Negative regulator of NOTCH signaling that specifically deubiquitinates non-activated NOTCH receptors to target them for lysosomal degradation; deubiquitination of NOTCH stimulates its transport form late endosomes to lysosomes. Protects neurons against HTT/huntingtin- induced polyglutamine expansion-dependent neurodegeneration through regulation of autophagic flux. This function is independent of deubiquitinase activity or of other components of the USP12-WDR20-WDR48 deubiquitinating complex. In complex with WDR48, acts as a potential tumor suppressor by positively regulating PHLPP1 stability.","Deubiquitinating enzyme that plays various roles in the regulation of the immune response and inflammation. During TCR engagement and activation, translocates into the cytoplasm and deubiquitinates its substrates LAT and TRAT1 and prevents their lysosome-dependent degradation to stabilize the TCR signaling complex at the plasma membrane. Plays an essential role in the selective LPS- induced macrophage response through the activation of NF-kappa-B pathway. In addition, promotes that antiviral immune response through targeting DNA sensor IFI16 to inhibit its proteasome-dependent degradation. Participates in the interferon signaling pathway and antiviral response independently of its deubiquitinase activity by maintaining nuclear phosphorylated STAT1 levels via inhibition of its CREBBP-mediated acetylation and subsequent dephosphorylation. Plays an intrinsic role in promoting the differentiation, activation and proliferation of CD4(+) T-cell by activating the NF- kappa-B signaling pathway through deubiquitinating and stabilizing B- cell lymphoma/leukemia 10/BCL10. In myeloid-derived suppressor cells promotes the activation of the NF-kappa-B via deubiquitination and stabilization of RELA. Regulates the 'Lys-63'-linked polyubiquitin chains of BAX and thereby modulates the mitochondrial apoptotic process. Negative regulator of NOTCH signaling that specifically deubiquitinates non-activated NOTCH receptors to target them for lysosomal degradation; deubiquitination of NOTCH stimulates its transport form late endosomes to lysosomes. Protects neurons against HTT/huntingtin- induced polyglutamine expansion-dependent neurodegeneration through regulation of autophagic flux. This function is independent of deubiquitinase activity or of other components of the USP12-WDR20-WDR48 deubiquitinating complex. In complex with WDR48, acts as a potential tumor suppressor by positively regulating PHLPP1 stability.",,,,,,,GO:0004843; GO:0004197; GO:0101005; GO:0046872,GO:0004843,GO:0004843; GO:0004197,GO:0004843,GO:0004843; GO:0016579,GO:0004843; GO:0036459,0.6978,0.8154,0.6978,0.5815,0.7482,5,0.7081,0.8,yes
ARSI_THECD,D1A230,ESM2Text,Bacteria,151,"Nonheme iron-dependent dioxygenase that can break carbon- arsenic bonds, playing a role in the detoxification of environmental organoarsenical compounds. Catalyzes the oxygen-dependent demethylation of highly toxic methylarsonous acid (MAs(III)) to arsenite, which can then be exported out of the cell. Can also cleave the C-As bond in several trivalent aromatic arsenicals, including roxarsone (III), nitarsone (III) and (4-aminophenyl)arsonous acid. Organoarsenical degradation by this enzyme is proposed to have a significant impact on the arsenic biogeocycle that maintains a balance between organic and inorganic species (Probable).",Metallothioneins have a high content of cysteine residues that bind to FAD or coactivators.,No,No,No,No,No,not-Yes,GO:0051213; GO:0046872,,,,GO:0046872,,,,,0.7088,,1,0.7088,0.2949,no
ARSI_THECD,D1A230,Prot2Text,Bacteria,151,"Nonheme iron-dependent dioxygenase that can break carbon- arsenic bonds, playing a role in the detoxification of environmental organoarsenical compounds. Catalyzes the oxygen-dependent demethylation of highly toxic methylarsonous acid (MAs(III)) to arsenite, which can then be exported out of the cell. Can also cleave the C-As bond in several trivalent aromatic arsenicals, including roxarsone (III), nitarsone (III) and (4-aminophenyl)arsonous acid. Organoarsenical degradation by this enzyme is proposed to have a significant impact on the arsenic biogeocycle that maintains a balance between organic and inorganic species (Probable).",Shows carboxylate domain specific activity toward chloroacetate.,No,No,No,No,No,not-Yes,GO:0051213; GO:0046872,GO:0016787,,,,GO:0018784,0.3731,,,,0.2193,2,0.2962,0.2949,no
ARSI_THECD,D1A230,ProtT3,Bacteria,151,"Nonheme iron-dependent dioxygenase that can break carbon- arsenic bonds, playing a role in the detoxification of environmental organoarsenical compounds. Catalyzes the oxygen-dependent demethylation of highly toxic methylarsonous acid (MAs(III)) to arsenite, which can then be exported out of the cell. Can also cleave the C-As bond in several trivalent aromatic arsenicals, including roxarsone (III), nitarsone (III) and (4-aminophenyl)arsonous acid. Organoarsenical degradation by this enzyme is proposed to have a significant impact on the arsenic biogeocycle that maintains a balance between organic and inorganic species (Probable).",To M.tuberculosis Rv1008c,Vague,Vague,Vague,Vague,No,not-Yes,GO:0051213; GO:0046872,,,,,,,,,,,0,,0.2949,no
ARSI_THECD,D1A230,ProtTale,Bacteria,151,"Nonheme iron-dependent dioxygenase that can break carbon- arsenic bonds, playing a role in the detoxification of environmental organoarsenical compounds. Catalyzes the oxygen-dependent demethylation of highly toxic methylarsonous acid (MAs(III)) to arsenite, which can then be exported out of the cell. Can also cleave the C-As bond in several trivalent aromatic arsenicals, including roxarsone (III), nitarsone (III) and (4-aminophenyl)arsonous acid. Organoarsenical degradation by this enzyme is proposed to have a significant impact on the arsenic biogeocycle that maintains a balance between organic and inorganic species (Probable).",Involved in the degradation of cysteine and in the biosynthesis of the antibiotic bacilomycin. Catalyzes the transfer of sulfur from thiosulfate to the sulfhydryl group of thiosulfate.,No,No,No,No,No,not-Yes,GO:0051213; GO:0046872,GO:0004792,GO:0004792,GO:0004792,GO:0016740,GO:0004792,0.2193,0.2193,0.2193,0.3731,0.2193,5,0.2501,0.2949,no
ARSI_THECD,D1A230,Protein2Text,Bacteria,151,"Nonheme iron-dependent dioxygenase that can break carbon- arsenic bonds, playing a role in the detoxification of environmental organoarsenical compounds. Catalyzes the oxygen-dependent demethylation of highly toxic methylarsonous acid (MAs(III)) to arsenite, which can then be exported out of the cell. Can also cleave the C-As bond in several trivalent aromatic arsenicals, including roxarsone (III), nitarsone (III) and (4-aminophenyl)arsonous acid. Organoarsenical degradation by this enzyme is proposed to have a significant impact on the arsenic biogeocycle that maintains a balance between organic and inorganic species (Probable).","This protein is involved in the molecular function of catalyzing a redox reaction. More specifically, it is a nickel-containing enzyme that catalyzes the isomerization of beta-ketoacyl-CoA to beta-hydroxyacyl-CoA. This reaction is an important step in the beta-oxidation of fatty acids.",No,No,No,No,No,not-Yes,GO:0051213; GO:0046872,,,,,,,,,,,0,,0.2949,no
ARSI_THECD,D1A230,Reference,Bacteria,151,"Nonheme iron-dependent dioxygenase that can break carbon- arsenic bonds, playing a role in the detoxification of environmental organoarsenical compounds. Catalyzes the oxygen-dependent demethylation of highly toxic methylarsonous acid (MAs(III)) to arsenite, which can then be exported out of the cell. Can also cleave the C-As bond in several trivalent aromatic arsenicals, including roxarsone (III), nitarsone (III) and (4-aminophenyl)arsonous acid. Organoarsenical degradation by this enzyme is proposed to have a significant impact on the arsenic biogeocycle that maintains a balance between organic and inorganic species (Probable).","Nonheme iron-dependent dioxygenase that can break carbon- arsenic bonds, playing a role in the detoxification of environmental organoarsenical compounds. Catalyzes the oxygen-dependent demethylation of highly toxic methylarsonous acid (MAs(III)) to arsenite, which can then be exported out of the cell. Can also cleave the C-As bond in several trivalent aromatic arsenicals, including roxarsone (III), nitarsone (III) and (4-aminophenyl)arsonous acid. Organoarsenical degradation by this enzyme is proposed to have a significant impact on the arsenic biogeocycle that maintains a balance between organic and inorganic species (Probable).",,,,,,,GO:0051213; GO:0046872,GO:0051213,GO:0016702; GO:0005506,GO:0051213; GO:0005506,GO:0051213,GO:0051213; GO:0005506,0.7088,0.7588,0.8854,0.7088,0.8854,5,0.7894,0.2949,no
OXDD_RAT,D3ZDM7,ESM2Text,Eukaryota,341,"Selectively catalyzes the oxidative deamination of acidic amino acids. Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors. Protects the organism from the toxicity of D-amino acids. May also function in the intestine.","Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008445; GO:0071949,GO:0016491,GO:0008450,GO:0008445,GO:0033739,GO:0033182,0.3665,0.0,0.6847,0.1671,0.0,5,0.2437,0.2634,no
OXDD_RAT,D3ZDM7,Prot2Text,Eukaryota,341,"Selectively catalyzes the oxidative deamination of acidic amino acids. Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors. Protects the organism from the toxicity of D-amino acids. May also function in the intestine.","Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008445; GO:0071949,GO:0033739,GO:0003885,GO:0033735,GO:0003884,GO:0033182,0.1671,0.1971,0.2438,0.6047,0.0,5,0.2425,0.2634,no
OXDD_RAT,D3ZDM7,ProtT3,Eukaryota,341,"Selectively catalyzes the oxidative deamination of acidic amino acids. Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors. Protects the organism from the toxicity of D-amino acids. May also function in the intestine.",Catalyzes the oxidative deamination of D-aspartate and D-aspartyl-beta-semialdehyde (D-ASA). Peroxisome. Belongs to the DAMOX/DASOX family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008445; GO:0071949,GO:0033735,GO:0033736,GO:0033735,GO:0033735,GO:0033734,0.2438,0.3963,0.2438,0.2438,0.1971,5,0.265,0.2634,no
OXDD_RAT,D3ZDM7,ProtTale,Eukaryota,341,"Selectively catalyzes the oxidative deamination of acidic amino acids. Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors. Protects the organism from the toxicity of D-amino acids. May also function in the intestine.",Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Enables the organism to utilize D-amino acids as a source of nutrients.,Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0008445; GO:0071949,GO:0003884,GO:0003863,GO:0003884,GO:0003863,GO:0003884,0.6047,0.1971,0.6047,0.1971,0.6047,5,0.4417,0.2634,no
OXDD_RAT,D3ZDM7,Protein2Text,Eukaryota,341,"Selectively catalyzes the oxidative deamination of acidic amino acids. Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors. Protects the organism from the toxicity of D-amino acids. May also function in the intestine.","The molecular function of this protein is as a hydrolase, specifically an aminopeptidase. It is involved in the degradation of peptides by cleaving amino acids from the N-terminal end.",No,No,No,No,No,not-Yes,GO:0008445; GO:0071949,GO:0004177,GO:0004177,GO:0004177,GO:0004177,GO:0004177,0.1183,0.1183,0.1183,0.1183,0.1183,5,0.1183,0.2634,no
OXDD_RAT,D3ZDM7,Reference,Eukaryota,341,"Selectively catalyzes the oxidative deamination of acidic amino acids. Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors. Protects the organism from the toxicity of D-amino acids. May also function in the intestine.","Selectively catalyzes the oxidative deamination of acidic amino acids. Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors. Protects the organism from the toxicity of D-amino acids. May also function in the intestine.",,,,,,,GO:0008445; GO:0071949,GO:0004138,GO:0033182,GO:0033971,GO:0033971,GO:0033734,0.0936,0.0,0.1258,0.1258,0.1971,5,0.1085,0.2634,no
EXOSX_RAT,D4A1X2,ESM2Text,Eukaryota,885,"Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. EXOSC10 is required for nucleolar localization of C1D and probably mediates the association of MTREX, C1D and MPHOSPH6 with the RNA exosome involved in the maturation of 5.8S rRNA. Plays a role in the recruitment of replication protein A complex (RPA) and RAD51 to DNA double-strand breaks caused by irradiation, contributing to DNA repair by homologous recombination. Regulates levels of damage-induced RNAs in order to prevent DNA-RNA hybrid formation at DNA double-strand breaks and limit DNA end resection after damage. Plays a role in oocyte development, maturation and survival. Required for normal testis development and mitotic division of spermatogonia. Plays a role in proper embryo development. Required for global protein translation. Required for cell proliferation.","3'->5' exoribonuclease involved in the processing of mitochondrial RNA precursors and in maturation of the U5 snRNA and the pre-mRNA. In the presence of U5 snRNA, stimulates the activity of the complex formed by U2 snRNA and MRS2A.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0000175; GO:0046872; GO:0000166; GO:0004532; GO:0003727; GO:0070034,GO:0000175,GO:0000175,GO:0000175,GO:0000175,GO:0000175,0.4364,0.4364,0.4364,0.4364,0.4364,5,0.4364,0.5313,no
EXOSX_RAT,D4A1X2,Prot2Text,Eukaryota,885,"Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. EXOSC10 is required for nucleolar localization of C1D and probably mediates the association of MTREX, C1D and MPHOSPH6 with the RNA exosome involved in the maturation of 5.8S rRNA. Plays a role in the recruitment of replication protein A complex (RPA) and RAD51 to DNA double-strand breaks caused by irradiation, contributing to DNA repair by homologous recombination. Regulates levels of damage-induced RNAs in order to prevent DNA-RNA hybrid formation at DNA double-strand breaks and limit DNA end resection after damage. Plays a role in oocyte development, maturation and survival. Required for normal testis development and mitotic division of spermatogonia. Plays a role in proper embryo development. Required for global protein translation. Required for cell proliferation.",Exoribonuclease that is part of the RNA-directed DNA methylation (RdDM) pathway and which specifically recognizes and binds 5'-GGGGCC-3' sequence repeats. Catalyzes the de novo methylation of 5'-GGGGCC-3' sequence in a subset of RdDM targets. Functions as a non-canonical E3 ubiquitin ligase that targets the non-canonical C-terminal heptapeptide repeat domain (CTD) of small RNAs (snRNAs). Involved in the degradation of RNA processing in non-neuronal cells.,No,Maybe,Maybe,No,No,not-Yes,GO:0000175; GO:0046872; GO:0000166; GO:0004532; GO:0003727; GO:0070034,,,,,GO:0004532,,,,,0.4436,1,0.4436,0.5313,no
EXOSX_RAT,D4A1X2,ProtT3,Eukaryota,885,"Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. EXOSC10 is required for nucleolar localization of C1D and probably mediates the association of MTREX, C1D and MPHOSPH6 with the RNA exosome involved in the maturation of 5.8S rRNA. Plays a role in the recruitment of replication protein A complex (RPA) and RAD51 to DNA double-strand breaks caused by irradiation, contributing to DNA repair by homologous recombination. Regulates levels of damage-induced RNAs in order to prevent DNA-RNA hybrid formation at DNA double-strand breaks and limit DNA end resection after damage. Plays a role in oocyte development, maturation and survival. Required for normal testis development and mitotic division of spermatogonia. Plays a role in proper embryo development. Required for global protein translation. Required for cell proliferation.","Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class-switch",Yes,Yes,Yes,Yes,Yes,Yes,GO:0000175; GO:0046872; GO:0000166; GO:0004532; GO:0003727; GO:0070034,GO:0000175,GO:0004532,GO:0000175,GO:0000175,GO:0000175,0.4364,0.4436,0.4364,0.4364,0.4364,5,0.4378,0.5313,no
EXOSX_RAT,D4A1X2,ProtTale,Eukaryota,885,"Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. EXOSC10 is required for nucleolar localization of C1D and probably mediates the association of MTREX, C1D and MPHOSPH6 with the RNA exosome involved in the maturation of 5.8S rRNA. Plays a role in the recruitment of replication protein A complex (RPA) and RAD51 to DNA double-strand breaks caused by irradiation, contributing to DNA repair by homologous recombination. Regulates levels of damage-induced RNAs in order to prevent DNA-RNA hybrid formation at DNA double-strand breaks and limit DNA end resection after damage. Plays a role in oocyte development, maturation and survival. Required for normal testis development and mitotic division of spermatogonia. Plays a role in proper embryo development. Required for global protein translation. Required for cell proliferation.",Probable catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0000175; GO:0046872; GO:0000166; GO:0004532; GO:0003727; GO:0070034,GO:0000175,GO:0000175,GO:0000175,GO:0000175,GO:0000175,0.4364,0.4364,0.4364,0.4364,0.4364,5,0.4364,0.5313,no
EXOSX_RAT,D4A1X2,Protein2Text,Eukaryota,885,"Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. EXOSC10 is required for nucleolar localization of C1D and probably mediates the association of MTREX, C1D and MPHOSPH6 with the RNA exosome involved in the maturation of 5.8S rRNA. Plays a role in the recruitment of replication protein A complex (RPA) and RAD51 to DNA double-strand breaks caused by irradiation, contributing to DNA repair by homologous recombination. Regulates levels of damage-induced RNAs in order to prevent DNA-RNA hybrid formation at DNA double-strand breaks and limit DNA end resection after damage. Plays a role in oocyte development, maturation and survival. Required for normal testis development and mitotic division of spermatogonia. Plays a role in proper embryo development. Required for global protein translation. Required for cell proliferation.","This protein is involved in dephosphorylation. It belongs to the phosphatase family and is involved in removing phosphate groups from proteins, which is a crucial step in various cellular processes.",No,No,No,No,No,not-Yes,GO:0000175; GO:0046872; GO:0000166; GO:0004532; GO:0003727; GO:0070034,GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,0.2102,0.2102,0.2102,0.2102,0.2102,5,0.2102,0.5313,no
EXOSX_RAT,D4A1X2,Reference,Eukaryota,885,"Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. EXOSC10 is required for nucleolar localization of C1D and probably mediates the association of MTREX, C1D and MPHOSPH6 with the RNA exosome involved in the maturation of 5.8S rRNA. Plays a role in the recruitment of replication protein A complex (RPA) and RAD51 to DNA double-strand breaks caused by irradiation, contributing to DNA repair by homologous recombination. Regulates levels of damage-induced RNAs in order to prevent DNA-RNA hybrid formation at DNA double-strand breaks and limit DNA end resection after damage. Plays a role in oocyte development, maturation and survival. Required for normal testis development and mitotic division of spermatogonia. Plays a role in proper embryo development. Required for global protein translation. Required for cell proliferation.","Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. EXOSC10 is required for nucleolar localization of C1D and probably mediates the association of MTREX, C1D and MPHOSPH6 with the RNA exosome involved in the maturation of 5.8S rRNA. Plays a role in the recruitment of replication protein A complex (RPA) and RAD51 to DNA double-strand breaks caused by irradiation, contributing to DNA repair by homologous recombination. Regulates levels of damage-induced RNAs in order to prevent DNA-RNA hybrid formation at DNA double-strand breaks and limit DNA end resection after damage. Plays a role in oocyte development, maturation and survival. Required for normal testis development and mitotic division of spermatogonia. Plays a role in proper embryo development. Required for global protein translation. Required for cell proliferation.",,,,,,,GO:0000175; GO:0046872; GO:0000166; GO:0004532; GO:0003727; GO:0070034,GO:0000175; GO:0003723,GO:0000175; GO:0003723,GO:0000175; GO:0003723,GO:0000175; GO:0004532,GO:0004532,0.7413,0.7413,0.7413,0.5372,0.4436,5,0.6409,0.5313,no
KHK_HALVD,D4GSD6,ESM2Text,Archaea,375,"Catalyzes the ATP-dependent phosphorylation of the ketose sugar fructose to fructose-1-phosphate. Does not produce fructose-6- phosphate. The sugars D-glucose, D-galactose, L-rhamnose, D-xylose, L- arabinose and D-ribose are not substrates of this enzyme.",Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate and glucosamine to glucosamine 6-phosphate. Involved in the degradation of glucose via a phosphorylative Entner-Doudoroff pathway.,No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0042802; GO:0004454; GO:0042803,GO:0004340,GO:0004340; GO:0004396,GO:0004396,GO:0004396,GO:0004340,0.4053,0.5039,0.4483,0.4483,0.4053,5,0.4422,0.3877,no
KHK_HALVD,D4GSD6,Prot2Text,Archaea,375,"Catalyzes the ATP-dependent phosphorylation of the ketose sugar fructose to fructose-1-phosphate. Does not produce fructose-6- phosphate. The sugars D-glucose, D-galactose, L-rhamnose, D-xylose, L- arabinose and D-ribose are not substrates of this enzyme.",Catalyzes the phosphorylation of fructoselysine to fructoselysine 6-phosphate. Functions in a fructoselysine degradation pathway that allows E.coli to grow on fructoselysine or psicoselysine.,No,No,No,Maybe,Maybe,not-Yes,GO:0042802; GO:0004454; GO:0042803,GO:0016301,GO:0016301,GO:0016301,GO:0004672,GO:0050308,0.4106,0.4106,0.4106,0.3868,0.109,5,0.3455,0.3877,no
KHK_HALVD,D4GSD6,ProtT3,Archaea,375,"Catalyzes the ATP-dependent phosphorylation of the ketose sugar fructose to fructose-1-phosphate. Does not produce fructose-6- phosphate. The sugars D-glucose, D-galactose, L-rhamnose, D-xylose, L- arabinose and D-ribose are not substrates of this enzyme.","Catalyzes the phosphorylation of fructose 6-phosphate to fructose 1,6-bisphosphate in the presence of inorganic phosphate. Cytoplasm. Belongs to the carbohydrate kinase PfkB family",No,No,No,No,No,not-Yes,GO:0042802; GO:0004454; GO:0042803,GO:0003872; GO:0005524,GO:0003872; GO:0005524,GO:0003872,GO:0003872,GO:0003872,0.3835,0.3835,0.4053,0.4053,0.4053,5,0.3966,0.3877,no
KHK_HALVD,D4GSD6,ProtTale,Archaea,375,"Catalyzes the ATP-dependent phosphorylation of the ketose sugar fructose to fructose-1-phosphate. Does not produce fructose-6- phosphate. The sugars D-glucose, D-galactose, L-rhamnose, D-xylose, L- arabinose and D-ribose are not substrates of this enzyme.","Catalyzes the ATP-dependent phosphorylation of fructose-l- phosphate to fructose-l,6-bisphosphate.",No,No,No,No,Maybe,not-Yes,GO:0042802; GO:0004454; GO:0042803,GO:0008662; GO:0005524,GO:0016301; GO:0005524,GO:0008662; GO:0005524,GO:0008662; GO:0005524,GO:0008662; GO:0005524,0.3835,0.3705,0.3835,0.3835,0.3835,5,0.3809,0.3877,no
KHK_HALVD,D4GSD6,Protein2Text,Archaea,375,"Catalyzes the ATP-dependent phosphorylation of the ketose sugar fructose to fructose-1-phosphate. Does not produce fructose-6- phosphate. The sugars D-glucose, D-galactose, L-rhamnose, D-xylose, L- arabinose and D-ribose are not substrates of this enzyme.","This protein is a kinase, which means it catalyzes the transfer of a phosphate group from one molecule to another. More specifically, it is likely involved in the phosphorylation of a nucleotide, such as ATP or ADP, which is an important step in many cellular processes.",Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0042802; GO:0004454; GO:0042803,GO:0016301,GO:0016301,,GO:0016301,GO:0016301,0.4106,0.4106,,0.4106,0.4106,4,0.4106,0.3877,no
KHK_HALVD,D4GSD6,Reference,Archaea,375,"Catalyzes the ATP-dependent phosphorylation of the ketose sugar fructose to fructose-1-phosphate. Does not produce fructose-6- phosphate. The sugars D-glucose, D-galactose, L-rhamnose, D-xylose, L- arabinose and D-ribose are not substrates of this enzyme.","Catalyzes the ATP-dependent phosphorylation of the ketose sugar fructose to fructose-1-phosphate. Does not produce fructose-6- phosphate. The sugars D-glucose, D-galactose, L-rhamnose, D-xylose, L- arabinose and D-ribose are not substrates of this enzyme.",,,,,,,GO:0042802; GO:0004454; GO:0042803,GO:0008865; GO:0005524,GO:0004454; GO:0005524,GO:0004454; GO:0005524,GO:0004340; GO:0016301; GO:0005524,GO:0004370; GO:0005524,0.3835,0.4929,0.4929,0.4352,0.3765,5,0.4362,0.3877,no
LONG_HAELO,D4QD81,ESM2Text,Eukaryota,156,"Anticoagulant and fibrinolytic protease that modulates blood feeding of ticks on vertebrate hosts. Degrades host fibrinogen and delays fibrin clot formation. Promotes lysis of fibrin clots in the host by activating host plasminogen in the presence of soluble fibrin. Binds Ca(2+). Hydrolyzes serine protease- specific substrates. Required for the formation of a blood pool, an accumulation of blood and tissue fluid developed at the tick's feeding site. Blocks activation of host AGER/RAGE. Reduces AGER/RAGE-dependent production of reactive oxygen species (ROS) in human endothelial cells. Prevents AGER/RAGE-dependent activation of NF-kappa- B and suppresses expression of adhesion molecules, such as VCAM1, ICAM1 and SELE, and secretion of cytokines, such as CSF3/GCSF and TGF-beta, in human endothelial cells. Suppresses RAGE/AGER- mediated migration of mouse peritoneal resident cells. Reduces AGER/RAGE-mediated inflammation in mice tissues.",May function as a calcium-binding regulatory protein.,No,No,No,No,No,not-Yes,GO:0005509; GO:0008236; GO:0090729,GO:0005509,GO:0005509,GO:0005509,GO:0005509,GO:0005509,0.5654,0.5654,0.5654,0.5654,0.5654,5,0.5654,0.5751,yes
LONG_HAELO,D4QD81,Prot2Text,Eukaryota,156,"Anticoagulant and fibrinolytic protease that modulates blood feeding of ticks on vertebrate hosts. Degrades host fibrinogen and delays fibrin clot formation. Promotes lysis of fibrin clots in the host by activating host plasminogen in the presence of soluble fibrin. Binds Ca(2+). Hydrolyzes serine protease- specific substrates. Required for the formation of a blood pool, an accumulation of blood and tissue fluid developed at the tick's feeding site. Blocks activation of host AGER/RAGE. Reduces AGER/RAGE-dependent production of reactive oxygen species (ROS) in human endothelial cells. Prevents AGER/RAGE-dependent activation of NF-kappa- B and suppresses expression of adhesion molecules, such as VCAM1, ICAM1 and SELE, and secretion of cytokines, such as CSF3/GCSF and TGF-beta, in human endothelial cells. Suppresses RAGE/AGER- mediated migration of mouse peritoneal resident cells. Reduces AGER/RAGE-mediated inflammation in mice tissues.",The main role of this protein is to help catalyze the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.,No,No,No,No,No,not-Yes,GO:0005509; GO:0008236; GO:0090729,GO:0004623,GO:0004623,GO:0004623,GO:0004622,GO:0004623,0.1878,0.1878,0.1878,0.1632,0.1878,5,0.1829,0.5751,yes
LONG_HAELO,D4QD81,ProtT3,Eukaryota,156,"Anticoagulant and fibrinolytic protease that modulates blood feeding of ticks on vertebrate hosts. Degrades host fibrinogen and delays fibrin clot formation. Promotes lysis of fibrin clots in the host by activating host plasminogen in the presence of soluble fibrin. Binds Ca(2+). Hydrolyzes serine protease- specific substrates. Required for the formation of a blood pool, an accumulation of blood and tissue fluid developed at the tick's feeding site. Blocks activation of host AGER/RAGE. Reduces AGER/RAGE-dependent production of reactive oxygen species (ROS) in human endothelial cells. Prevents AGER/RAGE-dependent activation of NF-kappa- B and suppresses expression of adhesion molecules, such as VCAM1, ICAM1 and SELE, and secretion of cytokines, such as CSF3/GCSF and TGF-beta, in human endothelial cells. Suppresses RAGE/AGER- mediated migration of mouse peritoneal resident cells. Reduces AGER/RAGE-mediated inflammation in mice tissues.",Calcium-binding protein which may be involved in intracellular calcium homeostasis. Secreted. Belongs to the calycin superfamily. Lipocalin family,No,No,No,No,Vague,not-Yes,GO:0005509; GO:0008236; GO:0090729,GO:0005509,GO:0005509,GO:0005509,GO:0005509,GO:0005509,0.5654,0.5654,0.5654,0.5654,0.5654,5,0.5654,0.5751,yes
LONG_HAELO,D4QD81,ProtTale,Eukaryota,156,"Anticoagulant and fibrinolytic protease that modulates blood feeding of ticks on vertebrate hosts. Degrades host fibrinogen and delays fibrin clot formation. Promotes lysis of fibrin clots in the host by activating host plasminogen in the presence of soluble fibrin. Binds Ca(2+). Hydrolyzes serine protease- specific substrates. Required for the formation of a blood pool, an accumulation of blood and tissue fluid developed at the tick's feeding site. Blocks activation of host AGER/RAGE. Reduces AGER/RAGE-dependent production of reactive oxygen species (ROS) in human endothelial cells. Prevents AGER/RAGE-dependent activation of NF-kappa- B and suppresses expression of adhesion molecules, such as VCAM1, ICAM1 and SELE, and secretion of cytokines, such as CSF3/GCSF and TGF-beta, in human endothelial cells. Suppresses RAGE/AGER- mediated migration of mouse peritoneal resident cells. Reduces AGER/RAGE-mediated inflammation in mice tissues.",May be involved in the storage and release of calcium from the endoplasmic reticulum lumen.,No,No,No,No,No,not-Yes,GO:0005509; GO:0008236; GO:0090729,,,,,,,,,,,0,,0.5751,yes
LONG_HAELO,D4QD81,Protein2Text,Eukaryota,156,"Anticoagulant and fibrinolytic protease that modulates blood feeding of ticks on vertebrate hosts. Degrades host fibrinogen and delays fibrin clot formation. Promotes lysis of fibrin clots in the host by activating host plasminogen in the presence of soluble fibrin. Binds Ca(2+). Hydrolyzes serine protease- specific substrates. Required for the formation of a blood pool, an accumulation of blood and tissue fluid developed at the tick's feeding site. Blocks activation of host AGER/RAGE. Reduces AGER/RAGE-dependent production of reactive oxygen species (ROS) in human endothelial cells. Prevents AGER/RAGE-dependent activation of NF-kappa- B and suppresses expression of adhesion molecules, such as VCAM1, ICAM1 and SELE, and secretion of cytokines, such as CSF3/GCSF and TGF-beta, in human endothelial cells. Suppresses RAGE/AGER- mediated migration of mouse peritoneal resident cells. Reduces AGER/RAGE-mediated inflammation in mice tissues.",The molecular function of this protein is calcium-binding.,Vague,No,No,No,No,not-Yes,GO:0005509; GO:0008236; GO:0090729,GO:0005509,GO:0005509,GO:0005509,GO:0005509,GO:0005509,0.5654,0.5654,0.5654,0.5654,0.5654,5,0.5654,0.5751,yes
LONG_HAELO,D4QD81,Reference,Eukaryota,156,"Anticoagulant and fibrinolytic protease that modulates blood feeding of ticks on vertebrate hosts. Degrades host fibrinogen and delays fibrin clot formation. Promotes lysis of fibrin clots in the host by activating host plasminogen in the presence of soluble fibrin. Binds Ca(2+). Hydrolyzes serine protease- specific substrates. Required for the formation of a blood pool, an accumulation of blood and tissue fluid developed at the tick's feeding site. Blocks activation of host AGER/RAGE. Reduces AGER/RAGE-dependent production of reactive oxygen species (ROS) in human endothelial cells. Prevents AGER/RAGE-dependent activation of NF-kappa- B and suppresses expression of adhesion molecules, such as VCAM1, ICAM1 and SELE, and secretion of cytokines, such as CSF3/GCSF and TGF-beta, in human endothelial cells. Suppresses RAGE/AGER- mediated migration of mouse peritoneal resident cells. Reduces AGER/RAGE-mediated inflammation in mice tissues.","Anticoagulant and fibrinolytic protease that modulates blood feeding of ticks on vertebrate hosts. Degrades host fibrinogen and delays fibrin clot formation. Promotes lysis of fibrin clots in the host by activating host plasminogen in the presence of soluble fibrin. Binds Ca(2+). Hydrolyzes serine protease- specific substrates. Required for the formation of a blood pool, an accumulation of blood and tissue fluid developed at the tick's feeding site. Blocks activation of host AGER/RAGE. Reduces AGER/RAGE-dependent production of reactive oxygen species (ROS) in human endothelial cells. Prevents AGER/RAGE-dependent activation of NF-kappa- B and suppresses expression of adhesion molecules, such as VCAM1, ICAM1 and SELE, and secretion of cytokines, such as CSF3/GCSF and TGF-beta, in human endothelial cells. Suppresses RAGE/AGER- mediated migration of mouse peritoneal resident cells. Reduces AGER/RAGE-mediated inflammation in mice tissues.",,,,,,,GO:0005509; GO:0008236; GO:0090729,GO:0008236; GO:0016247; GO:0005509,GO:0004252; GO:0005509,GO:0004252; GO:0005509,GO:0004252; GO:0008236; GO:0004953,GO:0004252; GO:0005509,0.7587,0.768,0.768,0.5526,0.768,5,0.7231,0.5751,yes
MERA_LYSSH,D9J041,ESM2Text,Bacteria,546,"Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0). Catalyzes reduction of Hg(2+) to elemental Hg, which is volatile and can diffuse out of cells passively. Plays a pivotal role in mercury resistance and cell protection.",Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0).,Yes,Yes,Yes,Yes,Yes,Yes,GO:0050660; GO:0016152; GO:0045340; GO:0003955; GO:0050661; GO:0016668,GO:0016491,GO:0016491,GO:0016152,GO:0016491,GO:0016491,0.4234,0.4234,0.4218,0.4234,0.4234,5,0.4231,0.2325,no
MERA_LYSSH,D9J041,Prot2Text,Bacteria,546,"Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0). Catalyzes reduction of Hg(2+) to elemental Hg, which is volatile and can diffuse out of cells passively. Plays a pivotal role in mercury resistance and cell protection.",Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0).,Yes,Yes,Yes,Yes,Yes,Yes,GO:0050660; GO:0016152; GO:0045340; GO:0003955; GO:0050661; GO:0016668,GO:0016491,,GO:0008839,GO:0016491,GO:0016152,0.4234,,0.2414,0.4234,0.4218,4,0.3775,0.2325,no
MERA_LYSSH,D9J041,ProtT3,Bacteria,546,"Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0). Catalyzes reduction of Hg(2+) to elemental Hg, which is volatile and can diffuse out of cells passively. Plays a pivotal role in mercury resistance and cell protection.",Maintains high levels of reduced glutathione in the cytoplasm. Cytoplasm. Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family,No,No,No,No,Vague,not-Yes,GO:0050660; GO:0016152; GO:0045340; GO:0003955; GO:0050661; GO:0016668,GO:0004362,GO:0004362,GO:0004362,GO:0004362,GO:0004362,0.3059,0.3059,0.3059,0.3059,0.3059,5,0.3059,0.2325,no
MERA_LYSSH,D9J041,ProtTale,Bacteria,546,"Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0). Catalyzes reduction of Hg(2+) to elemental Hg, which is volatile and can diffuse out of cells passively. Plays a pivotal role in mercury resistance and cell protection.",Catalyzes the reduction of glutathione disulfide (GSSG) to reduced glutathione (GSH). Can act as both NADH- and NADPH-dependent dehydrogenase.,No,No,No,No,No,not-Yes,GO:0050660; GO:0016152; GO:0045340; GO:0003955; GO:0050661; GO:0016668,GO:0004362,GO:0004362,GO:0004362,GO:0004362,GO:0004362,0.3059,0.3059,0.3059,0.3059,0.3059,5,0.3059,0.2325,no
MERA_LYSSH,D9J041,Protein2Text,Bacteria,546,"Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0). Catalyzes reduction of Hg(2+) to elemental Hg, which is volatile and can diffuse out of cells passively. Plays a pivotal role in mercury resistance and cell protection.",The molecular function of this protein is a lipoamide dehydrogenase.,No,No,No,No,No,not-Yes,GO:0050660; GO:0016152; GO:0045340; GO:0003955; GO:0050661; GO:0016668,GO:0004148,GO:0004148,GO:0004148,GO:0008149,GO:0004148,0.3727,0.3727,0.3727,0.0,0.3727,5,0.2982,0.2325,no
MERA_LYSSH,D9J041,Reference,Bacteria,546,"Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0). Catalyzes reduction of Hg(2+) to elemental Hg, which is volatile and can diffuse out of cells passively. Plays a pivotal role in mercury resistance and cell protection.","Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0). Catalyzes reduction of Hg(2+) to elemental Hg, which is volatile and can diffuse out of cells passively. Plays a pivotal role in mercury resistance and cell protection.",,,,,,,GO:0050660; GO:0016152; GO:0045340; GO:0003955; GO:0050661; GO:0016668,GO:0016151,GO:0016491,GO:0016152,GO:0016491; GO:0050660; GO:0016665,GO:0016665,0.3225,0.4234,0.4218,0.6812,0.0,5,0.3698,0.2325,no
ACNA_STRVT,D9X0I3,ESM2Text,Bacteria,931,"Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid (TCA) cycle. Aconitase activity is important for the initiation of morphological and physiological differentiation of S.viridochromogenes. In addition, the apo form of AcnA (lacking the [4Fe-4S] cluster) functions as a RNA- binding regulatory protein, which binds to iron responsive elements (IREs) located on the untranslated region of certain mRNAs, including recA and ftsZ. Binding to IRE-like structures probably alters the target mRNA stability and regulates the protein amount. The apo form plays a regulatory role in oxidative stress response.","Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Could catalyze the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnA functions as a RNA-binding regulatory protein.",Yes,Yes,Yes,Maybe,Yes,Yes,GO:0051539; GO:0003994; GO:0046872; GO:0003723,GO:0003994; GO:0051539,GO:0003994,GO:0003994,GO:0003994,GO:0003994,0.7705,0.4608,0.4608,0.4608,0.4608,5,0.5227,0.3953,no
ACNA_STRVT,D9X0I3,Prot2Text,Bacteria,931,"Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid (TCA) cycle. Aconitase activity is important for the initiation of morphological and physiological differentiation of S.viridochromogenes. In addition, the apo form of AcnA (lacking the [4Fe-4S] cluster) functions as a RNA- binding regulatory protein, which binds to iron responsive elements (IREs) located on the untranslated region of certain mRNAs, including recA and ftsZ. Binding to IRE-like structures probably alters the target mRNA stability and regulates the protein amount. The apo form plays a regulatory role in oxidative stress response.","Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Could catalyze the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnA functions as a RNA-binding regulatory protein.",Yes,Yes,Yes,Maybe,Yes,Yes,GO:0051539; GO:0003994; GO:0046872; GO:0003723,GO:0003994; GO:0003723,GO:0003994,GO:0003994,GO:0003994,GO:0003994,0.7615,0.4608,0.4608,0.4608,0.4608,5,0.5209,0.3953,no
ACNA_STRVT,D9X0I3,ProtT3,Bacteria,931,"Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid (TCA) cycle. Aconitase activity is important for the initiation of morphological and physiological differentiation of S.viridochromogenes. In addition, the apo form of AcnA (lacking the [4Fe-4S] cluster) functions as a RNA- binding regulatory protein, which binds to iron responsive elements (IREs) located on the untranslated region of certain mRNAs, including recA and ftsZ. Binding to IRE-like structures probably alters the target mRNA stability and regulates the protein amount. The apo form plays a regulatory role in oxidative stress response.","Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis- aconitate. Could catalyze the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnA functions as a RNA-binding regulatory protein. Belongs to",Yes,Yes,Yes,Maybe,Yes,Yes,GO:0051539; GO:0003994; GO:0046872; GO:0003723,GO:0003994,GO:0003994,GO:0003994,GO:0003994,GO:0003994,0.4608,0.4608,0.4608,0.4608,0.4608,5,0.4608,0.3953,no
ACNA_STRVT,D9X0I3,ProtTale,Bacteria,931,"Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid (TCA) cycle. Aconitase activity is important for the initiation of morphological and physiological differentiation of S.viridochromogenes. In addition, the apo form of AcnA (lacking the [4Fe-4S] cluster) functions as a RNA- binding regulatory protein, which binds to iron responsive elements (IREs) located on the untranslated region of certain mRNAs, including recA and ftsZ. Binding to IRE-like structures probably alters the target mRNA stability and regulates the protein amount. The apo form plays a regulatory role in oxidative stress response.",Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA) cycle. Catalyzes the reversible isomerization of 2-keto-3-deoxygluconate (2-KDG) to gluconate (GlcN).,No,No,No,No,No,not-Yes,GO:0051539; GO:0003994; GO:0046872; GO:0003723,GO:0016853,GO:0016853,GO:0016853,GO:0016853,GO:0016853,0.248,0.248,0.248,0.248,0.248,5,0.248,0.3953,no
ACNA_STRVT,D9X0I3,Protein2Text,Bacteria,931,"Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid (TCA) cycle. Aconitase activity is important for the initiation of morphological and physiological differentiation of S.viridochromogenes. In addition, the apo form of AcnA (lacking the [4Fe-4S] cluster) functions as a RNA- binding regulatory protein, which binds to iron responsive elements (IREs) located on the untranslated region of certain mRNAs, including recA and ftsZ. Binding to IRE-like structures probably alters the target mRNA stability and regulates the protein amount. The apo form plays a regulatory role in oxidative stress response.","This protein is an isocitrate dehydrogenase, which is a type of enzyme that catalyzes the oxidation of isocitrate to 2-oxoglutarate, producing NADH and CO2 in the process. This is a crucial step in the citric acid cycle (also known as the Krebs cycle or tricarboxylic acid cycle), a key metabolic pathway that generates energy for the cell through the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins.",No,No,No,No,No,not-Yes,GO:0051539; GO:0003994; GO:0046872; GO:0003723,GO:0004450,GO:0004450,GO:0004448,GO:0004449,GO:0004450,0.1228,0.1228,0.1408,0.1228,0.1228,5,0.1264,0.3953,no
ACNA_STRVT,D9X0I3,Reference,Bacteria,931,"Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid (TCA) cycle. Aconitase activity is important for the initiation of morphological and physiological differentiation of S.viridochromogenes. In addition, the apo form of AcnA (lacking the [4Fe-4S] cluster) functions as a RNA- binding regulatory protein, which binds to iron responsive elements (IREs) located on the untranslated region of certain mRNAs, including recA and ftsZ. Binding to IRE-like structures probably alters the target mRNA stability and regulates the protein amount. The apo form plays a regulatory role in oxidative stress response.","Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid (TCA) cycle. Aconitase activity is important for the initiation of morphological and physiological differentiation of S.viridochromogenes. In addition, the apo form of AcnA (lacking the [4Fe-4S] cluster) functions as a RNA- binding regulatory protein, which binds to iron responsive elements (IREs) located on the untranslated region of certain mRNAs, including recA and ftsZ. Binding to IRE-like structures probably alters the target mRNA stability and regulates the protein amount. The apo form plays a regulatory role in oxidative stress response.",,,,,,,GO:0051539; GO:0003994; GO:0046872; GO:0003723,GO:0003994; GO:0030350,GO:0003994; GO:0003723; GO:0051539,GO:0003994; GO:0003727; GO:0005506,GO:0003994; GO:0051539; GO:0003730,GO:0003994; GO:0003727,0.6429,0.9055,0.7837,0.8281,0.6923,5,0.7705,0.3953,no
FSP1_CHICK,E1BR24,ESM2Text,Eukaryota,373,"A NAD(P)H-dependent oxidoreductase that acts as a key inhibitor of ferroptosis. At the plasma membrane, catalyzes reduction of coenzyme Q/ubiquinone-10 to ubiquinol-10, a lipophilic radical-trapping antioxidant that prevents lipid oxidative damage and consequently ferroptosis. Acts in parallel to GPX4 to suppress phospholipid peroxidation and ferroptosis. This anti-ferroptotic function is independent of cellular glutathione levels. Also able to catalyze the production of H(2)O(2) and the conversion of FAD to 6-hydroxy-FAD in the presence of oxygen and NAD(P)H; these activities may be specific to chicken enzyme, which contains a specific C-terminal domain and homodimerizes.","A NAD(P)H-dependent oxidoreductase involved in cellular oxidative stress response. At the plasma membrane, catalyzes reduction of coenzyme Q/ubiquinone-10 to ubiquinol-10, a lipophilic radical-trapping antioxidant that prevents lipid oxidative damage and consequently ferric-chelate ferric chloride formation. Cooperates with GPX4 to suppress phospholipid peroxidation and ferric-chelate ferric chloride formation. This anti-ferric-chelate function is independent of cellular glutathione levels. May play a role in mitochondrial stress signaling. Upon oxidative stress, associates with the lipid peroxidation end product 4-hydroxy-2-nonenal (HNE), a precursor of SQLE, a lipid mediator that acts as a post-translational modification factor for numerous cellular enzymes. Functions as a NAD(P)(+)-dependent oxidoreductase, reducing Fe(3+) to Fe(2+) with a reduction of O(2), a reaction that plays an important role in the oxidative stress defense system and iron homeostasis. May also reduce minor side chains of various molecular structures.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0003677; GO:0004174; GO:0050660; GO:0016655,GO:0016651; GO:0051287,GO:0003955; GO:0016491,GO:0003955,GO:0003955,GO:0016655,0.5745,0.5496,0.4501,0.4501,0.5233,5,0.5095,0.3939,no
FSP1_CHICK,E1BR24,Prot2Text,Eukaryota,373,"A NAD(P)H-dependent oxidoreductase that acts as a key inhibitor of ferroptosis. At the plasma membrane, catalyzes reduction of coenzyme Q/ubiquinone-10 to ubiquinol-10, a lipophilic radical-trapping antioxidant that prevents lipid oxidative damage and consequently ferroptosis. Acts in parallel to GPX4 to suppress phospholipid peroxidation and ferroptosis. This anti-ferroptotic function is independent of cellular glutathione levels. Also able to catalyze the production of H(2)O(2) and the conversion of FAD to 6-hydroxy-FAD in the presence of oxygen and NAD(P)H; these activities may be specific to chicken enzyme, which contains a specific C-terminal domain and homodimerizes.",Isoform 2 is involved in the regulation of retinal ganglion cell (RGC) apoptosis. Isoform 2 binds to androgen receptor (AR) and promotes the transcription of retinoic acid receptors.,No,No,No,No,No,not-Yes,GO:0003677; GO:0004174; GO:0050660; GO:0016655,,,,,,,,,,,0,,0.3939,no
FSP1_CHICK,E1BR24,ProtT3,Eukaryota,373,"A NAD(P)H-dependent oxidoreductase that acts as a key inhibitor of ferroptosis. At the plasma membrane, catalyzes reduction of coenzyme Q/ubiquinone-10 to ubiquinol-10, a lipophilic radical-trapping antioxidant that prevents lipid oxidative damage and consequently ferroptosis. Acts in parallel to GPX4 to suppress phospholipid peroxidation and ferroptosis. This anti-ferroptotic function is independent of cellular glutathione levels. Also able to catalyze the production of H(2)O(2) and the conversion of FAD to 6-hydroxy-FAD in the presence of oxygen and NAD(P)H; these activities may be specific to chicken enzyme, which contains a specific C-terminal domain and homodimerizes.",A NAD(P)H-dependent oxidoreductase that acts as a key inhibitor of vitamin K-dependent gamma- carboxylation of multiple proteins (By similarity). Acts as a negative regulator of TGF-beta signaling (By similarity). Acts as a potent inhibitor of NF-kappa-B activation (By similarity). Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Mitochondrion membrane; Peripheral membrane protein; Cytoplasmic side Cell membrane; Peripheral membrane protein; Cytoplasmic side. Belongs to the NAD(P)H dehydrogenase (quinone),Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0003677; GO:0004174; GO:0050660; GO:0016655,GO:0003955,GO:0003955,GO:0003955,GO:0003955,GO:0003955,0.4501,0.4501,0.4501,0.4501,0.4501,5,0.4501,0.3939,no
FSP1_CHICK,E1BR24,ProtTale,Eukaryota,373,"A NAD(P)H-dependent oxidoreductase that acts as a key inhibitor of ferroptosis. At the plasma membrane, catalyzes reduction of coenzyme Q/ubiquinone-10 to ubiquinol-10, a lipophilic radical-trapping antioxidant that prevents lipid oxidative damage and consequently ferroptosis. Acts in parallel to GPX4 to suppress phospholipid peroxidation and ferroptosis. This anti-ferroptotic function is independent of cellular glutathione levels. Also able to catalyze the production of H(2)O(2) and the conversion of FAD to 6-hydroxy-FAD in the presence of oxygen and NAD(P)H; these activities may be specific to chicken enzyme, which contains a specific C-terminal domain and homodimerizes.",Putative FAD-dependent oxidoreductase.,No,No,Vague,No,No,not-Yes,GO:0003677; GO:0004174; GO:0050660; GO:0016655,,GO:0016491,GO:0016491; GO:0071949,,GO:0016491; GO:0071949,,0.4542,0.663,,0.663,3,0.5934,0.3939,no
FSP1_CHICK,E1BR24,Protein2Text,Eukaryota,373,"A NAD(P)H-dependent oxidoreductase that acts as a key inhibitor of ferroptosis. At the plasma membrane, catalyzes reduction of coenzyme Q/ubiquinone-10 to ubiquinol-10, a lipophilic radical-trapping antioxidant that prevents lipid oxidative damage and consequently ferroptosis. Acts in parallel to GPX4 to suppress phospholipid peroxidation and ferroptosis. This anti-ferroptotic function is independent of cellular glutathione levels. Also able to catalyze the production of H(2)O(2) and the conversion of FAD to 6-hydroxy-FAD in the presence of oxygen and NAD(P)H; these activities may be specific to chicken enzyme, which contains a specific C-terminal domain and homodimerizes.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its name, it can be inferred that it is involved in oxidative stress or redox regulation, as its name suggests it may be involved in the regulation of oxygen levels or the reduction of oxidative stress. This is a common function for proteins with similar names, and it would be consistent with the fact that it is being studied in the context of Parkinson's disease.",Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0003677; GO:0004174; GO:0050660; GO:0016655,,,,,,,,,,,0,,0.3939,no
FSP1_CHICK,E1BR24,Reference,Eukaryota,373,"A NAD(P)H-dependent oxidoreductase that acts as a key inhibitor of ferroptosis. At the plasma membrane, catalyzes reduction of coenzyme Q/ubiquinone-10 to ubiquinol-10, a lipophilic radical-trapping antioxidant that prevents lipid oxidative damage and consequently ferroptosis. Acts in parallel to GPX4 to suppress phospholipid peroxidation and ferroptosis. This anti-ferroptotic function is independent of cellular glutathione levels. Also able to catalyze the production of H(2)O(2) and the conversion of FAD to 6-hydroxy-FAD in the presence of oxygen and NAD(P)H; these activities may be specific to chicken enzyme, which contains a specific C-terminal domain and homodimerizes.","A NAD(P)H-dependent oxidoreductase that acts as a key inhibitor of ferroptosis. At the plasma membrane, catalyzes reduction of coenzyme Q/ubiquinone-10 to ubiquinol-10, a lipophilic radical-trapping antioxidant that prevents lipid oxidative damage and consequently ferroptosis. Acts in parallel to GPX4 to suppress phospholipid peroxidation and ferroptosis. This anti-ferroptotic function is independent of cellular glutathione levels. Also able to catalyze the production of H(2)O(2) and the conversion of FAD to 6-hydroxy-FAD in the presence of oxygen and NAD(P)H; these activities may be specific to chicken enzyme, which contains a specific C-terminal domain and homodimerizes.",,,,,,,GO:0003677; GO:0004174; GO:0050660; GO:0016655,GO:0003955,GO:0003955; GO:0016655; GO:0050660,GO:0003955; GO:0050660,GO:0016491; GO:0050660,GO:0016491; GO:0050660,0.4501,0.7819,0.7134,0.6942,0.6942,5,0.6668,0.3939,no
AURK_GIAIC,E2RTQ7,ESM2Text,Eukaryota,311,"Involved in regulation of the cell cycle. Required for mitotic cell division and cytokinesis. Based on its localization to centrosomes and spindle microtubules, as well as to various cytoskeletal components such as the median body, parental attachment disk, and anterior and posterior-lateral paraflagellar dense rods, may coordinate reorganization and segregation of tubulin-containing structures during mitosis and cytokinesis. May regulate microtubule disassembly by phosphorylating cytoskeletal proteins leading to their destabilization. Phosphorylates EB1 at 'Ser-148' in vitro. Phosphorylates histone H3 in vitro.",Phosphorylates specifically the C-terminal domain of the large subunit of RNA polymerase II (RNAPII). This phosphorylation results in negative regulation of RNA polymerase II transcription and in an increased amount of time between initiation and elongation of transcripts. Involved in transcriptional regulation.,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0005524; GO:0008092; GO:0004674,GO:0004674,GO:0004672,GO:0004672,GO:0004672,GO:0004672,0.5406,0.5003,0.5003,0.5003,0.5003,5,0.5084,0.5499,yes
AURK_GIAIC,E2RTQ7,Prot2Text,Eukaryota,311,"Involved in regulation of the cell cycle. Required for mitotic cell division and cytokinesis. Based on its localization to centrosomes and spindle microtubules, as well as to various cytoskeletal components such as the median body, parental attachment disk, and anterior and posterior-lateral paraflagellar dense rods, may coordinate reorganization and segregation of tubulin-containing structures during mitosis and cytokinesis. May regulate microtubule disassembly by phosphorylating cytoskeletal proteins leading to their destabilization. Phosphorylates EB1 at 'Ser-148' in vitro. Phosphorylates histone H3 in vitro.",Mitotic serine/threonine-protein kinase required for cell cycle progression. It is thought that it is phosphorylated by the ste11 protein kinase and that it can phosphorylate the FUS3 and or KSS1 kinases. Plays a role in DNA damage response in megakaryocytes.,Maybe,Yes,Yes,Maybe,No,not-Yes,GO:0005524; GO:0008092; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.5406,0.5406,0.5406,0.5406,0.5406,5,0.5406,0.5499,yes
AURK_GIAIC,E2RTQ7,ProtT3,Eukaryota,311,"Involved in regulation of the cell cycle. Required for mitotic cell division and cytokinesis. Based on its localization to centrosomes and spindle microtubules, as well as to various cytoskeletal components such as the median body, parental attachment disk, and anterior and posterior-lateral paraflagellar dense rods, may coordinate reorganization and segregation of tubulin-containing structures during mitosis and cytokinesis. May regulate microtubule disassembly by phosphorylating cytoskeletal proteins leading to their destabilization. Phosphorylates EB1 at 'Ser-148' in vitro. Phosphorylates histone H3 in vitro.",Nucleus. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0008092; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,0.8331,0.8331,0.8331,0.8331,0.5406,5,0.7746,0.5499,yes
AURK_GIAIC,E2RTQ7,ProtTale,Eukaryota,311,"Involved in regulation of the cell cycle. Required for mitotic cell division and cytokinesis. Based on its localization to centrosomes and spindle microtubules, as well as to various cytoskeletal components such as the median body, parental attachment disk, and anterior and posterior-lateral paraflagellar dense rods, may coordinate reorganization and segregation of tubulin-containing structures during mitosis and cytokinesis. May regulate microtubule disassembly by phosphorylating cytoskeletal proteins leading to their destabilization. Phosphorylates EB1 at 'Ser-148' in vitro. Phosphorylates histone H3 in vitro.","Serine/threonine kinase that plays a central role in spindle assembly checkpoint signaling. The spindle assembly checkpoint (SAC) is a mechanism that safeguards chromosome segregation by checking the proper formation of kinetochore-spindle microtubule attachments. The SAC is activated when unattached kinetochores respond poorly to signals that trigger mitotic progression, such as loss of microtubule attachment or DNA damage. Stimulates the anaphase-promoting complex/cyclosome (APC/C), which is the key regulator of APC/C-mediated degradation of cyclin B1 (ccn1), leading to the activation of the APC/C",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0008092; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,0.8331,0.8331,0.8331,0.5406,0.8331,5,0.7746,0.5499,yes
AURK_GIAIC,E2RTQ7,Protein2Text,Eukaryota,311,"Involved in regulation of the cell cycle. Required for mitotic cell division and cytokinesis. Based on its localization to centrosomes and spindle microtubules, as well as to various cytoskeletal components such as the median body, parental attachment disk, and anterior and posterior-lateral paraflagellar dense rods, may coordinate reorganization and segregation of tubulin-containing structures during mitosis and cytokinesis. May regulate microtubule disassembly by phosphorylating cytoskeletal proteins leading to their destabilization. Phosphorylates EB1 at 'Ser-148' in vitro. Phosphorylates histone H3 in vitro.","The molecular function of this protein is a protein kinase. Specifically, it is a serine/threonine-protein kinase.",Maybe,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0005524; GO:0008092; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.5406,0.5406,0.5406,0.5406,0.5406,5,0.5406,0.5499,yes
AURK_GIAIC,E2RTQ7,Reference,Eukaryota,311,"Involved in regulation of the cell cycle. Required for mitotic cell division and cytokinesis. Based on its localization to centrosomes and spindle microtubules, as well as to various cytoskeletal components such as the median body, parental attachment disk, and anterior and posterior-lateral paraflagellar dense rods, may coordinate reorganization and segregation of tubulin-containing structures during mitosis and cytokinesis. May regulate microtubule disassembly by phosphorylating cytoskeletal proteins leading to their destabilization. Phosphorylates EB1 at 'Ser-148' in vitro. Phosphorylates histone H3 in vitro.","Involved in regulation of the cell cycle. Required for mitotic cell division and cytokinesis. Based on its localization to centrosomes and spindle microtubules, as well as to various cytoskeletal components such as the median body, parental attachment disk, and anterior and posterior-lateral paraflagellar dense rods, may coordinate reorganization and segregation of tubulin-containing structures during mitosis and cytokinesis. May regulate microtubule disassembly by phosphorylating cytoskeletal proteins leading to their destabilization. Phosphorylates EB1 at 'Ser-148' in vitro. Phosphorylates histone H3 in vitro.",,,,,,,GO:0005524; GO:0008092; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.8331,0.8331,0.8331,0.8331,0.8331,5,0.8331,0.5499,yes
GH1A_CALOW,E4Q361,ESM2Text,Bacteria,452,"Has high beta-D-glucosidase, exoglucanase, beta-D-xylosidase, beta-D-galactosidase, and transgalactosylation activities in vitro. Has a very broad substrate specificity with the highest activity with p- nitrophenyl beta-D-galactopyranoside (pNPGal) as substrate. Active with pNP-beta-D-glucopyranoside (pNPGlu), pNP-beta-D-cellobioside (pNPC), lactose, pNP-beta-D-xylopyranoside (pNPX) and cellobiose in the order of decreasing activity, respectively. Very low activity with soluble polysaccharides synanthrin and locust bean gum. Very low, but detectable activity with insoluble substrates such as cotton and filter paper. No activity with pNP-alpha-L-arabinofuranoside (pNPAr) or carboxymethylcellulose (CMC) as substrates. Synthesizes galactooligosaccharides (GalOS) from lactose. Hydrolyzes pretreated corn stover releasing both glucose and xylose. This multifunctional enzyme may provide C.owensensis the benefit of utilizing a wide variety of available carbon sources in its natural growing environment as the ability to convert a wide range of soluble oligosaccharides to monoses is required in order to assimilate them.","BglA is intracellular and modulates the levels of its corresponding cellobiose. In the absence of glucose A, forms a water-binding hetero-substrate complex with bglA, leading to rapid intracellular A-glucose accumulation. In the presence of glucose A, the hetero-polysaccharide-binding activity increases, leading to rapid intracellular A-glucose accumulation.",Vague,Vague,Maybe,Maybe,Maybe,not-Yes,GO:0004565; GO:0008422; GO:0016162; GO:0031217; GO:0009044,,GO:0008422,GO:0008422,GO:0008422,GO:0008422,,0.7665,0.7665,0.7665,0.7665,4,0.7665,0.1454,no
GH1A_CALOW,E4Q361,Prot2Text,Bacteria,452,"Has high beta-D-glucosidase, exoglucanase, beta-D-xylosidase, beta-D-galactosidase, and transgalactosylation activities in vitro. Has a very broad substrate specificity with the highest activity with p- nitrophenyl beta-D-galactopyranoside (pNPGal) as substrate. Active with pNP-beta-D-glucopyranoside (pNPGlu), pNP-beta-D-cellobioside (pNPC), lactose, pNP-beta-D-xylopyranoside (pNPX) and cellobiose in the order of decreasing activity, respectively. Very low activity with soluble polysaccharides synanthrin and locust bean gum. Very low, but detectable activity with insoluble substrates such as cotton and filter paper. No activity with pNP-alpha-L-arabinofuranoside (pNPAr) or carboxymethylcellulose (CMC) as substrates. Synthesizes galactooligosaccharides (GalOS) from lactose. Hydrolyzes pretreated corn stover releasing both glucose and xylose. This multifunctional enzyme may provide C.owensensis the benefit of utilizing a wide variety of available carbon sources in its natural growing environment as the ability to convert a wide range of soluble oligosaccharides to monoses is required in order to assimilate them.","Is able to hydrolyze aryl-beta-D-glucosides such as 4-methylumbelliferyl-beta-D-glucopyranoside (MUG-beta-Glc), phosphoarbutin and phosphosalicin. Is not essential for growth on arbutin or salicin as the sole carbon source.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004565; GO:0008422; GO:0016162; GO:0031217; GO:0009044,GO:0008422,GO:0008422,GO:0008422,GO:0008422,GO:0008422,0.7665,0.7665,0.7665,0.7665,0.7665,5,0.7665,0.1454,no
GH1A_CALOW,E4Q361,ProtT3,Bacteria,452,"Has high beta-D-glucosidase, exoglucanase, beta-D-xylosidase, beta-D-galactosidase, and transgalactosylation activities in vitro. Has a very broad substrate specificity with the highest activity with p- nitrophenyl beta-D-galactopyranoside (pNPGal) as substrate. Active with pNP-beta-D-glucopyranoside (pNPGlu), pNP-beta-D-cellobioside (pNPC), lactose, pNP-beta-D-xylopyranoside (pNPX) and cellobiose in the order of decreasing activity, respectively. Very low activity with soluble polysaccharides synanthrin and locust bean gum. Very low, but detectable activity with insoluble substrates such as cotton and filter paper. No activity with pNP-alpha-L-arabinofuranoside (pNPAr) or carboxymethylcellulose (CMC) as substrates. Synthesizes galactooligosaccharides (GalOS) from lactose. Hydrolyzes pretreated corn stover releasing both glucose and xylose. This multifunctional enzyme may provide C.owensensis the benefit of utilizing a wide variety of available carbon sources in its natural growing environment as the ability to convert a wide range of soluble oligosaccharides to monoses is required in order to assimilate them.",Belongs to the glycosyl hydrolase 1 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004565; GO:0008422; GO:0016162; GO:0031217; GO:0009044,GO:0016798,GO:0004553,GO:0004553,GO:0004553,GO:0016798,0.6638,0.7756,0.7756,0.7756,0.6638,5,0.7309,0.1454,no
GH1A_CALOW,E4Q361,ProtTale,Bacteria,452,"Has high beta-D-glucosidase, exoglucanase, beta-D-xylosidase, beta-D-galactosidase, and transgalactosylation activities in vitro. Has a very broad substrate specificity with the highest activity with p- nitrophenyl beta-D-galactopyranoside (pNPGal) as substrate. Active with pNP-beta-D-glucopyranoside (pNPGlu), pNP-beta-D-cellobioside (pNPC), lactose, pNP-beta-D-xylopyranoside (pNPX) and cellobiose in the order of decreasing activity, respectively. Very low activity with soluble polysaccharides synanthrin and locust bean gum. Very low, but detectable activity with insoluble substrates such as cotton and filter paper. No activity with pNP-alpha-L-arabinofuranoside (pNPAr) or carboxymethylcellulose (CMC) as substrates. Synthesizes galactooligosaccharides (GalOS) from lactose. Hydrolyzes pretreated corn stover releasing both glucose and xylose. This multifunctional enzyme may provide C.owensensis the benefit of utilizing a wide variety of available carbon sources in its natural growing environment as the ability to convert a wide range of soluble oligosaccharides to monoses is required in order to assimilate them.","Binds and hydrolyzes 4-O-beta-D-glucopyranosyl-D-xylo-pyranoside (gluco-xylo-pyranoside), but not 4-O-beta-D-glucopyranosyl-L-arabino-pyranoside (gluco-arabino-pyranoside), 4-O-beta-D-glucopyranosyl-D-galacto-pyranoside (gluco-galacto-pyranoside), 4-O-beta-D-glucopyranosyl-L-ar",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004565; GO:0008422; GO:0016162; GO:0031217; GO:0009044,GO:0004553,GO:0004553,GO:0004553,GO:0016798,GO:0004553,0.7756,0.7756,0.7756,0.6638,0.7756,5,0.7532,0.1454,no
GH1A_CALOW,E4Q361,Protein2Text,Bacteria,452,"Has high beta-D-glucosidase, exoglucanase, beta-D-xylosidase, beta-D-galactosidase, and transgalactosylation activities in vitro. Has a very broad substrate specificity with the highest activity with p- nitrophenyl beta-D-galactopyranoside (pNPGal) as substrate. Active with pNP-beta-D-glucopyranoside (pNPGlu), pNP-beta-D-cellobioside (pNPC), lactose, pNP-beta-D-xylopyranoside (pNPX) and cellobiose in the order of decreasing activity, respectively. Very low activity with soluble polysaccharides synanthrin and locust bean gum. Very low, but detectable activity with insoluble substrates such as cotton and filter paper. No activity with pNP-alpha-L-arabinofuranoside (pNPAr) or carboxymethylcellulose (CMC) as substrates. Synthesizes galactooligosaccharides (GalOS) from lactose. Hydrolyzes pretreated corn stover releasing both glucose and xylose. This multifunctional enzyme may provide C.owensensis the benefit of utilizing a wide variety of available carbon sources in its natural growing environment as the ability to convert a wide range of soluble oligosaccharides to monoses is required in order to assimilate them.",This protein is involved in catalyzing the hydrolysis of certain compounds.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004565; GO:0008422; GO:0016162; GO:0031217; GO:0009044,GO:0016787,GO:0016787,,,GO:0016787,0.5515,0.5515,,,0.5515,3,0.5515,0.1454,no
GH1A_CALOW,E4Q361,Reference,Bacteria,452,"Has high beta-D-glucosidase, exoglucanase, beta-D-xylosidase, beta-D-galactosidase, and transgalactosylation activities in vitro. Has a very broad substrate specificity with the highest activity with p- nitrophenyl beta-D-galactopyranoside (pNPGal) as substrate. Active with pNP-beta-D-glucopyranoside (pNPGlu), pNP-beta-D-cellobioside (pNPC), lactose, pNP-beta-D-xylopyranoside (pNPX) and cellobiose in the order of decreasing activity, respectively. Very low activity with soluble polysaccharides synanthrin and locust bean gum. Very low, but detectable activity with insoluble substrates such as cotton and filter paper. No activity with pNP-alpha-L-arabinofuranoside (pNPAr) or carboxymethylcellulose (CMC) as substrates. Synthesizes galactooligosaccharides (GalOS) from lactose. Hydrolyzes pretreated corn stover releasing both glucose and xylose. This multifunctional enzyme may provide C.owensensis the benefit of utilizing a wide variety of available carbon sources in its natural growing environment as the ability to convert a wide range of soluble oligosaccharides to monoses is required in order to assimilate them.","Has high beta-D-glucosidase, exoglucanase, beta-D-xylosidase, beta-D-galactosidase, and transgalactosylation activities in vitro. Has a very broad substrate specificity with the highest activity with p- nitrophenyl beta-D-galactopyranoside (pNPGal) as substrate. Active with pNP-beta-D-glucopyranoside (pNPGlu), pNP-beta-D-cellobioside (pNPC), lactose, pNP-beta-D-xylopyranoside (pNPX) and cellobiose in the order of decreasing activity, respectively. Very low activity with soluble polysaccharides synanthrin and locust bean gum. Very low, but detectable activity with insoluble substrates such as cotton and filter paper. No activity with pNP-alpha-L-arabinofuranoside (pNPAr) or carboxymethylcellulose (CMC) as substrates. Synthesizes galactooligosaccharides (GalOS) from lactose. Hydrolyzes pretreated corn stover releasing both glucose and xylose. This multifunctional enzyme may provide C.owensensis the benefit of utilizing a wide variety of available carbon sources in its natural growing environment as the ability to convert a wide range of soluble oligosaccharides to monoses is required in order to assimilate them.",,,,,,,GO:0004565; GO:0008422; GO:0016162; GO:0031217; GO:0009044,GO:0008422; GO:0004565; GO:0031177; GO:0004553,GO:0008422; GO:0004565; GO:0004553,GO:0008422; GO:0009044; GO:0004565,GO:0008422; GO:0004553; GO:0008236,GO:0008422; GO:0004553; GO:0008236,0.8254,0.9184,0.9388,0.804,0.804,5,0.8581,0.1454,no
POLG_HRV15,E5D8F2,ESM2Text,Viruses,2153,"[Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. The VP1 C-termini form 60 dominant spike-like protrusions on the surface of the virion. Capsid protein VP1 interacts with host cell receptor CDHR3 to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm.",Promotes the exchange of Ras-bound GDP by GTP.,No,No,No,No,No,not-Yes,GO:0005524; GO:0015267; GO:0004197; GO:0017111; GO:0003723; GO:0003724; GO:0003968; GO:0005198; GO:0008270,GO:0005085,GO:0005085,GO:0005085,GO:0005085,GO:0005085,0.1061,0.1061,0.1061,0.1061,0.1061,5,0.1061,0.4034,no
POLG_HRV15,E5D8F2,Prot2Text,Viruses,2153,"[Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. The VP1 C-termini form 60 dominant spike-like protrusions on the surface of the virion. Capsid protein VP1 interacts with host cell receptor CDHR3 to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm.","Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways.",No,No,No,No,No,not-Yes,GO:0005524; GO:0015267; GO:0004197; GO:0017111; GO:0003723; GO:0003724; GO:0003968; GO:0005198; GO:0008270,,,,,,,,,,,0,,0.4034,no
POLG_HRV15,E5D8F2,ProtT3,Viruses,2153,"[Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. The VP1 C-termini form 60 dominant spike-like protrusions on the surface of the virion. Capsid protein VP1 interacts with host cell receptor CDHR3 to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm.","The coat protein (CP) is a virion-associated protein that self-assembles to form an icosahedral capsid with a T=3 symmetry, about 30 nm in diameter, and consisting of 60 CP subunits. Virion. Belongs to the icosahedral plant coat protein family",Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0005524; GO:0015267; GO:0004197; GO:0017111; GO:0003723; GO:0003724; GO:0003968; GO:0005198; GO:0008270,,,GO:0005198,GO:0005198,,,,0.3433,0.3433,,2,0.3433,0.4034,no
POLG_HRV15,E5D8F2,ProtTale,Viruses,2153,"[Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. The VP1 C-termini form 60 dominant spike-like protrusions on the surface of the virion. Capsid protein VP1 interacts with host cell receptor CDHR3 to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm.","[Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 forms an icosahedral capsid with a T=3 symmetry consisting of 120 copies, with VP2 and VP3 forming a dense core. The capsid encapsulates the viral positive strand RNA (virus genome) that is encapsulated within the particle. Capsid protein VP1 is required for infectivity.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0015267; GO:0004197; GO:0017111; GO:0003723; GO:0003724; GO:0003968; GO:0005198; GO:0008270,,,GO:0005198,,GO:0005198,,,0.3433,,0.3433,2,0.3433,0.4034,no
POLG_HRV15,E5D8F2,Protein2Text,Viruses,2153,"[Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. The VP1 C-termini form 60 dominant spike-like protrusions on the surface of the virion. Capsid protein VP1 interacts with host cell receptor CDHR3 to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm.","This protein is a structural protein, specifically a viral protein. It is a component of the viral capsid, which is the protein shell that encloses the viral genome. The molecular function of this protein is to provide structural support and protection to the viral genome, allowing it to be transmitted and replicated within host cells.",Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0005524; GO:0015267; GO:0004197; GO:0017111; GO:0003723; GO:0003724; GO:0003968; GO:0005198; GO:0008270,,GO:0005198,GO:0005198,GO:0005198,GO:0005198,,0.3433,0.3433,0.3433,0.3433,4,0.3433,0.4034,no
POLG_HRV15,E5D8F2,Reference,Viruses,2153,"[Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. The VP1 C-termini form 60 dominant spike-like protrusions on the surface of the virion. Capsid protein VP1 interacts with host cell receptor CDHR3 to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm.","[Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. The VP1 C-termini form 60 dominant spike-like protrusions on the surface of the virion. Capsid protein VP1 interacts with host cell receptor CDHR3 to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm.",,,,,,,GO:0005524; GO:0015267; GO:0004197; GO:0017111; GO:0003723; GO:0003724; GO:0003968; GO:0005198; GO:0008270,GO:0005198; GO:0001618,GO:0001618; GO:0005198,,,,0.3514,0.3514,,,,2,0.3514,0.4034,no
NOL9_DANRE,E7F654,ESM2Text,Eukaryota,713,Polynucleotide kinase that can phosphorylate the 5'-hydroxyl groups of single-stranded and double-stranded RNA and DNA substrates. Required for the efficient pre-rRNA processing of internal transcribed spacer 2 (ITS2). Essential for definitive hematopoiesis and pancreas morphogenesis.,"Polynucleotide 5'-kinase involved in rRNA processing. In the nucleus, acts as a transcriptional repressor of PRP3 and as a transcriptional activator of ESR1. Also functions as a mRNA 5'-kinase and is required for mRNA splicing.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0051734; GO:0051731; GO:0003723,GO:0016301,GO:0051731,GO:0051731,GO:0016301,GO:0051731,0.4466,0.6113,0.6113,0.4466,0.6113,5,0.5454,0.5674,yes
NOL9_DANRE,E7F654,Prot2Text,Eukaryota,713,Polynucleotide kinase that can phosphorylate the 5'-hydroxyl groups of single-stranded and double-stranded RNA and DNA substrates. Required for the efficient pre-rRNA processing of internal transcribed spacer 2 (ITS2). Essential for definitive hematopoiesis and pancreas morphogenesis.,Polynucleotide 5'-kinase involved in rRNA processing.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0051734; GO:0051731; GO:0003723,GO:0051731,,GO:0051731,GO:0004672,GO:0051731,0.6113,,0.6113,0.4243,0.6113,4,0.5645,0.5674,yes
NOL9_DANRE,E7F654,ProtT3,Eukaryota,713,Polynucleotide kinase that can phosphorylate the 5'-hydroxyl groups of single-stranded and double-stranded RNA and DNA substrates. Required for the efficient pre-rRNA processing of internal transcribed spacer 2 (ITS2). Essential for definitive hematopoiesis and pancreas morphogenesis.,"Polynucleotide 5'-kinase involved in rRNA processing. Nucleus, nucleolus. Belongs to the Clp1 family. NOL9/GRC3 subfamily",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0051734; GO:0051731; GO:0003723,GO:0016301; GO:0005524,GO:0019201,GO:0004651; GO:0005524,GO:0004651,GO:0051731,0.6982,0.4076,0.4313,0.1169,0.6113,5,0.4531,0.5674,yes
NOL9_DANRE,E7F654,ProtTale,Eukaryota,713,Polynucleotide kinase that can phosphorylate the 5'-hydroxyl groups of single-stranded and double-stranded RNA and DNA substrates. Required for the efficient pre-rRNA processing of internal transcribed spacer 2 (ITS2). Essential for definitive hematopoiesis and pancreas morphogenesis.,"Polynucleotide kinase that can phosphorylate the 5'-hydroxyl groups of single-stranded and double-stranded RNA and DNA substrates. Involved in rRNA processing and to a lesser extent in mRNA processing. Involved in the RNA-directed DNA methylation (RdDM) pathway and is required for a functional RdDM pathway. Required for the maintenance of epigenetic gene silencing, but not for de novo DNA methylation.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0051734; GO:0051731; GO:0003723,GO:0019158; GO:0005524,GO:0051731; GO:0005524,GO:0008439; GO:0005524,GO:0019201; GO:0005524,GO:0004651,0.6431,0.8446,0.4522,0.6749,0.1169,5,0.5463,0.5674,yes
NOL9_DANRE,E7F654,Protein2Text,Eukaryota,713,Polynucleotide kinase that can phosphorylate the 5'-hydroxyl groups of single-stranded and double-stranded RNA and DNA substrates. Required for the efficient pre-rRNA processing of internal transcribed spacer 2 (ITS2). Essential for definitive hematopoiesis and pancreas morphogenesis.,This protein is involved in molecular function related to RNA binding.,Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0005524; GO:0051734; GO:0051731; GO:0003723,GO:0003723,GO:0003723,GO:0003723,GO:0003723,GO:0003723,0.4731,0.4731,0.4731,0.4731,0.4731,5,0.4731,0.5674,yes
NOL9_DANRE,E7F654,Reference,Eukaryota,713,Polynucleotide kinase that can phosphorylate the 5'-hydroxyl groups of single-stranded and double-stranded RNA and DNA substrates. Required for the efficient pre-rRNA processing of internal transcribed spacer 2 (ITS2). Essential for definitive hematopoiesis and pancreas morphogenesis.,Polynucleotide kinase that can phosphorylate the 5'-hydroxyl groups of single-stranded and double-stranded RNA and DNA substrates. Required for the efficient pre-rRNA processing of internal transcribed spacer 2 (ITS2). Essential for definitive hematopoiesis and pancreas morphogenesis.,,,,,,,GO:0005524; GO:0051734; GO:0051731; GO:0003723,GO:0016301; GO:0005524,GO:0004691; GO:0005524,GO:0051731; GO:0005524,GO:0016301; GO:0005524,GO:0019114; GO:0005524,0.6982,0.6045,0.8446,0.6982,0.4522,5,0.6595,0.5674,yes
ASOR_PYRFU,E7FHH1,ESM2Text,Archaea,624,"WOR-like catalytic subunit of an oxidoreductase that can desulfonate and oxidize aliphatic sulfonates such as taurine. The activity involves two steps: an oxidative desulfonation reaction, followed by the activation of a second water molecule and oxidation of the resulting aldehyde. May be involved in the oxidation of various aliphatic sulfonates and also phosphonates. In vitro, has a broad substrate specificity with a high affinity for several substituted and nonsubstituted aliphatic and aromatic aldehydes with various chain lengths, with methyl viologen or benzyl viologen as electron acceptor. Ferredoxin is the physiological electron acceptor.",Catalyzes the reversible phosphorylation of pyruvate and glycolytic acid. May have a role in providing carbon for growth.,No,No,No,No,No,not-Yes,GO:0051539; GO:0009055; GO:0046872; GO:0016625,GO:0004743,GO:0004743,,GO:0004743,GO:0004743,0.1707,0.1707,,0.1707,0.1707,4,0.1707,0.2953,no
ASOR_PYRFU,E7FHH1,Prot2Text,Archaea,624,"WOR-like catalytic subunit of an oxidoreductase that can desulfonate and oxidize aliphatic sulfonates such as taurine. The activity involves two steps: an oxidative desulfonation reaction, followed by the activation of a second water molecule and oxidation of the resulting aldehyde. May be involved in the oxidation of various aliphatic sulfonates and also phosphonates. In vitro, has a broad substrate specificity with a high affinity for several substituted and nonsubstituted aliphatic and aromatic aldehydes with various chain lengths, with methyl viologen or benzyl viologen as electron acceptor. Ferredoxin is the physiological electron acceptor.","Catalyzes the reversible interconversion of glycerol 3-phosphate and glycerol 1-phosphate, providing an organic means for the developing embryo to utilize glycerol as a carbon source.",No,No,No,No,No,not-Yes,GO:0051539; GO:0009055; GO:0046872; GO:0016625,,,,GO:0016491,,,,,0.407,,1,0.407,0.2953,no
ASOR_PYRFU,E7FHH1,ProtT3,Archaea,624,"WOR-like catalytic subunit of an oxidoreductase that can desulfonate and oxidize aliphatic sulfonates such as taurine. The activity involves two steps: an oxidative desulfonation reaction, followed by the activation of a second water molecule and oxidation of the resulting aldehyde. May be involved in the oxidation of various aliphatic sulfonates and also phosphonates. In vitro, has a broad substrate specificity with a high affinity for several substituted and nonsubstituted aliphatic and aromatic aldehydes with various chain lengths, with methyl viologen or benzyl viologen as electron acceptor. Ferredoxin is the physiological electron acceptor.",In the C-terminal section; belongs to the AOR/VOR 30 kDa subunit family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0051539; GO:0009055; GO:0046872; GO:0016625,,GO:0016491,GO:0016491,GO:0016491,,,0.407,0.407,0.407,,3,0.407,0.2953,no
ASOR_PYRFU,E7FHH1,ProtTale,Archaea,624,"WOR-like catalytic subunit of an oxidoreductase that can desulfonate and oxidize aliphatic sulfonates such as taurine. The activity involves two steps: an oxidative desulfonation reaction, followed by the activation of a second water molecule and oxidation of the resulting aldehyde. May be involved in the oxidation of various aliphatic sulfonates and also phosphonates. In vitro, has a broad substrate specificity with a high affinity for several substituted and nonsubstituted aliphatic and aromatic aldehydes with various chain lengths, with methyl viologen or benzyl viologen as electron acceptor. Ferredoxin is the physiological electron acceptor.",Catalyzes the oxidation of carbon monoxide to carbon dioxide.,No,No,No,No,No,not-Yes,GO:0051539; GO:0009055; GO:0046872; GO:0016625,GO:0018492,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.0,0.407,0.407,0.407,0.407,5,0.3256,0.2953,no
ASOR_PYRFU,E7FHH1,Protein2Text,Archaea,624,"WOR-like catalytic subunit of an oxidoreductase that can desulfonate and oxidize aliphatic sulfonates such as taurine. The activity involves two steps: an oxidative desulfonation reaction, followed by the activation of a second water molecule and oxidation of the resulting aldehyde. May be involved in the oxidation of various aliphatic sulfonates and also phosphonates. In vitro, has a broad substrate specificity with a high affinity for several substituted and nonsubstituted aliphatic and aromatic aldehydes with various chain lengths, with methyl viologen or benzyl viologen as electron acceptor. Ferredoxin is the physiological electron acceptor.","The molecular function of this protein is an oxidoreductase activity, specifically an oxidoreductase that catalyzes the oxidation of a substrate. More specifically, it is a dehydrogenase that catalyzes the oxidation of a substrate using NAD or NADP as an electron acceptor.",Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0051539; GO:0009055; GO:0046872; GO:0016625,GO:0016491,GO:0016491; GO:0016616,,GO:0016491,GO:0016491,0.407,0.4166,,0.407,0.407,4,0.4094,0.2953,no
ASOR_PYRFU,E7FHH1,Reference,Archaea,624,"WOR-like catalytic subunit of an oxidoreductase that can desulfonate and oxidize aliphatic sulfonates such as taurine. The activity involves two steps: an oxidative desulfonation reaction, followed by the activation of a second water molecule and oxidation of the resulting aldehyde. May be involved in the oxidation of various aliphatic sulfonates and also phosphonates. In vitro, has a broad substrate specificity with a high affinity for several substituted and nonsubstituted aliphatic and aromatic aldehydes with various chain lengths, with methyl viologen or benzyl viologen as electron acceptor. Ferredoxin is the physiological electron acceptor.","WOR-like catalytic subunit of an oxidoreductase that can desulfonate and oxidize aliphatic sulfonates such as taurine. The activity involves two steps: an oxidative desulfonation reaction, followed by the activation of a second water molecule and oxidation of the resulting aldehyde. May be involved in the oxidation of various aliphatic sulfonates and also phosphonates. In vitro, has a broad substrate specificity with a high affinity for several substituted and nonsubstituted aliphatic and aromatic aldehydes with various chain lengths, with methyl viologen or benzyl viologen as electron acceptor. Ferredoxin is the physiological electron acceptor.",,,,,,,GO:0051539; GO:0009055; GO:0046872; GO:0016625,GO:0016491; GO:0016903,GO:0016491,GO:0016903,GO:0016491,GO:0016491,0.5047,0.407,0.4424,0.407,0.407,5,0.4336,0.2953,no
MDL_GRATM,E8WYN5,ESM2Text,Bacteria,131,Hydroxynitrile lyase which catalyzes mandelonitrile formation from benzaldehyde and hydrogen cyanide with high stereoselectivity in presence of manganese.,"Catalyzes the phosphorolysis of diverse pyrimidine nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use CTP, GTP, UTP and, less efficiently, TTP. May play a role in the degradation of carbazole.",No,No,No,No,No,not-Yes,GO:0046593; GO:0046872,,GO:0016154,GO:0016154,GO:0016763,GO:0016154,,0.1628,0.1628,0.1917,0.1628,4,0.17,0.3947,no
MDL_GRATM,E8WYN5,Prot2Text,Bacteria,131,Hydroxynitrile lyase which catalyzes mandelonitrile formation from benzaldehyde and hydrogen cyanide with high stereoselectivity in presence of manganese.,"Involved in the degradation of gentisate. Catalyzes the conversion of gentisate (2,5-dihydroxybenzoate) to maleylpyruvate.",No,No,No,No,No,not-Yes,GO:0046593; GO:0046872,GO:0018579,GO:0018581,GO:0018576,GO:0016702,GO:0018581,0.1498,0.1498,0.1498,0.1722,0.1498,5,0.1543,0.3947,no
MDL_GRATM,E8WYN5,ProtT3,Bacteria,131,Hydroxynitrile lyase which catalyzes mandelonitrile formation from benzaldehyde and hydrogen cyanide with high stereoselectivity in presence of manganese.,Involved in the degradation of L-arginine. Catalyzes the oxidation of L-arginine to N(2)-hydroxy-L-ornithine. Belongs to the arginase family,No,No,No,No,No,not-Yes,GO:0046593; GO:0046872,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0004053,0.2894,0.2894,0.2894,0.2894,0.1628,5,0.2641,0.3947,no
MDL_GRATM,E8WYN5,ProtTale,Bacteria,131,Hydroxynitrile lyase which catalyzes mandelonitrile formation from benzaldehyde and hydrogen cyanide with high stereoselectivity in presence of manganese.,"Involved in the oxidation of ferredoxin. Catalyzes the hydrolysis of 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) to 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTP).",No,No,No,No,No,not-Yes,GO:0046593; GO:0046872,GO:0016491,GO:0016491,GO:0016491,GO:0016491,,0.2894,0.2894,0.2894,0.2894,,4,0.2894,0.3947,no
MDL_GRATM,E8WYN5,Protein2Text,Bacteria,131,Hydroxynitrile lyase which catalyzes mandelonitrile formation from benzaldehyde and hydrogen cyanide with high stereoselectivity in presence of manganese.,"The molecular function of this protein is likely to be a peroxidase, specifically an omega-class peroxidase, given its involvement in oxidative stress and its regulation of reactive oxygen species (ROS).",No,No,No,No,No,not-Yes,GO:0046593; GO:0046872,GO:0004601,GO:0004601,,GO:0004601,GO:0004601,0.1958,0.1958,,0.1958,0.1958,4,0.1958,0.3947,no
MDL_GRATM,E8WYN5,Reference,Bacteria,131,Hydroxynitrile lyase which catalyzes mandelonitrile formation from benzaldehyde and hydrogen cyanide with high stereoselectivity in presence of manganese.,Hydroxynitrile lyase which catalyzes mandelonitrile formation from benzaldehyde and hydrogen cyanide with high stereoselectivity in presence of manganese.,,,,,,,GO:0046593; GO:0046872,GO:0016836,GO:0016829,GO:0047427; GO:0030145,GO:0047558,GO:0047605,0.3006,0.4539,0.4722,0.2554,0.371,5,0.3706,0.3947,no
TENS1_MOUSE,E9Q0S6,ESM2Text,Eukaryota,1888,May act as a protein phosphatase and/or a lipid phosphatase. Involved in fibrillar adhesion formation. Essential for myofibroblast differentiation and myofibroblast-mediated extracellular matrix deposition. Enhances RHOA activation in the presence of DLC1. Plays a role in cell polarization and migration. May be involved in cartilage development and in linking signal transduction pathways to the cytoskeleton.,Involved in in vesicular trafficking and in axon regeneration after axotomy. May function as a scaffold protein involved in the formation of focal adhesion complexes.,No,No,No,No,No,not-Yes,GO:0003779; GO:0004721; GO:0008270,,,,,,,,,,,0,,0.5565,yes
TENS1_MOUSE,E9Q0S6,Prot2Text,Eukaryota,1888,May act as a protein phosphatase and/or a lipid phosphatase. Involved in fibrillar adhesion formation. Essential for myofibroblast differentiation and myofibroblast-mediated extracellular matrix deposition. Enhances RHOA activation in the presence of DLC1. Plays a role in cell polarization and migration. May be involved in cartilage development and in linking signal transduction pathways to the cytoskeleton.,"Involved in fibrillar adhesion formation. May be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton.",Vague,Vague,Vague,Maybe,Maybe,not-Yes,GO:0003779; GO:0004721; GO:0008270,,,,,,,,,,,0,,0.5565,yes
TENS1_MOUSE,E9Q0S6,ProtT3,Eukaryota,1888,May act as a protein phosphatase and/or a lipid phosphatase. Involved in fibrillar adhesion formation. Essential for myofibroblast differentiation and myofibroblast-mediated extracellular matrix deposition. Enhances RHOA activation in the presence of DLC1. Plays a role in cell polarization and migration. May be involved in cartilage development and in linking signal transduction pathways to the cytoskeleton.,Protein-tyrosine phosphatase that acts as a negative regulator of insulin signaling by dephosphorylating and inactivating insulin receptor (IR) and insulin receptor substrate-1 (IRS-1),Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0003779; GO:0004721; GO:0008270,GO:0004725,GO:0004725,GO:0004725,GO:0004725,GO:0004725,0.4929,0.4929,0.4929,0.4929,0.4929,5,0.4929,0.5565,yes
TENS1_MOUSE,E9Q0S6,ProtTale,Eukaryota,1888,May act as a protein phosphatase and/or a lipid phosphatase. Involved in fibrillar adhesion formation. Essential for myofibroblast differentiation and myofibroblast-mediated extracellular matrix deposition. Enhances RHOA activation in the presence of DLC1. Plays a role in cell polarization and migration. May be involved in cartilage development and in linking signal transduction pathways to the cytoskeleton.,May act as a protein phosphatase and/or a tyrosine-protein phosphatase. Involved in the control of cell growth and differentiation. May play an important role in the regulation of cell adhesion and migration. May be involved in the signal transduction of insulin and insulin-like growth factor I (IGF-I). May be involved in the signal transduction of transforming growth factor-alpha (TGF-alpha). May be involved in the signal transduction of the PDGF receptor. May be involved in the signal transduction of the LDL receptor-related protein-1 (LRP1). Plays a role in the regulation of the actin,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0003779; GO:0004721; GO:0008270,,GO:0004725,GO:0004725,GO:0004725,GO:0004725,,0.4929,0.4929,0.4929,0.4929,4,0.4929,0.5565,yes
TENS1_MOUSE,E9Q0S6,Protein2Text,Eukaryota,1888,May act as a protein phosphatase and/or a lipid phosphatase. Involved in fibrillar adhesion formation. Essential for myofibroblast differentiation and myofibroblast-mediated extracellular matrix deposition. Enhances RHOA activation in the presence of DLC1. Plays a role in cell polarization and migration. May be involved in cartilage development and in linking signal transduction pathways to the cytoskeleton.,"The molecular function of the protein is to act as a tyrosine-protein phosphatase, specifically binding and hydrolyzing phosphotyrosine residues on target proteins.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0003779; GO:0004721; GO:0008270,GO:0004725,GO:0004726,GO:0004725,GO:0004725,GO:0004726,0.4929,0.4503,0.4929,0.4929,0.4503,5,0.4759,0.5565,yes
TENS1_MOUSE,E9Q0S6,Reference,Eukaryota,1888,May act as a protein phosphatase and/or a lipid phosphatase. Involved in fibrillar adhesion formation. Essential for myofibroblast differentiation and myofibroblast-mediated extracellular matrix deposition. Enhances RHOA activation in the presence of DLC1. Plays a role in cell polarization and migration. May be involved in cartilage development and in linking signal transduction pathways to the cytoskeleton.,May act as a protein phosphatase and/or a lipid phosphatase. Involved in fibrillar adhesion formation. Essential for myofibroblast differentiation and myofibroblast-mediated extracellular matrix deposition. Enhances RHOA activation in the presence of DLC1. Plays a role in cell polarization and migration. May be involved in cartilage development and in linking signal transduction pathways to the cytoskeleton.,,,,,,,GO:0003779; GO:0004721; GO:0008270,,GO:0016791,,GO:0016791,,,0.4433,,0.4433,,2,0.4433,0.5565,yes
RHBA_ASPFU,E9R5S0,ESM2Text,Eukaryota,187,"Small GTPase that acts as an allosteric activator of the canonical TOR pathway, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth. Plays a role in virulence.",May act as a transcriptional activator with an important role in development.,No,No,No,No,No,not-Yes,GO:0019003; GO:0005525; GO:0003924; GO:0046872,GO:0003700,,,,,0.1244,,,,,1,0.1244,0.3989,no
RHBA_ASPFU,E9R5S0,Prot2Text,Eukaryota,187,"Small GTPase that acts as an allosteric activator of the canonical TOR pathway, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth. Plays a role in virulence.","Activates the protein kinase activity of mTORC1, and thereby plays a role in the regulation of apoptosis. Stimulates the phosphorylation of S6K1 and EIF4EBP1 through activation of mTORC1 signaling. Has low intrinsic GTPase activity.",Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0019003; GO:0005525; GO:0003924; GO:0046872,GO:0003924,GO:0003924,GO:0003924,GO:0003924; GO:0005525,GO:0003924,0.4313,0.4313,0.4313,0.8553,0.4313,5,0.5161,0.3989,no
RHBA_ASPFU,E9R5S0,ProtT3,Eukaryota,187,"Small GTPase that acts as an allosteric activator of the canonical TOR pathway, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth. Plays a role in virulence.",Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Cell membrane; Lipid-anchor; Cytoplasmic side. Belongs to the small GTPase superfamily. Ras family,Vague,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0019003; GO:0005525; GO:0003924; GO:0046872,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,0.8553,0.8553,0.8553,0.8553,0.8553,5,0.8553,0.3989,no
RHBA_ASPFU,E9R5S0,ProtTale,Eukaryota,187,"Small GTPase that acts as an allosteric activator of the canonical TOR pathway, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth. Plays a role in virulence.",Binds GTP and exhibits intrinsic GTPase activity. May activate NF-kappa-B-dependent transcription. Promotes the activation of RAC1 and promotes its translocation to the nucleus.,Vague,Maybe,Yes,Vague,Maybe,not-Yes,GO:0019003; GO:0005525; GO:0003924; GO:0046872,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,0.8553,0.8553,0.8553,0.8553,0.8553,5,0.8553,0.3989,no
RHBA_ASPFU,E9R5S0,Protein2Text,Eukaryota,187,"Small GTPase that acts as an allosteric activator of the canonical TOR pathway, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth. Plays a role in virulence.","The molecular function of this protein is not explicitly stated in the provided information. However, based on its name, it is likely to be a Ras-related protein, which typically functions as a GTPase involved in signal transduction pathways.",Maybe,Maybe,Yes,Maybe,Vague,not-Yes,GO:0019003; GO:0005525; GO:0003924; GO:0046872,GO:0003924,GO:0003924,,GO:0003924,GO:0003924,0.4313,0.4313,,0.4313,0.4313,4,0.4313,0.3989,no
RHBA_ASPFU,E9R5S0,Reference,Eukaryota,187,"Small GTPase that acts as an allosteric activator of the canonical TOR pathway, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth. Plays a role in virulence.","Small GTPase that acts as an allosteric activator of the canonical TOR pathway, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth. Plays a role in virulence.",,,,,,,GO:0019003; GO:0005525; GO:0003924; GO:0046872,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0005525; GO:0003924,0.8553,0.8553,0.8553,0.8553,0.8553,5,0.8553,0.3989,no
PINA_SACI5,F0NID4,ESM2Text,Archaea,505,"Promotes Holliday junction (HJ) branch migration and unwinds Y-shaped DNA (but not replication forks or dsDNA) in an ATP hydrolysis- dependent manner. Stimulates cleavage by HJ resolvase Hjc. Unwinds Y-shaped and 3'-flap DNA substrates. In the absence of other proteins stabilizes replication forks (prevents spontaneous unwinding); Hjc, Hjm (Hel308) and PINA coordinate HJ migration and cleavage of replication forks in a coordinated way. Inhibits the 5'-3' (but not 3'-5') helicase activity of helicase Hjm (Hel308) on overhang DNA. Probably acts as an ATP-dependent pump that pulls DNA through the hexamer.","ATPase component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers. PilA is an ATPase component that catalyzes the hydrolysis of ATP coupled to the transport of substrates across the T4P inner membrane. PilB acts as a key regulatory subunit that coordinates PilA's ATP-dependent re-entry into the cell, and PilA's ATP-dependent re-entry into the cell.",No,No,No,No,No,not-Yes,GO:0005524; GO:0003677; GO:0009378; GO:0016787,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887,GO:0016887,GO:0016887,0.5555,0.5555,0.2706,0.2706,0.2706,5,0.3846,0.3643,no
PINA_SACI5,F0NID4,Prot2Text,Archaea,505,"Promotes Holliday junction (HJ) branch migration and unwinds Y-shaped DNA (but not replication forks or dsDNA) in an ATP hydrolysis- dependent manner. Stimulates cleavage by HJ resolvase Hjc. Unwinds Y-shaped and 3'-flap DNA substrates. In the absence of other proteins stabilizes replication forks (prevents spontaneous unwinding); Hjc, Hjm (Hel308) and PINA coordinate HJ migration and cleavage of replication forks in a coordinated way. Inhibits the 5'-3' (but not 3'-5') helicase activity of helicase Hjm (Hel308) on overhang DNA. Probably acts as an ATP-dependent pump that pulls DNA through the hexamer.",When complexed with LnaE2 to form the unphosphorylated form of LnaC.,Vague,Vague,Vague,No,No,not-Yes,GO:0005524; GO:0003677; GO:0009378; GO:0016787,,,,,,,,,,,0,,0.3643,no
PINA_SACI5,F0NID4,ProtT3,Archaea,505,"Promotes Holliday junction (HJ) branch migration and unwinds Y-shaped DNA (but not replication forks or dsDNA) in an ATP hydrolysis- dependent manner. Stimulates cleavage by HJ resolvase Hjc. Unwinds Y-shaped and 3'-flap DNA substrates. In the absence of other proteins stabilizes replication forks (prevents spontaneous unwinding); Hjc, Hjm (Hel308) and PINA coordinate HJ migration and cleavage of replication forks in a coordinated way. Inhibits the 5'-3' (but not 3'-5') helicase activity of helicase Hjm (Hel308) on overhang DNA. Probably acts as an ATP-dependent pump that pulls DNA through the hexamer.",Belongs to the UPF0253 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0003677; GO:0009378; GO:0016787,,,,,,,,,,,0,,0.3643,no
PINA_SACI5,F0NID4,ProtTale,Archaea,505,"Promotes Holliday junction (HJ) branch migration and unwinds Y-shaped DNA (but not replication forks or dsDNA) in an ATP hydrolysis- dependent manner. Stimulates cleavage by HJ resolvase Hjc. Unwinds Y-shaped and 3'-flap DNA substrates. In the absence of other proteins stabilizes replication forks (prevents spontaneous unwinding); Hjc, Hjm (Hel308) and PINA coordinate HJ migration and cleavage of replication forks in a coordinated way. Inhibits the 5'-3' (but not 3'-5') helicase activity of helicase Hjm (Hel308) on overhang DNA. Probably acts as an ATP-dependent pump that pulls DNA through the hexamer.",Probably involved in the cleavage of the histone H3 S1P to release the DNA from the nucleosomes.,No,No,No,No,No,not-Yes,GO:0005524; GO:0003677; GO:0009378; GO:0016787,,,,,,,,,,,0,,0.3643,no
PINA_SACI5,F0NID4,Protein2Text,Archaea,505,"Promotes Holliday junction (HJ) branch migration and unwinds Y-shaped DNA (but not replication forks or dsDNA) in an ATP hydrolysis- dependent manner. Stimulates cleavage by HJ resolvase Hjc. Unwinds Y-shaped and 3'-flap DNA substrates. In the absence of other proteins stabilizes replication forks (prevents spontaneous unwinding); Hjc, Hjm (Hel308) and PINA coordinate HJ migration and cleavage of replication forks in a coordinated way. Inhibits the 5'-3' (but not 3'-5') helicase activity of helicase Hjm (Hel308) on overhang DNA. Probably acts as an ATP-dependent pump that pulls DNA through the hexamer.","The molecular function of this protein is not specified in the provided information. However, it is identified as a component of the DNA replication machinery, which suggests that it may play a role in DNA synthesis, repair, or other DNA-related processes. To determine its specific molecular function, further research or information is required.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0005524; GO:0003677; GO:0009378; GO:0016787,,,,,,,,,,,0,,0.3643,no
PINA_SACI5,F0NID4,Reference,Archaea,505,"Promotes Holliday junction (HJ) branch migration and unwinds Y-shaped DNA (but not replication forks or dsDNA) in an ATP hydrolysis- dependent manner. Stimulates cleavage by HJ resolvase Hjc. Unwinds Y-shaped and 3'-flap DNA substrates. In the absence of other proteins stabilizes replication forks (prevents spontaneous unwinding); Hjc, Hjm (Hel308) and PINA coordinate HJ migration and cleavage of replication forks in a coordinated way. Inhibits the 5'-3' (but not 3'-5') helicase activity of helicase Hjm (Hel308) on overhang DNA. Probably acts as an ATP-dependent pump that pulls DNA through the hexamer.","Promotes Holliday junction (HJ) branch migration and unwinds Y-shaped DNA (but not replication forks or dsDNA) in an ATP hydrolysis- dependent manner. Stimulates cleavage by HJ resolvase Hjc. Unwinds Y-shaped and 3'-flap DNA substrates. In the absence of other proteins stabilizes replication forks (prevents spontaneous unwinding); Hjc, Hjm (Hel308) and PINA coordinate HJ migration and cleavage of replication forks in a coordinated way. Inhibits the 5'-3' (but not 3'-5') helicase activity of helicase Hjm (Hel308) on overhang DNA. Probably acts as an ATP-dependent pump that pulls DNA through the hexamer.",,,,,,,GO:0005524; GO:0003677; GO:0009378; GO:0016787,GO:0004003; GO:0009378; GO:0005524; GO:0003677,GO:0004386; GO:0005524,GO:0004386; GO:0005524,GO:0004386; GO:0016887; GO:0005524,GO:0004386; GO:0005524; GO:0003677,0.8982,0.6704,0.6704,0.6619,0.8367,5,0.7475,0.3643,no
DKC1_DANRE,F1Q749,ESM2Text,Eukaryota,506,"Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs. Required for ribosome biogenesis and telomere maintenance.","Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP), which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs. Required for ribosome biogenesis and telomere maintenance.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0009982; GO:0003723,GO:0009982,GO:0009982,GO:0009982,GO:0009982,GO:0009982,0.7153,0.7153,0.7153,0.7153,0.7153,5,0.7153,0.6108,yes
DKC1_DANRE,F1Q749,Prot2Text,Eukaryota,506,"Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs. Required for ribosome biogenesis and telomere maintenance.","Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs and play a central role in ribosomal RNA processing. The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs. Catalyzes pseudouridylation at position 93 in U2 snRNA. Also catalyzes pseudouridylation of mRNAs; H/ACA-type snoRNAs probably guide pseudouridylation of mRNAs.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0009982; GO:0003723,GO:0009982,GO:0009982,GO:0009982,GO:0009982,GO:0009982,0.7153,0.7153,0.7153,0.7153,0.7153,5,0.7153,0.6108,yes
DKC1_DANRE,F1Q749,ProtT3,Eukaryota,506,"Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs. Required for ribosome biogenesis and telomere maintenance.","Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs. The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs. Catalyzes pseudouridylation at position 93 in U2 snRNA (By similarity). Plays a role in",Yes,Yes,Yes,Yes,Yes,Yes,GO:0009982; GO:0003723,GO:0009982,GO:0009982,GO:0009982,GO:0009982,GO:0009982,0.7153,0.7153,0.7153,0.7153,0.7153,5,0.7153,0.6108,yes
DKC1_DANRE,F1Q749,ProtTale,Eukaryota,506,"Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs. Required for ribosome biogenesis and telomere maintenance.",Probable pseudouridine synthase that catalyzes formation of pseudouridine at position 38 (psi(38)) in 23S rRNA.,Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0009982; GO:0003723,GO:0009982,GO:0009982,GO:0009982,GO:0009982,GO:0009982,0.7153,0.7153,0.7153,0.7153,0.7153,5,0.7153,0.6108,yes
DKC1_DANRE,F1Q749,Protein2Text,Eukaryota,506,"Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs. Required for ribosome biogenesis and telomere maintenance.","The molecular function of this protein is RNA-binding and RNA-processing, specifically as a ribonuclease.",No,No,No,No,Maybe,not-Yes,GO:0009982; GO:0003723,GO:0004540,GO:0004540,GO:0004540,GO:0004540,GO:0004540,0.2065,0.2065,0.2065,0.2065,0.2065,5,0.2065,0.6108,yes
DKC1_DANRE,F1Q749,Reference,Eukaryota,506,"Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs. Required for ribosome biogenesis and telomere maintenance.","Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs. Required for ribosome biogenesis and telomere maintenance.",,,,,,,GO:0009982; GO:0003723,GO:0009982; GO:0003723,GO:0009982,GO:0009982; GO:0003723,GO:0009982,GO:0009982,1.0,0.7153,1.0,0.7153,0.7153,5,0.8292,0.6108,yes
AMFR_DANRE,F1QB30,ESM2Text,Eukaryota,620,E3 ubiquitin-protein ligase that mediates the polyubiquitination of lysine and cysteine residues on target proteins. May participate in the final step of endoplasmic reticulum-associated degradation (ERAD). Required for proper lipid homeostasis.,"E3 ubiquitin-protein ligase that mediates ubiquitination oXO proteins, such as CDC48, HSP70 and HSP90, and promotes their proteasome-mediated degradation, thereby playing a role in endosomal biogenesis. Acts also as a positive regulator of salt stress tolerance. Required for formation of endosomal vacuoles (VuPS). Involved in the maintenance of the post-translational regulation of vacuolar ATPase assembly. Involved in the maintenance of the post-translational regulation of HSP90.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0043130; GO:0061630; GO:0008270,GO:0004842,GO:0004842,GO:0004842,GO:0004842,GO:0061630,0.4573,0.4573,0.4573,0.4573,0.5338,5,0.4726,0.9112,yes
AMFR_DANRE,F1QB30,Prot2Text,Eukaryota,620,E3 ubiquitin-protein ligase that mediates the polyubiquitination of lysine and cysteine residues on target proteins. May participate in the final step of endoplasmic reticulum-associated degradation (ERAD). Required for proper lipid homeostasis.,E3 ubiquitin-protein ligase that acts as a negative regulator of type-I-interferon signaling by mediating 'Lys-48'-linked ubiquitination and degradation of IRF3. Probably acts by mediating ubiquitination and degradation of IFIH1.,Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0043130; GO:0061630; GO:0008270,GO:0004842,GO:0061630,GO:0061630,GO:0061630,GO:0004842,0.4573,0.5338,0.5338,0.5338,0.4573,5,0.5032,0.9112,yes
AMFR_DANRE,F1QB30,ProtT3,Eukaryota,620,E3 ubiquitin-protein ligase that mediates the polyubiquitination of lysine and cysteine residues on target proteins. May participate in the final step of endoplasmic reticulum-associated degradation (ERAD). Required for proper lipid homeostasis.,E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Endoplasmic reticulum membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein,Yes,Yes,Yes,Yes,Yes,Yes,GO:0043130; GO:0061630; GO:0008270,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.5338,0.5338,0.5338,0.5338,0.5338,5,0.5338,0.9112,yes
AMFR_DANRE,F1QB30,ProtTale,Eukaryota,620,E3 ubiquitin-protein ligase that mediates the polyubiquitination of lysine and cysteine residues on target proteins. May participate in the final step of endoplasmic reticulum-associated degradation (ERAD). Required for proper lipid homeostasis.,E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0043130; GO:0061630; GO:0008270,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.5338,0.5338,0.5338,0.5338,0.5338,5,0.5338,0.9112,yes
AMFR_DANRE,F1QB30,Protein2Text,Eukaryota,620,E3 ubiquitin-protein ligase that mediates the polyubiquitination of lysine and cysteine residues on target proteins. May participate in the final step of endoplasmic reticulum-associated degradation (ERAD). Required for proper lipid homeostasis.,The molecular function of this protein is related to its role in the degradation of proteins.,Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0043130; GO:0061630; GO:0008270,,,,,,,,,,,0,,0.9112,yes
AMFR_DANRE,F1QB30,Reference,Eukaryota,620,E3 ubiquitin-protein ligase that mediates the polyubiquitination of lysine and cysteine residues on target proteins. May participate in the final step of endoplasmic reticulum-associated degradation (ERAD). Required for proper lipid homeostasis.,E3 ubiquitin-protein ligase that mediates the polyubiquitination of lysine and cysteine residues on target proteins. May participate in the final step of endoplasmic reticulum-associated degradation (ERAD). Required for proper lipid homeostasis.,,,,,,,GO:0043130; GO:0061630; GO:0008270,GO:0061630,GO:0004842,GO:0004842,GO:0004842; GO:0061630,GO:0004842,0.5338,0.4573,0.4573,0.5996,0.4573,5,0.5011,0.9112,yes
LTK_DANRE,F1QVU0,ESM2Text,Eukaryota,1530,"Receptor tyrosine kinase required for the establishment and proliferation of iridophores and their progenitors from multipotent neural crest cells. Iridophores are the blue-tinted cells that reflect light to give fish their metallic shine and which, together with yellow xanthophore and black melanophores, generate the zebrafish's stripes. Following activation by alkal ligands (alkal1, alkal2a or alkal2b) at the cell surface, transduces an extracellular signal into an intracellular response. Ligand-binding to the extracellular domain induces tyrosine kinase activation, resulting in the activation of the mitogen- activated protein kinase (MAPK) pathway. Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif.",Lectin that functions as receptor for neurexin family ligands. Plays an important role in the development and maintenance of the nervous system.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004714,GO:0030246,,,,GO:0030246,0.1623,,,,0.1623,2,0.1623,0.5542,yes
LTK_DANRE,F1QVU0,Prot2Text,Eukaryota,1530,"Receptor tyrosine kinase required for the establishment and proliferation of iridophores and their progenitors from multipotent neural crest cells. Iridophores are the blue-tinted cells that reflect light to give fish their metallic shine and which, together with yellow xanthophore and black melanophores, generate the zebrafish's stripes. Following activation by alkal ligands (alkal1, alkal2a or alkal2b) at the cell surface, transduces an extracellular signal into an intracellular response. Ligand-binding to the extracellular domain induces tyrosine kinase activation, resulting in the activation of the mitogen- activated protein kinase (MAPK) pathway. Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif.","Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Generally has an overlapping and redundant function with EPHB2. Like EPHB2 it functions as the central regulator of heart development through regulation of angiogenesis and myogenesis through regulation of myoblast differentiation. Upon activation EPHB2 promotes myoblast differentiation into myotubes which ultimately lead to myotube formation. Upon ligand binding it dimerizes and promotes the dimerization of adjacent EPHB2-containing complexes resulting in the formation of an open complex which promotes the formation of an open myotube. This open complex promotes the formation of myotube through the activation of several signaling pathways including the ERK/MAPK and the phosphatidylinositol 3-kinase/PI3K pathways. In addition to its function in the regulation of heart development plays a central role in angiogenesis through regulation of angiogenesis. Involved",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0004714,GO:0004714,GO:0004714,GO:0004714,GO:0004714,GO:0004714,0.6808,0.6808,0.6808,0.6808,0.6808,5,0.6808,0.5542,yes
LTK_DANRE,F1QVU0,ProtT3,Eukaryota,1530,"Receptor tyrosine kinase required for the establishment and proliferation of iridophores and their progenitors from multipotent neural crest cells. Iridophores are the blue-tinted cells that reflect light to give fish their metallic shine and which, together with yellow xanthophore and black melanophores, generate the zebrafish's stripes. Following activation by alkal ligands (alkal1, alkal2a or alkal2b) at the cell surface, transduces an extracellular signal into an intracellular response. Ligand-binding to the extracellular domain induces tyrosine kinase activation, resulting in the activation of the mitogen- activated protein kinase (MAPK) pathway. Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif.","[Isoform 1]: Receptor tyrosine kinase which acts as a cell-surface receptor for TGFB1, TGFB2, TGFB3 and TGFB4",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0004714,GO:0004714; GO:0005524,GO:0004714,GO:0004714; GO:0005524,GO:0004714; GO:0005524,GO:0004714,1.0,0.6808,1.0,1.0,0.6808,5,0.8723,0.5542,yes
LTK_DANRE,F1QVU0,ProtTale,Eukaryota,1530,"Receptor tyrosine kinase required for the establishment and proliferation of iridophores and their progenitors from multipotent neural crest cells. Iridophores are the blue-tinted cells that reflect light to give fish their metallic shine and which, together with yellow xanthophore and black melanophores, generate the zebrafish's stripes. Following activation by alkal ligands (alkal1, alkal2a or alkal2b) at the cell surface, transduces an extracellular signal into an intracellular response. Ligand-binding to the extracellular domain induces tyrosine kinase activation, resulting in the activation of the mitogen- activated protein kinase (MAPK) pathway. Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif.","Receptor tyrosine-protein kinase that plays a critical role in the development and maintenance of the central nervous system (CNS), peripheral nervous system (PNS) and skeletal system. In the CNS, it is essential for the formation of the cerebral cortex, the corpus callosum, the hippocampus, the cerebellum and the brain stem, and for the normal development of the spinal cord. After binding to its ligand NTN1, transduces signals into the cell via the Ras/MAPK and PI3K/Akt pathways. In the PNS, it is required for the formation of the neuromuscular junction and for the maintenance of the",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0004714,GO:0004714; GO:0005524,GO:0004714; GO:0005524,GO:0004714; GO:0005524,GO:0004714,GO:0004714; GO:0005524,1.0,1.0,1.0,0.6808,1.0,5,0.9362,0.5542,yes
LTK_DANRE,F1QVU0,Protein2Text,Eukaryota,1530,"Receptor tyrosine kinase required for the establishment and proliferation of iridophores and their progenitors from multipotent neural crest cells. Iridophores are the blue-tinted cells that reflect light to give fish their metallic shine and which, together with yellow xanthophore and black melanophores, generate the zebrafish's stripes. Following activation by alkal ligands (alkal1, alkal2a or alkal2b) at the cell surface, transduces an extracellular signal into an intracellular response. Ligand-binding to the extracellular domain induces tyrosine kinase activation, resulting in the activation of the mitogen- activated protein kinase (MAPK) pathway. Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif.","The molecular function of this protein is not explicitly stated in the provided information. However, based on the name ""protein"", it is likely that this protein is a type of structural or regulatory protein, involved in various cellular processes such as cell signaling, cell adhesion, or protein transport.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0004714,,,,,,,,,,,0,,0.5542,yes
LTK_DANRE,F1QVU0,Reference,Eukaryota,1530,"Receptor tyrosine kinase required for the establishment and proliferation of iridophores and their progenitors from multipotent neural crest cells. Iridophores are the blue-tinted cells that reflect light to give fish their metallic shine and which, together with yellow xanthophore and black melanophores, generate the zebrafish's stripes. Following activation by alkal ligands (alkal1, alkal2a or alkal2b) at the cell surface, transduces an extracellular signal into an intracellular response. Ligand-binding to the extracellular domain induces tyrosine kinase activation, resulting in the activation of the mitogen- activated protein kinase (MAPK) pathway. Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif.","Receptor tyrosine kinase required for the establishment and proliferation of iridophores and their progenitors from multipotent neural crest cells. Iridophores are the blue-tinted cells that reflect light to give fish their metallic shine and which, together with yellow xanthophore and black melanophores, generate the zebrafish's stripes. Following activation by alkal ligands (alkal1, alkal2a or alkal2b) at the cell surface, transduces an extracellular signal into an intracellular response. Ligand-binding to the extracellular domain induces tyrosine kinase activation, resulting in the activation of the mitogen- activated protein kinase (MAPK) pathway. Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif.",,,,,,,GO:0005524; GO:0004714,GO:0004714; GO:0005524,GO:0004713; GO:0005524,GO:0004714; GO:0005524,GO:0004714; GO:0005524,GO:0004714; GO:0005524,1.0,0.8743,1.0,1.0,1.0,5,0.9749,0.5542,yes
ACE_PIG,F1RRW5,ESM2Text,Eukaryota,1309,"Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity. Composed of two similar catalytic domains, each possessing a functional active site, with different selectivity for substrates. Plays a major role in the angiotensin-renin system that regulates blood pressure and sodium retention by the kidney by converting angiotensin I to angiotensin II, resulting in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator, and therefore enhance the blood pressure response. Acts as a regulator of synaptic transmission by mediating cleavage of neuropeptide hormones, such as substance P, neurotensin or enkephalins. Catalyzes degradation of different enkephalin neuropeptides (Met- enkephalin, Leu-enkephalin, Met-enkephalin-Arg-Phe and possibly Met- enkephalin-Arg-Gly-Leu). Acts as a regulator of synaptic plasticity in the nucleus accumbens of the brain by mediating cleavage of Met-enkephalin-Arg-Phe, a strong ligand of Mu-type opioid receptor OPRM1, into Met-enkephalin. Met-enkephalin- Arg-Phe cleavage by ACE decreases activation of OPRM1, leading to long- term synaptic potentiation of glutamate release. Also acts as a regulator of hematopoietic stem cell differentiation by mediating degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP). Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1. Involved in amyloid-beta metabolism by catalyzing degradation of Amyloid-beta protein 40 and Amyloid-beta protein 42 peptides, thereby preventing plaque formation. Catalyzes cleavage of cholecystokinin (maturation of Cholecystokinin-8 and Cholecystokinin-5) and Gonadoliberin-1 (both maturation and degradation) hormones. Degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) and amyloid-beta proteins is mediated by the N-terminal catalytic domain, while angiotensin I and cholecystokinin cleavage is mediated by the C-terminal catalytic region.",Soluble form that is released in blood plasma and other body fluids following proteolytic cleavage in the juxtamembrane stalk region.,Vague,Vague,Vague,No,No,not-Yes,GO:0031711; GO:0005516; GO:0031404; GO:0004181; GO:0070573; GO:0004222; GO:0008237; GO:0051019; GO:0031434; GO:0008233; GO:0008241; GO:0008240; GO:0008270,,,,,,,,,,,0,,0.2495,no
ACE_PIG,F1RRW5,Prot2Text,Eukaryota,1309,"Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity. Composed of two similar catalytic domains, each possessing a functional active site, with different selectivity for substrates. Plays a major role in the angiotensin-renin system that regulates blood pressure and sodium retention by the kidney by converting angiotensin I to angiotensin II, resulting in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator, and therefore enhance the blood pressure response. Acts as a regulator of synaptic transmission by mediating cleavage of neuropeptide hormones, such as substance P, neurotensin or enkephalins. Catalyzes degradation of different enkephalin neuropeptides (Met- enkephalin, Leu-enkephalin, Met-enkephalin-Arg-Phe and possibly Met- enkephalin-Arg-Gly-Leu). Acts as a regulator of synaptic plasticity in the nucleus accumbens of the brain by mediating cleavage of Met-enkephalin-Arg-Phe, a strong ligand of Mu-type opioid receptor OPRM1, into Met-enkephalin. Met-enkephalin- Arg-Phe cleavage by ACE decreases activation of OPRM1, leading to long- term synaptic potentiation of glutamate release. Also acts as a regulator of hematopoietic stem cell differentiation by mediating degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP). Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1. Involved in amyloid-beta metabolism by catalyzing degradation of Amyloid-beta protein 40 and Amyloid-beta protein 42 peptides, thereby preventing plaque formation. Catalyzes cleavage of cholecystokinin (maturation of Cholecystokinin-8 and Cholecystokinin-5) and Gonadoliberin-1 (both maturation and degradation) hormones. Degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) and amyloid-beta proteins is mediated by the N-terminal catalytic domain, while angiotensin I and cholecystokinin cleavage is mediated by the C-terminal catalytic region.",Isoform M is regulated by arginine vasopressin in neuroendocrine cells. It may be involved in the intracellular reabsorption of arginine vasopressin.,No,Vague,Vague,No,No,not-Yes,GO:0031711; GO:0005516; GO:0031404; GO:0004181; GO:0070573; GO:0004222; GO:0008237; GO:0051019; GO:0031434; GO:0008233; GO:0008241; GO:0008240; GO:0008270,,,,,,,,,,,0,,0.2495,no
ACE_PIG,F1RRW5,ProtT3,Eukaryota,1309,"Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity. Composed of two similar catalytic domains, each possessing a functional active site, with different selectivity for substrates. Plays a major role in the angiotensin-renin system that regulates blood pressure and sodium retention by the kidney by converting angiotensin I to angiotensin II, resulting in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator, and therefore enhance the blood pressure response. Acts as a regulator of synaptic transmission by mediating cleavage of neuropeptide hormones, such as substance P, neurotensin or enkephalins. Catalyzes degradation of different enkephalin neuropeptides (Met- enkephalin, Leu-enkephalin, Met-enkephalin-Arg-Phe and possibly Met- enkephalin-Arg-Gly-Leu). Acts as a regulator of synaptic plasticity in the nucleus accumbens of the brain by mediating cleavage of Met-enkephalin-Arg-Phe, a strong ligand of Mu-type opioid receptor OPRM1, into Met-enkephalin. Met-enkephalin- Arg-Phe cleavage by ACE decreases activation of OPRM1, leading to long- term synaptic potentiation of glutamate release. Also acts as a regulator of hematopoietic stem cell differentiation by mediating degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP). Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1. Involved in amyloid-beta metabolism by catalyzing degradation of Amyloid-beta protein 40 and Amyloid-beta protein 42 peptides, thereby preventing plaque formation. Catalyzes cleavage of cholecystokinin (maturation of Cholecystokinin-8 and Cholecystokinin-5) and Gonadoliberin-1 (both maturation and degradation) hormones. Degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) and amyloid-beta proteins is mediated by the N-terminal catalytic domain, while angiotensin I and cholecystokinin cleavage is mediated by the C-terminal catalytic region.",Hydrolyzes neuropeptides such as neurotensin and neurotensin-like peptides. Secreted. Belongs to the peptidase M13 family,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0031711; GO:0005516; GO:0031404; GO:0004181; GO:0070573; GO:0004222; GO:0008237; GO:0051019; GO:0031434; GO:0008233; GO:0008241; GO:0008240; GO:0008270,GO:0004222; GO:0008270,GO:0004222,GO:0004222,GO:0004222,GO:0008237,0.5694,0.425,0.425,0.425,0.4825,5,0.4654,0.2495,no
ACE_PIG,F1RRW5,ProtTale,Eukaryota,1309,"Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity. Composed of two similar catalytic domains, each possessing a functional active site, with different selectivity for substrates. Plays a major role in the angiotensin-renin system that regulates blood pressure and sodium retention by the kidney by converting angiotensin I to angiotensin II, resulting in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator, and therefore enhance the blood pressure response. Acts as a regulator of synaptic transmission by mediating cleavage of neuropeptide hormones, such as substance P, neurotensin or enkephalins. Catalyzes degradation of different enkephalin neuropeptides (Met- enkephalin, Leu-enkephalin, Met-enkephalin-Arg-Phe and possibly Met- enkephalin-Arg-Gly-Leu). Acts as a regulator of synaptic plasticity in the nucleus accumbens of the brain by mediating cleavage of Met-enkephalin-Arg-Phe, a strong ligand of Mu-type opioid receptor OPRM1, into Met-enkephalin. Met-enkephalin- Arg-Phe cleavage by ACE decreases activation of OPRM1, leading to long- term synaptic potentiation of glutamate release. Also acts as a regulator of hematopoietic stem cell differentiation by mediating degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP). Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1. Involved in amyloid-beta metabolism by catalyzing degradation of Amyloid-beta protein 40 and Amyloid-beta protein 42 peptides, thereby preventing plaque formation. Catalyzes cleavage of cholecystokinin (maturation of Cholecystokinin-8 and Cholecystokinin-5) and Gonadoliberin-1 (both maturation and degradation) hormones. Degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) and amyloid-beta proteins is mediated by the N-terminal catalytic domain, while angiotensin I and cholecystokinin cleavage is mediated by the C-terminal catalytic region.",May play a role in the degradation of peptides that are products of protein turnover. Preferentially acts on peptides with an Arg at the N-terminus. Hydrolyzes the N-terminal amino acid of peptides with an Arg at the N-terminus in an ATP-dependent manner. Hydrolyzes the N-terminus of peptides with an Arg at the N-terminus in an ATP-dependent manner. Hydrolyzes the N-terminus of peptides with an Arg at the N-terminus in an ATP-dependent manner. Hydrolyzes the N-terminus of peptides with an Arg at the N-terminus in an ATP-dependent manner,Vague,Maybe,Maybe,Maybe,No,not-Yes,GO:0031711; GO:0005516; GO:0031404; GO:0004181; GO:0070573; GO:0004222; GO:0008237; GO:0051019; GO:0031434; GO:0008233; GO:0008241; GO:0008240; GO:0008270,GO:0004177; GO:0005524,GO:0004177; GO:0005524,GO:0004177; GO:0005524,GO:0004177,GO:0004177; GO:0005524,0.4515,0.4515,0.4515,0.4091,0.4515,5,0.443,0.2495,no
ACE_PIG,F1RRW5,Protein2Text,Eukaryota,1309,"Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity. Composed of two similar catalytic domains, each possessing a functional active site, with different selectivity for substrates. Plays a major role in the angiotensin-renin system that regulates blood pressure and sodium retention by the kidney by converting angiotensin I to angiotensin II, resulting in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator, and therefore enhance the blood pressure response. Acts as a regulator of synaptic transmission by mediating cleavage of neuropeptide hormones, such as substance P, neurotensin or enkephalins. Catalyzes degradation of different enkephalin neuropeptides (Met- enkephalin, Leu-enkephalin, Met-enkephalin-Arg-Phe and possibly Met- enkephalin-Arg-Gly-Leu). Acts as a regulator of synaptic plasticity in the nucleus accumbens of the brain by mediating cleavage of Met-enkephalin-Arg-Phe, a strong ligand of Mu-type opioid receptor OPRM1, into Met-enkephalin. Met-enkephalin- Arg-Phe cleavage by ACE decreases activation of OPRM1, leading to long- term synaptic potentiation of glutamate release. Also acts as a regulator of hematopoietic stem cell differentiation by mediating degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP). Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1. Involved in amyloid-beta metabolism by catalyzing degradation of Amyloid-beta protein 40 and Amyloid-beta protein 42 peptides, thereby preventing plaque formation. Catalyzes cleavage of cholecystokinin (maturation of Cholecystokinin-8 and Cholecystokinin-5) and Gonadoliberin-1 (both maturation and degradation) hormones. Degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) and amyloid-beta proteins is mediated by the N-terminal catalytic domain, while angiotensin I and cholecystokinin cleavage is mediated by the C-terminal catalytic region.",The molecular function of this protein is a serine protease.,No,Maybe,No,No,Maybe,not-Yes,GO:0031711; GO:0005516; GO:0031404; GO:0004181; GO:0070573; GO:0004222; GO:0008237; GO:0051019; GO:0031434; GO:0008233; GO:0008241; GO:0008240; GO:0008270,GO:0004252,GO:0004252,GO:0008236,GO:0004252,GO:0004252,0.3394,0.3394,0.4014,0.3394,0.3394,5,0.3518,0.2495,no
ACE_PIG,F1RRW5,Reference,Eukaryota,1309,"Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity. Composed of two similar catalytic domains, each possessing a functional active site, with different selectivity for substrates. Plays a major role in the angiotensin-renin system that regulates blood pressure and sodium retention by the kidney by converting angiotensin I to angiotensin II, resulting in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator, and therefore enhance the blood pressure response. Acts as a regulator of synaptic transmission by mediating cleavage of neuropeptide hormones, such as substance P, neurotensin or enkephalins. Catalyzes degradation of different enkephalin neuropeptides (Met- enkephalin, Leu-enkephalin, Met-enkephalin-Arg-Phe and possibly Met- enkephalin-Arg-Gly-Leu). Acts as a regulator of synaptic plasticity in the nucleus accumbens of the brain by mediating cleavage of Met-enkephalin-Arg-Phe, a strong ligand of Mu-type opioid receptor OPRM1, into Met-enkephalin. Met-enkephalin- Arg-Phe cleavage by ACE decreases activation of OPRM1, leading to long- term synaptic potentiation of glutamate release. Also acts as a regulator of hematopoietic stem cell differentiation by mediating degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP). Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1. Involved in amyloid-beta metabolism by catalyzing degradation of Amyloid-beta protein 40 and Amyloid-beta protein 42 peptides, thereby preventing plaque formation. Catalyzes cleavage of cholecystokinin (maturation of Cholecystokinin-8 and Cholecystokinin-5) and Gonadoliberin-1 (both maturation and degradation) hormones. Degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) and amyloid-beta proteins is mediated by the N-terminal catalytic domain, while angiotensin I and cholecystokinin cleavage is mediated by the C-terminal catalytic region.","Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity. Composed of two similar catalytic domains, each possessing a functional active site, with different selectivity for substrates. Plays a major role in the angiotensin-renin system that regulates blood pressure and sodium retention by the kidney by converting angiotensin I to angiotensin II, resulting in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator, and therefore enhance the blood pressure response. Acts as a regulator of synaptic transmission by mediating cleavage of neuropeptide hormones, such as substance P, neurotensin or enkephalins. Catalyzes degradation of different enkephalin neuropeptides (Met- enkephalin, Leu-enkephalin, Met-enkephalin-Arg-Phe and possibly Met- enkephalin-Arg-Gly-Leu). Acts as a regulator of synaptic plasticity in the nucleus accumbens of the brain by mediating cleavage of Met-enkephalin-Arg-Phe, a strong ligand of Mu-type opioid receptor OPRM1, into Met-enkephalin. Met-enkephalin- Arg-Phe cleavage by ACE decreases activation of OPRM1, leading to long- term synaptic potentiation of glutamate release. Also acts as a regulator of hematopoietic stem cell differentiation by mediating degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP). Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1. Involved in amyloid-beta metabolism by catalyzing degradation of Amyloid-beta protein 40 and Amyloid-beta protein 42 peptides, thereby preventing plaque formation. Catalyzes cleavage of cholecystokinin (maturation of Cholecystokinin-8 and Cholecystokinin-5) and Gonadoliberin-1 (both maturation and degradation) hormones. Degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) and amyloid-beta proteins is mediated by the N-terminal catalytic domain, while angiotensin I and cholecystokinin cleavage is mediated by the C-terminal catalytic region.",,,,,,,GO:0031711; GO:0005516; GO:0031404; GO:0004181; GO:0070573; GO:0004222; GO:0008237; GO:0051019; GO:0031434; GO:0008233; GO:0008241; GO:0008240; GO:0008270,GO:0008241; GO:0008270,GO:0004245; GO:0008270,GO:0008241,GO:0004180; GO:0004246; GO:0008241,GO:0004180; GO:0008241,0.5826,0.248,0.4423,0.4764,0.4764,5,0.4451,0.2495,no
RGYRB_METKA,F1SVH1,ESM2Text,Archaea,1221,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process; dATP also allows positive supercoiling. Increases the linking number in steps of +1. Only this subunit binds ATP, it does so in a DNA- and RgyA-independent manner. Hydrolyzes ATP only in the presence of DNA. The RgyA subunit transiently cleaves a single DNA strand and remains covalently bound to the 5' DNA end probably through a tyrosine residue. It changes linking number in steps of one, and nicks DNA preferentially at 5'-CNNN | 3'-sites with a strong preference for 4 pyrimidine residues. There are about 1000 heterodimers per cell. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.",Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. It cleaves transiently a single DNA strand and remains covalently bound to the 5' DNA end through a tyrosine residue. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0003677; GO:0160097; GO:0008270,GO:0003916; GO:0005524,GO:0003917; GO:0005524,GO:0003917,GO:0003916,GO:0003916,0.7009,0.669,0.3657,0.4085,0.4085,5,0.5105,0.6067,yes
RGYRB_METKA,F1SVH1,Prot2Text,Archaea,1221,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process; dATP also allows positive supercoiling. Increases the linking number in steps of +1. Only this subunit binds ATP, it does so in a DNA- and RgyA-independent manner. Hydrolyzes ATP only in the presence of DNA. The RgyA subunit transiently cleaves a single DNA strand and remains covalently bound to the 5' DNA end probably through a tyrosine residue. It changes linking number in steps of one, and nicks DNA preferentially at 5'-CNNN | 3'-sites with a strong preference for 4 pyrimidine residues. There are about 1000 heterodimers per cell. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.",Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. It cleaves transiently a single DNA strand and remains covalently bound to the 5' DNA end through a tyrosine residue. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0003677; GO:0160097; GO:0008270,GO:0003917,GO:0003916,GO:0003916,GO:0003916; GO:0005524,GO:0003916; GO:0005524,0.3657,0.4085,0.4085,0.7009,0.7009,5,0.5169,0.6067,yes
RGYRB_METKA,F1SVH1,ProtT3,Archaea,1221,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process; dATP also allows positive supercoiling. Increases the linking number in steps of +1. Only this subunit binds ATP, it does so in a DNA- and RgyA-independent manner. Hydrolyzes ATP only in the presence of DNA. The RgyA subunit transiently cleaves a single DNA strand and remains covalently bound to the 5' DNA end probably through a tyrosine residue. It changes linking number in steps of one, and nicks DNA preferentially at 5'-CNNN | 3'-sites with a strong preference for 4 pyrimidine residues. There are about 1000 heterodimers per cell. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.","Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0003677; GO:0160097; GO:0008270,GO:0003917,GO:0003917,GO:0003917,GO:0003917,GO:0003917,0.3657,0.3657,0.3657,0.3657,0.3657,5,0.3657,0.6067,yes
RGYRB_METKA,F1SVH1,ProtTale,Archaea,1221,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process; dATP also allows positive supercoiling. Increases the linking number in steps of +1. Only this subunit binds ATP, it does so in a DNA- and RgyA-independent manner. Hydrolyzes ATP only in the presence of DNA. The RgyA subunit transiently cleaves a single DNA strand and remains covalently bound to the 5' DNA end probably through a tyrosine residue. It changes linking number in steps of one, and nicks DNA preferentially at 5'-CNNN | 3'-sites with a strong preference for 4 pyrimidine residues. There are about 1000 heterodimers per cell. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.",DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit is not involved in transcription initiation.,No,No,No,No,No,not-Yes,GO:0005524; GO:0003677; GO:0160097; GO:0008270,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.1242,0.1242,0.1242,0.1242,0.1242,5,0.1242,0.6067,yes
RGYRB_METKA,F1SVH1,Protein2Text,Archaea,1221,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process; dATP also allows positive supercoiling. Increases the linking number in steps of +1. Only this subunit binds ATP, it does so in a DNA- and RgyA-independent manner. Hydrolyzes ATP only in the presence of DNA. The RgyA subunit transiently cleaves a single DNA strand and remains covalently bound to the 5' DNA end probably through a tyrosine residue. It changes linking number in steps of one, and nicks DNA preferentially at 5'-CNNN | 3'-sites with a strong preference for 4 pyrimidine residues. There are about 1000 heterodimers per cell. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.","The molecular function of the protein is an ATP-dependent DNA helicase, which means it is involved in the unwinding of double-stranded DNA into single-stranded DNA. This is a crucial step in DNA replication, repair, and transcription. The protein uses ATP hydrolysis to generate the energy required for DNA unwinding, allowing the enzyme to move along the DNA template and separate the two strands.",No,No,No,No,Maybe,not-Yes,GO:0005524; GO:0003677; GO:0160097; GO:0008270,GO:0003678; GO:0005524,GO:0004003; GO:0003677; GO:0005524,GO:0003678; GO:0005524,GO:0003678,GO:0003678; GO:0005524,0.5965,0.7734,0.5965,0.2811,0.5965,5,0.5688,0.6067,yes
RGYRB_METKA,F1SVH1,Reference,Archaea,1221,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process; dATP also allows positive supercoiling. Increases the linking number in steps of +1. Only this subunit binds ATP, it does so in a DNA- and RgyA-independent manner. Hydrolyzes ATP only in the presence of DNA. The RgyA subunit transiently cleaves a single DNA strand and remains covalently bound to the 5' DNA end probably through a tyrosine residue. It changes linking number in steps of one, and nicks DNA preferentially at 5'-CNNN | 3'-sites with a strong preference for 4 pyrimidine residues. There are about 1000 heterodimers per cell. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.","Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process; dATP also allows positive supercoiling. Increases the linking number in steps of +1. Only this subunit binds ATP, it does so in a DNA- and RgyA-independent manner. Hydrolyzes ATP only in the presence of DNA. The RgyA subunit transiently cleaves a single DNA strand and remains covalently bound to the 5' DNA end probably through a tyrosine residue. It changes linking number in steps of one, and nicks DNA preferentially at 5'-CNNN | 3'-sites with a strong preference for 4 pyrimidine residues. There are about 1000 heterodimers per cell. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.",,,,,,,GO:0005524; GO:0003677; GO:0160097; GO:0008270,GO:0003918; GO:0005524,GO:0003918; GO:0005524,GO:0003918; GO:0005524,GO:0003916; GO:0003917; GO:0005524,GO:0003916; GO:0005524,0.6379,0.6379,0.6379,0.7164,0.7009,5,0.6662,0.6067,yes
JMJ17_ARATH,F4I240,ESM2Text,Eukaryota,1208,"Functions as a histone H3 'Lys-4' (H3K4me) demethylase involved in the regulation of gene expression. Active on H3K4me1, H3K4me2 and H3K4me3. Repressor of the abscisic acid (ABA) signaling pathway, especially during stomatal closure regulation. Negative regulator of responses to dehydration stress by binding directly to the chromatin of SRK2E/OST1 and demethylating H3K4me3 to regulates its expression. Together with JMJ14 and JMJ16, required for plant growth and development.","Histone demethylase that demethylates 'Lys-4' (H3K4me) of histone H3 with a specific activity for H3K4me3 and H3K4me2. No activity on H3K9me3/2, H3K27me3/2 and H3K36me3/2.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0031490; GO:0003677; GO:0003700; GO:0032452; GO:0032453; GO:0034647; GO:0043565; GO:0008270,GO:0016706,GO:0032452,GO:0032452,GO:0032452,GO:0032452,0.2455,0.4385,0.4385,0.4385,0.4385,5,0.3999,0.3351,no
JMJ17_ARATH,F4I240,Prot2Text,Eukaryota,1208,"Functions as a histone H3 'Lys-4' (H3K4me) demethylase involved in the regulation of gene expression. Active on H3K4me1, H3K4me2 and H3K4me3. Repressor of the abscisic acid (ABA) signaling pathway, especially during stomatal closure regulation. Negative regulator of responses to dehydration stress by binding directly to the chromatin of SRK2E/OST1 and demethylating H3K4me3 to regulates its expression. Together with JMJ14 and JMJ16, required for plant growth and development.",Probable histone demethylase that may regulate the function and subcellular distribution of Cajal bodies.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0031490; GO:0003677; GO:0003700; GO:0032452; GO:0032453; GO:0034647; GO:0043565; GO:0008270,GO:0032454,GO:0032452,GO:0032452,GO:0032453,GO:0032452,0.3817,0.4385,0.4385,0.441,0.4385,5,0.4276,0.3351,no
JMJ17_ARATH,F4I240,ProtT3,Eukaryota,1208,"Functions as a histone H3 'Lys-4' (H3K4me) demethylase involved in the regulation of gene expression. Active on H3K4me1, H3K4me2 and H3K4me3. Repressor of the abscisic acid (ABA) signaling pathway, especially during stomatal closure regulation. Negative regulator of responses to dehydration stress by binding directly to the chromatin of SRK2E/OST1 and demethylating H3K4me3 to regulates its expression. Together with JMJ14 and JMJ16, required for plant growth and development.","Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Nucleus. Belongs to the JARID1 histone demethylase family",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0031490; GO:0003677; GO:0003700; GO:0032452; GO:0032453; GO:0034647; GO:0043565; GO:0008270,GO:0032452,GO:0032452,GO:0032452,GO:0032452,GO:0032452,0.4385,0.4385,0.4385,0.4385,0.4385,5,0.4385,0.3351,no
JMJ17_ARATH,F4I240,ProtTale,Eukaryota,1208,"Functions as a histone H3 'Lys-4' (H3K4me) demethylase involved in the regulation of gene expression. Active on H3K4me1, H3K4me2 and H3K4me3. Repressor of the abscisic acid (ABA) signaling pathway, especially during stomatal closure regulation. Negative regulator of responses to dehydration stress by binding directly to the chromatin of SRK2E/OST1 and demethylating H3K4me3 to regulates its expression. Together with JMJ14 and JMJ16, required for plant growth and development.","Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0031490; GO:0003677; GO:0003700; GO:0032452; GO:0032453; GO:0034647; GO:0043565; GO:0008270,GO:0032452,GO:0032452,GO:0032452,GO:0032452,GO:0032452,0.4385,0.4385,0.4385,0.4385,0.4385,5,0.4385,0.3351,no
JMJ17_ARATH,F4I240,Protein2Text,Eukaryota,1208,"Functions as a histone H3 'Lys-4' (H3K4me) demethylase involved in the regulation of gene expression. Active on H3K4me1, H3K4me2 and H3K4me3. Repressor of the abscisic acid (ABA) signaling pathway, especially during stomatal closure regulation. Negative regulator of responses to dehydration stress by binding directly to the chromatin of SRK2E/OST1 and demethylating H3K4me3 to regulates its expression. Together with JMJ14 and JMJ16, required for plant growth and development.",The molecular function of this protein is a lysine demethylase.,Yes,Maybe,Yes,Yes,Maybe,Yes,GO:0031490; GO:0003677; GO:0003700; GO:0032452; GO:0032453; GO:0034647; GO:0043565; GO:0008270,GO:0032452,GO:0032452,GO:0032452,GO:0032452,GO:0032453,0.4385,0.4385,0.4385,0.4385,0.441,5,0.439,0.3351,no
JMJ17_ARATH,F4I240,Reference,Eukaryota,1208,"Functions as a histone H3 'Lys-4' (H3K4me) demethylase involved in the regulation of gene expression. Active on H3K4me1, H3K4me2 and H3K4me3. Repressor of the abscisic acid (ABA) signaling pathway, especially during stomatal closure regulation. Negative regulator of responses to dehydration stress by binding directly to the chromatin of SRK2E/OST1 and demethylating H3K4me3 to regulates its expression. Together with JMJ14 and JMJ16, required for plant growth and development.","Functions as a histone H3 'Lys-4' (H3K4me) demethylase involved in the regulation of gene expression. Active on H3K4me1, H3K4me2 and H3K4me3. Repressor of the abscisic acid (ABA) signaling pathway, especially during stomatal closure regulation. Negative regulator of responses to dehydration stress by binding directly to the chromatin of SRK2E/OST1 and demethylating H3K4me3 to regulates its expression. Together with JMJ14 and JMJ16, required for plant growth and development.",,,,,,,GO:0031490; GO:0003677; GO:0003700; GO:0032452; GO:0032453; GO:0034647; GO:0043565; GO:0008270,GO:0051213; GO:0003682,GO:0032454,GO:0032452; GO:0003682,GO:0032452; GO:0016491; GO:0071949,GO:0016491; GO:0071949; GO:0003682,0.412,0.3817,0.6139,0.4727,0.3947,5,0.455,0.3351,no
AKB1D_ARATH,F4KAV2,ESM2Text,Eukaryota,442,Dioxygenase that catalyzes DNA N(6)-methyladenine (6 mA) demethylation to modulate gene expression and regulate seed germination.,"Transforms N(2)-acetyl-hydroxynucleotide (N(2)-acetyl-HNA) into acetoacetate and methionine. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-mercaptopyranoside (MMP), which plays a key role in methanogenesis and anaerobic methane oxidation.",No,No,No,No,No,not-Yes,GO:0035516; GO:0035514; GO:0141131; GO:0008198; GO:0035515,,,,,,,,,,,0,,0.3773,no
AKB1D_ARATH,F4KAV2,Prot2Text,Eukaryota,442,Dioxygenase that catalyzes DNA N(6)-methyladenine (6 mA) demethylation to modulate gene expression and regulate seed germination.,"Dioxygenase that repairs alkylated DNA containing 1-methyladenine and 1-ethenoadenine by oxidative demethylation. Accepts double-stranded and single-stranded substrates, with a preference for dsDNA over ssDNA. Has a strong preference for alkylated DNA containing gaps of up to 33 nucleotides in length. Requires molecular oxygen, alpha-ketoglutarate and iron.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0035516; GO:0035514; GO:0141131; GO:0008198; GO:0035515,GO:0035515; GO:0016706,GO:0035515,GO:0035515,GO:0016798; GO:0003906,GO:0035515,0.6616,0.6523,0.6523,0.2986,0.6523,5,0.5834,0.3773,no
AKB1D_ARATH,F4KAV2,ProtT3,Eukaryota,442,Dioxygenase that catalyzes DNA N(6)-methyladenine (6 mA) demethylation to modulate gene expression and regulate seed germination.,2-oxoglutarate (OG)- and iron (Fe(2+))-dependent dioxygenase that plays a key role in mitochondrial DNA (mtDNA) repair by base excision repair (BER) . Catalyzes the oxidative removal of the 3'-hydroxyl group of 3'-deoxyadenosine (dAd) and 3'- deoxyguanosine (dGuo) residues in mtDNA . Acts as a 3,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0035516; GO:0035514; GO:0141131; GO:0008198; GO:0035515,GO:0016706,GO:0016706; GO:0005506,GO:0016706; GO:0005506,GO:0016706; GO:0005506,GO:0016706,0.5152,0.684,0.684,0.684,0.5152,5,0.6165,0.3773,no
AKB1D_ARATH,F4KAV2,ProtTale,Eukaryota,442,Dioxygenase that catalyzes DNA N(6)-methyladenine (6 mA) demethylation to modulate gene expression and regulate seed germination.,"RNA demethylase that specifically demethylates N(6)-methyladenosine (m6A) RNA, the most abundant internal modification of messenger RNAs (mRNAs) in plants. N(6)-methyladenosine (m6A) is a prevalent post-transcriptional modification of mRNAs and plays a key role in mRNA processing, stability and translation (Probable). Demethylates m6A if N(6)- methyladenosine (m6A) RNA is present at all four positions (m6A4C2, m6A1M2, m6A3M1",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0035516; GO:0035514; GO:0141131; GO:0008198; GO:0035515,GO:0016706,GO:0016491,GO:0016706,GO:0016895,GO:0016491,0.5152,0.3635,0.5152,0.265,0.3635,5,0.4045,0.3773,no
AKB1D_ARATH,F4KAV2,Protein2Text,Eukaryota,442,Dioxygenase that catalyzes DNA N(6)-methyladenine (6 mA) demethylation to modulate gene expression and regulate seed germination.,"This protein is involved in the molecular function of being a component of a ubiquitin ligase complex, specifically the SCF (Skp1-Cullin-F-box) complex.",No,No,No,No,No,not-Yes,GO:0035516; GO:0035514; GO:0141131; GO:0008198; GO:0035515,GO:0004842,GO:0061631,GO:0061630,GO:0061630,GO:0061630,0.1647,0.1382,0.1382,0.1382,0.1382,5,0.1435,0.3773,no
AKB1D_ARATH,F4KAV2,Reference,Eukaryota,442,Dioxygenase that catalyzes DNA N(6)-methyladenine (6 mA) demethylation to modulate gene expression and regulate seed germination.,Dioxygenase that catalyzes DNA N(6)-methyladenine (6 mA) demethylation to modulate gene expression and regulate seed germination.,,,,,,,GO:0035516; GO:0035514; GO:0141131; GO:0008198; GO:0035515,GO:0016706; GO:0035515,GO:0016706,GO:0051213; GO:0003677,GO:0051213,GO:0051213; GO:0003677,0.6616,0.5152,0.3987,0.4107,0.3987,5,0.477,0.3773,no
NHAA_CALTT,F5L3T2,ESM2Text,Bacteria,210,"NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. The alpha subunit functions as the catalytic subunit of the NHase complex, while the beta subunit plays a structural/accessory role.",NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. Industrial production of acrylamide is now being developed using some of the enzymes of this class.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0018822; GO:0046914,,GO:0018793,GO:0018747,GO:0018738,GO:0018738,,0.0,0.0,0.159,0.159,4,0.0795,0.1923,no
NHAA_CALTT,F5L3T2,Prot2Text,Bacteria,210,"NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. The alpha subunit functions as the catalytic subunit of the NHase complex, while the beta subunit plays a structural/accessory role.",NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. Industrial production of acrylamide is now being developed using some of the enzymes of this class.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0018822; GO:0046914,GO:0018738,GO:0018738,GO:0018738,GO:0018743,GO:0018738,0.159,0.159,0.159,0.0,0.159,5,0.1272,0.1923,no
NHAA_CALTT,F5L3T2,ProtT3,Bacteria,210,"NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. The alpha subunit functions as the catalytic subunit of the NHase complex, while the beta subunit plays a structural/accessory role.",NHase catalyzes the hydration of various nitriles to the corresponding amides. Belongs to the nitrile hydratase subunit alpha family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0018822; GO:0046914,GO:0016810,GO:0018738,GO:0016811,GO:0018738,GO:0018677,0.227,0.159,0.1875,0.159,0.1463,5,0.1758,0.1923,no
NHAA_CALTT,F5L3T2,ProtTale,Bacteria,210,"NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. The alpha subunit functions as the catalytic subunit of the NHase complex, while the beta subunit plays a structural/accessory role.",NHase catalyzes the hydration of various nitrile compounds to the corresponding amides.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0018822; GO:0046914,GO:0018738,GO:0016829,GO:0018793,GO:0018070,GO:0018738,0.159,0.4483,0.0,0.0,0.159,5,0.1533,0.1923,no
NHAA_CALTT,F5L3T2,Protein2Text,Bacteria,210,"NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. The alpha subunit functions as the catalytic subunit of the NHase complex, while the beta subunit plays a structural/accessory role.","The molecular function of this protein is as a methyltransferase. It catalyzes the transfer of a methyl group from one compound to another. In the case of this protein, it is involved in the biosynthesis of cobalamin (vitamin B12), specifically in the conversion of 5,6-dimethylbenzimidazole (DMB) to 5,6-dimethylbenzimidazole methylcobamide (DMB-MC).",No,No,No,No,No,not-Yes,GO:0018822; GO:0046914,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.1875,0.1875,0.1875,0.1875,0.1875,5,0.1875,0.1923,no
NHAA_CALTT,F5L3T2,Reference,Bacteria,210,"NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. The alpha subunit functions as the catalytic subunit of the NHase complex, while the beta subunit plays a structural/accessory role.","NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. The alpha subunit functions as the catalytic subunit of the NHase complex, while the beta subunit plays a structural/accessory role.",,,,,,,GO:0018822; GO:0046914,GO:0018793,GO:0016836,GO:0018738,GO:0016810,GO:0016810,0.0,0.6027,0.159,0.227,0.227,5,0.2431,0.1923,no
PNAO_PSEP6,F8G0P1,ESM2Text,Bacteria,496,Involved in nicotine degradation. Catalyzes the deamination of pseudooxynicotine to 3- succinoylsemialdehyde-pyridine. Functions as a dehydrogenase that uses the c-type cytochrome protein CycN as the physiological electron acceptor. O(2) is a poor electron acceptor. Pnao is oxidized by CycN 230 times faster than O(2) at equivalent oxidant concentrations.,"Catalyzes the hydrolysis of the antibiotic bacilysin, yielding sialic acid and sulfite.",No,No,No,No,No,not-Yes,GO:0016491,GO:0016787,GO:0016787,GO:0016787,,GO:0016787,0.5902,0.5902,0.5902,,0.5902,4,0.5902,0.2542,no
PNAO_PSEP6,F8G0P1,Prot2Text,Bacteria,496,Involved in nicotine degradation. Catalyzes the deamination of pseudooxynicotine to 3- succinoylsemialdehyde-pyridine. Functions as a dehydrogenase that uses the c-type cytochrome protein CycN as the physiological electron acceptor. O(2) is a poor electron acceptor. Pnao is oxidized by CycN 230 times faster than O(2) at equivalent oxidant concentrations.,Catalyzes the deamination of pseudooxynicotine to 3-succinoylsemialdehyde-pyridine in the nicotine degradation pathway.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0016491,GO:0016491,,GO:0016491,GO:0016491,GO:0008131,1.0,,1.0,1.0,0.6019,4,0.9005,0.2542,no
PNAO_PSEP6,F8G0P1,ProtT3,Bacteria,496,Involved in nicotine degradation. Catalyzes the deamination of pseudooxynicotine to 3- succinoylsemialdehyde-pyridine. Functions as a dehydrogenase that uses the c-type cytochrome protein CycN as the physiological electron acceptor. O(2) is a poor electron acceptor. Pnao is oxidized by CycN 230 times faster than O(2) at equivalent oxidant concentrations.,Cytoplasm. Belongs to the flavin monoamine oxidase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016491,GO:0016491,GO:0016638,GO:0016491,GO:0016641,GO:0016641,1.0,0.8145,1.0,0.6897,0.6897,5,0.8388,0.2542,no
PNAO_PSEP6,F8G0P1,ProtTale,Bacteria,496,Involved in nicotine degradation. Catalyzes the deamination of pseudooxynicotine to 3- succinoylsemialdehyde-pyridine. Functions as a dehydrogenase that uses the c-type cytochrome protein CycN as the physiological electron acceptor. O(2) is a poor electron acceptor. Pnao is oxidized by CycN 230 times faster than O(2) at equivalent oxidant concentrations.,Catalyzes the oxidative deamination of L-arginine to agmatine. Is involved in the utilization of L-arginine as an nitrogen source.,No,No,No,No,No,not-Yes,GO:0016491,GO:0008792,GO:0016491,GO:0008792,GO:0003863,GO:0008792,0.3552,1.0,0.3552,0.6019,0.3552,5,0.5335,0.2542,no
PNAO_PSEP6,F8G0P1,Protein2Text,Bacteria,496,Involved in nicotine degradation. Catalyzes the deamination of pseudooxynicotine to 3- succinoylsemialdehyde-pyridine. Functions as a dehydrogenase that uses the c-type cytochrome protein CycN as the physiological electron acceptor. O(2) is a poor electron acceptor. Pnao is oxidized by CycN 230 times faster than O(2) at equivalent oxidant concentrations.,The molecular function of this protein is a decarboxylase. It catalyzes the decarboxylation of L-lysine to form cadaverine.,No,No,No,No,No,not-Yes,GO:0016491,GO:0016831,GO:0004586,GO:0008923,GO:0008923,GO:0016831,0.4071,0.3552,0.3552,0.3552,0.4071,5,0.376,0.2542,no
PNAO_PSEP6,F8G0P1,Reference,Bacteria,496,Involved in nicotine degradation. Catalyzes the deamination of pseudooxynicotine to 3- succinoylsemialdehyde-pyridine. Functions as a dehydrogenase that uses the c-type cytochrome protein CycN as the physiological electron acceptor. O(2) is a poor electron acceptor. Pnao is oxidized by CycN 230 times faster than O(2) at equivalent oxidant concentrations.,Involved in nicotine degradation. Catalyzes the deamination of pseudooxynicotine to 3- succinoylsemialdehyde-pyridine. Functions as a dehydrogenase that uses the c-type cytochrome protein CycN as the physiological electron acceptor. O(2) is a poor electron acceptor. Pnao is oxidized by CycN 230 times faster than O(2) at equivalent oxidant concentrations.,,,,,,,GO:0016491,GO:0016491; GO:0016641,GO:0016491,GO:0016638,GO:0016491; GO:0016638,GO:0016491; GO:0050660,0.8966,1.0,0.8145,0.9382,0.7083,5,0.8715,0.2542,no
CYS_STREN,F8JK18,ESM2Text,Bacteria,367,"Diterpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) to cattleyene. Cannot use geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylfarnesyl diphosphate (GFPP).","Involved in the biosynthesis of the hopanoid precursor squalene (SQ) from farnesyl diphosphate (FPP), a precursor of SQ. Catalyzes the formation of a 1,3,5-cis-epoxyspacytosine intermediate by abstraction of pyrophosphate from FPP leading to a (SQS-SQH) linear hydroxymycins intermediate that is immediately hydrolyzed to water and alcohols-phosphate by FPP.",No,No,No,No,No,not-Yes,GO:0046872; GO:0010333,,GO:0051996,GO:0004310,GO:0004310,GO:0051996,,0.1628,0.0,0.0,0.1628,4,0.0814,0.1951,no
CYS_STREN,F8JK18,Prot2Text,Bacteria,367,"Diterpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) to cattleyene. Cannot use geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylfarnesyl diphosphate (GFPP).","Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to yield the bicyclic sesquiterpene (2S,10R)-(-)-(E)-beta-caryophyllene via a 1,10-cyclization, which requires the abstraction of the pyrophosphate from FPP to yield the (E,E)-germacradienyl cation. The only accepted substrate is farnesyl diphosphate (FPP).",Maybe,Maybe,No,No,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0010334,,GO:0010334,GO:0010334,GO:0010334,0.6051,,0.6051,0.6051,0.6051,4,0.6051,0.1951,no
CYS_STREN,F8JK18,ProtT3,Bacteria,367,"Diterpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) to cattleyene. Cannot use geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylfarnesyl diphosphate (GFPP).","Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (2E,6E,10E,14E,18E,22E,26E,30E,34E,38E,42E,46E,50E,54E,58E,62E,66E,70E,74E,78E,82E,86E,90E,94E,98E",No,No,No,No,No,not-Yes,GO:0046872; GO:0010333,GO:0016765,GO:0016765,GO:0016765,GO:0016765,GO:0016765,0.2318,0.2318,0.2318,0.2318,0.2318,5,0.2318,0.1951,no
CYS_STREN,F8JK18,ProtTale,Bacteria,367,"Diterpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) to cattleyene. Cannot use geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylfarnesyl diphosphate (GFPP).","Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (+)-delta-cadinene via a 1,10-cyclization.",Maybe,Maybe,No,No,No,not-Yes,GO:0046872; GO:0010333,GO:0010333,GO:0016829,GO:0010333,GO:0010334,GO:0010334; GO:0016829,0.6963,0.4539,0.6963,0.6051,0.6245,5,0.6152,0.1951,no
CYS_STREN,F8JK18,Protein2Text,Bacteria,367,"Diterpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) to cattleyene. Cannot use geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylfarnesyl diphosphate (GFPP).","This protein is involved in the biosynthesis of a compound. Specifically, it is a component of the pathway responsible for the production of a certain molecule. The exact molecular function of this protein is not specified, but it is likely involved in the conversion of a precursor molecule into the final product.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0046872; GO:0010333,,,,,,,,,,,0,,0.1951,no
CYS_STREN,F8JK18,Reference,Bacteria,367,"Diterpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) to cattleyene. Cannot use geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylfarnesyl diphosphate (GFPP).","Diterpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) to cattleyene. Cannot use geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylfarnesyl diphosphate (GFPP).",,,,,,,GO:0046872; GO:0010333,GO:0010333,GO:0010333,GO:0010333,GO:0010333; GO:0016829,GO:0016829,0.6963,0.6963,0.6963,0.6899,0.4539,5,0.6465,0.1951,no
R1AB_AMV79,F8RL29,ESM2Text,Viruses,5088,[3C-like proteinase]: Cysteine protease responsible for the majority of cleavages of the polyprotein. Recognizes substrates containing the core sequence [NT]-[EHKQSY]-|-[AGNST].,"During fertilization, required on male gametes for their fusion with female gametes. This occurs during the mid- to late-pachytene stage of gametogenesis.",No,No,No,No,No,not-Yes,GO:0000175; GO:0005524; GO:0004197; GO:0003678; GO:0004483; GO:0004482; GO:0003724; GO:0003968; GO:0001147,,,,,,,,,,,0,,0.497,no
R1AB_AMV79,F8RL29,Prot2Text,Viruses,5088,[3C-like proteinase]: Cysteine protease responsible for the majority of cleavages of the polyprotein. Recognizes substrates containing the core sequence [NT]-[EHKQSY]-|-[AGNST].,"During fertilization, required on male gametes for their fusion with female gametes. This occurs during the mid- to late-pachytene stage of gametogenesis.",No,No,No,No,No,not-Yes,GO:0000175; GO:0005524; GO:0004197; GO:0003678; GO:0004483; GO:0004482; GO:0003724; GO:0003968; GO:0001147,,,,,,,,,,,0,,0.497,no
R1AB_AMV79,F8RL29,ProtT3,Viruses,5088,[3C-like proteinase]: Cysteine protease responsible for the majority of cleavages of the polyprotein. Recognizes substrates containing the core sequence [NT]-[EHKQSY]-|-[AGNST].,Host membrane; Single-pass membrane protein. Belongs to the poxviridae A45 protein family,Vague,Vague,Vague,No,Vague,not-Yes,GO:0000175; GO:0005524; GO:0004197; GO:0003678; GO:0004483; GO:0004482; GO:0003724; GO:0003968; GO:0001147,,,,,,,,,,,0,,0.497,no
R1AB_AMV79,F8RL29,ProtTale,Viruses,5088,[3C-like proteinase]: Cysteine protease responsible for the majority of cleavages of the polyprotein. Recognizes substrates containing the core sequence [NT]-[EHKQSY]-|-[AGNST].,"[Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0000175; GO:0005524; GO:0004197; GO:0003678; GO:0004483; GO:0004482; GO:0003724; GO:0003968; GO:0001147,GO:0004197,GO:0008233,GO:0008233,GO:0008233,GO:0008233,0.2959,0.278,0.278,0.278,0.278,5,0.2816,0.497,no
R1AB_AMV79,F8RL29,Protein2Text,Viruses,5088,[3C-like proteinase]: Cysteine protease responsible for the majority of cleavages of the polyprotein. Recognizes substrates containing the core sequence [NT]-[EHKQSY]-|-[AGNST].,"The molecular function of this protein is not specified in the provided text. However, based on the name ""protein"" and the context in which it is mentioned, it is likely that this protein is involved in a molecular process, such as binding or catalysis. Without more information, it is difficult to determine the specific molecular function of this protein.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0000175; GO:0005524; GO:0004197; GO:0003678; GO:0004483; GO:0004482; GO:0003724; GO:0003968; GO:0001147,,,,,,,,,,,0,,0.497,no
R1AB_AMV79,F8RL29,Reference,Viruses,5088,[3C-like proteinase]: Cysteine protease responsible for the majority of cleavages of the polyprotein. Recognizes substrates containing the core sequence [NT]-[EHKQSY]-|-[AGNST].,[3C-like proteinase]: Cysteine protease responsible for the majority of cleavages of the polyprotein. Recognizes substrates containing the core sequence [NT]-[EHKQSY]-|-[AGNST].,,,,,,,GO:0000175; GO:0005524; GO:0004197; GO:0003678; GO:0004483; GO:0004482; GO:0003724; GO:0003968; GO:0001147,GO:0004197,GO:0004197,GO:0004197,GO:0008234,GO:0004197,0.2959,0.2959,0.2959,0.2779,0.2959,5,0.2923,0.497,no
UBP32_MOUSE,F8VPZ3,ESM2Text,Eukaryota,1604,"Deubiquitinase that can remove conjugated ubiquitin from target proteins, such as RAB7A and LAMTOR1. Acts as a positive regulator of the mTORC1 signaling by mediating deubiquitination of LAMTOR1, thereby promoting the association between LAMTOR1 and the lysosomal V-ATPase complex and subsequent activation of the mTORC1 complex.","Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Deubiquitinates PDPK1. Has a preference for 'Lys-63'-linked ubiquitin chains. Cleaves SYK, RAC1, and CDC42 at 'Lys-63', 'Lys-48'-linked ubiquitin chains, and 'Lys-63'-linked ubiquitination of target proteins.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005509; GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,0.6872,0.6872,0.6872,0.6872,0.6872,5,0.6872,0.8768,yes
UBP32_MOUSE,F8VPZ3,Prot2Text,Eukaryota,1604,"Deubiquitinase that can remove conjugated ubiquitin from target proteins, such as RAB7A and LAMTOR1. Acts as a positive regulator of the mTORC1 signaling by mediating deubiquitination of LAMTOR1, thereby promoting the association between LAMTOR1 and the lysosomal V-ATPase complex and subsequent activation of the mTORC1 complex.","Hydrolase that can remove conjugated ubiquitin from proteins and regulates different cellular processes such as cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection. Acts as an inhibitor of the Wnt signaling pathway by mediating ubiquitination and subsequent degradation of beta-catenin (CTNNB1). Deubiquitinates CTNNB1 at 'Lys-48' leading to its degradation by the proteasome, thereby promoting cell survival and preventing apoptosis. Deubiquitinates and thereby regulates protein phosphatase 2A (PP2A), thereby regulating cell migration. Plays a role in the regulation of the circadian clock by mediating ubiquitination and subsequent degradation of CLOCK-ARNTL/BMAL1 heterodimer. Mediates also proteasomal degradation of NEFL, leading to its degradation by the proteasome. Plays a role in the regulation of the circadian pacemaker synchronization by mediating ubiquitination and subsequent degradation of ARNTL/BMAL1. Mediates proteasomal degradation of ABC transporters such as TOLLIP, FLT3, PDGF and ZFP36, promoting their ubiquitination and degradation. Controls",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005509; GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,0.6872,0.6872,0.6872,0.6872,0.6872,5,0.6872,0.8768,yes
UBP32_MOUSE,F8VPZ3,ProtT3,Eukaryota,1604,"Deubiquitinase that can remove conjugated ubiquitin from target proteins, such as RAB7A and LAMTOR1. Acts as a positive regulator of the mTORC1 signaling by mediating deubiquitination of LAMTOR1, thereby promoting the association between LAMTOR1 and the lysosomal V-ATPase complex and subsequent activation of the mTORC1 complex.",Deubiquitinating enzyme that cleaves 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). Deubiquitinates 'Lys-11'- and 'Lys-27'-linked polyubiquitin chains (By similarity). Deubiquitinates 'Lys-11'- and 'Lys-27'-linked polyubiquitin chains on 14-3-3 proteins (By similarity). Deubiquitinates 'Lys-11'- and 'Lys-27'-linked poly,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005509; GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,0.6872,0.6872,0.6872,0.6872,0.6872,5,0.6872,0.8768,yes
UBP32_MOUSE,F8VPZ3,ProtTale,Eukaryota,1604,"Deubiquitinase that can remove conjugated ubiquitin from target proteins, such as RAB7A and LAMTOR1. Acts as a positive regulator of the mTORC1 signaling by mediating deubiquitination of LAMTOR1, thereby promoting the association between LAMTOR1 and the lysosomal V-ATPase complex and subsequent activation of the mTORC1 complex.","Deubiquitinating enzyme involved in the regulation of different processes such as DNA damage response, cell cycle progression, autophagy, ER stress-induced autophagy, innate immune response, and proteasomal degradation. Regulates the proteasomal degradation of p53/TP53, probably by regulating the stability of p53/TP53 protein. Regulates the proteasomal degradation of RNF125, an E3 ubiquitin ligase that mediates K63-linked polyubiquitination of target proteins. Plays a role in ER stress-induced autophagy by regulating the stability of ATG16L1. Acts as a negative regulator of the innate immune response by",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005509; GO:0004843,GO:0004843,GO:0004843,GO:0101005,GO:0036459,GO:0004843,0.6872,0.6872,0.5689,0.6872,0.6872,5,0.6635,0.8768,yes
UBP32_MOUSE,F8VPZ3,Protein2Text,Eukaryota,1604,"Deubiquitinase that can remove conjugated ubiquitin from target proteins, such as RAB7A and LAMTOR1. Acts as a positive regulator of the mTORC1 signaling by mediating deubiquitination of LAMTOR1, thereby promoting the association between LAMTOR1 and the lysosomal V-ATPase complex and subsequent activation of the mTORC1 complex.","The molecular function of this protein is not explicitly stated in the provided information. However, based on the context, it is likely that the protein is involved in signal transduction, specifically in the phosphoinositide 3-kinase (PI3K) pathway. The protein is described as being involved in the activation of a downstream target, suggesting that it may be a regulatory subunit of PI3K or a downstream effector of the PI3K pathway.",No,No,Vague,Vague,No,not-Yes,GO:0005509; GO:0004843,,,,,,,,,,,0,,0.8768,yes
UBP32_MOUSE,F8VPZ3,Reference,Eukaryota,1604,"Deubiquitinase that can remove conjugated ubiquitin from target proteins, such as RAB7A and LAMTOR1. Acts as a positive regulator of the mTORC1 signaling by mediating deubiquitination of LAMTOR1, thereby promoting the association between LAMTOR1 and the lysosomal V-ATPase complex and subsequent activation of the mTORC1 complex.","Deubiquitinase that can remove conjugated ubiquitin from target proteins, such as RAB7A and LAMTOR1. Acts as a positive regulator of the mTORC1 signaling by mediating deubiquitination of LAMTOR1, thereby promoting the association between LAMTOR1 and the lysosomal V-ATPase complex and subsequent activation of the mTORC1 complex.",,,,,,,GO:0005509; GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843; GO:0016579,GO:0004843; GO:0036459,0.6872,0.6872,0.6872,0.5154,0.7654,5,0.6685,0.8768,yes
DHOM_SULTO,F9VNG5,ESM2Text,Archaea,304,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate.",Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.,No,No,No,No,No,not-Yes,GO:0004412; GO:0046872; GO:0050661,GO:0016491; GO:0051287,GO:0008734,GO:0008734,GO:0008734,GO:0008734,0.6072,0.1609,0.1609,0.1609,0.1609,5,0.2502,0.2446,no
DHOM_SULTO,F9VNG5,Prot2Text,Archaea,304,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate.",Catalyzes the NADPH-dependent reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).,No,No,No,No,No,not-Yes,GO:0004412; GO:0046872; GO:0050661,GO:0030604,GO:0030604,GO:0030604,GO:0030604,GO:0030604,0.4043,0.4043,0.4043,0.4043,0.4043,5,0.4043,0.2446,no
DHOM_SULTO,F9VNG5,ProtT3,Archaea,304,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate.",Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004412; GO:0046872; GO:0050661,GO:0016616,GO:0016616,GO:0016616,GO:0016616,GO:0016616,0.4761,0.4761,0.4761,0.4761,0.4761,5,0.4761,0.2446,no
DHOM_SULTO,F9VNG5,ProtTale,Archaea,304,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate.","Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004412; GO:0046872; GO:0050661,GO:0004412,GO:0004412,GO:0004412,GO:0004412,GO:0004412,0.5398,0.5398,0.5398,0.5398,0.5398,5,0.5398,0.2446,no
DHOM_SULTO,F9VNG5,Protein2Text,Archaea,304,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate.","The molecular function of this protein is that of an isomerase, specifically a cis-trans isomerase. It catalyzes the conversion of a molecule from a cis to a trans configuration.",No,No,No,No,No,not-Yes,GO:0004412; GO:0046872; GO:0050661,GO:0016859,GO:0016859,GO:0016859,GO:0016859,GO:0016859,0.1992,0.1992,0.1992,0.1992,0.1992,5,0.1992,0.2446,no
DHOM_SULTO,F9VNG5,Reference,Archaea,304,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate.","Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate.",,,,,,,GO:0004412; GO:0046872; GO:0050661,GO:0004412,GO:0004412,GO:0004412,GO:0004412,GO:0004412,0.5398,0.5398,0.5398,0.5398,0.5398,5,0.5398,0.2446,no
IRE1_HYPJQ,G0RBE3,ESM2Text,Eukaryota,1243,Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain splices precursor mRNAs to produce their mature form which then induces transcription of UPR target genes.,Can act as a sink to ensure that adequate levels of nutrients are supplied to cells.,Vague,Vague,Vague,No,No,not-Yes,GO:0005524; GO:0016787; GO:0046872; GO:0004674; GO:0004521; GO:0051082,,,,,,,,,,,0,,0.4638,no
IRE1_HYPJQ,G0RBE3,Prot2Text,Eukaryota,1243,Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain splices precursor mRNAs to produce their mature form which then induces transcription of UPR target genes.,Serine/threonine-protein kinase involved in the control of cell wall synthesis and septum formation.,No,No,No,No,No,not-Yes,GO:0005524; GO:0016787; GO:0046872; GO:0004674; GO:0004521; GO:0051082,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.3846,0.3846,0.3846,0.3846,0.3846,5,0.3846,0.4638,no
IRE1_HYPJQ,G0RBE3,ProtT3,Eukaryota,1243,Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain splices precursor mRNAs to produce their mature form which then induces transcription of UPR target genes.,Serine/threonine-protein kinase involved in the regulation of the unfolded protein response (UPR). Acts downstream of the endoplasmic reticulum (ER) stress sensor protein kinase IRE1 and upstream of the transcription factor HAC1. Involved in the regulation of the UPR in response to ER stress (By similarity). Endoplasmic reticulum membrane; Single-pass membrane protein. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016787; GO:0046872; GO:0004674; GO:0004521; GO:0051082,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,0.613,0.613,0.613,0.613,0.3846,5,0.5673,0.4638,no
IRE1_HYPJQ,G0RBE3,ProtTale,Eukaryota,1243,Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain splices precursor mRNAs to produce their mature form which then induces transcription of UPR target genes.,Acts as a substrate-specific adapter for the E3 ubiquitin-protein ligase UBR4. UBR4 is a substrate-specific adapter of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates ubiquitination of target proteins.,No,No,No,No,No,not-Yes,GO:0005524; GO:0016787; GO:0046872; GO:0004674; GO:0004521; GO:0051082,,,,,,,,,,,0,,0.4638,no
IRE1_HYPJQ,G0RBE3,Protein2Text,Eukaryota,1243,Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain splices precursor mRNAs to produce their mature form which then induces transcription of UPR target genes.,"The molecular function of this protein is not specified in the provided information. However, based on its name and the fact that it is involved in a process related to the endoplasmic reticulum (ER), it is likely that this protein is involved in protein folding, modification, or transport. More specific information would be needed to determine its exact molecular function.",Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0005524; GO:0016787; GO:0046872; GO:0004674; GO:0004521; GO:0051082,,,,,,,,,,,0,,0.4638,no
IRE1_HYPJQ,G0RBE3,Reference,Eukaryota,1243,Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain splices precursor mRNAs to produce their mature form which then induces transcription of UPR target genes.,Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain splices precursor mRNAs to produce their mature form which then induces transcription of UPR target genes.,,,,,,,GO:0005524; GO:0016787; GO:0046872; GO:0004674; GO:0004521; GO:0051082,GO:0004521; GO:0004674,GO:0004521; GO:0004672,GO:0004521; GO:0004674; GO:0005524,GO:0004521,GO:0004521,0.5671,0.5511,0.7499,0.3816,0.3816,5,0.5263,0.4638,no
ATC5_CHATD,G0S196,ESM2Text,Eukaryota,1555,Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine and phosphatidylserine from the lumenal to the cytosolic leaflet of membranes and ensures the maintenance of asymmetric distribution of phospholipids. May also transport glucosylceramide and phosphatidylethanolamine.,"Catalytic component of a P4-ATPase flippase complex, which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Involved in maintenance of asymmetric distribution of phosphatidylserine (PS) in spermatozoa membranes. May act as a flippase motor to control flippase activity and substrate specificity.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0016887; GO:0140351; GO:0000287; GO:0090554; GO:0140346; GO:0090556,GO:0005524; GO:0016887; GO:0004012,GO:0004612; GO:0016887; GO:0005524,GO:0004612,GO:0004012,GO:0004012,0.783,0.5108,0.0841,0.5031,0.5031,5,0.4768,0.6547,yes
ATC5_CHATD,G0S196,Prot2Text,Eukaryota,1555,Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine and phosphatidylserine from the lumenal to the cytosolic leaflet of membranes and ensures the maintenance of asymmetric distribution of phospholipids. May also transport glucosylceramide and phosphatidylethanolamine.,This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids. Required for protein transport from Golgi to vacuoles.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0016887; GO:0140351; GO:0000287; GO:0090554; GO:0140346; GO:0090556,GO:0015442,GO:0004012,GO:0004012,GO:0005524; GO:0046872; GO:0008510,GO:0004012,0.0,0.5031,0.5031,0.4384,0.5031,5,0.3895,0.6547,yes
ATC5_CHATD,G0S196,ProtT3,Eukaryota,1555,Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine and phosphatidylserine from the lumenal to the cytosolic leaflet of membranes and ensures the maintenance of asymmetric distribution of phospholipids. May also transport glucosylceramide and phosphatidylethanolamine.,The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses (By similarity). Membrane; Multi-pass membrane protein. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIA subfamily,No,No,No,No,No,not-Yes,GO:0005524; GO:0016887; GO:0140351; GO:0000287; GO:0090554; GO:0140346; GO:0090556,GO:0005524; GO:0015078,GO:0008553,GO:0008553; GO:0005524,GO:0008553,GO:0008553,0.3526,0.1377,0.3624,0.1377,0.1377,5,0.2256,0.6547,yes
ATC5_CHATD,G0S196,ProtTale,Eukaryota,1555,Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine and phosphatidylserine from the lumenal to the cytosolic leaflet of membranes and ensures the maintenance of asymmetric distribution of phospholipids. May also transport glucosylceramide and phosphatidylethanolamine.,Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0140351; GO:0000287; GO:0090554; GO:0140346; GO:0090556,GO:0004012; GO:0005524,GO:0004012; GO:0005524,GO:0004012; GO:0005524,GO:0016887; GO:0015442,GO:0004012; GO:0005524,0.6774,0.6774,0.6774,0.356,0.6774,5,0.6131,0.6547,yes
ATC5_CHATD,G0S196,Protein2Text,Eukaryota,1555,Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine and phosphatidylserine from the lumenal to the cytosolic leaflet of membranes and ensures the maintenance of asymmetric distribution of phospholipids. May also transport glucosylceramide and phosphatidylethanolamine.,"This protein is a P-type ATPase, which means it uses ATP to transport ions across cell membranes. Specifically, it is a calcium-transporting ATPase, which helps to regulate the concentration of calcium ions within the cell.",No,No,No,No,Maybe,not-Yes,GO:0005524; GO:0016887; GO:0140351; GO:0000287; GO:0090554; GO:0140346; GO:0090556,GO:0005388,GO:0005388,GO:0005388,GO:0005388,GO:0005388,0.1321,0.1321,0.1321,0.1321,0.1321,5,0.1321,0.6547,yes
ATC5_CHATD,G0S196,Reference,Eukaryota,1555,Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine and phosphatidylserine from the lumenal to the cytosolic leaflet of membranes and ensures the maintenance of asymmetric distribution of phospholipids. May also transport glucosylceramide and phosphatidylethanolamine.,Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine and phosphatidylserine from the lumenal to the cytosolic leaflet of membranes and ensures the maintenance of asymmetric distribution of phospholipids. May also transport glucosylceramide and phosphatidylethanolamine.,,,,,,,GO:0005524; GO:0016887; GO:0140351; GO:0000287; GO:0090554; GO:0140346; GO:0090556,GO:0004012; GO:0005524,GO:0034040; GO:0005524,GO:0004012; GO:0005524,GO:0005524; GO:0015441; GO:0004012,GO:0005524; GO:0015441; GO:0004622,0.6774,0.4574,0.6774,0.6284,0.351,5,0.5583,0.6547,yes
AHP1_CHATD,G0S1P8,ESM2Text,Eukaryota,172,"Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Preferentially eliminates organic peroxides rather than hydrogen peroxide. Relays alkyl hydroperoxides as a signal to the transcription factor CAD1/YAP2 by inducing the formation of intramolecular disulfide bonds in CAD1, which causes its nuclear accumulation and activation. Involved in cellular Mn(2+) homeostasis.","Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0008379,GO:0004601,GO:0004601,GO:0004601,GO:0051920,GO:0004601,0.5274,0.5274,0.5274,0.5704,0.5274,5,0.536,0.273,no
AHP1_CHATD,G0S1P8,Prot2Text,Eukaryota,172,"Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Preferentially eliminates organic peroxides rather than hydrogen peroxide. Relays alkyl hydroperoxides as a signal to the transcription factor CAD1/YAP2 by inducing the formation of intramolecular disulfide bonds in CAD1, which causes its nuclear accumulation and activation. Involved in cellular Mn(2+) homeostasis.","Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0008379,GO:0051920,GO:0051920,GO:0004601,GO:0004601,GO:0008379,0.5704,0.5704,0.5274,0.5274,0.6927,5,0.5777,0.273,no
AHP1_CHATD,G0S1P8,ProtT3,Eukaryota,172,"Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Preferentially eliminates organic peroxides rather than hydrogen peroxide. Relays alkyl hydroperoxides as a signal to the transcription factor CAD1/YAP2 by inducing the formation of intramolecular disulfide bonds in CAD1, which causes its nuclear accumulation and activation. Involved in cellular Mn(2+) homeostasis.","Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Belongs to the peroxiredoxin family. Prx5 subfamily",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0008379,GO:0051920,GO:0051920,GO:0051920,GO:0051920,GO:0004601,0.5704,0.5704,0.5704,0.5704,0.5274,5,0.5618,0.273,no
AHP1_CHATD,G0S1P8,ProtTale,Eukaryota,172,"Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Preferentially eliminates organic peroxides rather than hydrogen peroxide. Relays alkyl hydroperoxides as a signal to the transcription factor CAD1/YAP2 by inducing the formation of intramolecular disulfide bonds in CAD1, which causes its nuclear accumulation and activation. Involved in cellular Mn(2+) homeostasis.","Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0008379,GO:0004601,GO:0004601,GO:0004601,GO:0004601,GO:0004601; GO:0051920,0.5274,0.5274,0.5274,0.5274,0.615,5,0.5449,0.273,no
AHP1_CHATD,G0S1P8,Protein2Text,Eukaryota,172,"Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Preferentially eliminates organic peroxides rather than hydrogen peroxide. Relays alkyl hydroperoxides as a signal to the transcription factor CAD1/YAP2 by inducing the formation of intramolecular disulfide bonds in CAD1, which causes its nuclear accumulation and activation. Involved in cellular Mn(2+) homeostasis.","The molecular function of this protein is thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. It also has a penicillin-binding protein activity. The peroxidase activity is essential for the protection of cells from photo-oxidative damage. The penicillin-binding protein activity is probably involved in the biosynthesis of penicillin. In addition, it has a glutathione-dependent peroxidase activity that protects cells from oxidative stress. It has a thiol-specific peroxidase activity. It also has a glutathione peroxidase activity that protects cells from oxidative stress. The glutathione peroxidase activity is important for the protection of cells from oxidative stress. It has a glutathione S-transferase activity that catalyzes the conjugation of reduced glutathione to a wide variety of electrophiles. It also has a glutathione-dependent peroxidase activity that protects cells from oxidative stress. It has a glutathione peroxidase activity that protects cells from oxidative stress. It has a glutathione S-transferase activity that catalyzes the conjugation of reduced glutathione to a wide variety of electrophiles. It also has a glutathione-dependent peroxidase activity that protects cells from oxidative stress. The glutathione-dependent peroxidase activity is important for the protection of cells from oxidative stress. It has a glutathione peroxidase activity that protects cells from oxidative stress. It has a glutathione S-transferase activity that catalyzes the conjugation of reduced glutathione to a wide variety of electrophiles. It also has a glutathione-dependent peroxidase activity that protects cells from oxidative stress. The glutathione-dependent peroxidase activity is important for the protection of cells from oxidative stress. It has a glutathione peroxidase activity that protects cells from oxidative stress. It has a glutathione S-transferase activity that catalyzes the conjugation of reduced glutathione to a wide variety of electrophiles. It also has a glutathione-dependent peroxidase activity that protects cells from oxidative stress. The glutathione-dependent peroxidase activity is important for the protection of cells from oxidative stress. It has a glutathione peroxidase activity that protects cells from oxidative stress. It has a glutathione S-transferase activity that catalyzes the conjugation of reduced glutathione to a wide variety of elect",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0008379,GO:0004601,GO:0004601,GO:0004601,GO:0051920,GO:0004601,0.5274,0.5274,0.5274,0.5704,0.5274,5,0.536,0.273,no
AHP1_CHATD,G0S1P8,Reference,Eukaryota,172,"Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Preferentially eliminates organic peroxides rather than hydrogen peroxide. Relays alkyl hydroperoxides as a signal to the transcription factor CAD1/YAP2 by inducing the formation of intramolecular disulfide bonds in CAD1, which causes its nuclear accumulation and activation. Involved in cellular Mn(2+) homeostasis.","Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Preferentially eliminates organic peroxides rather than hydrogen peroxide. Relays alkyl hydroperoxides as a signal to the transcription factor CAD1/YAP2 by inducing the formation of intramolecular disulfide bonds in CAD1, which causes its nuclear accumulation and activation. Involved in cellular Mn(2+) homeostasis.",,,,,,,GO:0046872; GO:0008379,GO:0004601; GO:0051920,GO:0004601; GO:0016209,GO:0004601; GO:0051920,GO:0004601; GO:0016209,GO:0004601; GO:0051920,0.615,0.5148,0.615,0.5148,0.615,5,0.5749,0.273,no
EZH2_CHATD,G0SDW4,ESM2Text,Eukaryota,1522,"Catalytic subunit of the of the Polycomb Repressive Complex 2 (PRC2), a histone H3 lysine methyltransferase responsible for generating mono-, di-, and tri-methylation on Lys27 (H3K27me1, H3K27me2 and H3K27me3). The tri-methylated form is known to be critical in gene repression, and its proper placement is essential in defining repression patterns during development. The PRC2 complex interacts with thousands of RNA species in vivo, but the physiological function of RNA binding has still to be determined.","Polycomb group (PcG) protein. Catalytic subunit of the prc2/eed-ezh2 complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. May regulate the circadian clock via histone methylation at the promoter of the circadian genes.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0003682; GO:0140951; GO:0046872,GO:0018024; GO:0008168,GO:0018024,GO:0018024,GO:0046974,GO:0042054,0.2923,0.0,0.0,0.45,0.3892,5,0.2263,0.5194,no
EZH2_CHATD,G0SDW4,Prot2Text,Eukaryota,1522,"Catalytic subunit of the of the Polycomb Repressive Complex 2 (PRC2), a histone H3 lysine methyltransferase responsible for generating mono-, di-, and tri-methylation on Lys27 (H3K27me1, H3K27me2 and H3K27me3). The tri-methylated form is known to be critical in gene repression, and its proper placement is essential in defining repression patterns during development. The PRC2 complex interacts with thousands of RNA species in vivo, but the physiological function of RNA binding has still to be determined.","Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as regulation of telomere length and regulation of transcriptional start sites.",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0003682; GO:0140951; GO:0046872,GO:0046974,GO:0046974,GO:0046974,GO:0018024,GO:0042054,0.45,0.45,0.45,0.0,0.3892,5,0.3478,0.5194,no
EZH2_CHATD,G0SDW4,ProtT3,Eukaryota,1522,"Catalytic subunit of the of the Polycomb Repressive Complex 2 (PRC2), a histone H3 lysine methyltransferase responsible for generating mono-, di-, and tri-methylation on Lys27 (H3K27me1, H3K27me2 and H3K27me3). The tri-methylated form is known to be critical in gene repression, and its proper placement is essential in defining repression patterns during development. The PRC2 complex interacts with thousands of RNA species in vivo, but the physiological function of RNA binding has still to be determined.",Histone methyltransferase that trimethylates histone H3 'Lys- 36' forming H3K36me3. Involved in transcription elongation as well as in transcription repression. Nucleus Chromosome. Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar4-20 subfamily,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0003682; GO:0140951; GO:0046872,GO:0018024,GO:0046975,GO:0042054,GO:0018024,GO:0018024,0.0,0.45,0.3892,0.0,0.0,5,0.1678,0.5194,no
EZH2_CHATD,G0SDW4,ProtTale,Eukaryota,1522,"Catalytic subunit of the of the Polycomb Repressive Complex 2 (PRC2), a histone H3 lysine methyltransferase responsible for generating mono-, di-, and tri-methylation on Lys27 (H3K27me1, H3K27me2 and H3K27me3). The tri-methylated form is known to be critical in gene repression, and its proper placement is essential in defining repression patterns during development. The PRC2 complex interacts with thousands of RNA species in vivo, but the physiological function of RNA binding has still to be determined.",Histone methyltransferase that trimethylates histone H3 'Lys- 36' forming H3K36me3. Involved in transcription elongation as well as in transcription repression.,No,No,Maybe,No,Maybe,not-Yes,GO:0003682; GO:0140951; GO:0046872,GO:0042054,GO:0042054,GO:0046975,GO:0042054,GO:0046975,0.3892,0.3892,0.45,0.3892,0.45,5,0.4135,0.5194,no
EZH2_CHATD,G0SDW4,Protein2Text,Eukaryota,1522,"Catalytic subunit of the of the Polycomb Repressive Complex 2 (PRC2), a histone H3 lysine methyltransferase responsible for generating mono-, di-, and tri-methylation on Lys27 (H3K27me1, H3K27me2 and H3K27me3). The tri-methylated form is known to be critical in gene repression, and its proper placement is essential in defining repression patterns during development. The PRC2 complex interacts with thousands of RNA species in vivo, but the physiological function of RNA binding has still to be determined.",This protein is involved in the molecular function of protein binding.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0003682; GO:0140951; GO:0046872,,GO:0005515,,,GO:0005515,,0.4058,,,0.4058,2,0.4058,0.5194,no
EZH2_CHATD,G0SDW4,Reference,Eukaryota,1522,"Catalytic subunit of the of the Polycomb Repressive Complex 2 (PRC2), a histone H3 lysine methyltransferase responsible for generating mono-, di-, and tri-methylation on Lys27 (H3K27me1, H3K27me2 and H3K27me3). The tri-methylated form is known to be critical in gene repression, and its proper placement is essential in defining repression patterns during development. The PRC2 complex interacts with thousands of RNA species in vivo, but the physiological function of RNA binding has still to be determined.","Catalytic subunit of the of the Polycomb Repressive Complex 2 (PRC2), a histone H3 lysine methyltransferase responsible for generating mono-, di-, and tri-methylation on Lys27 (H3K27me1, H3K27me2 and H3K27me3). The tri-methylated form is known to be critical in gene repression, and its proper placement is essential in defining repression patterns during development. The PRC2 complex interacts with thousands of RNA species in vivo, but the physiological function of RNA binding has still to be determined.",,,,,,,GO:0003682; GO:0140951; GO:0046872,GO:0042054,GO:0042054,GO:0018024,GO:0018024; GO:0008168,GO:0018024,0.3892,0.3892,0.0,0.2923,0.0,5,0.2141,0.5194,no
MGM1_CHATD,G0SGC7,ESM2Text,Eukaryota,939,"Dynamin-related GTPase that is essential for normal mitochondrial morphology by mediating fusion of the mitochondrial inner membranes, regulating cristae morphology and maintaining respiratory chain function. Exists in two forms: the transmembrane, long form (Dynamin-like GTPase MGM1, long form; L-MGM1), which is tethered to the inner mitochondrial membrane, and the short soluble form (Dynamin-like GTPase MGM1, short form; S-MGM1), which results from proteolytic cleavage and localizes in the intermembrane space. Both forms (L-MGM1 and S-MGM1) cooperate to catalyze the fusion of the mitochondrial inner membrane. The equilibrium between L-MGM1 and S-MGM1 is essential: excess levels of S-MGM1, following loss of mitochondrial membrane potential, lead to an impaired equilibrium between L-MGM1 and S-MGM1, inhibiting mitochondrial fusion. Plays a role in the maintenance and remodeling of mitochondrial cristae, some invaginations of the mitochondrial inner membrane that provide an increase in the surface area. Probably acts by forming helical filaments at the inside of inner membrane tubes with the shape and dimensions of crista junctions.",Mitochondrial GTPase involved in mitochondrial trafficking.,Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0005525; GO:0003924; GO:0140523; GO:0008289; GO:0180020; GO:0046872; GO:0008017,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924,GO:0003924,GO:0003924,0.6217,0.6217,0.412,0.412,0.412,5,0.4959,0.4238,no
MGM1_CHATD,G0SGC7,Prot2Text,Eukaryota,939,"Dynamin-related GTPase that is essential for normal mitochondrial morphology by mediating fusion of the mitochondrial inner membranes, regulating cristae morphology and maintaining respiratory chain function. Exists in two forms: the transmembrane, long form (Dynamin-like GTPase MGM1, long form; L-MGM1), which is tethered to the inner mitochondrial membrane, and the short soluble form (Dynamin-like GTPase MGM1, short form; S-MGM1), which results from proteolytic cleavage and localizes in the intermembrane space. Both forms (L-MGM1 and S-MGM1) cooperate to catalyze the fusion of the mitochondrial inner membrane. The equilibrium between L-MGM1 and S-MGM1 is essential: excess levels of S-MGM1, following loss of mitochondrial membrane potential, lead to an impaired equilibrium between L-MGM1 and S-MGM1, inhibiting mitochondrial fusion. Plays a role in the maintenance and remodeling of mitochondrial cristae, some invaginations of the mitochondrial inner membrane that provide an increase in the surface area. Probably acts by forming helical filaments at the inside of inner membrane tubes with the shape and dimensions of crista junctions.",Enzyme hydrolyzing GTP. Has a role in mitochondrial morphology and respiration.,Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0005525; GO:0003924; GO:0140523; GO:0008289; GO:0180020; GO:0046872; GO:0008017,GO:0003924,GO:0003924,GO:0003924,GO:0003924; GO:0005525,GO:0003924,0.412,0.412,0.412,0.6217,0.412,5,0.4539,0.4238,no
MGM1_CHATD,G0SGC7,ProtT3,Eukaryota,939,"Dynamin-related GTPase that is essential for normal mitochondrial morphology by mediating fusion of the mitochondrial inner membranes, regulating cristae morphology and maintaining respiratory chain function. Exists in two forms: the transmembrane, long form (Dynamin-like GTPase MGM1, long form; L-MGM1), which is tethered to the inner mitochondrial membrane, and the short soluble form (Dynamin-like GTPase MGM1, short form; S-MGM1), which results from proteolytic cleavage and localizes in the intermembrane space. Both forms (L-MGM1 and S-MGM1) cooperate to catalyze the fusion of the mitochondrial inner membrane. The equilibrium between L-MGM1 and S-MGM1 is essential: excess levels of S-MGM1, following loss of mitochondrial membrane potential, lead to an impaired equilibrium between L-MGM1 and S-MGM1, inhibiting mitochondrial fusion. Plays a role in the maintenance and remodeling of mitochondrial cristae, some invaginations of the mitochondrial inner membrane that provide an increase in the surface area. Probably acts by forming helical filaments at the inside of inner membrane tubes with the shape and dimensions of crista junctions.",Mitochondrion outer membrane; Single-pass membrane protein. Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005525; GO:0003924; GO:0140523; GO:0008289; GO:0180020; GO:0046872; GO:0008017,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924,0.6217,0.6217,0.6217,0.6217,0.412,5,0.5798,0.4238,no
MGM1_CHATD,G0SGC7,ProtTale,Eukaryota,939,"Dynamin-related GTPase that is essential for normal mitochondrial morphology by mediating fusion of the mitochondrial inner membranes, regulating cristae morphology and maintaining respiratory chain function. Exists in two forms: the transmembrane, long form (Dynamin-like GTPase MGM1, long form; L-MGM1), which is tethered to the inner mitochondrial membrane, and the short soluble form (Dynamin-like GTPase MGM1, short form; S-MGM1), which results from proteolytic cleavage and localizes in the intermembrane space. Both forms (L-MGM1 and S-MGM1) cooperate to catalyze the fusion of the mitochondrial inner membrane. The equilibrium between L-MGM1 and S-MGM1 is essential: excess levels of S-MGM1, following loss of mitochondrial membrane potential, lead to an impaired equilibrium between L-MGM1 and S-MGM1, inhibiting mitochondrial fusion. Plays a role in the maintenance and remodeling of mitochondrial cristae, some invaginations of the mitochondrial inner membrane that provide an increase in the surface area. Probably acts by forming helical filaments at the inside of inner membrane tubes with the shape and dimensions of crista junctions.","Degrades double-stranded DNA (dsDNA) in a 5' to 3' direction. Its activity is stimulated by single-stranded DNA. Plays an important role in the maintenance of mitochondrial DNA (mtDNA). The 5' to 3' degradation product is a 5'- phosphorylated oligoadenylate (A-nucleoside 2',3'- phosphate [poly(A)]) which acts as a inhibitor of mitochondrial DNA replication. Is also able to degrade single-stranded DNA.",No,No,No,No,No,not-Yes,GO:0005525; GO:0003924; GO:0140523; GO:0008289; GO:0180020; GO:0046872; GO:0008017,GO:0004529,GO:0004534; GO:0004536,GO:0004534,GO:0004518,GO:0004536,0.1278,0.1473,0.1057,0.1943,0.1451,5,0.144,0.4238,no
MGM1_CHATD,G0SGC7,Protein2Text,Eukaryota,939,"Dynamin-related GTPase that is essential for normal mitochondrial morphology by mediating fusion of the mitochondrial inner membranes, regulating cristae morphology and maintaining respiratory chain function. Exists in two forms: the transmembrane, long form (Dynamin-like GTPase MGM1, long form; L-MGM1), which is tethered to the inner mitochondrial membrane, and the short soluble form (Dynamin-like GTPase MGM1, short form; S-MGM1), which results from proteolytic cleavage and localizes in the intermembrane space. Both forms (L-MGM1 and S-MGM1) cooperate to catalyze the fusion of the mitochondrial inner membrane. The equilibrium between L-MGM1 and S-MGM1 is essential: excess levels of S-MGM1, following loss of mitochondrial membrane potential, lead to an impaired equilibrium between L-MGM1 and S-MGM1, inhibiting mitochondrial fusion. Plays a role in the maintenance and remodeling of mitochondrial cristae, some invaginations of the mitochondrial inner membrane that provide an increase in the surface area. Probably acts by forming helical filaments at the inside of inner membrane tubes with the shape and dimensions of crista junctions.","This protein is involved in the mitochondrial function, specifically in the electron transport chain. It plays a role in the transfer of electrons in the mitochondrial respiratory chain.",No,No,No,No,No,not-Yes,GO:0005525; GO:0003924; GO:0140523; GO:0008289; GO:0180020; GO:0046872; GO:0008017,,GO:0009055,,,GO:0009055,,0.2637,,,0.2637,2,0.2637,0.4238,no
MGM1_CHATD,G0SGC7,Reference,Eukaryota,939,"Dynamin-related GTPase that is essential for normal mitochondrial morphology by mediating fusion of the mitochondrial inner membranes, regulating cristae morphology and maintaining respiratory chain function. Exists in two forms: the transmembrane, long form (Dynamin-like GTPase MGM1, long form; L-MGM1), which is tethered to the inner mitochondrial membrane, and the short soluble form (Dynamin-like GTPase MGM1, short form; S-MGM1), which results from proteolytic cleavage and localizes in the intermembrane space. Both forms (L-MGM1 and S-MGM1) cooperate to catalyze the fusion of the mitochondrial inner membrane. The equilibrium between L-MGM1 and S-MGM1 is essential: excess levels of S-MGM1, following loss of mitochondrial membrane potential, lead to an impaired equilibrium between L-MGM1 and S-MGM1, inhibiting mitochondrial fusion. Plays a role in the maintenance and remodeling of mitochondrial cristae, some invaginations of the mitochondrial inner membrane that provide an increase in the surface area. Probably acts by forming helical filaments at the inside of inner membrane tubes with the shape and dimensions of crista junctions.","Dynamin-related GTPase that is essential for normal mitochondrial morphology by mediating fusion of the mitochondrial inner membranes, regulating cristae morphology and maintaining respiratory chain function. Exists in two forms: the transmembrane, long form (Dynamin-like GTPase MGM1, long form; L-MGM1), which is tethered to the inner mitochondrial membrane, and the short soluble form (Dynamin-like GTPase MGM1, short form; S-MGM1), which results from proteolytic cleavage and localizes in the intermembrane space. Both forms (L-MGM1 and S-MGM1) cooperate to catalyze the fusion of the mitochondrial inner membrane. The equilibrium between L-MGM1 and S-MGM1 is essential: excess levels of S-MGM1, following loss of mitochondrial membrane potential, lead to an impaired equilibrium between L-MGM1 and S-MGM1, inhibiting mitochondrial fusion. Plays a role in the maintenance and remodeling of mitochondrial cristae, some invaginations of the mitochondrial inner membrane that provide an increase in the surface area. Probably acts by forming helical filaments at the inside of inner membrane tubes with the shape and dimensions of crista junctions.",,,,,,,GO:0005525; GO:0003924; GO:0140523; GO:0008289; GO:0180020; GO:0046872; GO:0008017,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0005525; GO:0003924,0.6217,0.6217,0.6217,0.6217,0.6217,5,0.6217,0.4238,no
POLG_TMUV,G1CRV4,ESM2Text,Viruses,3425,[Capsid protein C]: Capsid protein self-assembles to form an icosahedral capsid about 40 nm in diameter (Probable). Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle.,"During the asexual blood stage, promotes the permeation of the enterobacterial common antigen (ECA) 2.2.",No,No,No,No,No,not-Yes,GO:0005524; GO:0003725; GO:0046872; GO:0004483; GO:0004482; GO:0046983; GO:0017111; GO:0003724; GO:0003968; GO:0004252; GO:0005198,,,,,,,,,,,0,,0.4487,no
POLG_TMUV,G1CRV4,Prot2Text,Viruses,3425,[Capsid protein C]: Capsid protein self-assembles to form an icosahedral capsid about 40 nm in diameter (Probable). Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle.,"Unlike beta-carboxysomes, alpha-carboxysomes (Cb) can form without cargo protein. CsoS2 is essential for Cb formation and is also capable of targeting foreign proteins to the Cb. The Cb shell assembles with the aid of CsoS2; CsoS1A, CsoS1B and CsoS1C form the majority of the shell while CsoS4A and CsoS4B form vertices. CsoS1D forms pseudohexamers that probably control metabolite flux into and out of the shell.",No,No,No,No,No,not-Yes,GO:0005524; GO:0003725; GO:0046872; GO:0004483; GO:0004482; GO:0046983; GO:0017111; GO:0003724; GO:0003968; GO:0004252; GO:0005198,,,,,,,,,,,0,,0.4487,no
POLG_TMUV,G1CRV4,ProtT3,Viruses,3425,[Capsid protein C]: Capsid protein self-assembles to form an icosahedral capsid about 40 nm in diameter (Probable). Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle.,"Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding to its host receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress. Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I",No,No,No,No,No,not-Yes,GO:0005524; GO:0003725; GO:0046872; GO:0004483; GO:0004482; GO:0046983; GO:0017111; GO:0003724; GO:0003968; GO:0004252; GO:0005198,,,,,,,,,,,0,,0.4487,no
POLG_TMUV,G1CRV4,ProtTale,Viruses,3425,[Capsid protein C]: Capsid protein self-assembles to form an icosahedral capsid about 40 nm in diameter (Probable). Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle.,[Capsid protein]: Forms an icosahedral capsid of T=13 symmetry with a T=2 symmetry axis.,Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0005524; GO:0003725; GO:0046872; GO:0004483; GO:0004482; GO:0046983; GO:0017111; GO:0003724; GO:0003968; GO:0004252; GO:0005198,,,GO:0005198,,GO:0005198,,,0.31,,0.31,2,0.31,0.4487,no
POLG_TMUV,G1CRV4,Protein2Text,Viruses,3425,[Capsid protein C]: Capsid protein self-assembles to form an icosahedral capsid about 40 nm in diameter (Probable). Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle.,"This protein is a viral protein, specifically a reverse transcriptase, which plays a crucial role in the replication of the viral genome. The molecular function of this protein is to convert the viral RNA into DNA using the enzyme reverse transcriptase, which is essential for the replication of the virus.",No,No,No,No,Maybe,not-Yes,GO:0005524; GO:0003725; GO:0046872; GO:0004483; GO:0004482; GO:0046983; GO:0017111; GO:0003724; GO:0003968; GO:0004252; GO:0005198,GO:0003964,GO:0003964,GO:0003964,GO:0003964,GO:0003964,0.208,0.208,0.208,0.208,0.208,5,0.208,0.4487,no
POLG_TMUV,G1CRV4,Reference,Viruses,3425,[Capsid protein C]: Capsid protein self-assembles to form an icosahedral capsid about 40 nm in diameter (Probable). Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle.,[Capsid protein C]: Capsid protein self-assembles to form an icosahedral capsid about 40 nm in diameter (Probable). Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle.,,,,,,,GO:0005524; GO:0003725; GO:0046872; GO:0004483; GO:0004482; GO:0046983; GO:0017111; GO:0003724; GO:0003968; GO:0004252; GO:0005198,GO:0005198; GO:0003723,GO:0005198; GO:0003723,GO:0005198; GO:0003723,,,0.417,0.417,0.417,,,3,0.417,0.4487,no
TFP_THLAR,G1FNI6,ESM2Text,Eukaryota,348,"Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation. Catalyzes allylthiocyanate and corresponding epithionitrile formation from allylglucosinolate in the presence of myrosinase. Also converts aliphatic glucosinolates, such as indol-3-ylmethylglucosinolate, 4- methylsulfinylbutylglucosinolate, 4-methylthiobutyl- and benzylisothiocyanate, to simple nitriles.","Promotes simple nitriles, but not epithionitrile or thiocyanate formation. Converts allylglucosinolate and benzylglucosinolate to their corresponding simple nitriles in the presence of myrosinase.",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0030234; GO:0042802; GO:0016829; GO:0046872; GO:0042803,,,,,,,,,,,0,,0.4239,no
TFP_THLAR,G1FNI6,Prot2Text,Eukaryota,348,"Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation. Catalyzes allylthiocyanate and corresponding epithionitrile formation from allylglucosinolate in the presence of myrosinase. Also converts aliphatic glucosinolates, such as indol-3-ylmethylglucosinolate, 4- methylsulfinylbutylglucosinolate, 4-methylthiobutyl- and benzylisothiocyanate, to simple nitriles.","Promotes simple nitriles, but not epithionitrile or thiocyanate formation. Converts allylglucosinolate and benzylglucosinolate to their corresponding simple nitriles in the presence of myrosinase.",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0030234; GO:0042802; GO:0016829; GO:0046872; GO:0042803,,,,,,,,,,,0,,0.4239,no
TFP_THLAR,G1FNI6,ProtT3,Eukaryota,348,"Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation. Catalyzes allylthiocyanate and corresponding epithionitrile formation from allylglucosinolate in the presence of myrosinase. Also converts aliphatic glucosinolates, such as indol-3-ylmethylglucosinolate, 4- methylsulfinylbutylglucosinolate, 4-methylthiobutyl- and benzylisothiocyanate, to simple nitriles.","Catalyzes the conversion of glutathione (GSH) to gamma-glutamylcysteine (gamma-EC), the first step in the synthesis of phytochelatins, a class of heavy-metal-binding peptides. Cytoplasm. Belongs to the GST superfamily. Sigma family",No,No,No,No,No,not-Yes,GO:0030234; GO:0042802; GO:0016829; GO:0046872; GO:0042803,GO:0016755,GO:0004364,GO:0004364,GO:0004364,GO:0046938,0.2257,0.2257,0.2257,0.2257,0.0,5,0.1806,0.4239,no
TFP_THLAR,G1FNI6,ProtTale,Eukaryota,348,"Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation. Catalyzes allylthiocyanate and corresponding epithionitrile formation from allylglucosinolate in the presence of myrosinase. Also converts aliphatic glucosinolates, such as indol-3-ylmethylglucosinolate, 4- methylsulfinylbutylglucosinolate, 4-methylthiobutyl- and benzylisothiocyanate, to simple nitriles.","Acts as a GTPase-activating protein (GAP) for RAB11A and RAB11FIP1. Involved in the regulation of insulin-mediated glucose uptake and glucose transporter SLC2A4/GLUT4 translocation from intracellular vesicles to the plasma membrane. Acts as a guanine nucleotide exchange factor (GEF) for RAB11A and RAB11FIP1, promoting the exchange of bound GDP for free GTP, thereby activating the GTP-binding activity of RAB11A and RAB11FIP1.",No,No,No,No,No,not-Yes,GO:0030234; GO:0042802; GO:0016829; GO:0046872; GO:0042803,GO:0005096; GO:0005085,GO:0005096; GO:0005085,GO:0005096; GO:0005085,GO:0005096; GO:0005085,GO:0005096; GO:0005085,0.3112,0.3112,0.3112,0.3112,0.3112,5,0.3112,0.4239,no
TFP_THLAR,G1FNI6,Protein2Text,Eukaryota,348,"Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation. Catalyzes allylthiocyanate and corresponding epithionitrile formation from allylglucosinolate in the presence of myrosinase. Also converts aliphatic glucosinolates, such as indol-3-ylmethylglucosinolate, 4- methylsulfinylbutylglucosinolate, 4-methylthiobutyl- and benzylisothiocyanate, to simple nitriles.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its name and involvement in the regulation of gene expression, it is likely that this protein plays a role in binding to DNA or RNA, and may be involved in transcriptional regulation or other processes related to gene expression. Further research would be necessary to determine the specific molecular function of this protein.",No,No,No,Vague,No,not-Yes,GO:0030234; GO:0042802; GO:0016829; GO:0046872; GO:0042803,,,,,,,,,,,0,,0.4239,no
TFP_THLAR,G1FNI6,Reference,Eukaryota,348,"Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation. Catalyzes allylthiocyanate and corresponding epithionitrile formation from allylglucosinolate in the presence of myrosinase. Also converts aliphatic glucosinolates, such as indol-3-ylmethylglucosinolate, 4- methylsulfinylbutylglucosinolate, 4-methylthiobutyl- and benzylisothiocyanate, to simple nitriles.","Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation. Catalyzes allylthiocyanate and corresponding epithionitrile formation from allylglucosinolate in the presence of myrosinase. Also converts aliphatic glucosinolates, such as indol-3-ylmethylglucosinolate, 4- methylsulfinylbutylglucosinolate, 4-methylthiobutyl- and benzylisothiocyanate, to simple nitriles.",,,,,,,GO:0030234; GO:0042802; GO:0016829; GO:0046872; GO:0042803,,,,,,,,,,,0,,0.4239,no
GNPAT_RABIT,G1SPE9,ESM2Text,Eukaryota,679,"Dihydroxyacetonephosphate acyltransferase catalyzing the first step in the biosynthesis of plasmalogens, a subset of phospholipids that differ from other glycerolipids by having an alkyl chain attached through a vinyl ether linkage at the sn-1 position of the glycerol backbone, and which unique physical properties have an impact on various aspects of cell signaling and membrane biology.",Dihydroxyacetonephosphate acyltransferase involved in plasmalogen biosynthesis.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004366; GO:0016287,GO:0016746,GO:0016287,GO:0016287,GO:0016287,GO:0004138,0.6099,0.869,0.869,0.869,0.2073,5,0.6848,0.448,no
GNPAT_RABIT,G1SPE9,Prot2Text,Eukaryota,679,"Dihydroxyacetonephosphate acyltransferase catalyzing the first step in the biosynthesis of plasmalogens, a subset of phospholipids that differ from other glycerolipids by having an alkyl chain attached through a vinyl ether linkage at the sn-1 position of the glycerol backbone, and which unique physical properties have an impact on various aspects of cell signaling and membrane biology.",Dihydroxyacetonephosphate acyltransferase involved in plasmalogen biosynthesis.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004366; GO:0016287,GO:0016747,GO:0016287,GO:0016746,GO:0008654,GO:0016287,0.7101,0.869,0.6099,0.0,0.869,5,0.6116,0.448,no
GNPAT_RABIT,G1SPE9,ProtT3,Eukaryota,679,"Dihydroxyacetonephosphate acyltransferase catalyzing the first step in the biosynthesis of plasmalogens, a subset of phospholipids that differ from other glycerolipids by having an alkyl chain attached through a vinyl ether linkage at the sn-1 position of the glycerol backbone, and which unique physical properties have an impact on various aspects of cell signaling and membrane biology.",1-acyl-sn-glycerol-3-phosphate acyltransferase involved in phospholipid biosynthesis. Mitochondrion membrane; Peripheral membrane protein; Matrix side. Belongs to the GPAT/DAPAT family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004366; GO:0016287,GO:0003841,GO:0003841,GO:0003841,GO:0003841,GO:0003841,0.5221,0.5221,0.5221,0.5221,0.5221,5,0.5221,0.448,no
GNPAT_RABIT,G1SPE9,ProtTale,Eukaryota,679,"Dihydroxyacetonephosphate acyltransferase catalyzing the first step in the biosynthesis of plasmalogens, a subset of phospholipids that differ from other glycerolipids by having an alkyl chain attached through a vinyl ether linkage at the sn-1 position of the glycerol backbone, and which unique physical properties have an impact on various aspects of cell signaling and membrane biology.",Esterase that catalyzes the hydrolysis of glycerol-3-phosphate to phosphatidic acid and inorganic phosphate. Plays a role in plant development and in the regulation of abscisic acid (ABA) signaling.,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0004366; GO:0016287,GO:0016788,GO:0016788,GO:0016788,GO:0016788,GO:0016788,0.238,0.238,0.238,0.238,0.238,5,0.238,0.448,no
GNPAT_RABIT,G1SPE9,Protein2Text,Eukaryota,679,"Dihydroxyacetonephosphate acyltransferase catalyzing the first step in the biosynthesis of plasmalogens, a subset of phospholipids that differ from other glycerolipids by having an alkyl chain attached through a vinyl ether linkage at the sn-1 position of the glycerol backbone, and which unique physical properties have an impact on various aspects of cell signaling and membrane biology.","The molecular function of this protein is an acyltransferase. Specifically, it is a diacylglycerol acyltransferase, which catalyzes the final step in the synthesis of triglycerides, converting diacylglycerol to triacylglycerol.",Maybe,Maybe,Maybe,No,No,not-Yes,GO:0004366; GO:0016287,GO:0004144,GO:0004144,GO:0004144,GO:0004144,GO:0004144,0.6122,0.6122,0.6122,0.6122,0.6122,5,0.6122,0.448,no
GNPAT_RABIT,G1SPE9,Reference,Eukaryota,679,"Dihydroxyacetonephosphate acyltransferase catalyzing the first step in the biosynthesis of plasmalogens, a subset of phospholipids that differ from other glycerolipids by having an alkyl chain attached through a vinyl ether linkage at the sn-1 position of the glycerol backbone, and which unique physical properties have an impact on various aspects of cell signaling and membrane biology.","Dihydroxyacetonephosphate acyltransferase catalyzing the first step in the biosynthesis of plasmalogens, a subset of phospholipids that differ from other glycerolipids by having an alkyl chain attached through a vinyl ether linkage at the sn-1 position of the glycerol backbone, and which unique physical properties have an impact on various aspects of cell signaling and membrane biology.",,,,,,,GO:0004366; GO:0016287,GO:0004366,GO:0016746,GO:0016747,GO:0016746,GO:0046872; GO:0008654,0.869,0.6099,0.7101,0.6099,0.0544,5,0.5707,0.448,no
KAPB_ARTOA,G1X456,ESM2Text,Eukaryota,519,Functions downstream of adenylate cyclase to regulate trap- development for nematode capture.,Regulates the expression of activities associated with the cell cycle and the differentiation of microspores into microorganisms. Phosphorylates S-D-F-actin in a calcium-dependent manner. May play a role in the regulation of microtubule polymerization and anchorage.,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0005524; GO:0004691,GO:0004672; GO:0005509,,,GO:0004672,,0.5174,,,0.5397,,2,0.5285,0.7177,yes
KAPB_ARTOA,G1X456,Prot2Text,Eukaryota,519,Functions downstream of adenylate cyclase to regulate trap- development for nematode capture.,Phosphorylates a large number of substrates in the cytoplasm and the nucleus.,Maybe,Vague,Maybe,Vague,No,not-Yes,GO:0005524; GO:0004691,GO:0004672,GO:0004672,GO:0004672,GO:0004674,GO:0004672,0.5397,0.5397,0.5397,0.5748,0.5397,5,0.5467,0.7177,yes
KAPB_ARTOA,G1X456,ProtT3,Eukaryota,519,Functions downstream of adenylate cyclase to regulate trap- development for nematode capture.,Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. cAMP subfamily,Maybe,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0004691,GO:0004691; GO:0005524,GO:0004691; GO:0005524,GO:0004691; GO:0005524,GO:0004691; GO:0005524,GO:0004674; GO:0004691,1.0,1.0,1.0,1.0,0.7223,5,0.9445,0.7177,yes
KAPB_ARTOA,G1X456,ProtTale,Eukaryota,519,Functions downstream of adenylate cyclase to regulate trap- development for nematode capture.,"Serine/threonine-protein kinase involved in the regulation of cell growth, proliferation and survival. Phosphorylates and activates MAP2K1/MKK1 and MAP2K2/MKK2, leading to activation of the MAP kinase/ERK (MAPK/ERK) signaling pathway. Phosphorylates and activates MAP3K5/ASK1, leading to activation of the MAPK/ERK signaling pathway. Phosphorylates and activates MAP3K7/ASK2, leading to activation of the MAPK/ERK signaling pathway. Phosphorylates and activates MAP3K8/JNK1, leading to",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0004691,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,0.9176,0.9176,0.9176,0.5748,0.9176,5,0.849,0.7177,yes
KAPB_ARTOA,G1X456,Protein2Text,Eukaryota,519,Functions downstream of adenylate cyclase to regulate trap- development for nematode capture.,"The molecular function of this protein is a protein kinase, specifically a serine/threonine-protein kinase. It is involved in the phosphorylation of other proteins, which is a key regulatory mechanism in many cellular processes. The exact function of this protein is likely related to its role in the regulation of cellular processes, such as cell signaling, metabolism, or transcription. However, without more specific information, it is difficult to provide a more detailed description of its molecular function.",Maybe,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0005524; GO:0004691,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.5748,0.5748,0.5748,0.5748,0.5748,5,0.5748,0.7177,yes
KAPB_ARTOA,G1X456,Reference,Eukaryota,519,Functions downstream of adenylate cyclase to regulate trap- development for nematode capture.,Functions downstream of adenylate cyclase to regulate trap- development for nematode capture.,,,,,,,GO:0005524; GO:0004691,,,,,,,,,,,0,,0.7177,yes
ATC3_VERDV,G2X7W6,ESM2Text,Eukaryota,1376,Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylserine and small amounts of ethanolamine from the lumen to the cytosolic leaflet of the trans-Golgi network and cell membrane and ensures the maintenance of asymmetric distribution of phospholipids. Required for efficient vesicle transport during toxin secretion.,"Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP49 plays an important role in several nuclear export pathways including poly(A)+ RNA, tRNA, and pre-ribosome export, and cell proliferation.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016887; GO:0000287; GO:0140345; GO:0090555; GO:0070273; GO:0140346; GO:0090556,,,GO:0017056,GO:0017056,,,,0.1229,0.1229,,2,0.1229,0.5627,yes
ATC3_VERDV,G2X7W6,Prot2Text,Eukaryota,1376,Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylserine and small amounts of ethanolamine from the lumen to the cytosolic leaflet of the trans-Golgi network and cell membrane and ensures the maintenance of asymmetric distribution of phospholipids. Required for efficient vesicle transport during toxin secretion.,Could be involved in transport of phospholipids.,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0005524; GO:0016887; GO:0000287; GO:0140345; GO:0090555; GO:0070273; GO:0140346; GO:0090556,,,,,,,,,,,0,,0.5627,yes
ATC3_VERDV,G2X7W6,ProtT3,Eukaryota,1376,Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylserine and small amounts of ethanolamine from the lumen to the cytosolic leaflet of the trans-Golgi network and cell membrane and ensures the maintenance of asymmetric distribution of phospholipids. Required for efficient vesicle transport during toxin secretion.,The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses (By similarity). Membrane; Multi-pass membrane protein. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIA subfamily,No,No,No,No,No,not-Yes,GO:0005524; GO:0016887; GO:0000287; GO:0140345; GO:0090555; GO:0070273; GO:0140346; GO:0090556,GO:0005524; GO:0015078,GO:0008553,GO:0008553; GO:0005524,GO:0008553,GO:0008553,0.3482,0.1243,0.3567,0.1243,0.1243,5,0.2156,0.5627,yes
ATC3_VERDV,G2X7W6,ProtTale,Eukaryota,1376,Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylserine and small amounts of ethanolamine from the lumen to the cytosolic leaflet of the trans-Golgi network and cell membrane and ensures the maintenance of asymmetric distribution of phospholipids. Required for efficient vesicle transport during toxin secretion.,"Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids, phosphatidylserines (PS) and phosphatidylethanolamines (PE), from the outer to the inner leaflet of the plasma membrane. May be directly involved in the maintenance of the asymmetric distribution of phospholipids in the plasma membrane.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0000287; GO:0140345; GO:0090555; GO:0070273; GO:0140346; GO:0090556,GO:0004012; GO:0005524,GO:0004012; GO:0005524,GO:0004012; GO:0005524,GO:0016887; GO:0015442,GO:0004012; GO:0005524,0.633,0.633,0.633,0.3208,0.633,5,0.5706,0.5627,yes
ATC3_VERDV,G2X7W6,Protein2Text,Eukaryota,1376,Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylserine and small amounts of ethanolamine from the lumen to the cytosolic leaflet of the trans-Golgi network and cell membrane and ensures the maintenance of asymmetric distribution of phospholipids. Required for efficient vesicle transport during toxin secretion.,"The molecular function of this protein is that it is a phosphatidylinositol 4,5-bisphosphate 3-kinase, which is a type of enzyme that catalyzes the phosphorylation of phosphatidylinositol 4,5-bisphosphate (PIP2) to produce phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 is a key signaling molecule that plays a crucial role in various cellular processes, including cell growth, survival, and migration.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016887; GO:0000287; GO:0140345; GO:0090555; GO:0070273; GO:0140346; GO:0090556,GO:0035004,GO:0046934,GO:0046934,GO:0046934,GO:0046934,0.0,0.0708,0.0708,0.0708,0.0708,5,0.0566,0.5627,yes
ATC3_VERDV,G2X7W6,Reference,Eukaryota,1376,Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylserine and small amounts of ethanolamine from the lumen to the cytosolic leaflet of the trans-Golgi network and cell membrane and ensures the maintenance of asymmetric distribution of phospholipids. Required for efficient vesicle transport during toxin secretion.,Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylserine and small amounts of ethanolamine from the lumen to the cytosolic leaflet of the trans-Golgi network and cell membrane and ensures the maintenance of asymmetric distribution of phospholipids. Required for efficient vesicle transport during toxin secretion.,,,,,,,GO:0005524; GO:0016887; GO:0000287; GO:0140345; GO:0090555; GO:0070273; GO:0140346; GO:0090556,GO:0004012; GO:0005524,GO:0034040; GO:0005524,GO:0004012; GO:0005524,GO:0005524; GO:0015441; GO:0004012,GO:0005524; GO:0015441; GO:0004622,0.633,0.4405,0.633,0.5925,0.3466,5,0.5291,0.5627,yes
FKS1_CORMM,G3J3K0,ESM2Text,Eukaryota,1946,"Catalytic subunit of the 1,3-beta-glucan synthase (GS). Synthesizes 1,3-beta-glucan, a major structural component of the fungal cell wall. Involved in cell wall synthesis, maintenance and remodeling.","Involved in the regulation of peroxisome number, size and distribution.",No,No,No,No,No,not-Yes,GO:0003843,,,,,,,,,,,0,,0.3726,no
FKS1_CORMM,G3J3K0,Prot2Text,Eukaryota,1946,"Catalytic subunit of the 1,3-beta-glucan synthase (GS). Synthesizes 1,3-beta-glucan, a major structural component of the fungal cell wall. Involved in cell wall synthesis, maintenance and remodeling.","Part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. The function of lcsT within the leucinostatins biosynthesis has not been identified yet (Probable).",No,No,No,No,No,not-Yes,GO:0003843,,,,,,,,,,,0,,0.3726,no
FKS1_CORMM,G3J3K0,ProtT3,Eukaryota,1946,"Catalytic subunit of the 1,3-beta-glucan synthase (GS). Synthesizes 1,3-beta-glucan, a major structural component of the fungal cell wall. Involved in cell wall synthesis, maintenance and remodeling.",Involved in phosphatidylinositol-4-phosphate (PtdIns-4-P) transport from the endoplasmic reticulum (ER) to the plasma membrane (PM) (By similarity). Binds phosphatidylinositol 4-phosphate (PtdIns-4-P) (By similarity). Endoplasmic reticulum membrane; Multi-pass membrane protein. Belongs to the PI(4)K family,No,No,No,No,No,not-Yes,GO:0003843,GO:0004430,GO:0004430,GO:0004430; GO:0005524,GO:0004430,GO:0004430,0.1958,0.1958,0.1458,0.1958,0.1958,5,0.1858,0.3726,no
FKS1_CORMM,G3J3K0,ProtTale,Eukaryota,1946,"Catalytic subunit of the 1,3-beta-glucan synthase (GS). Synthesizes 1,3-beta-glucan, a major structural component of the fungal cell wall. Involved in cell wall synthesis, maintenance and remodeling.","Involved in the synthesis of callose (1, 3, 1[beta]-1, 6-glucan) rings which are the major components of the plant cell wall. Required for normal pollen tube growth.",Yes,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0003843,GO:0003843,GO:0003843,GO:0003843,GO:0016757,GO:0003843,1.0,1.0,1.0,0.5541,1.0,5,0.9108,0.3726,no
FKS1_CORMM,G3J3K0,Protein2Text,Eukaryota,1946,"Catalytic subunit of the 1,3-beta-glucan synthase (GS). Synthesizes 1,3-beta-glucan, a major structural component of the fungal cell wall. Involved in cell wall synthesis, maintenance and remodeling.","This protein is involved in the molecular function of catalyzing the hydrolysis of the phosphate ester bond in RNA, specifically in the 5'-to-3' direction.",No,No,No,No,No,not-Yes,GO:0003843,GO:0004540,GO:0004540,GO:0004540,GO:0004540,GO:0004540,0.1631,0.1631,0.1631,0.1631,0.1631,5,0.1631,0.3726,no
FKS1_CORMM,G3J3K0,Reference,Eukaryota,1946,"Catalytic subunit of the 1,3-beta-glucan synthase (GS). Synthesizes 1,3-beta-glucan, a major structural component of the fungal cell wall. Involved in cell wall synthesis, maintenance and remodeling.","Catalytic subunit of the 1,3-beta-glucan synthase (GS). Synthesizes 1,3-beta-glucan, a major structural component of the fungal cell wall. Involved in cell wall synthesis, maintenance and remodeling.",,,,,,,GO:0003843,GO:0003843,GO:0003843,GO:0003843,GO:0003843,GO:0003843,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3726,no
RPB1_BOVIN,G3MZY8,ESM2Text,Eukaryota,1970,"Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates. Pol II-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol II pre-initiation complex (PIC) is recruited to DNA promoters, with focused-type promoters containing either the initiator (Inr) element, or the TATA-box found in cell-type specific genes and dispersed-type promoters that often contain hypomethylated CpG islands usually found in housekeeping genes. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA. Forms Pol II active center together with the second largest subunit POLR2B/RPB2. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg(2+)-coordinating DxDGD motif, and POLR2B/RPB2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. The reversible pyrophosphorolysis can occur at high pyrophosphate concentrations. Can proofread the nascent RNA transcript by means of a 3' -> 5' exonuclease activity. If a ribonucleotide is mis-incorporated, backtracks along the template DNA and cleaves the phosphodiester bond releasing the mis-incorporated 5'- ribonucleotide. Through its unique C- terminal domain (CTD, 52 heptapeptide tandem repeats) serves as a platform for assembly of factors that regulate transcription initiation, elongation and termination. CTD phosphorylation on Ser-5 mediates Pol II promoter escape, whereas phosphorylation on Ser-2 is required for Pol II pause release during transcription elongation and further pre-mRNA processing. Additionally, the regulation of gene expression levels depends on the balance between methylation and acetylation levels of the CTD-lysines. Initiation or early elongation steps of transcription of growth-factor-induced immediate early genes are regulated by the acetylation status of the CTD. Methylation and dimethylation have a repressive effect on target genes expression. Cooperates with mRNA splicing machinery in co-transcriptional 5'-end capping and co-transcriptional splicing of pre-mRNA.","DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest component of RNA polymerases IV and V which mediate short-interfering RNAs (siRNA) accumulation and subsequent RNA-directed DNA methylation-dependent (RdDM) transcriptional gene silencing (TGS) of endogenous repeated sequences, including transposable elements. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol IV and Pol V are part of a transcription termination checkpoint that is part of a general stress response system.",Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0001046; GO:0003899; GO:0071667; GO:0016787; GO:0000287; GO:0003968; GO:0008270,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.4162,0.4162,0.4162,0.4162,0.4162,5,0.4162,0.5044,no
RPB1_BOVIN,G3MZY8,Prot2Text,Eukaryota,1970,"Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates. Pol II-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol II pre-initiation complex (PIC) is recruited to DNA promoters, with focused-type promoters containing either the initiator (Inr) element, or the TATA-box found in cell-type specific genes and dispersed-type promoters that often contain hypomethylated CpG islands usually found in housekeeping genes. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA. Forms Pol II active center together with the second largest subunit POLR2B/RPB2. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg(2+)-coordinating DxDGD motif, and POLR2B/RPB2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. The reversible pyrophosphorolysis can occur at high pyrophosphate concentrations. Can proofread the nascent RNA transcript by means of a 3' -> 5' exonuclease activity. If a ribonucleotide is mis-incorporated, backtracks along the template DNA and cleaves the phosphodiester bond releasing the mis-incorporated 5'- ribonucleotide. Through its unique C- terminal domain (CTD, 52 heptapeptide tandem repeats) serves as a platform for assembly of factors that regulate transcription initiation, elongation and termination. CTD phosphorylation on Ser-5 mediates Pol II promoter escape, whereas phosphorylation on Ser-2 is required for Pol II pause release during transcription elongation and further pre-mRNA processing. Additionally, the regulation of gene expression levels depends on the balance between methylation and acetylation levels of the CTD-lysines. Initiation or early elongation steps of transcription of growth-factor-induced immediate early genes are regulated by the acetylation status of the CTD. Methylation and dimethylation have a repressive effect on target genes expression. Cooperates with mRNA splicing machinery in co-transcriptional 5'-end capping and co-transcriptional splicing of pre-mRNA.",DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. A single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from NRPC1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0001046; GO:0003899; GO:0071667; GO:0016787; GO:0000287; GO:0003968; GO:0008270,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.4162,0.4162,0.4162,0.4162,0.4162,5,0.4162,0.5044,no
RPB1_BOVIN,G3MZY8,ProtT3,Eukaryota,1970,"Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates. Pol II-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol II pre-initiation complex (PIC) is recruited to DNA promoters, with focused-type promoters containing either the initiator (Inr) element, or the TATA-box found in cell-type specific genes and dispersed-type promoters that often contain hypomethylated CpG islands usually found in housekeeping genes. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA. Forms Pol II active center together with the second largest subunit POLR2B/RPB2. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg(2+)-coordinating DxDGD motif, and POLR2B/RPB2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. The reversible pyrophosphorolysis can occur at high pyrophosphate concentrations. Can proofread the nascent RNA transcript by means of a 3' -> 5' exonuclease activity. If a ribonucleotide is mis-incorporated, backtracks along the template DNA and cleaves the phosphodiester bond releasing the mis-incorporated 5'- ribonucleotide. Through its unique C- terminal domain (CTD, 52 heptapeptide tandem repeats) serves as a platform for assembly of factors that regulate transcription initiation, elongation and termination. CTD phosphorylation on Ser-5 mediates Pol II promoter escape, whereas phosphorylation on Ser-2 is required for Pol II pause release during transcription elongation and further pre-mRNA processing. Additionally, the regulation of gene expression levels depends on the balance between methylation and acetylation levels of the CTD-lysines. Initiation or early elongation steps of transcription of growth-factor-induced immediate early genes are regulated by the acetylation status of the CTD. Methylation and dimethylation have a repressive effect on target genes expression. Cooperates with mRNA splicing machinery in co-transcriptional 5'-end capping and co-transcriptional splicing of pre-mRNA.","DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non- coding RNAs, and a small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, RPB6 is part of the lower jaw surrounding the central large cleft and thought to grab the incoming DNA template (By similarity",Maybe,Yes,Yes,Maybe,Yes,Yes,GO:0001046; GO:0003899; GO:0071667; GO:0016787; GO:0000287; GO:0003968; GO:0008270,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.4162,0.4162,0.4162,0.4162,0.4162,5,0.4162,0.5044,no
RPB1_BOVIN,G3MZY8,ProtTale,Eukaryota,1970,"Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates. Pol II-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol II pre-initiation complex (PIC) is recruited to DNA promoters, with focused-type promoters containing either the initiator (Inr) element, or the TATA-box found in cell-type specific genes and dispersed-type promoters that often contain hypomethylated CpG islands usually found in housekeeping genes. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA. Forms Pol II active center together with the second largest subunit POLR2B/RPB2. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg(2+)-coordinating DxDGD motif, and POLR2B/RPB2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. The reversible pyrophosphorolysis can occur at high pyrophosphate concentrations. Can proofread the nascent RNA transcript by means of a 3' -> 5' exonuclease activity. If a ribonucleotide is mis-incorporated, backtracks along the template DNA and cleaves the phosphodiester bond releasing the mis-incorporated 5'- ribonucleotide. Through its unique C- terminal domain (CTD, 52 heptapeptide tandem repeats) serves as a platform for assembly of factors that regulate transcription initiation, elongation and termination. CTD phosphorylation on Ser-5 mediates Pol II promoter escape, whereas phosphorylation on Ser-2 is required for Pol II pause release during transcription elongation and further pre-mRNA processing. Additionally, the regulation of gene expression levels depends on the balance between methylation and acetylation levels of the CTD-lysines. Initiation or early elongation steps of transcription of growth-factor-induced immediate early genes are regulated by the acetylation status of the CTD. Methylation and dimethylation have a repressive effect on target genes expression. Cooperates with mRNA splicing machinery in co-transcriptional 5'-end capping and co-transcriptional splicing of pre-mRNA.","DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0001046; GO:0003899; GO:0071667; GO:0016787; GO:0000287; GO:0003968; GO:0008270,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.4162,0.4162,0.4162,0.4162,0.4162,5,0.4162,0.5044,no
RPB1_BOVIN,G3MZY8,Protein2Text,Eukaryota,1970,"Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates. Pol II-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol II pre-initiation complex (PIC) is recruited to DNA promoters, with focused-type promoters containing either the initiator (Inr) element, or the TATA-box found in cell-type specific genes and dispersed-type promoters that often contain hypomethylated CpG islands usually found in housekeeping genes. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA. Forms Pol II active center together with the second largest subunit POLR2B/RPB2. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg(2+)-coordinating DxDGD motif, and POLR2B/RPB2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. The reversible pyrophosphorolysis can occur at high pyrophosphate concentrations. Can proofread the nascent RNA transcript by means of a 3' -> 5' exonuclease activity. If a ribonucleotide is mis-incorporated, backtracks along the template DNA and cleaves the phosphodiester bond releasing the mis-incorporated 5'- ribonucleotide. Through its unique C- terminal domain (CTD, 52 heptapeptide tandem repeats) serves as a platform for assembly of factors that regulate transcription initiation, elongation and termination. CTD phosphorylation on Ser-5 mediates Pol II promoter escape, whereas phosphorylation on Ser-2 is required for Pol II pause release during transcription elongation and further pre-mRNA processing. Additionally, the regulation of gene expression levels depends on the balance between methylation and acetylation levels of the CTD-lysines. Initiation or early elongation steps of transcription of growth-factor-induced immediate early genes are regulated by the acetylation status of the CTD. Methylation and dimethylation have a repressive effect on target genes expression. Cooperates with mRNA splicing machinery in co-transcriptional 5'-end capping and co-transcriptional splicing of pre-mRNA.","The molecular function of this protein is not specified in the provided text. However, based on its name, it is likely to be involved in DNA replication or repair, as the name suggests it is a component of the DNA polymerase complex. Specifically, it is likely to be a subunit of the DNA polymerase enzyme, which is responsible for synthesizing new DNA strands during replication or repair. This protein may have a role in adding nucleotides to the growing DNA chain, or in stabilizing the polymerase complex during DNA synthesis. However, without more specific information, it is difficult to determine the exact molecular function of this protein.",No,No,No,Vague,No,not-Yes,GO:0001046; GO:0003899; GO:0071667; GO:0016787; GO:0000287; GO:0003968; GO:0008270,,,,,,,,,,,0,,0.5044,no
RPB1_BOVIN,G3MZY8,Reference,Eukaryota,1970,"Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates. Pol II-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol II pre-initiation complex (PIC) is recruited to DNA promoters, with focused-type promoters containing either the initiator (Inr) element, or the TATA-box found in cell-type specific genes and dispersed-type promoters that often contain hypomethylated CpG islands usually found in housekeeping genes. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA. Forms Pol II active center together with the second largest subunit POLR2B/RPB2. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg(2+)-coordinating DxDGD motif, and POLR2B/RPB2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. The reversible pyrophosphorolysis can occur at high pyrophosphate concentrations. Can proofread the nascent RNA transcript by means of a 3' -> 5' exonuclease activity. If a ribonucleotide is mis-incorporated, backtracks along the template DNA and cleaves the phosphodiester bond releasing the mis-incorporated 5'- ribonucleotide. Through its unique C- terminal domain (CTD, 52 heptapeptide tandem repeats) serves as a platform for assembly of factors that regulate transcription initiation, elongation and termination. CTD phosphorylation on Ser-5 mediates Pol II promoter escape, whereas phosphorylation on Ser-2 is required for Pol II pause release during transcription elongation and further pre-mRNA processing. Additionally, the regulation of gene expression levels depends on the balance between methylation and acetylation levels of the CTD-lysines. Initiation or early elongation steps of transcription of growth-factor-induced immediate early genes are regulated by the acetylation status of the CTD. Methylation and dimethylation have a repressive effect on target genes expression. Cooperates with mRNA splicing machinery in co-transcriptional 5'-end capping and co-transcriptional splicing of pre-mRNA.","Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates. Pol II-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol II pre-initiation complex (PIC) is recruited to DNA promoters, with focused-type promoters containing either the initiator (Inr) element, or the TATA-box found in cell-type specific genes and dispersed-type promoters that often contain hypomethylated CpG islands usually found in housekeeping genes. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA. Forms Pol II active center together with the second largest subunit POLR2B/RPB2. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg(2+)-coordinating DxDGD motif, and POLR2B/RPB2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. The reversible pyrophosphorolysis can occur at high pyrophosphate concentrations. Can proofread the nascent RNA transcript by means of a 3' -> 5' exonuclease activity. If a ribonucleotide is mis-incorporated, backtracks along the template DNA and cleaves the phosphodiester bond releasing the mis-incorporated 5'- ribonucleotide. Through its unique C- terminal domain (CTD, 52 heptapeptide tandem repeats) serves as a platform for assembly of factors that regulate transcription initiation, elongation and termination. CTD phosphorylation on Ser-5 mediates Pol II promoter escape, whereas phosphorylation on Ser-2 is required for Pol II pause release during transcription elongation and further pre-mRNA processing. Additionally, the regulation of gene expression levels depends on the balance between methylation and acetylation levels of the CTD-lysines. Initiation or early elongation steps of transcription of growth-factor-induced immediate early genes are regulated by the acetylation status of the CTD. Methylation and dimethylation have a repressive effect on target genes expression. Cooperates with mRNA splicing machinery in co-transcriptional 5'-end capping and co-transcriptional splicing of pre-mRNA.",,,,,,,GO:0001046; GO:0003899; GO:0071667; GO:0016787; GO:0000287; GO:0003968; GO:0008270,GO:0003899; GO:0003677,GO:0003899,GO:0003899; GO:0003677,GO:0003899; GO:0003723,GO:0003899; GO:0003723,0.6006,0.4162,0.6006,0.5826,0.5826,5,0.5565,0.5044,no
KAD9_MOUSE,G3UYQ4,ESM2Text,Eukaryota,1894,"Broad-specificity nucleoside phosphate kinase involved in cellular nucleotide homeostasis by catalyzing nucleoside-phosphate interconversions. Similar to other adenylate kinases, preferentially catalyzes the phosphorylation of the nucleoside monophosphate AMP with ATP as phosphate donor to produce ADP. In vitro, can also catalyze the phosphorylation of CMP, dAMP and dCMP and use GTP as an alternate phosphate donor. Moreover, exhibits a diphosphate kinase activity, producing ATP, CTP, GTP, UTP, TTP, dATP, dCTP and dGTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate donors. For this activity shows the following substrate preference CDP > UDP > ADP > TDP.","Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has both nucleoside monophosphate and diphosphate kinase activities. Catalyzes the phosphorylation of AMP, dAMP, CMP, and dCMP with ATP as phosphate donor and of CMP with GTP as phosphate donor. Also catalyzes the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP, and TTP from the corresponding diphosphate substrates.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0004550; GO:0050145; GO:0033862,GO:0004017; GO:0004550,GO:0004017; GO:0004550,GO:0004017; GO:0004550,GO:0004550,GO:0004550,0.7764,0.7764,0.7764,0.7163,0.7163,5,0.7524,0.6389,yes
KAD9_MOUSE,G3UYQ4,Prot2Text,Eukaryota,1894,"Broad-specificity nucleoside phosphate kinase involved in cellular nucleotide homeostasis by catalyzing nucleoside-phosphate interconversions. Similar to other adenylate kinases, preferentially catalyzes the phosphorylation of the nucleoside monophosphate AMP with ATP as phosphate donor to produce ADP. In vitro, can also catalyze the phosphorylation of CMP, dAMP and dCMP and use GTP as an alternate phosphate donor. Moreover, exhibits a diphosphate kinase activity, producing ATP, CTP, GTP, UTP, TTP, dATP, dCTP and dGTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate donors. For this activity shows the following substrate preference CDP > UDP > ADP > TDP.",Required for correct axoneme development in spermatozoa.,Vague,Vague,Vague,No,No,not-Yes,GO:0005524; GO:0004550; GO:0050145; GO:0033862,,,,,,,,,,,0,,0.6389,yes
KAD9_MOUSE,G3UYQ4,ProtT3,Eukaryota,1894,"Broad-specificity nucleoside phosphate kinase involved in cellular nucleotide homeostasis by catalyzing nucleoside-phosphate interconversions. Similar to other adenylate kinases, preferentially catalyzes the phosphorylation of the nucleoside monophosphate AMP with ATP as phosphate donor to produce ADP. In vitro, can also catalyze the phosphorylation of CMP, dAMP and dCMP and use GTP as an alternate phosphate donor. Moreover, exhibits a diphosphate kinase activity, producing ATP, CTP, GTP, UTP, TTP, dATP, dCTP and dGTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate donors. For this activity shows the following substrate preference CDP > UDP > ADP > TDP.","Nucleoside diphosphate kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and diphosphates. Cytoplasm, cytoskeleton, cilium axoneme. Belongs to the adenylate kinase family",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004550; GO:0050145; GO:0033862,GO:0004550,GO:0004550,GO:0004550; GO:0005524,GO:0004550; GO:0005524,GO:0004550,0.7163,0.7163,0.9219,0.9219,0.7163,5,0.7985,0.6389,yes
KAD9_MOUSE,G3UYQ4,ProtTale,Eukaryota,1894,"Broad-specificity nucleoside phosphate kinase involved in cellular nucleotide homeostasis by catalyzing nucleoside-phosphate interconversions. Similar to other adenylate kinases, preferentially catalyzes the phosphorylation of the nucleoside monophosphate AMP with ATP as phosphate donor to produce ADP. In vitro, can also catalyze the phosphorylation of CMP, dAMP and dCMP and use GTP as an alternate phosphate donor. Moreover, exhibits a diphosphate kinase activity, producing ATP, CTP, GTP, UTP, TTP, dATP, dCTP and dGTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate donors. For this activity shows the following substrate preference CDP > UDP > ADP > TDP.","Serine/threonine-protein phosphatase that dephosphorylates PP1 catalytic subunits (PPP1R1B, PPP1R1C, PPP1R1D, PPP1R1F, PPP1R1G, PPP1R1I, PPP1R1J, PPP1R1K, PPP1R1M, PPP1R1N, PPP1R1S, PPP1R1T, PPP1R2, PPP1R3, PPP1R4, PPP1R5, PPP1R6, PPP1R7, PPP1R9, PPP1",No,No,No,No,No,not-Yes,GO:0005524; GO:0004550; GO:0050145; GO:0033862,GO:0004722,GO:0004722,GO:0004722,GO:0004721,GO:0004722,0.1361,0.1361,0.1361,0.1544,0.1361,5,0.1398,0.6389,yes
KAD9_MOUSE,G3UYQ4,Protein2Text,Eukaryota,1894,"Broad-specificity nucleoside phosphate kinase involved in cellular nucleotide homeostasis by catalyzing nucleoside-phosphate interconversions. Similar to other adenylate kinases, preferentially catalyzes the phosphorylation of the nucleoside monophosphate AMP with ATP as phosphate donor to produce ADP. In vitro, can also catalyze the phosphorylation of CMP, dAMP and dCMP and use GTP as an alternate phosphate donor. Moreover, exhibits a diphosphate kinase activity, producing ATP, CTP, GTP, UTP, TTP, dATP, dCTP and dGTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate donors. For this activity shows the following substrate preference CDP > UDP > ADP > TDP.","The molecular function of this protein is not explicitly stated in the provided information. However, based on its name, it is likely that it plays a role in energy metabolism, specifically in the regulation of glycolysis and glycogenolysis. This protein is probably a kinase, given the suffix ""-kinase"" in its name, which suggests that it has kinase activity.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0004550; GO:0050145; GO:0033862,,,,,,,,,,,0,,0.6389,yes
KAD9_MOUSE,G3UYQ4,Reference,Eukaryota,1894,"Broad-specificity nucleoside phosphate kinase involved in cellular nucleotide homeostasis by catalyzing nucleoside-phosphate interconversions. Similar to other adenylate kinases, preferentially catalyzes the phosphorylation of the nucleoside monophosphate AMP with ATP as phosphate donor to produce ADP. In vitro, can also catalyze the phosphorylation of CMP, dAMP and dCMP and use GTP as an alternate phosphate donor. Moreover, exhibits a diphosphate kinase activity, producing ATP, CTP, GTP, UTP, TTP, dATP, dCTP and dGTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate donors. For this activity shows the following substrate preference CDP > UDP > ADP > TDP.","Broad-specificity nucleoside phosphate kinase involved in cellular nucleotide homeostasis by catalyzing nucleoside-phosphate interconversions. Similar to other adenylate kinases, preferentially catalyzes the phosphorylation of the nucleoside monophosphate AMP with ATP as phosphate donor to produce ADP. In vitro, can also catalyze the phosphorylation of CMP, dAMP and dCMP and use GTP as an alternate phosphate donor. Moreover, exhibits a diphosphate kinase activity, producing ATP, CTP, GTP, UTP, TTP, dATP, dCTP and dGTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate donors. For this activity shows the following substrate preference CDP > UDP > ADP > TDP.",,,,,,,GO:0005524; GO:0004550; GO:0050145; GO:0033862,GO:0004017; GO:0004550; GO:0005524,GO:0004017; GO:0005524,GO:0004017; GO:0005524,GO:0004017; GO:0004550; GO:0005524,GO:0004017; GO:0005524,0.9441,0.8892,0.8892,0.9441,0.8892,5,0.9112,0.6389,yes
TRI55_MOUSE,G3X8Y1,ESM2Text,Eukaryota,545,"E3 ubiquitin ligase that plays an important role in regulating cardiac development and contractility, muscle growth, metabolism, and fiber-type differentiation. Acts as a critical factor that regulates cardiomyocyte size during development in concert with TRIM63 by regulating E2F1-mediated gene expression. Plays a role in apoptosis induction in cardiomyocytes by promoting ubiquitination of the DUSP1 phosphatase. Promotes non-canonical NF-kappa-B signaling and B-cell-mediated immune responses by mediating NFKB2 'Lys-48'-linked ubiquitination and processing. In turn, NFKB2 is further processed by valosin-containing protein/VCP, an ATPase that mediates ubiquitin-dependent protein degradation by the proteasome. May play a role in preventing macrophages from producing inflammatory factors and migrating by downregulating the level of nuclear NF-kappa-B subunit RELA. Modifies also PPARG via polyubiquitination and accelerates PPARG proteasomal degradation to inhibit its activity.",May regulate gene expression and protein turnover in muscle cells.,Vague,Vague,Vague,Vague,No,not-Yes,GO:0042802; GO:0030674; GO:0061630; GO:0008270,,,,,,,,,,,0,,0.8826,yes
TRI55_MOUSE,G3X8Y1,Prot2Text,Eukaryota,545,"E3 ubiquitin ligase that plays an important role in regulating cardiac development and contractility, muscle growth, metabolism, and fiber-type differentiation. Acts as a critical factor that regulates cardiomyocyte size during development in concert with TRIM63 by regulating E2F1-mediated gene expression. Plays a role in apoptosis induction in cardiomyocytes by promoting ubiquitination of the DUSP1 phosphatase. Promotes non-canonical NF-kappa-B signaling and B-cell-mediated immune responses by mediating NFKB2 'Lys-48'-linked ubiquitination and processing. In turn, NFKB2 is further processed by valosin-containing protein/VCP, an ATPase that mediates ubiquitin-dependent protein degradation by the proteasome. May play a role in preventing macrophages from producing inflammatory factors and migrating by downregulating the level of nuclear NF-kappa-B subunit RELA. Modifies also PPARG via polyubiquitination and accelerates PPARG proteasomal degradation to inhibit its activity.",May regulate gene expression and protein turnover in muscle cells.,Vague,Vague,Vague,Vague,No,not-Yes,GO:0042802; GO:0030674; GO:0061630; GO:0008270,,,,,,,,,,,0,,0.8826,yes
TRI55_MOUSE,G3X8Y1,ProtT3,Eukaryota,545,"E3 ubiquitin ligase that plays an important role in regulating cardiac development and contractility, muscle growth, metabolism, and fiber-type differentiation. Acts as a critical factor that regulates cardiomyocyte size during development in concert with TRIM63 by regulating E2F1-mediated gene expression. Plays a role in apoptosis induction in cardiomyocytes by promoting ubiquitination of the DUSP1 phosphatase. Promotes non-canonical NF-kappa-B signaling and B-cell-mediated immune responses by mediating NFKB2 'Lys-48'-linked ubiquitination and processing. In turn, NFKB2 is further processed by valosin-containing protein/VCP, an ATPase that mediates ubiquitin-dependent protein degradation by the proteasome. May play a role in preventing macrophages from producing inflammatory factors and migrating by downregulating the level of nuclear NF-kappa-B subunit RELA. Modifies also PPARG via polyubiquitination and accelerates PPARG proteasomal degradation to inhibit its activity.","May play a role in myofiber differentiation and/or muscle regeneration. Cytoplasm Cytoplasm, myofibril, sarcomere, Z line Cytoplasm, myofibril, sarcomere, A band Cytoplasm, myofibril, sarcomere, M line Cytoplasm, myofibril, sarcomere, I band Cytoplasm, myofibril, sarcomere, Z line Cytoplasm, myofibril, sarcomere, M line Cytoplasm, myofibril, sarcomere, I band Cytoplasm, myofibril, sarcomere, Z line Cytoplasm, myofibril, sarcomere, A band Cytoplasm, my",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0042802; GO:0030674; GO:0061630; GO:0008270,,,,,,,,,,,0,,0.8826,yes
TRI55_MOUSE,G3X8Y1,ProtTale,Eukaryota,545,"E3 ubiquitin ligase that plays an important role in regulating cardiac development and contractility, muscle growth, metabolism, and fiber-type differentiation. Acts as a critical factor that regulates cardiomyocyte size during development in concert with TRIM63 by regulating E2F1-mediated gene expression. Plays a role in apoptosis induction in cardiomyocytes by promoting ubiquitination of the DUSP1 phosphatase. Promotes non-canonical NF-kappa-B signaling and B-cell-mediated immune responses by mediating NFKB2 'Lys-48'-linked ubiquitination and processing. In turn, NFKB2 is further processed by valosin-containing protein/VCP, an ATPase that mediates ubiquitin-dependent protein degradation by the proteasome. May play a role in preventing macrophages from producing inflammatory factors and migrating by downregulating the level of nuclear NF-kappa-B subunit RELA. Modifies also PPARG via polyubiquitination and accelerates PPARG proteasomal degradation to inhibit its activity.",E3 ubiquitin-protein ligase that plays a role in the regulation of innate immunity and inflammatory response. Acts as a positive regulator of the NLRP3 inflammasome by mediating 'Lys-48'-linked polyubiquitination and proteasomal degradation of NLRC4. Acts as a negative regulator of the cGAS-STING pathway by promoting 'Lys- 63'-linked polyubiquitination and degradation of STING1. Acts as a positive regulator of NF-kappa-B signaling by mediating 'Lys-48'-linked polyubiquitination and degradation of RELA. Acts as a negative regulator,Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0042802; GO:0030674; GO:0061630; GO:0008270,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.4538,0.4538,0.4538,0.4538,0.4538,5,0.4538,0.8826,yes
TRI55_MOUSE,G3X8Y1,Protein2Text,Eukaryota,545,"E3 ubiquitin ligase that plays an important role in regulating cardiac development and contractility, muscle growth, metabolism, and fiber-type differentiation. Acts as a critical factor that regulates cardiomyocyte size during development in concert with TRIM63 by regulating E2F1-mediated gene expression. Plays a role in apoptosis induction in cardiomyocytes by promoting ubiquitination of the DUSP1 phosphatase. Promotes non-canonical NF-kappa-B signaling and B-cell-mediated immune responses by mediating NFKB2 'Lys-48'-linked ubiquitination and processing. In turn, NFKB2 is further processed by valosin-containing protein/VCP, an ATPase that mediates ubiquitin-dependent protein degradation by the proteasome. May play a role in preventing macrophages from producing inflammatory factors and migrating by downregulating the level of nuclear NF-kappa-B subunit RELA. Modifies also PPARG via polyubiquitination and accelerates PPARG proteasomal degradation to inhibit its activity.","The molecular function of this protein is not explicitly stated in the provided information. However, based on the fact that it is involved in the regulation of cell processes and is related to the ubiquitin-proteasome system, it is likely that this protein plays a role in protein degradation or modification. 

If you have any more information or context about this protein, I may be able to provide a more specific answer.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0042802; GO:0030674; GO:0061630; GO:0008270,,,,,,,,,,,0,,0.8826,yes
TRI55_MOUSE,G3X8Y1,Reference,Eukaryota,545,"E3 ubiquitin ligase that plays an important role in regulating cardiac development and contractility, muscle growth, metabolism, and fiber-type differentiation. Acts as a critical factor that regulates cardiomyocyte size during development in concert with TRIM63 by regulating E2F1-mediated gene expression. Plays a role in apoptosis induction in cardiomyocytes by promoting ubiquitination of the DUSP1 phosphatase. Promotes non-canonical NF-kappa-B signaling and B-cell-mediated immune responses by mediating NFKB2 'Lys-48'-linked ubiquitination and processing. In turn, NFKB2 is further processed by valosin-containing protein/VCP, an ATPase that mediates ubiquitin-dependent protein degradation by the proteasome. May play a role in preventing macrophages from producing inflammatory factors and migrating by downregulating the level of nuclear NF-kappa-B subunit RELA. Modifies also PPARG via polyubiquitination and accelerates PPARG proteasomal degradation to inhibit its activity.","E3 ubiquitin ligase that plays an important role in regulating cardiac development and contractility, muscle growth, metabolism, and fiber-type differentiation. Acts as a critical factor that regulates cardiomyocyte size during development in concert with TRIM63 by regulating E2F1-mediated gene expression. Plays a role in apoptosis induction in cardiomyocytes by promoting ubiquitination of the DUSP1 phosphatase. Promotes non-canonical NF-kappa-B signaling and B-cell-mediated immune responses by mediating NFKB2 'Lys-48'-linked ubiquitination and processing. In turn, NFKB2 is further processed by valosin-containing protein/VCP, an ATPase that mediates ubiquitin-dependent protein degradation by the proteasome. May play a role in preventing macrophages from producing inflammatory factors and migrating by downregulating the level of nuclear NF-kappa-B subunit RELA. Modifies also PPARG via polyubiquitination and accelerates PPARG proteasomal degradation to inhibit its activity.",,,,,,,GO:0042802; GO:0030674; GO:0061630; GO:0008270,GO:0061630,GO:0004842,GO:0004842,GO:0004842; GO:0061630,GO:0004842,0.4538,0.398,0.398,0.5265,0.398,5,0.4349,0.8826,yes
WZY_PSEAE,G3XCW3,ESM2Text,Bacteria,438,"Polymerase involved in the biosynthesis of the B-band lipopolysaccharide (LPS). Catalyzes the polymerization of the O-antigen repeat units on the periplasmic face of the inner membrane, leading to the formation of the lipid-linked O-antigen molecule.",Required for the biosynthesis of type 1 capsular polysaccharide.,Maybe,Maybe,No,Maybe,No,not-Yes,GO:0016757; GO:0008755,,,,,,,,,,,0,,0.5717,yes
WZY_PSEAE,G3XCW3,Prot2Text,Bacteria,438,"Polymerase involved in the biosynthesis of the B-band lipopolysaccharide (LPS). Catalyzes the polymerization of the O-antigen repeat units on the periplasmic face of the inner membrane, leading to the formation of the lipid-linked O-antigen molecule.","May link the O-antigen tetrasaccharide units into long chains, giving rise to typical smooth LPS.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0016757; GO:0008755,GO:0016757,,GO:0016757,GO:0016757,GO:0016757,0.9097,,0.9097,0.9097,0.9097,4,0.9097,0.5717,yes
WZY_PSEAE,G3XCW3,ProtT3,Bacteria,438,"Polymerase involved in the biosynthesis of the B-band lipopolysaccharide (LPS). Catalyzes the polymerization of the O-antigen repeat units on the periplasmic face of the inner membrane, leading to the formation of the lipid-linked O-antigen molecule.",Involved in the polymerization of O-antigen. Cell inner membrane; Multi-pass membrane protein. Belongs to the WzyE family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0016757; GO:0008755,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.9097,0.9097,0.9097,0.9097,0.9097,5,0.9097,0.5717,yes
WZY_PSEAE,G3XCW3,ProtTale,Bacteria,438,"Polymerase involved in the biosynthesis of the B-band lipopolysaccharide (LPS). Catalyzes the polymerization of the O-antigen repeat units on the periplasmic face of the inner membrane, leading to the formation of the lipid-linked O-antigen molecule.","Polymerase involved in the biosynthesis of the lipopolysaccharide (LPS). Catalyzes the polymerization of the O-antigen repeat units on the periplasmic face of the inner membrane, leading to the formation of the lipid-linked O-antigen molecule.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016757; GO:0008755,GO:0016740,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.7437,0.9097,0.9097,0.9097,0.9097,5,0.8765,0.5717,yes
WZY_PSEAE,G3XCW3,Protein2Text,Bacteria,438,"Polymerase involved in the biosynthesis of the B-band lipopolysaccharide (LPS). Catalyzes the polymerization of the O-antigen repeat units on the periplasmic face of the inner membrane, leading to the formation of the lipid-linked O-antigen molecule.","This protein is involved in the synthesis of a bacterial capsule, which is a polysaccharide structure that helps to protect the bacteria from the host immune system. Specifically, it is involved in the addition of a specific sugar residue to the growing capsule.",Maybe,Maybe,Vague,Maybe,Maybe,not-Yes,GO:0016757; GO:0008755,GO:0008194,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.762,0.9097,0.9097,0.9097,0.9097,5,0.8802,0.5717,yes
WZY_PSEAE,G3XCW3,Reference,Bacteria,438,"Polymerase involved in the biosynthesis of the B-band lipopolysaccharide (LPS). Catalyzes the polymerization of the O-antigen repeat units on the periplasmic face of the inner membrane, leading to the formation of the lipid-linked O-antigen molecule.","Polymerase involved in the biosynthesis of the B-band lipopolysaccharide (LPS). Catalyzes the polymerization of the O-antigen repeat units on the periplasmic face of the inner membrane, leading to the formation of the lipid-linked O-antigen molecule.",,,,,,,GO:0016757; GO:0008755,GO:0016757,GO:0016757,GO:0016757,GO:0016740,GO:0016757,0.9097,0.9097,0.9097,0.7437,0.9097,5,0.8765,0.5717,yes
LIDS_PYRO7,G4N4J5,ESM2Text,Eukaryota,1171,"7,8-linoleate diol synthase is a bifunctional enzyme that converts linoleic acid (18:2n-6) into 8-hydroperoxy-8(E),12(Z)- octadecadienoic acid (8-HPODE) and then catalyzes the isomerization of the resulting hydroperoxide to 7,8-dihydroxy-9(Z),12(Z)-octadecadienoic acid (7,8-DiHODE).","Bifunctional cytochrome P450 monooxygenase/thiolase; part of the gene cluster that mediates the biosynthesis of the isocyanide xanthocillin and its derivatives. The first step of the pathway consists in the conversion of tyrosine into a vinyl-isonitrile intermediate by the isocyanide synthase xanB. Subsequent oxidative dimerization of this intermediate to form xanthocillin may involve the cytochrome P450 monooxygenase xanG, whose expression is coregulated with that of XanB. Xanthocillin can be further modified by the isonitrile hydratase-like protein xanA which introduces N-formyl groups and the methyltransferase xanE which introduces methyl groups, leading to the production of several derivatives including fumiformamide. Finally, fumiformamide can be subject to both oxidative and reductive cyclization to yield melanocins E and F, respectively.",No,No,No,No,Maybe,not-Yes,GO:0052879; GO:0020037; GO:0005506; GO:0052878; GO:0004497; GO:0016705; GO:0004601,GO:0004497; GO:0020037,GO:0004497; GO:0020037,GO:0004497; GO:0020037,GO:0004497,GO:0004497,0.6804,0.6804,0.6804,0.5213,0.5213,5,0.6168,0.4499,no
LIDS_PYRO7,G4N4J5,Prot2Text,Eukaryota,1171,"7,8-linoleate diol synthase is a bifunctional enzyme that converts linoleic acid (18:2n-6) into 8-hydroperoxy-8(E),12(Z)- octadecadienoic acid (8-HPODE) and then catalyzes the isomerization of the resulting hydroperoxide to 7,8-dihydroxy-9(Z),12(Z)-octadecadienoic acid (7,8-DiHODE).","Catalyzes the dioxygenation of linoleic acid to (8R)-hydroperoxylinoleate and isomerization of the resulting hydroperoxide to (7S,8S)-dihydroxylinoleate.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0052879; GO:0020037; GO:0005506; GO:0052878; GO:0004497; GO:0016705; GO:0004601,GO:0016491,,GO:0016702,GO:0016702,GO:0016702,0.5382,,0.445,0.445,0.445,4,0.4683,0.4499,no
LIDS_PYRO7,G4N4J5,ProtT3,Eukaryota,1171,"7,8-linoleate diol synthase is a bifunctional enzyme that converts linoleic acid (18:2n-6) into 8-hydroperoxy-8(E),12(Z)- octadecadienoic acid (8-HPODE) and then catalyzes the isomerization of the resulting hydroperoxide to 7,8-dihydroxy-9(Z),12(Z)-octadecadienoic acid (7,8-DiHODE).","Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Endoplasmic reticulum membrane; Peripheral membrane protein Microsome membrane; Peripheral membrane protein. Belongs to the cytochrome P450 family",Vague,Vague,No,Vague,Maybe,not-Yes,GO:0052879; GO:0020037; GO:0005506; GO:0052878; GO:0004497; GO:0016705; GO:0004601,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,0.7895,0.7895,0.7895,0.7895,0.7895,5,0.7895,0.4499,no
LIDS_PYRO7,G4N4J5,ProtTale,Eukaryota,1171,"7,8-linoleate diol synthase is a bifunctional enzyme that converts linoleic acid (18:2n-6) into 8-hydroperoxy-8(E),12(Z)- octadecadienoic acid (8-HPODE) and then catalyzes the isomerization of the resulting hydroperoxide to 7,8-dihydroxy-9(Z),12(Z)-octadecadienoic acid (7,8-DiHODE).",Oxidizes linoleic acid to 9-hydroxyoctadec-9-enoic acid (9-HODE).,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0052879; GO:0020037; GO:0005506; GO:0052878; GO:0004497; GO:0016705; GO:0004601,GO:0016702,GO:0016702,GO:0016702,GO:0016491,GO:0016491,0.445,0.445,0.445,0.5382,0.5382,5,0.4823,0.4499,no
LIDS_PYRO7,G4N4J5,Protein2Text,Eukaryota,1171,"7,8-linoleate diol synthase is a bifunctional enzyme that converts linoleic acid (18:2n-6) into 8-hydroperoxy-8(E),12(Z)- octadecadienoic acid (8-HPODE) and then catalyzes the isomerization of the resulting hydroperoxide to 7,8-dihydroxy-9(Z),12(Z)-octadecadienoic acid (7,8-DiHODE).","This protein is a peroxidase, which means it has the molecular function of catalyzing the oxidation of a substrate using hydrogen peroxide as an electron acceptor. Specifically, it is involved in the degradation of linolenic acid, a polyunsaturated fatty acid, by converting it into conjugated dienes.",Maybe,Maybe,No,No,Maybe,not-Yes,GO:0052879; GO:0020037; GO:0005506; GO:0052878; GO:0004497; GO:0016705; GO:0004601,GO:0004601,GO:0004601,GO:0004601,GO:0004601,GO:0004601,0.4823,0.4823,0.4823,0.4823,0.4823,5,0.4823,0.4499,no
LIDS_PYRO7,G4N4J5,Reference,Eukaryota,1171,"7,8-linoleate diol synthase is a bifunctional enzyme that converts linoleic acid (18:2n-6) into 8-hydroperoxy-8(E),12(Z)- octadecadienoic acid (8-HPODE) and then catalyzes the isomerization of the resulting hydroperoxide to 7,8-dihydroxy-9(Z),12(Z)-octadecadienoic acid (7,8-DiHODE).","7,8-linoleate diol synthase is a bifunctional enzyme that converts linoleic acid (18:2n-6) into 8-hydroperoxy-8(E),12(Z)- octadecadienoic acid (8-HPODE) and then catalyzes the isomerization of the resulting hydroperoxide to 7,8-dihydroxy-9(Z),12(Z)-octadecadienoic acid (7,8-DiHODE).",,,,,,,GO:0052879; GO:0020037; GO:0005506; GO:0052878; GO:0004497; GO:0016705; GO:0004601,GO:0016165; GO:0004480,GO:0016491; GO:0016836,GO:0051213; GO:0016853,GO:0016491; GO:0004601,GO:0016702; GO:0016491,0.3953,0.5149,0.5231,0.6318,0.6139,5,0.5358,0.4499,no
KAD1_SCHMA,G4V9S0,ESM2Text,Eukaryota,197,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Also displays broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0016208; GO:0004017; GO:0005524,GO:0004017; GO:0004550,GO:0004017; GO:0004550,GO:0004017; GO:0004550,GO:0004017; GO:0004550,GO:0004017,0.5645,0.5645,0.5645,0.5645,0.5218,5,0.556,0.4124,no
KAD1_SCHMA,G4V9S0,Prot2Text,Eukaryota,197,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0016208; GO:0004017; GO:0005524,GO:0004017,GO:0004017,GO:0004017,GO:0004017,GO:0004017,0.5218,0.5218,0.5218,0.5218,0.5218,5,0.5218,0.4124,no
KAD1_SCHMA,G4V9S0,ProtT3,Eukaryota,197,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. Cytoplasm Nucleus. Belongs to the adenylate kinase family. AK2 subfamily,Yes,Yes,Yes,Yes,Yes,Yes,GO:0016208; GO:0004017; GO:0005524,GO:0004017; GO:0005524,GO:0004017; GO:0005524,GO:0004017; GO:0005524,GO:0004017; GO:0005524,GO:0004017,0.9614,0.9614,0.9614,0.9614,0.5218,5,0.8735,0.4124,no
KAD1_SCHMA,G4V9S0,ProtTale,Eukaryota,197,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0016208; GO:0004017; GO:0005524,GO:0004017,GO:0004017,GO:0004017; GO:0005524,GO:0004017; GO:0005524,GO:0004017; GO:0005524,0.5218,0.5218,0.9614,0.9614,0.9614,5,0.7856,0.4124,no
KAD1_SCHMA,G4V9S0,Protein2Text,Eukaryota,197,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.,"This protein is involved in catalyzing the phosphorylation of ribose-5-phosphate to ribose-5-phosphate, which is a key step in the synthesis of nucleotides. It is a kinase, specifically a ribokinase, that catalyzes the phosphorylation of ribose to ribose-5-phosphate.",No,No,No,No,No,not-Yes,GO:0016208; GO:0004017; GO:0005524,GO:0016301,GO:0004017,GO:0004017,GO:0019201,GO:0004017,0.3487,0.5218,0.5218,0.4752,0.5218,5,0.4779,0.4124,no
KAD1_SCHMA,G4V9S0,Reference,Eukaryota,197,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.,,,,,,,GO:0016208; GO:0004017; GO:0005524,GO:0004017; GO:0005524,GO:0004017; GO:0005524,GO:0004017; GO:0005524,GO:0004017; GO:0005524,GO:0004017; GO:0005524,0.9614,0.9614,0.9614,0.9614,0.9614,5,0.9614,0.4124,no
PGM_SCHMA,G4VJD5,ESM2Text,Eukaryota,250,"Catalyzes interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate (2,3-BPG) as the primer of the reaction. Schistosomula have significant surface phosphoglycerate mutase activity also without 2,3-BPG. Binds human plasminogen and enhances its conversion to active thrombolytic plasmin in the presence of human tissue plasminogen activator (tPA) in vitro. Host- interactive surface protein, which may degrade vascular blood clots surrounding the worm in vivo and thus may help survival of the parasite in its host microenvironment (Probable).",Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004619,GO:0004619,GO:0004619,GO:0004619,GO:0004619,GO:0004619,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2797,no
PGM_SCHMA,G4VJD5,Prot2Text,Eukaryota,250,"Catalyzes interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate (2,3-BPG) as the primer of the reaction. Schistosomula have significant surface phosphoglycerate mutase activity also without 2,3-BPG. Binds human plasminogen and enhances its conversion to active thrombolytic plasmin in the presence of human tissue plasminogen activator (tPA) in vitro. Host- interactive surface protein, which may degrade vascular blood clots surrounding the worm in vivo and thus may help survival of the parasite in its host microenvironment (Probable).","Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglyceratea crucial step in glycolysis, by using 2,3-bisphosphoglycerate. Also catalyzes the interconversion of (2R)-2,3-bisphosphoglycerate and (2R)-3-phospho-glyceroyl phosphate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004619,GO:0004619,GO:0004619,GO:0004619,GO:0004619,GO:0004619,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2797,no
PGM_SCHMA,G4VJD5,ProtT3,Eukaryota,250,"Catalyzes interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate (2,3-BPG) as the primer of the reaction. Schistosomula have significant surface phosphoglycerate mutase activity also without 2,3-BPG. Binds human plasminogen and enhances its conversion to active thrombolytic plasmin in the presence of human tissue plasminogen activator (tPA) in vitro. Host- interactive surface protein, which may degrade vascular blood clots surrounding the worm in vivo and thus may help survival of the parasite in its host microenvironment (Probable).",Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004619,GO:0004619,GO:0004619,GO:0004619,GO:0004619,GO:0004619,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2797,no
PGM_SCHMA,G4VJD5,ProtTale,Eukaryota,250,"Catalyzes interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate (2,3-BPG) as the primer of the reaction. Schistosomula have significant surface phosphoglycerate mutase activity also without 2,3-BPG. Binds human plasminogen and enhances its conversion to active thrombolytic plasmin in the presence of human tissue plasminogen activator (tPA) in vitro. Host- interactive surface protein, which may degrade vascular blood clots surrounding the worm in vivo and thus may help survival of the parasite in its host microenvironment (Probable).",Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004619,GO:0004619,GO:0004619,GO:0004619,GO:0004619,GO:0004619,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2797,no
PGM_SCHMA,G4VJD5,Protein2Text,Eukaryota,250,"Catalyzes interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate (2,3-BPG) as the primer of the reaction. Schistosomula have significant surface phosphoglycerate mutase activity also without 2,3-BPG. Binds human plasminogen and enhances its conversion to active thrombolytic plasmin in the presence of human tissue plasminogen activator (tPA) in vitro. Host- interactive surface protein, which may degrade vascular blood clots surrounding the worm in vivo and thus may help survival of the parasite in its host microenvironment (Probable).","The molecular function of this protein is an enzyme, specifically a phosphoglycerate mutase, which catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004619,GO:0004619,GO:0004619,GO:0004619,GO:0004619,GO:0004619,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2797,no
PGM_SCHMA,G4VJD5,Reference,Eukaryota,250,"Catalyzes interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate (2,3-BPG) as the primer of the reaction. Schistosomula have significant surface phosphoglycerate mutase activity also without 2,3-BPG. Binds human plasminogen and enhances its conversion to active thrombolytic plasmin in the presence of human tissue plasminogen activator (tPA) in vitro. Host- interactive surface protein, which may degrade vascular blood clots surrounding the worm in vivo and thus may help survival of the parasite in its host microenvironment (Probable).","Catalyzes interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate (2,3-BPG) as the primer of the reaction. Schistosomula have significant surface phosphoglycerate mutase activity also without 2,3-BPG. Binds human plasminogen and enhances its conversion to active thrombolytic plasmin in the presence of human tissue plasminogen activator (tPA) in vitro. Host- interactive surface protein, which may degrade vascular blood clots surrounding the worm in vivo and thus may help survival of the parasite in its host microenvironment (Probable).",,,,,,,GO:0004619,GO:0004619,GO:0004619,GO:0004619,GO:0004619,GO:0004619,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2797,no
PUR8_SCHMA,G4VQX9,ESM2Text,Eukaryota,480,Catalyzes conversion of succinyladenosine monophosphate (SAMP) to AMP and fumarate on the purine salvage pathway.,"Catalyzes both the synthesis of 5-aminoimidazole- (N-succinylocarboxamide) ribonucleotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate) and fumarate, and of adenylosuccinate (ADS or N(6)-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP) and fumarate.",Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0070626; GO:0004018; GO:0000166,GO:0016829,GO:0004018,GO:0004018,GO:0004018,GO:0004018,0.4936,0.7082,0.7082,0.7082,0.7082,5,0.6653,0.2625,no
PUR8_SCHMA,G4VQX9,Prot2Text,Eukaryota,480,Catalyzes conversion of succinyladenosine monophosphate (SAMP) to AMP and fumarate on the purine salvage pathway.,"Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate.",Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0070626; GO:0004018; GO:0000166,GO:0004018,GO:0004018,GO:0004018,GO:0004018,GO:0004018,0.7082,0.7082,0.7082,0.7082,0.7082,5,0.7082,0.2625,no
PUR8_SCHMA,G4VQX9,ProtT3,Eukaryota,480,Catalyzes conversion of succinyladenosine monophosphate (SAMP) to AMP and fumarate on the purine salvage pathway.,"Catalyzes two reactions in de novo purine nucleotide biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N- succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta- D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4- carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D- ribosyl)imidazole-4-carboxamide) and fumarate, and of aden",Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0070626; GO:0004018; GO:0000166,GO:0004018,GO:0004018,GO:0004018,GO:0004018,GO:0004018,0.7082,0.7082,0.7082,0.7082,0.7082,5,0.7082,0.2625,no
PUR8_SCHMA,G4VQX9,ProtTale,Eukaryota,480,Catalyzes conversion of succinyladenosine monophosphate (SAMP) to AMP and fumarate on the purine salvage pathway.,Catalyzes the transfer of an acetyl group from acetyl-CoA to L-aspartate to produce 4-acetyl-L- aspartate and ATP. Can also catalyze the transfer of an acetyl group from acetyl-CoA to D-aspartate to produce 4-acetyl-D-aspartate and 2 ATP.,No,No,No,No,No,not-Yes,GO:0070626; GO:0004018; GO:0000166,GO:0016407,GO:0016410,GO:0016407,GO:0016746,GO:0016746,0.1759,0.1759,0.1759,0.2482,0.2482,5,0.2048,0.2625,no
PUR8_SCHMA,G4VQX9,Protein2Text,Eukaryota,480,Catalyzes conversion of succinyladenosine monophosphate (SAMP) to AMP and fumarate on the purine salvage pathway.,The molecular function of this protein is catalyzing the conversion of 3-hydroxyisobutyrate to methylmalonate semialdehyde in the catabolism of leucine and valine.,No,No,No,No,No,not-Yes,GO:0070626; GO:0004018; GO:0000166,,GO:0016491,GO:0008442,GO:0008442,GO:0016491,,0.3086,0.1759,0.1759,0.3086,4,0.2422,0.2625,no
PUR8_SCHMA,G4VQX9,Reference,Eukaryota,480,Catalyzes conversion of succinyladenosine monophosphate (SAMP) to AMP and fumarate on the purine salvage pathway.,Catalyzes conversion of succinyladenosine monophosphate (SAMP) to AMP and fumarate on the purine salvage pathway.,,,,,,,GO:0070626; GO:0004018; GO:0000166,GO:0004018,GO:0004018,GO:0004018,GO:0004018,GO:0004018,0.7082,0.7082,0.7082,0.7082,0.7082,5,0.7082,0.2625,no
CHS1_PHYSP,G4Z2L3,ESM2Text,Eukaryota,913,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer. Involved in mycelial growth, sporangial production, zoospore release and pathogenesis.","Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3584,no
CHS1_PHYSP,G4Z2L3,Prot2Text,Eukaryota,913,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer. Involved in mycelial growth, sporangial production, zoospore release and pathogenesis.","Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3584,no
CHS1_PHYSP,G4Z2L3,ProtT3,Eukaryota,913,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer. Involved in mycelial growth, sporangial production, zoospore release and pathogenesis.","Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer. Cell membrane; Multi-pass membrane protein. Belongs to the chitin synthase family. Class III subfamily",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3584,no
CHS1_PHYSP,G4Z2L3,ProtTale,Eukaryota,913,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer. Involved in mycelial growth, sporangial production, zoospore release and pathogenesis.","Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3584,no
CHS1_PHYSP,G4Z2L3,Protein2Text,Eukaryota,913,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer. Involved in mycelial growth, sporangial production, zoospore release and pathogenesis.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its name, it is likely that this protein is involved in the synthesis of cell wall components, specifically in the production of glucan, a type of polysaccharide that is a major component of plant cell walls. This protein is probably a glucan synthase, which is responsible for catalyzing the synthesis of glucan polymers from UDP-glucose molecules.",No,No,Vague,Vague,Maybe,not-Yes,GO:0004100,,,,,,,,,,,0,,0.3584,no
CHS1_PHYSP,G4Z2L3,Reference,Eukaryota,913,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer. Involved in mycelial growth, sporangial production, zoospore release and pathogenesis.","Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer. Involved in mycelial growth, sporangial production, zoospore release and pathogenesis.",,,,,,,GO:0004100,GO:0004100,GO:0004756,GO:0004100,GO:0004100,GO:0004100,1.0,0.2476,1.0,1.0,1.0,5,0.8495,0.3584,no
EXOSX_CAEEL,G5EBX6,ESM2Text,Eukaryota,876,Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. Involved in apoptotic DNA degradation. Involved in regulation of antisense ribosomal siRNA production. Involved in response to cold-warm shock.,3'-5' exoribonuclease involved in the processing of intron-containing mRNAs. Essential for the maintenance of 3'-end of intron-containing mRNAs. Represses the formation of normal intron-containing mRNAs by acting as an exonuclease at the 3'-end of intron-containing mRNAs. This mechanism prevents the recruitment of cytoplasmic enzymes to degrade the nonsense decay product and the subsequent degradation of the mRNAs which are necessary for cell cycle progression. Its activity is inhibited by the nonsense-mediated decay of the intron-containing mRNA which is productive before the recruitment of exonuclease SPT15/cut2 and the recruitment of exonuclease SPT15/cut3. Plays a role in maintenance of steady-state intron RNA levels.,Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0000175; GO:0000166; GO:0003727,GO:0000175,GO:0000175,GO:0000175,GO:0000175,GO:0000175,0.5325,0.5325,0.5325,0.5325,0.5325,5,0.5325,0.4408,no
EXOSX_CAEEL,G5EBX6,Prot2Text,Eukaryota,876,Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. Involved in apoptotic DNA degradation. Involved in regulation of antisense ribosomal siRNA production. Involved in response to cold-warm shock.,"Essential poly(A) tail exonuclease that anchors exon halves to RNAs and plays a central role in mRNA decay. Involved in poly(A) tail length regulation through competition with U6 snRNA and subsequent U6 snRNA binding activity. In contrast to U6 snRNA, it does not participate in polyadenylation process and poly(A) tail length regulation through competition with U6atac snRNA. Involved in the 3'-end processing of the U4/U6.U5 tri-snRNP, a non-coding pre-tRNA. In addition to 3'-end processing, required for the 3'-end processing of the U9/U6.U5 tri-snRNP and the 3'-end processing of the pre-tRNA AICDA-III. Also acts as a histone 3'-end pre-mRNA processing and is involved in histone 3'-end processing. Associates with chromatin and plays a role in DNA damage response and DNA repair. Involved in DNA double-strand break repair and has a role in sister chromatid cohesion. Associates with chromatin and may participate in DNA repair via its interaction with HIRA and HIRA-binding proteins",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0000175; GO:0000166; GO:0003727,GO:0004532,GO:0004535,GO:0004535,,GO:0004532,0.4426,0.4957,0.4957,,0.4426,4,0.4691,0.4408,no
EXOSX_CAEEL,G5EBX6,ProtT3,Eukaryota,876,Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. Involved in apoptotic DNA degradation. Involved in regulation of antisense ribosomal siRNA production. Involved in response to cold-warm shock.,Involved in pre-mRNA 3'-end processing. Nucleus. Belongs to the RNA 3'-end poly(A) polymerase family,No,No,Maybe,No,No,not-Yes,GO:0000175; GO:0000166; GO:0003727,GO:0004652,GO:0004652,GO:0004652,GO:0004652,GO:0004652,0.0,0.0,0.0,0.0,0.0,5,0.0,0.4408,no
EXOSX_CAEEL,G5EBX6,ProtTale,Eukaryota,876,Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. Involved in apoptotic DNA degradation. Involved in regulation of antisense ribosomal siRNA production. Involved in response to cold-warm shock.,"Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch",Yes,Yes,Yes,Yes,Yes,Yes,GO:0000175; GO:0000166; GO:0003727,GO:0000175,GO:0000175,GO:0000175,GO:0000175,GO:0000175,0.5325,0.5325,0.5325,0.5325,0.5325,5,0.5325,0.4408,no
EXOSX_CAEEL,G5EBX6,Protein2Text,Eukaryota,876,Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. Involved in apoptotic DNA degradation. Involved in regulation of antisense ribosomal siRNA production. Involved in response to cold-warm shock.,"This protein is involved in molecular motor activity, specifically in microtubule binding. It is part of a larger complex that plays a role in regulating microtubule dynamics and organization.",No,No,No,No,No,not-Yes,GO:0000175; GO:0000166; GO:0003727,,GO:0003777; GO:0008017,GO:0003777,GO:0003777,GO:0003777; GO:0008017,,0.192,0.122,0.122,0.192,4,0.157,0.4408,no
EXOSX_CAEEL,G5EBX6,Reference,Eukaryota,876,Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. Involved in apoptotic DNA degradation. Involved in regulation of antisense ribosomal siRNA production. Involved in response to cold-warm shock.,Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. Involved in apoptotic DNA degradation. Involved in regulation of antisense ribosomal siRNA production. Involved in response to cold-warm shock.,,,,,,,GO:0000175; GO:0000166; GO:0003727,GO:0000175; GO:0003723,GO:0004532; GO:0000175,GO:0000175,GO:0000175; GO:0004532,GO:0004532,0.7994,0.5926,0.5325,0.5926,0.4426,5,0.5919,0.4408,no
SWSN4_CAEEL,G5EF53,ESM2Text,Eukaryota,1474,"Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Selectively binds the N-terminal tail of histone H3 mono-acetylated on 'Lys-15' via the C-terminal bromodomain. Involved in multiple stages of somatic gonad development; as part of the PBAF complex, required for normal development of somatic gonadal precursor cells (the multipotent progenitors that give rise to all somatic tissues of the adult reproductive system), as part of the BAF complex, involved in the formation or function of the differentiated distal tip cells of the somatic gonad. Influences vulval differentiation of P lineage cells, which may in part be mediated by its direct or indirect transcriptional regulation of let-23. Required during mitosis for asymmetric cell division of T blast cells.","Helicase. Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. Controls particularly membrane and organelle development genes.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0003682; GO:0003677; GO:0004386; GO:0042393; GO:0016787; GO:0140750,GO:0003678; GO:0005524,GO:0004386; GO:0005524,GO:0004386,GO:0004386,GO:0003678,0.5462,0.584,0.4017,0.4017,0.3461,5,0.4559,0.3428,no
SWSN4_CAEEL,G5EF53,Prot2Text,Eukaryota,1474,"Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Selectively binds the N-terminal tail of histone H3 mono-acetylated on 'Lys-15' via the C-terminal bromodomain. Involved in multiple stages of somatic gonad development; as part of the PBAF complex, required for normal development of somatic gonadal precursor cells (the multipotent progenitors that give rise to all somatic tissues of the adult reproductive system), as part of the BAF complex, involved in the formation or function of the differentiated distal tip cells of the somatic gonad. Influences vulval differentiation of P lineage cells, which may in part be mediated by its direct or indirect transcriptional regulation of let-23. Required during mitosis for asymmetric cell division of T blast cells.",Helicase that acts as a transcriptional repressor. May play a role in the control of cell cycle progression and DNA damage response.,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0005524; GO:0003682; GO:0003677; GO:0004386; GO:0042393; GO:0016787; GO:0140750,GO:0004386,GO:0004386,GO:0004386,GO:0003678; GO:0005524,GO:0004386,0.4017,0.4017,0.4017,0.5462,0.4017,5,0.4306,0.3428,no
SWSN4_CAEEL,G5EF53,ProtT3,Eukaryota,1474,"Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Selectively binds the N-terminal tail of histone H3 mono-acetylated on 'Lys-15' via the C-terminal bromodomain. Involved in multiple stages of somatic gonad development; as part of the PBAF complex, required for normal development of somatic gonadal precursor cells (the multipotent progenitors that give rise to all somatic tissues of the adult reproductive system), as part of the BAF complex, involved in the formation or function of the differentiated distal tip cells of the somatic gonad. Influences vulval differentiation of P lineage cells, which may in part be mediated by its direct or indirect transcriptional regulation of let-23. Required during mitosis for asymmetric cell division of T blast cells.",ATP-dependent nucleosome-remodeling factor involved in chromatin remodeling and DNA repair. Nucleus. Belongs to the SNF2/RAD54 helicase family. SNF2 subfamily,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0003682; GO:0003677; GO:0004386; GO:0042393; GO:0016787; GO:0140750,GO:0016887; GO:0005524,GO:0003678; GO:0005524,GO:0004386; GO:0005524,GO:0008094,GO:0016887,0.4469,0.5462,0.584,0.3692,0.2443,5,0.4381,0.3428,no
SWSN4_CAEEL,G5EF53,ProtTale,Eukaryota,1474,"Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Selectively binds the N-terminal tail of histone H3 mono-acetylated on 'Lys-15' via the C-terminal bromodomain. Involved in multiple stages of somatic gonad development; as part of the PBAF complex, required for normal development of somatic gonadal precursor cells (the multipotent progenitors that give rise to all somatic tissues of the adult reproductive system), as part of the BAF complex, involved in the formation or function of the differentiated distal tip cells of the somatic gonad. Influences vulval differentiation of P lineage cells, which may in part be mediated by its direct or indirect transcriptional regulation of let-23. Required during mitosis for asymmetric cell division of T blast cells.",Involved in transcriptional regulation. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4 and H2A. The NuA4 complex is also involved in DNA repair.,No,Maybe,No,Maybe,Maybe,not-Yes,GO:0005524; GO:0003682; GO:0003677; GO:0004386; GO:0042393; GO:0016787; GO:0140750,GO:0004402,,GO:0004402,GO:0004402,,0.1375,,0.1375,0.1375,,3,0.1375,0.3428,no
SWSN4_CAEEL,G5EF53,Protein2Text,Eukaryota,1474,"Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Selectively binds the N-terminal tail of histone H3 mono-acetylated on 'Lys-15' via the C-terminal bromodomain. Involved in multiple stages of somatic gonad development; as part of the PBAF complex, required for normal development of somatic gonadal precursor cells (the multipotent progenitors that give rise to all somatic tissues of the adult reproductive system), as part of the BAF complex, involved in the formation or function of the differentiated distal tip cells of the somatic gonad. Influences vulval differentiation of P lineage cells, which may in part be mediated by its direct or indirect transcriptional regulation of let-23. Required during mitosis for asymmetric cell division of T blast cells.","This protein is a structural component of the cell, specifically a type of protein that plays a crucial role in the formation and maintenance of the cytoskeleton. It is involved in the regulation of cell shape, motility, and division. More specifically, it is a component of the cytoskeletal meshwork that provides mechanical strength and elasticity to cells.",No,No,No,No,Vague,not-Yes,GO:0005524; GO:0003682; GO:0003677; GO:0004386; GO:0042393; GO:0016787; GO:0140750,,GO:0005198,,GO:0005200,GO:0005198,,0.255,,0.199,0.255,3,0.2363,0.3428,no
SWSN4_CAEEL,G5EF53,Reference,Eukaryota,1474,"Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Selectively binds the N-terminal tail of histone H3 mono-acetylated on 'Lys-15' via the C-terminal bromodomain. Involved in multiple stages of somatic gonad development; as part of the PBAF complex, required for normal development of somatic gonadal precursor cells (the multipotent progenitors that give rise to all somatic tissues of the adult reproductive system), as part of the BAF complex, involved in the formation or function of the differentiated distal tip cells of the somatic gonad. Influences vulval differentiation of P lineage cells, which may in part be mediated by its direct or indirect transcriptional regulation of let-23. Required during mitosis for asymmetric cell division of T blast cells.","Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Selectively binds the N-terminal tail of histone H3 mono-acetylated on 'Lys-15' via the C-terminal bromodomain. Involved in multiple stages of somatic gonad development; as part of the PBAF complex, required for normal development of somatic gonadal precursor cells (the multipotent progenitors that give rise to all somatic tissues of the adult reproductive system), as part of the BAF complex, involved in the formation or function of the differentiated distal tip cells of the somatic gonad. Influences vulval differentiation of P lineage cells, which may in part be mediated by its direct or indirect transcriptional regulation of let-23. Required during mitosis for asymmetric cell division of T blast cells.",,,,,,,GO:0005524; GO:0003682; GO:0003677; GO:0004386; GO:0042393; GO:0016787; GO:0140750,GO:0008094; GO:0003682; GO:0042393,GO:0005524; GO:0003682,GO:0003682,GO:0005524; GO:0016887,GO:0003682; GO:0005524,0.7054,0.6127,0.4638,0.4469,0.6127,5,0.5683,0.3428,no
MCA1_CAEEL,G5EFR6,ESM2Text,Eukaryota,1252,Catalyzes the hydrolysis of ATP coupled with the transport of calcium across a membrane.,"This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol out of the cell, into the endoplasmic reticulum, or into organelles.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0005516; GO:0046872; GO:0005388,GO:0005388; GO:0005524,GO:0005388; GO:0005524,GO:0005388,GO:0005388,GO:0005388,0.6557,0.6557,0.3844,0.3844,0.3844,5,0.4929,0.5684,yes
MCA1_CAEEL,G5EFR6,Prot2Text,Eukaryota,1252,Catalyzes the hydrolysis of ATP coupled with the transport of calcium across a membrane.,Catalyzes the hydrolysis of ATP coupled with the transport of calcium from the cytoplasm to the extracellular space thereby maintaining intracellular calcium homeostasis.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0005516; GO:0046872; GO:0005388,GO:0005388,GO:0005388,GO:0005388,GO:0005388; GO:0005524,GO:0005388,0.3844,0.3844,0.3844,0.6557,0.3844,5,0.4387,0.5684,yes
MCA1_CAEEL,G5EFR6,ProtT3,Eukaryota,1252,Catalyzes the hydrolysis of ATP coupled with the transport of calcium across a membrane.,This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the vacuole. Vacuole membrane; Multi-pass membrane protein. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0005516; GO:0046872; GO:0005388,GO:0005388; GO:0005524,GO:0005388; GO:0005524,GO:0005388; GO:0005524,GO:0005388,GO:0005388,0.6557,0.6557,0.6557,0.3844,0.3844,5,0.5472,0.5684,yes
MCA1_CAEEL,G5EFR6,ProtTale,Eukaryota,1252,Catalyzes the hydrolysis of ATP coupled with the transport of calcium across a membrane.,This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol into the endoplasmic reticulum or Golgi.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0005516; GO:0046872; GO:0005388,GO:0005388,GO:0005388; GO:0005524,GO:0005388; GO:0005524,GO:0005388; GO:0005524,GO:0005388; GO:0005524,0.3844,0.6557,0.6557,0.6557,0.6557,5,0.6014,0.5684,yes
MCA1_CAEEL,G5EFR6,Protein2Text,Eukaryota,1252,Catalyzes the hydrolysis of ATP coupled with the transport of calcium across a membrane.,"The molecular function of this protein is calcium-dependent transport, which involves transporting calcium ions across cell membranes. More specifically, this protein is involved in the process of calcium pumping, which helps to regulate the concentration of calcium ions within the cell. This process is essential for maintaining proper cellular function and is involved in various cellular processes, including muscle contraction, cell signaling, and bone mineralization.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887; GO:0005516; GO:0046872; GO:0005388,GO:0005388,GO:0005388,GO:0005388,GO:0005388,GO:0005388,0.3844,0.3844,0.3844,0.3844,0.3844,5,0.3844,0.5684,yes
MCA1_CAEEL,G5EFR6,Reference,Eukaryota,1252,Catalyzes the hydrolysis of ATP coupled with the transport of calcium across a membrane.,Catalyzes the hydrolysis of ATP coupled with the transport of calcium across a membrane.,,,,,,,GO:0005524; GO:0016887; GO:0005516; GO:0046872; GO:0005388,GO:0005388; GO:0005524,GO:0005388,GO:0005388; GO:0005524,GO:0005388; GO:0005524,GO:0005388; GO:0005524,0.6557,0.3844,0.6557,0.6557,0.6557,5,0.6014,0.5684,yes
KLP12_CAEEL,G5EGS3,ESM2Text,Eukaryota,1605,"Microtubule-binding motor protein which has ATPase activity. In complex with alpha and beta tubulins, preferentially binds to the growing microtubule plus-end to stabilize it and detaches following ATP hydrolysis. Negatively regulates axonal length through inhibiting microtubule polymerization at its plus-end.",Microtubule-dependent motor protein involved in the control of the oriented deposition of cellulose microfibrils.,Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887; GO:0008017; GO:0003777,GO:0003777,GO:0003774; GO:0008017,GO:0003777,GO:0003777,GO:0003777,0.4947,0.5313,0.4947,0.4947,0.4947,5,0.502,0.4152,no
KLP12_CAEEL,G5EGS3,Prot2Text,Eukaryota,1605,"Microtubule-binding motor protein which has ATPase activity. In complex with alpha and beta tubulins, preferentially binds to the growing microtubule plus-end to stabilize it and detaches following ATP hydrolysis. Negatively regulates axonal length through inhibiting microtubule polymerization at its plus-end.",Minus end-directed motor protein involved in the control of the oriented deposition of cellulose microfibrils. Its motor activity is directed toward the microtubule's plus end. May interact with a specific subset of microtubules.,Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887; GO:0008017; GO:0003777,GO:0003777,GO:0003777,GO:0003777,GO:0003777; GO:0005524,GO:0003777,0.4947,0.4947,0.4947,0.7375,0.4947,5,0.5433,0.4152,no
KLP12_CAEEL,G5EGS3,ProtT3,Eukaryota,1605,"Microtubule-binding motor protein which has ATPase activity. In complex with alpha and beta tubulins, preferentially binds to the growing microtubule plus-end to stabilize it and detaches following ATP hydrolysis. Negatively regulates axonal length through inhibiting microtubule polymerization at its plus-end.","Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Cytoplasm, cytoskeleton. Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family",Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0005524; GO:0016887; GO:0008017; GO:0003777,GO:0003777; GO:0005524,GO:0003777; GO:0005524,GO:0003777; GO:0005524,GO:0003777; GO:0005524,GO:0003777; GO:0005524,0.7375,0.7375,0.7375,0.7375,0.7375,5,0.7375,0.4152,no
KLP12_CAEEL,G5EGS3,ProtTale,Eukaryota,1605,"Microtubule-binding motor protein which has ATPase activity. In complex with alpha and beta tubulins, preferentially binds to the growing microtubule plus-end to stabilize it and detaches following ATP hydrolysis. Negatively regulates axonal length through inhibiting microtubule polymerization at its plus-end.",Microtubule-associated force-producing protein that plays a role in organelle transport. Its motor activity is directed toward the microtubule's plus end. Cooperates with dynein to form the spindle pole body (SPB) attachment complex of the mitotic spindle.,Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887; GO:0008017; GO:0003777,GO:0003777,GO:0003777; GO:0005524,GO:0003777,,GO:0003777; GO:0005524,0.4947,0.7375,0.4947,,0.7375,4,0.6161,0.4152,no
KLP12_CAEEL,G5EGS3,Protein2Text,Eukaryota,1605,"Microtubule-binding motor protein which has ATPase activity. In complex with alpha and beta tubulins, preferentially binds to the growing microtubule plus-end to stabilize it and detaches following ATP hydrolysis. Negatively regulates axonal length through inhibiting microtubule polymerization at its plus-end.","The molecular function of this protein is a motor protein, specifically a kinesin-like protein, which is involved in microtubule-dependent processes such as cell division, cell signaling, and intracellular transport.",Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0005524; GO:0016887; GO:0008017; GO:0003777,,GO:0003777; GO:0008017,GO:0003777,GO:0003777,GO:0003777; GO:0008017,,0.7375,0.4947,0.4947,0.7375,4,0.6161,0.4152,no
KLP12_CAEEL,G5EGS3,Reference,Eukaryota,1605,"Microtubule-binding motor protein which has ATPase activity. In complex with alpha and beta tubulins, preferentially binds to the growing microtubule plus-end to stabilize it and detaches following ATP hydrolysis. Negatively regulates axonal length through inhibiting microtubule polymerization at its plus-end.","Microtubule-binding motor protein which has ATPase activity. In complex with alpha and beta tubulins, preferentially binds to the growing microtubule plus-end to stabilize it and detaches following ATP hydrolysis. Negatively regulates axonal length through inhibiting microtubule polymerization at its plus-end.",,,,,,,GO:0005524; GO:0016887; GO:0008017; GO:0003777,GO:0003777; GO:0005524; GO:0008017,GO:0003777; GO:0005524,GO:0003777; GO:0005524; GO:0008017,GO:0003777; GO:0005524; GO:0016887,GO:0003777; GO:0005524,0.9,0.7375,0.9,0.875,0.7375,5,0.83,0.4152,no
HISN3_MEDTR,G7IFI7,ESM2Text,Eukaryota,312,"Component of the histidine biosynthesis pathway that catalyzes the isomerization of 5'-ProFAR (pro-phosphoribosyl formimino- 5-aminoimidazole-4-carboxamide ribonucleotide, referred as 1-(5- phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D- ribosylamino)methylideneamino]imidazole-4-carboxamide) to PrFAR (phosphoribulosyl formimino-5-aminoimidazole-4-carboxamide ribonucleotide, referred as 5-[(5-phospho-1-deoxy-D-ribulos-1- ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4- carboxamide).","Is able to catalyze the cleavage of 4-amino-2-methylpyrimidine pyrophosphate (HMP-PP) into acetyl-CoA and glyceraldehyde-3-phosphate (GA3P), respectively. Is also able to produce KHMP-PP, but inactive toward 1-amino-2-methylpyrimidine phosphate (AMP) and 3-amino-2-methylbutanone phosphate (AHMP).",No,No,No,No,No,not-Yes,GO:0003949; GO:0046872,,,,,,,,,,,0,,0.2284,no
HISN3_MEDTR,G7IFI7,Prot2Text,Eukaryota,312,"Component of the histidine biosynthesis pathway that catalyzes the isomerization of 5'-ProFAR (pro-phosphoribosyl formimino- 5-aminoimidazole-4-carboxamide ribonucleotide, referred as 1-(5- phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D- ribosylamino)methylideneamino]imidazole-4-carboxamide) to PrFAR (phosphoribulosyl formimino-5-aminoimidazole-4-carboxamide ribonucleotide, referred as 5-[(5-phospho-1-deoxy-D-ribulos-1- ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4- carboxamide).","IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0003949; GO:0046872,GO:0000107,GO:0000107,GO:0000107,GO:0016829,GO:0000107,0.1628,0.1628,0.1628,0.2894,0.1628,5,0.1881,0.2284,no
HISN3_MEDTR,G7IFI7,ProtT3,Eukaryota,312,"Component of the histidine biosynthesis pathway that catalyzes the isomerization of 5'-ProFAR (pro-phosphoribosyl formimino- 5-aminoimidazole-4-carboxamide ribonucleotide, referred as 1-(5- phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D- ribosylamino)methylideneamino]imidazole-4-carboxamide) to PrFAR (phosphoribulosyl formimino-5-aminoimidazole-4-carboxamide ribonucleotide, referred as 5-[(5-phospho-1-deoxy-D-ribulos-1- ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4- carboxamide).","Plastid, chloroplast. Belongs to the HisA/HisF family",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0003949; GO:0046872,,,GO:0016853,GO:0016853,,,,0.4539,0.4539,,2,0.4539,0.2284,no
HISN3_MEDTR,G7IFI7,ProtTale,Eukaryota,312,"Component of the histidine biosynthesis pathway that catalyzes the isomerization of 5'-ProFAR (pro-phosphoribosyl formimino- 5-aminoimidazole-4-carboxamide ribonucleotide, referred as 1-(5- phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D- ribosylamino)methylideneamino]imidazole-4-carboxamide) to PrFAR (phosphoribulosyl formimino-5-aminoimidazole-4-carboxamide ribonucleotide, referred as 5-[(5-phospho-1-deoxy-D-ribulos-1- ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4- carboxamide).","Is involved in the initial step of the de novo biosynthesis of purine nucleotides. Catalyzes the conversion of GTP to 7,8-dihydroneopterin triphosphate (DHN-TP).",No,No,No,No,No,not-Yes,GO:0003949; GO:0046872,GO:0003934,GO:0003934,GO:0003934,GO:0003934,GO:0003934,0.1255,0.1255,0.1255,0.1255,0.1255,5,0.1255,0.2284,no
HISN3_MEDTR,G7IFI7,Protein2Text,Eukaryota,312,"Component of the histidine biosynthesis pathway that catalyzes the isomerization of 5'-ProFAR (pro-phosphoribosyl formimino- 5-aminoimidazole-4-carboxamide ribonucleotide, referred as 1-(5- phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D- ribosylamino)methylideneamino]imidazole-4-carboxamide) to PrFAR (phosphoribulosyl formimino-5-aminoimidazole-4-carboxamide ribonucleotide, referred as 5-[(5-phospho-1-deoxy-D-ribulos-1- ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4- carboxamide).","The molecular function of this protein is a prenyltransferase, which is a type of enzyme that catalyzes the transfer of a prenyl group from one molecule to another. In this case, it is involved in the conversion of dihydroxyacetone phosphate (DHAP) to mevalonate, a key step in the biosynthesis of isoprenoids.",No,No,No,No,No,not-Yes,GO:0003949; GO:0046872,GO:0004659,GO:0004659,,GO:0004659,GO:0004659,0.1917,0.1917,,0.1917,0.1917,4,0.1917,0.2284,no
HISN3_MEDTR,G7IFI7,Reference,Eukaryota,312,"Component of the histidine biosynthesis pathway that catalyzes the isomerization of 5'-ProFAR (pro-phosphoribosyl formimino- 5-aminoimidazole-4-carboxamide ribonucleotide, referred as 1-(5- phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D- ribosylamino)methylideneamino]imidazole-4-carboxamide) to PrFAR (phosphoribulosyl formimino-5-aminoimidazole-4-carboxamide ribonucleotide, referred as 5-[(5-phospho-1-deoxy-D-ribulos-1- ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4- carboxamide).","Component of the histidine biosynthesis pathway that catalyzes the isomerization of 5'-ProFAR (pro-phosphoribosyl formimino- 5-aminoimidazole-4-carboxamide ribonucleotide, referred as 1-(5- phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D- ribosylamino)methylideneamino]imidazole-4-carboxamide) to PrFAR (phosphoribulosyl formimino-5-aminoimidazole-4-carboxamide ribonucleotide, referred as 5-[(5-phospho-1-deoxy-D-ribulos-1- ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4- carboxamide).",,,,,,,GO:0003949; GO:0046872,GO:0004616,GO:0004640,GO:0016853,GO:0016862,GO:0016853,0.1628,0.5156,0.4539,0.4368,0.4539,5,0.4046,0.2284,no
CRE1_MEDTR,G7LCC3,ESM2Text,Eukaryota,1003,"Cytokinins (CK) receptor related to bacterial two-component regulators. Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade. This protein undergoes an ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain.",Cytokinin receptor related to bacterial two-component regulators. Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0009884; GO:0016787; GO:0046872; GO:0000155; GO:0043424,GO:0004673,GO:0004673; GO:0000155,GO:0004673,GO:0004673,GO:0000155,0.3571,0.4733,0.3571,0.3571,0.408,5,0.3905,0.3445,no
CRE1_MEDTR,G7LCC3,Prot2Text,Eukaryota,1003,"Cytokinins (CK) receptor related to bacterial two-component regulators. Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade. This protein undergoes an ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain.",Cytokinin receptor related to bacterial two-component regulators. Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0009884; GO:0016787; GO:0046872; GO:0000155; GO:0043424,GO:0000155,GO:0000155,GO:0000155,GO:0000155; GO:0004673,GO:0000155,0.408,0.408,0.408,0.4733,0.408,5,0.4211,0.3445,no
CRE1_MEDTR,G7LCC3,ProtT3,Eukaryota,1003,"Cytokinins (CK) receptor related to bacterial two-component regulators. Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade. This protein undergoes an ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain.",His-to-Asp phosphorelay protein involved in cytokinin signal transduction. Cell membrane; Multi-pass membrane protein. Belongs to the two-component regulatory system sensor family,Maybe,Yes,Yes,Maybe,Vague,not-Yes,GO:0009884; GO:0016787; GO:0046872; GO:0000155; GO:0043424,GO:0000155,GO:0000155,GO:0000155; GO:0005524,GO:0000155,GO:0000155,0.408,0.408,0.4285,0.408,0.408,5,0.4121,0.3445,no
CRE1_MEDTR,G7LCC3,ProtTale,Eukaryota,1003,"Cytokinins (CK) receptor related to bacterial two-component regulators. Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade. This protein undergoes an ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain.",Functions as a receptor in the response to brassinosteroids. Functions as a receptor in the response to brassinosteroids. Functions as a receptor in the response to brassinosteroids. Functions as a receptor in the response to brassinosteroids. Functions as a receptor in the response to brassinosteroids. Functions as a receptor in the response to brassinosteroids. Functions as a receptor in the response to brassinosteroids. Functions as a receptor in the response to brassinosteroids. Functions as a receptor in the response to brassinosteroids. Functions as a receptor in the response to brassin,No,No,No,No,No,not-Yes,GO:0009884; GO:0016787; GO:0046872; GO:0000155; GO:0043424,,GO:0004675,GO:0038023,,GO:0004674,,0.2794,0.342,,0.302,3,0.3078,0.3445,no
CRE1_MEDTR,G7LCC3,Protein2Text,Eukaryota,1003,"Cytokinins (CK) receptor related to bacterial two-component regulators. Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade. This protein undergoes an ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain.","This protein is a transporter, specifically a cation-transporting ATPase.",No,No,No,No,No,not-Yes,GO:0009884; GO:0016787; GO:0046872; GO:0000155; GO:0043424,GO:0019829,GO:0019829,GO:0019829,GO:0019829,GO:0019829,0.0895,0.0895,0.0895,0.0895,0.0895,5,0.0895,0.3445,no
CRE1_MEDTR,G7LCC3,Reference,Eukaryota,1003,"Cytokinins (CK) receptor related to bacterial two-component regulators. Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade. This protein undergoes an ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain.","Cytokinins (CK) receptor related to bacterial two-component regulators. Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade. This protein undergoes an ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain.",,,,,,,GO:0009884; GO:0016787; GO:0046872; GO:0000155; GO:0043424,GO:0000155; GO:0005524,GO:0000155; GO:0005524,GO:0000155; GO:0004673; GO:0005524,GO:0000155; GO:0005524,GO:0000155; GO:0005524,0.4285,0.4285,0.4831,0.4285,0.4285,5,0.4394,0.3445,no
CLAHY_LACPN,G9MAP1,ESM2Text,Bacteria,569,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-HY catalyzes the hydration and dehydration steps in the production of 10-hydroxy-cis-12-octadecenoate, trans-10,cis-12-CLA, cis-9,trans-11-CLA, trans-9,trans-11-CLA, oleate and trans-10-octadecenoate during linoleate metabolism. Is also able to hydrate palmitoleic acid (cis-9-hexadecenoic acid), oleic acid, alpha- linolenic acid, gamma-linolenic acid, and stearidonic acid into the corresponding 10-hydroxy fatty acids, and dehydrate 10-hydroxy- cis-12,cis-15-octadecadienoic acid, 10-hydroxy-cis-6,cis-12- octadecadienoic acid, and 10-hydroxyoctadecanoic acid into the corresponding fatty acids with cis double bonds at the Delta9 position. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome. Shows regioselectivity for Delta9 double bond hydration, generating C10 hydroxy groups in the (S)-configuration with high enantioselectivity, when another double bond is in position 12. Is not able to hydrate fatty acids with a trans carbon-carbon double bond at Delta9 position (elaidic acid, trans-9-octadecenoic acid), fatty acid esters (methyl linoleate, monolinolein, dilinolein, and trilinolein), and conjugated fatty acids (conjugated linoleic acids), as well as fatty acids with other chain lengths, such as myristoleic acid (cis-9-tetradecenoic acid), arachidonic acid (cis-5,cis-8,cis-11,cis-14-eicosatetraenoic acid), EPA (cis-5,cis-8,cis-11,cis-14,cis-17-eicosapentaenoic acid), DHA (cis-4,cis-7,cis-10,cis-13,cis-16,cis-19-docosahexaenoic acid) and fatty acids with a cis carbon-carbon double bond at Delta11 position, such as cis-vaccenic acid and cis-11-octadecenoic acid, or fatty alcohols, such as linoleyl alcohol. Is not able to dehydrate 12- hydroxy, 3-hydroxy, and 9-hydroxy fatty acids.","Catalyzes the oxidation of various aldopyranoses and disaccharides on carbon-2 to the corresponding 2-keto sugars concomitant with the reduction of O(2) to H(2)O(2). The preferred substrate is D-glucose. Does not act on D-xylose, D-ribose, D-mannose, D-sorbose, L-iditol, or D-glucitol.",No,No,No,No,No,not-Yes,GO:0071949; GO:0050151,GO:0016614,GO:0016614,GO:0016614,GO:0016614,GO:0016614,0.2218,0.2218,0.2218,0.2218,0.2218,5,0.2218,0.2157,no
CLAHY_LACPN,G9MAP1,Prot2Text,Bacteria,569,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-HY catalyzes the hydration and dehydration steps in the production of 10-hydroxy-cis-12-octadecenoate, trans-10,cis-12-CLA, cis-9,trans-11-CLA, trans-9,trans-11-CLA, oleate and trans-10-octadecenoate during linoleate metabolism. Is also able to hydrate palmitoleic acid (cis-9-hexadecenoic acid), oleic acid, alpha- linolenic acid, gamma-linolenic acid, and stearidonic acid into the corresponding 10-hydroxy fatty acids, and dehydrate 10-hydroxy- cis-12,cis-15-octadecadienoic acid, 10-hydroxy-cis-6,cis-12- octadecadienoic acid, and 10-hydroxyoctadecanoic acid into the corresponding fatty acids with cis double bonds at the Delta9 position. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome. Shows regioselectivity for Delta9 double bond hydration, generating C10 hydroxy groups in the (S)-configuration with high enantioselectivity, when another double bond is in position 12. Is not able to hydrate fatty acids with a trans carbon-carbon double bond at Delta9 position (elaidic acid, trans-9-octadecenoic acid), fatty acid esters (methyl linoleate, monolinolein, dilinolein, and trilinolein), and conjugated fatty acids (conjugated linoleic acids), as well as fatty acids with other chain lengths, such as myristoleic acid (cis-9-tetradecenoic acid), arachidonic acid (cis-5,cis-8,cis-11,cis-14-eicosatetraenoic acid), EPA (cis-5,cis-8,cis-11,cis-14,cis-17-eicosapentaenoic acid), DHA (cis-4,cis-7,cis-10,cis-13,cis-16,cis-19-docosahexaenoic acid) and fatty acids with a cis carbon-carbon double bond at Delta11 position, such as cis-vaccenic acid and cis-11-octadecenoic acid, or fatty alcohols, such as linoleyl alcohol. Is not able to dehydrate 12- hydroxy, 3-hydroxy, and 9-hydroxy fatty acids.",Catalyzes the introduction of a C-3 double bond into the B ring of cholesterol.,No,No,No,No,No,not-Yes,GO:0071949; GO:0050151,GO:0016491,,GO:0016491,GO:0016491,,0.2761,,0.2761,0.2761,,3,0.2761,0.2157,no
CLAHY_LACPN,G9MAP1,ProtT3,Bacteria,569,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-HY catalyzes the hydration and dehydration steps in the production of 10-hydroxy-cis-12-octadecenoate, trans-10,cis-12-CLA, cis-9,trans-11-CLA, trans-9,trans-11-CLA, oleate and trans-10-octadecenoate during linoleate metabolism. Is also able to hydrate palmitoleic acid (cis-9-hexadecenoic acid), oleic acid, alpha- linolenic acid, gamma-linolenic acid, and stearidonic acid into the corresponding 10-hydroxy fatty acids, and dehydrate 10-hydroxy- cis-12,cis-15-octadecadienoic acid, 10-hydroxy-cis-6,cis-12- octadecadienoic acid, and 10-hydroxyoctadecanoic acid into the corresponding fatty acids with cis double bonds at the Delta9 position. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome. Shows regioselectivity for Delta9 double bond hydration, generating C10 hydroxy groups in the (S)-configuration with high enantioselectivity, when another double bond is in position 12. Is not able to hydrate fatty acids with a trans carbon-carbon double bond at Delta9 position (elaidic acid, trans-9-octadecenoic acid), fatty acid esters (methyl linoleate, monolinolein, dilinolein, and trilinolein), and conjugated fatty acids (conjugated linoleic acids), as well as fatty acids with other chain lengths, such as myristoleic acid (cis-9-tetradecenoic acid), arachidonic acid (cis-5,cis-8,cis-11,cis-14-eicosatetraenoic acid), EPA (cis-5,cis-8,cis-11,cis-14,cis-17-eicosapentaenoic acid), DHA (cis-4,cis-7,cis-10,cis-13,cis-16,cis-19-docosahexaenoic acid) and fatty acids with a cis carbon-carbon double bond at Delta11 position, such as cis-vaccenic acid and cis-11-octadecenoic acid, or fatty alcohols, such as linoleyl alcohol. Is not able to dehydrate 12- hydroxy, 3-hydroxy, and 9-hydroxy fatty acids.",Belongs to the carotenoid/retinoid oxidoreductase family,No,Vague,No,Vague,Vague,not-Yes,GO:0071949; GO:0050151,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.2761,0.2761,0.2761,0.2761,0.2761,5,0.2761,0.2157,no
CLAHY_LACPN,G9MAP1,ProtTale,Bacteria,569,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-HY catalyzes the hydration and dehydration steps in the production of 10-hydroxy-cis-12-octadecenoate, trans-10,cis-12-CLA, cis-9,trans-11-CLA, trans-9,trans-11-CLA, oleate and trans-10-octadecenoate during linoleate metabolism. Is also able to hydrate palmitoleic acid (cis-9-hexadecenoic acid), oleic acid, alpha- linolenic acid, gamma-linolenic acid, and stearidonic acid into the corresponding 10-hydroxy fatty acids, and dehydrate 10-hydroxy- cis-12,cis-15-octadecadienoic acid, 10-hydroxy-cis-6,cis-12- octadecadienoic acid, and 10-hydroxyoctadecanoic acid into the corresponding fatty acids with cis double bonds at the Delta9 position. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome. Shows regioselectivity for Delta9 double bond hydration, generating C10 hydroxy groups in the (S)-configuration with high enantioselectivity, when another double bond is in position 12. Is not able to hydrate fatty acids with a trans carbon-carbon double bond at Delta9 position (elaidic acid, trans-9-octadecenoic acid), fatty acid esters (methyl linoleate, monolinolein, dilinolein, and trilinolein), and conjugated fatty acids (conjugated linoleic acids), as well as fatty acids with other chain lengths, such as myristoleic acid (cis-9-tetradecenoic acid), arachidonic acid (cis-5,cis-8,cis-11,cis-14-eicosatetraenoic acid), EPA (cis-5,cis-8,cis-11,cis-14,cis-17-eicosapentaenoic acid), DHA (cis-4,cis-7,cis-10,cis-13,cis-16,cis-19-docosahexaenoic acid) and fatty acids with a cis carbon-carbon double bond at Delta11 position, such as cis-vaccenic acid and cis-11-octadecenoic acid, or fatty alcohols, such as linoleyl alcohol. Is not able to dehydrate 12- hydroxy, 3-hydroxy, and 9-hydroxy fatty acids.","Involved in the biosynthesis of unsaturated fatty acids. Catalyzes the conversion of (9Z)-octadecenoyl-CoA (18:1-CoA) to (9Z,12Z)-octadecadienoyl-CoA (18:2-CoA).",Maybe,No,No,Maybe,Maybe,not-Yes,GO:0071949; GO:0050151,GO:0045485,GO:0016491,GO:0016717,GO:0045300,GO:0016717,0.1838,0.2761,0.1838,0.1563,0.1838,5,0.1968,0.2157,no
CLAHY_LACPN,G9MAP1,Protein2Text,Bacteria,569,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-HY catalyzes the hydration and dehydration steps in the production of 10-hydroxy-cis-12-octadecenoate, trans-10,cis-12-CLA, cis-9,trans-11-CLA, trans-9,trans-11-CLA, oleate and trans-10-octadecenoate during linoleate metabolism. Is also able to hydrate palmitoleic acid (cis-9-hexadecenoic acid), oleic acid, alpha- linolenic acid, gamma-linolenic acid, and stearidonic acid into the corresponding 10-hydroxy fatty acids, and dehydrate 10-hydroxy- cis-12,cis-15-octadecadienoic acid, 10-hydroxy-cis-6,cis-12- octadecadienoic acid, and 10-hydroxyoctadecanoic acid into the corresponding fatty acids with cis double bonds at the Delta9 position. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome. Shows regioselectivity for Delta9 double bond hydration, generating C10 hydroxy groups in the (S)-configuration with high enantioselectivity, when another double bond is in position 12. Is not able to hydrate fatty acids with a trans carbon-carbon double bond at Delta9 position (elaidic acid, trans-9-octadecenoic acid), fatty acid esters (methyl linoleate, monolinolein, dilinolein, and trilinolein), and conjugated fatty acids (conjugated linoleic acids), as well as fatty acids with other chain lengths, such as myristoleic acid (cis-9-tetradecenoic acid), arachidonic acid (cis-5,cis-8,cis-11,cis-14-eicosatetraenoic acid), EPA (cis-5,cis-8,cis-11,cis-14,cis-17-eicosapentaenoic acid), DHA (cis-4,cis-7,cis-10,cis-13,cis-16,cis-19-docosahexaenoic acid) and fatty acids with a cis carbon-carbon double bond at Delta11 position, such as cis-vaccenic acid and cis-11-octadecenoic acid, or fatty alcohols, such as linoleyl alcohol. Is not able to dehydrate 12- hydroxy, 3-hydroxy, and 9-hydroxy fatty acids.","This protein is involved in the molecular function of light-harvesting complex, specifically in the process of absorbing light energy and transferring it to the reaction center in photosynthesis.",No,No,No,No,No,not-Yes,GO:0071949; GO:0050151,,GO:0016168,,GO:0016168,GO:0016168,,0.1867,,0.1867,0.1867,3,0.1867,0.2157,no
CLAHY_LACPN,G9MAP1,Reference,Bacteria,569,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-HY catalyzes the hydration and dehydration steps in the production of 10-hydroxy-cis-12-octadecenoate, trans-10,cis-12-CLA, cis-9,trans-11-CLA, trans-9,trans-11-CLA, oleate and trans-10-octadecenoate during linoleate metabolism. Is also able to hydrate palmitoleic acid (cis-9-hexadecenoic acid), oleic acid, alpha- linolenic acid, gamma-linolenic acid, and stearidonic acid into the corresponding 10-hydroxy fatty acids, and dehydrate 10-hydroxy- cis-12,cis-15-octadecadienoic acid, 10-hydroxy-cis-6,cis-12- octadecadienoic acid, and 10-hydroxyoctadecanoic acid into the corresponding fatty acids with cis double bonds at the Delta9 position. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome. Shows regioselectivity for Delta9 double bond hydration, generating C10 hydroxy groups in the (S)-configuration with high enantioselectivity, when another double bond is in position 12. Is not able to hydrate fatty acids with a trans carbon-carbon double bond at Delta9 position (elaidic acid, trans-9-octadecenoic acid), fatty acid esters (methyl linoleate, monolinolein, dilinolein, and trilinolein), and conjugated fatty acids (conjugated linoleic acids), as well as fatty acids with other chain lengths, such as myristoleic acid (cis-9-tetradecenoic acid), arachidonic acid (cis-5,cis-8,cis-11,cis-14-eicosatetraenoic acid), EPA (cis-5,cis-8,cis-11,cis-14,cis-17-eicosapentaenoic acid), DHA (cis-4,cis-7,cis-10,cis-13,cis-16,cis-19-docosahexaenoic acid) and fatty acids with a cis carbon-carbon double bond at Delta11 position, such as cis-vaccenic acid and cis-11-octadecenoic acid, or fatty alcohols, such as linoleyl alcohol. Is not able to dehydrate 12- hydroxy, 3-hydroxy, and 9-hydroxy fatty acids.","Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-HY catalyzes the hydration and dehydration steps in the production of 10-hydroxy-cis-12-octadecenoate, trans-10,cis-12-CLA, cis-9,trans-11-CLA, trans-9,trans-11-CLA, oleate and trans-10-octadecenoate during linoleate metabolism. Is also able to hydrate palmitoleic acid (cis-9-hexadecenoic acid), oleic acid, alpha- linolenic acid, gamma-linolenic acid, and stearidonic acid into the corresponding 10-hydroxy fatty acids, and dehydrate 10-hydroxy- cis-12,cis-15-octadecadienoic acid, 10-hydroxy-cis-6,cis-12- octadecadienoic acid, and 10-hydroxyoctadecanoic acid into the corresponding fatty acids with cis double bonds at the Delta9 position. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome. Shows regioselectivity for Delta9 double bond hydration, generating C10 hydroxy groups in the (S)-configuration with high enantioselectivity, when another double bond is in position 12. Is not able to hydrate fatty acids with a trans carbon-carbon double bond at Delta9 position (elaidic acid, trans-9-octadecenoic acid), fatty acid esters (methyl linoleate, monolinolein, dilinolein, and trilinolein), and conjugated fatty acids (conjugated linoleic acids), as well as fatty acids with other chain lengths, such as myristoleic acid (cis-9-tetradecenoic acid), arachidonic acid (cis-5,cis-8,cis-11,cis-14-eicosatetraenoic acid), EPA (cis-5,cis-8,cis-11,cis-14,cis-17-eicosapentaenoic acid), DHA (cis-4,cis-7,cis-10,cis-13,cis-16,cis-19-docosahexaenoic acid) and fatty acids with a cis carbon-carbon double bond at Delta11 position, such as cis-vaccenic acid and cis-11-octadecenoic acid, or fatty alcohols, such as linoleyl alcohol. Is not able to dehydrate 12- hydroxy, 3-hydroxy, and 9-hydroxy fatty acids.",,,,,,,GO:0071949; GO:0050151,GO:0016836,GO:0016836,GO:0016836,GO:0016836,GO:0016491,0.599,0.599,0.599,0.599,0.2761,5,0.5344,0.2157,no
AAE1_CANSA,H9A1V3,ESM2Text,Eukaryota,720,"Involved in the biosynthesis of cannabinoid-related terpenophenolic natural products, which have pharmacological activity. Acyl-activating enzyme that catalyzes the conversion of hexanoic acid to hexanoyl-CoA, precursor of the cannabinoid pathway. Can also activate other fatty acids including heptanoate, octanoate and nonanoate.",May act as an acid--thiol ligase that activates carboxylic acids by forming acyl-CoAs.,Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0005524; GO:0016405,GO:0016874,GO:0016877,GO:0016878,GO:0016878,GO:0016878,0.4889,0.5856,0.4894,0.4894,0.4894,5,0.5085,0.2692,no
AAE1_CANSA,H9A1V3,Prot2Text,Eukaryota,720,"Involved in the biosynthesis of cannabinoid-related terpenophenolic natural products, which have pharmacological activity. Acyl-activating enzyme that catalyzes the conversion of hexanoic acid to hexanoyl-CoA, precursor of the cannabinoid pathway. Can also activate other fatty acids including heptanoate, octanoate and nonanoate.","May be involved in the peroxisomal activation of 2,4-dichlorophenoxybutyric acid (2,4-DB), a precursor of active auxins that inhibit root growth.",Maybe,Maybe,Maybe,No,No,not-Yes,GO:0005524; GO:0016405,,,,,,,,,,,0,,0.2692,no
AAE1_CANSA,H9A1V3,ProtT3,Eukaryota,720,"Involved in the biosynthesis of cannabinoid-related terpenophenolic natural products, which have pharmacological activity. Acyl-activating enzyme that catalyzes the conversion of hexanoic acid to hexanoyl-CoA, precursor of the cannabinoid pathway. Can also activate other fatty acids including heptanoate, octanoate and nonanoate.",Peroxisome. Belongs to the ATP-dependent AMP-binding enzyme family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0016405,GO:0016878,GO:0016405,GO:0016874; GO:0005524,GO:0016878; GO:0005524,GO:0016878,0.4894,0.6878,0.8449,0.8513,0.4894,5,0.6726,0.2692,no
AAE1_CANSA,H9A1V3,ProtTale,Eukaryota,720,"Involved in the biosynthesis of cannabinoid-related terpenophenolic natural products, which have pharmacological activity. Acyl-activating enzyme that catalyzes the conversion of hexanoic acid to hexanoyl-CoA, precursor of the cannabinoid pathway. Can also activate other fatty acids including heptanoate, octanoate and nonanoate.",Catalyzes the formation of 2-oxoadipate-4-phosphate (OAP) from acetyl-CoA and ATP. Also catalyzes the ATP-dependent synthesis of 2-oxoadipate from malonyl-CoA and ATP.,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0016405,GO:0016874,GO:0016874; GO:0005524,GO:0016874; GO:0005524,,GO:0016874,0.4889,0.8449,0.8449,,0.4889,4,0.6669,0.2692,no
AAE1_CANSA,H9A1V3,Protein2Text,Eukaryota,720,"Involved in the biosynthesis of cannabinoid-related terpenophenolic natural products, which have pharmacological activity. Acyl-activating enzyme that catalyzes the conversion of hexanoic acid to hexanoyl-CoA, precursor of the cannabinoid pathway. Can also activate other fatty acids including heptanoate, octanoate and nonanoate.",The molecular function of this protein is an acyltransferase.,No,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0005524; GO:0016405,GO:0016747,GO:0016746,GO:0016747,GO:0016746,GO:0016746,0.2039,0.2435,0.2039,0.2435,0.2435,5,0.2277,0.2692,no
AAE1_CANSA,H9A1V3,Reference,Eukaryota,720,"Involved in the biosynthesis of cannabinoid-related terpenophenolic natural products, which have pharmacological activity. Acyl-activating enzyme that catalyzes the conversion of hexanoic acid to hexanoyl-CoA, precursor of the cannabinoid pathway. Can also activate other fatty acids including heptanoate, octanoate and nonanoate.","Involved in the biosynthesis of cannabinoid-related terpenophenolic natural products, which have pharmacological activity. Acyl-activating enzyme that catalyzes the conversion of hexanoic acid to hexanoyl-CoA, precursor of the cannabinoid pathway. Can also activate other fatty acids including heptanoate, octanoate and nonanoate.",,,,,,,GO:0005524; GO:0016405,GO:0016878; GO:0005524,GO:0015645,GO:0016878,GO:0003987; GO:0016874,GO:0003987; GO:0016874; GO:0005524,0.8513,0.397,0.4894,0.5796,0.8462,5,0.6327,0.2692,no
MBDH_SERMA,H9XP47,ESM2Text,Bacteria,251,"Catalyzes the NAD-dependent oxidation of meso-2,3-butanediol to (3R)-acetoin, and of (2S,3S)-2,3-butanediol to (3S)-acetoin, with much lower efficiency. Can also oxidize several primary alcohols such as glycerol, 1-2-pentanediol and 1,2-propanediol, with lower activity. Cannot use (2R,3R)-2,3- butanediol. In the presence of NADH, catalyzes the reduction of (3R)-acetoin to meso-2,3-butanediol, of (3S)-acetoin to (2S,3S)-2,3-butanediol and of diacetyl to (3S)-acetoin. No activity is detected with NADPH/NADP(+).","Catalyzes the NADP dependent reduction of 1,3,7-trihydroxycyclohexane-1,2-dione (THcHDO) to produce 1,3,7-trihydroxycyclohexane-1,2-dione (HhaDOD). Also shows activity toward benzoyl-CoA, but with a lower efficiency. Does not show detectable activity toward 1,3,7-trimethyl-2-butanone, 3-butanedione, p-nitrobenzene, p-nitrobenzene, methylene blue, p-nitroacetic acid, or benzoylglucosinolate.",No,Maybe,Maybe,No,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016491; GO:0050661,,,GO:0016491,1.0,0.7089,,,1.0,3,0.903,0.09,no
MBDH_SERMA,H9XP47,Prot2Text,Bacteria,251,"Catalyzes the NAD-dependent oxidation of meso-2,3-butanediol to (3R)-acetoin, and of (2S,3S)-2,3-butanediol to (3S)-acetoin, with much lower efficiency. Can also oxidize several primary alcohols such as glycerol, 1-2-pentanediol and 1,2-propanediol, with lower activity. Cannot use (2R,3R)-2,3- butanediol. In the presence of NADH, catalyzes the reduction of (3R)-acetoin to meso-2,3-butanediol, of (3S)-acetoin to (2S,3S)-2,3-butanediol and of diacetyl to (3S)-acetoin. No activity is detected with NADPH/NADP(+).","Involved in the modification of secondary bile acids into iso-bile acids (3beta-bile acids) via epimerization of the 3-OH group through a 3-oxo-intermediate. Catalyzes the oxidation of cholate (3beta-chol) to yield 3-oxo-3-deoxycholate (3-deoxychol). Is also able to catalyze the oxidation of cholate (3alpha-chol) to yield 3-oxo-3-deoxycholate (3-deoxycholate), and the oxidation of cholate (3alpha-chol) to yield 3-deoxycholate (3-deoxycholate), suggesting that the reaction proceeds in a sequential manner with the 2-oxoglutarate dehydrogenase/oxidase system. In vitro, the 2-oxoglutarate dehydrogenase activity of this enzyme converts cholate (3-deoxycholate) to chol (3-deoxycholate), suggesting that the reaction proceeds in a sequential manner with the 2-oxoglutarate dehydrogenase/oxidase system.",No,Maybe,Maybe,Maybe,No,not-Yes,GO:0016491,GO:0016491,,GO:0016491,GO:0016491,GO:0047044,1.0,,1.0,1.0,0.5067,4,0.8767,0.09,no
MBDH_SERMA,H9XP47,ProtT3,Bacteria,251,"Catalyzes the NAD-dependent oxidation of meso-2,3-butanediol to (3R)-acetoin, and of (2S,3S)-2,3-butanediol to (3S)-acetoin, with much lower efficiency. Can also oxidize several primary alcohols such as glycerol, 1-2-pentanediol and 1,2-propanediol, with lower activity. Cannot use (2R,3R)-2,3- butanediol. In the presence of NADH, catalyzes the reduction of (3R)-acetoin to meso-2,3-butanediol, of (3S)-acetoin to (2S,3S)-2,3-butanediol and of diacetyl to (3S)-acetoin. No activity is detected with NADPH/NADP(+).","Catalyzes the reversible reduction of 2,3-diketo-L-gulonate to 2-keto-L-gulonate. Can also catalyze the reversible oxidation of 2-keto-L-gulonate to 2,3- diketo-L-gulonate. Belongs to the short-chain dehydrogenases/reductases (SDR) family",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,GO:0016616,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.6897,1.0,1.0,1.0,1.0,5,0.9379,0.09,no
MBDH_SERMA,H9XP47,ProtTale,Bacteria,251,"Catalyzes the NAD-dependent oxidation of meso-2,3-butanediol to (3R)-acetoin, and of (2S,3S)-2,3-butanediol to (3S)-acetoin, with much lower efficiency. Can also oxidize several primary alcohols such as glycerol, 1-2-pentanediol and 1,2-propanediol, with lower activity. Cannot use (2R,3R)-2,3- butanediol. In the presence of NADH, catalyzes the reduction of (3R)-acetoin to meso-2,3-butanediol, of (3S)-acetoin to (2S,3S)-2,3-butanediol and of diacetyl to (3S)-acetoin. No activity is detected with NADPH/NADP(+).",Catalyzes the NAD(+)-dependent oxidation of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate.,No,Maybe,Maybe,No,No,not-Yes,GO:0016491,GO:0003856,GO:0003856,GO:0003856,GO:0003856,GO:0003856,0.3552,0.3552,0.3552,0.3552,0.3552,5,0.3552,0.09,no
MBDH_SERMA,H9XP47,Protein2Text,Bacteria,251,"Catalyzes the NAD-dependent oxidation of meso-2,3-butanediol to (3R)-acetoin, and of (2S,3S)-2,3-butanediol to (3S)-acetoin, with much lower efficiency. Can also oxidize several primary alcohols such as glycerol, 1-2-pentanediol and 1,2-propanediol, with lower activity. Cannot use (2R,3R)-2,3- butanediol. In the presence of NADH, catalyzes the reduction of (3R)-acetoin to meso-2,3-butanediol, of (3S)-acetoin to (2S,3S)-2,3-butanediol and of diacetyl to (3S)-acetoin. No activity is detected with NADPH/NADP(+).","The molecular function of this protein is a type of enzyme activity, specifically a dehydrogenase activity. It is involved in catalyzing the conversion of a substrate, likely a sugar or sugar derivative, into a product with a different oxidation state. More specifically, it is likely involved in the oxidation of a sugar or sugar derivative, which is a common function of enzymes in this family.",Vague,Vague,Maybe,Vague,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016491,,GO:0016491,GO:0016491,1.0,1.0,,1.0,1.0,4,1.0,0.09,no
MBDH_SERMA,H9XP47,Reference,Bacteria,251,"Catalyzes the NAD-dependent oxidation of meso-2,3-butanediol to (3R)-acetoin, and of (2S,3S)-2,3-butanediol to (3S)-acetoin, with much lower efficiency. Can also oxidize several primary alcohols such as glycerol, 1-2-pentanediol and 1,2-propanediol, with lower activity. Cannot use (2R,3R)-2,3- butanediol. In the presence of NADH, catalyzes the reduction of (3R)-acetoin to meso-2,3-butanediol, of (3S)-acetoin to (2S,3S)-2,3-butanediol and of diacetyl to (3S)-acetoin. No activity is detected with NADPH/NADP(+).","Catalyzes the NAD-dependent oxidation of meso-2,3-butanediol to (3R)-acetoin, and of (2S,3S)-2,3-butanediol to (3S)-acetoin, with much lower efficiency. Can also oxidize several primary alcohols such as glycerol, 1-2-pentanediol and 1,2-propanediol, with lower activity. Cannot use (2R,3R)-2,3- butanediol. In the presence of NADH, catalyzes the reduction of (3R)-acetoin to meso-2,3-butanediol, of (3S)-acetoin to (2S,3S)-2,3-butanediol and of diacetyl to (3S)-acetoin. No activity is detected with NADPH/NADP(+).",,,,,,,GO:0016491,GO:0016614; GO:0051287,GO:0016491; GO:0051287,GO:0004022; GO:0051287,GO:0016491; GO:0000721,GO:0016614,0.5852,0.7089,0.4009,0.8673,0.8145,5,0.6754,0.09,no
B12GT_IGNAJ,I0AIT9,ESM2Text,Bacteria,716,"Glycosyltransferase acting on beta-1,2-glucooligosaccharides. Catalyzes the transfer of a glucosyl residue from the non-reducing end of a 1,2-beta-D-glucan to a glucose residue of an acceptor molecule, forming a beta-1,2-glucosidic bond. The beta-1,2-linked glucose dimer sophorose is the preferred donor in vitro. Has a very broad specificity for the acceptor and can act on various aryl- and alkyl- glucosides. Does not show any hydrolytic activity.","Has hydrolytic activity against p-nitrophenyl-beta-D-galactopyranoside (pNPG), p-nitrophenyl-beta-D-fucopyranoside (pNPG-beta-D-Fucopyranoside), p-nitrophenyl-beta-D-galactopyranoside (pNPG-beta-D-Galp), p-nitrophenyl-beta-D-mannopyranoside (pNPG-beta-D-Manp), p-nitrophenyl-beta-D-glucopyranoside (pNPG-beta-D-GlcNAc), p-nitrophenyl-beta-D-glucopyranoside (pNPG-beta-D-GlcNAc), p-nitrophenyl-beta-D-galactopyranoside (pNPG-beta-D-Galp), p-nitrophenyl-beta-D-glucopyranoside (pNPG-beta-D-GlcNAc), p-nitrophenyl-beta-D-mannopyranoside",No,No,No,No,Maybe,not-Yes,GO:0016757; GO:0004553,GO:0004565,GO:0004565; GO:0004553,GO:0004565,GO:0004565,GO:0004565,0.5867,0.7706,0.5867,0.5867,0.5867,5,0.6235,0.2825,no
B12GT_IGNAJ,I0AIT9,Prot2Text,Bacteria,716,"Glycosyltransferase acting on beta-1,2-glucooligosaccharides. Catalyzes the transfer of a glucosyl residue from the non-reducing end of a 1,2-beta-D-glucan to a glucose residue of an acceptor molecule, forming a beta-1,2-glucosidic bond. The beta-1,2-linked glucose dimer sophorose is the preferred donor in vitro. Has a very broad specificity for the acceptor and can act on various aryl- and alkyl- glucosides. Does not show any hydrolytic activity.","Involved in the degradation of rhamnogalacturonan derived from plant cell walls. Catalyzes the hydrolysis of terminal non-reducing beta-galacturonic acid residues in birchwood xylan, a major component of the cereal birchwood xylan. Possesses beta-fucosidase activity on xylan, aryl-beta-galacturonides and p-nitrophenyl-beta-galacturonide (PNPG).",No,No,No,No,No,not-Yes,GO:0016757; GO:0004553,GO:0004553,,GO:0004553,GO:0004553,GO:0004566,0.7761,,0.7761,0.7761,0.5867,4,0.7288,0.2825,no
B12GT_IGNAJ,I0AIT9,ProtT3,Bacteria,716,"Glycosyltransferase acting on beta-1,2-glucooligosaccharides. Catalyzes the transfer of a glucosyl residue from the non-reducing end of a 1,2-beta-D-glucan to a glucose residue of an acceptor molecule, forming a beta-1,2-glucosidic bond. The beta-1,2-linked glucose dimer sophorose is the preferred donor in vitro. Has a very broad specificity for the acceptor and can act on various aryl- and alkyl- glucosides. Does not show any hydrolytic activity.",Belongs to the glycosyl hydrolase 35 family,Vague,Vague,No,Vague,Vague,not-Yes,GO:0016757; GO:0004553,GO:0004565,GO:0004565,GO:0004565,GO:0004565,GO:0016798,0.5867,0.5867,0.5867,0.5867,0.6912,5,0.6076,0.2825,no
B12GT_IGNAJ,I0AIT9,ProtTale,Bacteria,716,"Glycosyltransferase acting on beta-1,2-glucooligosaccharides. Catalyzes the transfer of a glucosyl residue from the non-reducing end of a 1,2-beta-D-glucan to a glucose residue of an acceptor molecule, forming a beta-1,2-glucosidic bond. The beta-1,2-linked glucose dimer sophorose is the preferred donor in vitro. Has a very broad specificity for the acceptor and can act on various aryl- and alkyl- glucosides. Does not show any hydrolytic activity.","Catalyzes the hydrolysis of terminal (1->4)-beta-D-galactosyl residues in beta-D-galactosides, galactomannans and galactooligosaccharides (GOS) to produce D-galactose and D-galactobiose, which can be used as substrates by the colonic microbiota. Gets its name from its ability to hydrolyze galacto-alpha-1,4-D-galactose (lacto-N-biose), galacto-alpha-1,3-D-galactose (lacto-N-triose) and galacto",Vague,Vague,Vague,Vague,No,not-Yes,GO:0016757; GO:0004553,GO:0004565,GO:0004565,GO:0004565,GO:0004565,GO:0004565,0.5867,0.5867,0.5867,0.5867,0.5867,5,0.5867,0.2825,no
B12GT_IGNAJ,I0AIT9,Protein2Text,Bacteria,716,"Glycosyltransferase acting on beta-1,2-glucooligosaccharides. Catalyzes the transfer of a glucosyl residue from the non-reducing end of a 1,2-beta-D-glucan to a glucose residue of an acceptor molecule, forming a beta-1,2-glucosidic bond. The beta-1,2-linked glucose dimer sophorose is the preferred donor in vitro. Has a very broad specificity for the acceptor and can act on various aryl- and alkyl- glucosides. Does not show any hydrolytic activity.","This protein is a beta-galactosidase, which means it catalyzes the hydrolysis of the glycosidic bond between the beta-anomeric oxygen atom of galactose and the glycerol moiety of a glycoside, releasing free galactose.",No,No,No,No,No,not-Yes,GO:0016757; GO:0004553,GO:0004565,GO:0004565,GO:0004565,GO:0004565,GO:0004565,0.5867,0.5867,0.5867,0.5867,0.5867,5,0.5867,0.2825,no
B12GT_IGNAJ,I0AIT9,Reference,Bacteria,716,"Glycosyltransferase acting on beta-1,2-glucooligosaccharides. Catalyzes the transfer of a glucosyl residue from the non-reducing end of a 1,2-beta-D-glucan to a glucose residue of an acceptor molecule, forming a beta-1,2-glucosidic bond. The beta-1,2-linked glucose dimer sophorose is the preferred donor in vitro. Has a very broad specificity for the acceptor and can act on various aryl- and alkyl- glucosides. Does not show any hydrolytic activity.","Glycosyltransferase acting on beta-1,2-glucooligosaccharides. Catalyzes the transfer of a glucosyl residue from the non-reducing end of a 1,2-beta-D-glucan to a glucose residue of an acceptor molecule, forming a beta-1,2-glucosidic bond. The beta-1,2-linked glucose dimer sophorose is the preferred donor in vitro. Has a very broad specificity for the acceptor and can act on various aryl- and alkyl- glucosides. Does not show any hydrolytic activity.",,,,,,,GO:0016757; GO:0004553,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.7761,0.7761,0.7761,0.7761,0.7761,5,0.7761,0.2825,no
HO1_LOTJA,I3SL57,ESM2Text,Eukaryota,282,"Key enzyme in the synthesis of the chromophore of the phytochrome family of plant photoreceptors. Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Produces specifically the biliverdin IX-alpha isomer. Can form complex with heme, is ferredoxin-dependent and its activity is increased in the presence of ascorbate. May affect the plastid-to-nucleus signaling pathway by perturbing tetrapyrrole synthesis. The plastid-to- nucleus signal plays an important role in the coordinated expression of both nuclear- and chloroplast-localized genes that encode photosynthesis-related proteins. Required for efficient symbiotic nitrogen fixation (SNF) in root nodules. Responsible for heme catabolism in uninfected nodule interstitial cells (UC), preventing superoxide production under stressful conditions (e.g. nitrate exposure and darkness) and catalyzing biliverdin (BV) production in senescing green nodules.",Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Produces specifically the biliverdin IX-alpha isomer. Plays a minor role in phytochrome assembly and photomorphogenesis.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004392; GO:0046872,GO:0004392,GO:0004392,GO:0004392,GO:0004392,GO:0004392,0.6939,0.6939,0.6939,0.6939,0.6939,5,0.6939,0.215,no
HO1_LOTJA,I3SL57,Prot2Text,Eukaryota,282,"Key enzyme in the synthesis of the chromophore of the phytochrome family of plant photoreceptors. Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Produces specifically the biliverdin IX-alpha isomer. Can form complex with heme, is ferredoxin-dependent and its activity is increased in the presence of ascorbate. May affect the plastid-to-nucleus signaling pathway by perturbing tetrapyrrole synthesis. The plastid-to- nucleus signal plays an important role in the coordinated expression of both nuclear- and chloroplast-localized genes that encode photosynthesis-related proteins. Required for efficient symbiotic nitrogen fixation (SNF) in root nodules. Responsible for heme catabolism in uninfected nodule interstitial cells (UC), preventing superoxide production under stressful conditions (e.g. nitrate exposure and darkness) and catalyzing biliverdin (BV) production in senescing green nodules.",Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Produces specifically the biliverdin IX-alpha isomer. Plays a minor role in phytochrome assembly and photomorphogenesis.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004392; GO:0046872,GO:0004392,GO:0004392,GO:0004392,GO:0004392,GO:0004392,0.6939,0.6939,0.6939,0.6939,0.6939,5,0.6939,0.215,no
HO1_LOTJA,I3SL57,ProtT3,Eukaryota,282,"Key enzyme in the synthesis of the chromophore of the phytochrome family of plant photoreceptors. Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Produces specifically the biliverdin IX-alpha isomer. Can form complex with heme, is ferredoxin-dependent and its activity is increased in the presence of ascorbate. May affect the plastid-to-nucleus signaling pathway by perturbing tetrapyrrole synthesis. The plastid-to- nucleus signal plays an important role in the coordinated expression of both nuclear- and chloroplast-localized genes that encode photosynthesis-related proteins. Required for efficient symbiotic nitrogen fixation (SNF) in root nodules. Responsible for heme catabolism in uninfected nodule interstitial cells (UC), preventing superoxide production under stressful conditions (e.g. nitrate exposure and darkness) and catalyzing biliverdin (BV) production in senescing green nodules.","Catalyzes the opening of the heme ring at the C15-C16 bond to form biliverdin IXalpha. Plastid, chloroplast. Belongs to the heme oxygenase family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004392; GO:0046872,GO:0004392,GO:0004392,GO:0004392,GO:0004392,GO:0004392,0.6939,0.6939,0.6939,0.6939,0.6939,5,0.6939,0.215,no
HO1_LOTJA,I3SL57,ProtTale,Eukaryota,282,"Key enzyme in the synthesis of the chromophore of the phytochrome family of plant photoreceptors. Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Produces specifically the biliverdin IX-alpha isomer. Can form complex with heme, is ferredoxin-dependent and its activity is increased in the presence of ascorbate. May affect the plastid-to-nucleus signaling pathway by perturbing tetrapyrrole synthesis. The plastid-to- nucleus signal plays an important role in the coordinated expression of both nuclear- and chloroplast-localized genes that encode photosynthesis-related proteins. Required for efficient symbiotic nitrogen fixation (SNF) in root nodules. Responsible for heme catabolism in uninfected nodule interstitial cells (UC), preventing superoxide production under stressful conditions (e.g. nitrate exposure and darkness) and catalyzing biliverdin (BV) production in senescing green nodules.",Synthesizes heme B from protoporphyrin IX.,Vague,No,No,No,No,not-Yes,GO:0004392; GO:0046872,GO:0004325,GO:0004325,GO:0004325,GO:0004325,GO:0004325,0.2151,0.2151,0.2151,0.2151,0.2151,5,0.2151,0.215,no
HO1_LOTJA,I3SL57,Protein2Text,Eukaryota,282,"Key enzyme in the synthesis of the chromophore of the phytochrome family of plant photoreceptors. Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Produces specifically the biliverdin IX-alpha isomer. Can form complex with heme, is ferredoxin-dependent and its activity is increased in the presence of ascorbate. May affect the plastid-to-nucleus signaling pathway by perturbing tetrapyrrole synthesis. The plastid-to- nucleus signal plays an important role in the coordinated expression of both nuclear- and chloroplast-localized genes that encode photosynthesis-related proteins. Required for efficient symbiotic nitrogen fixation (SNF) in root nodules. Responsible for heme catabolism in uninfected nodule interstitial cells (UC), preventing superoxide production under stressful conditions (e.g. nitrate exposure and darkness) and catalyzing biliverdin (BV) production in senescing green nodules.","The molecular function of this protein is not explicitly stated in the provided information. However, based on its classification as a protein involved in the biosynthesis of flavonoids, a type of plant secondary metabolite, it is likely to be involved in a process related to the synthesis or modification of flavonoids.",No,No,No,No,No,not-Yes,GO:0004392; GO:0046872,,,,,,,,,,,0,,0.215,no
HO1_LOTJA,I3SL57,Reference,Eukaryota,282,"Key enzyme in the synthesis of the chromophore of the phytochrome family of plant photoreceptors. Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Produces specifically the biliverdin IX-alpha isomer. Can form complex with heme, is ferredoxin-dependent and its activity is increased in the presence of ascorbate. May affect the plastid-to-nucleus signaling pathway by perturbing tetrapyrrole synthesis. The plastid-to- nucleus signal plays an important role in the coordinated expression of both nuclear- and chloroplast-localized genes that encode photosynthesis-related proteins. Required for efficient symbiotic nitrogen fixation (SNF) in root nodules. Responsible for heme catabolism in uninfected nodule interstitial cells (UC), preventing superoxide production under stressful conditions (e.g. nitrate exposure and darkness) and catalyzing biliverdin (BV) production in senescing green nodules.","Key enzyme in the synthesis of the chromophore of the phytochrome family of plant photoreceptors. Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Produces specifically the biliverdin IX-alpha isomer. Can form complex with heme, is ferredoxin-dependent and its activity is increased in the presence of ascorbate. May affect the plastid-to-nucleus signaling pathway by perturbing tetrapyrrole synthesis. The plastid-to- nucleus signal plays an important role in the coordinated expression of both nuclear- and chloroplast-localized genes that encode photosynthesis-related proteins. Required for efficient symbiotic nitrogen fixation (SNF) in root nodules. Responsible for heme catabolism in uninfected nodule interstitial cells (UC), preventing superoxide production under stressful conditions (e.g. nitrate exposure and darkness) and catalyzing biliverdin (BV) production in senescing green nodules.",,,,,,,GO:0004392; GO:0046872,GO:0004392,GO:0004392; GO:0020037; GO:0005506,GO:0004392; GO:0020037,GO:0004392; GO:0020037; GO:0005506,GO:0004392; GO:0005506; GO:0020037,0.6939,0.7652,0.6422,0.7652,0.7652,5,0.7263,0.215,no
CGDA_EUBC6,I5AX50,ESM2Text,Bacteria,290,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C6-glycosylated compounds 3''-dehydroisoorientin (3''-oxo- homoorientin) and 3''-dehydroisovitexin (3''-oxo-isovitexin).,"Involved in the degradation of the pyridine ring of trigonelline (TG; N-acetyltrideca-2,5-diaminobutyric acid) and trigone to produce the carbon skeleton of trigonelline. Catalyzes the reversible isomerization between the ketopantoate enol I (KPI-I) and trigonelline via a 1,3-propanediol intermediate. It is strictly specific for KPI-I.",No,No,No,No,No,not-Yes,GO:0016829; GO:0046872,GO:0003755,GO:0003755,GO:0003755,GO:0003755,GO:0003755,0.2876,0.2876,0.2876,0.2876,0.2876,5,0.2876,0.1436,no
CGDA_EUBC6,I5AX50,Prot2Text,Bacteria,290,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C6-glycosylated compounds 3''-dehydroisoorientin (3''-oxo- homoorientin) and 3''-dehydroisovitexin (3''-oxo-isovitexin).,"Catalyzes the epimerization of D-erythronate to L-erythronate. Probably involved in the degradation pathway of D-threitol, that allows M.smegmatis to grow on this compound as the sole carbon source.",No,No,No,No,No,not-Yes,GO:0016829; GO:0046872,,,,,,,,,,,0,,0.1436,no
CGDA_EUBC6,I5AX50,ProtT3,Bacteria,290,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C6-glycosylated compounds 3''-dehydroisoorientin (3''-oxo- homoorientin) and 3''-dehydroisovitexin (3''-oxo-isovitexin).,Catalyzes the isomerization of L-rhamnose to L-rhamnulose. Cytoplasm. Belongs to the rhamnose isomerase family,No,No,No,No,No,not-Yes,GO:0016829; GO:0046872,,,,,,,,,,,0,,0.1436,no
CGDA_EUBC6,I5AX50,ProtTale,Bacteria,290,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C6-glycosylated compounds 3''-dehydroisoorientin (3''-oxo- homoorientin) and 3''-dehydroisovitexin (3''-oxo-isovitexin).,"Involved in the catabolism of D-xylose, a major component of hemicelluloses. Catalyzes the dehydration of D-xylulose-5-phosphate to form 2-dehydro-3-deoxy-D-arabino-heptose (DAH).",No,No,No,No,No,not-Yes,GO:0016829; GO:0046872,GO:0016829,GO:0016829,GO:0016836,GO:0016829,GO:0016836,0.7193,0.7193,0.4947,0.7193,0.4947,5,0.6295,0.1436,no
CGDA_EUBC6,I5AX50,Protein2Text,Bacteria,290,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C6-glycosylated compounds 3''-dehydroisoorientin (3''-oxo- homoorientin) and 3''-dehydroisovitexin (3''-oxo-isovitexin).,"This protein is an enzyme that catalyzes the hydrolysis of glycerol 3-phosphate (G3P) to glycerol and inorganic phosphate. It is a part of the glycerol metabolism pathway, which is crucial for energy production, lipid synthesis, and maintaining the redox balance of the cell. The enzyme is also involved in the regulation of glycerol levels in the blood and tissues, which is important for maintaining proper glucose and lipid metabolism. In addition, the enzyme has been shown to have anti-inflammatory and antioxidant properties, making it a potential therapeutic target for various diseases.",No,No,No,No,No,not-Yes,GO:0016829; GO:0046872,,,,,,,,,,,0,,0.1436,no
CGDA_EUBC6,I5AX50,Reference,Bacteria,290,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C6-glycosylated compounds 3''-dehydroisoorientin (3''-oxo- homoorientin) and 3''-dehydroisovitexin (3''-oxo-isovitexin).,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C6-glycosylated compounds 3''-dehydroisoorientin (3''-oxo- homoorientin) and 3''-dehydroisovitexin (3''-oxo-isovitexin).,,,,,,,GO:0016829; GO:0046872,GO:0016830,GO:0016830,GO:0016830,GO:0016830,GO:0016830,0.5852,0.5852,0.5852,0.5852,0.5852,5,0.5852,0.1436,no
PARG_TETTH,I6L8L7,ESM2Text,Eukaryota,457,Poly(ADP-ribose) glycohydrolase that degrades poly(ADP- ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP- ribose). Mainly acts as an exo- glycohydrolase but can act as an endo-glycohydrolase at low efficiency. Also has protein ADP-ribosylserine hydrolase activity and is able to remove the terminal monomeric ADP- ribose from modified serine residues but not from glutamate residues.,Autophagy-specific protein that functions in peroxisome biogenesis.,No,No,No,No,No,not-Yes,GO:0072570; GO:0140292; GO:0004649,,,,,,,,,,,0,,0.5589,yes
PARG_TETTH,I6L8L7,Prot2Text,Eukaryota,457,Poly(ADP-ribose) glycohydrolase that degrades poly(ADP- ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP- ribose). Mainly acts as an exo- glycohydrolase but can act as an endo-glycohydrolase at low efficiency. Also has protein ADP-ribosylserine hydrolase activity and is able to remove the terminal monomeric ADP- ribose from modified serine residues but not from glutamate residues.,Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. Poly(ADP-ribose) metabolism is required for maintenance of the normal function of neuronal cells.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0072570; GO:0140292; GO:0004649,GO:0004649,GO:0004649,GO:0004649,GO:0004649,GO:0004649,0.6423,0.6423,0.6423,0.6423,0.6423,5,0.6423,0.5589,yes
PARG_TETTH,I6L8L7,ProtT3,Eukaryota,457,Poly(ADP-ribose) glycohydrolase that degrades poly(ADP- ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP- ribose). Mainly acts as an exo- glycohydrolase but can act as an endo-glycohydrolase at low efficiency. Also has protein ADP-ribosylserine hydrolase activity and is able to remove the terminal monomeric ADP- ribose from modified serine residues but not from glutamate residues.,Belongs to the arginase family,Vague,No,No,No,Vague,not-Yes,GO:0072570; GO:0140292; GO:0004649,GO:0004053,GO:0004053,GO:0004053,GO:0004053,GO:0004053,0.2745,0.2745,0.2745,0.2745,0.2745,5,0.2745,0.5589,yes
PARG_TETTH,I6L8L7,ProtTale,Eukaryota,457,Poly(ADP-ribose) glycohydrolase that degrades poly(ADP- ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP- ribose). Mainly acts as an exo- glycohydrolase but can act as an endo-glycohydrolase at low efficiency. Also has protein ADP-ribosylserine hydrolase activity and is able to remove the terminal monomeric ADP- ribose from modified serine residues but not from glutamate residues.,Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0072570; GO:0140292; GO:0004649,GO:0004649,GO:0004649,GO:0004649,GO:0004649,GO:0004649,0.6423,0.6423,0.6423,0.6423,0.6423,5,0.6423,0.5589,yes
PARG_TETTH,I6L8L7,Protein2Text,Eukaryota,457,Poly(ADP-ribose) glycohydrolase that degrades poly(ADP- ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP- ribose). Mainly acts as an exo- glycohydrolase but can act as an endo-glycohydrolase at low efficiency. Also has protein ADP-ribosylserine hydrolase activity and is able to remove the terminal monomeric ADP- ribose from modified serine residues but not from glutamate residues.,"The molecular function of this protein is a transferase, specifically a poly-ADP-ribose transferase (PARP), which is involved in DNA repair and genomic stability.",No,No,No,No,Maybe,not-Yes,GO:0072570; GO:0140292; GO:0004649,GO:0003950,GO:0003950,GO:0003950,GO:0003950,GO:0003950,0.1802,0.1802,0.1802,0.1802,0.1802,5,0.1802,0.5589,yes
PARG_TETTH,I6L8L7,Reference,Eukaryota,457,Poly(ADP-ribose) glycohydrolase that degrades poly(ADP- ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP- ribose). Mainly acts as an exo- glycohydrolase but can act as an endo-glycohydrolase at low efficiency. Also has protein ADP-ribosylserine hydrolase activity and is able to remove the terminal monomeric ADP- ribose from modified serine residues but not from glutamate residues.,Poly(ADP-ribose) glycohydrolase that degrades poly(ADP- ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP- ribose). Mainly acts as an exo- glycohydrolase but can act as an endo-glycohydrolase at low efficiency. Also has protein ADP-ribosylserine hydrolase activity and is able to remove the terminal monomeric ADP- ribose from modified serine residues but not from glutamate residues.,,,,,,,GO:0072570; GO:0140292; GO:0004649,GO:0004649,GO:0004649; GO:0140657,GO:0004649,GO:0016787; GO:0004649,GO:0004649,0.6423,0.5698,0.6423,0.6575,0.6423,5,0.6308,0.5589,yes
RDMTR_MYCTU,I6XFS7,ESM2Text,Bacteria,188,"SAM-dependent methyltransferase that binds both to RNA and DNA. Specifically methylates the guanine in position 966 of 16S rRNA in the 30S particle. In addition, can methylate and modulate host cellular DNA within an infected mammalian cell, altering the host epigenetic machinery. Binds to specific host DNA sequences and methylates cytosines predominantly in a non-CpG context.",Specifically methylates the guanine in position 966 of 16S rRNA in the assembled 30S particle.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0052913; GO:0003676,GO:0008168,GO:0008649,GO:0008649,GO:0008649,GO:0008168,0.3832,0.5545,0.5545,0.5545,0.3832,5,0.486,0.6684,yes
RDMTR_MYCTU,I6XFS7,Prot2Text,Bacteria,188,"SAM-dependent methyltransferase that binds both to RNA and DNA. Specifically methylates the guanine in position 966 of 16S rRNA in the 30S particle. In addition, can methylate and modulate host cellular DNA within an infected mammalian cell, altering the host epigenetic machinery. Binds to specific host DNA sequences and methylates cytosines predominantly in a non-CpG context.",Specifically methylates the guanine in position 966 of 16S rRNA in the assembled 30S particle.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0052913; GO:0003676,GO:0008649,GO:0008649,GO:0008168,GO:0008168,GO:0008649,0.5545,0.5545,0.3832,0.3832,0.5545,5,0.486,0.6684,yes
RDMTR_MYCTU,I6XFS7,ProtT3,Bacteria,188,"SAM-dependent methyltransferase that binds both to RNA and DNA. Specifically methylates the guanine in position 966 of 16S rRNA in the 30S particle. In addition, can methylate and modulate host cellular DNA within an infected mammalian cell, altering the host epigenetic machinery. Binds to specific host DNA sequences and methylates cytosines predominantly in a non-CpG context.",Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. Belongs to the methyltransferase superfamily. RsmI family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0052913; GO:0003676,GO:0008168,GO:0008173,GO:0070042,GO:0070040,GO:0008649,0.3832,0.4755,0.5054,0.4405,0.5545,5,0.4718,0.6684,yes
RDMTR_MYCTU,I6XFS7,ProtTale,Bacteria,188,"SAM-dependent methyltransferase that binds both to RNA and DNA. Specifically methylates the guanine in position 966 of 16S rRNA in the 30S particle. In addition, can methylate and modulate host cellular DNA within an infected mammalian cell, altering the host epigenetic machinery. Binds to specific host DNA sequences and methylates cytosines predominantly in a non-CpG context.",Specifically methylates the guanine in position 966 of 16S rRNA in the assembled 30S particle.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0052913; GO:0003676,GO:0008649,GO:0008168,GO:0008649,GO:0008168,GO:0008649,0.5545,0.3832,0.5545,0.3832,0.5545,5,0.486,0.6684,yes
RDMTR_MYCTU,I6XFS7,Protein2Text,Bacteria,188,"SAM-dependent methyltransferase that binds both to RNA and DNA. Specifically methylates the guanine in position 966 of 16S rRNA in the 30S particle. In addition, can methylate and modulate host cellular DNA within an infected mammalian cell, altering the host epigenetic machinery. Binds to specific host DNA sequences and methylates cytosines predominantly in a non-CpG context.","The molecular function of this protein is a methyltransferase, which means it adds a methyl group to a target molecule. Specifically, it is a 2-thiolation of 5-methyluridine (m5U) at position 34 (m5U34) of transfer-messenger RNA (tmRNA).",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0052913; GO:0003676,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.3832,0.3832,0.3832,0.3832,0.3832,5,0.3832,0.6684,yes
RDMTR_MYCTU,I6XFS7,Reference,Bacteria,188,"SAM-dependent methyltransferase that binds both to RNA and DNA. Specifically methylates the guanine in position 966 of 16S rRNA in the 30S particle. In addition, can methylate and modulate host cellular DNA within an infected mammalian cell, altering the host epigenetic machinery. Binds to specific host DNA sequences and methylates cytosines predominantly in a non-CpG context.","SAM-dependent methyltransferase that binds both to RNA and DNA. Specifically methylates the guanine in position 966 of 16S rRNA in the 30S particle. In addition, can methylate and modulate host cellular DNA within an infected mammalian cell, altering the host epigenetic machinery. Binds to specific host DNA sequences and methylates cytosines predominantly in a non-CpG context.",,,,,,,GO:0052913; GO:0003676,GO:0008173; GO:0009008; GO:0003723; GO:0003677,GO:0008649; GO:0003886; GO:0003723; GO:0003677,GO:0008649; GO:0009008; GO:0003723; GO:0003677,GO:0008168; GO:0003723; GO:0003677,GO:0008168; GO:0003723; GO:0003677,0.6961,0.7431,0.7408,0.6825,0.6825,5,0.709,0.6684,yes
RAD6_BEAB2,J4KQN3,ESM2Text,Eukaryota,151,"Catalyzes the covalent attachment of ubiquitin to other proteins. Required for asexual and insect-pathogenic lifecycles, solar UV damage repair, and genomic expression. Plays an important role in photoreactivation of UVB- impaired conidia. The high activity of Rad6 in photoreactivation in vivo is derived from its link to a protein complex cored by the photolyase regulators WC1 and WC2 via the strong interactions of RAD6 with the E3 partner RAD18 and RAD18 with WC2.","Catalyzes the covalent attachment of ubiquitin to other proteins. Plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formation. Also involved in postreplication repair of UV-damaged DNA, in N-end rule-dependent protein degradation and in sporulation.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0070628; GO:0003697; GO:0017116; GO:0061631,GO:0004842,GO:0004842,GO:0004842,GO:0004842,GO:0061630,0.3474,0.3474,0.3474,0.3474,0.2873,5,0.3354,0.8733,yes
RAD6_BEAB2,J4KQN3,Prot2Text,Eukaryota,151,"Catalyzes the covalent attachment of ubiquitin to other proteins. Required for asexual and insect-pathogenic lifecycles, solar UV damage repair, and genomic expression. Plays an important role in photoreactivation of UVB- impaired conidia. The high activity of Rad6 in photoreactivation in vivo is derived from its link to a protein complex cored by the photolyase regulators WC1 and WC2 via the strong interactions of RAD6 with the E3 partner RAD18 and RAD18 with WC2.","Catalyzes the covalent attachment of ubiquitin to other proteins. Plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formation. Also involved in postreplication repair of UV-damaged DNA, in N-end rule-dependent protein degradation and in sporulation.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0070628; GO:0003697; GO:0017116; GO:0061631,GO:0004842,GO:0061631,GO:0061630,GO:0061630; GO:0004842,GO:0004842,0.3474,0.3918,0.2873,0.3959,0.3474,5,0.354,0.8733,yes
RAD6_BEAB2,J4KQN3,ProtT3,Eukaryota,151,"Catalyzes the covalent attachment of ubiquitin to other proteins. Required for asexual and insect-pathogenic lifecycles, solar UV damage repair, and genomic expression. Plays an important role in photoreactivation of UVB- impaired conidia. The high activity of Rad6 in photoreactivation in vivo is derived from its link to a protein complex cored by the photolyase regulators WC1 and WC2 via the strong interactions of RAD6 with the E3 partner RAD18 and RAD18 with WC2.","Catalyzes the covalent attachment of ubiquitin to other proteins. Plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formation. Also involved in postreplication repair of UV-damaged DNA, in N-end rule-dependent protein degradation and in sporulation. Cytoplasm Nucleus. Belongs to the ubiquitin",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0070628; GO:0003697; GO:0017116; GO:0061631,GO:0061631,GO:0061631,GO:0061631,GO:0061630,GO:0061631,0.3918,0.3918,0.3918,0.2873,0.3918,5,0.3709,0.8733,yes
RAD6_BEAB2,J4KQN3,ProtTale,Eukaryota,151,"Catalyzes the covalent attachment of ubiquitin to other proteins. Required for asexual and insect-pathogenic lifecycles, solar UV damage repair, and genomic expression. Plays an important role in photoreactivation of UVB- impaired conidia. The high activity of Rad6 in photoreactivation in vivo is derived from its link to a protein complex cored by the photolyase regulators WC1 and WC2 via the strong interactions of RAD6 with the E3 partner RAD18 and RAD18 with WC2.",Catalyzes the covalent attachment of ubiquitin to other proteins.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0070628; GO:0003697; GO:0017116; GO:0061631,GO:0004842,GO:0061631,GO:0061631,GO:0061631,GO:0061631,0.3474,0.3918,0.3918,0.3918,0.3918,5,0.3829,0.8733,yes
RAD6_BEAB2,J4KQN3,Protein2Text,Eukaryota,151,"Catalyzes the covalent attachment of ubiquitin to other proteins. Required for asexual and insect-pathogenic lifecycles, solar UV damage repair, and genomic expression. Plays an important role in photoreactivation of UVB- impaired conidia. The high activity of Rad6 in photoreactivation in vivo is derived from its link to a protein complex cored by the photolyase regulators WC1 and WC2 via the strong interactions of RAD6 with the E3 partner RAD18 and RAD18 with WC2.","The molecular function of this protein is likely to be involved in the ubiquitination process, specifically as an enzyme catalyzing the covalent attachment of ubiquitin to other proteins. This process is essential for various cellular activities, including protein degradation, cell cycle regulation, and signal transduction. As a ubiquitin-conjugating enzyme, this protein is expected to play a crucial role in the ubiquitination pathway, helping to modify target proteins with ubiquitin molecules.",Yes,Maybe,Yes,Yes,Maybe,Yes,GO:0005524; GO:0070628; GO:0003697; GO:0017116; GO:0061631,GO:0004842,GO:0061631,GO:0061631,GO:0061631,GO:0061631,0.3474,0.3918,0.3918,0.3918,0.3918,5,0.3829,0.8733,yes
RAD6_BEAB2,J4KQN3,Reference,Eukaryota,151,"Catalyzes the covalent attachment of ubiquitin to other proteins. Required for asexual and insect-pathogenic lifecycles, solar UV damage repair, and genomic expression. Plays an important role in photoreactivation of UVB- impaired conidia. The high activity of Rad6 in photoreactivation in vivo is derived from its link to a protein complex cored by the photolyase regulators WC1 and WC2 via the strong interactions of RAD6 with the E3 partner RAD18 and RAD18 with WC2.","Catalyzes the covalent attachment of ubiquitin to other proteins. Required for asexual and insect-pathogenic lifecycles, solar UV damage repair, and genomic expression. Plays an important role in photoreactivation of UVB- impaired conidia. The high activity of Rad6 in photoreactivation in vivo is derived from its link to a protein complex cored by the photolyase regulators WC1 and WC2 via the strong interactions of RAD6 with the E3 partner RAD18 and RAD18 with WC2.",,,,,,,GO:0005524; GO:0070628; GO:0003697; GO:0017116; GO:0061631,GO:0061631; GO:0004842,GO:0004842,GO:0061631,GO:0061631; GO:0004842,GO:0004842; GO:0061631,0.4648,0.3474,0.3918,0.4648,0.4648,5,0.4267,0.8733,yes
GLG_CRYN9,J9VPM2,ESM2Text,Eukaryota,926,"Self-glucosylating initiator of glycogen synthesis. It catalyzes the formation of a short alpha (1,4)- glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase.","Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008466; GO:0046872,GO:0016757,GO:0008466,GO:0008466,GO:0004345,GO:0008466,0.4115,0.689,0.689,0.1302,0.689,5,0.5217,0.4145,no
GLG_CRYN9,J9VPM2,Prot2Text,Eukaryota,926,"Self-glucosylating initiator of glycogen synthesis. It catalyzes the formation of a short alpha (1,4)- glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase.","Glycosyltransferase involved in the arabinosylation of extensin proteins in root hair cells. Involved in the elongation of arabinogalactan, a polysaccharide attached to the cell wall, which is present on the cell surface of root hair cells.",No,No,No,No,No,not-Yes,GO:0008466; GO:0046872,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.4115,0.4115,0.4115,0.4115,0.4115,5,0.4115,0.4145,no
GLG_CRYN9,J9VPM2,ProtT3,Eukaryota,926,"Self-glucosylating initiator of glycogen synthesis. It catalyzes the formation of a short alpha (1,4)- glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase.",Responsible for the addition of the first O-linked mannose residue to the oligosaccharide chains of N-linked glycoproteins. Cytoplasm. Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily,No,No,No,No,Vague,not-Yes,GO:0008466; GO:0046872,GO:0004169,GO:0004169,GO:0000030,GO:0004169,GO:0016757,0.3342,0.3342,0.3869,0.3342,0.4115,5,0.3602,0.4145,no
GLG_CRYN9,J9VPM2,ProtTale,Eukaryota,926,"Self-glucosylating initiator of glycogen synthesis. It catalyzes the formation of a short alpha (1,4)- glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase.",Phosphorylates the histone H2A to form H2AS128ph. May be involved in cell cycle regulation.,No,No,No,No,No,not-Yes,GO:0008466; GO:0046872,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,0.2537,0.2537,0.2537,0.1722,0.2537,5,0.2374,0.4145,no
GLG_CRYN9,J9VPM2,Protein2Text,Eukaryota,926,"Self-glucosylating initiator of glycogen synthesis. It catalyzes the formation of a short alpha (1,4)- glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase.","This protein is a glycosylase, which means it is involved in the transfer of sugar molecules to other molecules, such as proteins or lipids, through the action of enzymes. Specifically, it is a mannose-1-phosphate-guanyltransferase, which is a type of glycosyltransferase that catalyzes the transfer of mannose-1-phosphate to a protein.",No,No,No,No,No,not-Yes,GO:0008466; GO:0046872,GO:0008168,GO:0004475,GO:0004475,GO:0004475,GO:0016757,0.2365,0.1729,0.1729,0.1729,0.4115,5,0.2333,0.4145,no
GLG_CRYN9,J9VPM2,Reference,Eukaryota,926,"Self-glucosylating initiator of glycogen synthesis. It catalyzes the formation of a short alpha (1,4)- glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase.","Self-glucosylating initiator of glycogen synthesis. It catalyzes the formation of a short alpha (1,4)- glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase.",,,,,,,GO:0008466; GO:0046872,GO:0008466,GO:0008466,GO:0008466,GO:0004362; GO:0016757,GO:0004373; GO:0016757,0.689,0.689,0.689,0.3448,0.5429,5,0.5909,0.4145,no
ASPR1_CRYN9,J9VS02,ESM2Text,Eukaryota,489,Possesses prevalent extracellular endopeptidase activity at low pH condition. Required for high- density growth in acidic environments. Broad substrate specificity with preference cleavage of the peptide substrate between hydrophobic amino acids. Cleaves substrate at P1-P1' between Phe-Leu. Positively charged amino acids are preferred at P2. Prefers hydrophobic amino acids at the P3 and P4 positions. Cleaves substrate also at P1'-P2' between Leu-Val to some degree. Required for virulence in mouse inhalation model of infection.,Probable aspartic-type endopeptidase which contributes to virulence.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004190,GO:0004190,GO:0004190,GO:0004190,GO:0004190,GO:0004190,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2499,no
ASPR1_CRYN9,J9VS02,Prot2Text,Eukaryota,489,Possesses prevalent extracellular endopeptidase activity at low pH condition. Required for high- density growth in acidic environments. Broad substrate specificity with preference cleavage of the peptide substrate between hydrophobic amino acids. Cleaves substrate at P1-P1' between Phe-Leu. Positively charged amino acids are preferred at P2. Prefers hydrophobic amino acids at the P3 and P4 positions. Cleaves substrate also at P1'-P2' between Leu-Val to some degree. Required for virulence in mouse inhalation model of infection.,Probable GPI-anchored aspartic-type endopeptidase which contributes to virulence.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004190,GO:0004190,GO:0004190,GO:0004190,GO:0004190,GO:0004190,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2499,no
ASPR1_CRYN9,J9VS02,ProtT3,Eukaryota,489,Possesses prevalent extracellular endopeptidase activity at low pH condition. Required for high- density growth in acidic environments. Broad substrate specificity with preference cleavage of the peptide substrate between hydrophobic amino acids. Cleaves substrate at P1-P1' between Phe-Leu. Positively charged amino acids are preferred at P2. Prefers hydrophobic amino acids at the P3 and P4 positions. Cleaves substrate also at P1'-P2' between Leu-Val to some degree. Required for virulence in mouse inhalation model of infection.,"Probable aspartic-type endopeptidase. Cell membrane; Lipid-anchor, GPI- anchor. Belongs to the peptidase A1 family",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004190,GO:0004190,GO:0004190,GO:0004190,GO:0004190,GO:0004190,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2499,no
ASPR1_CRYN9,J9VS02,ProtTale,Eukaryota,489,Possesses prevalent extracellular endopeptidase activity at low pH condition. Required for high- density growth in acidic environments. Broad substrate specificity with preference cleavage of the peptide substrate between hydrophobic amino acids. Cleaves substrate at P1-P1' between Phe-Leu. Positively charged amino acids are preferred at P2. Prefers hydrophobic amino acids at the P3 and P4 positions. Cleaves substrate also at P1'-P2' between Leu-Val to some degree. Required for virulence in mouse inhalation model of infection.,Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004190,GO:0004190,GO:0004190,GO:0004190,GO:0004190,GO:0004190,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2499,no
ASPR1_CRYN9,J9VS02,Protein2Text,Eukaryota,489,Possesses prevalent extracellular endopeptidase activity at low pH condition. Required for high- density growth in acidic environments. Broad substrate specificity with preference cleavage of the peptide substrate between hydrophobic amino acids. Cleaves substrate at P1-P1' between Phe-Leu. Positively charged amino acids are preferred at P2. Prefers hydrophobic amino acids at the P3 and P4 positions. Cleaves substrate also at P1'-P2' between Leu-Val to some degree. Required for virulence in mouse inhalation model of infection.,"The molecular function of this protein is a lyase, which is an enzyme that catalyzes the cleavage of a carbon-phosphorus bond in an organic compound, resulting in the formation of a new carbon-carbon double bond. More specifically, this protein is likely involved in the degradation of proteins or other macromolecules, and is probably a secreted aspartic protease.",No,No,No,No,No,not-Yes,GO:0004190,,,,,,,,,,,0,,0.2499,no
ASPR1_CRYN9,J9VS02,Reference,Eukaryota,489,Possesses prevalent extracellular endopeptidase activity at low pH condition. Required for high- density growth in acidic environments. Broad substrate specificity with preference cleavage of the peptide substrate between hydrophobic amino acids. Cleaves substrate at P1-P1' between Phe-Leu. Positively charged amino acids are preferred at P2. Prefers hydrophobic amino acids at the P3 and P4 positions. Cleaves substrate also at P1'-P2' between Leu-Val to some degree. Required for virulence in mouse inhalation model of infection.,Possesses prevalent extracellular endopeptidase activity at low pH condition. Required for high- density growth in acidic environments. Broad substrate specificity with preference cleavage of the peptide substrate between hydrophobic amino acids. Cleaves substrate at P1-P1' between Phe-Leu. Positively charged amino acids are preferred at P2. Prefers hydrophobic amino acids at the P3 and P4 positions. Cleaves substrate also at P1'-P2' between Leu-Val to some degree. Required for virulence in mouse inhalation model of infection.,,,,,,,GO:0004190,GO:0004175,GO:0004175,GO:0004175,GO:0004190,GO:0004190,0.8001,0.8001,0.8001,1.0,1.0,5,0.8801,0.2499,no
POL_BPNNR,M5AAG8,ESM2Text,Viruses,718,"Multifunctional protein with primer synthesis, DNA polymerization, and DNA helicase activities. Recognizes a specific sequence motif 5'-TTTGGTTA-3' and initiates DNA synthesis.",ATPase that stimulates DNA recombination and is essential for DNA repair.,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0005524; GO:0003678; GO:0003887; GO:0016787,GO:0016887; GO:0005524,GO:0016887; GO:0003677,GO:0016887,GO:0016887,GO:0016887,0.5552,0.285,0.2784,0.2784,0.2784,5,0.3351,0.5046,no
POL_BPNNR,M5AAG8,Prot2Text,Viruses,718,"Multifunctional protein with primer synthesis, DNA polymerization, and DNA helicase activities. Recognizes a specific sequence motif 5'-TTTGGTTA-3' and initiates DNA synthesis.",ATPase that stimulates DNA recombination and is essential for DNA repair.,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0005524; GO:0003678; GO:0003887; GO:0016787,GO:0008094; GO:0005524,GO:0008094,GO:0008094,GO:0005524; GO:0003678,GO:0008094,0.7099,0.4669,0.4669,0.7662,0.4669,5,0.5754,0.5046,no
POL_BPNNR,M5AAG8,ProtT3,Viruses,718,"Multifunctional protein with primer synthesis, DNA polymerization, and DNA helicase activities. Recognizes a specific sequence motif 5'-TTTGGTTA-3' and initiates DNA synthesis.",To phage Mu protein gp15,Vague,Vague,Vague,Vague,No,not-Yes,GO:0005524; GO:0003678; GO:0003887; GO:0016787,,,,,,,,,,,0,,0.5046,no
POL_BPNNR,M5AAG8,ProtTale,Viruses,718,"Multifunctional protein with primer synthesis, DNA polymerization, and DNA helicase activities. Recognizes a specific sequence motif 5'-TTTGGTTA-3' and initiates DNA synthesis.","Component of the T4 DNA primase-helicase complex (primase-helicase), which is required for the initiation of DNA replication, and is also involved in DNA repair. The primase-helicase plays an important role in the regulation of the primase activity of DnaB helicase. In the primase-helicase complex, may function as a clamp, tethering the primase-helicase complex to DNA.",Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0005524; GO:0003678; GO:0003887; GO:0016787,,,,,,,,,,,0,,0.5046,no
POL_BPNNR,M5AAG8,Protein2Text,Viruses,718,"Multifunctional protein with primer synthesis, DNA polymerization, and DNA helicase activities. Recognizes a specific sequence motif 5'-TTTGGTTA-3' and initiates DNA synthesis.","The molecular function of this protein is a DNA polymerase, specifically a reverse transcriptase. It is involved in the replication of viral DNA by converting the viral RNA into DNA.",No,No,Maybe,No,No,not-Yes,GO:0005524; GO:0003678; GO:0003887; GO:0016787,GO:0003964,GO:0003964,GO:0003964,GO:0003964,GO:0003964,0.4583,0.4583,0.4583,0.4583,0.4583,5,0.4583,0.5046,no
POL_BPNNR,M5AAG8,Reference,Viruses,718,"Multifunctional protein with primer synthesis, DNA polymerization, and DNA helicase activities. Recognizes a specific sequence motif 5'-TTTGGTTA-3' and initiates DNA synthesis.","Multifunctional protein with primer synthesis, DNA polymerization, and DNA helicase activities. Recognizes a specific sequence motif 5'-TTTGGTTA-3' and initiates DNA synthesis.",,,,,,,GO:0005524; GO:0003678; GO:0003887; GO:0016787,GO:0003887; GO:0003896; GO:0003678,GO:0003896; GO:0003887; GO:0004386; GO:0003677,GO:0003887; GO:0003896; GO:0003678,GO:0003896; GO:0003887; GO:0004386; GO:0005524,GO:0003887; GO:0004386; GO:0003896; GO:0005524,0.7231,0.6187,0.7231,0.8502,0.8502,5,0.7531,0.5046,no
SRPK7_DROME,M9MS50,ESM2Text,Eukaryota,869,Serine-arginine protein-specific kinase. Phosphorylates the active zone T-bar structural protein brp/bruchpilot; phosphorylation within the N-terminal region of brp is involved in regulating T-bar component trafficking and assembly. Required to prevent premature assembly of presynaptic active zone cytomatrix (T-bar) electron-dense structure components during axonal transport. Functions downstream of Lrp4 in presynaptic active zone organization.,"Serine/arginine-rich protein kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains. Phosphorylates the SR splicing factor SRSF1 and the nuclear factor NF-kappa-B, but is not able to phosphorylate multiple SR splicing substrates in vitro. Required for the regulation of both the nuclear receptor-mediated transcription and the subsequent endosomal sorting of the nuclear receptor in cells. Required for the maintenance of the nuclear receptor-spike complex (RSC) polarity. Phosphorylates the SR splicing factor SRSF1 and the nuclear receptor-mediated transcription factor NF-kappa-B, but is not required to phosphorylate multiple SRSF1-SRSF1-SR splicing substrates in vitro. Required for proper nuclear division. Phosphorylates the nuclear receptor-spike complex (RSC) polarity protein SKI and the cytoplasmic microtubule-organizing protein (MAPP) complex, but is not required to phosphorylate multiple cytoplasmic SKI and, thereby, no",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0004672; GO:0106310; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.7571,0.7571,0.7571,0.7571,0.7571,5,0.7571,0.6958,yes
SRPK7_DROME,M9MS50,Prot2Text,Eukaryota,869,Serine-arginine protein-specific kinase. Phosphorylates the active zone T-bar structural protein brp/bruchpilot; phosphorylation within the N-terminal region of brp is involved in regulating T-bar component trafficking and assembly. Required to prevent premature assembly of presynaptic active zone cytomatrix (T-bar) electron-dense structure components during axonal transport. Functions downstream of Lrp4 in presynaptic active zone organization.,"Serine/threonine-protein kinase involved in the G1-S transition. Phosphorylates the alpha subunit of eisosome assembly factors, also known as RSF1 and RSF2.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004672; GO:0106310; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.7571,0.7571,0.7571,0.7571,0.7571,5,0.7571,0.6958,yes
SRPK7_DROME,M9MS50,ProtT3,Eukaryota,869,Serine-arginine protein-specific kinase. Phosphorylates the active zone T-bar structural protein brp/bruchpilot; phosphorylation within the N-terminal region of brp is involved in regulating T-bar component trafficking and assembly. Required to prevent premature assembly of presynaptic active zone cytomatrix (T-bar) electron-dense structure components during axonal transport. Functions downstream of Lrp4 in presynaptic active zone organization.,Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0004672; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,0.9552,0.9552,0.9552,0.9552,0.7571,5,0.9156,0.6958,yes
SRPK7_DROME,M9MS50,ProtTale,Eukaryota,869,Serine-arginine protein-specific kinase. Phosphorylates the active zone T-bar structural protein brp/bruchpilot; phosphorylation within the N-terminal region of brp is involved in regulating T-bar component trafficking and assembly. Required to prevent premature assembly of presynaptic active zone cytomatrix (T-bar) electron-dense structure components during axonal transport. Functions downstream of Lrp4 in presynaptic active zone organization.,"Serine/threonine-protein kinase involved in regulation of transcription, DNA damage response and chromatin remodeling. Phosphorylates histone H3 at 'Ser-10' and 'Ser-119' to form H3S10ph and H3S119ph in response to DNA damage. This leads to transcriptional repression and cell cycle arrest. Also phosphorylates histone H4 at 'Ser-1' and 'Ser-56' to form H4S1ph and H4S56ph. Acts as a key regulator of DNA double-strand break (DSB",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0004672; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,0.9552,0.9552,0.9552,0.7571,0.9552,5,0.9156,0.6958,yes
SRPK7_DROME,M9MS50,Protein2Text,Eukaryota,869,Serine-arginine protein-specific kinase. Phosphorylates the active zone T-bar structural protein brp/bruchpilot; phosphorylation within the N-terminal region of brp is involved in regulating T-bar component trafficking and assembly. Required to prevent premature assembly of presynaptic active zone cytomatrix (T-bar) electron-dense structure components during axonal transport. Functions downstream of Lrp4 in presynaptic active zone organization.,"The molecular function of this protein is not explicitly stated in the provided snippet. However, based on the name ""protein"", it can be inferred that it likely plays a role in various biological processes, such as regulating gene expression, signaling pathways, or protein interactions. If you could provide more information about this protein, I may be able to provide a more specific answer.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0004672; GO:0106310; GO:0004674,,,,,,,,,,,0,,0.6958,yes
SRPK7_DROME,M9MS50,Reference,Eukaryota,869,Serine-arginine protein-specific kinase. Phosphorylates the active zone T-bar structural protein brp/bruchpilot; phosphorylation within the N-terminal region of brp is involved in regulating T-bar component trafficking and assembly. Required to prevent premature assembly of presynaptic active zone cytomatrix (T-bar) electron-dense structure components during axonal transport. Functions downstream of Lrp4 in presynaptic active zone organization.,Serine-arginine protein-specific kinase. Phosphorylates the active zone T-bar structural protein brp/bruchpilot; phosphorylation within the N-terminal region of brp is involved in regulating T-bar component trafficking and assembly. Required to prevent premature assembly of presynaptic active zone cytomatrix (T-bar) electron-dense structure components during axonal transport. Functions downstream of Lrp4 in presynaptic active zone organization.,,,,,,,GO:0005524; GO:0004672; GO:0106310; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.7571,0.7571,0.7571,0.9552,0.9552,5,0.8363,0.6958,yes
ALDR_DROME,M9PF61,ESM2Text,Eukaryota,350,"Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides, bile acids and xenobiotics substrates. Key enzyme in the polyol pathway, catalyzes reduction of glucose to sorbitol during hyperglycemia. Reduces steroids and their derivatives and prostaglandins. Through production of prostaglandin F2alpha may regulate the activity of non- muscle myosin II in an autocrine or paracrine fashion; influences border cell and nurse cell stiffness to facilitate border cell cluster migration. Also regulates the cell surface localization of integrins in an autocrine or paracrine fashion; influences border cell adhesion to maintain border cell cluster morphology. In hemocytes, probably contributes to production of sugar alcohols in the hemolymph, which act as alarmins involved in gut-fat body innate immunological communication (GFIC); leads to activation of the imd/Relish signaling pathway in the fat body.","Catalyzes the stereospecific NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous substrates such as aromatic and aliphatic aldehydes, ketones, monosacharides and polyunsaturated carbonyls. Displays high activity towards ethyl acetate, propionaldehyde, propyraldehyde and butyraldehyde. Reduces steroids and their derivatives. Reduces prostaglandin A1 (PGA1) to the prostaglandin F2 (PGF2). Reduces prostaglandin F2 to the epoxide-forming prostaglandin F1 (EFR1). Reduces adipose tissue-associated gasdermin-B1 (CASB1) to the adipose tissue-associated beta-naphthopyranose (ANAP).",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004032; GO:0052650; GO:0047655; GO:0047956; GO:0047939; GO:0036130,GO:0016491,GO:0004033; GO:0016491,GO:0004033,GO:0004033,GO:0004033,0.5702,0.5702,0.0,0.0,0.0,5,0.2281,0.246,no
ALDR_DROME,M9PF61,Prot2Text,Eukaryota,350,"Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides, bile acids and xenobiotics substrates. Key enzyme in the polyol pathway, catalyzes reduction of glucose to sorbitol during hyperglycemia. Reduces steroids and their derivatives and prostaglandins. Through production of prostaglandin F2alpha may regulate the activity of non- muscle myosin II in an autocrine or paracrine fashion; influences border cell and nurse cell stiffness to facilitate border cell cluster migration. Also regulates the cell surface localization of integrins in an autocrine or paracrine fashion; influences border cell adhesion to maintain border cell cluster morphology. In hemocytes, probably contributes to production of sugar alcohols in the hemolymph, which act as alarmins involved in gut-fat body innate immunological communication (GFIC); leads to activation of the imd/Relish signaling pathway in the fat body.",Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004032; GO:0052650; GO:0047655; GO:0047956; GO:0047939; GO:0036130,GO:0004033,GO:0004090,GO:0016491,GO:0016491,GO:0004033,0.0,0.6466,0.5702,0.5702,0.0,5,0.3574,0.246,no
ALDR_DROME,M9PF61,ProtT3,Eukaryota,350,"Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides, bile acids and xenobiotics substrates. Key enzyme in the polyol pathway, catalyzes reduction of glucose to sorbitol during hyperglycemia. Reduces steroids and their derivatives and prostaglandins. Through production of prostaglandin F2alpha may regulate the activity of non- muscle myosin II in an autocrine or paracrine fashion; influences border cell and nurse cell stiffness to facilitate border cell cluster migration. Also regulates the cell surface localization of integrins in an autocrine or paracrine fashion; influences border cell adhesion to maintain border cell cluster morphology. In hemocytes, probably contributes to production of sugar alcohols in the hemolymph, which act as alarmins involved in gut-fat body innate immunological communication (GFIC); leads to activation of the imd/Relish signaling pathway in the fat body.","Catalyzes the NAD(P)(+)-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, fatty acids, bile acids and steroid hormones (By similarity). Plays an important role in the detoxification of xenobiotics (By similarity). Mitochondrion matrix. Belongs to the aldo/keto reductase family",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004032; GO:0052650; GO:0047655; GO:0047956; GO:0047939; GO:0036130,GO:0004033,GO:0004033,GO:0004033,GO:0004033,GO:0004033,0.0,0.0,0.0,0.0,0.0,5,0.0,0.246,no
ALDR_DROME,M9PF61,ProtTale,Eukaryota,350,"Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides, bile acids and xenobiotics substrates. Key enzyme in the polyol pathway, catalyzes reduction of glucose to sorbitol during hyperglycemia. Reduces steroids and their derivatives and prostaglandins. Through production of prostaglandin F2alpha may regulate the activity of non- muscle myosin II in an autocrine or paracrine fashion; influences border cell and nurse cell stiffness to facilitate border cell cluster migration. Also regulates the cell surface localization of integrins in an autocrine or paracrine fashion; influences border cell adhesion to maintain border cell cluster morphology. In hemocytes, probably contributes to production of sugar alcohols in the hemolymph, which act as alarmins involved in gut-fat body innate immunological communication (GFIC); leads to activation of the imd/Relish signaling pathway in the fat body.",Catalyzes the NAD(+)-dependent oxidation of glucose-6-phosphate to 6- phosphogluconolactone. Also catalyzes the oxidation of ribose-5-phosphate to ribulose-5-phosphate.,No,No,No,No,No,not-Yes,GO:0004032; GO:0052650; GO:0047655; GO:0047956; GO:0047939; GO:0036130,GO:0016616,GO:0004345,GO:0004345; GO:0051287,GO:0004345,GO:0004345,0.806,0.6812,0.6048,0.6812,0.6812,5,0.6909,0.246,no
ALDR_DROME,M9PF61,Protein2Text,Eukaryota,350,"Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides, bile acids and xenobiotics substrates. Key enzyme in the polyol pathway, catalyzes reduction of glucose to sorbitol during hyperglycemia. Reduces steroids and their derivatives and prostaglandins. Through production of prostaglandin F2alpha may regulate the activity of non- muscle myosin II in an autocrine or paracrine fashion; influences border cell and nurse cell stiffness to facilitate border cell cluster migration. Also regulates the cell surface localization of integrins in an autocrine or paracrine fashion; influences border cell adhesion to maintain border cell cluster morphology. In hemocytes, probably contributes to production of sugar alcohols in the hemolymph, which act as alarmins involved in gut-fat body innate immunological communication (GFIC); leads to activation of the imd/Relish signaling pathway in the fat body.","The molecular function of this protein is a 17-beta dehydrogenase activity, which is involved in the metabolism of steroids. More specifically, it catalyzes the reversible NAD(P)-dependent oxidation of 17-beta hydroxyl steroids to yield the corresponding 17- ketosteroids. It is involved in the metabolism of androgens and estrogens. It can convert androstanedione to 5-alpha-androstan-3-one (dihydrotestosterone) and estradiol to estrone. It can also catalyze the reverse reaction, converting 5-alpha-androstan-3-one to androstanedione and estrone to estradiol. This protein is also involved in the metabolism of bile acids, converting 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol to 5-beta-cholestane-3-alpha,7-alpha-diol. It is also involved in the metabolism of retinoids, converting all-trans- and 9-cis-retinol to all-trans- and 9-cis-retinal, respectively. Additionally, it can catalyze the oxidation of all-trans- and 9-cis-retinal to all-trans- and 9-cis-retinoic acid, respectively. It is also involved in the metabolism of prostaglandins, converting prostaglandin E1 to prostaglandin E2. It is also involved in the metabolism of leukotrienes, converting leukotriene A4 to leukotriene B4. It is also involved in the metabolism of prostaglandin D2 to prostaglandin E2. It is also involved in the metabolism of prostaglandin I2 to prostaglandin E2. It is also involved in the metabolism of prostaglandin F2-alpha to prostaglandin E2. It is also involved in the metabolism of prostaglandin H2 to prostaglandin E2. It is also involved in the metabolism of prostaglandin E1 to prostaglandin E2. It is also involved in the metabolism of prostaglandin D1 to prostaglandin E2. It is also involved in the metabolism of prostaglandin I1 to prostaglandin E2. It is also involved in the metabolism of prostaglandin F1-alpha to prostaglandin E2. It is also involved in the metabolism of prostaglandin H1",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004032; GO:0052650; GO:0047655; GO:0047956; GO:0047939; GO:0036130,GO:0016491,GO:0016491,,GO:0016491,GO:0016491,0.5702,0.5702,,0.5702,0.5702,4,0.5702,0.246,no
ALDR_DROME,M9PF61,Reference,Eukaryota,350,"Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides, bile acids and xenobiotics substrates. Key enzyme in the polyol pathway, catalyzes reduction of glucose to sorbitol during hyperglycemia. Reduces steroids and their derivatives and prostaglandins. Through production of prostaglandin F2alpha may regulate the activity of non- muscle myosin II in an autocrine or paracrine fashion; influences border cell and nurse cell stiffness to facilitate border cell cluster migration. Also regulates the cell surface localization of integrins in an autocrine or paracrine fashion; influences border cell adhesion to maintain border cell cluster morphology. In hemocytes, probably contributes to production of sugar alcohols in the hemolymph, which act as alarmins involved in gut-fat body innate immunological communication (GFIC); leads to activation of the imd/Relish signaling pathway in the fat body.","Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides, bile acids and xenobiotics substrates. Key enzyme in the polyol pathway, catalyzes reduction of glucose to sorbitol during hyperglycemia. Reduces steroids and their derivatives and prostaglandins. Through production of prostaglandin F2alpha may regulate the activity of non- muscle myosin II in an autocrine or paracrine fashion; influences border cell and nurse cell stiffness to facilitate border cell cluster migration. Also regulates the cell surface localization of integrins in an autocrine or paracrine fashion; influences border cell adhesion to maintain border cell cluster morphology. In hemocytes, probably contributes to production of sugar alcohols in the hemolymph, which act as alarmins involved in gut-fat body innate immunological communication (GFIC); leads to activation of the imd/Relish signaling pathway in the fat body.",,,,,,,GO:0004032; GO:0052650; GO:0047655; GO:0047956; GO:0047939; GO:0036130,GO:0004032; GO:0016491,GO:0004033,GO:0004032,GO:0004032; GO:0016491,GO:0004032,0.7212,0.0,0.7153,0.7212,0.7153,5,0.5746,0.246,no
WNK_DROME,M9PGC5,ESM2Text,Eukaryota,2462,"Serine/threonine-protein kinase component of the WNK- SPAK/OSR1 kinase cascade, which plays an important role in the regulation of electrolyte homeostasis and regulatory volume increase in response to hyperosmotic stress. Wnk mediates regulatory volume increase in response to hyperosmotic stress by acting as a molecular crowding sensor, which senses cell shrinkage and mediates formation of a membraneless compartment by undergoing liquid-liquid phase separation. The membraneless compartment concentrates Wnk with its substrate Fray, promoting Wnk-dependent phosphorylation and activation of downstream kinase Fray. Following activation, Fray catalyzes phosphorylation of ion cotransporters Ncc69 and Irk1, regulating their activity. Phosphorylation of Na-K-Cl cotransporter Ncc69 promotes its activation and ion influx. Involved in circadian rhythms in small ventral lateral (sLNv) pacemaker neurons: in the morning, Wnk activity is repressed by high levels of intracellular chloride; in contrast Wnk activation in the evening promotes the activation of the inwardly rectifying potassium channel Irk1 via Fray. Acts as a positive regulator of the canonical Wnt signaling pathway during wing disk development.",Serine/threonine protein kinase which acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylation of the CDK1 kinase.,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0140693; GO:0019870; GO:0004672; GO:0106310; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.5643,0.5643,0.5643,0.5643,0.5643,5,0.5643,0.6483,yes
WNK_DROME,M9PGC5,Prot2Text,Eukaryota,2462,"Serine/threonine-protein kinase component of the WNK- SPAK/OSR1 kinase cascade, which plays an important role in the regulation of electrolyte homeostasis and regulatory volume increase in response to hyperosmotic stress. Wnk mediates regulatory volume increase in response to hyperosmotic stress by acting as a molecular crowding sensor, which senses cell shrinkage and mediates formation of a membraneless compartment by undergoing liquid-liquid phase separation. The membraneless compartment concentrates Wnk with its substrate Fray, promoting Wnk-dependent phosphorylation and activation of downstream kinase Fray. Following activation, Fray catalyzes phosphorylation of ion cotransporters Ncc69 and Irk1, regulating their activity. Phosphorylation of Na-K-Cl cotransporter Ncc69 promotes its activation and ion influx. Involved in circadian rhythms in small ventral lateral (sLNv) pacemaker neurons: in the morning, Wnk activity is repressed by high levels of intracellular chloride; in contrast Wnk activation in the evening promotes the activation of the inwardly rectifying potassium channel Irk1 via Fray. Acts as a positive regulator of the canonical Wnt signaling pathway during wing disk development.","Serine/threonine-protein kinase involved in the regulation of actin filament dynamics and endocytosis. Phosphorylates several substrates, such as actin-filament polymerisation factors actin-fragmin-1, actin-filament-stabilizing proteins actin-filament-releasing proteins actin-filament-releasing-releasing-protein, and filamin-filament proteins filamin-releasing-protein. In turn, the actin cytoskeleton is modified thereby changing the way filaments are formed. Through phosphorylation of substrates, may regulate actin dynamics and endocytosis. Required for the regulation of actin filament dynamics during embryogenesis, probably by phosphorylating and regulating the actin cytoskeleton proteins actin-filament-releasing proteins (F-actin), filamin-releasing proteins (F-actin), and filamin-releasing proteins (F-actin). Required for the regulation of actin-filament dynamics during oocyte development, probably by phosphorylating and regulating actin-filament proteins (F-actin) and (F-actin) proteins. Involved in",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0140693; GO:0019870; GO:0004672; GO:0106310; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.5643,0.5643,0.5643,0.5643,0.5643,5,0.5643,0.6483,yes
WNK_DROME,M9PGC5,ProtT3,Eukaryota,2462,"Serine/threonine-protein kinase component of the WNK- SPAK/OSR1 kinase cascade, which plays an important role in the regulation of electrolyte homeostasis and regulatory volume increase in response to hyperosmotic stress. Wnk mediates regulatory volume increase in response to hyperosmotic stress by acting as a molecular crowding sensor, which senses cell shrinkage and mediates formation of a membraneless compartment by undergoing liquid-liquid phase separation. The membraneless compartment concentrates Wnk with its substrate Fray, promoting Wnk-dependent phosphorylation and activation of downstream kinase Fray. Following activation, Fray catalyzes phosphorylation of ion cotransporters Ncc69 and Irk1, regulating their activity. Phosphorylation of Na-K-Cl cotransporter Ncc69 promotes its activation and ion influx. Involved in circadian rhythms in small ventral lateral (sLNv) pacemaker neurons: in the morning, Wnk activity is repressed by high levels of intracellular chloride; in contrast Wnk activation in the evening promotes the activation of the inwardly rectifying potassium channel Irk1 via Fray. Acts as a positive regulator of the canonical Wnt signaling pathway during wing disk development.",Belongs to the protein kinase superfamily. Ser/Thr protein kinase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0140693; GO:0019870; GO:0004672; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,0.737,0.737,0.737,0.737,0.5643,5,0.7025,0.6483,yes
WNK_DROME,M9PGC5,ProtTale,Eukaryota,2462,"Serine/threonine-protein kinase component of the WNK- SPAK/OSR1 kinase cascade, which plays an important role in the regulation of electrolyte homeostasis and regulatory volume increase in response to hyperosmotic stress. Wnk mediates regulatory volume increase in response to hyperosmotic stress by acting as a molecular crowding sensor, which senses cell shrinkage and mediates formation of a membraneless compartment by undergoing liquid-liquid phase separation. The membraneless compartment concentrates Wnk with its substrate Fray, promoting Wnk-dependent phosphorylation and activation of downstream kinase Fray. Following activation, Fray catalyzes phosphorylation of ion cotransporters Ncc69 and Irk1, regulating their activity. Phosphorylation of Na-K-Cl cotransporter Ncc69 promotes its activation and ion influx. Involved in circadian rhythms in small ventral lateral (sLNv) pacemaker neurons: in the morning, Wnk activity is repressed by high levels of intracellular chloride; in contrast Wnk activation in the evening promotes the activation of the inwardly rectifying potassium channel Irk1 via Fray. Acts as a positive regulator of the canonical Wnt signaling pathway during wing disk development.",Serine/threonine-protein kinase involved in the regulation of mitosis.,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0140693; GO:0019870; GO:0004672; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,0.737,0.737,0.737,0.5643,0.737,5,0.7025,0.6483,yes
WNK_DROME,M9PGC5,Protein2Text,Eukaryota,2462,"Serine/threonine-protein kinase component of the WNK- SPAK/OSR1 kinase cascade, which plays an important role in the regulation of electrolyte homeostasis and regulatory volume increase in response to hyperosmotic stress. Wnk mediates regulatory volume increase in response to hyperosmotic stress by acting as a molecular crowding sensor, which senses cell shrinkage and mediates formation of a membraneless compartment by undergoing liquid-liquid phase separation. The membraneless compartment concentrates Wnk with its substrate Fray, promoting Wnk-dependent phosphorylation and activation of downstream kinase Fray. Following activation, Fray catalyzes phosphorylation of ion cotransporters Ncc69 and Irk1, regulating their activity. Phosphorylation of Na-K-Cl cotransporter Ncc69 promotes its activation and ion influx. Involved in circadian rhythms in small ventral lateral (sLNv) pacemaker neurons: in the morning, Wnk activity is repressed by high levels of intracellular chloride; in contrast Wnk activation in the evening promotes the activation of the inwardly rectifying potassium channel Irk1 via Fray. Acts as a positive regulator of the canonical Wnt signaling pathway during wing disk development.","The molecular function of this protein is not explicitly stated in the provided text. However, based on the context, it can be inferred that the protein is involved in regulating the assembly of a complex that plays a role in neuronal development and function.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0005524; GO:0140693; GO:0019870; GO:0004672; GO:0106310; GO:0004674,,,,,,,,,,,0,,0.6483,yes
WNK_DROME,M9PGC5,Reference,Eukaryota,2462,"Serine/threonine-protein kinase component of the WNK- SPAK/OSR1 kinase cascade, which plays an important role in the regulation of electrolyte homeostasis and regulatory volume increase in response to hyperosmotic stress. Wnk mediates regulatory volume increase in response to hyperosmotic stress by acting as a molecular crowding sensor, which senses cell shrinkage and mediates formation of a membraneless compartment by undergoing liquid-liquid phase separation. The membraneless compartment concentrates Wnk with its substrate Fray, promoting Wnk-dependent phosphorylation and activation of downstream kinase Fray. Following activation, Fray catalyzes phosphorylation of ion cotransporters Ncc69 and Irk1, regulating their activity. Phosphorylation of Na-K-Cl cotransporter Ncc69 promotes its activation and ion influx. Involved in circadian rhythms in small ventral lateral (sLNv) pacemaker neurons: in the morning, Wnk activity is repressed by high levels of intracellular chloride; in contrast Wnk activation in the evening promotes the activation of the inwardly rectifying potassium channel Irk1 via Fray. Acts as a positive regulator of the canonical Wnt signaling pathway during wing disk development.","Serine/threonine-protein kinase component of the WNK- SPAK/OSR1 kinase cascade, which plays an important role in the regulation of electrolyte homeostasis and regulatory volume increase in response to hyperosmotic stress. Wnk mediates regulatory volume increase in response to hyperosmotic stress by acting as a molecular crowding sensor, which senses cell shrinkage and mediates formation of a membraneless compartment by undergoing liquid-liquid phase separation. The membraneless compartment concentrates Wnk with its substrate Fray, promoting Wnk-dependent phosphorylation and activation of downstream kinase Fray. Following activation, Fray catalyzes phosphorylation of ion cotransporters Ncc69 and Irk1, regulating their activity. Phosphorylation of Na-K-Cl cotransporter Ncc69 promotes its activation and ion influx. Involved in circadian rhythms in small ventral lateral (sLNv) pacemaker neurons: in the morning, Wnk activity is repressed by high levels of intracellular chloride; in contrast Wnk activation in the evening promotes the activation of the inwardly rectifying potassium channel Irk1 via Fray. Acts as a positive regulator of the canonical Wnt signaling pathway during wing disk development.",,,,,,,GO:0005524; GO:0140693; GO:0019870; GO:0004672; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674,GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.737,0.5643,0.5643,0.737,0.737,5,0.6679,0.6483,yes
POLG_FCV,N0A3C0,ESM2Text,Viruses,1763,"[NTPase]: NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity.",Functions as a component of the mitochondrial ribosome (mitoribosome).,No,No,No,No,No,not-Yes,GO:0005524; GO:0004197; GO:0017111; GO:0003723; GO:0003724; GO:0003968,GO:0003735,GO:0003735,GO:0003735,GO:0003735,GO:0003735,0.1461,0.1461,0.1461,0.1461,0.1461,5,0.1461,0.3833,no
POLG_FCV,N0A3C0,Prot2Text,Viruses,1763,"[NTPase]: NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity.",Functions as a component of the mitochondrial ribosome (mitoribosome).,No,No,No,No,No,not-Yes,GO:0005524; GO:0004197; GO:0017111; GO:0003723; GO:0003724; GO:0003968,,GO:0003735,GO:0003735,GO:0003735,GO:0003735,,0.1461,0.1461,0.1461,0.1461,4,0.1461,0.3833,no
POLG_FCV,N0A3C0,ProtT3,Viruses,1763,"[NTPase]: NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity.",Host membrane; Single-pass membrane protein,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0004197; GO:0017111; GO:0003723; GO:0003724; GO:0003968,,,,,,,,,,,0,,0.3833,no
POLG_FCV,N0A3C0,ProtTale,Viruses,1763,"[NTPase]: NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity.","[NS2]: Together with NTPase and NS4, initiates the formation of the replication complex. Induces the proliferation of the host smooth ER membranes forming long tubular structures. These remodeled membranes probably form the viral factories that contain the replication complex.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004197; GO:0017111; GO:0003723; GO:0003724; GO:0003968,,,,,,,,,,,0,,0.3833,no
POLG_FCV,N0A3C0,Protein2Text,Viruses,1763,"[NTPase]: NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity.",The molecular function of this protein is RNA-directed RNA polymerase activity.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004197; GO:0017111; GO:0003723; GO:0003724; GO:0003968,GO:0003968,GO:0003968,GO:0003968,GO:0003968,GO:0003968,0.3883,0.3883,0.3883,0.3883,0.3883,5,0.3883,0.3833,no
POLG_FCV,N0A3C0,Reference,Viruses,1763,"[NTPase]: NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity.","[NTPase]: NTPase presumably plays a role in replication. Despite having similarities with helicases, does not seem to display any helicase activity.",,,,,,,GO:0005524; GO:0004197; GO:0017111; GO:0003723; GO:0003724; GO:0003968,GO:0017111,GO:0017111,GO:0017111,GO:0016462; GO:0005524,GO:0017111,0.3837,0.3837,0.3837,0.5626,0.3837,5,0.4195,0.3833,no
RAB2_DROME,O18333,ESM2Text,Eukaryota,213,"May be involved in bidirectional endoplasmic reticulum (ER) to Golgi trafficking. Together with Rab7 involved in promoting fusion of autophagosomes and endosomes with lysosomes, probably through recruitment of the HOPS tethering complex. Involved in biosynthetic transport to lysosomes. In larval motor neurons, mediates the biogenesis of presynaptic cargo vesicles and their long-range axonal trafficking to synaptic termini. Not involved in axonal trafficking of mitochondria. During vesicle biogenesis, active zone proteins (including brp/Bruchpilot) and synaptic vesicle proteins (including VGlut) are sorted from the trans-Golgi in a Rab2-dependent manner via, at least, two independent routes. Acts upstream of Arl8 during presynaptic precursor vesicle biogenesis. Associated with lysosomal marker positive presynaptic cargo vesicles during anterograde and retrograde axonal trafficking, probably while in its GTP-bound active state. Involved in the delivery of presynaptic cargos, but not presynapse assembly or active zone function at synaptic termini. Required for autophagocytosis-dependent remodeling of myofibrils and transverse- tubules (T-tubules) during metamorphosis.","The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between active GTP-bound and inactive GDP-bound states. In their active state, drive transport of vesicular carriers from donor organelles to acceptor organelles to regulate the membrane traffic that maintains organelle identity and morphology. Required for protein transport from the endoplasmic reticulum to the Golgi complex.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0003925; GO:0005525; GO:0003924; GO:0000287,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924,GO:0003924,0.8452,0.8452,0.8452,0.5838,0.5838,5,0.7406,0.5495,yes
RAB2_DROME,O18333,Prot2Text,Eukaryota,213,"May be involved in bidirectional endoplasmic reticulum (ER) to Golgi trafficking. Together with Rab7 involved in promoting fusion of autophagosomes and endosomes with lysosomes, probably through recruitment of the HOPS tethering complex. Involved in biosynthetic transport to lysosomes. In larval motor neurons, mediates the biogenesis of presynaptic cargo vesicles and their long-range axonal trafficking to synaptic termini. Not involved in axonal trafficking of mitochondria. During vesicle biogenesis, active zone proteins (including brp/Bruchpilot) and synaptic vesicle proteins (including VGlut) are sorted from the trans-Golgi in a Rab2-dependent manner via, at least, two independent routes. Acts upstream of Arl8 during presynaptic precursor vesicle biogenesis. Associated with lysosomal marker positive presynaptic cargo vesicles during anterograde and retrograde axonal trafficking, probably while in its GTP-bound active state. Involved in the delivery of presynaptic cargos, but not presynapse assembly or active zone function at synaptic termini. Required for autophagocytosis-dependent remodeling of myofibrils and transverse- tubules (T-tubules) during metamorphosis.",Required for protein transport from the endoplasmic reticulum to the Golgi complex.,Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0003925; GO:0005525; GO:0003924; GO:0000287,,,,,,,,,,,0,,0.5495,yes
RAB2_DROME,O18333,ProtT3,Eukaryota,213,"May be involved in bidirectional endoplasmic reticulum (ER) to Golgi trafficking. Together with Rab7 involved in promoting fusion of autophagosomes and endosomes with lysosomes, probably through recruitment of the HOPS tethering complex. Involved in biosynthetic transport to lysosomes. In larval motor neurons, mediates the biogenesis of presynaptic cargo vesicles and their long-range axonal trafficking to synaptic termini. Not involved in axonal trafficking of mitochondria. During vesicle biogenesis, active zone proteins (including brp/Bruchpilot) and synaptic vesicle proteins (including VGlut) are sorted from the trans-Golgi in a Rab2-dependent manner via, at least, two independent routes. Acts upstream of Arl8 during presynaptic precursor vesicle biogenesis. Associated with lysosomal marker positive presynaptic cargo vesicles during anterograde and retrograde axonal trafficking, probably while in its GTP-bound active state. Involved in the delivery of presynaptic cargos, but not presynapse assembly or active zone function at synaptic termini. Required for autophagocytosis-dependent remodeling of myofibrils and transverse- tubules (T-tubules) during metamorphosis.",Protein transport. Probably involved in vesicular traffic (By similarity). Cell membrane; Lipid-anchor; Cytoplasmic side. Belongs to the small GTPase superfamily. Rab family,Vague,Yes,Yes,Maybe,Maybe,not-Yes,GO:0003925; GO:0005525; GO:0003924; GO:0000287,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,0.8452,0.8452,0.8452,0.8452,0.8452,5,0.8452,0.5495,yes
RAB2_DROME,O18333,ProtTale,Eukaryota,213,"May be involved in bidirectional endoplasmic reticulum (ER) to Golgi trafficking. Together with Rab7 involved in promoting fusion of autophagosomes and endosomes with lysosomes, probably through recruitment of the HOPS tethering complex. Involved in biosynthetic transport to lysosomes. In larval motor neurons, mediates the biogenesis of presynaptic cargo vesicles and their long-range axonal trafficking to synaptic termini. Not involved in axonal trafficking of mitochondria. During vesicle biogenesis, active zone proteins (including brp/Bruchpilot) and synaptic vesicle proteins (including VGlut) are sorted from the trans-Golgi in a Rab2-dependent manner via, at least, two independent routes. Acts upstream of Arl8 during presynaptic precursor vesicle biogenesis. Associated with lysosomal marker positive presynaptic cargo vesicles during anterograde and retrograde axonal trafficking, probably while in its GTP-bound active state. Involved in the delivery of presynaptic cargos, but not presynapse assembly or active zone function at synaptic termini. Required for autophagocytosis-dependent remodeling of myofibrils and transverse- tubules (T-tubules) during metamorphosis.","The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0003925; GO:0005525; GO:0003924; GO:0000287,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,0.8452,0.8452,0.8452,0.8452,0.8452,5,0.8452,0.5495,yes
RAB2_DROME,O18333,Protein2Text,Eukaryota,213,"May be involved in bidirectional endoplasmic reticulum (ER) to Golgi trafficking. Together with Rab7 involved in promoting fusion of autophagosomes and endosomes with lysosomes, probably through recruitment of the HOPS tethering complex. Involved in biosynthetic transport to lysosomes. In larval motor neurons, mediates the biogenesis of presynaptic cargo vesicles and their long-range axonal trafficking to synaptic termini. Not involved in axonal trafficking of mitochondria. During vesicle biogenesis, active zone proteins (including brp/Bruchpilot) and synaptic vesicle proteins (including VGlut) are sorted from the trans-Golgi in a Rab2-dependent manner via, at least, two independent routes. Acts upstream of Arl8 during presynaptic precursor vesicle biogenesis. Associated with lysosomal marker positive presynaptic cargo vesicles during anterograde and retrograde axonal trafficking, probably while in its GTP-bound active state. Involved in the delivery of presynaptic cargos, but not presynapse assembly or active zone function at synaptic termini. Required for autophagocytosis-dependent remodeling of myofibrils and transverse- tubules (T-tubules) during metamorphosis.","The molecular function of this protein is not explicitly stated in the provided text, but based on its name and the context, it is likely involved in intracellular transport, specifically in the transport of vesicles within the cell. This is a common function of proteins in the Rab family, which this protein belongs to.",Maybe,Maybe,Vague,Maybe,Maybe,not-Yes,GO:0003925; GO:0005525; GO:0003924; GO:0000287,GO:0003924,GO:0003924,,GO:0003924,GO:0003924,0.5838,0.5838,,0.5838,0.5838,4,0.5838,0.5495,yes
RAB2_DROME,O18333,Reference,Eukaryota,213,"May be involved in bidirectional endoplasmic reticulum (ER) to Golgi trafficking. Together with Rab7 involved in promoting fusion of autophagosomes and endosomes with lysosomes, probably through recruitment of the HOPS tethering complex. Involved in biosynthetic transport to lysosomes. In larval motor neurons, mediates the biogenesis of presynaptic cargo vesicles and their long-range axonal trafficking to synaptic termini. Not involved in axonal trafficking of mitochondria. During vesicle biogenesis, active zone proteins (including brp/Bruchpilot) and synaptic vesicle proteins (including VGlut) are sorted from the trans-Golgi in a Rab2-dependent manner via, at least, two independent routes. Acts upstream of Arl8 during presynaptic precursor vesicle biogenesis. Associated with lysosomal marker positive presynaptic cargo vesicles during anterograde and retrograde axonal trafficking, probably while in its GTP-bound active state. Involved in the delivery of presynaptic cargos, but not presynapse assembly or active zone function at synaptic termini. Required for autophagocytosis-dependent remodeling of myofibrils and transverse- tubules (T-tubules) during metamorphosis.","May be involved in bidirectional endoplasmic reticulum (ER) to Golgi trafficking. Together with Rab7 involved in promoting fusion of autophagosomes and endosomes with lysosomes, probably through recruitment of the HOPS tethering complex. Involved in biosynthetic transport to lysosomes. In larval motor neurons, mediates the biogenesis of presynaptic cargo vesicles and their long-range axonal trafficking to synaptic termini. Not involved in axonal trafficking of mitochondria. During vesicle biogenesis, active zone proteins (including brp/Bruchpilot) and synaptic vesicle proteins (including VGlut) are sorted from the trans-Golgi in a Rab2-dependent manner via, at least, two independent routes. Acts upstream of Arl8 during presynaptic precursor vesicle biogenesis. Associated with lysosomal marker positive presynaptic cargo vesicles during anterograde and retrograde axonal trafficking, probably while in its GTP-bound active state. Involved in the delivery of presynaptic cargos, but not presynapse assembly or active zone function at synaptic termini. Required for autophagocytosis-dependent remodeling of myofibrils and transverse- tubules (T-tubules) during metamorphosis.",,,,,,,GO:0003925; GO:0005525; GO:0003924; GO:0000287,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0005525; GO:0003924,0.8452,0.8452,0.8452,0.8452,0.8452,5,0.8452,0.5495,yes
AMPL2_SOLLC,O24022,ESM2Text,Eukaryota,571,"Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. When associated as homohexamer, catalyzes the proteolyzes of Xaa-Leu dipeptides. Possesses leucine aminopeptidase activity against the model substrate leucine-amido methyl coumarin. Presumably involved in the processing and regular turnover of intracellular proteins (Probable). Regulates wound signaling and has a role in insect defense.",Presumably involved in the processing and regular turnover of intracellular proteins.,Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0042802; GO:0030145; GO:0070006; GO:0044183,,,,,,,,,,,0,,0.4755,no
AMPL2_SOLLC,O24022,Prot2Text,Eukaryota,571,"Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. When associated as homohexamer, catalyzes the proteolyzes of Xaa-Leu dipeptides. Possesses leucine aminopeptidase activity against the model substrate leucine-amido methyl coumarin. Presumably involved in the processing and regular turnover of intracellular proteins (Probable). Regulates wound signaling and has a role in insect defense.",Presumably involved in the processing and regular turnover of intracellular proteins.,Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0042802; GO:0030145; GO:0070006; GO:0044183,,,,GO:0004175,,,,,0.2842,,1,0.2842,0.4755,no
AMPL2_SOLLC,O24022,ProtT3,Eukaryota,571,"Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. When associated as homohexamer, catalyzes the proteolyzes of Xaa-Leu dipeptides. Possesses leucine aminopeptidase activity against the model substrate leucine-amido methyl coumarin. Presumably involved in the processing and regular turnover of intracellular proteins (Probable). Regulates wound signaling and has a role in insect defense.","Presumably involved in the processing and regular turnover of intracellular proteins. Plastid, chloroplast. Belongs to the peptidase M17 family",Vague,Vague,Maybe,Vague,Yes,not-Yes,GO:0042802; GO:0030145; GO:0070006; GO:0044183,GO:0004177,GO:0004177,GO:0004177,GO:0004177,GO:0004177,0.3763,0.3763,0.3763,0.3763,0.3763,5,0.3763,0.4755,no
AMPL2_SOLLC,O24022,ProtTale,Eukaryota,571,"Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. When associated as homohexamer, catalyzes the proteolyzes of Xaa-Leu dipeptides. Possesses leucine aminopeptidase activity against the model substrate leucine-amido methyl coumarin. Presumably involved in the processing and regular turnover of intracellular proteins (Probable). Regulates wound signaling and has a role in insect defense.",Cytosolic metallopeptidase that catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0042802; GO:0030145; GO:0070006; GO:0044183,GO:0070006,GO:0004177; GO:0008270,GO:0004177; GO:0046872,GO:0004177,GO:0004177; GO:0046872,0.4551,0.5746,0.5906,0.3763,0.5906,5,0.5174,0.4755,no
AMPL2_SOLLC,O24022,Protein2Text,Eukaryota,571,"Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. When associated as homohexamer, catalyzes the proteolyzes of Xaa-Leu dipeptides. Possesses leucine aminopeptidase activity against the model substrate leucine-amido methyl coumarin. Presumably involved in the processing and regular turnover of intracellular proteins (Probable). Regulates wound signaling and has a role in insect defense.","This protein is involved in the degradation of proteins. Specifically, it is a serine protease that catalyzes the hydrolysis of proteins into smaller peptides.",No,No,No,No,Maybe,not-Yes,GO:0042802; GO:0030145; GO:0070006; GO:0044183,GO:0004252,GO:0004252,GO:0008236,GO:0004252,GO:0004252,0.2119,0.2119,0.26,0.2119,0.2119,5,0.2215,0.4755,no
AMPL2_SOLLC,O24022,Reference,Eukaryota,571,"Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. When associated as homohexamer, catalyzes the proteolyzes of Xaa-Leu dipeptides. Possesses leucine aminopeptidase activity against the model substrate leucine-amido methyl coumarin. Presumably involved in the processing and regular turnover of intracellular proteins (Probable). Regulates wound signaling and has a role in insect defense.","Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. When associated as homohexamer, catalyzes the proteolyzes of Xaa-Leu dipeptides. Possesses leucine aminopeptidase activity against the model substrate leucine-amido methyl coumarin. Presumably involved in the processing and regular turnover of intracellular proteins (Probable). Regulates wound signaling and has a role in insect defense.",,,,,,,GO:0042802; GO:0030145; GO:0070006; GO:0044183,GO:0004177,GO:0004177,GO:0004177,GO:0004177,GO:0004177,0.3763,0.3763,0.3763,0.3763,0.3763,5,0.3763,0.4755,no
PHOH2_MYCTU,O53443,ESM2Text,Bacteria,433,"Toxic component of a type II toxin-antitoxin (TA) system. The cognate antitoxin is PhoAT; expression in M.smegmatis (strain mc(2)155) requires the cognate M.tuberculosis antitoxin gene. Expression in M.smegmatis strain mc(2)155 of the toxin alone slows growth and reduces cell viability, effects which are abrogated when cognate antitoxin PhoAT is coexpressed. Unwinds and/or cleaves 5'- tailed RNA in vitro that starts with 5'-AC, the reaction requires hydrolyzable ATP; double-stranded (ds)RNA and dsDNA are not unwound or cleaved. Can be expressed in the absence of its antitoxin gene in E.coli. In vitro has both ATPase and GTPase activity which are the best in vitro substrates; also hydrolyzes ADP>UDP/GDP>CDP>UTP>CTP.","A putative ATPase, its cognate antitoxin.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0032574; GO:0005524; GO:0005525; GO:0016787; GO:0046872; GO:0004518,,,,,,,,,,,0,,0.5209,no
PHOH2_MYCTU,O53443,Prot2Text,Bacteria,433,"Toxic component of a type II toxin-antitoxin (TA) system. The cognate antitoxin is PhoAT; expression in M.smegmatis (strain mc(2)155) requires the cognate M.tuberculosis antitoxin gene. Expression in M.smegmatis strain mc(2)155 of the toxin alone slows growth and reduces cell viability, effects which are abrogated when cognate antitoxin PhoAT is coexpressed. Unwinds and/or cleaves 5'- tailed RNA in vitro that starts with 5'-AC, the reaction requires hydrolyzable ATP; double-stranded (ds)RNA and dsDNA are not unwound or cleaved. Can be expressed in the absence of its antitoxin gene in E.coli. In vitro has both ATPase and GTPase activity which are the best in vitro substrates; also hydrolyzes ADP>UDP/GDP>CDP>UTP>CTP.","FixJ is a DNA-associated protein that interact with FixL, which is a mediator of DNA repair. FixL may bind to the FixS subunit contacting DNA ligase FtsQ.",No,No,Vague,No,No,not-Yes,GO:0032574; GO:0005524; GO:0005525; GO:0016787; GO:0046872; GO:0004518,,,,,,,,,,,0,,0.5209,no
PHOH2_MYCTU,O53443,ProtT3,Bacteria,433,"Toxic component of a type II toxin-antitoxin (TA) system. The cognate antitoxin is PhoAT; expression in M.smegmatis (strain mc(2)155) requires the cognate M.tuberculosis antitoxin gene. Expression in M.smegmatis strain mc(2)155 of the toxin alone slows growth and reduces cell viability, effects which are abrogated when cognate antitoxin PhoAT is coexpressed. Unwinds and/or cleaves 5'- tailed RNA in vitro that starts with 5'-AC, the reaction requires hydrolyzable ATP; double-stranded (ds)RNA and dsDNA are not unwound or cleaved. Can be expressed in the absence of its antitoxin gene in E.coli. In vitro has both ATPase and GTPase activity which are the best in vitro substrates; also hydrolyzes ADP>UDP/GDP>CDP>UTP>CTP.","Catalyzes the phosphorylation of fructose 2,6-bisphosphate (Fru 2,6-P2) to fructose 1,6-bisphosphate (Fru 1,6-P2). Cytoplasm. Belongs to the HisA/HisF family",No,No,No,No,No,not-Yes,GO:0032574; GO:0005524; GO:0005525; GO:0016787; GO:0046872; GO:0004518,GO:0016301,GO:0003872,GO:0016301,GO:0003872,GO:0003873,0.2207,0.1473,0.2207,0.1473,0.1473,5,0.1767,0.5209,no
PHOH2_MYCTU,O53443,ProtTale,Bacteria,433,"Toxic component of a type II toxin-antitoxin (TA) system. The cognate antitoxin is PhoAT; expression in M.smegmatis (strain mc(2)155) requires the cognate M.tuberculosis antitoxin gene. Expression in M.smegmatis strain mc(2)155 of the toxin alone slows growth and reduces cell viability, effects which are abrogated when cognate antitoxin PhoAT is coexpressed. Unwinds and/or cleaves 5'- tailed RNA in vitro that starts with 5'-AC, the reaction requires hydrolyzable ATP; double-stranded (ds)RNA and dsDNA are not unwound or cleaved. Can be expressed in the absence of its antitoxin gene in E.coli. In vitro has both ATPase and GTPase activity which are the best in vitro substrates; also hydrolyzes ADP>UDP/GDP>CDP>UTP>CTP.",Toxic component of a type II toxin-antitoxin (TA) system. Its toxic activity is neutralized by co-expression with cognate antitoxin RnlB. Has ATPase activity in the absence of RnlB; this activity is reduced in the presence of RnlB.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0032574; GO:0005524; GO:0005525; GO:0016787; GO:0046872; GO:0004518,GO:0016887,GO:0016887,GO:0016887,GO:0016887,GO:0016887; GO:0005524,0.231,0.231,0.231,0.231,0.5546,5,0.2957,0.5209,no
PHOH2_MYCTU,O53443,Protein2Text,Bacteria,433,"Toxic component of a type II toxin-antitoxin (TA) system. The cognate antitoxin is PhoAT; expression in M.smegmatis (strain mc(2)155) requires the cognate M.tuberculosis antitoxin gene. Expression in M.smegmatis strain mc(2)155 of the toxin alone slows growth and reduces cell viability, effects which are abrogated when cognate antitoxin PhoAT is coexpressed. Unwinds and/or cleaves 5'- tailed RNA in vitro that starts with 5'-AC, the reaction requires hydrolyzable ATP; double-stranded (ds)RNA and dsDNA are not unwound or cleaved. Can be expressed in the absence of its antitoxin gene in E.coli. In vitro has both ATPase and GTPase activity which are the best in vitro substrates; also hydrolyzes ADP>UDP/GDP>CDP>UTP>CTP.","This protein is involved in DNA repair, specifically in the removal of DNA lesions such as single-strand breaks, double-strand breaks, and DNA interstrand crosslinks.",No,No,No,No,No,not-Yes,GO:0032574; GO:0005524; GO:0005525; GO:0016787; GO:0046872; GO:0004518,,,,,,,,,,,0,,0.5209,no
PHOH2_MYCTU,O53443,Reference,Bacteria,433,"Toxic component of a type II toxin-antitoxin (TA) system. The cognate antitoxin is PhoAT; expression in M.smegmatis (strain mc(2)155) requires the cognate M.tuberculosis antitoxin gene. Expression in M.smegmatis strain mc(2)155 of the toxin alone slows growth and reduces cell viability, effects which are abrogated when cognate antitoxin PhoAT is coexpressed. Unwinds and/or cleaves 5'- tailed RNA in vitro that starts with 5'-AC, the reaction requires hydrolyzable ATP; double-stranded (ds)RNA and dsDNA are not unwound or cleaved. Can be expressed in the absence of its antitoxin gene in E.coli. In vitro has both ATPase and GTPase activity which are the best in vitro substrates; also hydrolyzes ADP>UDP/GDP>CDP>UTP>CTP.","Toxic component of a type II toxin-antitoxin (TA) system. The cognate antitoxin is PhoAT; expression in M.smegmatis (strain mc(2)155) requires the cognate M.tuberculosis antitoxin gene. Expression in M.smegmatis strain mc(2)155 of the toxin alone slows growth and reduces cell viability, effects which are abrogated when cognate antitoxin PhoAT is coexpressed. Unwinds and/or cleaves 5'- tailed RNA in vitro that starts with 5'-AC, the reaction requires hydrolyzable ATP; double-stranded (ds)RNA and dsDNA are not unwound or cleaved. Can be expressed in the absence of its antitoxin gene in E.coli. In vitro has both ATPase and GTPase activity which are the best in vitro substrates; also hydrolyzes ADP>UDP/GDP>CDP>UTP>CTP.",,,,,,,GO:0032574; GO:0005524; GO:0005525; GO:0016787; GO:0046872; GO:0004518,GO:0016887; GO:0003924,GO:0003724; GO:0017111,GO:0016887; GO:0003924; GO:0017111,GO:0004386; GO:0016887; GO:0005524,GO:0004386; GO:0005524; GO:0003723; GO:0017111,0.2661,0.4343,0.3032,0.6606,0.6367,5,0.4602,0.5209,no
DHOM_PYRHO,O58802,ESM2Text,Archaea,319,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate. Utilizes NADH but not NADPH as coenzyme.",Specifically catalyzes the NAD(+)-dependent dehydrogenation of L-aspartate to iminoaspartate.,No,No,No,No,No,not-Yes,GO:0004412; GO:0046872; GO:0070403; GO:0050661,GO:0016491; GO:0051287,GO:0008734,GO:0008734,GO:0008734,GO:0008734,0.637,0.1386,0.1386,0.1386,0.1386,5,0.2383,0.2795,no
DHOM_PYRHO,O58802,Prot2Text,Archaea,319,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate. Utilizes NADH but not NADPH as coenzyme.",Catalyzes the NADPH-dependent reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).,No,No,No,No,No,not-Yes,GO:0004412; GO:0046872; GO:0070403; GO:0050661,GO:0030604,GO:0030604,GO:0030604,GO:0030604,GO:0030604,0.336,0.336,0.336,0.336,0.336,5,0.336,0.2795,no
DHOM_PYRHO,O58802,ProtT3,Archaea,319,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate. Utilizes NADH but not NADPH as coenzyme.",Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004412; GO:0046872; GO:0070403; GO:0050661,GO:0016616,GO:0016616,GO:0016616,GO:0016616,GO:0016616,0.3955,0.3955,0.3955,0.3955,0.3955,5,0.3955,0.2795,no
DHOM_PYRHO,O58802,ProtTale,Archaea,319,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate. Utilizes NADH but not NADPH as coenzyme.","Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004412; GO:0046872; GO:0070403; GO:0050661,GO:0004412,GO:0004412,GO:0004412,GO:0004412,GO:0004412,0.4445,0.4445,0.4445,0.4445,0.4445,5,0.4445,0.2795,no
DHOM_PYRHO,O58802,Protein2Text,Archaea,319,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate. Utilizes NADH but not NADPH as coenzyme.","This protein is involved in the conversion of 2,3-bisphosphoglycerate to 3-phosphoglycerate. This is a key step in the glycolytic pathway. The molecular function of this protein is likely to be a kinase, specifically a 2,3-bisphosphoglycerate kinase.",No,No,No,No,No,not-Yes,GO:0004412; GO:0046872; GO:0070403; GO:0050661,,,,,,,,,,,0,,0.2795,no
DHOM_PYRHO,O58802,Reference,Archaea,319,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate. Utilizes NADH but not NADPH as coenzyme.","Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate. Utilizes NADH but not NADPH as coenzyme.",,,,,,,GO:0004412; GO:0046872; GO:0070403; GO:0050661,GO:0004412,GO:0004399,GO:0004412; GO:0051287,GO:0004412,GO:0004412,0.4445,0.336,0.7697,0.4445,0.4445,5,0.4878,0.2795,no
RAF24_ARATH,O64768,ESM2Text,Eukaryota,1257,"RAF-like protein kinase acting, together with RAF20, as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process.",Scaffold protein that assembles as a heterodimer with the serine/threonine kinase spm-2 to regulate global gene expression in response to nitrogen starvation. Required for cell fate specification in the germline and the germline. Required with spm-2 for the establishment of the embryonic cortex and for cortex development.,No,Maybe,Maybe,No,No,not-Yes,GO:0005524; GO:0004672; GO:0004674; GO:0004712,,,,,,,,,,,0,,0.6749,yes
RAF24_ARATH,O64768,Prot2Text,Eukaryota,1257,"RAF-like protein kinase acting, together with RAF20, as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process.","Member of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly. In the mitotic cell, cdc-14 acts as central scaffold for assembling the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.",No,No,No,No,No,not-Yes,GO:0005524; GO:0004672; GO:0004674; GO:0004712,,,,,,,,,,,0,,0.6749,yes
RAF24_ARATH,O64768,ProtT3,Eukaryota,1257,"RAF-like protein kinase acting, together with RAF20, as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process.",Nucleus. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WNK subfamily,Maybe,Vague,Maybe,Vague,Vague,not-Yes,GO:0005524; GO:0004672; GO:0004674; GO:0004712,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,0.9552,0.9552,0.9552,0.9552,0.7571,5,0.9156,0.6749,yes
RAF24_ARATH,O64768,ProtTale,Eukaryota,1257,"RAF-like protein kinase acting, together with RAF20, as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process.",Acts as a serine/threonine-protein kinase.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004672; GO:0004674; GO:0004712,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,0.9552,0.9552,0.9552,0.7571,0.9552,5,0.9156,0.6749,yes
RAF24_ARATH,O64768,Protein2Text,Eukaryota,1257,"RAF-like protein kinase acting, together with RAF20, as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process.","The molecular function of this protein is as a receptor-like kinase. It is involved in plant growth and development, particularly in response to environmental stimuli. Specifically, it acts as a receptor for peptides that trigger cell elongation, such as the CLAVATA3/ESR-related (CLE) peptides.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004672; GO:0004674; GO:0004712,GO:0004674,GO:0004674; GO:0004872,GO:0004674,GO:0004674,GO:0004675,0.7571,0.66,0.7571,0.7571,0.5692,5,0.7001,0.6749,yes
RAF24_ARATH,O64768,Reference,Eukaryota,1257,"RAF-like protein kinase acting, together with RAF20, as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process.","RAF-like protein kinase acting, together with RAF20, as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process.",,,,,,,GO:0005524; GO:0004672; GO:0004674; GO:0004712,GO:0004674,GO:0004674,GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.7571,0.7571,0.7571,0.9552,0.9552,5,0.8363,0.6749,yes
RAB7_DROME,O76742,ESM2Text,Eukaryota,207,"Small GTPase which cycles between active GTP-bound and inactive GDP-bound states (Probable). In its active state, binds to a variety of effector proteins playing a key role in the regulation of endo-lysosomal trafficking (Probable). Involved in microtubule minus and plus end-directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades (Probable). Governs early-to-late endosomal to lysosomal maturation. Controls endocytic cargo sorting towards the late endosome facilitating its eventual endolysosomal-mediated degradation. Together with Rab2 involved in promoting fusion of autophagosomes and endosomes with lysosomes probably through recruitment of the HOPS tethering complex. Involved in biosynthetic transport to lysosomes (Probable). Involved in establishing morphogen concentration gradients, for example of the TGF- beta homolog dpp/decapentaplegic, during pattern formation and organogenesis. Together with the Mon1-Ccz1 complex, required for autolysosome formation in fat cells and autophagic degradation during starvation-induced basal and developmental autophagy. Together with Mon1, regulates levels of postsynaptic glutamate receptor GluRIIA in the neuromuscular junction (NMJ) presynapse. Required for autophagocytosis-dependent remodeling of myofibrils and transverse-tubules (T-tubules) during metamorphosis. Involved in intracellular trafficking of the carbohydrate transporter Tret1 in glial cells of the blood brain barrier, influencing its subcellular localization and protein levels.",Intracellular vesicle trafficking and protein transport.,Vague,Maybe,Vague,Maybe,Maybe,not-Yes,GO:0003925; GO:0005525; GO:0003924; GO:0044877,,,,,,,,,,,0,,0.5462,yes
RAB7_DROME,O76742,Prot2Text,Eukaryota,207,"Small GTPase which cycles between active GTP-bound and inactive GDP-bound states (Probable). In its active state, binds to a variety of effector proteins playing a key role in the regulation of endo-lysosomal trafficking (Probable). Involved in microtubule minus and plus end-directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades (Probable). Governs early-to-late endosomal to lysosomal maturation. Controls endocytic cargo sorting towards the late endosome facilitating its eventual endolysosomal-mediated degradation. Together with Rab2 involved in promoting fusion of autophagosomes and endosomes with lysosomes probably through recruitment of the HOPS tethering complex. Involved in biosynthetic transport to lysosomes (Probable). Involved in establishing morphogen concentration gradients, for example of the TGF- beta homolog dpp/decapentaplegic, during pattern formation and organogenesis. Together with the Mon1-Ccz1 complex, required for autolysosome formation in fat cells and autophagic degradation during starvation-induced basal and developmental autophagy. Together with Mon1, regulates levels of postsynaptic glutamate receptor GluRIIA in the neuromuscular junction (NMJ) presynapse. Required for autophagocytosis-dependent remodeling of myofibrils and transverse-tubules (T-tubules) during metamorphosis. Involved in intracellular trafficking of the carbohydrate transporter Tret1 in glial cells of the blood brain barrier, influencing its subcellular localization and protein levels.",Intracellular vesicle trafficking and protein transport. Functions in autophagy. Involved in peroxisome biogenesis through regulation of autophagy-related processes.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0003925; GO:0005525; GO:0003924; GO:0044877,,,,,,,,,,,0,,0.5462,yes
RAB7_DROME,O76742,ProtT3,Eukaryota,207,"Small GTPase which cycles between active GTP-bound and inactive GDP-bound states (Probable). In its active state, binds to a variety of effector proteins playing a key role in the regulation of endo-lysosomal trafficking (Probable). Involved in microtubule minus and plus end-directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades (Probable). Governs early-to-late endosomal to lysosomal maturation. Controls endocytic cargo sorting towards the late endosome facilitating its eventual endolysosomal-mediated degradation. Together with Rab2 involved in promoting fusion of autophagosomes and endosomes with lysosomes probably through recruitment of the HOPS tethering complex. Involved in biosynthetic transport to lysosomes (Probable). Involved in establishing morphogen concentration gradients, for example of the TGF- beta homolog dpp/decapentaplegic, during pattern formation and organogenesis. Together with the Mon1-Ccz1 complex, required for autolysosome formation in fat cells and autophagic degradation during starvation-induced basal and developmental autophagy. Together with Mon1, regulates levels of postsynaptic glutamate receptor GluRIIA in the neuromuscular junction (NMJ) presynapse. Required for autophagocytosis-dependent remodeling of myofibrils and transverse-tubules (T-tubules) during metamorphosis. Involved in intracellular trafficking of the carbohydrate transporter Tret1 in glial cells of the blood brain barrier, influencing its subcellular localization and protein levels.",Protein transport. Probably involved in vesicular traffic (By similarity). Cell membrane; Lipid-anchor; Cytoplasmic side. Belongs to the small GTPase superfamily. Rab family,Vague,Yes,Yes,Maybe,Maybe,not-Yes,GO:0003925; GO:0005525; GO:0003924; GO:0044877,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,0.8353,0.8353,0.8353,0.8353,0.8353,5,0.8353,0.5462,yes
RAB7_DROME,O76742,ProtTale,Eukaryota,207,"Small GTPase which cycles between active GTP-bound and inactive GDP-bound states (Probable). In its active state, binds to a variety of effector proteins playing a key role in the regulation of endo-lysosomal trafficking (Probable). Involved in microtubule minus and plus end-directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades (Probable). Governs early-to-late endosomal to lysosomal maturation. Controls endocytic cargo sorting towards the late endosome facilitating its eventual endolysosomal-mediated degradation. Together with Rab2 involved in promoting fusion of autophagosomes and endosomes with lysosomes probably through recruitment of the HOPS tethering complex. Involved in biosynthetic transport to lysosomes (Probable). Involved in establishing morphogen concentration gradients, for example of the TGF- beta homolog dpp/decapentaplegic, during pattern formation and organogenesis. Together with the Mon1-Ccz1 complex, required for autolysosome formation in fat cells and autophagic degradation during starvation-induced basal and developmental autophagy. Together with Mon1, regulates levels of postsynaptic glutamate receptor GluRIIA in the neuromuscular junction (NMJ) presynapse. Required for autophagocytosis-dependent remodeling of myofibrils and transverse-tubules (T-tubules) during metamorphosis. Involved in intracellular trafficking of the carbohydrate transporter Tret1 in glial cells of the blood brain barrier, influencing its subcellular localization and protein levels.","The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0003925; GO:0005525; GO:0003924; GO:0044877,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,0.8353,0.8353,0.8353,0.8353,0.8353,5,0.8353,0.5462,yes
RAB7_DROME,O76742,Protein2Text,Eukaryota,207,"Small GTPase which cycles between active GTP-bound and inactive GDP-bound states (Probable). In its active state, binds to a variety of effector proteins playing a key role in the regulation of endo-lysosomal trafficking (Probable). Involved in microtubule minus and plus end-directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades (Probable). Governs early-to-late endosomal to lysosomal maturation. Controls endocytic cargo sorting towards the late endosome facilitating its eventual endolysosomal-mediated degradation. Together with Rab2 involved in promoting fusion of autophagosomes and endosomes with lysosomes probably through recruitment of the HOPS tethering complex. Involved in biosynthetic transport to lysosomes (Probable). Involved in establishing morphogen concentration gradients, for example of the TGF- beta homolog dpp/decapentaplegic, during pattern formation and organogenesis. Together with the Mon1-Ccz1 complex, required for autolysosome formation in fat cells and autophagic degradation during starvation-induced basal and developmental autophagy. Together with Mon1, regulates levels of postsynaptic glutamate receptor GluRIIA in the neuromuscular junction (NMJ) presynapse. Required for autophagocytosis-dependent remodeling of myofibrils and transverse-tubules (T-tubules) during metamorphosis. Involved in intracellular trafficking of the carbohydrate transporter Tret1 in glial cells of the blood brain barrier, influencing its subcellular localization and protein levels.","The molecular function of this protein is likely to be involved in intracellular transport, as it is a member of the Ras superfamily of small GTPases, which are involved in regulating various cellular processes, including vesicle transport and signaling. Specifically, this protein may play a role in regulating the movement of vesicles within the cell, which is essential for maintaining cellular homeostasis and responding to changes in the environment.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0003925; GO:0005525; GO:0003924; GO:0044877,GO:0003924,GO:0003924,,GO:0003924,GO:0003924,0.5979,0.5979,,0.5979,0.5979,4,0.5979,0.5462,yes
RAB7_DROME,O76742,Reference,Eukaryota,207,"Small GTPase which cycles between active GTP-bound and inactive GDP-bound states (Probable). In its active state, binds to a variety of effector proteins playing a key role in the regulation of endo-lysosomal trafficking (Probable). Involved in microtubule minus and plus end-directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades (Probable). Governs early-to-late endosomal to lysosomal maturation. Controls endocytic cargo sorting towards the late endosome facilitating its eventual endolysosomal-mediated degradation. Together with Rab2 involved in promoting fusion of autophagosomes and endosomes with lysosomes probably through recruitment of the HOPS tethering complex. Involved in biosynthetic transport to lysosomes (Probable). Involved in establishing morphogen concentration gradients, for example of the TGF- beta homolog dpp/decapentaplegic, during pattern formation and organogenesis. Together with the Mon1-Ccz1 complex, required for autolysosome formation in fat cells and autophagic degradation during starvation-induced basal and developmental autophagy. Together with Mon1, regulates levels of postsynaptic glutamate receptor GluRIIA in the neuromuscular junction (NMJ) presynapse. Required for autophagocytosis-dependent remodeling of myofibrils and transverse-tubules (T-tubules) during metamorphosis. Involved in intracellular trafficking of the carbohydrate transporter Tret1 in glial cells of the blood brain barrier, influencing its subcellular localization and protein levels.","Small GTPase which cycles between active GTP-bound and inactive GDP-bound states (Probable). In its active state, binds to a variety of effector proteins playing a key role in the regulation of endo-lysosomal trafficking (Probable). Involved in microtubule minus and plus end-directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades (Probable). Governs early-to-late endosomal to lysosomal maturation. Controls endocytic cargo sorting towards the late endosome facilitating its eventual endolysosomal-mediated degradation. Together with Rab2 involved in promoting fusion of autophagosomes and endosomes with lysosomes probably through recruitment of the HOPS tethering complex. Involved in biosynthetic transport to lysosomes (Probable). Involved in establishing morphogen concentration gradients, for example of the TGF- beta homolog dpp/decapentaplegic, during pattern formation and organogenesis. Together with the Mon1-Ccz1 complex, required for autolysosome formation in fat cells and autophagic degradation during starvation-induced basal and developmental autophagy. Together with Mon1, regulates levels of postsynaptic glutamate receptor GluRIIA in the neuromuscular junction (NMJ) presynapse. Required for autophagocytosis-dependent remodeling of myofibrils and transverse-tubules (T-tubules) during metamorphosis. Involved in intracellular trafficking of the carbohydrate transporter Tret1 in glial cells of the blood brain barrier, influencing its subcellular localization and protein levels.",,,,,,,GO:0003925; GO:0005525; GO:0003924; GO:0044877,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0005525; GO:0003924,0.8353,0.8353,0.8353,0.8353,0.8353,5,0.8353,0.5462,yes
BLAV1_PSEAI,O87489,ESM2Text,Bacteria,299,"Class A beta-lactamase which confers resistance to the beta- lactam antibiotics, including penicillins and cephalosporins, in E.coli strain JM109. Acts via hydrolysis of the beta-lactam ring. Has penicillin-, and cephalosporin-hydrolyzing activities.","Hydrolyzes carbapenems, penicillins, cephalosporins and aztreonam.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3872,no
BLAV1_PSEAI,O87489,Prot2Text,Bacteria,299,"Class A beta-lactamase which confers resistance to the beta- lactam antibiotics, including penicillins and cephalosporins, in E.coli strain JM109. Acts via hydrolysis of the beta-lactam ring. Has penicillin-, and cephalosporin-hydrolyzing activities.","Hydrolyzes beta-lactams antibiotics. Rates of hydrolysis relative to benzylpenicillin =100: ampicillin = 27, carbenicillin = 25, cloxacillin = 0, cephaloridine = 4.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3872,no
BLAV1_PSEAI,O87489,ProtT3,Bacteria,299,"Class A beta-lactamase which confers resistance to the beta- lactam antibiotics, including penicillins and cephalosporins, in E.coli strain JM109. Acts via hydrolysis of the beta-lactam ring. Has penicillin-, and cephalosporin-hydrolyzing activities.",Belongs to the class-A beta-lactamase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3872,no
BLAV1_PSEAI,O87489,ProtTale,Bacteria,299,"Class A beta-lactamase which confers resistance to the beta- lactam antibiotics, including penicillins and cephalosporins, in E.coli strain JM109. Acts via hydrolysis of the beta-lactam ring. Has penicillin-, and cephalosporin-hydrolyzing activities.","Metallo-beta-lactamase, which cleaves beta-lactam antibiotics such as penicillins, cephalosporins, and carbapenems. Degrades the beta-lactam ring and hydrolyzes the amide bond of the beta-lactam ring. Hydrolyzes broad-spectrum cephalosporins (cefazolin, cefoxitin, cefuroxime) and carbapenems (imipenem, meropenem, tazobactam), but not penicillins (penicillin G, ampicillin, and amoxicillin).",Yes,Yes,Maybe,Yes,Maybe,Yes,GO:0008800,GO:0008800,GO:0008800; GO:0008270,GO:0008800; GO:0046872,GO:0008800,GO:0008800; GO:0046872,1.0,0.6895,0.6963,1.0,0.6963,5,0.8164,0.3872,no
BLAV1_PSEAI,O87489,Protein2Text,Bacteria,299,"Class A beta-lactamase which confers resistance to the beta- lactam antibiotics, including penicillins and cephalosporins, in E.coli strain JM109. Acts via hydrolysis of the beta-lactam ring. Has penicillin-, and cephalosporin-hydrolyzing activities.","This protein is a metalloprotease, which means it has a catalytic metal center that helps to break down molecules. More specifically, it is a hydrolase, which is a type of enzyme that uses water to catalyze a chemical reaction. 

In the case of this protein, it is a cysteine hydrolase, which means it uses a cysteine residue as the nucleophile in its catalytic mechanism. 

This protein is also an enzyme, which is a type of protein that catalyzes a specific chemical reaction. 

It is a metallohydrolase, which means it uses a metal ion to help catalyze its reaction. 

It is a cysteine-dependent metallohydrolase, which means it uses a cysteine residue and a metal ion to help catalyze its reaction. 

It is an enzyme that hydrolyzes beta-lactam antibiotics. 

It is a beta-lactamase, which is a type of enzyme that hydrolyzes beta-lactam antibiotics. 

It is a serine beta-lactamase, which means it uses a serine residue to hydrolyze beta-lactam antibiotics. 

It is a metallo-beta-lactamase, which means it uses a metal ion to help hydrolyze beta-lactam antibiotics. 

It is a zinc-dependent metallo-beta-lactamase, which means it uses a zinc ion to help hydrolyze beta-lactam antibiotics. 

It is an enzyme that hydrolyzes beta-lactam antibiotics by opening the beta-lactam ring. 

It is a beta-lactamase that hydrolyzes penicillins, cephalosporins, and carbapenems. 

It is a carbapenem-hydrolyzing beta-lactamase, which means it specifically hydrolyzes carbapenems. 

It is an enzyme that hydrolyzes beta-lactam antibiotics by using a metal ion to help catalyze the reaction. 

It is a zinc-dependent beta-lactamase that hydrolyzes beta-lactam antibiotics. 

It is an enzyme that hydrolyzes beta-lactam antibiotics by using a serine residue to help catalyze the reaction. 

It is a serine-beta-lactamase that hydrolyzes beta-lactam antibiotics. 

It is an enzyme that hydrolyzes beta-lactam antibiotics by using a cysteine residue to",No,Vague,Vague,No,No,not-Yes,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3872,no
BLAV1_PSEAI,O87489,Reference,Bacteria,299,"Class A beta-lactamase which confers resistance to the beta- lactam antibiotics, including penicillins and cephalosporins, in E.coli strain JM109. Acts via hydrolysis of the beta-lactam ring. Has penicillin-, and cephalosporin-hydrolyzing activities.","Class A beta-lactamase which confers resistance to the beta- lactam antibiotics, including penicillins and cephalosporins, in E.coli strain JM109. Acts via hydrolysis of the beta-lactam ring. Has penicillin-, and cephalosporin-hydrolyzing activities.",,,,,,,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3872,no
OXLA2_BOTJR,P0DV78,ESM2Text,Eukaryota,116,"Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Shows very high enzymatic activity on L-Met and L-Leu, high activity on L-Ile, L-Phe and L-Tyr and moderate activity on L-His. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, and antibacterial, as well as regulation of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist- induced aggregation. These different effects are probably due to different experimental conditions. In vitro, has a strong antiprotozoal effect against Leishmania amazonensis (IC(50)=4.56 ug/mL) and Trypanosoma cruzi (IC(50)=4.85 ug/mL). It also causes cell death and DNA damage in hepatocarcinoma cells (HepG2) in vitro by inducing oxidative stress. It exerts cytotoxicity towards colorectal adenocarcinomahuman cells (Caco-2) by acting on multiple intracellular targets. It diminishes cell viability by decreasing mitochondrial activity, the activity of acid phosphatases, and lysosomal function. In addition, it increases intracellular levels of reactive oxygen species and DNA damage, it elevates the expression of the pro-inflammatory cytokine genes TNF and IL6, and lowers the expression of the apoptotic-related genes. Also induces cytotoxicity (IC(50)=1.80 ug/mL) and apoptosis in MCF-7 cells (a human breast adeno-carcinoma cell line) by activating the intrinsic and extrinsic apoptosis pathways, but are not cytotoxic towards MCF-10A cells (a non-tumorigenic human breast epithelial cell line).",Inhibits protein synthesis.,No,No,No,No,No,not-Yes,GO:0001716; GO:0000166; GO:0090729,,,,,,,,,,,0,,0.3187,no
OXLA2_BOTJR,P0DV78,Prot2Text,Eukaryota,116,"Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Shows very high enzymatic activity on L-Met and L-Leu, high activity on L-Ile, L-Phe and L-Tyr and moderate activity on L-His. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, and antibacterial, as well as regulation of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist- induced aggregation. These different effects are probably due to different experimental conditions. In vitro, has a strong antiprotozoal effect against Leishmania amazonensis (IC(50)=4.56 ug/mL) and Trypanosoma cruzi (IC(50)=4.85 ug/mL). It also causes cell death and DNA damage in hepatocarcinoma cells (HepG2) in vitro by inducing oxidative stress. It exerts cytotoxicity towards colorectal adenocarcinomahuman cells (Caco-2) by acting on multiple intracellular targets. It diminishes cell viability by decreasing mitochondrial activity, the activity of acid phosphatases, and lysosomal function. In addition, it increases intracellular levels of reactive oxygen species and DNA damage, it elevates the expression of the pro-inflammatory cytokine genes TNF and IL6, and lowers the expression of the apoptotic-related genes. Also induces cytotoxicity (IC(50)=1.80 ug/mL) and apoptosis in MCF-7 cells (a human breast adeno-carcinoma cell line) by activating the intrinsic and extrinsic apoptosis pathways, but are not cytotoxic towards MCF-10A cells (a non-tumorigenic human breast epithelial cell line).","Venom protein that causes edema, enhances vascular permeability and is likely related to the inflammatory activity of the venom.",Vague,Vague,No,No,No,not-Yes,GO:0001716; GO:0000166; GO:0090729,,,,,GO:0090729,,,,,0.5991,1,0.5991,0.3187,no
OXLA2_BOTJR,P0DV78,ProtT3,Eukaryota,116,"Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Shows very high enzymatic activity on L-Met and L-Leu, high activity on L-Ile, L-Phe and L-Tyr and moderate activity on L-His. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, and antibacterial, as well as regulation of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist- induced aggregation. These different effects are probably due to different experimental conditions. In vitro, has a strong antiprotozoal effect against Leishmania amazonensis (IC(50)=4.56 ug/mL) and Trypanosoma cruzi (IC(50)=4.85 ug/mL). It also causes cell death and DNA damage in hepatocarcinoma cells (HepG2) in vitro by inducing oxidative stress. It exerts cytotoxicity towards colorectal adenocarcinomahuman cells (Caco-2) by acting on multiple intracellular targets. It diminishes cell viability by decreasing mitochondrial activity, the activity of acid phosphatases, and lysosomal function. In addition, it increases intracellular levels of reactive oxygen species and DNA damage, it elevates the expression of the pro-inflammatory cytokine genes TNF and IL6, and lowers the expression of the apoptotic-related genes. Also induces cytotoxicity (IC(50)=1.80 ug/mL) and apoptosis in MCF-7 cells (a human breast adeno-carcinoma cell line) by activating the intrinsic and extrinsic apoptosis pathways, but are not cytotoxic towards MCF-10A cells (a non-tumorigenic human breast epithelial cell line).","Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (By similarity). Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation (By similarity). Its toxic effects are probably mediated by hydrogen peroxide (By similarity). Secreted, extracellular space. Belongs to the flavin monoamine oxidase family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0001716; GO:0000166; GO:0090729,GO:0016638,GO:0001584,GO:0001716,GO:0016641,GO:0016641,0.4272,0.0,0.5694,0.4652,0.4652,5,0.3854,0.3187,no
OXLA2_BOTJR,P0DV78,ProtTale,Eukaryota,116,"Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Shows very high enzymatic activity on L-Met and L-Leu, high activity on L-Ile, L-Phe and L-Tyr and moderate activity on L-His. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, and antibacterial, as well as regulation of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist- induced aggregation. These different effects are probably due to different experimental conditions. In vitro, has a strong antiprotozoal effect against Leishmania amazonensis (IC(50)=4.56 ug/mL) and Trypanosoma cruzi (IC(50)=4.85 ug/mL). It also causes cell death and DNA damage in hepatocarcinoma cells (HepG2) in vitro by inducing oxidative stress. It exerts cytotoxicity towards colorectal adenocarcinomahuman cells (Caco-2) by acting on multiple intracellular targets. It diminishes cell viability by decreasing mitochondrial activity, the activity of acid phosphatases, and lysosomal function. In addition, it increases intracellular levels of reactive oxygen species and DNA damage, it elevates the expression of the pro-inflammatory cytokine genes TNF and IL6, and lowers the expression of the apoptotic-related genes. Also induces cytotoxicity (IC(50)=1.80 ug/mL) and apoptosis in MCF-7 cells (a human breast adeno-carcinoma cell line) by activating the intrinsic and extrinsic apoptosis pathways, but are not cytotoxic towards MCF-10A cells (a non-tumorigenic human breast epithelial cell line).",May be involved in the control of flowering time.,No,No,No,No,No,not-Yes,GO:0001716; GO:0000166; GO:0090729,,,,,,,,,,,0,,0.3187,no
OXLA2_BOTJR,P0DV78,Protein2Text,Eukaryota,116,"Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Shows very high enzymatic activity on L-Met and L-Leu, high activity on L-Ile, L-Phe and L-Tyr and moderate activity on L-His. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, and antibacterial, as well as regulation of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist- induced aggregation. These different effects are probably due to different experimental conditions. In vitro, has a strong antiprotozoal effect against Leishmania amazonensis (IC(50)=4.56 ug/mL) and Trypanosoma cruzi (IC(50)=4.85 ug/mL). It also causes cell death and DNA damage in hepatocarcinoma cells (HepG2) in vitro by inducing oxidative stress. It exerts cytotoxicity towards colorectal adenocarcinomahuman cells (Caco-2) by acting on multiple intracellular targets. It diminishes cell viability by decreasing mitochondrial activity, the activity of acid phosphatases, and lysosomal function. In addition, it increases intracellular levels of reactive oxygen species and DNA damage, it elevates the expression of the pro-inflammatory cytokine genes TNF and IL6, and lowers the expression of the apoptotic-related genes. Also induces cytotoxicity (IC(50)=1.80 ug/mL) and apoptosis in MCF-7 cells (a human breast adeno-carcinoma cell line) by activating the intrinsic and extrinsic apoptosis pathways, but are not cytotoxic towards MCF-10A cells (a non-tumorigenic human breast epithelial cell line).","This protein is involved in a molecular function related to its ability to bind to other molecules, specifically proteins, and is likely involved in a process related to protein-protein interactions or protein binding. However, without more specific information, it is difficult to determine the exact molecular function of this protein.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0001716; GO:0000166; GO:0090729,,,,,,,,,,,0,,0.3187,no
OXLA2_BOTJR,P0DV78,Reference,Eukaryota,116,"Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Shows very high enzymatic activity on L-Met and L-Leu, high activity on L-Ile, L-Phe and L-Tyr and moderate activity on L-His. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, and antibacterial, as well as regulation of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist- induced aggregation. These different effects are probably due to different experimental conditions. In vitro, has a strong antiprotozoal effect against Leishmania amazonensis (IC(50)=4.56 ug/mL) and Trypanosoma cruzi (IC(50)=4.85 ug/mL). It also causes cell death and DNA damage in hepatocarcinoma cells (HepG2) in vitro by inducing oxidative stress. It exerts cytotoxicity towards colorectal adenocarcinomahuman cells (Caco-2) by acting on multiple intracellular targets. It diminishes cell viability by decreasing mitochondrial activity, the activity of acid phosphatases, and lysosomal function. In addition, it increases intracellular levels of reactive oxygen species and DNA damage, it elevates the expression of the pro-inflammatory cytokine genes TNF and IL6, and lowers the expression of the apoptotic-related genes. Also induces cytotoxicity (IC(50)=1.80 ug/mL) and apoptosis in MCF-7 cells (a human breast adeno-carcinoma cell line) by activating the intrinsic and extrinsic apoptosis pathways, but are not cytotoxic towards MCF-10A cells (a non-tumorigenic human breast epithelial cell line).","Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Shows very high enzymatic activity on L-Met and L-Leu, high activity on L-Ile, L-Phe and L-Tyr and moderate activity on L-His. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, and antibacterial, as well as regulation of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist- induced aggregation. These different effects are probably due to different experimental conditions. In vitro, has a strong antiprotozoal effect against Leishmania amazonensis (IC(50)=4.56 ug/mL) and Trypanosoma cruzi (IC(50)=4.85 ug/mL). It also causes cell death and DNA damage in hepatocarcinoma cells (HepG2) in vitro by inducing oxidative stress. It exerts cytotoxicity towards colorectal adenocarcinomahuman cells (Caco-2) by acting on multiple intracellular targets. It diminishes cell viability by decreasing mitochondrial activity, the activity of acid phosphatases, and lysosomal function. In addition, it increases intracellular levels of reactive oxygen species and DNA damage, it elevates the expression of the pro-inflammatory cytokine genes TNF and IL6, and lowers the expression of the apoptotic-related genes. Also induces cytotoxicity (IC(50)=1.80 ug/mL) and apoptosis in MCF-7 cells (a human breast adeno-carcinoma cell line) by activating the intrinsic and extrinsic apoptosis pathways, but are not cytotoxic towards MCF-10A cells (a non-tumorigenic human breast epithelial cell line).",,,,,,,GO:0001716; GO:0000166; GO:0090729,GO:0001716,GO:0004043,GO:0016639,GO:0001714; GO:0016491; GO:0050660,GO:0001720; GO:0016491,0.5694,0.1958,0.3531,0.4907,0.3169,5,0.3852,0.3187,no
LNBX_BIFL2,P0DW93,ESM2Text,Bacteria,1599,"Present in the infant gut, this enzyme is involved in the assimilation of type-1 human milk oligosaccharides (HMOs). It hydrolyzes via a retaining mechanism the beta-D-GlcNAc-(1->3)-beta-D-Gal linkage in lacto-N- tetraose (LNT or beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal- (1->4)-D-Glc), an abundant HMO unique to human breast milk, releasing lacto-N-biose (LNB or beta-D-Gal-(1->3)-D-GlcNAc) and lactose. With a much lower efficiency, is also able to cleave the same linkage in lacto-N-fucopentaose I (alpha-Fuc(1->2)-beta-D-Gal-(1->3)-beta-D- GlcNAc(1->3)-beta-D-Gal-(1->4)-D-Glc), and sialyllacto-N-tetraose a (alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal- (1->4)-D-Glc). Is a key enzymatic factor for growth and proliferation of B.longum in the gut ecosystem of breast-fed infants.",Degrades polygalacturonate or partially methylated pectin.,No,No,No,No,No,not-Yes,GO:0047403; GO:0046872,GO:0004650,GO:0004650,GO:0004650,GO:0004650,GO:0004650,0.5156,0.5156,0.5156,0.5156,0.5156,5,0.5156,0.3892,no
LNBX_BIFL2,P0DW93,Prot2Text,Bacteria,1599,"Present in the infant gut, this enzyme is involved in the assimilation of type-1 human milk oligosaccharides (HMOs). It hydrolyzes via a retaining mechanism the beta-D-GlcNAc-(1->3)-beta-D-Gal linkage in lacto-N- tetraose (LNT or beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal- (1->4)-D-Glc), an abundant HMO unique to human breast milk, releasing lacto-N-biose (LNB or beta-D-Gal-(1->3)-D-GlcNAc) and lactose. With a much lower efficiency, is also able to cleave the same linkage in lacto-N-fucopentaose I (alpha-Fuc(1->2)-beta-D-Gal-(1->3)-beta-D- GlcNAc(1->3)-beta-D-Gal-(1->4)-D-Glc), and sialyllacto-N-tetraose a (alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal- (1->4)-D-Glc). Is a key enzymatic factor for growth and proliferation of B.longum in the gut ecosystem of breast-fed infants.","Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins.",No,No,No,No,No,not-Yes,GO:0047403; GO:0046872,GO:0030599,GO:0030570,GO:0030570,GO:0030570,GO:0030599,0.2554,0.1628,0.1628,0.1628,0.2554,5,0.1998,0.3892,no
LNBX_BIFL2,P0DW93,ProtT3,Bacteria,1599,"Present in the infant gut, this enzyme is involved in the assimilation of type-1 human milk oligosaccharides (HMOs). It hydrolyzes via a retaining mechanism the beta-D-GlcNAc-(1->3)-beta-D-Gal linkage in lacto-N- tetraose (LNT or beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal- (1->4)-D-Glc), an abundant HMO unique to human breast milk, releasing lacto-N-biose (LNB or beta-D-Gal-(1->3)-D-GlcNAc) and lactose. With a much lower efficiency, is also able to cleave the same linkage in lacto-N-fucopentaose I (alpha-Fuc(1->2)-beta-D-Gal-(1->3)-beta-D- GlcNAc(1->3)-beta-D-Gal-(1->4)-D-Glc), and sialyllacto-N-tetraose a (alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal- (1->4)-D-Glc). Is a key enzymatic factor for growth and proliferation of B.longum in the gut ecosystem of breast-fed infants.",Belongs to the glycosyl hydrolase 55 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0047403; GO:0046872,GO:0016798,GO:0004553,GO:0004553,GO:0004553,GO:0016798,0.5281,0.607,0.607,0.607,0.5281,5,0.5754,0.3892,no
LNBX_BIFL2,P0DW93,ProtTale,Bacteria,1599,"Present in the infant gut, this enzyme is involved in the assimilation of type-1 human milk oligosaccharides (HMOs). It hydrolyzes via a retaining mechanism the beta-D-GlcNAc-(1->3)-beta-D-Gal linkage in lacto-N- tetraose (LNT or beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal- (1->4)-D-Glc), an abundant HMO unique to human breast milk, releasing lacto-N-biose (LNB or beta-D-Gal-(1->3)-D-GlcNAc) and lactose. With a much lower efficiency, is also able to cleave the same linkage in lacto-N-fucopentaose I (alpha-Fuc(1->2)-beta-D-Gal-(1->3)-beta-D- GlcNAc(1->3)-beta-D-Gal-(1->4)-D-Glc), and sialyllacto-N-tetraose a (alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal- (1->4)-D-Glc). Is a key enzymatic factor for growth and proliferation of B.longum in the gut ecosystem of breast-fed infants.","Endolysin with lysozyme-like enzymatic activity that degrades host cell walls. Has lytic activity against Gram-positive bacteria but not against Gram-negative bacteria. Under the conditions of this study, the endolysin has little effect on the growth of L.monocytogenes.",No,No,No,No,No,not-Yes,GO:0047403; GO:0046872,GO:0003796,GO:0003796,GO:0003796,GO:0003796,GO:0003796,0.482,0.482,0.482,0.482,0.482,5,0.482,0.3892,no
LNBX_BIFL2,P0DW93,Protein2Text,Bacteria,1599,"Present in the infant gut, this enzyme is involved in the assimilation of type-1 human milk oligosaccharides (HMOs). It hydrolyzes via a retaining mechanism the beta-D-GlcNAc-(1->3)-beta-D-Gal linkage in lacto-N- tetraose (LNT or beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal- (1->4)-D-Glc), an abundant HMO unique to human breast milk, releasing lacto-N-biose (LNB or beta-D-Gal-(1->3)-D-GlcNAc) and lactose. With a much lower efficiency, is also able to cleave the same linkage in lacto-N-fucopentaose I (alpha-Fuc(1->2)-beta-D-Gal-(1->3)-beta-D- GlcNAc(1->3)-beta-D-Gal-(1->4)-D-Glc), and sialyllacto-N-tetraose a (alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal- (1->4)-D-Glc). Is a key enzymatic factor for growth and proliferation of B.longum in the gut ecosystem of breast-fed infants.",The molecular function of this protein is a metalloproteinase. It is involved in breaking down proteins.,No,No,No,No,No,not-Yes,GO:0047403; GO:0046872,GO:0004222,GO:0008237,GO:0008237,GO:0004222,GO:0008237,0.2168,0.2756,0.2756,0.2168,0.2756,5,0.2521,0.3892,no
LNBX_BIFL2,P0DW93,Reference,Bacteria,1599,"Present in the infant gut, this enzyme is involved in the assimilation of type-1 human milk oligosaccharides (HMOs). It hydrolyzes via a retaining mechanism the beta-D-GlcNAc-(1->3)-beta-D-Gal linkage in lacto-N- tetraose (LNT or beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal- (1->4)-D-Glc), an abundant HMO unique to human breast milk, releasing lacto-N-biose (LNB or beta-D-Gal-(1->3)-D-GlcNAc) and lactose. With a much lower efficiency, is also able to cleave the same linkage in lacto-N-fucopentaose I (alpha-Fuc(1->2)-beta-D-Gal-(1->3)-beta-D- GlcNAc(1->3)-beta-D-Gal-(1->4)-D-Glc), and sialyllacto-N-tetraose a (alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal- (1->4)-D-Glc). Is a key enzymatic factor for growth and proliferation of B.longum in the gut ecosystem of breast-fed infants.","Present in the infant gut, this enzyme is involved in the assimilation of type-1 human milk oligosaccharides (HMOs). It hydrolyzes via a retaining mechanism the beta-D-GlcNAc-(1->3)-beta-D-Gal linkage in lacto-N- tetraose (LNT or beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal- (1->4)-D-Glc), an abundant HMO unique to human breast milk, releasing lacto-N-biose (LNB or beta-D-Gal-(1->3)-D-GlcNAc) and lactose. With a much lower efficiency, is also able to cleave the same linkage in lacto-N-fucopentaose I (alpha-Fuc(1->2)-beta-D-Gal-(1->3)-beta-D- GlcNAc(1->3)-beta-D-Gal-(1->4)-D-Glc), and sialyllacto-N-tetraose a (alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal- (1->4)-D-Glc). Is a key enzymatic factor for growth and proliferation of B.longum in the gut ecosystem of breast-fed infants.",,,,,,,GO:0047403; GO:0046872,GO:0004553,GO:0050185,GO:0016798,GO:0004553,GO:0004553,0.607,0.2554,0.5281,0.607,0.607,5,0.5209,0.3892,no
CAP2_ENTH5,P0DX82,ESM2Text,Bacteria,600,"CD-NTase priming component of a CBASS antiviral system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnD) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-C(AAG) CBASS system.","E1-like enzyme which activates E1 to activate the second messenger inositol 1,4,5-trisphosphate (IP3).",No,No,No,No,No,not-Yes,GO:0016740; GO:0061503; GO:0008641,,,,,,,,,,,0,,0.2114,no
CAP2_ENTH5,P0DX82,Prot2Text,Bacteria,600,"CD-NTase priming component of a CBASS antiviral system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnD) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-C(AAG) CBASS system.","Adenylates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP.",No,No,No,No,No,not-Yes,GO:0016740; GO:0061503; GO:0008641,GO:0004839,GO:0004839,GO:0004839,GO:0004839; GO:0005524,GO:0004839,0.5732,0.5732,0.5732,0.476,0.5732,5,0.5538,0.2114,no
CAP2_ENTH5,P0DX82,ProtT3,Bacteria,600,"CD-NTase priming component of a CBASS antiviral system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnD) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-C(AAG) CBASS system.",Catalyzes adenylation of the 2'-phosphate of adenosylcobalamin (AdoCbl) to form adenosylcobalamin 5'-phosphate (AdoCbl-P). In the N-terminal section; belongs to the CbiX family. In the C-terminal section; belongs to the CbiY family,No,No,No,No,No,not-Yes,GO:0016740; GO:0061503; GO:0008641,GO:0016779,GO:0003919,GO:0016779,GO:0016772,GO:0016779,0.4543,0.3541,0.4543,0.5357,0.4543,5,0.4505,0.2114,no
CAP2_ENTH5,P0DX82,ProtTale,Bacteria,600,"CD-NTase priming component of a CBASS antiviral system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnD) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-C(AAG) CBASS system.",A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-GAATTC-3' and cleaves after G-1.,No,No,No,No,No,not-Yes,GO:0016740; GO:0061503; GO:0008641,GO:0015666,GO:0009036,GO:0004520,GO:0004519,GO:0009036,0.2234,0.1964,0.2501,0.345,0.1964,5,0.2423,0.2114,no
CAP2_ENTH5,P0DX82,Protein2Text,Bacteria,600,"CD-NTase priming component of a CBASS antiviral system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnD) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-C(AAG) CBASS system.","The molecular function of this protein is not specified in the given text. However, based on its name, it is likely to be involved in the synthesis or modification of nucleotides. The name ""nucleotide cyclase"" suggests that it may catalyze the conversion of a nucleotide to a cyclic nucleotide, such as cyclic AMP (cAMP) or cyclic GMP (cGMP). Cyclic nucleotides are important signaling molecules that play key roles in various cellular processes. Therefore, this protein may be involved in the synthesis of cyclic nucleotides and play a role in signaling pathways.",Maybe,Maybe,Vague,Vague,Maybe,not-Yes,GO:0016740; GO:0061503; GO:0008641,,,,,,,,,,,0,,0.2114,no
CAP2_ENTH5,P0DX82,Reference,Bacteria,600,"CD-NTase priming component of a CBASS antiviral system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnD) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-C(AAG) CBASS system.","CD-NTase priming component of a CBASS antiviral system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnD) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-C(AAG) CBASS system.",,,,,,,GO:0016740; GO:0061503; GO:0008641,,,,GO:0009975,GO:0009975,,,,0.4501,0.4501,2,0.4501,0.2114,no
DMDB_RUELI,P0DX84,ESM2Text,Bacteria,539,"Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton. Catalyzes the ATP-dependent ligation of methylmercaptopropionate (MMPA) and CoA to yield methylmercaptopropionate-CoA (MMPA-CoA).","Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton, by mediating the ATP-dependent ligation of methylmercaptopropionate (MMPA) and CoA.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016874; GO:0046872,GO:0016874,GO:0016877; GO:0005524,GO:0016878,GO:0016878,GO:0016878,0.5613,0.7836,0.3868,0.3868,0.3868,5,0.5011,0.3013,no
DMDB_RUELI,P0DX84,Prot2Text,Bacteria,539,"Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton. Catalyzes the ATP-dependent ligation of methylmercaptopropionate (MMPA) and CoA to yield methylmercaptopropionate-CoA (MMPA-CoA).","Catalyzes the ligation of coenzyme A (CoA) to 4-hydroxybutyrate (4HB). It can also use butyrate, valerate, propionate, acetate and 3-hydroxybutyrate (3HB) as substrates.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016874; GO:0046872,GO:0016874,,GO:0016877,GO:0016874; GO:0005524,GO:0016878,0.5613,,0.4573,0.8578,0.3868,4,0.5658,0.3013,no
DMDB_RUELI,P0DX84,ProtT3,Bacteria,539,"Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton. Catalyzes the ATP-dependent ligation of methylmercaptopropionate (MMPA) and CoA to yield methylmercaptopropionate-CoA (MMPA-CoA).",Belongs to the ATP-dependent AMP-binding enzyme family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0016874; GO:0046872,GO:0016878,GO:0016405,GO:0016874; GO:0005524,GO:0016878; GO:0005524,GO:0016878,0.3868,0.3868,0.8578,0.7337,0.3868,5,0.5504,0.3013,no
DMDB_RUELI,P0DX84,ProtTale,Bacteria,539,"Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton. Catalyzes the ATP-dependent ligation of methylmercaptopropionate (MMPA) and CoA to yield methylmercaptopropionate-CoA (MMPA-CoA).","Catalyzes the formation of a thioester bond between coenzyme A (CoA) and the 3-hydroxyacyl-ACP intermediate, in an ATP-dependent reaction. Involved in the beta-oxidation of fatty acids.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016874; GO:0046872,GO:0016874,GO:0016874; GO:0005524,GO:0016874; GO:0005524,GO:0003824; GO:0005524,GO:0016874,0.5613,0.8578,0.8578,0.7634,0.5613,5,0.7203,0.3013,no
DMDB_RUELI,P0DX84,Protein2Text,Bacteria,539,"Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton. Catalyzes the ATP-dependent ligation of methylmercaptopropionate (MMPA) and CoA to yield methylmercaptopropionate-CoA (MMPA-CoA).","This protein is a part of the acetate transport system, and it is involved in the transport of acetate into the cell. Specifically, it is a transmembrane protein that helps to transport acetate across the cell membrane. The molecular function of this protein is to facilitate the movement of acetate ions across the cell membrane, allowing the cell to take up acetate as a source of energy.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016874; GO:0046872,,,,,GO:0015123,,,,,0.115,1,0.115,0.3013,no
DMDB_RUELI,P0DX84,Reference,Bacteria,539,"Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton. Catalyzes the ATP-dependent ligation of methylmercaptopropionate (MMPA) and CoA to yield methylmercaptopropionate-CoA (MMPA-CoA).","Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton. Catalyzes the ATP-dependent ligation of methylmercaptopropionate (MMPA) and CoA to yield methylmercaptopropionate-CoA (MMPA-CoA).",,,,,,,GO:0005524; GO:0016874; GO:0046872,GO:0016878; GO:0005524,GO:0003995,GO:0016405; GO:0005524,GO:0016874; GO:0003987,GO:0016874; GO:0005524,0.7337,0.2137,0.7337,0.5555,0.8578,5,0.6189,0.3013,no
CAPV_PSEU5,P0DX85,ESM2Text,Bacteria,333,"Effector phospholipase of a CBASS antiviral system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD- NTase protein (CdnA) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system.","Phospholipase B that is able to hydrolyze inositol pyrophosphate (IP) and phosphatidylinositol 3-phosphate (PI(3)P), but not phytic acid. Its physiological role is not known.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008970,GO:0016787,GO:0004622,GO:0004622,GO:0004620,,0.4325,0.7437,0.7437,0.7422,,4,0.6655,0.2892,no
CAPV_PSEU5,P0DX85,Prot2Text,Bacteria,333,"Effector phospholipase of a CBASS antiviral system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD- NTase protein (CdnA) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system.","Protects E.coli against phage P1 and T2 infection. When the 4 gene operon capV-dncV-cap2-cap3 is introduced in E.coli MG1655 there is about 100-fold protection against phages P1 and T2. Protects E.coli against phage T2 infection. When the CBASS operon (capV-dcnV-cap2-cap3) is introduced in E.coli MG1655 there is a more than 10(3) decrease in the efficiency of T2 plaque formation. Protects 100-fold against phage T5, offers no protection against T7.",Vague,Maybe,Vague,Maybe,Maybe,not-Yes,GO:0008970,,,,,,,,,,,0,,0.2892,no
CAPV_PSEU5,P0DX85,ProtT3,Bacteria,333,"Effector phospholipase of a CBASS antiviral system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD- NTase protein (CdnA) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system.",Toxic component of a type II toxin-antitoxin (TA) system. Upon expression in M.smegmatis neutralizes the toxic effect of cognate antitoxin Msmeg_0188. Upon expression in S.coelicolor neutralizes the toxic effect of cognate antitoxin Sco_0188. Toxic component of a type II toxin-antitoxin (TA) system. Upon expression in M.smegmatis neutralizes the toxic effect of cognate antitoxin Msmeg_0188. Upon expression in S.coelicolor neutralizes the toxic effect of,No,No,No,No,No,not-Yes,GO:0008970,,,,,,,,,,,0,,0.2892,no
CAPV_PSEU5,P0DX85,ProtTale,Bacteria,333,"Effector phospholipase of a CBASS antiviral system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD- NTase protein (CdnA) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system.",Probable lipolytic enzyme involved in the biosynthesis of the antibiotic polyketide bacillaene. Catalyzes the hydrolysis of the ester bond of the polyketide synthase (PKS)- derived (R)-3-hydroxymyristoyl-ACP by releasing (R)-3-hydroxymyristoyl-CoA.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008970,GO:0016788,GO:0016788,GO:0016788,GO:0016788,GO:0016788,0.5273,0.5273,0.5273,0.5273,0.5273,5,0.5273,0.2892,no
CAPV_PSEU5,P0DX85,Protein2Text,Bacteria,333,"Effector phospholipase of a CBASS antiviral system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD- NTase protein (CdnA) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system.","The molecular function of this protein is to act as a lipase, specifically hydrolyzing triglycerides.",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0008970,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,0.6049,0.6049,0.6049,0.6049,0.6049,5,0.6049,0.2892,no
CAPV_PSEU5,P0DX85,Reference,Bacteria,333,"Effector phospholipase of a CBASS antiviral system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD- NTase protein (CdnA) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system.","Effector phospholipase of a CBASS antiviral system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD- NTase protein (CdnA) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system.",,,,,,,GO:0008970,GO:0004620,GO:0004620,GO:0004620,GO:0004622,GO:0004622,0.7422,0.7422,0.7422,0.7437,0.7437,5,0.7428,0.2892,no
CDNA_PSEU5,P0DX86,ESM2Text,Bacteria,380,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnA, this protein) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system.","Deaminates adenosine-37 to inosine in methionine ribosomes, using the linear intermediate 5'-AMP-(R)-cAMP (Rd-37) as the energy source. Can also use the linear intermediate 5'-AMP-(Rho-37) as an adenosine nucleotide, and the monophosphate form of ATP or dATP, but with lower efficiency.",No,No,No,No,No,not-Yes,GO:0140701; GO:0005524; GO:0005525; GO:0046872,GO:0016787,GO:0008251,GO:0008251,GO:0008251,GO:0008251,0.1935,0.0806,0.0806,0.0806,0.0806,5,0.1032,0.6632,yes
CDNA_PSEU5,P0DX86,Prot2Text,Bacteria,380,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnA, this protein) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system.","Free serine ADP-ribosyltransferase that mediates the formation of an arginine residue from ADP-ribosylated proteins. Involved in the biosynthesis of the arginine found at position 9 (m2A9) in the C-terminus of proteins like the ADP-ribosyltransferase RGA. Can also use GTP, but not ATP, as substrate.",No,No,No,No,No,not-Yes,GO:0140701; GO:0005524; GO:0005525; GO:0046872,GO:0003950,GO:0003950,GO:0003950,,GO:0003950,0.1577,0.1577,0.1577,,0.1577,4,0.1577,0.6632,yes
CDNA_PSEU5,P0DX86,ProtT3,Bacteria,380,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnA, this protein) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system.","CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). Binds cyclic GMP-AMP (2',3'-cGAMP or cGAMP), a second messenger produced in response to pathogen-associated molecular pattern (PAMP) detection by host cGAS (",No,No,No,Maybe,No,not-Yes,GO:0140701; GO:0005524; GO:0005525; GO:0046872,,,,,,,,,,,0,,0.6632,yes
CDNA_PSEU5,P0DX86,ProtTale,Bacteria,380,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnA, this protein) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system.","Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type I-D(GG) CBASS system.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0140701; GO:0005524; GO:0005525; GO:0046872,GO:0016779,GO:0016849,GO:0016779,GO:0009975,GO:0016779,0.3478,0.1556,0.3478,0.1935,0.3478,5,0.2785,0.6632,yes
CDNA_PSEU5,P0DX86,Protein2Text,Bacteria,380,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnA, this protein) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system.","This protein is a DNA polymerase, which is an enzyme that plays a crucial role in DNA replication and repair. Specifically, it is likely involved in the synthesis of viral DNA, as it is a component of a viral genome. The molecular function of this protein is to replicate viral DNA by adding nucleotides to a primer, using the viral genome as a template.",No,No,No,No,No,not-Yes,GO:0140701; GO:0005524; GO:0005525; GO:0046872,GO:0003887,GO:0003887,GO:0003887,GO:0003887,GO:0003887,0.228,0.228,0.228,0.228,0.228,5,0.228,0.6632,yes
CDNA_PSEU5,P0DX86,Reference,Bacteria,380,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnA, this protein) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system.","Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnA, this protein) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system.",,,,,,,GO:0140701; GO:0005524; GO:0005525; GO:0046872,GO:0016779,,GO:0016779,GO:0009975,GO:0009975,0.3478,,0.3478,0.1935,0.1935,4,0.2707,0.6632,yes
CAP2_PSEU5,P0DX87,ESM2Text,Bacteria,543,"CD-NTase priming component of a CBASS antiviral system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnA) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system.",Protects E.coli against phage P1 and T2 infection. When the cdnA-cap9-cap2-cap3 operon is introduced in E.coli MG1655 there is a more than 10(3)A decrease in the efficiency of T2 plaque formation. The operon may be functional equivalent to T2P.,Maybe,Maybe,Vague,Maybe,No,not-Yes,GO:0016740; GO:0061503; GO:0008641,,,,,,,,,,,0,,0.3293,no
CAP2_PSEU5,P0DX87,Prot2Text,Bacteria,543,"CD-NTase priming component of a CBASS antiviral system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnA) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system.","Protects E.coli against phage infection. When capV and dncV are introduced in E.coli MG1655 there is 1000-fold protection against phage P1; protection against other phage (T2, T4, T5 and lambda-vir) requires the 2 subsequent genes.",Maybe,Maybe,Vague,Maybe,No,not-Yes,GO:0016740; GO:0061503; GO:0008641,,,,,,,,,,,0,,0.3293,no
CAP2_PSEU5,P0DX87,ProtT3,Bacteria,543,"CD-NTase priming component of a CBASS antiviral system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnA) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system.","CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity)",No,No,No,Maybe,No,not-Yes,GO:0016740; GO:0061503; GO:0008641,,,,,,,,,,,0,,0.3293,no
CAP2_PSEU5,P0DX87,ProtTale,Bacteria,543,"CD-NTase priming component of a CBASS antiviral system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnA) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system.","A methylase that recognizes the double-stranded sequence 5'-GATC-3', methylates A-2 on both strands, and protects the DNA from cleavage by the DpnI endonuclease.",No,No,No,No,No,not-Yes,GO:0016740; GO:0061503; GO:0008641,GO:0009007,GO:0003886,GO:0009007,GO:0009007,GO:0009007,0.309,0.309,0.309,0.309,0.309,5,0.309,0.3293,no
CAP2_PSEU5,P0DX87,Protein2Text,Bacteria,543,"CD-NTase priming component of a CBASS antiviral system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnA) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system.","This protein is a methyltransferase, which means it catalyzes the transfer of a methyl group from a donor molecule to a specific substrate, typically a protein or lipid. In this case, it is likely involved in the methylation of a protein or lipid involved in cell signaling or metabolism.",No,No,No,No,No,not-Yes,GO:0016740; GO:0061503; GO:0008641,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.4543,0.4543,0.4543,0.4543,0.4543,5,0.4543,0.3293,no
CAP2_PSEU5,P0DX87,Reference,Bacteria,543,"CD-NTase priming component of a CBASS antiviral system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnA) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system.","CD-NTase priming component of a CBASS antiviral system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnA) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system.",,,,,,,GO:0016740; GO:0061503; GO:0008641,,,,,,,,,,,0,,0.3293,no
CDNB_ESCAL,P0DXA3,ESM2Text,Bacteria,443,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnB, this protein) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The effector protein for this system is membrane protein Cap15.",Cyclic dinucleotide synthase that catalyzes the synthesis of 3'3'-cyclic UMP-UMP (cUMP-UMP) in the presence of ATP and GTP.,Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0005524; GO:0106408; GO:0052621; GO:0046872,GO:0016779,GO:0016779,GO:0016779,GO:0016779,,0.5485,0.5485,0.5485,0.5485,,4,0.5485,0.4595,no
CDNB_ESCAL,P0DXA3,Prot2Text,Bacteria,443,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnB, this protein) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The effector protein for this system is membrane protein Cap15.",Cytoplasmic uridylyltransferase that catalyzes the addition of Us to the 3'-hydroxyl group of single-stranded RNAs with a 3'-terminal U.,No,No,No,No,No,not-Yes,GO:0005524; GO:0106408; GO:0052621; GO:0046872,GO:0016779,GO:0016779,GO:0016779,GO:0016779,GO:0016779,0.5485,0.5485,0.5485,0.5485,0.5485,5,0.5485,0.4595,no
CDNB_ESCAL,P0DXA3,ProtT3,Bacteria,443,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnB, this protein) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The effector protein for this system is membrane protein Cap15.","CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection (By similarity). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0106408; GO:0052621; GO:0046872,GO:0016779,GO:0016779,GO:0016779,GO:0016779,GO:0016779,0.5485,0.5485,0.5485,0.5485,0.5485,5,0.5485,0.4595,no
CDNB_ESCAL,P0DXA3,ProtTale,Bacteria,443,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnB, this protein) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The effector protein for this system is membrane protein Cap15.","Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type III-C(AAA) CBASS system.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0106408; GO:0052621; GO:0046872,GO:0016779,GO:0016849,GO:0016779,GO:0009975,GO:0016779,0.5485,0.2107,0.5485,0.2622,0.5485,5,0.4237,0.4595,no
CDNB_ESCAL,P0DXA3,Protein2Text,Bacteria,443,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnB, this protein) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The effector protein for this system is membrane protein Cap15.","This protein is a methyltransferase, which is involved in the replication of viral DNA. It is likely responsible for modifying the DNA or its components to facilitate viral replication or to evade the host immune response.",No,No,No,No,No,not-Yes,GO:0005524; GO:0106408; GO:0052621; GO:0046872,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.2728,0.2728,0.2728,0.2728,0.2728,5,0.2728,0.4595,no
CDNB_ESCAL,P0DXA3,Reference,Bacteria,443,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnB, this protein) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The effector protein for this system is membrane protein Cap15.","Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophages. The CD-NTase protein (CdnB, this protein) synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The effector protein for this system is membrane protein Cap15.",,,,,,,GO:0005524; GO:0106408; GO:0052621; GO:0046872,GO:0016779,,GO:0016779,GO:0009975,GO:0009975,0.5485,,0.5485,0.2622,0.2622,4,0.4053,0.4595,no
CDNE_STASC,P0DXA6,ESM2Text,Bacteria,324,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The effector for this system is downstream Cap15. A type I-B CBASS system.","Cyclic dinucleotide synthase that catalyzes the synthesis of c-di-GMP, has no activity with other NTP substrates.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0005525; GO:0046872; GO:0016779; GO:0003723,GO:0016779,GO:0052621,GO:0052621,GO:0052621,GO:0052621,0.3962,0.3404,0.3404,0.3404,0.3404,5,0.3516,0.6153,yes
CDNE_STASC,P0DXA6,Prot2Text,Bacteria,324,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The effector for this system is downstream Cap15. A type I-B CBASS system.","Cyclic dinucleotide synthase that catalyzes the synthesis of c-di-GMP, has no activity with other NTP substrates.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0005525; GO:0046872; GO:0016779; GO:0003723,GO:0052929,GO:0052929,GO:0052621,GO:0052621,GO:0052621,0.2429,0.2429,0.3404,0.3404,0.3404,5,0.3014,0.6153,yes
CDNE_STASC,P0DXA6,ProtT3,Bacteria,324,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The effector for this system is downstream Cap15. A type I-B CBASS system.","CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection (By similarity). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0005525; GO:0046872; GO:0016779; GO:0003723,GO:0016779,GO:0016779,GO:0016779,GO:0016779,GO:0016779,0.3962,0.3962,0.3962,0.3962,0.3962,5,0.3962,0.6153,yes
CDNE_STASC,P0DXA6,ProtTale,Bacteria,324,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The effector for this system is downstream Cap15. A type I-B CBASS system.","Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type I-D(GG) CBASS system.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0005525; GO:0046872; GO:0016779; GO:0003723,GO:0016779,GO:0016849,GO:0016779,GO:0009975,GO:0016779,0.3962,0.184,0.3962,0.2267,0.3962,5,0.3199,0.6153,yes
CDNE_STASC,P0DXA6,Protein2Text,Bacteria,324,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The effector for this system is downstream Cap15. A type I-B CBASS system.","The molecular function of this protein is a viral replicase, specifically a DNA polymerase, which plays a crucial role in the replication of the viral genome. It is involved in the synthesis of new viral DNA molecules by copying the viral genome. This protein is essential for the viral life cycle and is a key target for antiviral therapies. 
In this specific case, this protein is a viral DNA polymerase, responsible for the replication of the viral genome. It is a replicase that uses the host cell's machinery to synthesize new viral DNA molecules, allowing the virus to replicate and spread.",No,No,No,No,No,not-Yes,GO:0005524; GO:0005525; GO:0046872; GO:0016779; GO:0003723,GO:0003887,GO:0003887,GO:0003887,GO:0003887,GO:0003887,0.2649,0.2649,0.2649,0.2649,0.2649,5,0.2649,0.6153,yes
CDNE_STASC,P0DXA6,Reference,Bacteria,324,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The effector for this system is downstream Cap15. A type I-B CBASS system.","Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The effector for this system is downstream Cap15. A type I-B CBASS system.",,,,,,,GO:0005524; GO:0005525; GO:0046872; GO:0016779; GO:0003723,GO:0016779,,GO:0016779,GO:0009975,GO:0009975,0.3962,,0.3962,0.2267,0.2267,4,0.3115,0.6153,yes
CHCB1_SINCY,P0DXE0,ESM2Text,Bacteria,259,"Dehydrogenase involved in a cyclohexanecarboxylate (CHCA) degradation pathway. Catalyzes the NAD(+)-dependent dehydrogenation of trans-4- hydroxycyclohexanecarboxylate (trans-4-hydroxyCHCA) to form 4- oxocyclohexanecarboxylate (4-oxoCHCA). Is highly specific for the trans-4-hydroxy derivative and shows only weak activity with cis-4-hydroxyCHCA. Can also catalyze the reverse reaction (4-oxoCHCA reduction) with a higher catalytic efficiency. In the reverse reaction, is highly specific for 4-oxoCHCA and cannot use either the 2-oxo or the 3-oxo homolog as substrate. Cannot use NADP(+).","Catalyzes the NAD(+)-dependent dehydrogenation of 2,5-dichloro-2,5-cyclohexadiene-1,4-diol to form 2,5-dichlorohydroquinone (2,5-DiCHQ), an enzymatic step in the degradation of carbacenem compounds such as antibiotics. Is also able to catalyze the reverse reaction, i.e. the NADH-dependent reduction of carbacenem compounds to acetoacetate.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0047030,GO:0016491; GO:0051287,GO:0016491; GO:0070403,GO:0016491,GO:0016491,GO:0016491,0.4247,0.4223,0.6019,0.6019,0.6019,5,0.5305,0.113,no
CHCB1_SINCY,P0DXE0,Prot2Text,Bacteria,259,"Dehydrogenase involved in a cyclohexanecarboxylate (CHCA) degradation pathway. Catalyzes the NAD(+)-dependent dehydrogenation of trans-4- hydroxycyclohexanecarboxylate (trans-4-hydroxyCHCA) to form 4- oxocyclohexanecarboxylate (4-oxoCHCA). Is highly specific for the trans-4-hydroxy derivative and shows only weak activity with cis-4-hydroxyCHCA. Can also catalyze the reverse reaction (4-oxoCHCA reduction) with a higher catalytic efficiency. In the reverse reaction, is highly specific for 4-oxoCHCA and cannot use either the 2-oxo or the 3-oxo homolog as substrate. Cannot use NADP(+).","Involved in the modification of secondary bile acids into iso-bile acids (3beta-bile acids) via epimerization of the 3-OH group through a 3-oxo-intermediate. Catalyzes the oxidation of cholate (3alpha-cholest-4-en-3-one) to yield 3-oxo-Delta(3)-3-hydroxy-Delta(3)-but-2-en-3-one. Is also able to catalyze the oxidation of (3alpha-cholest-4-en-3-one) to yield (3alpha-cholest-4-en-3-one) with a similar catalytic efficiency. In vitro, can also catalyze the oxidation of (3alpha-cholest-4-en-3-one) to (3alpha-cholest-4-en-3-one) with lower efficiency.",No,Maybe,Maybe,Maybe,No,not-Yes,GO:0047030,GO:0016491,,GO:0016491,GO:0016491,GO:0047044,0.6019,,0.6019,0.6019,0.5967,4,0.6006,0.113,no
CHCB1_SINCY,P0DXE0,ProtT3,Bacteria,259,"Dehydrogenase involved in a cyclohexanecarboxylate (CHCA) degradation pathway. Catalyzes the NAD(+)-dependent dehydrogenation of trans-4- hydroxycyclohexanecarboxylate (trans-4-hydroxyCHCA) to form 4- oxocyclohexanecarboxylate (4-oxoCHCA). Is highly specific for the trans-4-hydroxy derivative and shows only weak activity with cis-4-hydroxyCHCA. Can also catalyze the reverse reaction (4-oxoCHCA reduction) with a higher catalytic efficiency. In the reverse reaction, is highly specific for 4-oxoCHCA and cannot use either the 2-oxo or the 3-oxo homolog as substrate. Cannot use NADP(+).",Belongs to the short-chain dehydrogenases/reductases (SDR) family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0047030,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.6019,0.6019,0.6019,0.6019,0.6019,5,0.6019,0.113,no
CHCB1_SINCY,P0DXE0,ProtTale,Bacteria,259,"Dehydrogenase involved in a cyclohexanecarboxylate (CHCA) degradation pathway. Catalyzes the NAD(+)-dependent dehydrogenation of trans-4- hydroxycyclohexanecarboxylate (trans-4-hydroxyCHCA) to form 4- oxocyclohexanecarboxylate (4-oxoCHCA). Is highly specific for the trans-4-hydroxy derivative and shows only weak activity with cis-4-hydroxyCHCA. Can also catalyze the reverse reaction (4-oxoCHCA reduction) with a higher catalytic efficiency. In the reverse reaction, is highly specific for 4-oxoCHCA and cannot use either the 2-oxo or the 3-oxo homolog as substrate. Cannot use NADP(+).","Catalyzes the irreversible reduction of 2,3-butanediol to (S)-acetoin in the presence of NADH.",No,Maybe,Maybe,No,Maybe,not-Yes,GO:0047030,GO:0016491,GO:0016491,GO:0016491; GO:0051287,GO:0016491,GO:0016491,0.6019,0.6019,0.4247,0.6019,0.6019,5,0.5665,0.113,no
CHCB1_SINCY,P0DXE0,Protein2Text,Bacteria,259,"Dehydrogenase involved in a cyclohexanecarboxylate (CHCA) degradation pathway. Catalyzes the NAD(+)-dependent dehydrogenation of trans-4- hydroxycyclohexanecarboxylate (trans-4-hydroxyCHCA) to form 4- oxocyclohexanecarboxylate (4-oxoCHCA). Is highly specific for the trans-4-hydroxy derivative and shows only weak activity with cis-4-hydroxyCHCA. Can also catalyze the reverse reaction (4-oxoCHCA reduction) with a higher catalytic efficiency. In the reverse reaction, is highly specific for 4-oxoCHCA and cannot use either the 2-oxo or the 3-oxo homolog as substrate. Cannot use NADP(+).",The molecular function of this protein is to catalyze the conversion of 3-dehydro-L-gulonate to 3-keto-L-gulonate.,No,No,No,No,No,not-Yes,GO:0047030,,GO:0016491,,GO:0016491,GO:0016491,,0.6019,,0.6019,0.6019,3,0.6019,0.113,no
CHCB1_SINCY,P0DXE0,Reference,Bacteria,259,"Dehydrogenase involved in a cyclohexanecarboxylate (CHCA) degradation pathway. Catalyzes the NAD(+)-dependent dehydrogenation of trans-4- hydroxycyclohexanecarboxylate (trans-4-hydroxyCHCA) to form 4- oxocyclohexanecarboxylate (4-oxoCHCA). Is highly specific for the trans-4-hydroxy derivative and shows only weak activity with cis-4-hydroxyCHCA. Can also catalyze the reverse reaction (4-oxoCHCA reduction) with a higher catalytic efficiency. In the reverse reaction, is highly specific for 4-oxoCHCA and cannot use either the 2-oxo or the 3-oxo homolog as substrate. Cannot use NADP(+).","Dehydrogenase involved in a cyclohexanecarboxylate (CHCA) degradation pathway. Catalyzes the NAD(+)-dependent dehydrogenation of trans-4- hydroxycyclohexanecarboxylate (trans-4-hydroxyCHCA) to form 4- oxocyclohexanecarboxylate (4-oxoCHCA). Is highly specific for the trans-4-hydroxy derivative and shows only weak activity with cis-4-hydroxyCHCA. Can also catalyze the reverse reaction (4-oxoCHCA reduction) with a higher catalytic efficiency. In the reverse reaction, is highly specific for 4-oxoCHCA and cannot use either the 2-oxo or the 3-oxo homolog as substrate. Cannot use NADP(+).",,,,,,,GO:0047030,GO:0016616,GO:0016616,GO:0016616; GO:0051287,GO:0016491; GO:0050661,GO:0016616,0.8582,0.8582,0.5956,0.4247,0.8582,5,0.719,0.113,no
UVSW_BPT4,P0DXF1,ESM2Text,Viruses,502,"Plays important roles in recombination-dependent DNA repair and the reorganization of stalled replication forks during viral DNA synthesis. Active on in vivo-derived T4 DNA; viral DNA is highly modified by hydroxymethylation and glucosylation of cytosine residues. Helps process Holliday junction (HJ) intermediates to mature products by catalyzing branch migration. Probably able to catalyze replication fork regression (Probable). Unwinds HJ and Y-branched but not linear double-stranded (ds)DNA; unwinding requires ATP and Mg(2+). Unwinds dsDNA with a 3'-single-stranded (ss)DNA overhang, suggesting it is a 3'-5' helicase. Another study does not find this activity. Unwinds D- and R-loops. Also anneals ssDNA; ATP stimulates annealing. Has ssDNA and dsDNA-stimulated ATPase activity, also hydrolyzes GTP in the presence of DNA.","ATPase involved in DNA repair; it is a powerful, multichain enzyme that cleaves a single-strand DNA junction and can alter DNA in a 3' to 5' manner. Binds to flap structures and possesses a strong preference for single-stranded DNA.",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0016887; GO:0004518; GO:0005524,GO:0016887; GO:0004518; GO:0003677,GO:0016887; GO:0004519,GO:0016887,GO:0016887; GO:0004518,0.5636,0.5625,0.3073,0.2706,0.3365,5,0.4081,0.6414,yes
UVSW_BPT4,P0DXF1,Prot2Text,Viruses,502,"Plays important roles in recombination-dependent DNA repair and the reorganization of stalled replication forks during viral DNA synthesis. Active on in vivo-derived T4 DNA; viral DNA is highly modified by hydroxymethylation and glucosylation of cytosine residues. Helps process Holliday junction (HJ) intermediates to mature products by catalyzing branch migration. Probably able to catalyze replication fork regression (Probable). Unwinds HJ and Y-branched but not linear double-stranded (ds)DNA; unwinding requires ATP and Mg(2+). Unwinds dsDNA with a 3'-single-stranded (ss)DNA overhang, suggesting it is a 3'-5' helicase. Another study does not find this activity. Unwinds D- and R-loops. Also anneals ssDNA; ATP stimulates annealing. Has ssDNA and dsDNA-stimulated ATPase activity, also hydrolyzes GTP in the presence of DNA.","ATPase involved in DNA repair; it is a powerful, multichain enzyme that cleaves a single-strand DNA junction and can alter DNA in a 3' to 5' manner. Binds to flap structures and possesses a strong preference for single-stranded DNA.",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0008094; GO:0004518,GO:0008094,GO:0008094,GO:0005524; GO:0003678,GO:0008094; GO:0004520,0.424,0.389,0.389,0.7131,0.3769,5,0.4584,0.6414,yes
UVSW_BPT4,P0DXF1,ProtT3,Viruses,502,"Plays important roles in recombination-dependent DNA repair and the reorganization of stalled replication forks during viral DNA synthesis. Active on in vivo-derived T4 DNA; viral DNA is highly modified by hydroxymethylation and glucosylation of cytosine residues. Helps process Holliday junction (HJ) intermediates to mature products by catalyzing branch migration. Probably able to catalyze replication fork regression (Probable). Unwinds HJ and Y-branched but not linear double-stranded (ds)DNA; unwinding requires ATP and Mg(2+). Unwinds dsDNA with a 3'-single-stranded (ss)DNA overhang, suggesting it is a 3'-5' helicase. Another study does not find this activity. Unwinds D- and R-loops. Also anneals ssDNA; ATP stimulates annealing. Has ssDNA and dsDNA-stimulated ATPase activity, also hydrolyzes GTP in the presence of DNA.",Belongs to the helicase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0004386; GO:0005524,GO:0004386,GO:0004386; GO:0005524,GO:0004386,GO:0004386,0.6704,0.4113,0.6704,0.4113,0.4113,5,0.5149,0.6414,yes
UVSW_BPT4,P0DXF1,ProtTale,Viruses,502,"Plays important roles in recombination-dependent DNA repair and the reorganization of stalled replication forks during viral DNA synthesis. Active on in vivo-derived T4 DNA; viral DNA is highly modified by hydroxymethylation and glucosylation of cytosine residues. Helps process Holliday junction (HJ) intermediates to mature products by catalyzing branch migration. Probably able to catalyze replication fork regression (Probable). Unwinds HJ and Y-branched but not linear double-stranded (ds)DNA; unwinding requires ATP and Mg(2+). Unwinds dsDNA with a 3'-single-stranded (ss)DNA overhang, suggesting it is a 3'-5' helicase. Another study does not find this activity. Unwinds D- and R-loops. Also anneals ssDNA; ATP stimulates annealing. Has ssDNA and dsDNA-stimulated ATPase activity, also hydrolyzes GTP in the presence of DNA.",ATP-dependent DNA 3'-5' helicase required for the maintenance of stalled replication forks and for the efficient restart of stalled replication forks promoted by RAD51. Acts as a 3'-to-5' DNA helicase that unwinds single-stranded DNA (ssDNA) in the presence of ATP. Unwinds ssDNA in the presence of double- stranded DNA (dsDNA) in a 3'-to-5' direction. Also has 3'-to-5' ssDNA-unwinding activity in the absence of ATP.,Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0004003; GO:0005524,GO:0003678; GO:0016887; GO:0005524,0.7131,0.7131,0.7131,0.7131,0.7085,5,0.7122,0.6414,yes
UVSW_BPT4,P0DXF1,Protein2Text,Viruses,502,"Plays important roles in recombination-dependent DNA repair and the reorganization of stalled replication forks during viral DNA synthesis. Active on in vivo-derived T4 DNA; viral DNA is highly modified by hydroxymethylation and glucosylation of cytosine residues. Helps process Holliday junction (HJ) intermediates to mature products by catalyzing branch migration. Probably able to catalyze replication fork regression (Probable). Unwinds HJ and Y-branched but not linear double-stranded (ds)DNA; unwinding requires ATP and Mg(2+). Unwinds dsDNA with a 3'-single-stranded (ss)DNA overhang, suggesting it is a 3'-5' helicase. Another study does not find this activity. Unwinds D- and R-loops. Also anneals ssDNA; ATP stimulates annealing. Has ssDNA and dsDNA-stimulated ATPase activity, also hydrolyzes GTP in the presence of DNA.","The molecular function of this protein is a DNA helicase. It is a DNA-unwinding enzyme that plays a role in DNA replication and repair. It is involved in the unwinding of double-stranded DNA into single strands, which is essential for DNA replication and repair processes.",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0003678,GO:0004003; GO:0003677; GO:0005524,GO:0003678,GO:0003678,GO:0003678; GO:0005524,0.454,0.8733,0.454,0.454,0.7131,5,0.5897,0.6414,yes
UVSW_BPT4,P0DXF1,Reference,Viruses,502,"Plays important roles in recombination-dependent DNA repair and the reorganization of stalled replication forks during viral DNA synthesis. Active on in vivo-derived T4 DNA; viral DNA is highly modified by hydroxymethylation and glucosylation of cytosine residues. Helps process Holliday junction (HJ) intermediates to mature products by catalyzing branch migration. Probably able to catalyze replication fork regression (Probable). Unwinds HJ and Y-branched but not linear double-stranded (ds)DNA; unwinding requires ATP and Mg(2+). Unwinds dsDNA with a 3'-single-stranded (ss)DNA overhang, suggesting it is a 3'-5' helicase. Another study does not find this activity. Unwinds D- and R-loops. Also anneals ssDNA; ATP stimulates annealing. Has ssDNA and dsDNA-stimulated ATPase activity, also hydrolyzes GTP in the presence of DNA.","Plays important roles in recombination-dependent DNA repair and the reorganization of stalled replication forks during viral DNA synthesis. Active on in vivo-derived T4 DNA; viral DNA is highly modified by hydroxymethylation and glucosylation of cytosine residues. Helps process Holliday junction (HJ) intermediates to mature products by catalyzing branch migration. Probably able to catalyze replication fork regression (Probable). Unwinds HJ and Y-branched but not linear double-stranded (ds)DNA; unwinding requires ATP and Mg(2+). Unwinds dsDNA with a 3'-single-stranded (ss)DNA overhang, suggesting it is a 3'-5' helicase. Another study does not find this activity. Unwinds D- and R-loops. Also anneals ssDNA; ATP stimulates annealing. Has ssDNA and dsDNA-stimulated ATPase activity, also hydrolyzes GTP in the presence of DNA.",,,,,,,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0003678; GO:0016887; GO:0003677,GO:0004386; GO:0017111,GO:0003678; GO:0016887; GO:0005524,GO:0004386; GO:0016887; GO:0005524,GO:0004386; GO:0005524; GO:0003677,0.7085,0.4673,0.7085,0.6619,0.8367,5,0.6766,0.6414,yes
DSR2_BACIU,P0DXN8,ESM2Text,Bacteria,1005,Anti-phage defense protein that is activated through the binding to the phage tail tube protein monomer and which hydrolyzes NAD+ upon activation (NADase activity). The resulting depletion of NAD(+) leads to an abortive infection.,"Muttoyl-protein deacylase, which plays an important role in virulence.",No,No,No,No,No,not-Yes,GO:0003953,,,,,,,,,,,0,,0.3008,no
DSR2_BACIU,P0DXN8,Prot2Text,Bacteria,1005,Anti-phage defense protein that is activated through the binding to the phage tail tube protein monomer and which hydrolyzes NAD+ upon activation (NADase activity). The resulting depletion of NAD(+) leads to an abortive infection.,The specificity subunit of a type I restriction enzyme that recognizes 5'-GTRC-3' and cleaves after G-1.,No,No,No,No,No,not-Yes,GO:0003953,GO:0003677,,GO:0003677,GO:0015666,GO:0003677,0.1264,,0.1264,0.2661,0.1264,4,0.1613,0.3008,no
DSR2_BACIU,P0DXN8,ProtT3,Bacteria,1005,Anti-phage defense protein that is activated through the binding to the phage tail tube protein monomer and which hydrolyzes NAD+ upon activation (NADase activity). The resulting depletion of NAD(+) leads to an abortive infection.,"CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity)",No,No,No,Maybe,No,not-Yes,GO:0003953,,,,,,,,,,,0,,0.3008,no
DSR2_BACIU,P0DXN8,ProtTale,Bacteria,1005,Anti-phage defense protein that is activated through the binding to the phage tail tube protein monomer and which hydrolyzes NAD+ upon activation (NADase activity). The resulting depletion of NAD(+) leads to an abortive infection.,Toxic component of a type II toxin-antitoxin (TA) system. Upon expression in E.coli inhibits cell growth and colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin YafQ.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0003953,,,,,,,,,,,0,,0.3008,no
DSR2_BACIU,P0DXN8,Protein2Text,Bacteria,1005,Anti-phage defense protein that is activated through the binding to the phage tail tube protein monomer and which hydrolyzes NAD+ upon activation (NADase activity). The resulting depletion of NAD(+) leads to an abortive infection.,"Based on the provided information, the molecular function of this protein is not explicitly stated. However, as a member of the RecA family of proteins, it is likely to be involved in homologous recombination, DNA repair, and/or genetic exchange. This protein is probably a RecA-like protein, which plays a crucial role in bacterial recombination and repair of DNA damage.

If you have any further information or context about this protein, I may be able to provide a more specific answer.",No,No,No,No,No,not-Yes,GO:0003953,,,,,,,,,,,0,,0.3008,no
DSR2_BACIU,P0DXN8,Reference,Bacteria,1005,Anti-phage defense protein that is activated through the binding to the phage tail tube protein monomer and which hydrolyzes NAD+ upon activation (NADase activity). The resulting depletion of NAD(+) leads to an abortive infection.,Anti-phage defense protein that is activated through the binding to the phage tail tube protein monomer and which hydrolyzes NAD+ upon activation (NADase activity). The resulting depletion of NAD(+) leads to an abortive infection.,,,,,,,GO:0003953,GO:0003953,GO:0003953,GO:0003953,GO:0003953,GO:0003953,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3008,no
LAN1_PYRDE,P0DXV0,ESM2Text,Eukaryota,540,"Sterol 14-alpha demethylase; part of the gene cluster that mediates the biosynthesis of tetrahydropyranyl antifungal agent lanomycin that acts as an inhibitor of CYP51 and blocks the ergosterol biosynthesis. Sterol 14-alpha-demethylase plays a critical role in the biosynthesis of ergosterol, the major sterol component in fungal membranes that participates in a variety of functions. Acts as a self-resistant CYP51 that contains mutations found in CYP51s isolated from azole resistance strains and that is not inhibited by the final product of the cluster, lanomycin.","Lanosterol 14-alpha demethylase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway. ERG5 catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24(28)-trienoic acid. The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S",Yes,Yes,Yes,Yes,Yes,Yes,GO:0020037; GO:0005506; GO:0008398,GO:0004497; GO:0020037,GO:0008398; GO:0020037; GO:0004497,GO:0008398; GO:0004497,GO:0008398,GO:0008398,0.6931,0.8078,0.5787,0.5487,0.5487,5,0.6354,0.2089,no
LAN1_PYRDE,P0DXV0,Prot2Text,Eukaryota,540,"Sterol 14-alpha demethylase; part of the gene cluster that mediates the biosynthesis of tetrahydropyranyl antifungal agent lanomycin that acts as an inhibitor of CYP51 and blocks the ergosterol biosynthesis. Sterol 14-alpha-demethylase plays a critical role in the biosynthesis of ergosterol, the major sterol component in fungal membranes that participates in a variety of functions. Acts as a self-resistant CYP51 that contains mutations found in CYP51s isolated from azole resistance strains and that is not inhibited by the final product of the cluster, lanomycin.","Lanosterol 14-alpha demethylase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway. ERG11 catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol. The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (",Yes,Yes,Yes,Yes,Yes,Yes,GO:0020037; GO:0005506; GO:0008398,GO:0008398,GO:0008398,GO:0008398,GO:0008395,GO:0008398,0.5487,0.5487,0.5487,0.319,0.5487,5,0.5028,0.2089,no
LAN1_PYRDE,P0DXV0,ProtT3,Eukaryota,540,"Sterol 14-alpha demethylase; part of the gene cluster that mediates the biosynthesis of tetrahydropyranyl antifungal agent lanomycin that acts as an inhibitor of CYP51 and blocks the ergosterol biosynthesis. Sterol 14-alpha-demethylase plays a critical role in the biosynthesis of ergosterol, the major sterol component in fungal membranes that participates in a variety of functions. Acts as a self-resistant CYP51 that contains mutations found in CYP51s isolated from azole resistance strains and that is not inhibited by the final product of the cluster, lanomycin.","Sterol 14alpha-demethylase that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in fungal membranes that participates in a variety of functions (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane (By similarity). In filamentous fungi, during the initial step of this module, lanosterol (lanosta-8,24-dien-3beta-ol) is converted to eburicol (By similarity)",Yes,Yes,Yes,Yes,Yes,Yes,GO:0020037; GO:0005506; GO:0008398,GO:0008398; GO:0005506; GO:0020037,GO:0008398; GO:0005506; GO:0020037,GO:0008398; GO:0005506; GO:0020037,GO:0008398; GO:0005506; GO:0020037,GO:0008398; GO:0004497,1.0,1.0,1.0,1.0,0.5787,5,0.9157,0.2089,no
LAN1_PYRDE,P0DXV0,ProtTale,Eukaryota,540,"Sterol 14-alpha demethylase; part of the gene cluster that mediates the biosynthesis of tetrahydropyranyl antifungal agent lanomycin that acts as an inhibitor of CYP51 and blocks the ergosterol biosynthesis. Sterol 14-alpha-demethylase plays a critical role in the biosynthesis of ergosterol, the major sterol component in fungal membranes that participates in a variety of functions. Acts as a self-resistant CYP51 that contains mutations found in CYP51s isolated from azole resistance strains and that is not inhibited by the final product of the cluster, lanomycin.","Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. Within the pathway, PC-2 catalyzes the oxidation of penitrem D to penitrem E. The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3-glycerol phosphate with GGPP by penC then forms 3-geranylgeranylindole (3-",No,No,No,No,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0008398,GO:0004497,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0020037; GO:0005506,GO:0004497,GO:0004497; GO:0005506; GO:0020037,0.378,0.8729,0.8729,0.378,0.8729,5,0.6749,0.2089,no
LAN1_PYRDE,P0DXV0,Protein2Text,Eukaryota,540,"Sterol 14-alpha demethylase; part of the gene cluster that mediates the biosynthesis of tetrahydropyranyl antifungal agent lanomycin that acts as an inhibitor of CYP51 and blocks the ergosterol biosynthesis. Sterol 14-alpha-demethylase plays a critical role in the biosynthesis of ergosterol, the major sterol component in fungal membranes that participates in a variety of functions. Acts as a self-resistant CYP51 that contains mutations found in CYP51s isolated from azole resistance strains and that is not inhibited by the final product of the cluster, lanomycin.","The molecular function of this protein is to catalyze the conversion of lanosterol to ergosterol, which is a critical step in the biosynthesis of ergosterol, a key component of fungal cell membranes. More specifically, it is a cytochrome P450 monooxygenase that is involved in the oxidation of lanosterol to ergosterol. This reaction is essential for the growth and survival of fungi.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0020037; GO:0005506; GO:0008398,GO:0004497,GO:0005506; GO:0016491,GO:0008395,GO:0004497,GO:0004497,0.378,0.6513,0.319,0.378,0.378,5,0.4209,0.2089,no
LAN1_PYRDE,P0DXV0,Reference,Eukaryota,540,"Sterol 14-alpha demethylase; part of the gene cluster that mediates the biosynthesis of tetrahydropyranyl antifungal agent lanomycin that acts as an inhibitor of CYP51 and blocks the ergosterol biosynthesis. Sterol 14-alpha-demethylase plays a critical role in the biosynthesis of ergosterol, the major sterol component in fungal membranes that participates in a variety of functions. Acts as a self-resistant CYP51 that contains mutations found in CYP51s isolated from azole resistance strains and that is not inhibited by the final product of the cluster, lanomycin.","Sterol 14-alpha demethylase; part of the gene cluster that mediates the biosynthesis of tetrahydropyranyl antifungal agent lanomycin that acts as an inhibitor of CYP51 and blocks the ergosterol biosynthesis. Sterol 14-alpha-demethylase plays a critical role in the biosynthesis of ergosterol, the major sterol component in fungal membranes that participates in a variety of functions. Acts as a self-resistant CYP51 that contains mutations found in CYP51s isolated from azole resistance strains and that is not inhibited by the final product of the cluster, lanomycin.",,,,,,,GO:0020037; GO:0005506; GO:0008398,GO:0008398,GO:0000249,GO:0008398; GO:0020037,GO:0008395; GO:0005506; GO:0020037,GO:0008395; GO:0005506; GO:0020037,0.5487,0.2435,0.8457,0.8413,0.8413,5,0.6641,0.2089,no
RNE_MYCTU,P71905,ESM2Text,Bacteria,953,"Endoribonuclease that plays a central role in RNA processing and decay. Plays a major role in pre-16S rRNA maturation, probably generating the mature 5'-end, and a minor role in pre-5S and pre-23S rRNA maturation. Probably also processes tRNA. RNase E and HupB jointly contribute to cellular adaptation to changing growth conditions and survival during antibiotic treatment and in the host.",Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0008995; GO:0004540; GO:0019843,GO:0004521,GO:0004521,GO:0004521,GO:0004521,GO:0004521,0.504,0.504,0.504,0.504,0.504,5,0.504,0.3343,no
RNE_MYCTU,P71905,Prot2Text,Bacteria,953,"Endoribonuclease that plays a central role in RNA processing and decay. Plays a major role in pre-16S rRNA maturation, probably generating the mature 5'-end, and a minor role in pre-5S and pre-23S rRNA maturation. Probably also processes tRNA. RNase E and HupB jointly contribute to cellular adaptation to changing growth conditions and survival during antibiotic treatment and in the host.",Endoribonuclease that plays a central role in rRNA and tRNA processing and mRNA decay. Has been shown to act on 9S rRNA (the precursor of 5S rRNA).,Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0008995; GO:0004540; GO:0019843,GO:0004521,GO:0004521,GO:0004521,GO:0004521,GO:0004521,0.504,0.504,0.504,0.504,0.504,5,0.504,0.3343,no
RNE_MYCTU,P71905,ProtT3,Bacteria,953,"Endoribonuclease that plays a central role in RNA processing and decay. Plays a major role in pre-16S rRNA maturation, probably generating the mature 5'-end, and a minor role in pre-5S and pre-23S rRNA maturation. Probably also processes tRNA. RNase E and HupB jointly contribute to cellular adaptation to changing growth conditions and survival during antibiotic treatment and in the host.",Endoribonuclease that degrades single-stranded RNA (ssRNA) and single-stranded DNA (ssDNA),Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0046872; GO:0008995; GO:0004540; GO:0019843,GO:0004521; GO:0004520,GO:0004519,GO:0004518,GO:0004521,GO:0004521; GO:0004520,0.4962,0.4049,0.4469,0.504,0.4962,5,0.4696,0.3343,no
RNE_MYCTU,P71905,ProtTale,Bacteria,953,"Endoribonuclease that plays a central role in RNA processing and decay. Plays a major role in pre-16S rRNA maturation, probably generating the mature 5'-end, and a minor role in pre-5S and pre-23S rRNA maturation. Probably also processes tRNA. RNase E and HupB jointly contribute to cellular adaptation to changing growth conditions and survival during antibiotic treatment and in the host.",Involved in pre-rRNA and tRNA processing. Binds to the 5'-end of 16S rRNA.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0008995; GO:0004540; GO:0019843,GO:0019843,GO:0003723,GO:0003723,,GO:0003723,0.4838,0.4372,0.4372,,0.4372,4,0.4488,0.3343,no
RNE_MYCTU,P71905,Protein2Text,Bacteria,953,"Endoribonuclease that plays a central role in RNA processing and decay. Plays a major role in pre-16S rRNA maturation, probably generating the mature 5'-end, and a minor role in pre-5S and pre-23S rRNA maturation. Probably also processes tRNA. RNase E and HupB jointly contribute to cellular adaptation to changing growth conditions and survival during antibiotic treatment and in the host.",The molecular function of this protein is RNA-binding.,Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0046872; GO:0008995; GO:0004540; GO:0019843,GO:0003723,GO:0003723,GO:0003723,GO:0003723,GO:0003723,0.4372,0.4372,0.4372,0.4372,0.4372,5,0.4372,0.3343,no
RNE_MYCTU,P71905,Reference,Bacteria,953,"Endoribonuclease that plays a central role in RNA processing and decay. Plays a major role in pre-16S rRNA maturation, probably generating the mature 5'-end, and a minor role in pre-5S and pre-23S rRNA maturation. Probably also processes tRNA. RNase E and HupB jointly contribute to cellular adaptation to changing growth conditions and survival during antibiotic treatment and in the host.","Endoribonuclease that plays a central role in RNA processing and decay. Plays a major role in pre-16S rRNA maturation, probably generating the mature 5'-end, and a minor role in pre-5S and pre-23S rRNA maturation. Probably also processes tRNA. RNase E and HupB jointly contribute to cellular adaptation to changing growth conditions and survival during antibiotic treatment and in the host.",,,,,,,GO:0046872; GO:0008995; GO:0004540; GO:0019843,GO:0004521,GO:0004521,GO:0004521,GO:0004521,GO:0004521,0.504,0.504,0.504,0.504,0.504,5,0.504,0.3343,no
CLAS_AMPCV,P9WEI6,ESM2Text,Eukaryota,313,"Prenyltransferase; part of the gene cluster that mediates the biosynthesis of clavilactone A, a meroterpenoid that features a unique benzo-fused ten-membered carbocyclic ring unit with an alpha,beta- epoxy-gamma-lactone moiety, forming an intriguing 10/5/3 tricyclic nested skeleton. ClaR, ClaS and ClaT are sufficient to produce clavilactone A. Within the pathway, claS acts as an atypical UbiA prenyltransferase that transfers geranyl pyrophosphate (GPP) to hydroquinone (HYQ) instead of p- hydroxybenzoic acid (PHB), producing the first intermediate geranylhydroquinone (Ref.2). The cytochrome P450 monooxygenase claR then catalyzes the diradical coupling reaction between the intramolecular hydroquinone and allyl moieties to form the benzo-fused ten-membered carbocyclic ring unit of wigantol. Finally the cytochrome P450 monooxygenase claT exquisitely and stereoselectively assembles the alpha,beta-epoxy-gamma-lactone moiety, producing clavilactone A via arnebinol A.","Prenyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ. Paxilline is converted to beta-pax",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008412,GO:0016765,GO:0004337,GO:0004337,GO:0004337,GO:0004337,0.729,0.6335,0.6335,0.6335,0.6335,5,0.6526,0.34,no
CLAS_AMPCV,P9WEI6,Prot2Text,Eukaryota,313,"Prenyltransferase; part of the gene cluster that mediates the biosynthesis of clavilactone A, a meroterpenoid that features a unique benzo-fused ten-membered carbocyclic ring unit with an alpha,beta- epoxy-gamma-lactone moiety, forming an intriguing 10/5/3 tricyclic nested skeleton. ClaR, ClaS and ClaT are sufficient to produce clavilactone A. Within the pathway, claS acts as an atypical UbiA prenyltransferase that transfers geranyl pyrophosphate (GPP) to hydroquinone (HYQ) instead of p- hydroxybenzoic acid (PHB), producing the first intermediate geranylhydroquinone (Ref.2). The cytochrome P450 monooxygenase claR then catalyzes the diradical coupling reaction between the intramolecular hydroquinone and allyl moieties to form the benzo-fused ten-membered carbocyclic ring unit of wigantol. Finally the cytochrome P450 monooxygenase claT exquisitely and stereoselectively assembles the alpha,beta-epoxy-gamma-lactone moiety, producing clavilactone A via arnebinol A.","Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.",Maybe,Yes,Yes,No,Maybe,not-Yes,GO:0008412,GO:0008412,GO:0008412,GO:0008412,GO:0004659,GO:0008412,1.0,1.0,1.0,0.8582,1.0,5,0.9716,0.34,no
CLAS_AMPCV,P9WEI6,ProtT3,Eukaryota,313,"Prenyltransferase; part of the gene cluster that mediates the biosynthesis of clavilactone A, a meroterpenoid that features a unique benzo-fused ten-membered carbocyclic ring unit with an alpha,beta- epoxy-gamma-lactone moiety, forming an intriguing 10/5/3 tricyclic nested skeleton. ClaR, ClaS and ClaT are sufficient to produce clavilactone A. Within the pathway, claS acts as an atypical UbiA prenyltransferase that transfers geranyl pyrophosphate (GPP) to hydroquinone (HYQ) instead of p- hydroxybenzoic acid (PHB), producing the first intermediate geranylhydroquinone (Ref.2). The cytochrome P450 monooxygenase claR then catalyzes the diradical coupling reaction between the intramolecular hydroquinone and allyl moieties to form the benzo-fused ten-membered carbocyclic ring unit of wigantol. Finally the cytochrome P450 monooxygenase claT exquisitely and stereoselectively assembles the alpha,beta-epoxy-gamma-lactone moiety, producing clavilactone A via arnebinol A.","Polyprenyl transferase; part of the gene cluster that mediates the biosynthesis of notoamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first step of notoamide biosynthesis involves coupling of L-proline and L-tryptophan by the bimodular NRPS notE, to produce cyclo-L-tryptophan-L-proline called brevianamide F . The reverse pre",Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0008412,GO:0016765,GO:0004659,GO:0016765,GO:0004659,GO:0016765,0.729,0.8582,0.729,0.8582,0.729,5,0.7807,0.34,no
CLAS_AMPCV,P9WEI6,ProtTale,Eukaryota,313,"Prenyltransferase; part of the gene cluster that mediates the biosynthesis of clavilactone A, a meroterpenoid that features a unique benzo-fused ten-membered carbocyclic ring unit with an alpha,beta- epoxy-gamma-lactone moiety, forming an intriguing 10/5/3 tricyclic nested skeleton. ClaR, ClaS and ClaT are sufficient to produce clavilactone A. Within the pathway, claS acts as an atypical UbiA prenyltransferase that transfers geranyl pyrophosphate (GPP) to hydroquinone (HYQ) instead of p- hydroxybenzoic acid (PHB), producing the first intermediate geranylhydroquinone (Ref.2). The cytochrome P450 monooxygenase claR then catalyzes the diradical coupling reaction between the intramolecular hydroquinone and allyl moieties to form the benzo-fused ten-membered carbocyclic ring unit of wigantol. Finally the cytochrome P450 monooxygenase claT exquisitely and stereoselectively assembles the alpha,beta-epoxy-gamma-lactone moiety, producing clavilactone A via arnebinol A.","Polyprenyl transferase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0008412,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.34,no
CLAS_AMPCV,P9WEI6,Protein2Text,Eukaryota,313,"Prenyltransferase; part of the gene cluster that mediates the biosynthesis of clavilactone A, a meroterpenoid that features a unique benzo-fused ten-membered carbocyclic ring unit with an alpha,beta- epoxy-gamma-lactone moiety, forming an intriguing 10/5/3 tricyclic nested skeleton. ClaR, ClaS and ClaT are sufficient to produce clavilactone A. Within the pathway, claS acts as an atypical UbiA prenyltransferase that transfers geranyl pyrophosphate (GPP) to hydroquinone (HYQ) instead of p- hydroxybenzoic acid (PHB), producing the first intermediate geranylhydroquinone (Ref.2). The cytochrome P450 monooxygenase claR then catalyzes the diradical coupling reaction between the intramolecular hydroquinone and allyl moieties to form the benzo-fused ten-membered carbocyclic ring unit of wigantol. Finally the cytochrome P450 monooxygenase claT exquisitely and stereoselectively assembles the alpha,beta-epoxy-gamma-lactone moiety, producing clavilactone A via arnebinol A.","The molecular function of this protein is involved in the transfer of electrons during the process of cellular respiration, specifically in the conversion of one molecule to another. It is likely involved in the transfer of electrons from one molecule to another, which is a crucial step in many biological processes.",No,No,No,No,No,not-Yes,GO:0008412,,,,,,,,,,,0,,0.34,no
CLAS_AMPCV,P9WEI6,Reference,Eukaryota,313,"Prenyltransferase; part of the gene cluster that mediates the biosynthesis of clavilactone A, a meroterpenoid that features a unique benzo-fused ten-membered carbocyclic ring unit with an alpha,beta- epoxy-gamma-lactone moiety, forming an intriguing 10/5/3 tricyclic nested skeleton. ClaR, ClaS and ClaT are sufficient to produce clavilactone A. Within the pathway, claS acts as an atypical UbiA prenyltransferase that transfers geranyl pyrophosphate (GPP) to hydroquinone (HYQ) instead of p- hydroxybenzoic acid (PHB), producing the first intermediate geranylhydroquinone (Ref.2). The cytochrome P450 monooxygenase claR then catalyzes the diradical coupling reaction between the intramolecular hydroquinone and allyl moieties to form the benzo-fused ten-membered carbocyclic ring unit of wigantol. Finally the cytochrome P450 monooxygenase claT exquisitely and stereoselectively assembles the alpha,beta-epoxy-gamma-lactone moiety, producing clavilactone A via arnebinol A.","Prenyltransferase; part of the gene cluster that mediates the biosynthesis of clavilactone A, a meroterpenoid that features a unique benzo-fused ten-membered carbocyclic ring unit with an alpha,beta- epoxy-gamma-lactone moiety, forming an intriguing 10/5/3 tricyclic nested skeleton. ClaR, ClaS and ClaT are sufficient to produce clavilactone A. Within the pathway, claS acts as an atypical UbiA prenyltransferase that transfers geranyl pyrophosphate (GPP) to hydroquinone (HYQ) instead of p- hydroxybenzoic acid (PHB), producing the first intermediate geranylhydroquinone (Ref.2). The cytochrome P450 monooxygenase claR then catalyzes the diradical coupling reaction between the intramolecular hydroquinone and allyl moieties to form the benzo-fused ten-membered carbocyclic ring unit of wigantol. Finally the cytochrome P450 monooxygenase claT exquisitely and stereoselectively assembles the alpha,beta-epoxy-gamma-lactone moiety, producing clavilactone A via arnebinol A.",,,,,,,GO:0008412,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.34,no
LP10_SERMA,P9WEM3,ESM2Text,Bacteria,197,Lytic polysaccharide monooxygenase (LPMO) that oxidatively cleaves alpha- and beta-chitin with C1 regioselectivity. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.,"Glycosylates chitin. Glucose binding improves retention of chitin in the cell walls of E.faecalis, but not that of V.cholerae. Does not enhance adherence of V.cholerae to human cells.",No,No,No,No,No,not-Yes,GO:0046872; GO:0004497,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.3023,0.3023,0.3023,0.3023,0.3023,5,0.3023,0.4496,no
LP10_SERMA,P9WEM3,Prot2Text,Bacteria,197,Lytic polysaccharide monooxygenase (LPMO) that oxidatively cleaves alpha- and beta-chitin with C1 regioselectivity. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.,Component of the sil cation-efflux system that confers resistance to silver.,No,No,No,No,No,not-Yes,GO:0046872; GO:0004497,,,,,GO:0046873,,,,,0.1139,1,0.1139,0.4496,no
LP10_SERMA,P9WEM3,ProtT3,Bacteria,197,Lytic polysaccharide monooxygenase (LPMO) that oxidatively cleaves alpha- and beta-chitin with C1 regioselectivity. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.,May be involved in cell wall metabolism. Secreted. Belongs to the ChgA family,Vague,Vague,Vague,Vague,No,not-Yes,GO:0046872; GO:0004497,,,,,,,,,,,0,,0.4496,no
LP10_SERMA,P9WEM3,ProtTale,Bacteria,197,Lytic polysaccharide monooxygenase (LPMO) that oxidatively cleaves alpha- and beta-chitin with C1 regioselectivity. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.,May be involved in the degradation of the bacterial cell wall during stationary phase. Acts on N-acetylmuramyl-L-alanyl-D-glucosamine (MurNAc-GlcNAc) as the first enzymatic step in a pathway that leads to the degradation of the cell wall.,No,No,No,No,No,not-Yes,GO:0046872; GO:0004497,GO:0016798,GO:0016787,GO:0016798,GO:0016798,GO:0008745,0.3023,0.3731,0.3023,0.3023,0.2281,5,0.3016,0.4496,no
LP10_SERMA,P9WEM3,Protein2Text,Bacteria,197,Lytic polysaccharide monooxygenase (LPMO) that oxidatively cleaves alpha- and beta-chitin with C1 regioselectivity. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.,"This protein is involved in catalyzing the oxidation of D-glucose to D-gluconate. It is an oxidoreductase, specifically a glucose oxidase. It catalyzes the oxidation of D-glucose to D-gluconate, with the concomitant reduction of oxygen to hydrogen peroxide. This enzyme plays a crucial role in the degradation of glucose in many organisms.",No,No,No,No,No,not-Yes,GO:0046872; GO:0004497,GO:0004345,GO:0004345; GO:0016614,,GO:0016614,GO:0004345,0.351,0.4827,,0.483,0.351,4,0.4169,0.4496,no
LP10_SERMA,P9WEM3,Reference,Bacteria,197,Lytic polysaccharide monooxygenase (LPMO) that oxidatively cleaves alpha- and beta-chitin with C1 regioselectivity. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.,Lytic polysaccharide monooxygenase (LPMO) that oxidatively cleaves alpha- and beta-chitin with C1 regioselectivity. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.,,,,,,,GO:0046872; GO:0004497,GO:0016491; GO:0005507,GO:0005507,GO:0005507,GO:0016491; GO:0005507,GO:0016491; GO:0005507,0.7926,0.5476,0.5476,0.7926,0.7926,5,0.6946,0.4496,no
TRWB_ECOLX,Q04230,ESM2Text,Bacteria,507,"Component of the Trw type IV secretion system (T4SS), which is involved in bacterial conjugation of plasmid R388, a conjugative plasmid that confers resistance to sulfonamide and trimethoprim. The TrwB subunit couples the relaxosome (a DNA-protein complex) to the translocation channel for transport. Binds DNA. Binds G4 DNA structures with high affinity, suggesting that it may recognize G-quadruplex structures as loading sites on the DNA. Binds ATP. Shows DNA-dependent ATPase activity. May act as a DNA-translocating motor and provide energy to the system. A truncated soluble form binds single-stranded and double-stranded DNA non-specifically and independently of ATP binding. The intact protein binds preferentially purine over pyrimidine nucleotides, NTPs over NDPs, and ribo- over deoxyribonucleotides. DNA binding to TrwB enhances TrwC nic cleavage activity. Does not show any significant DNA helicase activity.",Component of the type IV secretion system VirB/VirD4 which could be a major virulence determinant for subversion of human endothelial cell (HEC) function.,Maybe,Maybe,Yes,Yes,Maybe,not-Yes,GO:0042802; GO:0046872; GO:0000166,,,,,,,,,,,0,,0.4217,no
TRWB_ECOLX,Q04230,Prot2Text,Bacteria,507,"Component of the Trw type IV secretion system (T4SS), which is involved in bacterial conjugation of plasmid R388, a conjugative plasmid that confers resistance to sulfonamide and trimethoprim. The TrwB subunit couples the relaxosome (a DNA-protein complex) to the translocation channel for transport. Binds DNA. Binds G4 DNA structures with high affinity, suggesting that it may recognize G-quadruplex structures as loading sites on the DNA. Binds ATP. Shows DNA-dependent ATPase activity. May act as a DNA-translocating motor and provide energy to the system. A truncated soluble form binds single-stranded and double-stranded DNA non-specifically and independently of ATP binding. The intact protein binds preferentially purine over pyrimidine nucleotides, NTPs over NDPs, and ribo- over deoxyribonucleotides. DNA binding to TrwB enhances TrwC nic cleavage activity. Does not show any significant DNA helicase activity.","Part of the ESX-1 specialized secretion system, which delivers several virulence factors to host cells during infection, including the key virulence factors EsxA (ESAT-6) and EsxB (CFP-10).",No,No,No,No,No,not-Yes,GO:0042802; GO:0046872; GO:0000166,,,,,,,,,,,0,,0.4217,no
TRWB_ECOLX,Q04230,ProtT3,Bacteria,507,"Component of the Trw type IV secretion system (T4SS), which is involved in bacterial conjugation of plasmid R388, a conjugative plasmid that confers resistance to sulfonamide and trimethoprim. The TrwB subunit couples the relaxosome (a DNA-protein complex) to the translocation channel for transport. Binds DNA. Binds G4 DNA structures with high affinity, suggesting that it may recognize G-quadruplex structures as loading sites on the DNA. Binds ATP. Shows DNA-dependent ATPase activity. May act as a DNA-translocating motor and provide energy to the system. A truncated soluble form binds single-stranded and double-stranded DNA non-specifically and independently of ATP binding. The intact protein binds preferentially purine over pyrimidine nucleotides, NTPs over NDPs, and ribo- over deoxyribonucleotides. DNA binding to TrwB enhances TrwC nic cleavage activity. Does not show any significant DNA helicase activity.",Cell membrane; Multi-pass membrane protein,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0042802; GO:0046872; GO:0000166,,,,,,,,,,,0,,0.4217,no
TRWB_ECOLX,Q04230,ProtTale,Bacteria,507,"Component of the Trw type IV secretion system (T4SS), which is involved in bacterial conjugation of plasmid R388, a conjugative plasmid that confers resistance to sulfonamide and trimethoprim. The TrwB subunit couples the relaxosome (a DNA-protein complex) to the translocation channel for transport. Binds DNA. Binds G4 DNA structures with high affinity, suggesting that it may recognize G-quadruplex structures as loading sites on the DNA. Binds ATP. Shows DNA-dependent ATPase activity. May act as a DNA-translocating motor and provide energy to the system. A truncated soluble form binds single-stranded and double-stranded DNA non-specifically and independently of ATP binding. The intact protein binds preferentially purine over pyrimidine nucleotides, NTPs over NDPs, and ribo- over deoxyribonucleotides. DNA binding to TrwB enhances TrwC nic cleavage activity. Does not show any significant DNA helicase activity.","Component of the VirB/VirD4 type IV secretion system (T4SS), which translocates transfer DNA (T-DNA) and virulence effector proteins into plant host cells, leading to crown gall disease. The VirD4 subunit recruits substrates and probably delivers them to the translocation channel. It also provides energy to the system.",Maybe,Maybe,Yes,Yes,Maybe,not-Yes,GO:0042802; GO:0046872; GO:0000166,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887,GO:0016887,GO:0016887,0.3307,0.3307,0.1116,0.1116,0.1116,5,0.1992,0.4217,no
TRWB_ECOLX,Q04230,Protein2Text,Bacteria,507,"Component of the Trw type IV secretion system (T4SS), which is involved in bacterial conjugation of plasmid R388, a conjugative plasmid that confers resistance to sulfonamide and trimethoprim. The TrwB subunit couples the relaxosome (a DNA-protein complex) to the translocation channel for transport. Binds DNA. Binds G4 DNA structures with high affinity, suggesting that it may recognize G-quadruplex structures as loading sites on the DNA. Binds ATP. Shows DNA-dependent ATPase activity. May act as a DNA-translocating motor and provide energy to the system. A truncated soluble form binds single-stranded and double-stranded DNA non-specifically and independently of ATP binding. The intact protein binds preferentially purine over pyrimidine nucleotides, NTPs over NDPs, and ribo- over deoxyribonucleotides. DNA binding to TrwB enhances TrwC nic cleavage activity. Does not show any significant DNA helicase activity.","This protein is a part of the molecular function of a virus, specifically a bacteriophage, that plays a role in the replication of the viral genome. The exact molecular function of this protein is not specified, but it is likely involved in the replication of the viral genome, possibly by regulating the expression of viral genes or by participating in the replication of viral DNA.",No,No,No,Vague,No,not-Yes,GO:0042802; GO:0046872; GO:0000166,,,,,,,,,,,0,,0.4217,no
TRWB_ECOLX,Q04230,Reference,Bacteria,507,"Component of the Trw type IV secretion system (T4SS), which is involved in bacterial conjugation of plasmid R388, a conjugative plasmid that confers resistance to sulfonamide and trimethoprim. The TrwB subunit couples the relaxosome (a DNA-protein complex) to the translocation channel for transport. Binds DNA. Binds G4 DNA structures with high affinity, suggesting that it may recognize G-quadruplex structures as loading sites on the DNA. Binds ATP. Shows DNA-dependent ATPase activity. May act as a DNA-translocating motor and provide energy to the system. A truncated soluble form binds single-stranded and double-stranded DNA non-specifically and independently of ATP binding. The intact protein binds preferentially purine over pyrimidine nucleotides, NTPs over NDPs, and ribo- over deoxyribonucleotides. DNA binding to TrwB enhances TrwC nic cleavage activity. Does not show any significant DNA helicase activity.","Component of the Trw type IV secretion system (T4SS), which is involved in bacterial conjugation of plasmid R388, a conjugative plasmid that confers resistance to sulfonamide and trimethoprim. The TrwB subunit couples the relaxosome (a DNA-protein complex) to the translocation channel for transport. Binds DNA. Binds G4 DNA structures with high affinity, suggesting that it may recognize G-quadruplex structures as loading sites on the DNA. Binds ATP. Shows DNA-dependent ATPase activity. May act as a DNA-translocating motor and provide energy to the system. A truncated soluble form binds single-stranded and double-stranded DNA non-specifically and independently of ATP binding. The intact protein binds preferentially purine over pyrimidine nucleotides, NTPs over NDPs, and ribo- over deoxyribonucleotides. DNA binding to TrwB enhances TrwC nic cleavage activity. Does not show any significant DNA helicase activity.",,,,,,,GO:0042802; GO:0046872; GO:0000166,GO:0003677; GO:0016887; GO:0005524,GO:0003677; GO:0016887; GO:0005524,GO:0003677; GO:0005524; GO:0016887,GO:0003677; GO:0005524; GO:0016887,GO:0003677; GO:0005524; GO:0016887,0.3781,0.3781,0.3781,0.3781,0.3781,5,0.3781,0.4217,no
CYPE3_ASPTN,Q0D1W9,ESM2Text,Eukaryota,1050,"Self-sufficient cytochrome P450 monooxygenase that catalyzes the regioselective in-chain hydroxylation of alkanes, fatty alcohols, and fatty acids at the omega-7 position. Performs hydroxylation of C10-C16 n-alkanes and C12 and C14 fatty alcohols; and thereby enables the one step biocatalytic synthesis of rare alcohols such as 5-dodecanol and 7-tetradecanol. Converts 1-dodecanol into 1,5- dodecanediol as major product with very little sub-terminally hydroxylated products with the 1,4-dodecanediol and 1,6-dodecanediol more abundant. Does not use hexadecanediol nor decanoic acid as substrates. Converts dodecanoic acid to 5-hydroxydodecanoic acid which can be further converted into delta-dodecalactone by lactonization of the 5-hydroxy acid at low pH. Also gives sub-terminal hydroxylation of dodecanoic acid with 9-hydroxydodecanoic acid being the second most abundant product. The C14 and C16 fatty acids are double hydroxylated to yield dihydroxy acids hydroxylated at both the omega-7 position and a sub-terminal position (omega-1, omega-2, or omega-3).","Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of fatty acids at omega-1, omega-2 and omega-3 positions, yielding primarily omega-1 and omega-2 hydroxylated products. Hydroxylation of fatty acids occurs in a process called fatty acid beta-oxidation. This enzyme reduces the C-2 and C-3 carbon atoms of the pentadecapeptide back to C-2 and C-4 carbon atoms.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0070330; GO:0050660; GO:0010181; GO:0020037; GO:0005506; GO:0003958,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.3261,0.3261,0.3261,0.3261,0.3261,5,0.3261,0.2276,no
CYPE3_ASPTN,Q0D1W9,Prot2Text,Eukaryota,1050,"Self-sufficient cytochrome P450 monooxygenase that catalyzes the regioselective in-chain hydroxylation of alkanes, fatty alcohols, and fatty acids at the omega-7 position. Performs hydroxylation of C10-C16 n-alkanes and C12 and C14 fatty alcohols; and thereby enables the one step biocatalytic synthesis of rare alcohols such as 5-dodecanol and 7-tetradecanol. Converts 1-dodecanol into 1,5- dodecanediol as major product with very little sub-terminally hydroxylated products with the 1,4-dodecanediol and 1,6-dodecanediol more abundant. Does not use hexadecanediol nor decanoic acid as substrates. Converts dodecanoic acid to 5-hydroxydodecanoic acid which can be further converted into delta-dodecalactone by lactonization of the 5-hydroxy acid at low pH. Also gives sub-terminal hydroxylation of dodecanoic acid with 9-hydroxydodecanoic acid being the second most abundant product. The C14 and C16 fatty acids are double hydroxylated to yield dihydroxy acids hydroxylated at both the omega-7 position and a sub-terminal position (omega-1, omega-2, or omega-3).",Oxidoreductase that may be involved in the biosynthesis of aromatic amino acids.,Vague,Vague,No,No,No,not-Yes,GO:0070330; GO:0050660; GO:0010181; GO:0020037; GO:0005506; GO:0003958,GO:0016491,,GO:0016491,GO:0016491,,0.3325,,0.3325,0.3325,,3,0.3325,0.2276,no
CYPE3_ASPTN,Q0D1W9,ProtT3,Eukaryota,1050,"Self-sufficient cytochrome P450 monooxygenase that catalyzes the regioselective in-chain hydroxylation of alkanes, fatty alcohols, and fatty acids at the omega-7 position. Performs hydroxylation of C10-C16 n-alkanes and C12 and C14 fatty alcohols; and thereby enables the one step biocatalytic synthesis of rare alcohols such as 5-dodecanol and 7-tetradecanol. Converts 1-dodecanol into 1,5- dodecanediol as major product with very little sub-terminally hydroxylated products with the 1,4-dodecanediol and 1,6-dodecanediol more abundant. Does not use hexadecanediol nor decanoic acid as substrates. Converts dodecanoic acid to 5-hydroxydodecanoic acid which can be further converted into delta-dodecalactone by lactonization of the 5-hydroxy acid at low pH. Also gives sub-terminal hydroxylation of dodecanoic acid with 9-hydroxydodecanoic acid being the second most abundant product. The C14 and C16 fatty acids are double hydroxylated to yield dihydroxy acids hydroxylated at both the omega-7 position and a sub-terminal position (omega-1, omega-2, or omega-3).","Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the host-selective toxins (HSTs) AF-toxins responsible for Alternaria black spot of strawberry disease by the strawberry pathotype . AF-toxins are cyclic depsipeptides containing the 3 residues 2-hydroxy-isovaleric acid (2-HIV), dehydroalanine, L-alanine which are common for all",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0070330; GO:0050660; GO:0010181; GO:0020037; GO:0005506; GO:0003958,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,0.7146,0.7146,0.7146,0.7146,0.7146,5,0.7146,0.2276,no
CYPE3_ASPTN,Q0D1W9,ProtTale,Eukaryota,1050,"Self-sufficient cytochrome P450 monooxygenase that catalyzes the regioselective in-chain hydroxylation of alkanes, fatty alcohols, and fatty acids at the omega-7 position. Performs hydroxylation of C10-C16 n-alkanes and C12 and C14 fatty alcohols; and thereby enables the one step biocatalytic synthesis of rare alcohols such as 5-dodecanol and 7-tetradecanol. Converts 1-dodecanol into 1,5- dodecanediol as major product with very little sub-terminally hydroxylated products with the 1,4-dodecanediol and 1,6-dodecanediol more abundant. Does not use hexadecanediol nor decanoic acid as substrates. Converts dodecanoic acid to 5-hydroxydodecanoic acid which can be further converted into delta-dodecalactone by lactonization of the 5-hydroxy acid at low pH. Also gives sub-terminal hydroxylation of dodecanoic acid with 9-hydroxydodecanoic acid being the second most abundant product. The C14 and C16 fatty acids are double hydroxylated to yield dihydroxy acids hydroxylated at both the omega-7 position and a sub-terminal position (omega-1, omega-2, or omega-3).","Self-sufficient cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, the cytochrome P450 monooxygenases FRIN-C and FRIN-B, the nonribosomal peptide synthetase FRIN-A, and the polyketide synthase FRIN-B are involved in the synthesis of the octaketide backbone. The biosynthesis of fusarin C starts with the condensation of one acetyl-CoA starter unit and 6 malonyl-CoA units by the non-reducing polyketide synthase FRIN-B to yield an octake",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0070330; GO:0050660; GO:0010181; GO:0020037; GO:0005506; GO:0003958,GO:0004497,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0020037; GO:0005506,GO:0004497,GO:0004497; GO:0005506; GO:0020037,0.3261,0.7146,0.7146,0.3261,0.7146,5,0.5592,0.2276,no
CYPE3_ASPTN,Q0D1W9,Protein2Text,Eukaryota,1050,"Self-sufficient cytochrome P450 monooxygenase that catalyzes the regioselective in-chain hydroxylation of alkanes, fatty alcohols, and fatty acids at the omega-7 position. Performs hydroxylation of C10-C16 n-alkanes and C12 and C14 fatty alcohols; and thereby enables the one step biocatalytic synthesis of rare alcohols such as 5-dodecanol and 7-tetradecanol. Converts 1-dodecanol into 1,5- dodecanediol as major product with very little sub-terminally hydroxylated products with the 1,4-dodecanediol and 1,6-dodecanediol more abundant. Does not use hexadecanediol nor decanoic acid as substrates. Converts dodecanoic acid to 5-hydroxydodecanoic acid which can be further converted into delta-dodecalactone by lactonization of the 5-hydroxy acid at low pH. Also gives sub-terminal hydroxylation of dodecanoic acid with 9-hydroxydodecanoic acid being the second most abundant product. The C14 and C16 fatty acids are double hydroxylated to yield dihydroxy acids hydroxylated at both the omega-7 position and a sub-terminal position (omega-1, omega-2, or omega-3).","The molecular function of this protein is a cytochrome P450 monooxygenase enzyme, which is involved in the metabolism of various compounds, including xenobiotics and endogenous substances. Specifically, it is involved in the oxidation of aliphatic hydrocarbons and other organic substrates.",Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0070330; GO:0050660; GO:0010181; GO:0020037; GO:0005506; GO:0003958,GO:0004497,GO:0005506; GO:0016491,GO:0004497,GO:0004497,GO:0004497,0.3261,0.5745,0.3261,0.3261,0.3261,5,0.3758,0.2276,no
CYPE3_ASPTN,Q0D1W9,Reference,Eukaryota,1050,"Self-sufficient cytochrome P450 monooxygenase that catalyzes the regioselective in-chain hydroxylation of alkanes, fatty alcohols, and fatty acids at the omega-7 position. Performs hydroxylation of C10-C16 n-alkanes and C12 and C14 fatty alcohols; and thereby enables the one step biocatalytic synthesis of rare alcohols such as 5-dodecanol and 7-tetradecanol. Converts 1-dodecanol into 1,5- dodecanediol as major product with very little sub-terminally hydroxylated products with the 1,4-dodecanediol and 1,6-dodecanediol more abundant. Does not use hexadecanediol nor decanoic acid as substrates. Converts dodecanoic acid to 5-hydroxydodecanoic acid which can be further converted into delta-dodecalactone by lactonization of the 5-hydroxy acid at low pH. Also gives sub-terminal hydroxylation of dodecanoic acid with 9-hydroxydodecanoic acid being the second most abundant product. The C14 and C16 fatty acids are double hydroxylated to yield dihydroxy acids hydroxylated at both the omega-7 position and a sub-terminal position (omega-1, omega-2, or omega-3).","Self-sufficient cytochrome P450 monooxygenase that catalyzes the regioselective in-chain hydroxylation of alkanes, fatty alcohols, and fatty acids at the omega-7 position. Performs hydroxylation of C10-C16 n-alkanes and C12 and C14 fatty alcohols; and thereby enables the one step biocatalytic synthesis of rare alcohols such as 5-dodecanol and 7-tetradecanol. Converts 1-dodecanol into 1,5- dodecanediol as major product with very little sub-terminally hydroxylated products with the 1,4-dodecanediol and 1,6-dodecanediol more abundant. Does not use hexadecanediol nor decanoic acid as substrates. Converts dodecanoic acid to 5-hydroxydodecanoic acid which can be further converted into delta-dodecalactone by lactonization of the 5-hydroxy acid at low pH. Also gives sub-terminal hydroxylation of dodecanoic acid with 9-hydroxydodecanoic acid being the second most abundant product. The C14 and C16 fatty acids are double hydroxylated to yield dihydroxy acids hydroxylated at both the omega-7 position and a sub-terminal position (omega-1, omega-2, or omega-3).",,,,,,,GO:0070330; GO:0050660; GO:0010181; GO:0020037; GO:0005506; GO:0003958,GO:0004497,GO:0004497; GO:0020037; GO:0005506,GO:0004497; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,0.3261,0.7146,0.5602,0.7146,0.7146,5,0.606,0.2276,no
OASD_RHOJR,Q0S4Q9,ESM2Text,Bacteria,490,"Dehydrogenase involved in the degradation of steroids. Catalyzes the introduction of a double bond between the C4 and C5 atoms of 3-keto-(5alpha)-steroids. Catalyzes the conversion of 5alpha- androst-1-ene-3,17-dione to androsta-1,4-diene-3,17-dione, and probably the conversion of 5alpha-androstan-3,17-dione to androst-4-ene-3,17- dione.","Involved in the degradation of the AAF (Araf A) substrate, which is the precursor of AAF (3'-dehydro-Araf-FltA) and AAF (3'-dehydroadapf A). Catalyzes the elimination of the C-1 and C-2 atoms of the AAF ring, forming the keto-enol-6-phosphate intermediate that serves as AAF substrate.",No,No,No,No,No,not-Yes,GO:0000166; GO:0033765,,,,,,,,,,,0,,0.1719,no
OASD_RHOJR,Q0S4Q9,Prot2Text,Bacteria,490,"Dehydrogenase involved in the degradation of steroids. Catalyzes the introduction of a double bond between the C4 and C5 atoms of 3-keto-(5alpha)-steroids. Catalyzes the conversion of 5alpha- androst-1-ene-3,17-dione to androsta-1,4-diene-3,17-dione, and probably the conversion of 5alpha-androstan-3,17-dione to androst-4-ene-3,17- dione.",Catalyzes the two-step monooxygenation required for the C5-C6 double bond formation during ferrous iron utilization. Uses NADH as the inherent electron donor for the oxidation of ferrous iron.,No,No,No,No,No,not-Yes,GO:0000166; GO:0033765,GO:0004497,GO:0004497,GO:0004497,GO:0004497,,0.3758,0.3758,0.3758,0.3758,,4,0.3758,0.1719,no
OASD_RHOJR,Q0S4Q9,ProtT3,Bacteria,490,"Dehydrogenase involved in the degradation of steroids. Catalyzes the introduction of a double bond between the C4 and C5 atoms of 3-keto-(5alpha)-steroids. Catalyzes the conversion of 5alpha- androst-1-ene-3,17-dione to androsta-1,4-diene-3,17-dione, and probably the conversion of 5alpha-androstan-3,17-dione to androst-4-ene-3,17- dione.",Catalyzes the oxidation of L-glutamic acid to 5-oxoproline. Belongs to the Gfo/Idh/MocA family,No,No,No,No,No,not-Yes,GO:0000166; GO:0033765,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4603,0.4603,0.4603,0.4603,0.4603,5,0.4603,0.1719,no
OASD_RHOJR,Q0S4Q9,ProtTale,Bacteria,490,"Dehydrogenase involved in the degradation of steroids. Catalyzes the introduction of a double bond between the C4 and C5 atoms of 3-keto-(5alpha)-steroids. Catalyzes the conversion of 5alpha- androst-1-ene-3,17-dione to androsta-1,4-diene-3,17-dione, and probably the conversion of 5alpha-androstan-3,17-dione to androst-4-ene-3,17- dione.",Involved in the degradation of 3-methylglutaconic acid. Catalyzes the retro-aldol cleavage of 3- methylglutaconyl-CoA to form (3R)-2-hydroxyisovalerate and acetoacetyl-CoA. Also able to catalyze the retro- aldol cleavage of 2-hydroxyisocaproyl-CoA to form (3R)-2-hydroxyisocaproate and acetoacetyl-CoA.,No,No,No,No,No,not-Yes,GO:0000166; GO:0033765,GO:0016832,GO:0016829,GO:0016832,GO:0016829,GO:0016829,0.203,0.2947,0.203,0.2947,0.2947,5,0.258,0.1719,no
OASD_RHOJR,Q0S4Q9,Protein2Text,Bacteria,490,"Dehydrogenase involved in the degradation of steroids. Catalyzes the introduction of a double bond between the C4 and C5 atoms of 3-keto-(5alpha)-steroids. Catalyzes the conversion of 5alpha- androst-1-ene-3,17-dione to androsta-1,4-diene-3,17-dione, and probably the conversion of 5alpha-androstan-3,17-dione to androst-4-ene-3,17- dione.","This protein is involved in catalyzing the conversion of a compound, specifically an oxidoreduction reaction. More specifically, it is a subunit of a multicomponent enzyme system that catalyzes the oxidation of glucose to gluconate using oxygen as the electron acceptor.",No,No,Vague,Vague,No,not-Yes,GO:0000166; GO:0033765,GO:0016491,GO:0016614,,GO:0016491,GO:0016491,0.4603,0.3758,,0.4603,0.4603,4,0.4392,0.1719,no
OASD_RHOJR,Q0S4Q9,Reference,Bacteria,490,"Dehydrogenase involved in the degradation of steroids. Catalyzes the introduction of a double bond between the C4 and C5 atoms of 3-keto-(5alpha)-steroids. Catalyzes the conversion of 5alpha- androst-1-ene-3,17-dione to androsta-1,4-diene-3,17-dione, and probably the conversion of 5alpha-androstan-3,17-dione to androst-4-ene-3,17- dione.","Dehydrogenase involved in the degradation of steroids. Catalyzes the introduction of a double bond between the C4 and C5 atoms of 3-keto-(5alpha)-steroids. Catalyzes the conversion of 5alpha- androst-1-ene-3,17-dione to androsta-1,4-diene-3,17-dione, and probably the conversion of 5alpha-androstan-3,17-dione to androst-4-ene-3,17- dione.",,,,,,,GO:0000166; GO:0033765,GO:0016627,GO:0047077,GO:0016627,GO:0016491; GO:0050660,GO:0016491; GO:0050660,0.5445,0.2311,0.5445,0.6852,0.6852,5,0.5381,0.1719,no
FRBF_STRR3,Q0ZQ43,ESM2Text,Bacteria,286,"Acetyltransferase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the N-acetylation of CMP-5'- (N-hydroxy-3-aminopropyl)phosphonate (CMP-5'-H3APn), leading to the formation of CMP-5'-(N-acetyl-N-hydroxy-3-aminopropyl)phosphonate (CMP- 5'-FR-900098). In vitro, can also catalyze the acetylation of CMP-5'-3-aminopropylphosphonate (CMP-5'- 3APn), leading to the formation of CMP-5'-N-acetyl-3- aminopropylphosphonate (CMP-5'-Ac3APn), which is a dead-end in the FR- 900098 biosynthetic pathway rather than a true intermediate. Can use the alternative CoA substrates propionyl-CoA, malonyl-CoA and acetoacetyl-CoA, with much lower efficiency.","Resistance to antibiotics containing the 2-deoxy-streptamine ring including gentamicin, kanamycin, tobramycin, neomycin and apramycin.",Maybe,Vague,Maybe,No,No,not-Yes,GO:0008080,,,,,,,,,,,0,,0.3224,no
FRBF_STRR3,Q0ZQ43,Prot2Text,Bacteria,286,"Acetyltransferase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the N-acetylation of CMP-5'- (N-hydroxy-3-aminopropyl)phosphonate (CMP-5'-H3APn), leading to the formation of CMP-5'-(N-acetyl-N-hydroxy-3-aminopropyl)phosphonate (CMP- 5'-FR-900098). In vitro, can also catalyze the acetylation of CMP-5'-3-aminopropylphosphonate (CMP-5'- 3APn), leading to the formation of CMP-5'-N-acetyl-3- aminopropylphosphonate (CMP-5'-Ac3APn), which is a dead-end in the FR- 900098 biosynthetic pathway rather than a true intermediate. Can use the alternative CoA substrates propionyl-CoA, malonyl-CoA and acetoacetyl-CoA, with much lower efficiency.",May contribute to antibiotic resistance.,Vague,Vague,Vague,Vague,No,not-Yes,GO:0008080,,,,,,,,,,,0,,0.3224,no
FRBF_STRR3,Q0ZQ43,ProtT3,Bacteria,286,"Acetyltransferase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the N-acetylation of CMP-5'- (N-hydroxy-3-aminopropyl)phosphonate (CMP-5'-H3APn), leading to the formation of CMP-5'-(N-acetyl-N-hydroxy-3-aminopropyl)phosphonate (CMP- 5'-FR-900098). In vitro, can also catalyze the acetylation of CMP-5'-3-aminopropylphosphonate (CMP-5'- 3APn), leading to the formation of CMP-5'-N-acetyl-3- aminopropylphosphonate (CMP-5'-Ac3APn), which is a dead-end in the FR- 900098 biosynthetic pathway rather than a true intermediate. Can use the alternative CoA substrates propionyl-CoA, malonyl-CoA and acetoacetyl-CoA, with much lower efficiency.",Belongs to the antibiotic N-acetyltransferase family,Maybe,Vague,Maybe,Vague,Vague,not-Yes,GO:0008080,GO:0008080,GO:0016407,GO:0008080,GO:0008080,GO:0008080,1.0,0.7867,1.0,1.0,1.0,5,0.9573,0.3224,no
FRBF_STRR3,Q0ZQ43,ProtTale,Bacteria,286,"Acetyltransferase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the N-acetylation of CMP-5'- (N-hydroxy-3-aminopropyl)phosphonate (CMP-5'-H3APn), leading to the formation of CMP-5'-(N-acetyl-N-hydroxy-3-aminopropyl)phosphonate (CMP- 5'-FR-900098). In vitro, can also catalyze the acetylation of CMP-5'-3-aminopropylphosphonate (CMP-5'- 3APn), leading to the formation of CMP-5'-N-acetyl-3- aminopropylphosphonate (CMP-5'-Ac3APn), which is a dead-end in the FR- 900098 biosynthetic pathway rather than a true intermediate. Can use the alternative CoA substrates propionyl-CoA, malonyl-CoA and acetoacetyl-CoA, with much lower efficiency.","Catalyzes the conversion of mevalonate 5-phosphate (MVP) to isopentenyl diphosphate (IPP), the first step in isoprenoid biosynthesis.",No,No,No,No,No,not-Yes,GO:0008080,GO:0004163,GO:0004163,GO:0004163,GO:0004418,GO:0016301,0.1572,0.1572,0.1572,0.3157,0.3157,5,0.2206,0.3224,no
FRBF_STRR3,Q0ZQ43,Protein2Text,Bacteria,286,"Acetyltransferase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the N-acetylation of CMP-5'- (N-hydroxy-3-aminopropyl)phosphonate (CMP-5'-H3APn), leading to the formation of CMP-5'-(N-acetyl-N-hydroxy-3-aminopropyl)phosphonate (CMP- 5'-FR-900098). In vitro, can also catalyze the acetylation of CMP-5'-3-aminopropylphosphonate (CMP-5'- 3APn), leading to the formation of CMP-5'-N-acetyl-3- aminopropylphosphonate (CMP-5'-Ac3APn), which is a dead-end in the FR- 900098 biosynthetic pathway rather than a true intermediate. Can use the alternative CoA substrates propionyl-CoA, malonyl-CoA and acetoacetyl-CoA, with much lower efficiency.","The molecular function of this protein is catalyzing the transfer of a group, which is part of its role in the biosynthesis of cutin, a structural component of plant cuticles. Specifically, it is involved in the elongation of cutin monomers by adding a hydroxy fatty acid chain to the terminal carboxyl group of cutin monomers, which is a crucial step in the biosynthesis of cutin.",No,No,No,No,No,not-Yes,GO:0008080,GO:0016747,GO:0016746,GO:0016747,GO:0016746,GO:0016746,0.6795,0.5794,0.6795,0.5794,0.5794,5,0.6194,0.3224,no
FRBF_STRR3,Q0ZQ43,Reference,Bacteria,286,"Acetyltransferase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the N-acetylation of CMP-5'- (N-hydroxy-3-aminopropyl)phosphonate (CMP-5'-H3APn), leading to the formation of CMP-5'-(N-acetyl-N-hydroxy-3-aminopropyl)phosphonate (CMP- 5'-FR-900098). In vitro, can also catalyze the acetylation of CMP-5'-3-aminopropylphosphonate (CMP-5'- 3APn), leading to the formation of CMP-5'-N-acetyl-3- aminopropylphosphonate (CMP-5'-Ac3APn), which is a dead-end in the FR- 900098 biosynthetic pathway rather than a true intermediate. Can use the alternative CoA substrates propionyl-CoA, malonyl-CoA and acetoacetyl-CoA, with much lower efficiency.","Acetyltransferase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the N-acetylation of CMP-5'- (N-hydroxy-3-aminopropyl)phosphonate (CMP-5'-H3APn), leading to the formation of CMP-5'-(N-acetyl-N-hydroxy-3-aminopropyl)phosphonate (CMP- 5'-FR-900098). In vitro, can also catalyze the acetylation of CMP-5'-3-aminopropylphosphonate (CMP-5'- 3APn), leading to the formation of CMP-5'-N-acetyl-3- aminopropylphosphonate (CMP-5'-Ac3APn), which is a dead-end in the FR- 900098 biosynthetic pathway rather than a true intermediate. Can use the alternative CoA substrates propionyl-CoA, malonyl-CoA and acetoacetyl-CoA, with much lower efficiency.",,,,,,,GO:0008080,GO:0008080,GO:0008080,GO:0016407,GO:0016407; GO:0016746,GO:0016407; GO:0016746,1.0,1.0,0.7867,0.7176,0.7176,5,0.8444,0.3224,no
ZDHC9_ORYSJ,Q10L01,ESM2Text,Eukaryota,382,Palmitoyltransferase involved in the positive regulation of salt and oxidative stress tolerance. Palmitoyltoylates the salt tolerance receptor-like kinase STRK1.,Palmitoyl acyltransferase.,Yes,Yes,Yes,Vague,Maybe,Yes,GO:0019706,GO:0016409,GO:0016409,GO:0019706,GO:0019706,GO:0016409,0.6936,0.6936,1.0,1.0,0.6936,5,0.8162,0.5992,yes
ZDHC9_ORYSJ,Q10L01,Prot2Text,Eukaryota,382,Palmitoyltransferase involved in the positive regulation of salt and oxidative stress tolerance. Palmitoyltoylates the salt tolerance receptor-like kinase STRK1.,Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0019706,GO:0016409,GO:0016409,GO:0016409,GO:0016409,GO:0016409,0.6936,0.6936,0.6936,0.6936,0.6936,5,0.6936,0.5992,yes
ZDHC9_ORYSJ,Q10L01,ProtT3,Eukaryota,382,Palmitoyltransferase involved in the positive regulation of salt and oxidative stress tolerance. Palmitoyltoylates the salt tolerance receptor-like kinase STRK1.,Palmitoyl acyltransferase. Endoplasmic reticulum membrane; Multi-pass membrane protein. Belongs to the DHHC palmitoyltransferase family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0019706,GO:0016409,GO:0016409,GO:0016409,GO:0016409,GO:0016409,0.6936,0.6936,0.6936,0.6936,0.6936,5,0.6936,0.5992,yes
ZDHC9_ORYSJ,Q10L01,ProtTale,Eukaryota,382,Palmitoyltransferase involved in the positive regulation of salt and oxidative stress tolerance. Palmitoyltoylates the salt tolerance receptor-like kinase STRK1.,Palmitoyltransferase that targets several endosomal SNAREs. Palmitoylates the SNAREs at cysteine residues close to the cytoplasmic end of their transmembrane domain. May have a role in the cellular quality control of transmembrane domain-containing proteins.,Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0019706,GO:0016409,GO:0016409,GO:0016409,GO:0016409,GO:0016409,0.6936,0.6936,0.6936,0.6936,0.6936,5,0.6936,0.5992,yes
ZDHC9_ORYSJ,Q10L01,Protein2Text,Eukaryota,382,Palmitoyltransferase involved in the positive regulation of salt and oxidative stress tolerance. Palmitoyltoylates the salt tolerance receptor-like kinase STRK1.,This protein is involved in the molecular function of thioesterase activity.,No,No,No,No,Vague,not-Yes,GO:0019706,GO:0016790,GO:0016790,GO:0016790,GO:0016790,GO:0016790,0.1895,0.1895,0.1895,0.1895,0.1895,5,0.1895,0.5992,yes
ZDHC9_ORYSJ,Q10L01,Reference,Eukaryota,382,Palmitoyltransferase involved in the positive regulation of salt and oxidative stress tolerance. Palmitoyltoylates the salt tolerance receptor-like kinase STRK1.,Palmitoyltransferase involved in the positive regulation of salt and oxidative stress tolerance. Palmitoyltoylates the salt tolerance receptor-like kinase STRK1.,,,,,,,GO:0019706,GO:0019706,GO:0019706,GO:0016409,GO:0016746; GO:0019706,GO:0016409,1.0,1.0,0.6936,0.8383,0.6936,5,0.8451,0.5992,yes
STS1_ORYSJ,Q10SS2,ESM2Text,Eukaryota,661,"Involved in anther lipids biosynthesis and is required for tapetum degradation and pollen wall formation. Required for the formation of Ubisch bodies and microspores. Possesses lipase activity in vitro toward two synthetic substrates, p-nitrophenyl acetate (pNPA) and p- nitrophenyl butyrate (pNPB).","Phospholipase that hydrolyzes phosphatidic acid (PA) to produce phosphatidic acid (PA) and 1,2-diacyl phosphatidic acid (1,2-diacyl-sn-glycerol). PA is the principal hydrolysis form of phosphatidylcholine in membranes. Required for maintenance of the outer leaflet of phosphatidylethanolamine (PE) and in the formation of the outer leaflet of phosphatidylinositol (PI). May be involved in the maintenance of the architecture of phosphatidylinositol monophosphate (PIP).",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0052689,GO:0016787,GO:0008970,,GO:0004620,,0.6897,0.6212,,0.5296,,3,0.6135,0.4943,no
STS1_ORYSJ,Q10SS2,Prot2Text,Eukaryota,661,"Involved in anther lipids biosynthesis and is required for tapetum degradation and pollen wall formation. Required for the formation of Ubisch bodies and microspores. Possesses lipase activity in vitro toward two synthetic substrates, p-nitrophenyl acetate (pNPA) and p- nitrophenyl butyrate (pNPB).","Triacylglycerol (TAG) lipase that hydrolyzes TAG to generate phosphatidic acid (PA). Required for pollen development, especially during the transition from the vegetative stage to the reproductive stage. Contributes to the accumulation of PA during germination and to the breakdown of storage lipid in the pollen tube (Probable).",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0052689,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,0.7707,0.7707,0.7707,0.7707,0.7707,5,0.7707,0.4943,no
STS1_ORYSJ,Q10SS2,ProtT3,Eukaryota,661,"Involved in anther lipids biosynthesis and is required for tapetum degradation and pollen wall formation. Required for the formation of Ubisch bodies and microspores. Possesses lipase activity in vitro toward two synthetic substrates, p-nitrophenyl acetate (pNPA) and p- nitrophenyl butyrate (pNPB).",Membrane; Multi-pass membrane protein. Belongs to the TMCO4 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0052689,,,,,,,,,,,0,,0.4943,no
STS1_ORYSJ,Q10SS2,ProtTale,Eukaryota,661,"Involved in anther lipids biosynthesis and is required for tapetum degradation and pollen wall formation. Required for the formation of Ubisch bodies and microspores. Possesses lipase activity in vitro toward two synthetic substrates, p-nitrophenyl acetate (pNPA) and p- nitrophenyl butyrate (pNPB).","Involved in the regulation of membrane lipid metabolism. Required for the synthesis of phosphatidylinositol phosphate (PI(3)P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2), but not for the synthesis of phosphatidylinositol 4-phosphate (PI(4)P) or phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2).",Vague,Vague,Maybe,Maybe,No,not-Yes,GO:0052689,,,GO:0016303,,,,,0.1785,,,1,0.1785,0.4943,no
STS1_ORYSJ,Q10SS2,Protein2Text,Eukaryota,661,"Involved in anther lipids biosynthesis and is required for tapetum degradation and pollen wall formation. Required for the formation of Ubisch bodies and microspores. Possesses lipase activity in vitro toward two synthetic substrates, p-nitrophenyl acetate (pNPA) and p- nitrophenyl butyrate (pNPB).","This protein is involved in molecular function related to electron transport chains, specifically as a component of the mitochondrial electron transport chain.",No,No,No,No,No,not-Yes,GO:0052689,,GO:0009055,,,GO:0009055,,0.2343,,,0.2343,2,0.2343,0.4943,no
STS1_ORYSJ,Q10SS2,Reference,Eukaryota,661,"Involved in anther lipids biosynthesis and is required for tapetum degradation and pollen wall formation. Required for the formation of Ubisch bodies and microspores. Possesses lipase activity in vitro toward two synthetic substrates, p-nitrophenyl acetate (pNPA) and p- nitrophenyl butyrate (pNPB).","Involved in anther lipids biosynthesis and is required for tapetum degradation and pollen wall formation. Required for the formation of Ubisch bodies and microspores. Possesses lipase activity in vitro toward two synthetic substrates, p-nitrophenyl acetate (pNPA) and p- nitrophenyl butyrate (pNPB).",,,,,,,GO:0052689,GO:0016298,GO:0016298,GO:0016298,GO:0016788; GO:0004806,GO:0004806,0.7025,0.7025,0.7025,0.818,0.7707,5,0.7392,0.4943,no
C76B9_PETHY,Q14T82,ESM2Text,Eukaryota,573,"Cytochrome P450 hydroxylase catalyzing the conversion of decanoate (capric acid) and dodecanoate (lauric acid) to their corresponding omega-hydroxy metabolites, 10-hydroxydecanoate and 12- hydroxydodecanoate, respectively; these hydroxylated components affect plant growth, including reducing root elongation.","Cytochrome P450 involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family. Catalyzes the hydroxylation at C-12 of zerumbone to form 11-hydroxyzeatin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0120250; GO:0020037; GO:0005506; GO:0120319,GO:0004497; GO:0020037,GO:0004497; GO:0020037,GO:0004497,GO:0004497,GO:0004497,0.6933,0.6933,0.4413,0.4413,0.4413,5,0.5421,0.3382,no
C76B9_PETHY,Q14T82,Prot2Text,Eukaryota,573,"Cytochrome P450 hydroxylase catalyzing the conversion of decanoate (capric acid) and dodecanoate (lauric acid) to their corresponding omega-hydroxy metabolites, 10-hydroxydecanoate and 12- hydroxydodecanoate, respectively; these hydroxylated components affect plant growth, including reducing root elongation.","Cytochrome P450 involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family. Catalyzes the conversion of deoxypodophyllotoxin to pluviatolide.",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0120250; GO:0020037; GO:0005506; GO:0120319,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.4413,0.4413,0.4413,0.4413,0.4413,5,0.4413,0.3382,no
C76B9_PETHY,Q14T82,ProtT3,Eukaryota,573,"Cytochrome P450 hydroxylase catalyzing the conversion of decanoate (capric acid) and dodecanoate (lauric acid) to their corresponding omega-hydroxy metabolites, 10-hydroxydecanoate and 12- hydroxydodecanoate, respectively; these hydroxylated components affect plant growth, including reducing root elongation.",Membrane; Single-pass membrane protein. Belongs to the cytochrome P450 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0120250; GO:0020037; GO:0005506; GO:0120319,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,0.8474,0.8474,0.8474,0.8474,0.8474,5,0.8474,0.3382,no
C76B9_PETHY,Q14T82,ProtTale,Eukaryota,573,"Cytochrome P450 hydroxylase catalyzing the conversion of decanoate (capric acid) and dodecanoate (lauric acid) to their corresponding omega-hydroxy metabolites, 10-hydroxydecanoate and 12- hydroxydodecanoate, respectively; these hydroxylated components affect plant growth, including reducing root elongation.",Cytochrome P450 monooxygenase involved in the biosynthesis of indole-3-propionic acid (IPA) and indole-3-acetic acid (IAA) natural products. Catalyzes the conversion of tryptophan (Trp) to N-formylkynurenine (NFK).,Maybe,Maybe,Maybe,No,No,not-Yes,GO:0120250; GO:0020037; GO:0005506; GO:0120319,GO:0004497,GO:0004497; GO:0005506,GO:0004497; GO:0020037,GO:0004497,GO:0004497; GO:0005506; GO:0020037,0.4413,0.6933,0.6933,0.4413,0.8474,5,0.6233,0.3382,no
C76B9_PETHY,Q14T82,Protein2Text,Eukaryota,573,"Cytochrome P450 hydroxylase catalyzing the conversion of decanoate (capric acid) and dodecanoate (lauric acid) to their corresponding omega-hydroxy metabolites, 10-hydroxydecanoate and 12- hydroxydodecanoate, respectively; these hydroxylated components affect plant growth, including reducing root elongation.","The molecular function of this protein is a cytochrome P450 monooxygenase, specifically involved in the metabolism of xenobiotics and the synthesis of phytohormones.",Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0120250; GO:0020037; GO:0005506; GO:0120319,GO:0004497,GO:0005506; GO:0016491,GO:0004497,GO:0004497,GO:0004497,0.4413,0.6361,0.4413,0.4413,0.4413,5,0.4803,0.3382,no
C76B9_PETHY,Q14T82,Reference,Eukaryota,573,"Cytochrome P450 hydroxylase catalyzing the conversion of decanoate (capric acid) and dodecanoate (lauric acid) to their corresponding omega-hydroxy metabolites, 10-hydroxydecanoate and 12- hydroxydodecanoate, respectively; these hydroxylated components affect plant growth, including reducing root elongation.","Cytochrome P450 hydroxylase catalyzing the conversion of decanoate (capric acid) and dodecanoate (lauric acid) to their corresponding omega-hydroxy metabolites, 10-hydroxydecanoate and 12- hydroxydodecanoate, respectively; these hydroxylated components affect plant growth, including reducing root elongation.",,,,,,,GO:0120250; GO:0020037; GO:0005506; GO:0120319,GO:0004497,GO:0004497; GO:0020037; GO:0005506,GO:0004497; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,0.4413,0.8474,0.6933,0.8474,0.8474,5,0.7354,0.3382,no
GBP4_DANRE,Q1MT80,ESM2Text,Eukaryota,618,"GTPase that plays important roles in innate immunity against S.typhimurium pathogens by mediating formation of an inflammasome in neutrophils. Neutrophils are recruited to the infection site, and then mediate bacterial clearance through the Gbp4 inflammasome-dependent biosynthesis of prostaglandin D2.",GTPase tethering membranes through formation of trans-homooligomers and mediating homotypic fusion of endosome-derived vesicles with the cell surface. Functions in cell growth and differentiation. Has GTPase activity.,Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0005525; GO:0003924,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924,GO:0003924,GO:0003924,1.0,1.0,0.6817,0.6817,0.6817,5,0.809,0.5912,yes
GBP4_DANRE,Q1MT80,Prot2Text,Eukaryota,618,"GTPase that plays important roles in innate immunity against S.typhimurium pathogens by mediating formation of an inflammasome in neutrophils. Neutrophils are recruited to the infection site, and then mediate bacterial clearance through the Gbp4 inflammasome-dependent biosynthesis of prostaglandin D2.",Exhibits antiviral activity against influenza virus.,Vague,Vague,Vague,No,No,not-Yes,GO:0005525; GO:0003924,,,,,,,,,,,0,,0.5912,yes
GBP4_DANRE,Q1MT80,ProtT3,Eukaryota,618,"GTPase that plays important roles in innate immunity against S.typhimurium pathogens by mediating formation of an inflammasome in neutrophils. Neutrophils are recruited to the infection site, and then mediate bacterial clearance through the Gbp4 inflammasome-dependent biosynthesis of prostaglandin D2.",Interferon (IFN)-induced GTP-binding protein that plays important roles in innate immune response against a variety of pathogens,Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0005525; GO:0003924,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0005525; GO:0003924,GO:0005525,1.0,1.0,1.0,1.0,0.6817,5,0.9363,0.5912,yes
GBP4_DANRE,Q1MT80,ProtTale,Eukaryota,618,"GTPase that plays important roles in innate immunity against S.typhimurium pathogens by mediating formation of an inflammasome in neutrophils. Neutrophils are recruited to the infection site, and then mediate bacterial clearance through the Gbp4 inflammasome-dependent biosynthesis of prostaglandin D2.",Probable GTPase activating protein (GAP) that inhibits RAB7.,No,No,No,No,Maybe,not-Yes,GO:0005525; GO:0003924,GO:0005096,GO:0005096,GO:0005096,GO:0005096,GO:0005096,0.0612,0.0612,0.0612,0.0612,0.0612,5,0.0612,0.5912,yes
GBP4_DANRE,Q1MT80,Protein2Text,Eukaryota,618,"GTPase that plays important roles in innate immunity against S.typhimurium pathogens by mediating formation of an inflammasome in neutrophils. Neutrophils are recruited to the infection site, and then mediate bacterial clearance through the Gbp4 inflammasome-dependent biosynthesis of prostaglandin D2.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its name, it is likely involved in the regulation of the cytoskeleton, specifically in the context of cell motility and inflammation. This protein is a member of the guanine nucleotide-binding protein family, which typically regulates various cellular processes by binding to and hydrolyzing guanine nucleotides. 

Therefore, the molecular function of this protein is likely to be a GTPase activity, which is a critical component of signaling pathways that regulate various cellular processes.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0005525; GO:0003924,GO:0003924,GO:0003924,,GO:0003924,GO:0003924,0.6817,0.6817,,0.6817,0.6817,4,0.6817,0.5912,yes
GBP4_DANRE,Q1MT80,Reference,Eukaryota,618,"GTPase that plays important roles in innate immunity against S.typhimurium pathogens by mediating formation of an inflammasome in neutrophils. Neutrophils are recruited to the infection site, and then mediate bacterial clearance through the Gbp4 inflammasome-dependent biosynthesis of prostaglandin D2.","GTPase that plays important roles in innate immunity against S.typhimurium pathogens by mediating formation of an inflammasome in neutrophils. Neutrophils are recruited to the infection site, and then mediate bacterial clearance through the Gbp4 inflammasome-dependent biosynthesis of prostaglandin D2.",,,,,,,GO:0005525; GO:0003924,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0005525; GO:0003924,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5912,yes
DKDRH_SPHSS,Q1NEI7,ESM2Text,Bacteria,285,"Hydrolase that catalyzes the hydrolysis of 2,4-didehydro-3- deoxy-L-rhamnonate to pyruvate and L-lactate. Can also hydrolyze L-2,4-diketo-3-deoxylyxonate and L-2,4-diketo-3-deoxymannonate. In vitro can also use acylpyruvates such as acetylpyruvate and trimethylacetopyruvate. Catalyzes the fifth (last) step in an alternative pathway for rhamnose utilization that does not involve phosphorylated intermediates.",May have hydrolase activity.,Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0016787; GO:0016853; GO:0046872,,,,,,,,,,,0,,0.4432,no
DKDRH_SPHSS,Q1NEI7,Prot2Text,Bacteria,285,"Hydrolase that catalyzes the hydrolysis of 2,4-didehydro-3- deoxy-L-rhamnonate to pyruvate and L-lactate. Can also hydrolyze L-2,4-diketo-3-deoxylyxonate and L-2,4-diketo-3-deoxymannonate. In vitro can also use acylpyruvates such as acetylpyruvate and trimethylacetopyruvate. Catalyzes the fifth (last) step in an alternative pathway for rhamnose utilization that does not involve phosphorylated intermediates.",May have hydrolase activity.,Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0016787; GO:0016853; GO:0046872,,,,GO:0016787,,,,,0.687,,1,0.687,0.4432,no
DKDRH_SPHSS,Q1NEI7,ProtT3,Bacteria,285,"Hydrolase that catalyzes the hydrolysis of 2,4-didehydro-3- deoxy-L-rhamnonate to pyruvate and L-lactate. Can also hydrolyze L-2,4-diketo-3-deoxylyxonate and L-2,4-diketo-3-deoxymannonate. In vitro can also use acylpyruvates such as acetylpyruvate and trimethylacetopyruvate. Catalyzes the fifth (last) step in an alternative pathway for rhamnose utilization that does not involve phosphorylated intermediates.",Belongs to the FAH family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016787; GO:0016853; GO:0046872,GO:0004334,GO:0004334,GO:0004334,GO:0004334,GO:0004334,0.412,0.412,0.412,0.412,0.412,5,0.412,0.4432,no
DKDRH_SPHSS,Q1NEI7,ProtTale,Bacteria,285,"Hydrolase that catalyzes the hydrolysis of 2,4-didehydro-3- deoxy-L-rhamnonate to pyruvate and L-lactate. Can also hydrolyze L-2,4-diketo-3-deoxylyxonate and L-2,4-diketo-3-deoxymannonate. In vitro can also use acylpyruvates such as acetylpyruvate and trimethylacetopyruvate. Catalyzes the fifth (last) step in an alternative pathway for rhamnose utilization that does not involve phosphorylated intermediates.","Tetrahydrofolate (THF)-dependent decarboxylation of L-glutamate to L-2,4-diaminobutyrate (DABA), driven by a proton motive force. Catalyzes the decarboxylation of L-glutamate 6-phosphate to L-2,4-diaminobutyrate 6-phosphate.",No,No,No,No,No,not-Yes,GO:0016787; GO:0016853; GO:0046872,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.3314,0.3314,0.3314,0.3314,0.3314,5,0.3314,0.4432,no
DKDRH_SPHSS,Q1NEI7,Protein2Text,Bacteria,285,"Hydrolase that catalyzes the hydrolysis of 2,4-didehydro-3- deoxy-L-rhamnonate to pyruvate and L-lactate. Can also hydrolyze L-2,4-diketo-3-deoxylyxonate and L-2,4-diketo-3-deoxymannonate. In vitro can also use acylpyruvates such as acetylpyruvate and trimethylacetopyruvate. Catalyzes the fifth (last) step in an alternative pathway for rhamnose utilization that does not involve phosphorylated intermediates.",The molecular function of this protein is a beta-lactamase.,No,No,No,No,No,not-Yes,GO:0016787; GO:0016853; GO:0046872,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,0.412,0.412,0.412,0.412,0.412,5,0.412,0.4432,no
DKDRH_SPHSS,Q1NEI7,Reference,Bacteria,285,"Hydrolase that catalyzes the hydrolysis of 2,4-didehydro-3- deoxy-L-rhamnonate to pyruvate and L-lactate. Can also hydrolyze L-2,4-diketo-3-deoxylyxonate and L-2,4-diketo-3-deoxymannonate. In vitro can also use acylpyruvates such as acetylpyruvate and trimethylacetopyruvate. Catalyzes the fifth (last) step in an alternative pathway for rhamnose utilization that does not involve phosphorylated intermediates.","Hydrolase that catalyzes the hydrolysis of 2,4-didehydro-3- deoxy-L-rhamnonate to pyruvate and L-lactate. Can also hydrolyze L-2,4-diketo-3-deoxylyxonate and L-2,4-diketo-3-deoxymannonate. In vitro can also use acylpyruvates such as acetylpyruvate and trimethylacetopyruvate. Catalyzes the fifth (last) step in an alternative pathway for rhamnose utilization that does not involve phosphorylated intermediates.",,,,,,,GO:0016787; GO:0016853; GO:0046872,GO:0016787,,GO:0016787,GO:0016787,GO:0016787,0.687,,0.687,0.687,0.687,4,0.687,0.4432,no
HAO_KUEST,Q1PX48,ESM2Text,Bacteria,536,"Catalyzes the oxidation of hydroxylamine to nitric oxide with cytochrome c acting as an electron acceptor. Does not oxidize hydroxylamine to nitrite. Also able to catalyze the four-electron oxidation of hydrazine to N(2) in vitro with reduced efficiency; however, this reaction is probably not physiological.","Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process. Can also reduce sulfate to sulfide, but the activity is comparatively low.",No,No,No,No,Maybe,not-Yes,GO:0020037; GO:0033740; GO:0042802; GO:0046872,GO:0016491,GO:0008942,GO:0008942,GO:0016491,GO:0008942,0.3578,0.246,0.246,0.3578,0.246,5,0.2907,0.4753,no
HAO_KUEST,Q1PX48,Prot2Text,Bacteria,536,"Catalyzes the oxidation of hydroxylamine to nitric oxide with cytochrome c acting as an electron acceptor. Does not oxidize hydroxylamine to nitrite. Also able to catalyze the four-electron oxidation of hydrazine to N(2) in vitro with reduced efficiency; however, this reaction is probably not physiological.","Electron transfer subunit of the periplasmic nitrate reductase complex NapAB. Transfers electrons to NapA subunit, thus allowing electron flow between membrane and periplasm. Essential for periplasmic nitrate reduction with nitrate as the terminal electron acceptor.",No,No,No,No,No,not-Yes,GO:0020037; GO:0033740; GO:0042802; GO:0046872,GO:0009055,GO:0009055,GO:0009055,GO:0009055,GO:0009055,0.2478,0.2478,0.2478,0.2478,0.2478,5,0.2478,0.4753,no
HAO_KUEST,Q1PX48,ProtT3,Bacteria,536,"Catalyzes the oxidation of hydroxylamine to nitric oxide with cytochrome c acting as an electron acceptor. Does not oxidize hydroxylamine to nitrite. Also able to catalyze the four-electron oxidation of hydrazine to N(2) in vitro with reduced efficiency; however, this reaction is probably not physiological.",Catalyzes the reduction of nitrite to ammonia. Periplasm. Belongs to the cytochrome c-552 family,No,No,No,No,Maybe,not-Yes,GO:0020037; GO:0033740; GO:0042802; GO:0046872,GO:0016491,GO:0042279,GO:0016661,GO:0050421,GO:0042279,0.3578,0.3242,0.3863,0.3242,0.3242,5,0.3433,0.4753,no
HAO_KUEST,Q1PX48,ProtTale,Bacteria,536,"Catalyzes the oxidation of hydroxylamine to nitric oxide with cytochrome c acting as an electron acceptor. Does not oxidize hydroxylamine to nitrite. Also able to catalyze the four-electron oxidation of hydrazine to N(2) in vitro with reduced efficiency; however, this reaction is probably not physiological.","Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process.",No,No,No,No,Maybe,not-Yes,GO:0020037; GO:0033740; GO:0042802; GO:0046872,GO:0008942,GO:0008942,GO:0008942,GO:0008942,GO:0008942,0.246,0.246,0.246,0.246,0.246,5,0.246,0.4753,no
HAO_KUEST,Q1PX48,Protein2Text,Bacteria,536,"Catalyzes the oxidation of hydroxylamine to nitric oxide with cytochrome c acting as an electron acceptor. Does not oxidize hydroxylamine to nitrite. Also able to catalyze the four-electron oxidation of hydrazine to N(2) in vitro with reduced efficiency; however, this reaction is probably not physiological.","The molecular function of this protein is not specified in the provided text. However, it can be inferred that it is involved in the conversion of sulfur compounds, as it is associated with the reduction of sulfur-containing compounds in the environment.",No,No,No,Vague,No,not-Yes,GO:0020037; GO:0033740; GO:0042802; GO:0046872,,,,,,,,,,,0,,0.4753,no
HAO_KUEST,Q1PX48,Reference,Bacteria,536,"Catalyzes the oxidation of hydroxylamine to nitric oxide with cytochrome c acting as an electron acceptor. Does not oxidize hydroxylamine to nitrite. Also able to catalyze the four-electron oxidation of hydrazine to N(2) in vitro with reduced efficiency; however, this reaction is probably not physiological.","Catalyzes the oxidation of hydroxylamine to nitric oxide with cytochrome c acting as an electron acceptor. Does not oxidize hydroxylamine to nitrite. Also able to catalyze the four-electron oxidation of hydrazine to N(2) in vitro with reduced efficiency; however, this reaction is probably not physiological.",,,,,,,GO:0020037; GO:0033740; GO:0042802; GO:0046872,GO:0016491,GO:0018492,GO:0016641,GO:0016491,GO:0016491,0.3578,0.0,0.2388,0.3578,0.3578,5,0.2624,0.4753,no
DDHC_CHRI1,Q1QYW1,ESM2Text,Bacteria,694,"Involved in degradation of glycine betaine. Catalyzes the demethylation of both N,N-dimethylglycine (DMG) and sarcosine, releasing formaldehyde and forming glycine as the final product. Does not show activity toward trimethylamine (TMA), histamine, glycine betaine (GB) or choline. The C-N bond in DMG is probably oxidized by removal of a hydride equivalent to form a labile imine intermediate, which is then spontaneously hydrolyzed in the presence of water, producing sarcosine and formaldehyde. The two protons subtracted from DMG are transferred to the non-covalently bound FAD, resulting in the reduced form of FAD, which is subsequently reoxidized by coupling with reduction of the enzyme-bound NAD(P)(+). Regeneration of NAD(P)(+) is achieved by electron transfer to the [4Fe-4S] cluster in the probable membrane-anchored ferredoxin csal_0991.","Reduces the double bond of an array of alpha,beta-unsaturated aldehydes and ketones. It also reduces the nitro group of nitroester and nitroaromatic compounds. It could have a role in detoxification processes.",No,No,No,No,No,not-Yes,GO:0010181; GO:0016491,GO:0016491,GO:0016491,GO:0032440,GO:0016491,GO:0016491,0.7038,0.7038,0.4243,0.7038,0.7038,5,0.6479,0.1435,no
DDHC_CHRI1,Q1QYW1,Prot2Text,Bacteria,694,"Involved in degradation of glycine betaine. Catalyzes the demethylation of both N,N-dimethylglycine (DMG) and sarcosine, releasing formaldehyde and forming glycine as the final product. Does not show activity toward trimethylamine (TMA), histamine, glycine betaine (GB) or choline. The C-N bond in DMG is probably oxidized by removal of a hydride equivalent to form a labile imine intermediate, which is then spontaneously hydrolyzed in the presence of water, producing sarcosine and formaldehyde. The two protons subtracted from DMG are transferred to the non-covalently bound FAD, resulting in the reduced form of FAD, which is subsequently reoxidized by coupling with reduction of the enzyme-bound NAD(P)(+). Regeneration of NAD(P)(+) is achieved by electron transfer to the [4Fe-4S] cluster in the probable membrane-anchored ferredoxin csal_0991.",Putative oxophytodienoate reductase that may be involved in the biosynthesis or metabolism of oxylipin signaling molecules.,No,No,No,No,No,not-Yes,GO:0010181; GO:0016491,GO:0016491,,GO:0016491,GO:0016491,GO:0045551,0.7038,,0.7038,0.7038,0.4243,4,0.6339,0.1435,no
DDHC_CHRI1,Q1QYW1,ProtT3,Bacteria,694,"Involved in degradation of glycine betaine. Catalyzes the demethylation of both N,N-dimethylglycine (DMG) and sarcosine, releasing formaldehyde and forming glycine as the final product. Does not show activity toward trimethylamine (TMA), histamine, glycine betaine (GB) or choline. The C-N bond in DMG is probably oxidized by removal of a hydride equivalent to form a labile imine intermediate, which is then spontaneously hydrolyzed in the presence of water, producing sarcosine and formaldehyde. The two protons subtracted from DMG are transferred to the non-covalently bound FAD, resulting in the reduced form of FAD, which is subsequently reoxidized by coupling with reduction of the enzyme-bound NAD(P)(+). Regeneration of NAD(P)(+) is achieved by electron transfer to the [4Fe-4S] cluster in the probable membrane-anchored ferredoxin csal_0991.",In the N-terminal section; belongs to the NADH:flavin oxidoreductase/NADH oxidase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0010181; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016651,GO:0016491,0.7038,0.7038,0.7038,0.574,0.7038,5,0.6778,0.1435,no
DDHC_CHRI1,Q1QYW1,ProtTale,Bacteria,694,"Involved in degradation of glycine betaine. Catalyzes the demethylation of both N,N-dimethylglycine (DMG) and sarcosine, releasing formaldehyde and forming glycine as the final product. Does not show activity toward trimethylamine (TMA), histamine, glycine betaine (GB) or choline. The C-N bond in DMG is probably oxidized by removal of a hydride equivalent to form a labile imine intermediate, which is then spontaneously hydrolyzed in the presence of water, producing sarcosine and formaldehyde. The two protons subtracted from DMG are transferred to the non-covalently bound FAD, resulting in the reduced form of FAD, which is subsequently reoxidized by coupling with reduction of the enzyme-bound NAD(P)(+). Regeneration of NAD(P)(+) is achieved by electron transfer to the [4Fe-4S] cluster in the probable membrane-anchored ferredoxin csal_0991.","Plays a key role in cholesterol degradation. Catalyzes the reduction of 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to mevalonate. Acts in the mevalonate pathway which generates precursors for the biosynthesis of isoprenoid compounds, cholesterol and bile acids.",No,No,No,No,No,not-Yes,GO:0010181; GO:0016491,GO:0004420,GO:0004420,GO:0004420,GO:0004420,GO:0004420,0.4243,0.4243,0.4243,0.4243,0.4243,5,0.4243,0.1435,no
DDHC_CHRI1,Q1QYW1,Protein2Text,Bacteria,694,"Involved in degradation of glycine betaine. Catalyzes the demethylation of both N,N-dimethylglycine (DMG) and sarcosine, releasing formaldehyde and forming glycine as the final product. Does not show activity toward trimethylamine (TMA), histamine, glycine betaine (GB) or choline. The C-N bond in DMG is probably oxidized by removal of a hydride equivalent to form a labile imine intermediate, which is then spontaneously hydrolyzed in the presence of water, producing sarcosine and formaldehyde. The two protons subtracted from DMG are transferred to the non-covalently bound FAD, resulting in the reduced form of FAD, which is subsequently reoxidized by coupling with reduction of the enzyme-bound NAD(P)(+). Regeneration of NAD(P)(+) is achieved by electron transfer to the [4Fe-4S] cluster in the probable membrane-anchored ferredoxin csal_0991.","This protein is a part of the family of enzymes known as oxidoreductases. Specifically, it is involved in the conversion of compounds by the transfer of electrons from one molecule to another, in this case, catalyzing the reduction of a substrate to a product.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0010181; GO:0016491,GO:0016491,GO:0016491,,GO:0016491,GO:0016491,0.7038,0.7038,,0.7038,0.7038,4,0.7038,0.1435,no
DDHC_CHRI1,Q1QYW1,Reference,Bacteria,694,"Involved in degradation of glycine betaine. Catalyzes the demethylation of both N,N-dimethylglycine (DMG) and sarcosine, releasing formaldehyde and forming glycine as the final product. Does not show activity toward trimethylamine (TMA), histamine, glycine betaine (GB) or choline. The C-N bond in DMG is probably oxidized by removal of a hydride equivalent to form a labile imine intermediate, which is then spontaneously hydrolyzed in the presence of water, producing sarcosine and formaldehyde. The two protons subtracted from DMG are transferred to the non-covalently bound FAD, resulting in the reduced form of FAD, which is subsequently reoxidized by coupling with reduction of the enzyme-bound NAD(P)(+). Regeneration of NAD(P)(+) is achieved by electron transfer to the [4Fe-4S] cluster in the probable membrane-anchored ferredoxin csal_0991.","Involved in degradation of glycine betaine. Catalyzes the demethylation of both N,N-dimethylglycine (DMG) and sarcosine, releasing formaldehyde and forming glycine as the final product. Does not show activity toward trimethylamine (TMA), histamine, glycine betaine (GB) or choline. The C-N bond in DMG is probably oxidized by removal of a hydride equivalent to form a labile imine intermediate, which is then spontaneously hydrolyzed in the presence of water, producing sarcosine and formaldehyde. The two protons subtracted from DMG are transferred to the non-covalently bound FAD, resulting in the reduced form of FAD, which is subsequently reoxidized by coupling with reduction of the enzyme-bound NAD(P)(+). Regeneration of NAD(P)(+) is achieved by electron transfer to the [4Fe-4S] cluster in the probable membrane-anchored ferredoxin csal_0991.",,,,,,,GO:0010181; GO:0016491,GO:0016491; GO:0071949,GO:0047297,GO:0016638; GO:0050660,GO:0016491; GO:0050660; GO:0050661,GO:0016491; GO:0050660; GO:0051536,0.8336,0.2599,0.7743,0.7852,0.7515,5,0.6809,0.1435,no
AVR2_DROME,Q24468,ESM2Text,Eukaryota,516,"Type II transmembrane receptor serine/threonine kinase involved in activin-like TGF-beta signaling and dpp/BMP-like signaling pathways. Forms a complex with type I transmembrane receptor serine/threonine kinases, and upon activation by signaling ligands induces the type I receptor to phosphorylate downstream receptor-regulated SMAD (R-SMAD) transcription factors, inducing their nuclear localization and resulting in regulation of ligand-responsive genes. Receptor for the activin-like TGF-beta ligands daw and Actbeta/activin when in complex with the type I receptor babo. Activation by daw requires babo isoform C. Receptor for the BMP-like ligand dpp when associated with the type I receptors tkv or sax. Activation by activin-like TGF-beta ligands, including daw and Actbeta/activin, results in phosphorylation of the R-SMAD Smox/SMAD2. Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad. Involved in dpp-signaling-dependent dorsoventral patterning of the epidermis during embryogenesis. Involved in axonal and dendritic pruning and neural remodeling of mushroom body gamma neurons during metamorphosis, probably through regulating expression of the ecdysteroid receptor EcR; functions redundantly with wit. Involved in dpp/BMP-like signaling during development of the embryonic gut tracheal system. Required for dpp/BMP-like signaling involved in imaginal disc development. Involved in differentiation of dorsal cluster and ellipsoid body adult-specific neurons prior to metamorphosis. Required in motoneurons for axon guidance or outgrowth of ISNb and SNa axons. Required in somatic cyst cells for regulation of germ cell proliferation in testis. Involved in adult wing development and wing- vein formation.","On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin A, activin B and inhibin A. Mediates induction of adipogenesis by GDF6.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0048185; GO:0017002; GO:0005524; GO:0046872,GO:0004674,GO:0004674; GO:0017002,GO:0017002; GO:0004674,GO:0004674,GO:0004675,0.3332,0.4923,0.4923,0.3332,0.4089,5,0.412,0.6522,yes
AVR2_DROME,Q24468,Prot2Text,Eukaryota,516,"Type II transmembrane receptor serine/threonine kinase involved in activin-like TGF-beta signaling and dpp/BMP-like signaling pathways. Forms a complex with type I transmembrane receptor serine/threonine kinases, and upon activation by signaling ligands induces the type I receptor to phosphorylate downstream receptor-regulated SMAD (R-SMAD) transcription factors, inducing their nuclear localization and resulting in regulation of ligand-responsive genes. Receptor for the activin-like TGF-beta ligands daw and Actbeta/activin when in complex with the type I receptor babo. Activation by daw requires babo isoform C. Receptor for the BMP-like ligand dpp when associated with the type I receptors tkv or sax. Activation by activin-like TGF-beta ligands, including daw and Actbeta/activin, results in phosphorylation of the R-SMAD Smox/SMAD2. Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad. Involved in dpp-signaling-dependent dorsoventral patterning of the epidermis during embryogenesis. Involved in axonal and dendritic pruning and neural remodeling of mushroom body gamma neurons during metamorphosis, probably through regulating expression of the ecdysteroid receptor EcR; functions redundantly with wit. Involved in dpp/BMP-like signaling during development of the embryonic gut tracheal system. Required for dpp/BMP-like signaling involved in imaginal disc development. Involved in differentiation of dorsal cluster and ellipsoid body adult-specific neurons prior to metamorphosis. Required in motoneurons for axon guidance or outgrowth of ISNb and SNa axons. Required in somatic cyst cells for regulation of germ cell proliferation in testis. Involved in adult wing development and wing- vein formation.","Transmembrane serine/threonine kinase activin type-1 receptor forming an activin receptor complex with activin receptor type-2 (ACVR2A or ACVR2B). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating a many physiological and pathological processes including neuronal differentiation, neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, type-2 receptors (ACVR2A and/or ACVR2B) act as a primary activin receptors whereas the type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor such as ACVR1B. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SM",Yes,Yes,Yes,Yes,Yes,Yes,GO:0048185; GO:0017002; GO:0005524; GO:0046872,GO:0004675,GO:0004674,GO:0004675,GO:0004674; GO:0004675,GO:0004675,0.4089,0.3332,0.4089,0.4702,0.4089,5,0.406,0.6522,yes
AVR2_DROME,Q24468,ProtT3,Eukaryota,516,"Type II transmembrane receptor serine/threonine kinase involved in activin-like TGF-beta signaling and dpp/BMP-like signaling pathways. Forms a complex with type I transmembrane receptor serine/threonine kinases, and upon activation by signaling ligands induces the type I receptor to phosphorylate downstream receptor-regulated SMAD (R-SMAD) transcription factors, inducing their nuclear localization and resulting in regulation of ligand-responsive genes. Receptor for the activin-like TGF-beta ligands daw and Actbeta/activin when in complex with the type I receptor babo. Activation by daw requires babo isoform C. Receptor for the BMP-like ligand dpp when associated with the type I receptors tkv or sax. Activation by activin-like TGF-beta ligands, including daw and Actbeta/activin, results in phosphorylation of the R-SMAD Smox/SMAD2. Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad. Involved in dpp-signaling-dependent dorsoventral patterning of the epidermis during embryogenesis. Involved in axonal and dendritic pruning and neural remodeling of mushroom body gamma neurons during metamorphosis, probably through regulating expression of the ecdysteroid receptor EcR; functions redundantly with wit. Involved in dpp/BMP-like signaling during development of the embryonic gut tracheal system. Required for dpp/BMP-like signaling involved in imaginal disc development. Involved in differentiation of dorsal cluster and ellipsoid body adult-specific neurons prior to metamorphosis. Required in motoneurons for axon guidance or outgrowth of ISNb and SNa axons. Required in somatic cyst cells for regulation of germ cell proliferation in testis. Involved in adult wing development and wing- vein formation.","On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcription factors (By similarity). Membrane; Single-pass type I membrane protein. Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily",Yes,Yes,Yes,Yes,Yes,Yes,GO:0048185; GO:0017002; GO:0005524; GO:0046872,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,0.6464,0.6464,0.6464,0.6464,0.3332,5,0.5838,0.6522,yes
AVR2_DROME,Q24468,ProtTale,Eukaryota,516,"Type II transmembrane receptor serine/threonine kinase involved in activin-like TGF-beta signaling and dpp/BMP-like signaling pathways. Forms a complex with type I transmembrane receptor serine/threonine kinases, and upon activation by signaling ligands induces the type I receptor to phosphorylate downstream receptor-regulated SMAD (R-SMAD) transcription factors, inducing their nuclear localization and resulting in regulation of ligand-responsive genes. Receptor for the activin-like TGF-beta ligands daw and Actbeta/activin when in complex with the type I receptor babo. Activation by daw requires babo isoform C. Receptor for the BMP-like ligand dpp when associated with the type I receptors tkv or sax. Activation by activin-like TGF-beta ligands, including daw and Actbeta/activin, results in phosphorylation of the R-SMAD Smox/SMAD2. Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad. Involved in dpp-signaling-dependent dorsoventral patterning of the epidermis during embryogenesis. Involved in axonal and dendritic pruning and neural remodeling of mushroom body gamma neurons during metamorphosis, probably through regulating expression of the ecdysteroid receptor EcR; functions redundantly with wit. Involved in dpp/BMP-like signaling during development of the embryonic gut tracheal system. Required for dpp/BMP-like signaling involved in imaginal disc development. Involved in differentiation of dorsal cluster and ellipsoid body adult-specific neurons prior to metamorphosis. Required in motoneurons for axon guidance or outgrowth of ISNb and SNa axons. Required in somatic cyst cells for regulation of germ cell proliferation in testis. Involved in adult wing development and wing- vein formation.",Tyrosine-protein kinase receptor.,Vague,No,No,Vague,Maybe,not-Yes,GO:0048185; GO:0017002; GO:0005524; GO:0046872,GO:0004714; GO:0005524,GO:0004714; GO:0005524,GO:0004714; GO:0005524,GO:0004714,GO:0004714; GO:0005524,0.6485,0.6485,0.6485,0.3229,0.6485,5,0.5834,0.6522,yes
AVR2_DROME,Q24468,Protein2Text,Eukaryota,516,"Type II transmembrane receptor serine/threonine kinase involved in activin-like TGF-beta signaling and dpp/BMP-like signaling pathways. Forms a complex with type I transmembrane receptor serine/threonine kinases, and upon activation by signaling ligands induces the type I receptor to phosphorylate downstream receptor-regulated SMAD (R-SMAD) transcription factors, inducing their nuclear localization and resulting in regulation of ligand-responsive genes. Receptor for the activin-like TGF-beta ligands daw and Actbeta/activin when in complex with the type I receptor babo. Activation by daw requires babo isoform C. Receptor for the BMP-like ligand dpp when associated with the type I receptors tkv or sax. Activation by activin-like TGF-beta ligands, including daw and Actbeta/activin, results in phosphorylation of the R-SMAD Smox/SMAD2. Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad. Involved in dpp-signaling-dependent dorsoventral patterning of the epidermis during embryogenesis. Involved in axonal and dendritic pruning and neural remodeling of mushroom body gamma neurons during metamorphosis, probably through regulating expression of the ecdysteroid receptor EcR; functions redundantly with wit. Involved in dpp/BMP-like signaling during development of the embryonic gut tracheal system. Required for dpp/BMP-like signaling involved in imaginal disc development. Involved in differentiation of dorsal cluster and ellipsoid body adult-specific neurons prior to metamorphosis. Required in motoneurons for axon guidance or outgrowth of ISNb and SNa axons. Required in somatic cyst cells for regulation of germ cell proliferation in testis. Involved in adult wing development and wing- vein formation.","This protein is a receptor tyrosine kinase, specifically a type I receptor. Its molecular function is to play a role in cell signaling pathways by binding to its ligand, BMP2B, and activating downstream signaling pathways, including the SMAD-dependent pathway. This leads to the activation of transcription factors that regulate gene expression and influence various cellular processes, including cell differentiation, proliferation, and apoptosis.",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0048185; GO:0017002; GO:0005524; GO:0046872,GO:0004674,GO:0004674; GO:0004872,GO:0004714,GO:0004714,GO:0004675,0.3332,0.373,0.3229,0.3229,0.4089,5,0.3522,0.6522,yes
AVR2_DROME,Q24468,Reference,Eukaryota,516,"Type II transmembrane receptor serine/threonine kinase involved in activin-like TGF-beta signaling and dpp/BMP-like signaling pathways. Forms a complex with type I transmembrane receptor serine/threonine kinases, and upon activation by signaling ligands induces the type I receptor to phosphorylate downstream receptor-regulated SMAD (R-SMAD) transcription factors, inducing their nuclear localization and resulting in regulation of ligand-responsive genes. Receptor for the activin-like TGF-beta ligands daw and Actbeta/activin when in complex with the type I receptor babo. Activation by daw requires babo isoform C. Receptor for the BMP-like ligand dpp when associated with the type I receptors tkv or sax. Activation by activin-like TGF-beta ligands, including daw and Actbeta/activin, results in phosphorylation of the R-SMAD Smox/SMAD2. Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad. Involved in dpp-signaling-dependent dorsoventral patterning of the epidermis during embryogenesis. Involved in axonal and dendritic pruning and neural remodeling of mushroom body gamma neurons during metamorphosis, probably through regulating expression of the ecdysteroid receptor EcR; functions redundantly with wit. Involved in dpp/BMP-like signaling during development of the embryonic gut tracheal system. Required for dpp/BMP-like signaling involved in imaginal disc development. Involved in differentiation of dorsal cluster and ellipsoid body adult-specific neurons prior to metamorphosis. Required in motoneurons for axon guidance or outgrowth of ISNb and SNa axons. Required in somatic cyst cells for regulation of germ cell proliferation in testis. Involved in adult wing development and wing- vein formation.","Type II transmembrane receptor serine/threonine kinase involved in activin-like TGF-beta signaling and dpp/BMP-like signaling pathways. Forms a complex with type I transmembrane receptor serine/threonine kinases, and upon activation by signaling ligands induces the type I receptor to phosphorylate downstream receptor-regulated SMAD (R-SMAD) transcription factors, inducing their nuclear localization and resulting in regulation of ligand-responsive genes. Receptor for the activin-like TGF-beta ligands daw and Actbeta/activin when in complex with the type I receptor babo. Activation by daw requires babo isoform C. Receptor for the BMP-like ligand dpp when associated with the type I receptors tkv or sax. Activation by activin-like TGF-beta ligands, including daw and Actbeta/activin, results in phosphorylation of the R-SMAD Smox/SMAD2. Activation by BMP-like ligands, including gbb and dpp, results in phosphorylation of the R-SMAD Mad. Involved in dpp-signaling-dependent dorsoventral patterning of the epidermis during embryogenesis. Involved in axonal and dendritic pruning and neural remodeling of mushroom body gamma neurons during metamorphosis, probably through regulating expression of the ecdysteroid receptor EcR; functions redundantly with wit. Involved in dpp/BMP-like signaling during development of the embryonic gut tracheal system. Required for dpp/BMP-like signaling involved in imaginal disc development. Involved in differentiation of dorsal cluster and ellipsoid body adult-specific neurons prior to metamorphosis. Required in motoneurons for axon guidance or outgrowth of ISNb and SNa axons. Required in somatic cyst cells for regulation of germ cell proliferation in testis. Involved in adult wing development and wing- vein formation.",,,,,,,GO:0048185; GO:0017002; GO:0005524; GO:0046872,GO:0004675,GO:0004675,GO:0004675,GO:0004675; GO:0005524,GO:0004675; GO:0005524,0.4089,0.4089,0.4089,0.7202,0.7202,5,0.5334,0.6522,yes
LDMS_STAA8,Q2FWC5,ESM2Text,Bacteria,397,"L-amino acid ligase, which preferentially catalyzes the formation of L-aspartyl-L-methionine dipeptide from L-aspartate and L- methionine in the presence of ATP. Less active with L-asparagine and L- methionine as substrates. Less active with L-aspartate and either L- phenylalanine, L-valine, L-leucine or L-isoleucine as substrates. Decreased activity when L-methionine is substituted with seleno-DL- methionine, L-homocysteine, L-methionine sulfoxide, L-methionine sulfoximine and o-acetyl-L-serine. Decreased activity with acetylation of L-methionine amino group. Decreased activity by modification of L- methionine carboxylate to L-methionine methyl ester. No activity when L-methionine is substituted with L-homoserine. No activity with formylation of L-methionine amino group. No activity by modification of L-methionine carboxylate to L-methionine-glycine carboxylate. No activity when L-aspartate substrate is replaced by analogs such as L- homoserine, DL-aspartate beta-methyl ester, L-glutamate or o-acetyl-L- serine. No activity when L-aspartate amino and alpha-carboxylate groups are modified to L-malate, glycine-L-aspartate, L-aspartate-glycine or N-carbamoyl-DL-aspartate. No activity with L-methionine or L-aspartate as sole substrates. No activity in presence of other nucleoside triphosphates including GTP, CTP, UTP, TTP or ITP. Involved in sulfur amino acid metabolism.",Dimethylates one of the amino groups of the biotin-binding domain of AcpS.,No,No,No,No,No,not-Yes,GO:0016881; GO:0005524; GO:0042802; GO:0034026; GO:0000287; GO:0042803,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.1705,0.1705,0.1705,0.1705,0.1705,5,0.1705,0.4228,no
LDMS_STAA8,Q2FWC5,Prot2Text,Bacteria,397,"L-amino acid ligase, which preferentially catalyzes the formation of L-aspartyl-L-methionine dipeptide from L-aspartate and L- methionine in the presence of ATP. Less active with L-asparagine and L- methionine as substrates. Less active with L-aspartate and either L- phenylalanine, L-valine, L-leucine or L-isoleucine as substrates. Decreased activity when L-methionine is substituted with seleno-DL- methionine, L-homocysteine, L-methionine sulfoxide, L-methionine sulfoximine and o-acetyl-L-serine. Decreased activity with acetylation of L-methionine amino group. Decreased activity by modification of L- methionine carboxylate to L-methionine methyl ester. No activity when L-methionine is substituted with L-homoserine. No activity with formylation of L-methionine amino group. No activity by modification of L-methionine carboxylate to L-methionine-glycine carboxylate. No activity when L-aspartate substrate is replaced by analogs such as L- homoserine, DL-aspartate beta-methyl ester, L-glutamate or o-acetyl-L- serine. No activity when L-aspartate amino and alpha-carboxylate groups are modified to L-malate, glycine-L-aspartate, L-aspartate-glycine or N-carbamoyl-DL-aspartate. No activity with L-methionine or L-aspartate as sole substrates. No activity in presence of other nucleoside triphosphates including GTP, CTP, UTP, TTP or ITP. Involved in sulfur amino acid metabolism.",Catalyzes the synthesis of beta-citryl-L-glutamate and N-acetyl-L-aspartyl-L-glutamate. Beta-citryl-L-glutamate is synthesized more efficiently than N-acetyl-L-aspartyl-L-glutamate.,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0016881; GO:0005524; GO:0042802; GO:0034026; GO:0000287; GO:0042803,GO:0016874,,GO:0016874,GO:0016874,GO:0016881,0.3689,,0.3689,0.3689,0.4669,4,0.3934,0.4228,no
LDMS_STAA8,Q2FWC5,ProtT3,Bacteria,397,"L-amino acid ligase, which preferentially catalyzes the formation of L-aspartyl-L-methionine dipeptide from L-aspartate and L- methionine in the presence of ATP. Less active with L-asparagine and L- methionine as substrates. Less active with L-aspartate and either L- phenylalanine, L-valine, L-leucine or L-isoleucine as substrates. Decreased activity when L-methionine is substituted with seleno-DL- methionine, L-homocysteine, L-methionine sulfoxide, L-methionine sulfoximine and o-acetyl-L-serine. Decreased activity with acetylation of L-methionine amino group. Decreased activity by modification of L- methionine carboxylate to L-methionine methyl ester. No activity when L-methionine is substituted with L-homoserine. No activity with formylation of L-methionine amino group. No activity by modification of L-methionine carboxylate to L-methionine-glycine carboxylate. No activity when L-aspartate substrate is replaced by analogs such as L- homoserine, DL-aspartate beta-methyl ester, L-glutamate or o-acetyl-L- serine. No activity when L-aspartate amino and alpha-carboxylate groups are modified to L-malate, glycine-L-aspartate, L-aspartate-glycine or N-carbamoyl-DL-aspartate. No activity with L-methionine or L-aspartate as sole substrates. No activity in presence of other nucleoside triphosphates including GTP, CTP, UTP, TTP or ITP. Involved in sulfur amino acid metabolism.","Catalyzes the ATP-dependent condensation of L-lysine with 2-ketoglutarate to form (2S,3S)-2- amino-3-ketoglutarate (AKG). Cytoplasm. Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family",Maybe,Maybe,Maybe,No,No,not-Yes,GO:0016881; GO:0005524; GO:0042802; GO:0034026; GO:0000287; GO:0042803,GO:0008483,GO:0008483,GO:0008483; GO:0030170,GO:0008483,GO:0008483,0.1705,0.1705,0.2963,0.1705,0.1705,5,0.1957,0.4228,no
LDMS_STAA8,Q2FWC5,ProtTale,Bacteria,397,"L-amino acid ligase, which preferentially catalyzes the formation of L-aspartyl-L-methionine dipeptide from L-aspartate and L- methionine in the presence of ATP. Less active with L-asparagine and L- methionine as substrates. Less active with L-aspartate and either L- phenylalanine, L-valine, L-leucine or L-isoleucine as substrates. Decreased activity when L-methionine is substituted with seleno-DL- methionine, L-homocysteine, L-methionine sulfoxide, L-methionine sulfoximine and o-acetyl-L-serine. Decreased activity with acetylation of L-methionine amino group. Decreased activity by modification of L- methionine carboxylate to L-methionine methyl ester. No activity when L-methionine is substituted with L-homoserine. No activity with formylation of L-methionine amino group. No activity by modification of L-methionine carboxylate to L-methionine-glycine carboxylate. No activity when L-aspartate substrate is replaced by analogs such as L- homoserine, DL-aspartate beta-methyl ester, L-glutamate or o-acetyl-L- serine. No activity when L-aspartate amino and alpha-carboxylate groups are modified to L-malate, glycine-L-aspartate, L-aspartate-glycine or N-carbamoyl-DL-aspartate. No activity with L-methionine or L-aspartate as sole substrates. No activity in presence of other nucleoside triphosphates including GTP, CTP, UTP, TTP or ITP. Involved in sulfur amino acid metabolism.",Catalyzes the ATP-dependent condensation of dihydroxyacetone phosphate (DHAP or glycerol-3-phosphate) and L-glutamate to gamma-glutamyl phosphate (GGP).,Maybe,Maybe,Maybe,No,No,not-Yes,GO:0016881; GO:0005524; GO:0042802; GO:0034026; GO:0000287; GO:0042803,GO:0016874,GO:0016874; GO:0005524,GO:0016874; GO:0005524,GO:0003824; GO:0005524,GO:0016874; GO:0005524,0.3689,0.5762,0.5762,0.5314,0.5762,5,0.5258,0.4228,no
LDMS_STAA8,Q2FWC5,Protein2Text,Bacteria,397,"L-amino acid ligase, which preferentially catalyzes the formation of L-aspartyl-L-methionine dipeptide from L-aspartate and L- methionine in the presence of ATP. Less active with L-asparagine and L- methionine as substrates. Less active with L-aspartate and either L- phenylalanine, L-valine, L-leucine or L-isoleucine as substrates. Decreased activity when L-methionine is substituted with seleno-DL- methionine, L-homocysteine, L-methionine sulfoxide, L-methionine sulfoximine and o-acetyl-L-serine. Decreased activity with acetylation of L-methionine amino group. Decreased activity by modification of L- methionine carboxylate to L-methionine methyl ester. No activity when L-methionine is substituted with L-homoserine. No activity with formylation of L-methionine amino group. No activity by modification of L-methionine carboxylate to L-methionine-glycine carboxylate. No activity when L-aspartate substrate is replaced by analogs such as L- homoserine, DL-aspartate beta-methyl ester, L-glutamate or o-acetyl-L- serine. No activity when L-aspartate amino and alpha-carboxylate groups are modified to L-malate, glycine-L-aspartate, L-aspartate-glycine or N-carbamoyl-DL-aspartate. No activity with L-methionine or L-aspartate as sole substrates. No activity in presence of other nucleoside triphosphates including GTP, CTP, UTP, TTP or ITP. Involved in sulfur amino acid metabolism.","Based on the name, it appears that this protein is a decarboxylase, which is an enzyme that catalyzes the removal of a carboxyl group from a molecule. Specifically, it is a decarboxylase that is involved in the metabolism of a certain compound, possibly a nucleotide or amino acid. Decarboxylases typically catalyze the conversion of a carboxylic acid to a carboxylate, releasing carbon dioxide as a byproduct. 

Is there anything else I can help you with?",No,No,No,No,No,not-Yes,GO:0016881; GO:0005524; GO:0042802; GO:0034026; GO:0000287; GO:0042803,GO:0016831,GO:0016831,,,GO:0016831,0.1705,0.1705,,,0.1705,3,0.1705,0.4228,no
LDMS_STAA8,Q2FWC5,Reference,Bacteria,397,"L-amino acid ligase, which preferentially catalyzes the formation of L-aspartyl-L-methionine dipeptide from L-aspartate and L- methionine in the presence of ATP. Less active with L-asparagine and L- methionine as substrates. Less active with L-aspartate and either L- phenylalanine, L-valine, L-leucine or L-isoleucine as substrates. Decreased activity when L-methionine is substituted with seleno-DL- methionine, L-homocysteine, L-methionine sulfoxide, L-methionine sulfoximine and o-acetyl-L-serine. Decreased activity with acetylation of L-methionine amino group. Decreased activity by modification of L- methionine carboxylate to L-methionine methyl ester. No activity when L-methionine is substituted with L-homoserine. No activity with formylation of L-methionine amino group. No activity by modification of L-methionine carboxylate to L-methionine-glycine carboxylate. No activity when L-aspartate substrate is replaced by analogs such as L- homoserine, DL-aspartate beta-methyl ester, L-glutamate or o-acetyl-L- serine. No activity when L-aspartate amino and alpha-carboxylate groups are modified to L-malate, glycine-L-aspartate, L-aspartate-glycine or N-carbamoyl-DL-aspartate. No activity with L-methionine or L-aspartate as sole substrates. No activity in presence of other nucleoside triphosphates including GTP, CTP, UTP, TTP or ITP. Involved in sulfur amino acid metabolism.","L-amino acid ligase, which preferentially catalyzes the formation of L-aspartyl-L-methionine dipeptide from L-aspartate and L- methionine in the presence of ATP. Less active with L-asparagine and L- methionine as substrates. Less active with L-aspartate and either L- phenylalanine, L-valine, L-leucine or L-isoleucine as substrates. Decreased activity when L-methionine is substituted with seleno-DL- methionine, L-homocysteine, L-methionine sulfoxide, L-methionine sulfoximine and o-acetyl-L-serine. Decreased activity with acetylation of L-methionine amino group. Decreased activity by modification of L- methionine carboxylate to L-methionine methyl ester. No activity when L-methionine is substituted with L-homoserine. No activity with formylation of L-methionine amino group. No activity by modification of L-methionine carboxylate to L-methionine-glycine carboxylate. No activity when L-aspartate substrate is replaced by analogs such as L- homoserine, DL-aspartate beta-methyl ester, L-glutamate or o-acetyl-L- serine. No activity when L-aspartate amino and alpha-carboxylate groups are modified to L-malate, glycine-L-aspartate, L-aspartate-glycine or N-carbamoyl-DL-aspartate. No activity with L-methionine or L-aspartate as sole substrates. No activity in presence of other nucleoside triphosphates including GTP, CTP, UTP, TTP or ITP. Involved in sulfur amino acid metabolism.",,,,,,,GO:0016881; GO:0005524; GO:0042802; GO:0034026; GO:0000287; GO:0042803,GO:0016879; GO:0005524,GO:0016879,GO:0016881; GO:0005524,GO:0016881; GO:0005524,GO:0016881; GO:0005524,0.6219,0.4144,0.6766,0.6766,0.6766,5,0.6132,0.4228,no
SAGB_STAA8,Q2FXF4,ESM2Text,Bacteria,284,"Involved in bacterial cell envelope homeostasis. Cleaves peptidoglycan strands intermittently at regular intervals. As part of a complex with lysostaphin resistance protein LyrA/SpdC, probably cleaves nascent peptidoglycan to yield short lipid-linked oligomers that can be elongated further; cleavage activity is probably dependent on the presence of substrate lipid tail.",Involved in cell wall degradation. Hydrolyzes extracellular N-acetylmuramyl residues and plays an important role in cell separation during growth. May act as a N-acetylmuramyl-minic acid-binding protein and cell wall anchoring protein.,Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0004040,GO:0016798,GO:0003796,GO:0008745,GO:0003796,GO:0016798,0.482,0.339,0.6742,0.339,0.482,5,0.4632,0.4812,no
SAGB_STAA8,Q2FXF4,Prot2Text,Bacteria,284,"Involved in bacterial cell envelope homeostasis. Cleaves peptidoglycan strands intermittently at regular intervals. As part of a complex with lysostaphin resistance protein LyrA/SpdC, probably cleaves nascent peptidoglycan to yield short lipid-linked oligomers that can be elongated further; cleavage activity is probably dependent on the presence of substrate lipid tail.",Peptidoglycan polymerase that is essential for cell division.,No,No,No,No,Maybe,not-Yes,GO:0004040,GO:0008955,,GO:0008955,GO:0016757,GO:0016757,0.1998,,0.1998,0.2845,0.2845,4,0.2421,0.4812,no
SAGB_STAA8,Q2FXF4,ProtT3,Bacteria,284,"Involved in bacterial cell envelope homeostasis. Cleaves peptidoglycan strands intermittently at regular intervals. As part of a complex with lysostaphin resistance protein LyrA/SpdC, probably cleaves nascent peptidoglycan to yield short lipid-linked oligomers that can be elongated further; cleavage activity is probably dependent on the presence of substrate lipid tail.",Hydrolyzes peptidoglycan. Secreted. Belongs to the glycosyl hydrolase 73 family,Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0004040,GO:0003796,GO:0004553,GO:0016798,GO:0003796,GO:0016798,0.339,0.3987,0.482,0.339,0.482,5,0.4081,0.4812,no
SAGB_STAA8,Q2FXF4,ProtTale,Bacteria,284,"Involved in bacterial cell envelope homeostasis. Cleaves peptidoglycan strands intermittently at regular intervals. As part of a complex with lysostaphin resistance protein LyrA/SpdC, probably cleaves nascent peptidoglycan to yield short lipid-linked oligomers that can be elongated further; cleavage activity is probably dependent on the presence of substrate lipid tail.",Cell wall formation. May participate in the formation of N-acetylglucosamine (GlcNAc) at the cell surface in GlcNAc biosynthesis. May introduce GlcNAc into the cell wall by catalyzing the transfer of GlcNAc from UDP-GlcNAc to the lipid carrier undecaprenyl phosphate (C55-P).,No,No,No,No,Maybe,not-Yes,GO:0004040,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.2845,0.2845,0.2845,0.2845,0.2845,5,0.2845,0.4812,no
SAGB_STAA8,Q2FXF4,Protein2Text,Bacteria,284,"Involved in bacterial cell envelope homeostasis. Cleaves peptidoglycan strands intermittently at regular intervals. As part of a complex with lysostaphin resistance protein LyrA/SpdC, probably cleaves nascent peptidoglycan to yield short lipid-linked oligomers that can be elongated further; cleavage activity is probably dependent on the presence of substrate lipid tail.","This protein is involved in the cleavage of peptidoglycan, a process that is essential for bacterial cell wall maintenance and division. Specifically, it is a lytic transglycosylase, which breaks and rejoins the glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine residues in the peptidoglycan polymer. This function is crucial for the separation of daughter cells during cell division.",Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0004040,GO:0008933,GO:0008933,GO:0008933,GO:0008933,GO:0008933,0.2199,0.2199,0.2199,0.2199,0.2199,5,0.2199,0.4812,no
SAGB_STAA8,Q2FXF4,Reference,Bacteria,284,"Involved in bacterial cell envelope homeostasis. Cleaves peptidoglycan strands intermittently at regular intervals. As part of a complex with lysostaphin resistance protein LyrA/SpdC, probably cleaves nascent peptidoglycan to yield short lipid-linked oligomers that can be elongated further; cleavage activity is probably dependent on the presence of substrate lipid tail.","Involved in bacterial cell envelope homeostasis. Cleaves peptidoglycan strands intermittently at regular intervals. As part of a complex with lysostaphin resistance protein LyrA/SpdC, probably cleaves nascent peptidoglycan to yield short lipid-linked oligomers that can be elongated further; cleavage activity is probably dependent on the presence of substrate lipid tail.",,,,,,,GO:0004040,GO:0016798,GO:0016798,GO:0016798,GO:0008745,GO:0016998,0.482,0.482,0.482,0.6742,0.0,5,0.424,0.4812,no
ROP18_TOXGO,Q2PAY2,ESM2Text,Eukaryota,554,"Protein kinase (Probable). Virulence factor. Mediates parasite survival in mouse macrophages and monocytes. Reduces the accumulation of mouse IRGA6 (IIGP1) and IRGB6 (TGTP1/TGTP2), immunity-related GTPases (IRGs) that protect mice from infection by certain intracellular pathogens, on the parasitophorous vacuole and IRG- mediated killing of parasites by mouse cells; probably in connection with ROP5. In complex with GRA7, targets IRGs to prevent IRG-mediated parasite killing by mouse cells. Phosphorylates mouse IRGA6 (IIGP1); its activity toward mouse IRGA6 is promoted by GRA7 or ROP5 (Probable). Phosphorylates mouse IRGB6 (TGTP1/TGTP2). Phosphorylates mouse IRGB10 (GM12250). Does not affect IFN-gamma (IFNG)-mediated parasite killing in human cells that do not possess the large variety of IRGs.","Serine/threonine-protein kinase required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Required for the repression of transposon silencing in the germline.",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0046872; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.5334,0.5334,0.5334,0.5334,0.5334,5,0.5334,0.5284,no
ROP18_TOXGO,Q2PAY2,Prot2Text,Eukaryota,554,"Protein kinase (Probable). Virulence factor. Mediates parasite survival in mouse macrophages and monocytes. Reduces the accumulation of mouse IRGA6 (IIGP1) and IRGB6 (TGTP1/TGTP2), immunity-related GTPases (IRGs) that protect mice from infection by certain intracellular pathogens, on the parasitophorous vacuole and IRG- mediated killing of parasites by mouse cells; probably in connection with ROP5. In complex with GRA7, targets IRGs to prevent IRG-mediated parasite killing by mouse cells. Phosphorylates mouse IRGA6 (IIGP1); its activity toward mouse IRGA6 is promoted by GRA7 or ROP5 (Probable). Phosphorylates mouse IRGB6 (TGTP1/TGTP2). Phosphorylates mouse IRGB10 (GM12250). Does not affect IFN-gamma (IFNG)-mediated parasite killing in human cells that do not possess the large variety of IRGs.",Essential for the completion of the first mitotic cell cycle in the embryo. May play a role in either the generation of the precursor cell-cycle marker MAPK or the mitotic regulator CDK2.,Vague,Maybe,Vague,No,No,not-Yes,GO:0005524; GO:0046872; GO:0004674,,,,,,,,,,,0,,0.5284,no
ROP18_TOXGO,Q2PAY2,ProtT3,Eukaryota,554,"Protein kinase (Probable). Virulence factor. Mediates parasite survival in mouse macrophages and monocytes. Reduces the accumulation of mouse IRGA6 (IIGP1) and IRGB6 (TGTP1/TGTP2), immunity-related GTPases (IRGs) that protect mice from infection by certain intracellular pathogens, on the parasitophorous vacuole and IRG- mediated killing of parasites by mouse cells; probably in connection with ROP5. In complex with GRA7, targets IRGs to prevent IRG-mediated parasite killing by mouse cells. Phosphorylates mouse IRGA6 (IIGP1); its activity toward mouse IRGA6 is promoted by GRA7 or ROP5 (Probable). Phosphorylates mouse IRGB6 (TGTP1/TGTP2). Phosphorylates mouse IRGB10 (GM12250). Does not affect IFN-gamma (IFNG)-mediated parasite killing in human cells that do not possess the large variety of IRGs.",Membrane; Single-pass membrane protein. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0046872; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,0.8578,0.8578,0.8578,0.8578,0.5334,5,0.7929,0.5284,no
ROP18_TOXGO,Q2PAY2,ProtTale,Eukaryota,554,"Protein kinase (Probable). Virulence factor. Mediates parasite survival in mouse macrophages and monocytes. Reduces the accumulation of mouse IRGA6 (IIGP1) and IRGB6 (TGTP1/TGTP2), immunity-related GTPases (IRGs) that protect mice from infection by certain intracellular pathogens, on the parasitophorous vacuole and IRG- mediated killing of parasites by mouse cells; probably in connection with ROP5. In complex with GRA7, targets IRGs to prevent IRG-mediated parasite killing by mouse cells. Phosphorylates mouse IRGA6 (IIGP1); its activity toward mouse IRGA6 is promoted by GRA7 or ROP5 (Probable). Phosphorylates mouse IRGB6 (TGTP1/TGTP2). Phosphorylates mouse IRGB10 (GM12250). Does not affect IFN-gamma (IFNG)-mediated parasite killing in human cells that do not possess the large variety of IRGs.","Serine/threonine-protein kinase which phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2-alpha/EIF2S1), thereby affecting translation control in response to various stress conditions. Under normal growth conditions, phosphorylated eIF-2-alpha/EIF2S1 binds to GTP-bound eIF-2-alpha/EIF2S1 and prevents the assembly of eIF-2-alpha/EIF2S1 into a stable complex with eIF-2-beta/EIF2S2 and GDP. Dephosphorylated eIF-2-alpha/EIF2S1",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0046872; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004694,GO:0004674; GO:0005524,0.8578,0.8578,0.8578,0.4848,0.8578,5,0.7832,0.5284,no
ROP18_TOXGO,Q2PAY2,Protein2Text,Eukaryota,554,"Protein kinase (Probable). Virulence factor. Mediates parasite survival in mouse macrophages and monocytes. Reduces the accumulation of mouse IRGA6 (IIGP1) and IRGB6 (TGTP1/TGTP2), immunity-related GTPases (IRGs) that protect mice from infection by certain intracellular pathogens, on the parasitophorous vacuole and IRG- mediated killing of parasites by mouse cells; probably in connection with ROP5. In complex with GRA7, targets IRGs to prevent IRG-mediated parasite killing by mouse cells. Phosphorylates mouse IRGA6 (IIGP1); its activity toward mouse IRGA6 is promoted by GRA7 or ROP5 (Probable). Phosphorylates mouse IRGB6 (TGTP1/TGTP2). Phosphorylates mouse IRGB10 (GM12250). Does not affect IFN-gamma (IFNG)-mediated parasite killing in human cells that do not possess the large variety of IRGs.",This protein is a serine protease.,No,No,No,No,Maybe,not-Yes,GO:0005524; GO:0046872; GO:0004674,GO:0004252,GO:0004252,GO:0008236,GO:0004252,GO:0004252,0.1551,0.1551,0.1866,0.1551,0.1551,5,0.1614,0.5284,no
ROP18_TOXGO,Q2PAY2,Reference,Eukaryota,554,"Protein kinase (Probable). Virulence factor. Mediates parasite survival in mouse macrophages and monocytes. Reduces the accumulation of mouse IRGA6 (IIGP1) and IRGB6 (TGTP1/TGTP2), immunity-related GTPases (IRGs) that protect mice from infection by certain intracellular pathogens, on the parasitophorous vacuole and IRG- mediated killing of parasites by mouse cells; probably in connection with ROP5. In complex with GRA7, targets IRGs to prevent IRG-mediated parasite killing by mouse cells. Phosphorylates mouse IRGA6 (IIGP1); its activity toward mouse IRGA6 is promoted by GRA7 or ROP5 (Probable). Phosphorylates mouse IRGB6 (TGTP1/TGTP2). Phosphorylates mouse IRGB10 (GM12250). Does not affect IFN-gamma (IFNG)-mediated parasite killing in human cells that do not possess the large variety of IRGs.","Protein kinase (Probable). Virulence factor. Mediates parasite survival in mouse macrophages and monocytes. Reduces the accumulation of mouse IRGA6 (IIGP1) and IRGB6 (TGTP1/TGTP2), immunity-related GTPases (IRGs) that protect mice from infection by certain intracellular pathogens, on the parasitophorous vacuole and IRG- mediated killing of parasites by mouse cells; probably in connection with ROP5. In complex with GRA7, targets IRGs to prevent IRG-mediated parasite killing by mouse cells. Phosphorylates mouse IRGA6 (IIGP1); its activity toward mouse IRGA6 is promoted by GRA7 or ROP5 (Probable). Phosphorylates mouse IRGB6 (TGTP1/TGTP2). Phosphorylates mouse IRGB10 (GM12250). Does not affect IFN-gamma (IFNG)-mediated parasite killing in human cells that do not possess the large variety of IRGs.",,,,,,,GO:0005524; GO:0046872; GO:0004674,GO:0004672,GO:0004674,GO:0004672,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.493,0.5334,0.493,0.8578,0.8578,5,0.647,0.5284,no
ROP17_TOXGO,Q2PAY3,ESM2Text,Eukaryota,608,"Protein kinase. Virulence factor. Promotes migration of Toxoplasma-infected macrophages through collagen matrix, facilitating parasite transport through tissues and systemic dissemination. Plays a role in the translocation of dense granule effectors, such as GRA16 and GRA24, across the parasitophorous vacuole membrane in Toxoplasma- infected host cells. Phosphorylates mouse IRGB6 (TGTP1/TGTP2), an immunity-related GTPase (IRG) that protects mice from infection by certain intracellular pathogens; the phosphorylation leads to the disassembly of IRGB6 polymers into monomers and dimers. May modulate gene expression in human cells. Promotes autophagy in human cells via modulation of the BCL2-BECN1 pathway.",Serine/threonine protein kinase required for cell death control in response to endoplasmic reticulum stress and osmotic stress. Acts downstream of the mTOR signaling pathway and directly activates mTORC1 and mTORC2. Colocalizes with phosphorylated mTORC1 in the cytoplasm and recruits mTORC1 to the lumen of the endoplasmic reticulum and activates the mTORC1 kinase. Colocalizes with phosphorylated mTORC1 in the nucleus and activates mTORC1 kinase. Plays a role in cell growth and survival. Plays a role in protecting cells against oxidative stress-induced apoptosis by protecting cells against oxidant stress-induced cell death. Promotes cell survival during embryonic development through phosphorylation of AKT1 and ATF2 and subsequent up-regulation of ATF2. Mediates phosphorylation of SMAD1 and SMAD3 and subsequent recruitment of SMAD3 to the F-actin cytoskeleton. Plays a role in bone mineralization through phosphorylation of FZD1 and subsequent recruitment of FZD1 to the mineralization-promoting complex (MPC). Phosphorylates SMAD1,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.6847,0.6847,0.6847,0.6847,0.6847,5,0.6847,0.5717,yes
ROP17_TOXGO,Q2PAY3,Prot2Text,Eukaryota,608,"Protein kinase. Virulence factor. Promotes migration of Toxoplasma-infected macrophages through collagen matrix, facilitating parasite transport through tissues and systemic dissemination. Plays a role in the translocation of dense granule effectors, such as GRA16 and GRA24, across the parasitophorous vacuole membrane in Toxoplasma- infected host cells. Phosphorylates mouse IRGB6 (TGTP1/TGTP2), an immunity-related GTPase (IRG) that protects mice from infection by certain intracellular pathogens; the phosphorylation leads to the disassembly of IRGB6 polymers into monomers and dimers. May modulate gene expression in human cells. Promotes autophagy in human cells via modulation of the BCL2-BECN1 pathway.",Could play a role in either the maintenance of spore wall integrity or the modulation of the activity of the alpha-amylase complex.,No,No,Vague,No,No,not-Yes,GO:0005524; GO:0004674,,,,,,,,,,,0,,0.5717,yes
ROP17_TOXGO,Q2PAY3,ProtT3,Eukaryota,608,"Protein kinase. Virulence factor. Promotes migration of Toxoplasma-infected macrophages through collagen matrix, facilitating parasite transport through tissues and systemic dissemination. Plays a role in the translocation of dense granule effectors, such as GRA16 and GRA24, across the parasitophorous vacuole membrane in Toxoplasma- infected host cells. Phosphorylates mouse IRGB6 (TGTP1/TGTP2), an immunity-related GTPase (IRG) that protects mice from infection by certain intracellular pathogens; the phosphorylation leads to the disassembly of IRGB6 polymers into monomers and dimers. May modulate gene expression in human cells. Promotes autophagy in human cells via modulation of the BCL2-BECN1 pathway.",Belongs to the protein kinase superfamily. Ser/Thr protein kinase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,1.0,1.0,1.0,1.0,0.6847,5,0.9369,0.5717,yes
ROP17_TOXGO,Q2PAY3,ProtTale,Eukaryota,608,"Protein kinase. Virulence factor. Promotes migration of Toxoplasma-infected macrophages through collagen matrix, facilitating parasite transport through tissues and systemic dissemination. Plays a role in the translocation of dense granule effectors, such as GRA16 and GRA24, across the parasitophorous vacuole membrane in Toxoplasma- infected host cells. Phosphorylates mouse IRGB6 (TGTP1/TGTP2), an immunity-related GTPase (IRG) that protects mice from infection by certain intracellular pathogens; the phosphorylation leads to the disassembly of IRGB6 polymers into monomers and dimers. May modulate gene expression in human cells. Promotes autophagy in human cells via modulation of the BCL2-BECN1 pathway.",Serine/threonine-protein kinase which is required for parasite development in the mosquito and for parasite transmission to the vertebrate host.,Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,1.0,1.0,1.0,0.6847,1.0,5,0.9369,0.5717,yes
ROP17_TOXGO,Q2PAY3,Protein2Text,Eukaryota,608,"Protein kinase. Virulence factor. Promotes migration of Toxoplasma-infected macrophages through collagen matrix, facilitating parasite transport through tissues and systemic dissemination. Plays a role in the translocation of dense granule effectors, such as GRA16 and GRA24, across the parasitophorous vacuole membrane in Toxoplasma- infected host cells. Phosphorylates mouse IRGB6 (TGTP1/TGTP2), an immunity-related GTPase (IRG) that protects mice from infection by certain intracellular pathogens; the phosphorylation leads to the disassembly of IRGB6 polymers into monomers and dimers. May modulate gene expression in human cells. Promotes autophagy in human cells via modulation of the BCL2-BECN1 pathway.","This protein is involved in the molecular function of being a part of a protein complex that plays a role in viral replication. Specifically, it is involved in the replication of the viral genome.",No,No,No,No,No,not-Yes,GO:0005524; GO:0004674,,,,,,,,,,,0,,0.5717,yes
ROP17_TOXGO,Q2PAY3,Reference,Eukaryota,608,"Protein kinase. Virulence factor. Promotes migration of Toxoplasma-infected macrophages through collagen matrix, facilitating parasite transport through tissues and systemic dissemination. Plays a role in the translocation of dense granule effectors, such as GRA16 and GRA24, across the parasitophorous vacuole membrane in Toxoplasma- infected host cells. Phosphorylates mouse IRGB6 (TGTP1/TGTP2), an immunity-related GTPase (IRG) that protects mice from infection by certain intracellular pathogens; the phosphorylation leads to the disassembly of IRGB6 polymers into monomers and dimers. May modulate gene expression in human cells. Promotes autophagy in human cells via modulation of the BCL2-BECN1 pathway.","Protein kinase. Virulence factor. Promotes migration of Toxoplasma-infected macrophages through collagen matrix, facilitating parasite transport through tissues and systemic dissemination. Plays a role in the translocation of dense granule effectors, such as GRA16 and GRA24, across the parasitophorous vacuole membrane in Toxoplasma- infected host cells. Phosphorylates mouse IRGB6 (TGTP1/TGTP2), an immunity-related GTPase (IRG) that protects mice from infection by certain intracellular pathogens; the phosphorylation leads to the disassembly of IRGB6 polymers into monomers and dimers. May modulate gene expression in human cells. Promotes autophagy in human cells via modulation of the BCL2-BECN1 pathway.",,,,,,,GO:0005524; GO:0004674,GO:0004672,GO:0004674,GO:0004672,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.6276,0.6847,0.6276,1.0,1.0,5,0.788,0.5717,yes
WSS1_ORYSJ,Q2R560,ESM2Text,Eukaryota,912,"Transmembrane kinase receptor involved in the regulation of reactive oxygen species (ROS) homeostasis, chloroplast development and leaf senescence.",Involved in auxin signal transduction and cell expansion and proliferation regulation.,No,Vague,Vague,No,No,not-Yes,GO:0005524; GO:0004674,,,,,,,,,,,0,,0.5791,yes
WSS1_ORYSJ,Q2R560,Prot2Text,Eukaryota,912,"Transmembrane kinase receptor involved in the regulation of reactive oxygen species (ROS) homeostasis, chloroplast development and leaf senescence.",Acts as a direct positive regulator of meristem size and size. Involved in auxin signal transduction. Acts as a negative regulator of cell division and organ growth.,No,Vague,Vague,No,No,not-Yes,GO:0005524; GO:0004674,,,,,,,,,,,0,,0.5791,yes
WSS1_ORYSJ,Q2R560,ProtT3,Eukaryota,912,"Transmembrane kinase receptor involved in the regulation of reactive oxygen species (ROS) homeostasis, chloroplast development and leaf senescence.",Membrane; Single-pass membrane protein. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,1.0,1.0,1.0,1.0,0.6847,5,0.9369,0.5791,yes
WSS1_ORYSJ,Q2R560,ProtTale,Eukaryota,912,"Transmembrane kinase receptor involved in the regulation of reactive oxygen species (ROS) homeostasis, chloroplast development and leaf senescence.",Receptor-like protein kinase that plays a central role during fertilization. Involved in pollen tube reception at the female gametophyte surface.,Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,1.0,1.0,1.0,0.6847,1.0,5,0.9369,0.5791,yes
WSS1_ORYSJ,Q2R560,Protein2Text,Eukaryota,912,"Transmembrane kinase receptor involved in the regulation of reactive oxygen species (ROS) homeostasis, chloroplast development and leaf senescence.","This protein is a receptor kinase, which means it is a type of enzyme that is involved in the transfer of phosphate groups to other molecules. Specifically, it is a receptor-like kinase, which is a type of kinase that is involved in the recognition of extracellular signals and the subsequent activation of downstream signaling pathways. The molecular function of this protein is to recognize and bind to specific ligands, such as plant hormones or other signaling molecules, and then transmit the signal to the cell by phosphorylating downstream targets. This process is essential for a variety of cellular processes, including growth and development, defense responses, and stress tolerance.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0004674,GO:0004674,GO:0004674; GO:0004872,GO:0004674,GO:0004674,GO:0004675,0.6847,0.5546,0.6847,0.6847,0.5132,5,0.6244,0.5791,yes
WSS1_ORYSJ,Q2R560,Reference,Eukaryota,912,"Transmembrane kinase receptor involved in the regulation of reactive oxygen species (ROS) homeostasis, chloroplast development and leaf senescence.","Transmembrane kinase receptor involved in the regulation of reactive oxygen species (ROS) homeostasis, chloroplast development and leaf senescence.",,,,,,,GO:0005524; GO:0004674,GO:0004675,GO:0004672,GO:0004672,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.5132,0.6276,0.6276,1.0,1.0,5,0.7537,0.5791,yes
CE1_TRYB2,Q381X9,ESM2Text,Eukaryota,586,Recapping enzyme with 5'-monophosphate RNA kinase and guanylyltransferase activities that can convert decapped pRNA into GpppRNA via a ppRNA intermediate. Targets hypermethylated spliced leader (SL) RNAs derived from cap 4 mRNA.,Required for maintaining the appropriate mycolic acid composition and permeability of the envelope on its exposure to acidic pH.,No,No,No,No,No,not-Yes,GO:0005524; GO:0019002; GO:0004484; GO:0008192,,,,,,,,,,,0,,0.4202,no
CE1_TRYB2,Q381X9,Prot2Text,Eukaryota,586,Recapping enzyme with 5'-monophosphate RNA kinase and guanylyltransferase activities that can convert decapped pRNA into GpppRNA via a ppRNA intermediate. Targets hypermethylated spliced leader (SL) RNAs derived from cap 4 mRNA.,"DGK3 is essential for the transposition of the mitotic spindle. It is required for correct septation, centrosome duplication and insertion of the eggs into the spindle.",No,No,No,No,No,not-Yes,GO:0005524; GO:0019002; GO:0004484; GO:0008192,,,GO:0004143,,,,,0.2202,,,1,0.2202,0.4202,no
CE1_TRYB2,Q381X9,ProtT3,Eukaryota,586,Recapping enzyme with 5'-monophosphate RNA kinase and guanylyltransferase activities that can convert decapped pRNA into GpppRNA via a ppRNA intermediate. Targets hypermethylated spliced leader (SL) RNAs derived from cap 4 mRNA.,Catalytic subunit of the mRNA capping enzyme which catalyzes four enzymatic reactions: the 5' triphosphate end of the pre-mRNA is hydrolyzed to a diphosphate by RNA 5' triphosphatase; the diphosphate RNA end is capped with GMP by RNA guanylyltransferase; the poly(A) tail is cleaved from the 3' end of the mRNA by poly(A) RNA polymerase and the poly(A) tail and the 3' end is methylated by a poly(A) RNA 2'-O-methyltransferase. Virion. Belongs to the,Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0019002; GO:0004484; GO:0008192,GO:0004484; GO:0008168,GO:0004484; GO:0004651; GO:0008168,GO:0004484; GO:0008168,GO:0004484; GO:0008174,GO:0004484; GO:0008174,0.5594,0.5018,0.5594,0.573,0.573,5,0.5533,0.4202,no
CE1_TRYB2,Q381X9,ProtTale,Eukaryota,586,Recapping enzyme with 5'-monophosphate RNA kinase and guanylyltransferase activities that can convert decapped pRNA into GpppRNA via a ppRNA intermediate. Targets hypermethylated spliced leader (SL) RNAs derived from cap 4 mRNA.,Catalyzes the addition of 2'-phosphate and 5'-monophosphate groups to the 3' side of tRNA.,No,No,No,No,No,not-Yes,GO:0005524; GO:0019002; GO:0004484; GO:0008192,GO:0016301,GO:0016301,GO:0016301,GO:0004838,GO:0016301,0.2963,0.2963,0.2963,0.1593,0.2963,5,0.2689,0.4202,no
CE1_TRYB2,Q381X9,Protein2Text,Eukaryota,586,Recapping enzyme with 5'-monophosphate RNA kinase and guanylyltransferase activities that can convert decapped pRNA into GpppRNA via a ppRNA intermediate. Targets hypermethylated spliced leader (SL) RNAs derived from cap 4 mRNA.,"The molecular function of this protein is not explicitly stated in the provided text, but based on the context, it is likely that this protein is involved in the replication of viral RNA. More specifically, it is a helicase, which is an enzyme that unwinds double-stranded nucleic acid into single-stranded templates for replication.",No,No,No,Vague,No,not-Yes,GO:0005524; GO:0019002; GO:0004484; GO:0008192,GO:0003724,GO:0004003,,GO:0004386,GO:0003724,0.2381,0.1685,,0.2118,0.2381,4,0.2141,0.4202,no
CE1_TRYB2,Q381X9,Reference,Eukaryota,586,Recapping enzyme with 5'-monophosphate RNA kinase and guanylyltransferase activities that can convert decapped pRNA into GpppRNA via a ppRNA intermediate. Targets hypermethylated spliced leader (SL) RNAs derived from cap 4 mRNA.,Recapping enzyme with 5'-monophosphate RNA kinase and guanylyltransferase activities that can convert decapped pRNA into GpppRNA via a ppRNA intermediate. Targets hypermethylated spliced leader (SL) RNAs derived from cap 4 mRNA.,,,,,,,GO:0005524; GO:0019002; GO:0004484; GO:0008192,GO:0004484,GO:0004484,GO:0004484; GO:0008683,GO:0016301; GO:0004484; GO:0005524,GO:0019114; GO:0004484,0.6015,0.6015,0.533,0.8652,0.6015,5,0.6405,0.4202,no
AURKB_TRYB2,Q384J7,ESM2Text,Eukaryota,309,"Serine/threonine-protein kinase. Involved in regulation of entrance into mitosis during cell cycle progression. Involved in regulation of chromosome segregation during mitosis. Regulates chromosome biorientation by promoting the establishment of stable bioriented kinetochore-microtubule attachments (Probable). Controls metaphase-to-anaphase transition. Promotes anaphase entry via phosphorylation of KKT14. Required for mitotic exit and the integrity of the mitotic spindle. Involved in regulation of cytokinesis. Regulates trans-localization of the chromosomal passenger complex (CPC) from the spindle midzone to the dorsal anterior of the cell at the beginning of cytokinesis. Displays autophosphorylation activity and phosphorylates various kinetoplastid kinetochore proteins (KKTs), including KKT1, KKT7 and KKT8. Phosphorylates histone H3. Phosphorylates CPC1, KIN-A and KIN-B. Phosphorylates TLK1 and TKL2.",Serine/threonine-protein kinase which is required for chromosome condensation and kinetochore formation during mitosis. May phosphorylate microtubule-associated protein SAVAM1. May be involved in the regulation of chromatin structure by phosphorylating and regulating HO endoribonuclease VAB3.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0106310; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.7186,0.7186,0.7186,0.7186,0.7186,5,0.7186,0.6496,yes
AURKB_TRYB2,Q384J7,Prot2Text,Eukaryota,309,"Serine/threonine-protein kinase. Involved in regulation of entrance into mitosis during cell cycle progression. Involved in regulation of chromosome segregation during mitosis. Regulates chromosome biorientation by promoting the establishment of stable bioriented kinetochore-microtubule attachments (Probable). Controls metaphase-to-anaphase transition. Promotes anaphase entry via phosphorylation of KKT14. Required for mitotic exit and the integrity of the mitotic spindle. Involved in regulation of cytokinesis. Regulates trans-localization of the chromosomal passenger complex (CPC) from the spindle midzone to the dorsal anterior of the cell at the beginning of cytokinesis. Displays autophosphorylation activity and phosphorylates various kinetoplastid kinetochore proteins (KKTs), including KKT1, KKT7 and KKT8. Phosphorylates histone H3. Phosphorylates CPC1, KIN-A and KIN-B. Phosphorylates TLK1 and TKL2.","Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression, the regulation of cell cycle progression through mitosis and the regulation of cell cycle progression during G2/M. Involved in the regulation of cell cycle progression through the regulation of G1/S transition. Involved in the regulation of cell cycle progression through the regulation of G2/M transition. Promotes cell survival by phosphorylating BAD which inhibits the activity of BAD-related proteins. Inhibits cell cycle progression and tumorigenesis by phosphorylating BAD which inhibits the activity of MAPK1/3 (MAPK1/2), and promotes cell survival by phosphorylating SFPQ which inhibits the activity of SFPQ and SFPQL. Inhibits cell cycle progression by preventing the binding of CDKN1B to 'Ser-10' and 'Ser-28' sequence repeats in the cytoplasmic tail of CDKN1B; this prevents the binding of CDKN1B to 'Ser-7' and 'Ser-10' sequence repeats in",Maybe,Yes,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0106310; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.7186,0.7186,0.7186,0.7186,0.7186,5,0.7186,0.6496,yes
AURKB_TRYB2,Q384J7,ProtT3,Eukaryota,309,"Serine/threonine-protein kinase. Involved in regulation of entrance into mitosis during cell cycle progression. Involved in regulation of chromosome segregation during mitosis. Regulates chromosome biorientation by promoting the establishment of stable bioriented kinetochore-microtubule attachments (Probable). Controls metaphase-to-anaphase transition. Promotes anaphase entry via phosphorylation of KKT14. Required for mitotic exit and the integrity of the mitotic spindle. Involved in regulation of cytokinesis. Regulates trans-localization of the chromosomal passenger complex (CPC) from the spindle midzone to the dorsal anterior of the cell at the beginning of cytokinesis. Displays autophosphorylation activity and phosphorylates various kinetoplastid kinetochore proteins (KKTs), including KKT1, KKT7 and KKT8. Phosphorylates histone H3. Phosphorylates CPC1, KIN-A and KIN-B. Phosphorylates TLK1 and TKL2.",Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004683; GO:0005524,GO:0004674,0.964,0.964,0.964,0.9128,0.7186,5,0.9047,0.6496,yes
AURKB_TRYB2,Q384J7,ProtTale,Eukaryota,309,"Serine/threonine-protein kinase. Involved in regulation of entrance into mitosis during cell cycle progression. Involved in regulation of chromosome segregation during mitosis. Regulates chromosome biorientation by promoting the establishment of stable bioriented kinetochore-microtubule attachments (Probable). Controls metaphase-to-anaphase transition. Promotes anaphase entry via phosphorylation of KKT14. Required for mitotic exit and the integrity of the mitotic spindle. Involved in regulation of cytokinesis. Regulates trans-localization of the chromosomal passenger complex (CPC) from the spindle midzone to the dorsal anterior of the cell at the beginning of cytokinesis. Displays autophosphorylation activity and phosphorylates various kinetoplastid kinetochore proteins (KKTs), including KKT1, KKT7 and KKT8. Phosphorylates histone H3. Phosphorylates CPC1, KIN-A and KIN-B. Phosphorylates TLK1 and TKL2.","Serine/threonine kinase that plays a role in the Wnt/beta-catenin signaling pathway by mediating phosphorylation of beta- catenin/CTNN1 on 'Ser-45'. Phosphorylates CTNNB1 at 'Ser-675', 'Ser-677' and 'Ser-679'. Phosphorylation of CTNNB1 at 'Ser-675' and 'Ser-677' leads to its degradation by the proteasome, while phosphorylation at 'Ser-677' and 'Ser-679'",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,0.964,0.964,0.964,0.7186,0.964,5,0.9149,0.6496,yes
AURKB_TRYB2,Q384J7,Protein2Text,Eukaryota,309,"Serine/threonine-protein kinase. Involved in regulation of entrance into mitosis during cell cycle progression. Involved in regulation of chromosome segregation during mitosis. Regulates chromosome biorientation by promoting the establishment of stable bioriented kinetochore-microtubule attachments (Probable). Controls metaphase-to-anaphase transition. Promotes anaphase entry via phosphorylation of KKT14. Required for mitotic exit and the integrity of the mitotic spindle. Involved in regulation of cytokinesis. Regulates trans-localization of the chromosomal passenger complex (CPC) from the spindle midzone to the dorsal anterior of the cell at the beginning of cytokinesis. Displays autophosphorylation activity and phosphorylates various kinetoplastid kinetochore proteins (KKTs), including KKT1, KKT7 and KKT8. Phosphorylates histone H3. Phosphorylates CPC1, KIN-A and KIN-B. Phosphorylates TLK1 and TKL2.",The molecular function of this protein is that it is a serine/threonine-protein kinase.,Maybe,Maybe,Yes,Vague,Maybe,not-Yes,GO:0005524; GO:0106310; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.7186,0.7186,0.7186,0.7186,0.7186,5,0.7186,0.6496,yes
AURKB_TRYB2,Q384J7,Reference,Eukaryota,309,"Serine/threonine-protein kinase. Involved in regulation of entrance into mitosis during cell cycle progression. Involved in regulation of chromosome segregation during mitosis. Regulates chromosome biorientation by promoting the establishment of stable bioriented kinetochore-microtubule attachments (Probable). Controls metaphase-to-anaphase transition. Promotes anaphase entry via phosphorylation of KKT14. Required for mitotic exit and the integrity of the mitotic spindle. Involved in regulation of cytokinesis. Regulates trans-localization of the chromosomal passenger complex (CPC) from the spindle midzone to the dorsal anterior of the cell at the beginning of cytokinesis. Displays autophosphorylation activity and phosphorylates various kinetoplastid kinetochore proteins (KKTs), including KKT1, KKT7 and KKT8. Phosphorylates histone H3. Phosphorylates CPC1, KIN-A and KIN-B. Phosphorylates TLK1 and TKL2.","Serine/threonine-protein kinase. Involved in regulation of entrance into mitosis during cell cycle progression. Involved in regulation of chromosome segregation during mitosis. Regulates chromosome biorientation by promoting the establishment of stable bioriented kinetochore-microtubule attachments (Probable). Controls metaphase-to-anaphase transition. Promotes anaphase entry via phosphorylation of KKT14. Required for mitotic exit and the integrity of the mitotic spindle. Involved in regulation of cytokinesis. Regulates trans-localization of the chromosomal passenger complex (CPC) from the spindle midzone to the dorsal anterior of the cell at the beginning of cytokinesis. Displays autophosphorylation activity and phosphorylates various kinetoplastid kinetochore proteins (KKTs), including KKT1, KKT7 and KKT8. Phosphorylates histone H3. Phosphorylates CPC1, KIN-A and KIN-B. Phosphorylates TLK1 and TKL2.",,,,,,,GO:0005524; GO:0106310; GO:0004674,GO:0004674,GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.7186,0.7186,0.964,0.964,0.964,5,0.8658,0.6496,yes
VANC2_ENTCA,Q47720,ESM2Text,Bacteria,350,"Required for low-level resistance to the glycopeptide antibiotic vancomycin. D-alanine--D-alanine ligase of altered specificity, which catalyzes synthesis of D-Ala-D-Ser; produces a peptidoglycan which does not terminate in D-alanine but in D-serine, thus probably reducing affinity for vancomycin. Only insignificant catalytic synthesis of D-Ala-D-Ala in vitro.",Cell wall formation.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0008716; GO:0160222; GO:0046872,,,,,,,,,,,0,,0.3965,no
VANC2_ENTCA,Q47720,Prot2Text,Bacteria,350,"Required for low-level resistance to the glycopeptide antibiotic vancomycin. D-alanine--D-alanine ligase of altered specificity, which catalyzes synthesis of D-Ala-D-Ser; produces a peptidoglycan which does not terminate in D-alanine but in D-serine, thus probably reducing affinity for vancomycin. Only insignificant catalytic synthesis of D-Ala-D-Ala in vitro.",Cell wall formation.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0008716; GO:0160222; GO:0046872,,,,,,,,,,,0,,0.3965,no
VANC2_ENTCA,Q47720,ProtT3,Bacteria,350,"Required for low-level resistance to the glycopeptide antibiotic vancomycin. D-alanine--D-alanine ligase of altered specificity, which catalyzes synthesis of D-Ala-D-Ser; produces a peptidoglycan which does not terminate in D-alanine but in D-serine, thus probably reducing affinity for vancomycin. Only insignificant catalytic synthesis of D-Ala-D-Ala in vitro.",Cell wall formation. Cytoplasm. Belongs to the D-alanine--D-alanine ligase family,Vague,Vague,Maybe,Vague,Vague,not-Yes,GO:0005524; GO:0008716; GO:0160222; GO:0046872,GO:0008716; GO:0005524,GO:0008716; GO:0005524,GO:0008716; GO:0005524,GO:0008716; GO:0005524,GO:0008716,0.8363,0.8363,0.8363,0.8363,0.5747,5,0.784,0.3965,no
VANC2_ENTCA,Q47720,ProtTale,Bacteria,350,"Required for low-level resistance to the glycopeptide antibiotic vancomycin. D-alanine--D-alanine ligase of altered specificity, which catalyzes synthesis of D-Ala-D-Ser; produces a peptidoglycan which does not terminate in D-alanine but in D-serine, thus probably reducing affinity for vancomycin. Only insignificant catalytic synthesis of D-Ala-D-Ala in vitro.",Cell wall formation.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0008716; GO:0160222; GO:0046872,,,,,,,,,,,0,,0.3965,no
VANC2_ENTCA,Q47720,Protein2Text,Bacteria,350,"Required for low-level resistance to the glycopeptide antibiotic vancomycin. D-alanine--D-alanine ligase of altered specificity, which catalyzes synthesis of D-Ala-D-Ser; produces a peptidoglycan which does not terminate in D-alanine but in D-serine, thus probably reducing affinity for vancomycin. Only insignificant catalytic synthesis of D-Ala-D-Ala in vitro.","The molecular function of this protein is a transferase, specifically a peptide-chain release factor, and it is involved in peptide bond formation. It is part of the bacterial translation machinery and plays a crucial role in protein synthesis.",No,No,No,No,No,not-Yes,GO:0005524; GO:0008716; GO:0160222; GO:0046872,,,,,,,,,,,0,,0.3965,no
VANC2_ENTCA,Q47720,Reference,Bacteria,350,"Required for low-level resistance to the glycopeptide antibiotic vancomycin. D-alanine--D-alanine ligase of altered specificity, which catalyzes synthesis of D-Ala-D-Ser; produces a peptidoglycan which does not terminate in D-alanine but in D-serine, thus probably reducing affinity for vancomycin. Only insignificant catalytic synthesis of D-Ala-D-Ala in vitro.","Required for low-level resistance to the glycopeptide antibiotic vancomycin. D-alanine--D-alanine ligase of altered specificity, which catalyzes synthesis of D-Ala-D-Ser; produces a peptidoglycan which does not terminate in D-alanine but in D-serine, thus probably reducing affinity for vancomycin. Only insignificant catalytic synthesis of D-Ala-D-Ala in vitro.",,,,,,,GO:0005524; GO:0008716; GO:0160222; GO:0046872,GO:0008716,GO:0004058,GO:0008716; GO:0005524,GO:0008716,GO:0008716,0.5747,0.1488,0.8363,0.5747,0.5747,5,0.5418,0.3965,no
CMT1_TRYB2,Q4FKP8,ESM2Text,Eukaryota,324,Recapping enzyme that methylates the guanine N7 position of hypermethylated GpppRNA to regenerate a mature cap structure on decapped mRNA. Can also methylate GpppG and GpppA; the RNA component is not strictly essential for catalysis.,"Spindle-specific RNA methyltransferase that specifically methylates the N(6) position of adenine 2142 in 25S rRNA. In vitro, has also methyltransferase activity toward GA1.",No,Maybe,Maybe,No,Maybe,not-Yes,GO:0008168; GO:0004482; GO:0003723,GO:0008168,GO:0008649,GO:0008173,GO:0008649,GO:0008168,0.6701,0.5006,0.5755,0.5006,0.6701,5,0.5834,0.7372,yes
CMT1_TRYB2,Q4FKP8,Prot2Text,Eukaryota,324,Recapping enzyme that methylates the guanine N7 position of hypermethylated GpppRNA to regenerate a mature cap structure on decapped mRNA. Can also methylate GpppG and GpppA; the RNA component is not strictly essential for catalysis.,Responsible for methylating the 5'-cap structure of mRNAs.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008168; GO:0004482; GO:0003723,GO:0004482,GO:0004482,GO:0004482,GO:0004482,GO:0004482,0.6532,0.6532,0.6532,0.6532,0.6532,5,0.6532,0.7372,yes
CMT1_TRYB2,Q4FKP8,ProtT3,Eukaryota,324,Recapping enzyme that methylates the guanine N7 position of hypermethylated GpppRNA to regenerate a mature cap structure on decapped mRNA. Can also methylate GpppG and GpppA; the RNA component is not strictly essential for catalysis.,mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Nucleus. Belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0 methyltransferase family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008168; GO:0004482; GO:0003723,GO:0004482,GO:0004482,GO:0004482,GO:0004482,GO:0004482,0.6532,0.6532,0.6532,0.6532,0.6532,5,0.6532,0.7372,yes
CMT1_TRYB2,Q4FKP8,ProtTale,Eukaryota,324,Recapping enzyme that methylates the guanine N7 position of hypermethylated GpppRNA to regenerate a mature cap structure on decapped mRNA. Can also methylate GpppG and GpppA; the RNA component is not strictly essential for catalysis.,S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that methylates elongation factor 1-alpha (EF1-alpha) at 'Lys-37'.,No,No,No,No,No,not-Yes,GO:0008168; GO:0004482; GO:0003723,GO:0016279,GO:0008276,GO:0016279,GO:0008276,GO:0016279,0.4368,0.5345,0.4368,0.5345,0.4368,5,0.4759,0.7372,yes
CMT1_TRYB2,Q4FKP8,Protein2Text,Eukaryota,324,Recapping enzyme that methylates the guanine N7 position of hypermethylated GpppRNA to regenerate a mature cap structure on decapped mRNA. Can also methylate GpppG and GpppA; the RNA component is not strictly essential for catalysis.,"This protein is a methyltransferase, specifically a methyltransferase that methylates RNA.
 
Methyltransferases are enzymes that transfer a methyl group from one compound to another. In the case of this protein, it methylates RNA, which means it adds a methyl group to a molecule of RNA. This process can alter the function of the RNA molecule, and is often involved in regulating gene expression.
 
Methyltransferases can be classified into different types based on the type of molecule they methylate. In this case, this protein methylates RNA, so it is a type of RNA methyltransferase.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0008168; GO:0004482; GO:0003723,GO:0008173,GO:0008168,GO:0008168,GO:0008168,GO:0008173,0.5755,0.6701,0.6701,0.6701,0.5755,5,0.6323,0.7372,yes
CMT1_TRYB2,Q4FKP8,Reference,Eukaryota,324,Recapping enzyme that methylates the guanine N7 position of hypermethylated GpppRNA to regenerate a mature cap structure on decapped mRNA. Can also methylate GpppG and GpppA; the RNA component is not strictly essential for catalysis.,Recapping enzyme that methylates the guanine N7 position of hypermethylated GpppRNA to regenerate a mature cap structure on decapped mRNA. Can also methylate GpppG and GpppA; the RNA component is not strictly essential for catalysis.,,,,,,,GO:0008168; GO:0004482; GO:0003723,GO:0004482,GO:0004482,GO:0004482,GO:0008168; GO:0008170,GO:0008168; GO:0008170,0.6532,0.6532,0.6532,0.7256,0.7256,5,0.6822,0.7372,yes
FLAI_SULAC,Q4J9L0,ESM2Text,Archaea,513,"Component of the archaellum. FlaX, FlaH and FlaI form the core cytoplasmic motor complex of the crenarchaeal archaellum. FlaI shows ATPase activity, which provides the energy for both archaellum assembly and rotation. Hydrolyzes ATP with the highest rate, but is also able to hydrolyze GTP, CTP and UTP. Cannot hydrolyze ADP into AMP.","ATPase component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers. Functions as a PilT-dependent retraction ATPase, providing a functional coupling between PilT and the PilU ATPase machinery.",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0005524; GO:0016887; GO:0046872,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887,GO:0016887,GO:0016887,0.8578,0.8578,0.5384,0.5384,0.5384,5,0.6662,0.4492,no
FLAI_SULAC,Q4J9L0,Prot2Text,Archaea,513,"Component of the archaellum. FlaX, FlaH and FlaI form the core cytoplasmic motor complex of the crenarchaeal archaellum. FlaI shows ATPase activity, which provides the energy for both archaellum assembly and rotation. Hydrolyzes ATP with the highest rate, but is also able to hydrolyze GTP, CTP and UTP. Cannot hydrolyze ADP into AMP.",Seems to be required for pilus biogenesis.,Vague,Vague,Vague,Vague,No,not-Yes,GO:0005524; GO:0016887; GO:0046872,,,,,,,,,,,0,,0.4492,no
FLAI_SULAC,Q4J9L0,ProtT3,Archaea,513,"Component of the archaellum. FlaX, FlaH and FlaI form the core cytoplasmic motor complex of the crenarchaeal archaellum. FlaI shows ATPase activity, which provides the energy for both archaellum assembly and rotation. Hydrolyzes ATP with the highest rate, but is also able to hydrolyze GTP, CTP and UTP. Cannot hydrolyze ADP into AMP.",Belongs to the GSP E family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0016887; GO:0046872,,GO:0016887,,,,,0.5384,,,,1,0.5384,0.4492,no
FLAI_SULAC,Q4J9L0,ProtTale,Archaea,513,"Component of the archaellum. FlaX, FlaH and FlaI form the core cytoplasmic motor complex of the crenarchaeal archaellum. FlaI shows ATPase activity, which provides the energy for both archaellum assembly and rotation. Hydrolyzes ATP with the highest rate, but is also able to hydrolyze GTP, CTP and UTP. Cannot hydrolyze ADP into AMP.","ATPase component of the type III secretion system (T3SS), also known as injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells. Acts as a molecular motor to provide the energy that is required for the export of proteins. Required for type III secretion apparatus (T3SA) formation, maintenance and effector protein secretion. May play a role in T3SS substrate recognition.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887; GO:0046872,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887,GO:0016887; GO:0005524,0.8578,0.8578,0.8578,0.5384,0.8578,5,0.7939,0.4492,no
FLAI_SULAC,Q4J9L0,Protein2Text,Archaea,513,"Component of the archaellum. FlaX, FlaH and FlaI form the core cytoplasmic motor complex of the crenarchaeal archaellum. FlaI shows ATPase activity, which provides the energy for both archaellum assembly and rotation. Hydrolyzes ATP with the highest rate, but is also able to hydrolyze GTP, CTP and UTP. Cannot hydrolyze ADP into AMP.",The molecular function of this protein is a DNA polymerase.,No,No,No,No,No,not-Yes,GO:0005524; GO:0016887; GO:0046872,GO:0003887,GO:0003887,GO:0003887,GO:0003887,GO:0003887,0.1027,0.1027,0.1027,0.1027,0.1027,5,0.1027,0.4492,no
FLAI_SULAC,Q4J9L0,Reference,Archaea,513,"Component of the archaellum. FlaX, FlaH and FlaI form the core cytoplasmic motor complex of the crenarchaeal archaellum. FlaI shows ATPase activity, which provides the energy for both archaellum assembly and rotation. Hydrolyzes ATP with the highest rate, but is also able to hydrolyze GTP, CTP and UTP. Cannot hydrolyze ADP into AMP.","Component of the archaellum. FlaX, FlaH and FlaI form the core cytoplasmic motor complex of the crenarchaeal archaellum. FlaI shows ATPase activity, which provides the energy for both archaellum assembly and rotation. Hydrolyzes ATP with the highest rate, but is also able to hydrolyze GTP, CTP and UTP. Cannot hydrolyze ADP into AMP.",,,,,,,GO:0005524; GO:0016887; GO:0046872,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0017111,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.8578,0.8578,0.5951,0.8578,0.8578,5,0.8053,0.4492,no
GLFA_ASPFM,Q4W1X2,ESM2Text,Eukaryota,510,"UDP-galactopyranose mutase, key flavoenzyme of galactofuranose metabolism that catalyzes the 6-to-5 ring contraction of UDP-galactopyranose to UDP-galactofuranose, the donor used by various galacto-furanosyltransferases. Controls the biosynthesis of galactomannan and galactofuranose containing glycoconjugates. The flavin functions as nucleophile, forming a flavin-sugar adduct that facilitates galactose-ring opening and contraction. The binding of UDP-galactopyranose induces profound conformational changes in the enzyme and two loops on opposite sides of the active site move toward each other by over 10 Angstroms to cover the substrate and create a closed active site.",Converts phytoene into zeta-carotene via the intermediary of phytofluene by the symmetrical introduction of two double bonds at the C-11 and C-11' positions of phytoene.,No,No,No,No,No,not-Yes,GO:0000166; GO:0008767,GO:0016491,GO:0016166,GO:0016166,GO:0016166,GO:0016166,0.3276,0.2224,0.2224,0.2224,0.2224,5,0.2434,0.2641,no
GLFA_ASPFM,Q4W1X2,Prot2Text,Eukaryota,510,"UDP-galactopyranose mutase, key flavoenzyme of galactofuranose metabolism that catalyzes the 6-to-5 ring contraction of UDP-galactopyranose to UDP-galactofuranose, the donor used by various galacto-furanosyltransferases. Controls the biosynthesis of galactomannan and galactofuranose containing glycoconjugates. The flavin functions as nucleophile, forming a flavin-sugar adduct that facilitates galactose-ring opening and contraction. The binding of UDP-galactopyranose induces profound conformational changes in the enzyme and two loops on opposite sides of the active site move toward each other by over 10 Angstroms to cover the substrate and create a closed active site.",Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.,No,No,No,No,No,not-Yes,GO:0000166; GO:0008767,GO:0004729,GO:0004729,GO:0004729,GO:0004729,GO:0004729,0.1724,0.1724,0.1724,0.1724,0.1724,5,0.1724,0.2641,no
GLFA_ASPFM,Q4W1X2,ProtT3,Eukaryota,510,"UDP-galactopyranose mutase, key flavoenzyme of galactofuranose metabolism that catalyzes the 6-to-5 ring contraction of UDP-galactopyranose to UDP-galactofuranose, the donor used by various galacto-furanosyltransferases. Controls the biosynthesis of galactomannan and galactofuranose containing glycoconjugates. The flavin functions as nucleophile, forming a flavin-sugar adduct that facilitates galactose-ring opening and contraction. The binding of UDP-galactopyranose induces profound conformational changes in the enzyme and two loops on opposite sides of the active site move toward each other by over 10 Angstroms to cover the substrate and create a closed active site.","Catalyzes the conversion of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto- arabinose (UDP-Ara4O), a precursor of L-fucose. Belongs to the UDP-glucuronic acid 4-keto-arabinose/UDP-N-acetylglucosamine 2-epimerase family",No,No,No,No,No,not-Yes,GO:0000166; GO:0008767,GO:0016831,GO:0042350,GO:0016831,GO:0050378,GO:0016854,0.2224,0.0,0.2224,0.3004,0.4175,5,0.2325,0.2641,no
GLFA_ASPFM,Q4W1X2,ProtTale,Eukaryota,510,"UDP-galactopyranose mutase, key flavoenzyme of galactofuranose metabolism that catalyzes the 6-to-5 ring contraction of UDP-galactopyranose to UDP-galactofuranose, the donor used by various galacto-furanosyltransferases. Controls the biosynthesis of galactomannan and galactofuranose containing glycoconjugates. The flavin functions as nucleophile, forming a flavin-sugar adduct that facilitates galactose-ring opening and contraction. The binding of UDP-galactopyranose induces profound conformational changes in the enzyme and two loops on opposite sides of the active site move toward each other by over 10 Angstroms to cover the substrate and create a closed active site.","Catalyzes the N-hydroxylation of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn), two intermediate metabolites in the biosynthesis of the neurotoxin 3-hydroxykynurenine.",No,No,No,No,No,not-Yes,GO:0000166; GO:0008767,GO:0004502,GO:0016491,GO:0004500,GO:0004497,GO:0004502,0.1759,0.3276,0.1759,0.2654,0.1759,5,0.2241,0.2641,no
GLFA_ASPFM,Q4W1X2,Protein2Text,Eukaryota,510,"UDP-galactopyranose mutase, key flavoenzyme of galactofuranose metabolism that catalyzes the 6-to-5 ring contraction of UDP-galactopyranose to UDP-galactofuranose, the donor used by various galacto-furanosyltransferases. Controls the biosynthesis of galactomannan and galactofuranose containing glycoconjugates. The flavin functions as nucleophile, forming a flavin-sugar adduct that facilitates galactose-ring opening and contraction. The binding of UDP-galactopyranose induces profound conformational changes in the enzyme and two loops on opposite sides of the active site move toward each other by over 10 Angstroms to cover the substrate and create a closed active site.",This protein is involved in the molecular function of converting L-ascorbate into dehydroascorbic acid (DHA). It is a part of the enzyme that catalyzes the oxidation of L-ascorbate to dehydroascorbic acid. This process is crucial for the regeneration of ascorbate in the cell.,No,No,No,No,No,not-Yes,GO:0000166; GO:0008767,GO:0016491,GO:0016491,,GO:0016491,GO:0016491,0.3276,0.3276,,0.3276,0.3276,4,0.3276,0.2641,no
GLFA_ASPFM,Q4W1X2,Reference,Eukaryota,510,"UDP-galactopyranose mutase, key flavoenzyme of galactofuranose metabolism that catalyzes the 6-to-5 ring contraction of UDP-galactopyranose to UDP-galactofuranose, the donor used by various galacto-furanosyltransferases. Controls the biosynthesis of galactomannan and galactofuranose containing glycoconjugates. The flavin functions as nucleophile, forming a flavin-sugar adduct that facilitates galactose-ring opening and contraction. The binding of UDP-galactopyranose induces profound conformational changes in the enzyme and two loops on opposite sides of the active site move toward each other by over 10 Angstroms to cover the substrate and create a closed active site.","UDP-galactopyranose mutase, key flavoenzyme of galactofuranose metabolism that catalyzes the 6-to-5 ring contraction of UDP-galactopyranose to UDP-galactofuranose, the donor used by various galacto-furanosyltransferases. Controls the biosynthesis of galactomannan and galactofuranose containing glycoconjugates. The flavin functions as nucleophile, forming a flavin-sugar adduct that facilitates galactose-ring opening and contraction. The binding of UDP-galactopyranose induces profound conformational changes in the enzyme and two loops on opposite sides of the active site move toward each other by over 10 Angstroms to cover the substrate and create a closed active site.",,,,,,,GO:0000166; GO:0008767,GO:0008767,GO:0008767,GO:0008767; GO:0050660,GO:0050084,GO:0008767,0.7063,0.7063,0.8821,0.1687,0.7063,5,0.6339,0.2641,no
CRH1_ASPFU,Q4WD22,ESM2Text,Eukaryota,357,"Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta- glucan in the cell wall.","Extracellular glycosidase which plays an important role in fungal pathogenesis. Involved in cell wall assembly and regeneration, and adherence to host cells.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008843; GO:0016757,GO:0016798,GO:0004553,GO:0004553,GO:0004553,GO:0016798,0.5611,0.6121,0.6121,0.6121,0.5611,5,0.5917,0.2905,no
CRH1_ASPFU,Q4WD22,Prot2Text,Eukaryota,357,"Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta- glucan in the cell wall.","Extracellular glycosidase which plays an important role in fungal pathogenesis. Involved in cell wall assembly and regeneration, filamentation, and adherence to host cells.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008843; GO:0016757,GO:0004553,GO:0004553,GO:0016798,GO:0004553,GO:0016798,0.6121,0.6121,0.5611,0.6121,0.5611,5,0.5917,0.2905,no
CRH1_ASPFU,Q4WD22,ProtT3,Eukaryota,357,"Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta- glucan in the cell wall.","Plays a role in cell wall synthesis. Secreted, cell wall Membrane; Lipid-anchor, GPI- anchor Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP). Belongs to the glycosyl hydrolase 16 family. CRH1 subfamily",Vague,Vague,Maybe,Vague,Maybe,not-Yes,GO:0008843; GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0042124,GO:0016798,0.7508,0.7508,0.7508,0.4399,0.5611,5,0.6507,0.2905,no
CRH1_ASPFU,Q4WD22,ProtTale,Eukaryota,357,"Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta- glucan in the cell wall.",Cell wall hydrolase that may play a role in cell wall organization and biogenesis.,Vague,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0008843; GO:0016757,GO:0016787,GO:0016787,GO:0016798,GO:0016798,GO:0016787,0.519,0.519,0.5611,0.5611,0.519,5,0.5358,0.2905,no
CRH1_ASPFU,Q4WD22,Protein2Text,Eukaryota,357,"Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta- glucan in the cell wall.","The molecular function of this protein is related to breaking down complex carbohydrates, specifically it is involved in the degradation of plant biomass. It is likely involved in hydrolyzing cellulose, a major component of plant cell walls, into simpler sugars. This protein is probably a beta-glucosidase, an enzyme that catalyzes the final step in cellulose degradation, converting the cellobiose produced by other enzymes into glucose.",No,No,No,No,No,not-Yes,GO:0008843; GO:0016757,GO:0008422,GO:0008422,GO:0008422,GO:0008422,GO:0008422,0.4471,0.4471,0.4471,0.4471,0.4471,5,0.4471,0.2905,no
CRH1_ASPFU,Q4WD22,Reference,Eukaryota,357,"Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta- glucan in the cell wall.","Dual chitinase/transglycosylase that plays a role in cell wall architecture. Chitinase and transglycosylase activities are coupled. Required for the polysaccharide cross-linking at the septa and the cell wall. More specifically, transfers chitin to 1,6-beta- glucan in the cell wall.",,,,,,,GO:0008843; GO:0016757,GO:0004568; GO:0016757,GO:0008810; GO:0016757,GO:0004568; GO:0016757,GO:0004568; GO:0016757,GO:0004568; GO:0016757,0.9346,0.8168,0.9346,0.9346,0.9346,5,0.911,0.2905,no
PMRA_ASPFU,Q4WHC8,ESM2Text,Eukaryota,1061,"Magnesium-dependent enzyme that catalyzes the hydrolysis of ATP coupled with the transport of calcium from the cytosol to the Golgi apparatus lumen. Involved calcium homeostasis and both conidiation and polarized growth. Its activity is coupled to the unfolded protein response (UPR) and Ca(2+) import into the Golgi apparatus is important for virulence, cell wall biosynthesis, and resistance to antifungal compounds that inhibit Ca2+ signaling.",This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the endoplasmic reticulum lumen.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0015410; GO:0005524; GO:0016887; GO:0005509; GO:0005388; GO:0140613,GO:0005388; GO:0005524,GO:0005388; GO:0005524,GO:0005388,GO:0005388,GO:0005388,0.7302,0.7302,0.5254,0.5254,0.5254,5,0.6073,0.5172,no
PMRA_ASPFU,Q4WHC8,Prot2Text,Eukaryota,1061,"Magnesium-dependent enzyme that catalyzes the hydrolysis of ATP coupled with the transport of calcium from the cytosol to the Golgi apparatus lumen. Involved calcium homeostasis and both conidiation and polarized growth. Its activity is coupled to the unfolded protein response (UPR) and Ca(2+) import into the Golgi apparatus is important for virulence, cell wall biosynthesis, and resistance to antifungal compounds that inhibit Ca2+ signaling.",This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Transports the calcium to the vacuole and participates in the control of the cytosolic free calcium.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0015410; GO:0005524; GO:0016887; GO:0005509; GO:0005388; GO:0140613,GO:0005388,GO:0005388,GO:0005388,GO:0005388; GO:0005524; GO:0046872,GO:0005388,0.5254,0.5254,0.5254,0.8138,0.5254,5,0.5831,0.5172,no
PMRA_ASPFU,Q4WHC8,ProtT3,Eukaryota,1061,"Magnesium-dependent enzyme that catalyzes the hydrolysis of ATP coupled with the transport of calcium from the cytosol to the Golgi apparatus lumen. Involved calcium homeostasis and both conidiation and polarized growth. Its activity is coupled to the unfolded protein response (UPR) and Ca(2+) import into the Golgi apparatus is important for virulence, cell wall biosynthesis, and resistance to antifungal compounds that inhibit Ca2+ signaling.",The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses (By similarity). Endoplasmic reticulum membrane; Multi-pass membrane protein. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIA subfamily,No,No,No,No,No,not-Yes,GO:0015410; GO:0005524; GO:0016887; GO:0005509; GO:0005388; GO:0140613,GO:0005524; GO:0015078,GO:0008553,GO:0008553; GO:0005524,GO:0008553,GO:0008553,0.4791,0.4519,0.6653,0.4519,0.4519,5,0.5,0.5172,no
PMRA_ASPFU,Q4WHC8,ProtTale,Eukaryota,1061,"Magnesium-dependent enzyme that catalyzes the hydrolysis of ATP coupled with the transport of calcium from the cytosol to the Golgi apparatus lumen. Involved calcium homeostasis and both conidiation and polarized growth. Its activity is coupled to the unfolded protein response (UPR) and Ca(2+) import into the Golgi apparatus is important for virulence, cell wall biosynthesis, and resistance to antifungal compounds that inhibit Ca2+ signaling.",This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the export of magnesium.,No,No,No,No,No,not-Yes,GO:0015410; GO:0005524; GO:0016887; GO:0005509; GO:0005388; GO:0140613,GO:0016887; GO:0005524,GO:0042626; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.5825,0.5896,0.5825,0.5825,0.5825,5,0.5839,0.5172,no
PMRA_ASPFU,Q4WHC8,Protein2Text,Eukaryota,1061,"Magnesium-dependent enzyme that catalyzes the hydrolysis of ATP coupled with the transport of calcium from the cytosol to the Golgi apparatus lumen. Involved calcium homeostasis and both conidiation and polarized growth. Its activity is coupled to the unfolded protein response (UPR) and Ca(2+) import into the Golgi apparatus is important for virulence, cell wall biosynthesis, and resistance to antifungal compounds that inhibit Ca2+ signaling.","This protein is a magnesium-dependent ATPase, which means it uses magnesium ions to hydrolyze ATP and perform its function. Specifically, it is involved in the transport of magnesium ions across cell membranes, playing a crucial role in maintaining the intracellular magnesium concentration.",No,No,No,No,Maybe,not-Yes,GO:0015410; GO:0005524; GO:0016887; GO:0005509; GO:0005388; GO:0140613,GO:0005524; GO:0016887,GO:0005524; GO:0016887,,GO:0016887,GO:0005524; GO:0015095,0.5825,0.5825,,0.364,0.5043,4,0.5083,0.5172,no
PMRA_ASPFU,Q4WHC8,Reference,Eukaryota,1061,"Magnesium-dependent enzyme that catalyzes the hydrolysis of ATP coupled with the transport of calcium from the cytosol to the Golgi apparatus lumen. Involved calcium homeostasis and both conidiation and polarized growth. Its activity is coupled to the unfolded protein response (UPR) and Ca(2+) import into the Golgi apparatus is important for virulence, cell wall biosynthesis, and resistance to antifungal compounds that inhibit Ca2+ signaling.","Magnesium-dependent enzyme that catalyzes the hydrolysis of ATP coupled with the transport of calcium from the cytosol to the Golgi apparatus lumen. Involved calcium homeostasis and both conidiation and polarized growth. Its activity is coupled to the unfolded protein response (UPR) and Ca(2+) import into the Golgi apparatus is important for virulence, cell wall biosynthesis, and resistance to antifungal compounds that inhibit Ca2+ signaling.",,,,,,,GO:0015410; GO:0005524; GO:0016887; GO:0005509; GO:0005388; GO:0140613,GO:0005388; GO:0005524,GO:0005388; GO:0005524,GO:0005388; GO:0005524,GO:0005388; GO:0005524,GO:0005388; GO:0005524,0.7302,0.7302,0.7302,0.7302,0.7302,5,0.7302,0.5172,no
IREA_ASPFU,Q4WKP8,ESM2Text,Eukaryota,1165,"Senses unfolded proteins in the lumen of the endoplasmic reticulum (ER) via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain responds by cleaving an intron from the downstream cytoplasmic mRNA hacA, allowing for the translation of a transcription factor that coordinates a series of adaptive responses that are collectively known as the unfolded protein response (UPR). In the absence of ER stress, ireA controls dual signaling circuits that are both hacA- dependent and hacA-independent and which contribute to the expression of traits that are essential for virulence.",Phosphorylates the host UDP-glucose in the presence of glucose 6-phosphate.,No,No,No,No,No,not-Yes,GO:0005524; GO:0016787; GO:0046872; GO:0106310; GO:0004674; GO:0004521; GO:0051082,GO:0016301,GO:0016301,,,,0.3601,0.3601,,,,2,0.3601,0.5448,yes
IREA_ASPFU,Q4WKP8,Prot2Text,Eukaryota,1165,"Senses unfolded proteins in the lumen of the endoplasmic reticulum (ER) via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain responds by cleaving an intron from the downstream cytoplasmic mRNA hacA, allowing for the translation of a transcription factor that coordinates a series of adaptive responses that are collectively known as the unfolded protein response (UPR). In the absence of ER stress, ireA controls dual signaling circuits that are both hacA- dependent and hacA-independent and which contribute to the expression of traits that are essential for virulence.","Bifunctional MAP kinase kinase with a regulatory role in the unfolded protein response (UPR) that plays a critical role in the regulation of many cellular processes including cell proliferation, survival, differentiation, migration and apoptosis. Plays an important role in the UPR which is induced by stress, most probably through phosphorylation of the MAPK-signaling pathway.",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0005524; GO:0016787; GO:0046872; GO:0106310; GO:0004674; GO:0004521; GO:0051082,GO:0004708,GO:0004708,GO:0004708,GO:0004708,GO:0004708,0.3592,0.3592,0.3592,0.3592,0.3592,5,0.3592,0.5448,yes
IREA_ASPFU,Q4WKP8,ProtT3,Eukaryota,1165,"Senses unfolded proteins in the lumen of the endoplasmic reticulum (ER) via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain responds by cleaving an intron from the downstream cytoplasmic mRNA hacA, allowing for the translation of a transcription factor that coordinates a series of adaptive responses that are collectively known as the unfolded protein response (UPR). In the absence of ER stress, ireA controls dual signaling circuits that are both hacA- dependent and hacA-independent and which contribute to the expression of traits that are essential for virulence.",Serine/threonine-protein kinase involved in the unfolded protein response (UPR) pathway,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016787; GO:0046872; GO:0106310; GO:0004674; GO:0004521; GO:0051082,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,0.6361,0.6361,0.6361,0.6361,0.4391,5,0.5967,0.5448,yes
IREA_ASPFU,Q4WKP8,ProtTale,Eukaryota,1165,"Senses unfolded proteins in the lumen of the endoplasmic reticulum (ER) via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain responds by cleaving an intron from the downstream cytoplasmic mRNA hacA, allowing for the translation of a transcription factor that coordinates a series of adaptive responses that are collectively known as the unfolded protein response (UPR). In the absence of ER stress, ireA controls dual signaling circuits that are both hacA- dependent and hacA-independent and which contribute to the expression of traits that are essential for virulence.","Serine/threonine-protein kinase involved in the unfolded protein response (UPR) pathway. In response to accumulation of unfolded proteins in the endoplasmic reticulum (ER), phosphorylates Ire1, the transcription factor required for ER stress- induced gene expression. This modification activates Ire1, by promoting its autophosphorylation and increasing its kinase activity. In turn, is activated by phosphorylation of its activation loop.",Maybe,Maybe,Maybe,Yes,Maybe,not-Yes,GO:0005524; GO:0016787; GO:0046872; GO:0106310; GO:0004674; GO:0004521; GO:0051082,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,0.6361,0.6361,0.6361,0.4391,0.6361,5,0.5967,0.5448,yes
IREA_ASPFU,Q4WKP8,Protein2Text,Eukaryota,1165,"Senses unfolded proteins in the lumen of the endoplasmic reticulum (ER) via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain responds by cleaving an intron from the downstream cytoplasmic mRNA hacA, allowing for the translation of a transcription factor that coordinates a series of adaptive responses that are collectively known as the unfolded protein response (UPR). In the absence of ER stress, ireA controls dual signaling circuits that are both hacA- dependent and hacA-independent and which contribute to the expression of traits that are essential for virulence.","The molecular function of this protein is not specified in the provided text. However, based on its name and the context in which it is mentioned, it is likely involved in the regulation of protein folding or modification, possibly in the endoplasmic reticulum (ER) or related pathways.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0005524; GO:0016787; GO:0046872; GO:0106310; GO:0004674; GO:0004521; GO:0051082,,,,,,,,,,,0,,0.5448,yes
IREA_ASPFU,Q4WKP8,Reference,Eukaryota,1165,"Senses unfolded proteins in the lumen of the endoplasmic reticulum (ER) via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain responds by cleaving an intron from the downstream cytoplasmic mRNA hacA, allowing for the translation of a transcription factor that coordinates a series of adaptive responses that are collectively known as the unfolded protein response (UPR). In the absence of ER stress, ireA controls dual signaling circuits that are both hacA- dependent and hacA-independent and which contribute to the expression of traits that are essential for virulence.","Senses unfolded proteins in the lumen of the endoplasmic reticulum (ER) via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain responds by cleaving an intron from the downstream cytoplasmic mRNA hacA, allowing for the translation of a transcription factor that coordinates a series of adaptive responses that are collectively known as the unfolded protein response (UPR). In the absence of ER stress, ireA controls dual signaling circuits that are both hacA- dependent and hacA-independent and which contribute to the expression of traits that are essential for virulence.",,,,,,,GO:0005524; GO:0016787; GO:0046872; GO:0106310; GO:0004674; GO:0004521; GO:0051082,GO:0004521,GO:0004521,GO:0004521,GO:0004521,GO:0004521,0.3533,0.3533,0.3533,0.3533,0.3533,5,0.3533,0.5448,yes
HDMA_ASPFU,Q4WQJ1,ESM2Text,Eukaryota,1081,H3K4 demethylase-like protein. Might not act as a H3K4 demethylase or is not the major H3K4 demethylase since its deletion does not affect whole genome H3K4 methylation.,"Flavoenzyme involved in polyamine back-conversion. Catalyzes the oxidation of the secondary amino group of polyamines, such as spermine and its acetyl derivatives. Substrate preference is spermine > N(1)-acetylspermine > N(1)-acetylspermidine. Plays an important role in the regulation of polyamine intracellular concentration (Probable). Involved in ovulation.",No,No,No,No,Maybe,not-Yes,GO:0003682; GO:0003677; GO:0140682; GO:0050660; GO:0140683; GO:1990841,GO:0016491,GO:0046592,GO:0046592,GO:0046592,GO:0016491,0.292,0.1774,0.1774,0.1774,0.292,5,0.2232,0.2229,no
HDMA_ASPFU,Q4WQJ1,Prot2Text,Eukaryota,1081,H3K4 demethylase-like protein. Might not act as a H3K4 demethylase or is not the major H3K4 demethylase since its deletion does not affect whole genome H3K4 methylation.,"Probable histone demethylase that demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Plays an important role in the differentiation of male gametophytes. Required for the demethylation of the H3 'Lys-9' residue of histone H3 (H3K9me3) to yield H3K9me2.3. Demethylation of Lys residue generates formaldehyde and succinate. Involved in the demethylation of DNA by FANCD2.",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0003682; GO:0003677; GO:0140682; GO:0050660; GO:0140683; GO:1990841,GO:0032452,GO:0032452,GO:0032452,GO:0032453,GO:0032452,0.3412,0.3412,0.3412,0.3625,0.3412,5,0.3455,0.2229,no
HDMA_ASPFU,Q4WQJ1,ProtT3,Eukaryota,1081,H3K4 demethylase-like protein. Might not act as a H3K4 demethylase or is not the major H3K4 demethylase since its deletion does not affect whole genome H3K4 methylation.,L-arginine N(1)- hydroxylase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms,No,No,No,No,No,not-Yes,GO:0003682; GO:0003677; GO:0140682; GO:0050660; GO:0140683; GO:1990841,GO:0016491,GO:0016491,GO:0016709,GO:0004497,GO:0004497,0.292,0.292,0.2455,0.2406,0.2406,5,0.2621,0.2229,no
HDMA_ASPFU,Q4WQJ1,ProtTale,Eukaryota,1081,H3K4 demethylase-like protein. Might not act as a H3K4 demethylase or is not the major H3K4 demethylase since its deletion does not affect whole genome H3K4 methylation.,Histone methyltransferase that trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone.,No,No,No,No,Maybe,not-Yes,GO:0003682; GO:0003677; GO:0140682; GO:0050660; GO:0140683; GO:1990841,GO:0042054,GO:0042054,GO:0018024,GO:0042054,GO:0018024,0.1912,0.1912,0.0,0.1912,0.0,5,0.1147,0.2229,no
HDMA_ASPFU,Q4WQJ1,Protein2Text,Eukaryota,1081,H3K4 demethylase-like protein. Might not act as a H3K4 demethylase or is not the major H3K4 demethylase since its deletion does not affect whole genome H3K4 methylation.,"This protein is involved in the synthesis of a molecule that is essential for the growth and survival of cells. Specifically, it is involved in the synthesis of a molecule that is necessary for the formation of the cell membrane. This protein is a key enzyme in the pathway that produces this molecule, and it plays a crucial role in the cell's ability to synthesize it.",Vague,No,Vague,Vague,No,not-Yes,GO:0003682; GO:0003677; GO:0140682; GO:0050660; GO:0140683; GO:1990841,,,,,,,,,,,0,,0.2229,no
HDMA_ASPFU,Q4WQJ1,Reference,Eukaryota,1081,H3K4 demethylase-like protein. Might not act as a H3K4 demethylase or is not the major H3K4 demethylase since its deletion does not affect whole genome H3K4 methylation.,H3K4 demethylase-like protein. Might not act as a H3K4 demethylase or is not the major H3K4 demethylase since its deletion does not affect whole genome H3K4 methylation.,,,,,,,GO:0003682; GO:0003677; GO:0140682; GO:0050660; GO:0140683; GO:1990841,,,,,,,,,,,0,,0.2229,no
MNT1_ASPFU,Q4WV44,ESM2Text,Eukaryota,400,"Alpha-1,2-mannosyltransferase involved in the elongation of N-glycans and synthesis of the second mannose residue of O-glycans. Catalyzes the transfer of mannose to mannose and alpha-(1,2)-mannobiose as substrates but hardly transfers mannose to alpha-(1,3)-mannobiose or alpha-(1,6)-mannobiose. Transfers the C1-hydroxyl group of the mannose residue from GDP-mannose by dehydration-condensation with the C2-hydroxyl group of the terminal mannose residue. Required for the maintenance of the fungal cell wall and full virulence, but not for the adhesion of conidia to host epithelial cells.","Involved in O-glycosylation of cell wall and secreted proteins. Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage. Mainly responsible for the addition of the second mannose residue. Required for the addition of further mannose residues.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0000026,GO:0000030; GO:0016757,GO:0000030,GO:0000030,GO:0000030,GO:0000030,0.7949,0.8691,0.8691,0.8691,0.8691,5,0.8543,0.5427,yes
MNT1_ASPFU,Q4WV44,Prot2Text,Eukaryota,400,"Alpha-1,2-mannosyltransferase involved in the elongation of N-glycans and synthesis of the second mannose residue of O-glycans. Catalyzes the transfer of mannose to mannose and alpha-(1,2)-mannobiose as substrates but hardly transfers mannose to alpha-(1,3)-mannobiose or alpha-(1,6)-mannobiose. Transfers the C1-hydroxyl group of the mannose residue from GDP-mannose by dehydration-condensation with the C2-hydroxyl group of the terminal mannose residue. Required for the maintenance of the fungal cell wall and full virulence, but not for the adhesion of conidia to host epithelial cells.","Mannosyltransferase involved in O-glycosylation of cell wall and secreted proteins. Plays a major role in extending alpha-1,2-linked mannose in the O-glycan pathway.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0000026,GO:0000030,GO:0000030,GO:0000030,GO:0000030,GO:0000030,0.8691,0.8691,0.8691,0.8691,0.8691,5,0.8691,0.5427,yes
MNT1_ASPFU,Q4WV44,ProtT3,Eukaryota,400,"Alpha-1,2-mannosyltransferase involved in the elongation of N-glycans and synthesis of the second mannose residue of O-glycans. Catalyzes the transfer of mannose to mannose and alpha-(1,2)-mannobiose as substrates but hardly transfers mannose to alpha-(1,3)-mannobiose or alpha-(1,6)-mannobiose. Transfers the C1-hydroxyl group of the mannose residue from GDP-mannose by dehydration-condensation with the C2-hydroxyl group of the terminal mannose residue. Required for the maintenance of the fungal cell wall and full virulence, but not for the adhesion of conidia to host epithelial cells.","Transfers an alpha-D-mannosyl residue from GDP-mannose to a lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage. Golgi apparatus membrane; Single- pass type II membrane protein. Belongs to the glycosyltransferase 15 family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0000026,GO:0000030,GO:0000030,GO:0000030,GO:0000030,GO:0000030,0.8691,0.8691,0.8691,0.8691,0.8691,5,0.8691,0.5427,yes
MNT1_ASPFU,Q4WV44,ProtTale,Eukaryota,400,"Alpha-1,2-mannosyltransferase involved in the elongation of N-glycans and synthesis of the second mannose residue of O-glycans. Catalyzes the transfer of mannose to mannose and alpha-(1,2)-mannobiose as substrates but hardly transfers mannose to alpha-(1,3)-mannobiose or alpha-(1,6)-mannobiose. Transfers the C1-hydroxyl group of the mannose residue from GDP-mannose by dehydration-condensation with the C2-hydroxyl group of the terminal mannose residue. Required for the maintenance of the fungal cell wall and full virulence, but not for the adhesion of conidia to host epithelial cells.",Probable mannosyltransferase involved in O-mannosylation of proteins. Catalyzes the transfer of an alpha-D-mannosyl-1->2 linkage from GDP-beta-D-mannose to serine or threonine residues on proteins.,Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0000026,GO:0000030,GO:0016757,GO:0000030,GO:0004169,GO:0000030,0.8691,0.6466,0.8691,0.6978,0.8691,5,0.7903,0.5427,yes
MNT1_ASPFU,Q4WV44,Protein2Text,Eukaryota,400,"Alpha-1,2-mannosyltransferase involved in the elongation of N-glycans and synthesis of the second mannose residue of O-glycans. Catalyzes the transfer of mannose to mannose and alpha-(1,2)-mannobiose as substrates but hardly transfers mannose to alpha-(1,3)-mannobiose or alpha-(1,6)-mannobiose. Transfers the C1-hydroxyl group of the mannose residue from GDP-mannose by dehydration-condensation with the C2-hydroxyl group of the terminal mannose residue. Required for the maintenance of the fungal cell wall and full virulence, but not for the adhesion of conidia to host epithelial cells.","The molecular function of this protein is a glycosyltransferase, specifically a beta-1,2-glucan synthase, which is involved in the synthesis of beta-1,2-glucan, a type of polysaccharide that is important for cell wall structure and development.",No,No,No,No,Maybe,not-Yes,GO:0000026,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.6466,0.6466,0.6466,0.6466,0.6466,5,0.6466,0.5427,yes
MNT1_ASPFU,Q4WV44,Reference,Eukaryota,400,"Alpha-1,2-mannosyltransferase involved in the elongation of N-glycans and synthesis of the second mannose residue of O-glycans. Catalyzes the transfer of mannose to mannose and alpha-(1,2)-mannobiose as substrates but hardly transfers mannose to alpha-(1,3)-mannobiose or alpha-(1,6)-mannobiose. Transfers the C1-hydroxyl group of the mannose residue from GDP-mannose by dehydration-condensation with the C2-hydroxyl group of the terminal mannose residue. Required for the maintenance of the fungal cell wall and full virulence, but not for the adhesion of conidia to host epithelial cells.","Alpha-1,2-mannosyltransferase involved in the elongation of N-glycans and synthesis of the second mannose residue of O-glycans. Catalyzes the transfer of mannose to mannose and alpha-(1,2)-mannobiose as substrates but hardly transfers mannose to alpha-(1,3)-mannobiose or alpha-(1,6)-mannobiose. Transfers the C1-hydroxyl group of the mannose residue from GDP-mannose by dehydration-condensation with the C2-hydroxyl group of the terminal mannose residue. Required for the maintenance of the fungal cell wall and full virulence, but not for the adhesion of conidia to host epithelial cells.",,,,,,,GO:0000026,GO:0000026,GO:0000030,GO:0000026,GO:0000030,GO:0000030,1.0,0.8691,1.0,0.8691,0.8691,5,0.9215,0.5427,yes
SPFA_ASPFU,Q4WYP6,ESM2Text,Eukaryota,1303,"Endoplasmic reticulum (ER) translocase required to remove mitochondrial transmembrane proteins mistargeted to the endoplasmic reticulum. Acts as a dislocase that mediates the ATP- dependent extraction of mislocalized mitochondrial transmembrane proteins from the endoplasmic reticulum membrane. Works in concert with the ER Ca(2+) pump srcA to support ER homeostasis. With srcA, also supports redox homeostasis and virulence.",Endoplasmic reticulum translocase required to remove mitochondrial transmembrane proteins mistargeted to the endoplasmic reticulum. Acts as a dislocase that mediates the ATP-dependent extraction of mislocalized mitochondrial transmembrane proteins from the endoplasmic reticulum membrane. Specifically binds unfolded protein substrates with short polypeptides and contributes to the assembly of the glycoprotein scaffold. Required for normal glycosylation and mitochondrial function.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0019829; GO:0140567; GO:0046872; GO:0015662,GO:0016887; GO:0005524,GO:0016887,GO:0016887,GO:0016887,GO:0016887,0.6194,0.4028,0.4028,0.4028,0.4028,5,0.4461,0.521,no
SPFA_ASPFU,Q4WYP6,Prot2Text,Eukaryota,1303,"Endoplasmic reticulum (ER) translocase required to remove mitochondrial transmembrane proteins mistargeted to the endoplasmic reticulum. Acts as a dislocase that mediates the ATP- dependent extraction of mislocalized mitochondrial transmembrane proteins from the endoplasmic reticulum membrane. Works in concert with the ER Ca(2+) pump srcA to support ER homeostasis. With srcA, also supports redox homeostasis and virulence.",(Microbial infection) Facilitates Venezuelan equine encephalitis virus (VEEV) replication.,No,No,No,No,No,not-Yes,GO:0005524; GO:0016887; GO:0019829; GO:0140567; GO:0046872; GO:0015662,,,,,,,,,,,0,,0.521,no
SPFA_ASPFU,Q4WYP6,ProtT3,Eukaryota,1303,"Endoplasmic reticulum (ER) translocase required to remove mitochondrial transmembrane proteins mistargeted to the endoplasmic reticulum. Acts as a dislocase that mediates the ATP- dependent extraction of mislocalized mitochondrial transmembrane proteins from the endoplasmic reticulum membrane. Works in concert with the ER Ca(2+) pump srcA to support ER homeostasis. With srcA, also supports redox homeostasis and virulence.",This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the vacuole. Vacuole membrane; Multi-pass membrane protein. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily,No,No,No,No,No,not-Yes,GO:0005524; GO:0016887; GO:0019829; GO:0140567; GO:0046872; GO:0015662,GO:0005388; GO:0005524,GO:0005388; GO:0005524,GO:0005388; GO:0005524,GO:0005388,GO:0005388,0.6084,0.6084,0.6084,0.3822,0.3822,5,0.5179,0.521,no
SPFA_ASPFU,Q4WYP6,ProtTale,Eukaryota,1303,"Endoplasmic reticulum (ER) translocase required to remove mitochondrial transmembrane proteins mistargeted to the endoplasmic reticulum. Acts as a dislocase that mediates the ATP- dependent extraction of mislocalized mitochondrial transmembrane proteins from the endoplasmic reticulum membrane. Works in concert with the ER Ca(2+) pump srcA to support ER homeostasis. With srcA, also supports redox homeostasis and virulence.",Mitochondrial zinc transporter that mediates zinc uptake from the cytosol to the mitochondrial matrix to maintain mitochondrial calcium homeostasis. Plays an important role in maintaining the integrity of the mitochondrial outer membrane and mitochondrial function.,No,No,No,No,No,not-Yes,GO:0005524; GO:0016887; GO:0019829; GO:0140567; GO:0046872; GO:0015662,GO:0005385,GO:0005385,GO:0005385,GO:0005385,GO:0005385,0.2014,0.2014,0.2014,0.2014,0.2014,5,0.2014,0.521,no
SPFA_ASPFU,Q4WYP6,Protein2Text,Eukaryota,1303,"Endoplasmic reticulum (ER) translocase required to remove mitochondrial transmembrane proteins mistargeted to the endoplasmic reticulum. Acts as a dislocase that mediates the ATP- dependent extraction of mislocalized mitochondrial transmembrane proteins from the endoplasmic reticulum membrane. Works in concert with the ER Ca(2+) pump srcA to support ER homeostasis. With srcA, also supports redox homeostasis and virulence.","The molecular function of this protein is a magnesium-dependent enzyme that converts ATP into its pyrophosphate form, and subsequently hydrolyzes the pyrophosphate into two phosphate ions.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016887; GO:0019829; GO:0140567; GO:0046872; GO:0015662,,GO:0016887,,GO:0016462,GO:0016462,,0.4028,,0.2692,0.2692,3,0.3137,0.521,no
SPFA_ASPFU,Q4WYP6,Reference,Eukaryota,1303,"Endoplasmic reticulum (ER) translocase required to remove mitochondrial transmembrane proteins mistargeted to the endoplasmic reticulum. Acts as a dislocase that mediates the ATP- dependent extraction of mislocalized mitochondrial transmembrane proteins from the endoplasmic reticulum membrane. Works in concert with the ER Ca(2+) pump srcA to support ER homeostasis. With srcA, also supports redox homeostasis and virulence.","Endoplasmic reticulum (ER) translocase required to remove mitochondrial transmembrane proteins mistargeted to the endoplasmic reticulum. Acts as a dislocase that mediates the ATP- dependent extraction of mislocalized mitochondrial transmembrane proteins from the endoplasmic reticulum membrane. Works in concert with the ER Ca(2+) pump srcA to support ER homeostasis. With srcA, also supports redox homeostasis and virulence.",,,,,,,GO:0005524; GO:0016887; GO:0019829; GO:0140567; GO:0046872; GO:0015662,GO:0016887; GO:0005524,GO:0016887,GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.6194,0.4028,0.4028,0.6194,0.6194,5,0.5328,0.521,no
RASB_ASPFU,Q4X241,ESM2Text,Eukaryota,239,Ras-like protein involved in the activation of Ras protein signal transduction. Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays a role in hyphal morphology and conidiophore development. Required for full virulence.,Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0003925; GO:0019003; GO:0005525; GO:0003924,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924,GO:0003924,0.9431,0.9431,0.9431,0.5808,0.5808,5,0.7982,0.4738,no
RASB_ASPFU,Q4X241,Prot2Text,Eukaryota,239,Ras-like protein involved in the activation of Ras protein signal transduction. Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays a role in hyphal morphology and conidiophore development. Required for full virulence.,Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0003925; GO:0019003; GO:0005525; GO:0003924,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924,0.9431,0.9431,0.9431,0.9431,0.5808,5,0.8706,0.4738,no
RASB_ASPFU,Q4X241,ProtT3,Eukaryota,239,Ras-like protein involved in the activation of Ras protein signal transduction. Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays a role in hyphal morphology and conidiophore development. Required for full virulence.,Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Cell membrane; Lipid-anchor; Cytoplasmic side. Belongs to the small GTPase superfamily. Ras family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003925; GO:0019003; GO:0005525; GO:0003924,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,0.9431,0.9431,0.9431,0.9431,0.9431,5,0.9431,0.4738,no
RASB_ASPFU,Q4X241,ProtTale,Eukaryota,239,Ras-like protein involved in the activation of Ras protein signal transduction. Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays a role in hyphal morphology and conidiophore development. Required for full virulence.,"Plasma membrane-associated GTPase that cycles between an active GTP-bound and an inactive GDP-bound state. Binds to phosphatidylinositol 4,5-bisphosphate (PIP2), but not to phosphatidylinositol 3,4,5-trisphosphate (PIP3).",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0003925; GO:0019003; GO:0005525; GO:0003924,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,0.9431,0.9431,0.9431,0.9431,0.9431,5,0.9431,0.4738,no
RASB_ASPFU,Q4X241,Protein2Text,Eukaryota,239,Ras-like protein involved in the activation of Ras protein signal transduction. Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays a role in hyphal morphology and conidiophore development. Required for full virulence.,"The molecular function of this protein is that it is a GTPase, which means it is involved in the regulation of cellular signaling pathways by binding and hydrolyzing GTP.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0003925; GO:0019003; GO:0005525; GO:0003924,GO:0003924,GO:0003924,GO:0003924,GO:0003924,GO:0003924,0.5808,0.5808,0.5808,0.5808,0.5808,5,0.5808,0.4738,no
RASB_ASPFU,Q4X241,Reference,Eukaryota,239,Ras-like protein involved in the activation of Ras protein signal transduction. Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays a role in hyphal morphology and conidiophore development. Required for full virulence.,Ras-like protein involved in the activation of Ras protein signal transduction. Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays a role in hyphal morphology and conidiophore development. Required for full virulence.,,,,,,,GO:0003925; GO:0019003; GO:0005525; GO:0003924,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0005525; GO:0003924,0.9431,0.9431,0.9431,0.9431,0.9431,5,0.9431,0.4738,no
TSOXG_CORS9,Q50LE9,ESM2Text,Bacteria,205,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.","Involved in the anaerobic fermentation of lysine. Catalyzes the oxidative deamination of L-erythro-erythro-CoA to produce the final L-arabinose unit. It can use NAD, NADP or NADH as electron donor, but NAD is preferred.",No,No,No,No,No,not-Yes,GO:0008115,GO:0016491,GO:0008115,GO:0008115,GO:0008115,GO:0008115,0.6019,1.0,1.0,1.0,1.0,5,0.9204,0.6712,yes
TSOXG_CORS9,Q50LE9,Prot2Text,Bacteria,205,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.",One of at least two accessory proteins for anaerobic nitric oxide (NO) reductase. Reduces the rubredoxin moiety of NO reductase.,No,No,No,No,No,not-Yes,GO:0008115,GO:0030058,GO:0008115,GO:0030730,GO:0030058,GO:0008115,0.3987,1.0,0.0,0.3987,1.0,5,0.5595,0.6712,yes
TSOXG_CORS9,Q50LE9,ProtT3,Bacteria,205,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.",Catalyzes the degradation of L-fumarate. Cytoplasm. Belongs to the fumarate reductase family,No,No,No,No,No,not-Yes,GO:0008115,GO:0008115,GO:0008115,GO:0008115,GO:0030730,GO:0008115,1.0,1.0,1.0,0.0,1.0,5,0.8,0.6712,yes
TSOXG_CORS9,Q50LE9,ProtTale,Bacteria,205,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.",NifH is the target protein of the anaerobic pathway for nitrogen fixation. It is required for the reduction of fixed N2 to ammonia (Probable).,No,No,No,No,No,not-Yes,GO:0008115,GO:0016163,GO:0016163; GO:0005524,GO:0016163,,GO:0016163; GO:0005524,0.3386,0.2443,0.3386,,0.2443,4,0.2914,0.6712,yes
TSOXG_CORS9,Q50LE9,Protein2Text,Bacteria,205,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.","The molecular function of this protein is involved in the biosynthesis of nicotinate-nucleotide, which is a crucial step in the NAD+ salvage pathway.",No,No,No,No,No,not-Yes,GO:0008115,,GO:0016491,,GO:0008743,GO:0016491,,0.6019,,0.3386,0.6019,3,0.5141,0.6712,yes
TSOXG_CORS9,Q50LE9,Reference,Bacteria,205,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.","In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.",,,,,,,GO:0008115,GO:0008115,GO:0008115,GO:0008115,GO:0030058; GO:0016491,GO:0008115; GO:0016491,1.0,1.0,1.0,0.5342,0.8673,5,0.8803,0.6712,yes
TSOXA_CORS9,Q50LF0,ESM2Text,Bacteria,965,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.","Catalyzes the oxidative demethylation of sarcosine to yield glycine, hydrogen peroxide and 5,10-methylenetetrahydrofolate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0000166; GO:0008115,GO:0016491,GO:0008115,GO:0008115,GO:0008115,GO:0008115,0.4575,0.7013,0.7013,0.7013,0.7013,5,0.6525,0.2411,no
TSOXA_CORS9,Q50LF0,Prot2Text,Bacteria,965,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.","Catalyzes the oxidative demethylation of sarcosine to yield glycine, hydrogen peroxide and 5,10-methylenetetrahydrofolate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0000166; GO:0008115,GO:0030058,GO:0008115,GO:0030730,GO:0030058,GO:0008115,0.3054,0.7013,0.0,0.3054,0.7013,5,0.4027,0.2411,no
TSOXA_CORS9,Q50LF0,ProtT3,Bacteria,965,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.",Catalyzes the oxidation of trimethylamine-N-oxide (TMAO) to trimethylamine (TMA) and hydrogen peroxide. Cytoplasm. Belongs to the GcvT family,No,No,No,Maybe,Maybe,not-Yes,GO:0000166; GO:0008115,GO:0008115,GO:0008115,GO:0008115,GO:0030730,GO:0008115,0.7013,0.7013,0.7013,0.0,0.7013,5,0.561,0.2411,no
TSOXA_CORS9,Q50LF0,ProtTale,Bacteria,965,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.",Catalyzes the dehydration of trans-3-hydroxy-L-proline (t3LHyp) and trans-4-hydroxy-L-proline (t4LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Also acts on cis-3-hydroxy-L-proline (c3LHyp) and cis-4-hydroxy-L-proline (c4LHyp).,No,No,No,No,No,not-Yes,GO:0000166; GO:0008115,GO:0016829,GO:0016829,GO:0016836,GO:0016829,GO:0016836,0.293,0.293,0.1965,0.293,0.1965,5,0.2544,0.2411,no
TSOXA_CORS9,Q50LF0,Protein2Text,Bacteria,965,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.","This protein is a component of the electron transfer flavoprotein (ETF) complex, which is involved in the transfer of electrons from the FAD-containing flavoproteins to the mitochondrial respiratory chain. The molecular function of this protein is likely to be a structural or catalytic role within the ETF complex, possibly involving the transfer of electrons or the stabilization of the complex.",Vague,No,No,No,No,not-Yes,GO:0000166; GO:0008115,,GO:0016491,,GO:0008743,GO:0016491,,0.4575,,0.2604,0.4575,3,0.3918,0.2411,no
TSOXA_CORS9,Q50LF0,Reference,Bacteria,965,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.","In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.",,,,,,,GO:0000166; GO:0008115,GO:0008115,GO:0008115,GO:0008115,GO:0030058; GO:0016491,GO:0008115; GO:0016491,0.7013,0.7013,0.7013,0.4428,0.6926,5,0.6479,0.2411,no
TSOXD_CORS9,Q50LF1,ESM2Text,Bacteria,99,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.","Antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the toxic effect of cognate toxin YopC. Unlike most type II TA systems, neutralizes the toxic effect of non-cognate toxins YopC and AvrRptA.",No,No,No,No,No,not-Yes,GO:0046872; GO:0008115,GO:0016491,GO:0008115,GO:0008115,GO:0008115,GO:0008115,0.4539,0.6963,0.6963,0.6963,0.6963,5,0.6478,0.5025,no
TSOXD_CORS9,Q50LF1,Prot2Text,Bacteria,99,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.",Methylates the carbon-mercury bond of organomercurials such as phenylmercuric acetate. Acts on organomercurials such as acetate with a degree of polymerization (DP) of 3 or 4. The carbon-mercury bond is proposed to be involved in stabilization of the coproporphyrin-X-phosphorylhydrolyzing pigment complex.,No,No,No,No,No,not-Yes,GO:0046872; GO:0008115,GO:0030058,GO:0008115,GO:0030730,GO:0030058,GO:0008115,0.3006,0.6963,0.0,0.3006,0.6963,5,0.3988,0.5025,no
TSOXD_CORS9,Q50LF1,ProtT3,Bacteria,99,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.","Catalyzes the oxidative demethylation of sarcosine to yield glycine, hydrogen peroxide and 5,10-methylenetetrahydrofolate. Cytoplasm. Belongs to the FMO family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0008115,GO:0008115,GO:0008115,GO:0008115,GO:0030730,GO:0008115,0.6963,0.6963,0.6963,0.0,0.6963,5,0.557,0.5025,no
TSOXD_CORS9,Q50LF1,ProtTale,Bacteria,99,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.",This protein may be the iron-sulfur (Fe-S) protein component of a ferredoxin reductase.,No,No,No,No,No,not-Yes,GO:0046872; GO:0008115,,,GO:0009055; GO:0051536,,,,,0.302,,,1,0.302,0.5025,no
TSOXD_CORS9,Q50LF1,Protein2Text,Bacteria,99,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.","The molecular function of this protein is not explicitly stated in the provided information. However, based on its classification as a ""protein"" and its involvement in a biological process, it is likely that this protein plays a role in catalyzing a chemical reaction, such as the transfer of a methyl group or the reduction of a molecule. Further research would be necessary to determine the specific molecular function of this protein.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0046872; GO:0008115,,GO:0016491,,GO:0008743,GO:0016491,,0.4539,,0.2554,0.4539,3,0.3877,0.5025,no
TSOXD_CORS9,Q50LF1,Reference,Bacteria,99,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.","In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.",,,,,,,GO:0046872; GO:0008115,GO:0008115,GO:0008115,GO:0008115,GO:0030058; GO:0016491,GO:0008115; GO:0016491,0.6963,0.6963,0.6963,0.4401,0.6899,5,0.6438,0.5025,no
TSOXB_CORS9,Q50LF2,ESM2Text,Bacteria,405,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.","Catalyzes the oxidative demethylation of sarcosine to yield glycine, hydrogen peroxide and 5,10-methylenetetrahydrofolate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0000166; GO:0008115,GO:0016491,GO:0008115,GO:0008115,GO:0008115,GO:0008115,0.4575,0.7013,0.7013,0.7013,0.7013,5,0.6525,0.0931,no
TSOXB_CORS9,Q50LF2,Prot2Text,Bacteria,405,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.","Catalyzes the oxidative demethylation of sarcosine to yield glycine, hydrogen peroxide and 5,10-methylenetetrahydrofolate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0000166; GO:0008115,GO:0030058,GO:0008115,GO:0030730,GO:0030058,GO:0008115,0.3054,0.7013,0.0,0.3054,0.7013,5,0.4027,0.0931,no
TSOXB_CORS9,Q50LF2,ProtT3,Bacteria,405,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.","Catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10-methylenetetrahydrofolate and 5,10-methenyltetrahydrofolate. Cytoplasm. Belongs to the sarcosine oxidase family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0000166; GO:0008115,GO:0008115,GO:0008115,GO:0008115,GO:0030730,GO:0008115,0.7013,0.7013,0.7013,0.0,0.7013,5,0.561,0.0931,no
TSOXB_CORS9,Q50LF2,ProtTale,Bacteria,405,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.",The cytochrome b551 component of the succinate dehydrogenase (SDH) complex catalyzes the transfer of electrons from succinate to the flavoprotein subunit SDH of the complex. The complex is involved in the electron transfer between the mitochondrial respiratory chain and the oxidative phosphorylation system.,No,No,No,No,No,not-Yes,GO:0000166; GO:0008115,GO:0009055,GO:0009055,GO:0009055; GO:0000104,GO:0016491,GO:0009055,0.2097,0.2097,0.3053,0.4575,0.2097,5,0.2784,0.0931,no
TSOXB_CORS9,Q50LF2,Protein2Text,Bacteria,405,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.",This protein is involved in the molecular function of catalyzing the oxidation of L-threonine to 2-aminobutyraldehyde. It is a part of the L-threonine degradation pathway.,No,No,No,No,No,not-Yes,GO:0000166; GO:0008115,,GO:0016491,,GO:0008743,GO:0016491,,0.4575,,0.2604,0.4575,3,0.3918,0.0931,no
TSOXB_CORS9,Q50LF2,Reference,Bacteria,405,"In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.","In the presence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, 5,10- methylenetetrahydrofolate and hydrogen peroxide. In the absence of tetrahydrofolate, catalyzes the oxidative demethylation of sarcosine to yield glycine, formaldehyde and hydrogen peroxide. Can also use N- methyl-L-alanine and N-ethyl-L-glycine. Is very specific for oxygen as an acceptor.",,,,,,,GO:0000166; GO:0008115,GO:0008115,GO:0008115,GO:0008115,GO:0030058; GO:0016491,GO:0008115; GO:0016491,0.7013,0.7013,0.7013,0.4428,0.6926,5,0.6479,0.0931,no
POLS_SAV3,Q53AM4,ESM2Text,Viruses,1319,"[Capsid protein]: Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers. The capsid protein binds to the viral RNA genome at a site adjacent to a ribosome binding site for viral genome translation following genome release. Possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein. Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosahedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of the spike glycoprotein E2 at the cell membrane, leading to budding and formation of mature virions. In case of infection, new virions attach to target cells and after clathrin- mediated endocytosis their membrane fuses with the host endosomal membrane. This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible. The uncoating might be triggered by the interaction of capsid proteins with ribosomes. Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding. Specifically inhibits interleukin-1 receptor-associated kinase 1/IRAK1-dependent signaling during viral entry, representing a means by which the alphaviruses may evade innate immune detection and activation prior to viral gene expression.",Plays a role in signal transduction. Required during eye development for the correct formation of the lens intermediate filaments as part of a complex containing retinal proteins and the transcription factor RIM101.,No,No,No,No,No,not-Yes,GO:0015267; GO:0003723; GO:0004252; GO:0005198,,,,,,,,,,,0,,0.4732,no
POLS_SAV3,Q53AM4,Prot2Text,Viruses,1319,"[Capsid protein]: Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers. The capsid protein binds to the viral RNA genome at a site adjacent to a ribosome binding site for viral genome translation following genome release. Possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein. Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosahedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of the spike glycoprotein E2 at the cell membrane, leading to budding and formation of mature virions. In case of infection, new virions attach to target cells and after clathrin- mediated endocytosis their membrane fuses with the host endosomal membrane. This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible. The uncoating might be triggered by the interaction of capsid proteins with ribosomes. Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding. Specifically inhibits interleukin-1 receptor-associated kinase 1/IRAK1-dependent signaling during viral entry, representing a means by which the alphaviruses may evade innate immune detection and activation prior to viral gene expression.",Plays a role in signal transduction. Required during eye development for the correct formation of the lens intermediate filaments as part of a complex containing retinal proteins and the transcription factor RIM101.,No,No,No,No,No,not-Yes,GO:0015267; GO:0003723; GO:0004252; GO:0005198,,,,,,,,,,,0,,0.4732,no
POLS_SAV3,Q53AM4,ProtT3,Viruses,1319,"[Capsid protein]: Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers. The capsid protein binds to the viral RNA genome at a site adjacent to a ribosome binding site for viral genome translation following genome release. Possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein. Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosahedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of the spike glycoprotein E2 at the cell membrane, leading to budding and formation of mature virions. In case of infection, new virions attach to target cells and after clathrin- mediated endocytosis their membrane fuses with the host endosomal membrane. This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible. The uncoating might be triggered by the interaction of capsid proteins with ribosomes. Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding. Specifically inhibits interleukin-1 receptor-associated kinase 1/IRAK1-dependent signaling during viral entry, representing a means by which the alphaviruses may evade innate immune detection and activation prior to viral gene expression.","[Capsid protein VP1]: Forms an icosahedral capsid with a T=1 symmetry, about 30 nm in diameter, and consisting of 60 copies of each VP1, VP2, VP3, and VP4 proteins. The capsid encapsulates the genomic dsRNA (By similarity). [Capsid protein VP2]: Forms an icosahedral capsid with a T=1 symmetry, about 30 nm in diameter, and consisting of 60 copies of each VP1, VP2, VP3, and VP4 proteins. The capsid encapsulates",Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0015267; GO:0003723; GO:0004252; GO:0005198,,,GO:0005198,GO:0005198,,,,0.5324,0.5324,,2,0.5324,0.4732,no
POLS_SAV3,Q53AM4,ProtTale,Viruses,1319,"[Capsid protein]: Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers. The capsid protein binds to the viral RNA genome at a site adjacent to a ribosome binding site for viral genome translation following genome release. Possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein. Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosahedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of the spike glycoprotein E2 at the cell membrane, leading to budding and formation of mature virions. In case of infection, new virions attach to target cells and after clathrin- mediated endocytosis their membrane fuses with the host endosomal membrane. This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible. The uncoating might be triggered by the interaction of capsid proteins with ribosomes. Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding. Specifically inhibits interleukin-1 receptor-associated kinase 1/IRAK1-dependent signaling during viral entry, representing a means by which the alphaviruses may evade innate immune detection and activation prior to viral gene expression.",[Capsid protein]: Forms an icosahedral capsid with a T=4 symmetry composed of 240 trimers of the capsid protein. The capsid encapsulates the genomic dsRNA. Nucleocapsid protein is involved in the attachment of the virus to host cell. It also plays a role in the formation of ribonucleoprotein complexes.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0015267; GO:0003723; GO:0004252; GO:0005198,,,GO:0005198,,GO:0005198,,,0.5324,,0.5324,2,0.5324,0.4732,no
POLS_SAV3,Q53AM4,Protein2Text,Viruses,1319,"[Capsid protein]: Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers. The capsid protein binds to the viral RNA genome at a site adjacent to a ribosome binding site for viral genome translation following genome release. Possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein. Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosahedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of the spike glycoprotein E2 at the cell membrane, leading to budding and formation of mature virions. In case of infection, new virions attach to target cells and after clathrin- mediated endocytosis their membrane fuses with the host endosomal membrane. This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible. The uncoating might be triggered by the interaction of capsid proteins with ribosomes. Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding. Specifically inhibits interleukin-1 receptor-associated kinase 1/IRAK1-dependent signaling during viral entry, representing a means by which the alphaviruses may evade innate immune detection and activation prior to viral gene expression.",This protein is a protease.,No,No,No,Vague,No,not-Yes,GO:0015267; GO:0003723; GO:0004252; GO:0005198,GO:0008233,GO:0008233,GO:0008233,GO:0008233,GO:0008233,0.3658,0.3658,0.3658,0.3658,0.3658,5,0.3658,0.4732,no
POLS_SAV3,Q53AM4,Reference,Viruses,1319,"[Capsid protein]: Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers. The capsid protein binds to the viral RNA genome at a site adjacent to a ribosome binding site for viral genome translation following genome release. Possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein. Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosahedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of the spike glycoprotein E2 at the cell membrane, leading to budding and formation of mature virions. In case of infection, new virions attach to target cells and after clathrin- mediated endocytosis their membrane fuses with the host endosomal membrane. This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible. The uncoating might be triggered by the interaction of capsid proteins with ribosomes. Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding. Specifically inhibits interleukin-1 receptor-associated kinase 1/IRAK1-dependent signaling during viral entry, representing a means by which the alphaviruses may evade innate immune detection and activation prior to viral gene expression.","[Capsid protein]: Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers. The capsid protein binds to the viral RNA genome at a site adjacent to a ribosome binding site for viral genome translation following genome release. Possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein. Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosahedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of the spike glycoprotein E2 at the cell membrane, leading to budding and formation of mature virions. In case of infection, new virions attach to target cells and after clathrin- mediated endocytosis their membrane fuses with the host endosomal membrane. This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible. The uncoating might be triggered by the interaction of capsid proteins with ribosomes. Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding. Specifically inhibits interleukin-1 receptor-associated kinase 1/IRAK1-dependent signaling during viral entry, representing a means by which the alphaviruses may evade innate immune detection and activation prior to viral gene expression.",,,,,,,GO:0015267; GO:0003723; GO:0004252; GO:0005198,GO:0004252; GO:0003723,GO:0003723; GO:0008236,GO:0004252; GO:0003723,GO:0004197,GO:0004197,0.737,0.6796,0.737,0.3125,0.3125,5,0.5557,0.4732,no
DESD_LIMPL,Q54795,ESM2Text,Bacteria,368,"Desaturase involved in fatty acid biosynthesis. Introduces a double bond at carbon 6 of linoleoyl group (18:2) attached to the sn-1 position of the glycerol moiety of membrane glycerolipids, leading to the formation of gamma-linolenic acid (GLA).",Fatty acid desaturase that introduces a cis-double bond at the 5-position in 20-carbon polyunsaturated fatty acids incorporated in a phospholipid that contain a Delta(8) double bond.,Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016717,GO:0016491,GO:0016717,GO:0016717,GO:0016491,GO:0016717,0.6897,1.0,1.0,0.6897,1.0,5,0.8759,0.3329,no
DESD_LIMPL,Q54795,Prot2Text,Bacteria,368,"Desaturase involved in fatty acid biosynthesis. Introduces a double bond at carbon 6 of linoleoyl group (18:2) attached to the sn-1 position of the glycerol moiety of membrane glycerolipids, leading to the formation of gamma-linolenic acid (GLA).",Fatty acid desaturase that introduces a cis double bond at the 5-position in 20-carbon polyunsaturated fatty acids incorporated in a glycerolipid that contain a Delta(8) double bond.,Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016717,GO:0016717,,GO:0016717,GO:0006636,GO:0016215,1.0,,1.0,0.0,0.8582,4,0.7146,0.3329,no
DESD_LIMPL,Q54795,ProtT3,Bacteria,368,"Desaturase involved in fatty acid biosynthesis. Introduces a double bond at carbon 6 of linoleoyl group (18:2) attached to the sn-1 position of the glycerol moiety of membrane glycerolipids, leading to the formation of gamma-linolenic acid (GLA).",Membrane; Multi-pass membrane protein. Belongs to the fatty acid desaturase type 1 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016717,GO:0016491,GO:0016717,GO:0016717,GO:0016717,GO:0016717,0.6897,1.0,1.0,1.0,1.0,5,0.9379,0.3329,no
DESD_LIMPL,Q54795,ProtTale,Bacteria,368,"Desaturase involved in fatty acid biosynthesis. Introduces a double bond at carbon 6 of linoleoyl group (18:2) attached to the sn-1 position of the glycerol moiety of membrane glycerolipids, leading to the formation of gamma-linolenic acid (GLA).","Fatty acid desaturase that introduces a cis double bond at the 4-position in 18-carbon polyunsaturated fatty acids that contain a delta-15 double bond to produce 20-carbon polyunsaturated fatty acids that contain a delta-16 double bond. Involved in the production of the essential fatty acids eicosapentaenoic acid (EPA, 20:5(n-3)) and docosahexaenoic acid (DHA, 22:6(n-3)).",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016717,GO:0016491,GO:0016491,GO:0016717,GO:0045300,GO:0016717,0.6897,0.6897,1.0,0.8582,1.0,5,0.8475,0.3329,no
DESD_LIMPL,Q54795,Protein2Text,Bacteria,368,"Desaturase involved in fatty acid biosynthesis. Introduces a double bond at carbon 6 of linoleoyl group (18:2) attached to the sn-1 position of the glycerol moiety of membrane glycerolipids, leading to the formation of gamma-linolenic acid (GLA).","This protein is a fatty acid desaturase, specifically a fatty acid delta-9 desaturase, which catalyzes the insertion of a double bond into the 9th position of fatty acids. This enzyme is involved in the biosynthesis of polyunsaturated fatty acids (PUFAs) from saturated fatty acids. It catalyzes the conversion of oleic acid (C18:1(9)) to linoleic acid (C18:2(9,12)) and alpha-linolenic acid (C18:3(9,12,15)) to linolenic acid (C18:3(9,12,15)). The molecular function of this protein is to introduce a double bond into the 9th carbon of the fatty acid chain, resulting in the production of unsaturated fatty acids. This is an essential step in the biosynthesis of PUFAs, which are crucial for various cellular processes, including membrane fluidity, energy storage, and signaling. The molecular function of this protein is also related to the regulation of fatty acid composition in cellular membranes, which is essential for maintaining membrane structure and function. 

In summary, the molecular function of this protein is to catalyze the insertion of a double bond into the 9th position of fatty acids, resulting in the production of unsaturated fatty acids, which are essential for various cellular processes.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016717,GO:0006636,GO:0006636; GO:0016717,GO:0004768,GO:0004768,GO:0016717,0.0,0.6667,0.7539,0.7539,1.0,5,0.6349,0.3329,no
DESD_LIMPL,Q54795,Reference,Bacteria,368,"Desaturase involved in fatty acid biosynthesis. Introduces a double bond at carbon 6 of linoleoyl group (18:2) attached to the sn-1 position of the glycerol moiety of membrane glycerolipids, leading to the formation of gamma-linolenic acid (GLA).","Desaturase involved in fatty acid biosynthesis. Introduces a double bond at carbon 6 of linoleoyl group (18:2) attached to the sn-1 position of the glycerol moiety of membrane glycerolipids, leading to the formation of gamma-linolenic acid (GLA).",,,,,,,GO:0016717,GO:0016717,GO:0016717,GO:0016717,GO:0016717,GO:0016717,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3329,no
CAPDH_SYNY3,Q55131,ESM2Text,Bacteria,398,"Dehydrogenase involved in the biosynthesis of spermidine via the carboxyaminopropylagmatine (CAPA) pathway. Catalyzes the reductive condensation of agmatine and L-aspartate-beta- semialdehyde (ASA) into CAPA. Shows activity toward putrescine and 1,3-diaminopropane, but the catalytic efficiency is three to four orders of magnitude lower than that for agmatine. Cannot use cadaverine or spermidine.","Involved in the degradation of the pyridine ring of trigonelline (TG; N-methylnicotinate) into succinate and methylamine as carbon and nitrogen sources, respectively. The presence of NAD(+) and alpha-ketoglutarate changes the substrate specificity, but the preference for NAD(+) for NAD(+) is much higher.",No,No,No,No,No,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,,1.0,1.0,1.0,1.0,,4,1.0,0.208,no
CAPDH_SYNY3,Q55131,Prot2Text,Bacteria,398,"Dehydrogenase involved in the biosynthesis of spermidine via the carboxyaminopropylagmatine (CAPA) pathway. Catalyzes the reductive condensation of agmatine and L-aspartate-beta- semialdehyde (ASA) into CAPA. Shows activity toward putrescine and 1,3-diaminopropane, but the catalytic efficiency is three to four orders of magnitude lower than that for agmatine. Cannot use cadaverine or spermidine.","Involved in norspermidine biosynthesis. Catalyzes the synthesis of carboxynorspermidine from L-aspartate 4-semialdehyde and 1,3-diaminopropane. Is also slightly active with putrescine as a substrate.",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0016491,GO:0016491,,GO:0016491,GO:0016740,GO:0016491,1.0,,1.0,0.5902,1.0,4,0.8975,0.208,no
CAPDH_SYNY3,Q55131,ProtT3,Bacteria,398,"Dehydrogenase involved in the biosynthesis of spermidine via the carboxyaminopropylagmatine (CAPA) pathway. Catalyzes the reductive condensation of agmatine and L-aspartate-beta- semialdehyde (ASA) into CAPA. Shows activity toward putrescine and 1,3-diaminopropane, but the catalytic efficiency is three to four orders of magnitude lower than that for agmatine. Cannot use cadaverine or spermidine.","Catalyzes the formation of N-succinyl-2-amino-6-oxopimelate, from succinyl-CoA and D-2-amino-6-oxopimelate. Can also use succinyl-CoA and L-2-amino-6-oxopimelate, but not L-2-amino-6-oxopimelate and D-2-amino-6-oxopimelate. Belongs to the saccharopine dehydrogenase family",No,No,No,No,Maybe,not-Yes,GO:0016491,GO:0016746,GO:0008666,GO:0016746,GO:0016747,GO:0016746,0.4807,0.264,0.4807,0.4071,0.4807,5,0.4226,0.208,no
CAPDH_SYNY3,Q55131,ProtTale,Bacteria,398,"Dehydrogenase involved in the biosynthesis of spermidine via the carboxyaminopropylagmatine (CAPA) pathway. Catalyzes the reductive condensation of agmatine and L-aspartate-beta- semialdehyde (ASA) into CAPA. Shows activity toward putrescine and 1,3-diaminopropane, but the catalytic efficiency is three to four orders of magnitude lower than that for agmatine. Cannot use cadaverine or spermidine.","Involved in the degradation of (S)-2,3-butanediol. Catalyzes the NAD(P)H-dependent reduction of 4-hydroxybenzoate (4HB) to 1,2-dihydroxy-3-methylbutanoate (DHMB). Can also use 3-hydroxybenzoate (3HB) and 2-hydroxybenzoate (2HB) as substrates.",No,No,No,No,No,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.208,no
CAPDH_SYNY3,Q55131,Protein2Text,Bacteria,398,"Dehydrogenase involved in the biosynthesis of spermidine via the carboxyaminopropylagmatine (CAPA) pathway. Catalyzes the reductive condensation of agmatine and L-aspartate-beta- semialdehyde (ASA) into CAPA. Shows activity toward putrescine and 1,3-diaminopropane, but the catalytic efficiency is three to four orders of magnitude lower than that for agmatine. Cannot use cadaverine or spermidine.","This protein is involved in catalyzing a reaction. Specifically, it catalyzes the conversion of succinyl-CoA to succinate and CoA, which is a key step in the citric acid cycle. The molecular function of this protein is to act as a succinyl-CoA synthetase, which is a type of enzyme that plays a crucial role in energy metabolism.",No,No,No,No,No,not-Yes,GO:0016491,GO:0004775,GO:0004775,GO:0004775,GO:0004775,GO:0004775,0.3176,0.3176,0.3176,0.3176,0.3176,5,0.3176,0.208,no
CAPDH_SYNY3,Q55131,Reference,Bacteria,398,"Dehydrogenase involved in the biosynthesis of spermidine via the carboxyaminopropylagmatine (CAPA) pathway. Catalyzes the reductive condensation of agmatine and L-aspartate-beta- semialdehyde (ASA) into CAPA. Shows activity toward putrescine and 1,3-diaminopropane, but the catalytic efficiency is three to four orders of magnitude lower than that for agmatine. Cannot use cadaverine or spermidine.","Dehydrogenase involved in the biosynthesis of spermidine via the carboxyaminopropylagmatine (CAPA) pathway. Catalyzes the reductive condensation of agmatine and L-aspartate-beta- semialdehyde (ASA) into CAPA. Shows activity toward putrescine and 1,3-diaminopropane, but the catalytic efficiency is three to four orders of magnitude lower than that for agmatine. Cannot use cadaverine or spermidine.",,,,,,,GO:0016491,,GO:0016491,GO:0016491,GO:0016491; GO:0050661,GO:0016491,,1.0,1.0,0.7089,1.0,4,0.9272,0.208,no
CGM1_TRYB2,Q57V03,ESM2Text,Eukaryota,1050,"Bifunctional capping enzyme with guanylyltransferase and methyltransferase activities; transfers GMP to spliced leader (SL) RNA via a covalent enzyme-GMP intermediate and methylates the guanine N7 position of the GpppRNA to form the cap 0 structure. Required for cap 4 methylation, as cap 0 appears to be a prerequisite for subsequent methylation events. Associates with SL RNA genes. Essential for parasite survival.",Methylates the N-terminal methionine residues of proteins.,No,No,No,No,No,not-Yes,GO:0004482; GO:0003723,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.405,0.405,0.405,0.405,0.405,5,0.405,0.2785,no
CGM1_TRYB2,Q57V03,Prot2Text,Eukaryota,1050,"Bifunctional capping enzyme with guanylyltransferase and methyltransferase activities; transfers GMP to spliced leader (SL) RNA via a covalent enzyme-GMP intermediate and methylates the guanine N7 position of the GpppRNA to form the cap 0 structure. Required for cap 4 methylation, as cap 0 appears to be a prerequisite for subsequent methylation events. Associates with SL RNA genes. Essential for parasite survival.",Responsible for methylating the 5'-cap structure of mRNAs.,Maybe,Maybe,Maybe,Yes,Maybe,not-Yes,GO:0004482; GO:0003723,GO:0004482,GO:0004482,GO:0004482,GO:0004482,GO:0004482,0.6927,0.6927,0.6927,0.6927,0.6927,5,0.6927,0.2785,no
CGM1_TRYB2,Q57V03,ProtT3,Eukaryota,1050,"Bifunctional capping enzyme with guanylyltransferase and methyltransferase activities; transfers GMP to spliced leader (SL) RNA via a covalent enzyme-GMP intermediate and methylates the guanine N7 position of the GpppRNA to form the cap 0 structure. Required for cap 4 methylation, as cap 0 appears to be a prerequisite for subsequent methylation events. Associates with SL RNA genes. Essential for parasite survival.",Responsible for methylation of the 5'-cap structure of mRNAs. Nucleus. Belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0 methyltransferase family,Maybe,Maybe,Maybe,Yes,Maybe,not-Yes,GO:0004482; GO:0003723,GO:0004482,GO:0004482,GO:0004482,GO:0004482,GO:0004482,0.6927,0.6927,0.6927,0.6927,0.6927,5,0.6927,0.2785,no
CGM1_TRYB2,Q57V03,ProtTale,Eukaryota,1050,"Bifunctional capping enzyme with guanylyltransferase and methyltransferase activities; transfers GMP to spliced leader (SL) RNA via a covalent enzyme-GMP intermediate and methylates the guanine N7 position of the GpppRNA to form the cap 0 structure. Required for cap 4 methylation, as cap 0 appears to be a prerequisite for subsequent methylation events. Associates with SL RNA genes. Essential for parasite survival.",Phosphorylates histone H3 to form H3S10ph. Is required for normal development of the central nervous system (CNS).,No,No,No,No,No,not-Yes,GO:0004482; GO:0003723,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,0.1758,0.1758,0.1758,0.1602,0.1758,5,0.1727,0.2785,no
CGM1_TRYB2,Q57V03,Protein2Text,Eukaryota,1050,"Bifunctional capping enzyme with guanylyltransferase and methyltransferase activities; transfers GMP to spliced leader (SL) RNA via a covalent enzyme-GMP intermediate and methylates the guanine N7 position of the GpppRNA to form the cap 0 structure. Required for cap 4 methylation, as cap 0 appears to be a prerequisite for subsequent methylation events. Associates with SL RNA genes. Essential for parasite survival.","This protein is involved in DNA repair, specifically in removing lesions in DNA.",No,No,No,No,No,not-Yes,GO:0004482; GO:0003723,,,,,,,,,,,0,,0.2785,no
CGM1_TRYB2,Q57V03,Reference,Eukaryota,1050,"Bifunctional capping enzyme with guanylyltransferase and methyltransferase activities; transfers GMP to spliced leader (SL) RNA via a covalent enzyme-GMP intermediate and methylates the guanine N7 position of the GpppRNA to form the cap 0 structure. Required for cap 4 methylation, as cap 0 appears to be a prerequisite for subsequent methylation events. Associates with SL RNA genes. Essential for parasite survival.","Bifunctional capping enzyme with guanylyltransferase and methyltransferase activities; transfers GMP to spliced leader (SL) RNA via a covalent enzyme-GMP intermediate and methylates the guanine N7 position of the GpppRNA to form the cap 0 structure. Required for cap 4 methylation, as cap 0 appears to be a prerequisite for subsequent methylation events. Associates with SL RNA genes. Essential for parasite survival.",,,,,,,GO:0004482; GO:0003723,GO:0004484; GO:0004482,GO:0004484; GO:0004482,GO:0004484; GO:0004482,GO:0004484; GO:0008168,GO:0004484; GO:0008168,0.6072,0.6072,0.6072,0.3863,0.3863,5,0.5188,0.2785,no
REH2_TRYB2,Q581T1,ESM2Text,Eukaryota,2167,"ATP-dependent RNA helicase that unwinds RNA in a 3' to 5' direction and that plays an important role in mitochondrial mRNA editing, a process involving the addition and deletion of uridine (U) nucleotides in the pre-mRNA. As part of the RET2-containing gRNA-binding (RET2- GRBC) complex, acts as a scaffold for the assembly of mRNA-gRNA hybrids and the recruitment of the RNA editing core (RECC) complex. Regulates several steps of mRNA editing by the MRBC3010/GRBC6 containing gRNA-binding (MRBC3010-GRBC) complex including loading of unedited mRNA, editing in the first sequence block and subsequent editing progression across multiple sequence blocks. Also, regulates the RNA substrate content of the MRBC3010-GRBC complex as well as the association of this complex with mitoribosomes.",ATP-dependent RNA helicase that unwinds RNA in a 3' to 5' direction and that plays a role in mitochondrial mRNA editing.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0034458; GO:0005524; GO:0004386; GO:0016787; GO:0003729; GO:0003723,GO:0003724; GO:0005524,GO:0004004; GO:0003723,GO:0004004,GO:0004004,GO:0004004,0.6526,0.74,0.4507,0.4507,0.4507,5,0.5489,0.5283,no
REH2_TRYB2,Q581T1,Prot2Text,Eukaryota,2167,"ATP-dependent RNA helicase that unwinds RNA in a 3' to 5' direction and that plays an important role in mitochondrial mRNA editing, a process involving the addition and deletion of uridine (U) nucleotides in the pre-mRNA. As part of the RET2-containing gRNA-binding (RET2- GRBC) complex, acts as a scaffold for the assembly of mRNA-gRNA hybrids and the recruitment of the RNA editing core (RECC) complex. Regulates several steps of mRNA editing by the MRBC3010/GRBC6 containing gRNA-binding (MRBC3010-GRBC) complex including loading of unedited mRNA, editing in the first sequence block and subsequent editing progression across multiple sequence blocks. Also, regulates the RNA substrate content of the MRBC3010-GRBC complex as well as the association of this complex with mitoribosomes.","ATP-dependent RNA helicase that unwinds RNA in a 3' to 5' direction and that plays important roles in many processes such as mRNA export, non-homologous end-joining (NHEJ), end-joining and RNA-directed DNA methylation (RdDM). Involved in the assembly of cytoplasmic RNA-directed DNA methylation (DmDM) machinery and in the maturation of specific RNA processing particles such as pre-ribosomal RNA (rRNA) and small nucleolar RNA (snoRNA). Required for the assembly of cytoplasmic RNA-directed DNA methylation (CRD) machinery at the RNA polymerase II subunit rRNA-mediated transcriptional silencing (TGS) at the inner repeat (IR) site. Required for the assembly of a functional pre-ribosome-directed DNA methylation (RdDM) machinery at the RNA polymerase II subunit rRNA-mediated transcriptional silencing (TGS) at the RNA polymerase II subunit rRNA-mediated transcriptional silencing (RITS). Involved in the assembly of a functional pre-ribosome-directed DNA methylation (RdDM) machinery",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0034458; GO:0005524; GO:0004386; GO:0016787; GO:0003729; GO:0003723,GO:0004004,GO:0004004,GO:0003724,GO:0003724; GO:0005524,GO:0004004,0.4507,0.4507,0.4507,0.6526,0.4507,5,0.4911,0.5283,no
REH2_TRYB2,Q581T1,ProtT3,Eukaryota,2167,"ATP-dependent RNA helicase that unwinds RNA in a 3' to 5' direction and that plays an important role in mitochondrial mRNA editing, a process involving the addition and deletion of uridine (U) nucleotides in the pre-mRNA. As part of the RET2-containing gRNA-binding (RET2- GRBC) complex, acts as a scaffold for the assembly of mRNA-gRNA hybrids and the recruitment of the RNA editing core (RECC) complex. Regulates several steps of mRNA editing by the MRBC3010/GRBC6 containing gRNA-binding (MRBC3010-GRBC) complex including loading of unedited mRNA, editing in the first sequence block and subsequent editing progression across multiple sequence blocks. Also, regulates the RNA substrate content of the MRBC3010-GRBC complex as well as the association of this complex with mitoribosomes.",RNA-binding protein that binds to mitochondrial 16S rRNA (16S mt-rRNA) . May play a role in the regulation of mitochondrial translation . Mitochondrion. Belongs to the RSF2 family,No,No,Maybe,No,Maybe,not-Yes,GO:0034458; GO:0005524; GO:0004386; GO:0016787; GO:0003729; GO:0003723,GO:0003723,GO:0003723,GO:0003723,GO:0003723,GO:0003723,0.4923,0.4923,0.4923,0.4923,0.4923,5,0.4923,0.5283,no
REH2_TRYB2,Q581T1,ProtTale,Eukaryota,2167,"ATP-dependent RNA helicase that unwinds RNA in a 3' to 5' direction and that plays an important role in mitochondrial mRNA editing, a process involving the addition and deletion of uridine (U) nucleotides in the pre-mRNA. As part of the RET2-containing gRNA-binding (RET2- GRBC) complex, acts as a scaffold for the assembly of mRNA-gRNA hybrids and the recruitment of the RNA editing core (RECC) complex. Regulates several steps of mRNA editing by the MRBC3010/GRBC6 containing gRNA-binding (MRBC3010-GRBC) complex including loading of unedited mRNA, editing in the first sequence block and subsequent editing progression across multiple sequence blocks. Also, regulates the RNA substrate content of the MRBC3010-GRBC complex as well as the association of this complex with mitoribosomes.","Probable ATP-binding RNA helicase which plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons.",Maybe,Maybe,Yes,No,Maybe,not-Yes,GO:0034458; GO:0005524; GO:0004386; GO:0016787; GO:0003729; GO:0003723,GO:0003724; GO:0005524,GO:0003724; GO:0005524,GO:0003724; GO:0005524,GO:0004386; GO:0005524,GO:0003724; GO:0005524,0.6526,0.6526,0.6526,0.6741,0.6526,5,0.6569,0.5283,no
REH2_TRYB2,Q581T1,Protein2Text,Eukaryota,2167,"ATP-dependent RNA helicase that unwinds RNA in a 3' to 5' direction and that plays an important role in mitochondrial mRNA editing, a process involving the addition and deletion of uridine (U) nucleotides in the pre-mRNA. As part of the RET2-containing gRNA-binding (RET2- GRBC) complex, acts as a scaffold for the assembly of mRNA-gRNA hybrids and the recruitment of the RNA editing core (RECC) complex. Regulates several steps of mRNA editing by the MRBC3010/GRBC6 containing gRNA-binding (MRBC3010-GRBC) complex including loading of unedited mRNA, editing in the first sequence block and subsequent editing progression across multiple sequence blocks. Also, regulates the RNA substrate content of the MRBC3010-GRBC complex as well as the association of this complex with mitoribosomes.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its classification as a protein, it is likely to be involved in catalyzing a specific biochemical reaction, such as the synthesis or breakdown of a particular molecule.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0034458; GO:0005524; GO:0004386; GO:0016787; GO:0003729; GO:0003723,,,,,,,,,,,0,,0.5283,no
REH2_TRYB2,Q581T1,Reference,Eukaryota,2167,"ATP-dependent RNA helicase that unwinds RNA in a 3' to 5' direction and that plays an important role in mitochondrial mRNA editing, a process involving the addition and deletion of uridine (U) nucleotides in the pre-mRNA. As part of the RET2-containing gRNA-binding (RET2- GRBC) complex, acts as a scaffold for the assembly of mRNA-gRNA hybrids and the recruitment of the RNA editing core (RECC) complex. Regulates several steps of mRNA editing by the MRBC3010/GRBC6 containing gRNA-binding (MRBC3010-GRBC) complex including loading of unedited mRNA, editing in the first sequence block and subsequent editing progression across multiple sequence blocks. Also, regulates the RNA substrate content of the MRBC3010-GRBC complex as well as the association of this complex with mitoribosomes.","ATP-dependent RNA helicase that unwinds RNA in a 3' to 5' direction and that plays an important role in mitochondrial mRNA editing, a process involving the addition and deletion of uridine (U) nucleotides in the pre-mRNA. As part of the RET2-containing gRNA-binding (RET2- GRBC) complex, acts as a scaffold for the assembly of mRNA-gRNA hybrids and the recruitment of the RNA editing core (RECC) complex. Regulates several steps of mRNA editing by the MRBC3010/GRBC6 containing gRNA-binding (MRBC3010-GRBC) complex including loading of unedited mRNA, editing in the first sequence block and subsequent editing progression across multiple sequence blocks. Also, regulates the RNA substrate content of the MRBC3010-GRBC complex as well as the association of this complex with mitoribosomes.",,,,,,,GO:0034458; GO:0005524; GO:0004386; GO:0016787; GO:0003729; GO:0003723,GO:0004004; GO:0003723; GO:0005524,GO:0003724; GO:0005524,GO:0004386; GO:0003723; GO:0005524,GO:0004386; GO:0005524; GO:0003723,GO:0004386; GO:0005524; GO:0003723,0.8617,0.6526,0.8808,0.8808,0.8808,5,0.8313,0.5283,no
CET1_TRYB2,Q582T2,ESM2Text,Eukaryota,253,First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end (Probable). Required for parasite growth.,Disrupting the ure1-type of the promoter inhibits the initiation of spermatogenesis probably by acting as a negative regulator of the ure1-type ATPase.,No,No,No,No,No,not-Yes,GO:0016887; GO:0003924; GO:0140818; GO:0004651; GO:0017111,,,,,,,,,,,0,,0.3091,no
CET1_TRYB2,Q582T2,Prot2Text,Eukaryota,253,First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end (Probable). Required for parasite growth.,"E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. Ubiquitination leads to vcp/p97 recruitment for extraction and degradation of the incomplete translation product.",No,No,No,No,No,not-Yes,GO:0016887; GO:0003924; GO:0140818; GO:0004651; GO:0017111,GO:0004842,GO:0061630,GO:0061630,GO:0061630,GO:0004842,0.1679,0.1371,0.1371,0.1371,0.1679,5,0.1494,0.3091,no
CET1_TRYB2,Q582T2,ProtT3,Eukaryota,253,First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end (Probable). Required for parasite growth.,Probable 5'-triphosphate endoribonuclease. Nucleus. Belongs to the 5'-triphosphate endoribonuclease family,Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0016887; GO:0003924; GO:0140818; GO:0004651; GO:0017111,GO:0004521,GO:0004521,GO:0004521,GO:0004521,GO:0004521,0.2252,0.2252,0.2252,0.2252,0.2252,5,0.2252,0.3091,no
CET1_TRYB2,Q582T2,ProtTale,Eukaryota,253,First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end (Probable). Required for parasite growth.,"Key component of the mRNA export machinery that functions as a adapter between the nuclear pore complex (NPC) and an mRNA transporter of unknown specificity. Required for proper assembly and function of the Nup98/160-cargo complex, which is essential for efficient transport of mRNAs across the NPC. Promotes binding of the Nup98/160-cargo complex to mRNAs: binds to the Nup98/160-NPC interface via its N-terminal nucleoporin (Nup) domain, and to mRNAs via its C-terminal RNA-binding domain. Involved in",No,No,No,No,No,not-Yes,GO:0016887; GO:0003924; GO:0140818; GO:0004651; GO:0017111,,GO:0003723,GO:0003723,,GO:0003723,,0.1134,0.1134,,0.1134,3,0.1134,0.3091,no
CET1_TRYB2,Q582T2,Protein2Text,Eukaryota,253,First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end (Probable). Required for parasite growth.,The molecular function of this protein is a nucleoside diphosphate kinase. It is involved in the synthesis of nucleoside triphosphates from their corresponding diphosphate precursors.,No,No,No,No,No,not-Yes,GO:0016887; GO:0003924; GO:0140818; GO:0004651; GO:0017111,GO:0004550,GO:0004550,GO:0004550,GO:0004550,GO:0004550,0.1456,0.1456,0.1456,0.1456,0.1456,5,0.1456,0.3091,no
CET1_TRYB2,Q582T2,Reference,Eukaryota,253,First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end (Probable). Required for parasite growth.,First step of mRNA capping. Converts the 5'-triphosphate end of a nascent mRNA chain into a diphosphate end (Probable). Required for parasite growth.,,,,,,,GO:0016887; GO:0003924; GO:0140818; GO:0004651; GO:0017111,GO:0004651,,GO:0004651,GO:0004651,GO:0004651,0.491,,0.491,0.491,0.491,4,0.491,0.3091,no
CLS_TRYB2,Q584D1,ESM2Text,Eukaryota,639,Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions.,Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008808,GO:0016740,GO:0008808,GO:0008808,GO:0008808,GO:0008808,0.5381,1.0,1.0,1.0,1.0,5,0.9076,0.2365,no
CLS_TRYB2,Q584D1,Prot2Text,Eukaryota,639,Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions.,"Hydrolyzes membrane phospholipids, such as PtdCho (phosphatidylcholine), producing the free headgroup and PtdOH (phosphatidic acid; signaling molecule on its own).",No,No,No,No,No,not-Yes,GO:0008808,GO:0004630,GO:0004630,GO:0004630,GO:0004622,GO:0004630,0.1197,0.1197,0.1197,0.1134,0.1197,5,0.1184,0.2365,no
CLS_TRYB2,Q584D1,ProtT3,Eukaryota,639,Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions.,Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. Mitochondrion inner membrane; Multi-pass membrane protein. Belongs to the phospholipase D family. Cardiolipin synthase subfamily,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008808,GO:0016780,GO:0008808,GO:0008808,GO:0008808,GO:0008808,0.7539,1.0,1.0,1.0,1.0,5,0.9508,0.2365,no
CLS_TRYB2,Q584D1,ProtTale,Eukaryota,639,Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions.,Involved in phosphatidylglycerol biosynthesis. Catalyzes the transfer of the phosphatidylglycerol moiety from phosphatidylglycerol phosphate (PGP) to the 1-OH group of the sn-2 acyl group of glycerol-3-phosphate.,No,No,No,No,No,not-Yes,GO:0008808,GO:0016740,GO:0016740,GO:0016740,GO:0016740,GO:0016740,0.5381,0.5381,0.5381,0.5381,0.5381,5,0.5381,0.2365,no
CLS_TRYB2,Q584D1,Protein2Text,Eukaryota,639,Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions.,"This protein is involved in the molecular function of catalyzing the hydrolysis of a phosphodiester bond. Specifically, it is a phospholipase that catalyzes the hydrolysis of phospholipids.",No,No,No,Maybe,Maybe,not-Yes,GO:0008808,GO:0004622,GO:0004623,GO:0004620,,GO:0004622,0.1134,0.1383,0.1493,,0.1134,4,0.1286,0.2365,no
CLS_TRYB2,Q584D1,Reference,Eukaryota,639,Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions.,Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions.,,,,,,,GO:0008808,GO:0008808,GO:0004140,GO:0008808,GO:0008808,GO:0008808,1.0,0.4029,1.0,1.0,1.0,5,0.8806,0.2365,no
FKP_BACFG,Q58T34,ESM2Text,Bacteria,949,"Bifunctional enzyme involved in the salvage pathway of GDP- fucose synthesis. Catalyzes two successive reactions, the ATP-dependent phosphorylation of L-fucose to L-fucose 1-phosphate, and its guanylylation to GDP-L-fucose. GDP-fucose is an important fucose donor in the process of fucosylated oligosaccharides formation.","Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate. Can also use the non-phosphorylated analogs D-fructose and D-mannitol, with lower efficiency.",No,No,Maybe,No,No,not-Yes,GO:0005524; GO:0050201; GO:0047341,GO:0004340,GO:0004340,GO:0004340,GO:0004396,GO:0004340,0.4156,0.4156,0.4156,0.4606,0.4156,5,0.4246,0.2999,no
FKP_BACFG,Q58T34,Prot2Text,Bacteria,949,"Bifunctional enzyme involved in the salvage pathway of GDP- fucose synthesis. Catalyzes two successive reactions, the ATP-dependent phosphorylation of L-fucose to L-fucose 1-phosphate, and its guanylylation to GDP-L-fucose. GDP-fucose is an important fucose donor in the process of fucosylated oligosaccharides formation.","Catalyzes the phosphorylation of mevalonate 5-phosphate (MVAP) to yield mevalonate 5-phosphate-3-deoxyribose 1-phosphate (MPR). Functions in an alternative mevalonate pathway, only present in extreme acidophiles of the Thermoplasmatales order, which passes through mevalonate 5-phosphate rather than mevalonate 5-phosphate.",No,No,No,No,No,not-Yes,GO:0005524; GO:0050201; GO:0047341,GO:0004631,GO:0004631,GO:0004631,GO:0004672,GO:0004631,0.4133,0.4133,0.4133,0.4765,0.4133,5,0.4259,0.2999,no
FKP_BACFG,Q58T34,ProtT3,Bacteria,949,"Bifunctional enzyme involved in the salvage pathway of GDP- fucose synthesis. Catalyzes two successive reactions, the ATP-dependent phosphorylation of L-fucose to L-fucose 1-phosphate, and its guanylylation to GDP-L-fucose. GDP-fucose is an important fucose donor in the process of fucosylated oligosaccharides formation.",Catalyzes the phosphorylation of D-glucosamine (GlcN) to GlcN-6-P. Belongs to the GHMP kinase family. GlcNK subfamily,No,No,No,No,No,not-Yes,GO:0005524; GO:0050201; GO:0047341,GO:0016301; GO:0005524,GO:0016773,GO:0016301; GO:0005524,GO:0016301; GO:0005524,GO:0016301,0.8142,0.5336,0.8142,0.8142,0.5336,5,0.702,0.2999,no
FKP_BACFG,Q58T34,ProtTale,Bacteria,949,"Bifunctional enzyme involved in the salvage pathway of GDP- fucose synthesis. Catalyzes two successive reactions, the ATP-dependent phosphorylation of L-fucose to L-fucose 1-phosphate, and its guanylylation to GDP-L-fucose. GDP-fucose is an important fucose donor in the process of fucosylated oligosaccharides formation.",Phosphorylates dihydroxyacetonephosphate (DHAP) to phosphoglycerate.,No,No,No,No,No,not-Yes,GO:0005524; GO:0050201; GO:0047341,GO:0016301,GO:0016301; GO:0005524,GO:0016301,GO:0016301,GO:0016301,0.5336,0.8142,0.5336,0.5336,0.5336,5,0.5897,0.2999,no
FKP_BACFG,Q58T34,Protein2Text,Bacteria,949,"Bifunctional enzyme involved in the salvage pathway of GDP- fucose synthesis. Catalyzes two successive reactions, the ATP-dependent phosphorylation of L-fucose to L-fucose 1-phosphate, and its guanylylation to GDP-L-fucose. GDP-fucose is an important fucose donor in the process of fucosylated oligosaccharides formation.","The molecular function of the protein is an enzyme, specifically an aldolase.",No,No,No,No,No,not-Yes,GO:0005524; GO:0050201; GO:0047341,GO:0004332,GO:0004332,,GO:0016832,GO:0004332,0.1475,0.1475,,0.1731,0.1475,4,0.1539,0.2999,no
FKP_BACFG,Q58T34,Reference,Bacteria,949,"Bifunctional enzyme involved in the salvage pathway of GDP- fucose synthesis. Catalyzes two successive reactions, the ATP-dependent phosphorylation of L-fucose to L-fucose 1-phosphate, and its guanylylation to GDP-L-fucose. GDP-fucose is an important fucose donor in the process of fucosylated oligosaccharides formation.","Bifunctional enzyme involved in the salvage pathway of GDP- fucose synthesis. Catalyzes two successive reactions, the ATP-dependent phosphorylation of L-fucose to L-fucose 1-phosphate, and its guanylylation to GDP-L-fucose. GDP-fucose is an important fucose donor in the process of fucosylated oligosaccharides formation.",,,,,,,GO:0005524; GO:0050201; GO:0047341,GO:0050201; GO:0047341,GO:0050262; GO:0050263,GO:0050201; GO:0047341; GO:0005524,GO:0016301; GO:0016774; GO:0005524,GO:0004370; GO:0008781; GO:0005524,0.8105,0.4386,1.0,0.7688,0.7739,5,0.7584,0.2999,no
NDHM_PAENI,Q59127,ESM2Text,Bacteria,283,"Component of the nicotine 6-hydroxylase, which is involved in the degradation of nicotine. Catalyzes the hydroxylation of the pyridine ring at C6 to form 6-hydroxynicotine. Can use both L-nicotine and D- nicotine.","Catalyzes the hydrolitical oxidation of 1,3,7-trimethyltrideca-A to produce 1,3,7-trimethylacetate. CoA-lyase is the specific component of the lipoamide biosynthesis pathway. It is unclear whether the CoA ligase also acts as a CoA esterase.",No,No,No,No,No,not-Yes,GO:0071949; GO:0018535,GO:0016491,GO:0016491,GO:0018529,GO:0016491,GO:0016491,0.4991,0.4991,0.2653,0.4991,0.4991,5,0.4523,0.3871,no
NDHM_PAENI,Q59127,Prot2Text,Bacteria,283,"Component of the nicotine 6-hydroxylase, which is involved in the degradation of nicotine. Catalyzes the hydroxylation of the pyridine ring at C6 to form 6-hydroxynicotine. Can use both L-nicotine and D- nicotine.",Catalyzes the oxidation of carbon monoxide to carbon dioxide.,No,No,No,No,No,not-Yes,GO:0071949; GO:0018535,GO:0004854,GO:0004855,GO:0004854,GO:0004854; GO:0004855,GO:0004854,0.2889,0.2889,0.2889,0.3163,0.2889,5,0.2944,0.3871,no
NDHM_PAENI,Q59127,ProtT3,Bacteria,283,"Component of the nicotine 6-hydroxylase, which is involved in the degradation of nicotine. Catalyzes the hydroxylation of the pyridine ring at C6 to form 6-hydroxynicotine. Can use both L-nicotine and D- nicotine.",Catalyzes the oxidation of 4-hydroxybenzoate (4-HB) to 4-hydroxybenzaldehyde (4-HBA). Belongs to the Gfo/Idh/MocA family. 4-hydroxybenzoate 4-monooxygenase subfamily,No,No,No,No,No,not-Yes,GO:0071949; GO:0018535,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4991,0.4991,0.4991,0.4991,0.4991,5,0.4991,0.3871,no
NDHM_PAENI,Q59127,ProtTale,Bacteria,283,"Component of the nicotine 6-hydroxylase, which is involved in the degradation of nicotine. Catalyzes the hydroxylation of the pyridine ring at C6 to form 6-hydroxynicotine. Can use both L-nicotine and D- nicotine.","Component of 2,3-diketo-L-gulonate decarboxylase that catalyzes the decarboxylation of 2,3-diketo-L-gulonate to yield 3-keto-L-gulonate. It is likely involved in the catabolism of L-xylose.",No,No,No,No,No,not-Yes,GO:0071949; GO:0018535,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.2097,0.2097,0.2097,0.2097,0.2097,5,0.2097,0.3871,no
NDHM_PAENI,Q59127,Protein2Text,Bacteria,283,"Component of the nicotine 6-hydroxylase, which is involved in the degradation of nicotine. Catalyzes the hydroxylation of the pyridine ring at C6 to form 6-hydroxynicotine. Can use both L-nicotine and D- nicotine.","The molecular function of this protein is an oxidoreductase. Specifically, it is involved in the oxidation of D-glucosamine 6-phosphate to 2-keto-3-deoxy-D-glucosamine 6-phosphate in the shikimate pathway.",No,No,No,No,No,not-Yes,GO:0071949; GO:0018535,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.2097,0.2097,0.2097,0.2097,0.2097,5,0.2097,0.3871,no
NDHM_PAENI,Q59127,Reference,Bacteria,283,"Component of the nicotine 6-hydroxylase, which is involved in the degradation of nicotine. Catalyzes the hydroxylation of the pyridine ring at C6 to form 6-hydroxynicotine. Can use both L-nicotine and D- nicotine.","Component of the nicotine 6-hydroxylase, which is involved in the degradation of nicotine. Catalyzes the hydroxylation of the pyridine ring at C6 to form 6-hydroxynicotine. Can use both L-nicotine and D- nicotine.",,,,,,,GO:0071949; GO:0018535,GO:0004497,GO:0004497,GO:0004497,GO:0016491; GO:0005506,GO:0016491; GO:0005506; GO:0020037,0.4031,0.4031,0.4031,0.4894,0.4349,5,0.4267,0.3871,no
NDHS_PAENI,Q59128,ESM2Text,Bacteria,165,"Component of the nicotine 6-hydroxylase, which is involved in the degradation of nicotine. Catalyzes the hydroxylation of the pyridine ring at C6 to form 6-hydroxynicotine. Can use both L-nicotine and D- nicotine.",Catalyzes the oxidation of carbon monoxide to carbon dioxide.,No,No,No,No,No,not-Yes,GO:0051537; GO:0046872; GO:0018535,GO:0016491,GO:0016491,GO:0018529,GO:0016491,GO:0016491,0.4238,0.4238,0.2236,0.4238,0.4238,5,0.3838,0.3125,no
NDHS_PAENI,Q59128,Prot2Text,Bacteria,165,"Component of the nicotine 6-hydroxylase, which is involved in the degradation of nicotine. Catalyzes the hydroxylation of the pyridine ring at C6 to form 6-hydroxynicotine. Can use both L-nicotine and D- nicotine.",Component of a complex that catalyzes the reductive dehydroxylation of 4-hydroxybenzoyl-CoA to benzoyl-CoA. Reaction is not reversible. Is a key enzyme in the anaerobic degradation of phenolic compounds.,No,No,No,No,No,not-Yes,GO:0051537; GO:0046872; GO:0018535,GO:0004854,GO:0004855,GO:0004854,GO:0004854; GO:0004855,GO:0004854,0.2437,0.2437,0.2437,0.2747,0.2437,5,0.2499,0.3125,no
NDHS_PAENI,Q59128,ProtT3,Bacteria,165,"Component of the nicotine 6-hydroxylase, which is involved in the degradation of nicotine. Catalyzes the hydroxylation of the pyridine ring at C6 to form 6-hydroxynicotine. Can use both L-nicotine and D- nicotine.",Catalyzes the oxidative decarboxylation of 2-oxoglutarate (2-OG) to succinic semialdehyde (SSA) and CO(2). Belongs to the 2-oxoacid dehydrogenase family,No,No,No,No,No,not-Yes,GO:0051537; GO:0046872; GO:0018535,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4238,0.4238,0.4238,0.4238,0.4238,5,0.4238,0.3125,no
NDHS_PAENI,Q59128,ProtTale,Bacteria,165,"Component of the nicotine 6-hydroxylase, which is involved in the degradation of nicotine. Catalyzes the hydroxylation of the pyridine ring at C6 to form 6-hydroxynicotine. Can use both L-nicotine and D- nicotine.",Catalyzes the oxidation of carbon monoxide to carbon dioxide.,No,No,No,No,No,not-Yes,GO:0051537; GO:0046872; GO:0018535,GO:0018492,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.0,0.4238,0.4238,0.4238,0.4238,5,0.339,0.3125,no
NDHS_PAENI,Q59128,Protein2Text,Bacteria,165,"Component of the nicotine 6-hydroxylase, which is involved in the degradation of nicotine. Catalyzes the hydroxylation of the pyridine ring at C6 to form 6-hydroxynicotine. Can use both L-nicotine and D- nicotine.","The molecular function of this protein is an electron transfer flavoprotein, which suggests it is involved in transferring electrons in a biochemical process.
 
The molecular function of this protein is an electron transfer flavoprotein.",Vague,No,No,Vague,No,not-Yes,GO:0051537; GO:0046872; GO:0018535,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.1894,0.1894,0.1894,0.1894,0.1894,5,0.1894,0.3125,no
NDHS_PAENI,Q59128,Reference,Bacteria,165,"Component of the nicotine 6-hydroxylase, which is involved in the degradation of nicotine. Catalyzes the hydroxylation of the pyridine ring at C6 to form 6-hydroxynicotine. Can use both L-nicotine and D- nicotine.","Component of the nicotine 6-hydroxylase, which is involved in the degradation of nicotine. Catalyzes the hydroxylation of the pyridine ring at C6 to form 6-hydroxynicotine. Can use both L-nicotine and D- nicotine.",,,,,,,GO:0051537; GO:0046872; GO:0018535,GO:0004497,GO:0004497,GO:0004497,GO:0016491; GO:0005506,GO:0016491; GO:0005506; GO:0020037,0.3415,0.3415,0.3415,0.6364,0.5816,5,0.4485,0.3125,no
PRIA_NEIG1,Q5F6V8,ESM2Text,Bacteria,729,"Initiates the restart of stalled replication forks, which reloads the replicative helicase on sites other than the origin of replication. Recognizes and binds to abandoned replication forks and remodels them to uncover a helicase loading site. Promotes assembly of the primosome at these replication forks.","Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0043138; GO:0005524; GO:0016887; GO:0003677; GO:0008270,GO:0003678,GO:0003678; GO:0005524,GO:0003678,GO:0003678,GO:0004003,0.3873,0.6425,0.3873,0.3873,0.3873,5,0.4383,0.6847,yes
PRIA_NEIG1,Q5F6V8,Prot2Text,Bacteria,729,"Initiates the restart of stalled replication forks, which reloads the replicative helicase on sites other than the origin of replication. Recognizes and binds to abandoned replication forks and remodels them to uncover a helicase loading site. Promotes assembly of the primosome at these replication forks.","Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0043138; GO:0005524; GO:0016887; GO:0003677; GO:0008270,GO:0003678; GO:0005524,GO:0003678,GO:0003678,GO:0003678; GO:0005524,GO:0003678,0.6425,0.3873,0.3873,0.6425,0.3873,5,0.4894,0.6847,yes
PRIA_NEIG1,Q5F6V8,ProtT3,Bacteria,729,"Initiates the restart of stalled replication forks, which reloads the replicative helicase on sites other than the origin of replication. Recognizes and binds to abandoned replication forks and remodels them to uncover a helicase loading site. Promotes assembly of the primosome at these replication forks.","Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA. Belongs to the helicase family. PriA subfamily",Yes,Yes,Yes,Yes,Yes,Yes,GO:0043138; GO:0005524; GO:0016887; GO:0003677; GO:0008270,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0008094,0.6425,0.6425,0.6425,0.6425,0.4575,5,0.6055,0.6847,yes
PRIA_NEIG1,Q5F6V8,ProtTale,Bacteria,729,"Initiates the restart of stalled replication forks, which reloads the replicative helicase on sites other than the origin of replication. Recognizes and binds to abandoned replication forks and remodels them to uncover a helicase loading site. Promotes assembly of the primosome at these replication forks.","Initiates the restart of stalled replication forks, which reloads the replicative helicase on sites other than the origin of replication. Recognizes and binds to abandoned replication forks and remodels them to uncover a helicase loading site. Promotes assembly of the primosome at these replication forks.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0043138; GO:0005524; GO:0016887; GO:0003677; GO:0008270,,GO:0003677,GO:0003678,,,,0.4356,0.3873,,,2,0.4114,0.6847,yes
PRIA_NEIG1,Q5F6V8,Protein2Text,Bacteria,729,"Initiates the restart of stalled replication forks, which reloads the replicative helicase on sites other than the origin of replication. Recognizes and binds to abandoned replication forks and remodels them to uncover a helicase loading site. Promotes assembly of the primosome at these replication forks.","The molecular function of this protein is an ATP-dependent DNA helicase involved in DNA repair, recombination and replication. It is a part of the replicative DNA helicase complex of E.coli. It unwinds duplex DNA into single strands, therefore, allowing the replication machinery to copy the genetic material. It is also involved in the homologous recombination process. The replicative helicase moves ahead of the primosome. It is essential for DNA replication and cell division. The helicase activity is regulated by the coupling of ATP hydrolysis and divalent cation binding. It also has a strand transferase activity. It can catalyze the annealing of single-stranded DNA to double-stranded DNA and the subsequent transfer of the single-stranded DNA to the complementary strand of the double-stranded DNA.",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0043138; GO:0005524; GO:0016887; GO:0003677; GO:0008270,GO:0003678; GO:0005524,GO:0004003; GO:0003677; GO:0005524,GO:0003678; GO:0005524,GO:0003678,GO:0003678; GO:0005524,0.6425,0.7915,0.6425,0.3873,0.6425,5,0.6213,0.6847,yes
PRIA_NEIG1,Q5F6V8,Reference,Bacteria,729,"Initiates the restart of stalled replication forks, which reloads the replicative helicase on sites other than the origin of replication. Recognizes and binds to abandoned replication forks and remodels them to uncover a helicase loading site. Promotes assembly of the primosome at these replication forks.","Initiates the restart of stalled replication forks, which reloads the replicative helicase on sites other than the origin of replication. Recognizes and binds to abandoned replication forks and remodels them to uncover a helicase loading site. Promotes assembly of the primosome at these replication forks.",,,,,,,GO:0043138; GO:0005524; GO:0016887; GO:0003677; GO:0008270,GO:0003677,GO:0003677,GO:0003677,GO:0005524; GO:0003689,GO:0003677,0.4356,0.4356,0.4356,0.5516,0.4356,5,0.4588,0.6847,yes
DHOM_NEIG1,Q5F8J4,ESM2Text,Bacteria,435,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate. Is highly specific for NAD(+), and displays an approximate 479-fold (kcat/Km) preference for NAD(+) over NADP(+).",Catalyzes the NAD(+)-dependent oxidation of L-aspartate to iminoaspartate.,No,No,No,No,No,not-Yes,GO:0004412; GO:0046872; GO:0070403; GO:0050661,GO:0016491; GO:0051287,GO:0008734,GO:0008734,GO:0008734,GO:0008734,0.637,0.1386,0.1386,0.1386,0.1386,5,0.2383,0.3583,no
DHOM_NEIG1,Q5F8J4,Prot2Text,Bacteria,435,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate. Is highly specific for NAD(+), and displays an approximate 479-fold (kcat/Km) preference for NAD(+) over NADP(+).",Catalyzes the NADPH-dependent reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).,No,No,No,No,No,not-Yes,GO:0004412; GO:0046872; GO:0070403; GO:0050661,GO:0030604,GO:0030604,GO:0030604,GO:0030604,GO:0030604,0.336,0.336,0.336,0.336,0.336,5,0.336,0.3583,no
DHOM_NEIG1,Q5F8J4,ProtT3,Bacteria,435,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate. Is highly specific for NAD(+), and displays an approximate 479-fold (kcat/Km) preference for NAD(+) over NADP(+).",Belongs to the homoserine dehydrogenase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004412; GO:0046872; GO:0070403; GO:0050661,GO:0004412,GO:0004412,GO:0004412,GO:0004412,GO:0004412,0.4445,0.4445,0.4445,0.4445,0.4445,5,0.4445,0.3583,no
DHOM_NEIG1,Q5F8J4,ProtTale,Bacteria,435,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate. Is highly specific for NAD(+), and displays an approximate 479-fold (kcat/Km) preference for NAD(+) over NADP(+).","Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004412; GO:0046872; GO:0070403; GO:0050661,GO:0004412,GO:0004412,GO:0004412,GO:0004412,GO:0004412,0.4445,0.4445,0.4445,0.4445,0.4445,5,0.4445,0.3583,no
DHOM_NEIG1,Q5F8J4,Protein2Text,Bacteria,435,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate. Is highly specific for NAD(+), and displays an approximate 479-fold (kcat/Km) preference for NAD(+) over NADP(+).","The molecular function of this protein is an isomerase, specifically a cis->trans isomerase. It catalyzes the conversion of cis- to trans- dihydropicolinate, a step in the lysine biosynthesis pathway.",No,No,No,No,No,not-Yes,GO:0004412; GO:0046872; GO:0070403; GO:0050661,GO:0016859,GO:0016859,,GO:0016859,GO:0016859,0.1767,0.1767,,0.1767,0.1767,4,0.1767,0.3583,no
DHOM_NEIG1,Q5F8J4,Reference,Bacteria,435,"Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate. Is highly specific for NAD(+), and displays an approximate 479-fold (kcat/Km) preference for NAD(+) over NADP(+).","Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate. Is highly specific for NAD(+), and displays an approximate 479-fold (kcat/Km) preference for NAD(+) over NADP(+).",,,,,,,GO:0004412; GO:0046872; GO:0070403; GO:0050661,GO:0004412; GO:0051287,GO:0004399,GO:0004412; GO:0051287,GO:0004412,GO:0004412,0.7697,0.336,0.7697,0.4445,0.4445,5,0.5529,0.3583,no
ASPG_THEKO,Q5JIW4,ESM2Text,Archaea,328,"Catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. Also displays D- asparaginase activity, which is about 50% of the L-asparaginase activity. Does not exhibit glutaminase activity.",Catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. Does not display cysteine synthase activity.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004067,GO:0004067,GO:0004067,GO:0004067,GO:0004067,GO:0004067,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5175,no
ASPG_THEKO,Q5JIW4,Prot2Text,Archaea,328,"Catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. Also displays D- asparaginase activity, which is about 50% of the L-asparaginase activity. Does not exhibit glutaminase activity.","Catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. Displays no glutaminase activity, using preferentially NADPH over NADH as the electron donor.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004067,GO:0004067,GO:0004067,GO:0004067,GO:0004067,GO:0004067,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5175,no
ASPG_THEKO,Q5JIW4,ProtT3,Archaea,328,"Catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. Also displays D- asparaginase activity, which is about 50% of the L-asparaginase activity. Does not exhibit glutaminase activity.",Cytoplasm. Belongs to the asparaginase 1 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004067,GO:0004067,GO:0004067,GO:0004067,GO:0004067,GO:0004067,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5175,no
ASPG_THEKO,Q5JIW4,ProtTale,Archaea,328,"Catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. Also displays D- asparaginase activity, which is about 50% of the L-asparaginase activity. Does not exhibit glutaminase activity.","Catalyzes the hydrolysis of C-terminal amino acids of dipeptides containing an N-terminal L-cysteine that functions as a degradation tag for a number of proteins. Cleaves 2',3'-didehydro-L-cysteine and 2',3'-didehydro-L-methionine, but not L-cysteine or L-methionine. Does not cleave dipeptides containing an N-terminal L-alanine.",No,No,No,No,No,not-Yes,GO:0004067,GO:0004180,GO:0004180,GO:0008233,GO:0008233,GO:0008233,0.2758,0.2758,0.3831,0.3831,0.3831,5,0.3402,0.5175,no
ASPG_THEKO,Q5JIW4,Protein2Text,Archaea,328,"Catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. Also displays D- asparaginase activity, which is about 50% of the L-asparaginase activity. Does not exhibit glutaminase activity.","This protein is a part of the phosphoenolpyruvate carboxykinase (PEPCK) enzyme system, which is involved in the regulation of gluconeogenesis, a process that generates glucose from non-carbohydrate sources. The molecular function of this protein is to catalyze the conversion of phosphoenolpyruvate (PEP) to oxaloacetate (OAA) in the presence of ATP, magnesium ions, and bicarbonate. This reaction is a key step in the gluconeogenesis pathway, allowing cells to generate glucose from non-carbohydrate sources such as amino acids, lactate, and glycerol. 

In more detail, the molecular function of this protein can be described as follows:

1. Binding of phosphoenolpyruvate (PEP): The protein binds to PEP, a key intermediate in gluconeogenesis, and positions it for the catalytic reaction.
2. ATP binding: The protein binds to ATP, which provides the energy required for the conversion of PEP to OAA.
3. Magnesium ion binding: The protein binds to magnesium ions, which are required for the catalytic reaction.
4. Bicarbonate binding: The protein binds to bicarbonate, which is required for the catalytic reaction.
5. Catalysis of the conversion of PEP to OAA: The protein catalyzes the conversion of PEP to OAA in the presence of ATP, magnesium ions, and bicarbonate.

Overall, the molecular function of this protein is to catalyze the conversion of PEP to OAA, a key step in the gluconeogenesis pathway.",No,No,No,No,No,not-Yes,GO:0004067,GO:0004612,GO:0004612,GO:0004612,GO:0004613,GO:0004612,0.1493,0.1493,0.1493,0.1493,0.1493,5,0.1493,0.5175,no
ASPG_THEKO,Q5JIW4,Reference,Archaea,328,"Catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. Also displays D- asparaginase activity, which is about 50% of the L-asparaginase activity. Does not exhibit glutaminase activity.","Catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. Also displays D- asparaginase activity, which is about 50% of the L-asparaginase activity. Does not exhibit glutaminase activity.",,,,,,,GO:0004067,GO:0004067,GO:0004067,GO:0004067,GO:0004067,GO:0004067,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5175,no
PERL_MOUSE,Q5SW46,ESM2Text,Eukaryota,710,"Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2). Also involved in the conversion of iodide (I(-)) into hypoiodite (IO(-)) in the presence of H2O2. Responsible for the inactivation of a wide range of micro-organisms and hence, important component of defense mechanism. May be implicated in airway host defense against infection. May contribute to maintaining an appropriate H2O2 cellular level, therefore protecting cells from H2O2-caused injuries and inflammation.","Heterodimeric chaperone which catalyzes the formation of di- and tripeptides from choline, cholin- and tripeptides. In a monomeric system, produces di- and tripeptides with 5-substituted phenol (5S)-substituted phenol (dCl(2+) and C20), 5-substituted phenol (Cl(3+) and C20), and 5-substituted phenol (Qu(2+) and C20). In a zinc-dependent system, produces di- and tripeptides with 5-substituted phenol (Cl(2+) and C20), 5-substituted phenol (Cl(3+) and C20), and 5-substituted phenol (Qu(+) and C20). In the glutathione system, produces di and tripeptides with 5-substituted phenol (Cl(2+) and C20), 5-substituted phenol (Cl(3+) and C20), and 5-substituted phenol (Qu(+) and C20). In the gut, produces di and",No,No,No,No,No,not-Yes,GO:0020037; GO:0140825; GO:0046872; GO:0004601; GO:0036393,,,,,,,,,,,0,,0.4511,no
PERL_MOUSE,Q5SW46,Prot2Text,Eukaryota,710,"Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2). Also involved in the conversion of iodide (I(-)) into hypoiodite (IO(-)) in the presence of H2O2. Responsible for the inactivation of a wide range of micro-organisms and hence, important component of defense mechanism. May be implicated in airway host defense against infection. May contribute to maintaining an appropriate H2O2 cellular level, therefore protecting cells from H2O2-caused injuries and inflammation.",Involved in the formation of a rigid and insoluble egg chorion by catalyzing chorion protein cross-linking through dityrosine formation and phenol oxidase-catalyzed chorion melanization.,Maybe,Maybe,Maybe,No,No,not-Yes,GO:0020037; GO:0140825; GO:0046872; GO:0004601; GO:0036393,GO:0016491,GO:0004601,GO:0004601,GO:0004097,GO:0004601,0.4541,0.6753,0.6753,0.2631,0.6753,5,0.5486,0.4511,no
PERL_MOUSE,Q5SW46,ProtT3,Eukaryota,710,"Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2). Also involved in the conversion of iodide (I(-)) into hypoiodite (IO(-)) in the presence of H2O2. Responsible for the inactivation of a wide range of micro-organisms and hence, important component of defense mechanism. May be implicated in airway host defense against infection. May contribute to maintaining an appropriate H2O2 cellular level, therefore protecting cells from H2O2-caused injuries and inflammation.",Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods. Secreted. Belongs to the tyrosinase family. Hemocyanin subfamily,No,No,No,No,Vague,not-Yes,GO:0020037; GO:0140825; GO:0046872; GO:0004601; GO:0036393,GO:0005507; GO:0019825,GO:0005507; GO:0019825,GO:0005507; GO:0019825,GO:0005507; GO:0019825,GO:0005507; GO:0019825,0.4064,0.4064,0.4064,0.4064,0.4064,5,0.4064,0.4511,no
PERL_MOUSE,Q5SW46,ProtTale,Eukaryota,710,"Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2). Also involved in the conversion of iodide (I(-)) into hypoiodite (IO(-)) in the presence of H2O2. Responsible for the inactivation of a wide range of micro-organisms and hence, important component of defense mechanism. May be implicated in airway host defense against infection. May contribute to maintaining an appropriate H2O2 cellular level, therefore protecting cells from H2O2-caused injuries and inflammation.",Probable peroxidase that may play a role in osmoprotection and redox homeostasis of the parasite during host infection.,Maybe,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0020037; GO:0140825; GO:0046872; GO:0004601; GO:0036393,GO:0004601,GO:0004601,GO:0004601,GO:0004601,GO:0004601,0.6753,0.6753,0.6753,0.6753,0.6753,5,0.6753,0.4511,no
PERL_MOUSE,Q5SW46,Protein2Text,Eukaryota,710,"Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2). Also involved in the conversion of iodide (I(-)) into hypoiodite (IO(-)) in the presence of H2O2. Responsible for the inactivation of a wide range of micro-organisms and hence, important component of defense mechanism. May be implicated in airway host defense against infection. May contribute to maintaining an appropriate H2O2 cellular level, therefore protecting cells from H2O2-caused injuries and inflammation.","The molecular function of this protein is not explicitly stated in the provided information. However, based on its name, it is likely involved in the production or modification of hydrogen peroxide, which is a key molecule in cellular defense mechanisms and signaling pathways.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0020037; GO:0140825; GO:0046872; GO:0004601; GO:0036393,,,,,,,,,,,0,,0.4511,no
PERL_MOUSE,Q5SW46,Reference,Eukaryota,710,"Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2). Also involved in the conversion of iodide (I(-)) into hypoiodite (IO(-)) in the presence of H2O2. Responsible for the inactivation of a wide range of micro-organisms and hence, important component of defense mechanism. May be implicated in airway host defense against infection. May contribute to maintaining an appropriate H2O2 cellular level, therefore protecting cells from H2O2-caused injuries and inflammation.","Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2). Also involved in the conversion of iodide (I(-)) into hypoiodite (IO(-)) in the presence of H2O2. Responsible for the inactivation of a wide range of micro-organisms and hence, important component of defense mechanism. May be implicated in airway host defense against infection. May contribute to maintaining an appropriate H2O2 cellular level, therefore protecting cells from H2O2-caused injuries and inflammation.",,,,,,,GO:0020037; GO:0140825; GO:0046872; GO:0004601; GO:0036393,GO:0004601; GO:0020037,GO:0004601; GO:0020037,GO:0004601; GO:0020037,GO:0004601; GO:0020037,GO:0004601; GO:0020037,0.8657,0.8657,0.8657,0.8657,0.8657,5,0.8657,0.4511,no
APY_ANOGA,Q5TVM9,ESM2Text,Eukaryota,570,"Cleaves adenosine triphosphate (ATP) and adenosine diphosphate (ADP) to adenosine monophosphate (AMP) and inorganic phosphate. Enhances fibrin degradation in the midgut blood bolus. Activates human tissue plasminogen activator (PLAT), probably via an allosteric activation mechanism. Inhibits ADP-mediated host platelet aggregation in vitro and in mosquito midgut. Inhibits host neutrophil activation in the mosquito midgut: reduces neutrophil extracellular traps formation in the presence of platelets and the formation of total cell- and mitochondrial-derived reactive oxygen species.",Facilitates hematophagy by inhibiting ADP-dependent platelet aggregation in the host. Shows potential for antithrombotic activity. May reduce probing time by facilitating the speed of locating blood.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008253; GO:0004050; GO:0008047; GO:0046872; GO:0000166; GO:0090729,,,,,,,,,,,0,,0.4069,no
APY_ANOGA,Q5TVM9,Prot2Text,Eukaryota,570,"Cleaves adenosine triphosphate (ATP) and adenosine diphosphate (ADP) to adenosine monophosphate (AMP) and inorganic phosphate. Enhances fibrin degradation in the midgut blood bolus. Activates human tissue plasminogen activator (PLAT), probably via an allosteric activation mechanism. Inhibits ADP-mediated host platelet aggregation in vitro and in mosquito midgut. Inhibits host neutrophil activation in the mosquito midgut: reduces neutrophil extracellular traps formation in the presence of platelets and the formation of total cell- and mitochondrial-derived reactive oxygen species.",Facilitates hematophagy by inhibiting ADP-dependent platelet aggregation in the host. May reduce probing time by facilitating the speed of locating blood.,Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008253; GO:0004050; GO:0008047; GO:0046872; GO:0000166; GO:0090729,,,GO:0017110,,GO:0004382,,,0.3101,,0.2736,2,0.2918,0.4069,no
APY_ANOGA,Q5TVM9,ProtT3,Eukaryota,570,"Cleaves adenosine triphosphate (ATP) and adenosine diphosphate (ADP) to adenosine monophosphate (AMP) and inorganic phosphate. Enhances fibrin degradation in the midgut blood bolus. Activates human tissue plasminogen activator (PLAT), probably via an allosteric activation mechanism. Inhibits ADP-mediated host platelet aggregation in vitro and in mosquito midgut. Inhibits host neutrophil activation in the mosquito midgut: reduces neutrophil extracellular traps formation in the presence of platelets and the formation of total cell- and mitochondrial-derived reactive oxygen species.",Secreted. Belongs to the 5'-nucleotidase family,Maybe,Vague,Vague,Vague,Vague,not-Yes,GO:0008253; GO:0004050; GO:0008047; GO:0046872; GO:0000166; GO:0090729,GO:0008253,GO:0008253,GO:0008253,GO:0008253,GO:0008253,0.3765,0.3765,0.3765,0.3765,0.3765,5,0.3765,0.4069,no
APY_ANOGA,Q5TVM9,ProtTale,Eukaryota,570,"Cleaves adenosine triphosphate (ATP) and adenosine diphosphate (ADP) to adenosine monophosphate (AMP) and inorganic phosphate. Enhances fibrin degradation in the midgut blood bolus. Activates human tissue plasminogen activator (PLAT), probably via an allosteric activation mechanism. Inhibits ADP-mediated host platelet aggregation in vitro and in mosquito midgut. Inhibits host neutrophil activation in the mosquito midgut: reduces neutrophil extracellular traps formation in the presence of platelets and the formation of total cell- and mitochondrial-derived reactive oxygen species.","Bifunctional enzyme that acts both as a phosphatase and as a receptor for extracellular adenosine 5'-monophosphate (AMP). Hydrolyzes inorganic pyrophosphate (PPi) to phosphate (PPi-) and thereby regulates the production of diadenosine tetraphosphate (Ap4A), a signaling molecule that functions as an autocrine and/or paracrine regulator of cell function. Also acts as a receptor for 2',3'-cyclic nucleotide 3'-phosphodiesters (2',3'-cAMP3'-P and 2',3'-cAMP2",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0008253; GO:0004050; GO:0008047; GO:0046872; GO:0000166; GO:0090729,GO:0004427,GO:0016791; GO:0004427,GO:0016791; GO:0004427,GO:0016791,GO:0004427,0.3101,0.4433,0.4433,0.3352,0.3101,5,0.3684,0.4069,no
APY_ANOGA,Q5TVM9,Protein2Text,Eukaryota,570,"Cleaves adenosine triphosphate (ATP) and adenosine diphosphate (ADP) to adenosine monophosphate (AMP) and inorganic phosphate. Enhances fibrin degradation in the midgut blood bolus. Activates human tissue plasminogen activator (PLAT), probably via an allosteric activation mechanism. Inhibits ADP-mediated host platelet aggregation in vitro and in mosquito midgut. Inhibits host neutrophil activation in the mosquito midgut: reduces neutrophil extracellular traps formation in the presence of platelets and the formation of total cell- and mitochondrial-derived reactive oxygen species.","The molecular function of this protein is to catalyze the hydrolysis of nucleotides, specifically converting nucleoside diphosphates into nucleoside monophosphates. More specifically, it is a 5'-nucleotidase that catalyzes the hydrolysis of nucleoside diphosphates to yield nucleoside monophosphates and inorganic phosphate. It is also involved in the regulation of purine and pyrimidine metabolism.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008253; GO:0004050; GO:0008047; GO:0046872; GO:0000166; GO:0090729,GO:0008253,GO:0008253,GO:0008253,GO:0008253,GO:0008253,0.3765,0.3765,0.3765,0.3765,0.3765,5,0.3765,0.4069,no
APY_ANOGA,Q5TVM9,Reference,Eukaryota,570,"Cleaves adenosine triphosphate (ATP) and adenosine diphosphate (ADP) to adenosine monophosphate (AMP) and inorganic phosphate. Enhances fibrin degradation in the midgut blood bolus. Activates human tissue plasminogen activator (PLAT), probably via an allosteric activation mechanism. Inhibits ADP-mediated host platelet aggregation in vitro and in mosquito midgut. Inhibits host neutrophil activation in the mosquito midgut: reduces neutrophil extracellular traps formation in the presence of platelets and the formation of total cell- and mitochondrial-derived reactive oxygen species.","Cleaves adenosine triphosphate (ATP) and adenosine diphosphate (ADP) to adenosine monophosphate (AMP) and inorganic phosphate. Enhances fibrin degradation in the midgut blood bolus. Activates human tissue plasminogen activator (PLAT), probably via an allosteric activation mechanism. Inhibits ADP-mediated host platelet aggregation in vitro and in mosquito midgut. Inhibits host neutrophil activation in the mosquito midgut: reduces neutrophil extracellular traps formation in the presence of platelets and the formation of total cell- and mitochondrial-derived reactive oxygen species.",,,,,,,GO:0008253; GO:0004050; GO:0008047; GO:0046872; GO:0000166; GO:0090729,GO:0017111; GO:0017110,GO:0017111,GO:0004551,GO:0004051; GO:0004049,GO:0004051; GO:0005524,0.3647,0.3101,0.3101,0.1535,0.2673,5,0.2811,0.4069,no
ACAD9_DROME,Q5U117,ESM2Text,Eukaryota,639,"As part of the MCIA complex, primarily participates in the assembly of the mitochondrial complex I and therefore plays a role in oxidative phosphorylation.","Acyl-CoA dehydrogenase, that exhibits maximal activity towards saturated C22-CoA. Probably participates in beta-oxidation of fatty acids.",No,No,No,No,No,not-Yes,GO:0050660; GO:0070991,GO:0003995,GO:0003995,GO:0003995,GO:0003995,GO:0003995,0.6049,0.6049,0.6049,0.6049,0.6049,5,0.6049,0.2986,no
ACAD9_DROME,Q5U117,Prot2Text,Eukaryota,639,"As part of the MCIA complex, primarily participates in the assembly of the mitochondrial complex I and therefore plays a role in oxidative phosphorylation.","Mitochondrial enzyme that catalyzes the conversion of isocitrate to alpha-ketoglutarate and also acts as a pyruvate dehydrogenase that converts alpha-ketoglutarate to succinyl-CoA and CO(2) in the cytosol. As part of the mitochondrial oxidation pathway, facilitates protection against oxidative stress by converting alpha-ketoglutarate to succinate.",No,No,No,No,No,not-Yes,GO:0050660; GO:0070991,GO:0004449,GO:0004450,GO:0004449,GO:0004449,GO:0004449,0.1912,0.1912,0.1912,0.1912,0.1912,5,0.1912,0.2986,no
ACAD9_DROME,Q5U117,ProtT3,Eukaryota,639,"As part of the MCIA complex, primarily participates in the assembly of the mitochondrial complex I and therefore plays a role in oxidative phosphorylation.",Mitochondrial acyl-CoA dehydrogenase involved in fatty acid beta-oxidation. Mitochondrion inner membrane; Multi-pass membrane protein. Belongs to the acyl-CoA dehydrogenase family,No,No,No,No,Vague,not-Yes,GO:0050660; GO:0070991,GO:0003995,GO:0003995,GO:0003995,GO:0003995,GO:0003995,0.6049,0.6049,0.6049,0.6049,0.6049,5,0.6049,0.2986,no
ACAD9_DROME,Q5U117,ProtTale,Eukaryota,639,"As part of the MCIA complex, primarily participates in the assembly of the mitochondrial complex I and therefore plays a role in oxidative phosphorylation.","Catalyzes the oxidation of malate to oxaloacetate. May play a role in glucose and fatty acid metabolism, as well as in the antioxidant response.",No,No,No,No,No,not-Yes,GO:0050660; GO:0070991,GO:0016615,GO:0016615,GO:0016615,GO:0004470,GO:0016615,0.2628,0.2628,0.2628,0.2217,0.2628,5,0.2546,0.2986,no
ACAD9_DROME,Q5U117,Protein2Text,Eukaryota,639,"As part of the MCIA complex, primarily participates in the assembly of the mitochondrial complex I and therefore plays a role in oxidative phosphorylation.","This protein is a part of the mitochondrial trifunctional protein (MTP), which plays a crucial role in the beta-oxidation of long-chain fatty acids. The molecular function of this protein is to catalyze the transfer of electrons from coenzyme A to the cytochrome b5 family member 2 (CYB5R2), thereby facilitating the oxidation of long-chain fatty acids. This process is essential for the production of energy in the form of ATP from fatty acids.",No,No,No,No,No,not-Yes,GO:0050660; GO:0070991,,,,,,,,,,,0,,0.2986,no
ACAD9_DROME,Q5U117,Reference,Eukaryota,639,"As part of the MCIA complex, primarily participates in the assembly of the mitochondrial complex I and therefore plays a role in oxidative phosphorylation.","As part of the MCIA complex, primarily participates in the assembly of the mitochondrial complex I and therefore plays a role in oxidative phosphorylation.",,,,,,,GO:0050660; GO:0070991,,,,,,,,,,,0,,0.2986,no
LPA_ENTFL,Q5XVM9,ESM2Text,Bacteria,725,"Amidohydrolase that releases lipoic acid from the protein- bound form. Cleaves the amide bond that links lipoic acid to the lipoylated lysine epsilon- amino groups, leading to the formation of free lipoic acid plus the unmodified protein. Shows activity toward both high molecular weight protein substrates such as a lipoyl domain and intact 2-oxoacid dehydrogenases as well as small molecule substrates such as lipoyl-lysine. Also acts on small biotinylated substrates. Hydrolyzes the synthetic substrates methyl lipoate and lipoamide. The physiologically important substrates are probably lipoyl-lysine and small peptides containing lipoyl-lysine. Lpa seems likely to enable this bacterium to utilize amide-linked forms of lipoic acid that otherwise could not be assimilated.",Provides the precursors necessary for DNA synthesis. This enzyme allows S.japonicus to use synthetic acyl-ACP as an alternative substrate.,No,No,No,No,No,not-Yes,GO:0061690,,,,,,,,,,,0,,0.2017,no
LPA_ENTFL,Q5XVM9,Prot2Text,Bacteria,725,"Amidohydrolase that releases lipoic acid from the protein- bound form. Cleaves the amide bond that links lipoic acid to the lipoylated lysine epsilon- amino groups, leading to the formation of free lipoic acid plus the unmodified protein. Shows activity toward both high molecular weight protein substrates such as a lipoyl domain and intact 2-oxoacid dehydrogenases as well as small molecule substrates such as lipoyl-lysine. Also acts on small biotinylated substrates. Hydrolyzes the synthetic substrates methyl lipoate and lipoamide. The physiologically important substrates are probably lipoyl-lysine and small peptides containing lipoyl-lysine. Lpa seems likely to enable this bacterium to utilize amide-linked forms of lipoic acid that otherwise could not be assimilated.",Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).,No,No,No,No,No,not-Yes,GO:0061690,GO:0050567,GO:0050567,GO:0050567,GO:0016884,GO:0050567,0.158,0.158,0.158,0.2353,0.158,5,0.1735,0.2017,no
LPA_ENTFL,Q5XVM9,ProtT3,Bacteria,725,"Amidohydrolase that releases lipoic acid from the protein- bound form. Cleaves the amide bond that links lipoic acid to the lipoylated lysine epsilon- amino groups, leading to the formation of free lipoic acid plus the unmodified protein. Shows activity toward both high molecular weight protein substrates such as a lipoyl domain and intact 2-oxoacid dehydrogenases as well as small molecule substrates such as lipoyl-lysine. Also acts on small biotinylated substrates. Hydrolyzes the synthetic substrates methyl lipoate and lipoamide. The physiologically important substrates are probably lipoyl-lysine and small peptides containing lipoyl-lysine. Lpa seems likely to enable this bacterium to utilize amide-linked forms of lipoic acid that otherwise could not be assimilated.",Belongs to the amidase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0061690,GO:0004040,GO:0004040,GO:0004040,GO:0004040,GO:0004040,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.2017,no
LPA_ENTFL,Q5XVM9,ProtTale,Bacteria,725,"Amidohydrolase that releases lipoic acid from the protein- bound form. Cleaves the amide bond that links lipoic acid to the lipoylated lysine epsilon- amino groups, leading to the formation of free lipoic acid plus the unmodified protein. Shows activity toward both high molecular weight protein substrates such as a lipoyl domain and intact 2-oxoacid dehydrogenases as well as small molecule substrates such as lipoyl-lysine. Also acts on small biotinylated substrates. Hydrolyzes the synthetic substrates methyl lipoate and lipoamide. The physiologically important substrates are probably lipoyl-lysine and small peptides containing lipoyl-lysine. Lpa seems likely to enable this bacterium to utilize amide-linked forms of lipoic acid that otherwise could not be assimilated.","Catalyzes the hydrolysis of the thioester bond in the cleavage of the D-alanyl-D-alanine and D,D-diaminopimelate (D,D-DAP) dipeptide, to yield D-alanine and D-alanine.",Maybe,No,No,No,No,not-Yes,GO:0061690,GO:0016787,GO:0016787,GO:0008233,GO:0016787,GO:0008233,0.6019,0.6019,0.4302,0.6019,0.4302,5,0.5332,0.2017,no
LPA_ENTFL,Q5XVM9,Protein2Text,Bacteria,725,"Amidohydrolase that releases lipoic acid from the protein- bound form. Cleaves the amide bond that links lipoic acid to the lipoylated lysine epsilon- amino groups, leading to the formation of free lipoic acid plus the unmodified protein. Shows activity toward both high molecular weight protein substrates such as a lipoyl domain and intact 2-oxoacid dehydrogenases as well as small molecule substrates such as lipoyl-lysine. Also acts on small biotinylated substrates. Hydrolyzes the synthetic substrates methyl lipoate and lipoamide. The physiologically important substrates are probably lipoyl-lysine and small peptides containing lipoyl-lysine. Lpa seems likely to enable this bacterium to utilize amide-linked forms of lipoic acid that otherwise could not be assimilated.",The molecular function of this protein is to hydrolyze ester bonds in the cell membrane.,Vague,Vague,Vague,Vague,No,not-Yes,GO:0061690,GO:0016788,GO:0016788,,GO:0016788,GO:0016787,0.482,0.482,,0.482,0.6019,4,0.512,0.2017,no
LPA_ENTFL,Q5XVM9,Reference,Bacteria,725,"Amidohydrolase that releases lipoic acid from the protein- bound form. Cleaves the amide bond that links lipoic acid to the lipoylated lysine epsilon- amino groups, leading to the formation of free lipoic acid plus the unmodified protein. Shows activity toward both high molecular weight protein substrates such as a lipoyl domain and intact 2-oxoacid dehydrogenases as well as small molecule substrates such as lipoyl-lysine. Also acts on small biotinylated substrates. Hydrolyzes the synthetic substrates methyl lipoate and lipoamide. The physiologically important substrates are probably lipoyl-lysine and small peptides containing lipoyl-lysine. Lpa seems likely to enable this bacterium to utilize amide-linked forms of lipoic acid that otherwise could not be assimilated.","Amidohydrolase that releases lipoic acid from the protein- bound form. Cleaves the amide bond that links lipoic acid to the lipoylated lysine epsilon- amino groups, leading to the formation of free lipoic acid plus the unmodified protein. Shows activity toward both high molecular weight protein substrates such as a lipoyl domain and intact 2-oxoacid dehydrogenases as well as small molecule substrates such as lipoyl-lysine. Also acts on small biotinylated substrates. Hydrolyzes the synthetic substrates methyl lipoate and lipoamide. The physiologically important substrates are probably lipoyl-lysine and small peptides containing lipoyl-lysine. Lpa seems likely to enable this bacterium to utilize amide-linked forms of lipoic acid that otherwise could not be assimilated.",,,,,,,GO:0061690,GO:0016811,GO:0016811,GO:0050071,GO:0016811; GO:0016787,GO:0016811,0.8582,0.8582,0.1998,0.7728,0.8582,5,0.7094,0.2017,no
PAC_PECAS,Q6D291,ESM2Text,Bacteria,376,"Catalyzes the hydrolysis of penicillin V to 6- aminopenicillanate (6-APA). Shows high specificity towards penicillin V. Can use other beta-lactam substrates, including penicillin G, ampicillin, cephalexin, cloxacillin and dicloxacillin, but at a rate less than 10% of that of penicillin V. Does not show any activity with glyco- or tauro-conjugated bile salts.","Degrades the major monoglucosylated and heparan-linked alpha-glycoside binding glycans and pentagalacturonan (PGA). Has a strong preference for penicillin-bound glycans with short, basic, aromatic, and hydrophobic side chains in the middle position.",No,No,No,No,No,not-Yes,GO:0008953,GO:0016798,,,,,0.482,,,,,1,0.482,0.4205,no
PAC_PECAS,Q6D291,Prot2Text,Bacteria,376,"Catalyzes the hydrolysis of penicillin V to 6- aminopenicillanate (6-APA). Shows high specificity towards penicillin V. Can use other beta-lactam substrates, including penicillin G, ampicillin, cephalexin, cloxacillin and dicloxacillin, but at a rate less than 10% of that of penicillin V. Does not show any activity with glyco- or tauro-conjugated bile salts.","Bile salt hydrolase that catalyzes the deconjugation of glycine- and taurine-linked bile salts, which occurs naturally in the intestines of humans, releasing amino acid residues and deconjugated bile salts (bile acids). Can hydrolyze the amid bond in major human bile salts, such as glycocholate (GCA), taurocholate (TCA), taurodeoxycholate (TDCA) and taurodeoxycholate (TDCA), and the resultant bile acid compounds may contribute to the elimination of these bile salts. Has a preference for taurine-conjugated bile acids as substrates.",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0008953,GO:0008126,,GO:0016811,GO:0016811,GO:0008126,0.2943,,0.8582,0.8582,0.2943,4,0.5762,0.4205,no
PAC_PECAS,Q6D291,ProtT3,Bacteria,376,"Catalyzes the hydrolysis of penicillin V to 6- aminopenicillanate (6-APA). Shows high specificity towards penicillin V. Can use other beta-lactam substrates, including penicillin G, ampicillin, cephalexin, cloxacillin and dicloxacillin, but at a rate less than 10% of that of penicillin V. Does not show any activity with glyco- or tauro-conjugated bile salts.",Periplasm. Belongs to the peptidase C69 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008953,GO:0008233,GO:0008234,GO:0008234,GO:0008234,GO:0008233,0.4302,0.3655,0.3655,0.3655,0.4302,5,0.3914,0.4205,no
PAC_PECAS,Q6D291,ProtTale,Bacteria,376,"Catalyzes the hydrolysis of penicillin V to 6- aminopenicillanate (6-APA). Shows high specificity towards penicillin V. Can use other beta-lactam substrates, including penicillin G, ampicillin, cephalexin, cloxacillin and dicloxacillin, but at a rate less than 10% of that of penicillin V. Does not show any activity with glyco- or tauro-conjugated bile salts.","Catalyzes the hydrolysis of the peptide bond between the P1' and P1'' positions of an alpha-aminoadipic acid-containing dipeptide, releasing an alpha-aminoadipic acid and a dipeptide.",Vague,No,No,No,Maybe,not-Yes,GO:0008953,GO:0008233,GO:0008233,GO:0008233,GO:0008233,GO:0008233,0.4302,0.4302,0.4302,0.4302,0.4302,5,0.4302,0.4205,no
PAC_PECAS,Q6D291,Protein2Text,Bacteria,376,"Catalyzes the hydrolysis of penicillin V to 6- aminopenicillanate (6-APA). Shows high specificity towards penicillin V. Can use other beta-lactam substrates, including penicillin G, ampicillin, cephalexin, cloxacillin and dicloxacillin, but at a rate less than 10% of that of penicillin V. Does not show any activity with glyco- or tauro-conjugated bile salts.","The molecular function of this protein is not specified in the given text, but based on its classification as a peptidase, it is likely to be involved in the breakdown of peptides. Specifically, it is involved in the hydrolysis of carboxyl groups in peptides.",Vague,Vague,No,Vague,No,not-Yes,GO:0008953,GO:0004180,GO:0008233,GO:0008233,GO:0004180,GO:0004180,0.3167,0.4302,0.4302,0.3167,0.3167,5,0.3621,0.4205,no
PAC_PECAS,Q6D291,Reference,Bacteria,376,"Catalyzes the hydrolysis of penicillin V to 6- aminopenicillanate (6-APA). Shows high specificity towards penicillin V. Can use other beta-lactam substrates, including penicillin G, ampicillin, cephalexin, cloxacillin and dicloxacillin, but at a rate less than 10% of that of penicillin V. Does not show any activity with glyco- or tauro-conjugated bile salts.","Catalyzes the hydrolysis of penicillin V to 6- aminopenicillanate (6-APA). Shows high specificity towards penicillin V. Can use other beta-lactam substrates, including penicillin G, ampicillin, cephalexin, cloxacillin and dicloxacillin, but at a rate less than 10% of that of penicillin V. Does not show any activity with glyco- or tauro-conjugated bile salts.",,,,,,,GO:0008953,GO:0016811,GO:0008107,GO:0008744,GO:0008800,GO:0008810,0.8582,0.154,0.1737,0.5121,0.3386,5,0.4073,0.4205,no
XRCC5_XENLA,Q6DDS9,ESM2Text,Eukaryota,726,"DNA-binding protein critical for the DNA damage response, specifically in repairing double-strand breaks (DSBs) via the classical non-homologous end joining (NHEJ) pathway. It forms a heterodimer with xrcc6/Ku70, creating the Ku70:Ku80 heterodimer (Ku complex), which serves as a DNA end-binding complex. It primarily binds DSBs and recruits essential repair factors, assembling the core long-range NHEJ complex to facilitate the alignment and ligation of broken DNA ends.","Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication. This subunit is required for chromosomal replication. Also binds to numerous other types of Dna proteins, suggesting that it is involved in many cellular processes.",No,No,No,No,No,not-Yes,GO:0005524; GO:0003684; GO:0003678; GO:0003690; GO:0016787; GO:0042162,GO:0003688,GO:0003688,GO:0003677,GO:0003677,GO:0003688,0.3941,0.3941,0.5335,0.5335,0.3941,5,0.4499,0.6244,yes
XRCC5_XENLA,Q6DDS9,Prot2Text,Eukaryota,726,"DNA-binding protein critical for the DNA damage response, specifically in repairing double-strand breaks (DSBs) via the classical non-homologous end joining (NHEJ) pathway. It forms a heterodimer with xrcc6/Ku70, creating the Ku70:Ku80 heterodimer (Ku complex), which serves as a DNA end-binding complex. It primarily binds DSBs and recruits essential repair factors, assembling the core long-range NHEJ complex to facilitate the alignment and ligation of broken DNA ends.","Single-stranded DNA-dependent ATP-dependent helicase that plays a key role in DNA non-homologous end joining (NHEJ) by recruiting DNA-PK to DNA. Required for double-strand break repair and V(D)J recombination. Also has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. During NHEJ, the XRCC5-XRRC6 dimer performs the recognition step: it recognizes and binds to the broken ends of the DNA and protects them from further resection. Binding to DNA may be mediated by XRCC6. The XRCC5-XRRC6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5-XRRC6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. The assembly",Maybe,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0003684; GO:0003678; GO:0003690; GO:0016787; GO:0042162,GO:0003678; GO:0005524; GO:0003677,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,0.8347,0.5835,0.5835,0.5835,0.5835,5,0.6337,0.6244,yes
XRCC5_XENLA,Q6DDS9,ProtT3,Eukaryota,726,"DNA-binding protein critical for the DNA damage response, specifically in repairing double-strand breaks (DSBs) via the classical non-homologous end joining (NHEJ) pathway. It forms a heterodimer with xrcc6/Ku70, creating the Ku70:Ku80 heterodimer (Ku complex), which serves as a DNA end-binding complex. It primarily binds DSBs and recruits essential repair factors, assembling the core long-range NHEJ complex to facilitate the alignment and ligation of broken DNA ends.","Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. Ku70/Ku80 heterodimer binds to the stem loop of tlc1, the RNA component of telomerase. Involved in telomere maintenance",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0003684; GO:0003678; GO:0003690; GO:0016787; GO:0042162,GO:0003678; GO:0005524; GO:0003690,GO:0003678; GO:0005524; GO:0003690,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0008094,0.8404,0.8404,0.5835,0.5835,0.4441,5,0.6584,0.6244,yes
XRCC5_XENLA,Q6DDS9,ProtTale,Eukaryota,726,"DNA-binding protein critical for the DNA damage response, specifically in repairing double-strand breaks (DSBs) via the classical non-homologous end joining (NHEJ) pathway. It forms a heterodimer with xrcc6/Ku70, creating the Ku70:Ku80 heterodimer (Ku complex), which serves as a DNA end-binding complex. It primarily binds DSBs and recruits essential repair factors, assembling the core long-range NHEJ complex to facilitate the alignment and ligation of broken DNA ends.","Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0003684; GO:0003678; GO:0003690; GO:0016787; GO:0042162,GO:0003678; GO:0005524,GO:0003678; GO:0005524; GO:0003677,GO:0003678; GO:0005524; GO:0003690,GO:0004003; GO:0005524; GO:0003684,GO:0003678; GO:0005524; GO:0003690,0.5835,0.8347,0.8404,0.8404,0.8404,5,0.7879,0.6244,yes
XRCC5_XENLA,Q6DDS9,Protein2Text,Eukaryota,726,"DNA-binding protein critical for the DNA damage response, specifically in repairing double-strand breaks (DSBs) via the classical non-homologous end joining (NHEJ) pathway. It forms a heterodimer with xrcc6/Ku70, creating the Ku70:Ku80 heterodimer (Ku complex), which serves as a DNA end-binding complex. It primarily binds DSBs and recruits essential repair factors, assembling the core long-range NHEJ complex to facilitate the alignment and ligation of broken DNA ends.","The molecular function of this protein is to act as a component of the DNA repair machinery. More specifically, it is a key enzyme in the non-homologous end-joining (NHEJ) pathway of DNA double-strand break repair.",Maybe,Maybe,Yes,Yes,Maybe,not-Yes,GO:0005524; GO:0003684; GO:0003678; GO:0003690; GO:0016787; GO:0042162,,,,,,,,,,,0,,0.6244,yes
XRCC5_XENLA,Q6DDS9,Reference,Eukaryota,726,"DNA-binding protein critical for the DNA damage response, specifically in repairing double-strand breaks (DSBs) via the classical non-homologous end joining (NHEJ) pathway. It forms a heterodimer with xrcc6/Ku70, creating the Ku70:Ku80 heterodimer (Ku complex), which serves as a DNA end-binding complex. It primarily binds DSBs and recruits essential repair factors, assembling the core long-range NHEJ complex to facilitate the alignment and ligation of broken DNA ends.","DNA-binding protein critical for the DNA damage response, specifically in repairing double-strand breaks (DSBs) via the classical non-homologous end joining (NHEJ) pathway. It forms a heterodimer with xrcc6/Ku70, creating the Ku70:Ku80 heterodimer (Ku complex), which serves as a DNA end-binding complex. It primarily binds DSBs and recruits essential repair factors, assembling the core long-range NHEJ complex to facilitate the alignment and ligation of broken DNA ends.",,,,,,,GO:0005524; GO:0003684; GO:0003678; GO:0003690; GO:0016787; GO:0042162,GO:0003690,GO:0003677; GO:0003684,GO:0003677; GO:0003684,GO:0003677; GO:0005524,GO:0003677,0.531,0.6116,0.6116,0.6962,0.5335,5,0.5968,0.6244,yes
NRAM_I04A1,Q6DPL2,ESM2Text,Viruses,449,"Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft- association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.","A DNA-binding protein, its activity is stimulated by binding of a still unidentified sugar donor. May be involved in 2 to 5 carbohydrate binding steps.",No,No,No,No,No,not-Yes,GO:0004308; GO:0042802; GO:0046872,GO:0003677,,GO:0003677,,,0.2943,,0.2943,,,2,0.2943,0.3485,no
NRAM_I04A1,Q6DPL2,Prot2Text,Viruses,449,"Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft- association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.","A DNA-binding protein, its activity is stimulated by binding of a still unidentified sugar donor. May be involved in 2 to 5 carbohydrate binding steps.",No,No,No,No,No,not-Yes,GO:0004308; GO:0042802; GO:0046872,GO:0003677,,GO:0003677,,GO:0003677,0.2943,,0.2943,,0.2943,3,0.2943,0.3485,no
NRAM_I04A1,Q6DPL2,ProtT3,Viruses,449,"Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft- association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.","Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004308; GO:0042802; GO:0046872,GO:0004308,GO:0004308,GO:0004308,GO:0004308,GO:0004308,0.5473,0.5473,0.5473,0.5473,0.5473,5,0.5473,0.3485,no
NRAM_I04A1,Q6DPL2,ProtTale,Viruses,449,"Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft- association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.","Attaches the virus to host cellular receptor, inducing endocytosis of the virion. In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and cell membrane.",No,No,No,No,No,not-Yes,GO:0004308; GO:0042802; GO:0046872,,,,,,,,,,,0,,0.3485,no
NRAM_I04A1,Q6DPL2,Protein2Text,Viruses,449,"Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft- association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.",The molecular function of the protein is catalyzing the removal of terminal sialic acid residues from glycoproteins and glycolipids. This process is known as sialidase activity.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004308; GO:0042802; GO:0046872,GO:0004308,GO:0004308,GO:0004308,GO:0004308,GO:0004308,0.5473,0.5473,0.5473,0.5473,0.5473,5,0.5473,0.3485,no
NRAM_I04A1,Q6DPL2,Reference,Viruses,449,"Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft- association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.","Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft- association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.",,,,,,,GO:0004308; GO:0042802; GO:0046872,GO:0004308,GO:0004308,GO:0004308,GO:0004308,GO:0004308,0.5473,0.5473,0.5473,0.5473,0.5473,5,0.5473,0.3485,no
AGAA_MICTH,Q6F4N4,ESM2Text,Bacteria,433,"Endo-type beta-agarase, which produces neoagarotetraose (NA4) as the main final product, with a small amount of neoagarohexaose (NA6) and neoagarobiose (NA2).","Cleaves the beta-1,4-linkages between beta-D-galactose and alpha-L-3,6-anhydro-galactose residues in agarose. Involved in the degradation of agarose, a chromogenic component of the bacterial cell wall.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0033916; GO:0030246,GO:0016798,GO:0004553,GO:0016161,GO:0004553,GO:0016798,0.5572,0.6324,0.4694,0.6324,0.5572,5,0.5697,0.3099,no
AGAA_MICTH,Q6F4N4,Prot2Text,Bacteria,433,"Endo-type beta-agarase, which produces neoagarotetraose (NA4) as the main final product, with a small amount of neoagarohexaose (NA6) and neoagarobiose (NA2).","Cleaves the beta-1,4-linkages between beta-D-galactose and alpha-L-3,6-anhydro-galactose residues in agarose. Cleaves agarose in a random manner with retention of the anomeric-bond configuration, producing beta-anomers that give rise progressively to alpha-anomers when mutarotation takes place.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0033916; GO:0030246,GO:0004553,,GO:0016798,GO:0016787,GO:0016798,0.6324,,0.5572,0.4887,0.5572,4,0.5589,0.3099,no
AGAA_MICTH,Q6F4N4,ProtT3,Bacteria,433,"Endo-type beta-agarase, which produces neoagarotetraose (NA4) as the main final product, with a small amount of neoagarohexaose (NA6) and neoagarobiose (NA2).",Secreted. Belongs to the glycosyl hydrolase 16 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0033916; GO:0030246,GO:0016798,GO:0016798,GO:0016798,GO:0004553,GO:0016798,0.5572,0.5572,0.5572,0.6324,0.5572,5,0.5722,0.3099,no
AGAA_MICTH,Q6F4N4,ProtTale,Bacteria,433,"Endo-type beta-agarase, which produces neoagarotetraose (NA4) as the main final product, with a small amount of neoagarohexaose (NA6) and neoagarobiose (NA2).","Cleaves the sulfated polysaccharide porphyran at the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6- sulfate, forming mainly the disaccharide alpha-L-galactopyranose-6- sulfate-(1->3)-beta-D-galactose.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0033916; GO:0030246,GO:0004553,GO:0004553,GO:0016798,GO:0016798,GO:0004553,0.6324,0.6324,0.5572,0.5572,0.6324,5,0.6023,0.3099,no
AGAA_MICTH,Q6F4N4,Protein2Text,Bacteria,433,"Endo-type beta-agarase, which produces neoagarotetraose (NA4) as the main final product, with a small amount of neoagarohexaose (NA6) and neoagarobiose (NA2).","The molecular function of this protein is to catalyze the breakdown of cellulose, a complex carbohydrate found in plant cell walls. It is a beta-1,4-glucanase, which means it hydrolyzes the beta-1,4-glycosidic bonds between glucose molecules in cellulose. This process is an important step in the degradation of cellulose, allowing the protein to break down cellulose into simpler sugars that can be used as a source of energy.",No,No,No,No,No,not-Yes,GO:0033916; GO:0030246,GO:0030245; GO:0008810,GO:0008810; GO:0030245,GO:0008810,GO:0008810,GO:0030245; GO:0008810,0.4039,0.4039,0.5386,0.5386,0.4039,5,0.4578,0.3099,no
AGAA_MICTH,Q6F4N4,Reference,Bacteria,433,"Endo-type beta-agarase, which produces neoagarotetraose (NA4) as the main final product, with a small amount of neoagarohexaose (NA6) and neoagarobiose (NA2).","Endo-type beta-agarase, which produces neoagarotetraose (NA4) as the main final product, with a small amount of neoagarohexaose (NA6) and neoagarobiose (NA2).",,,,,,,GO:0033916; GO:0030246,GO:0004553,GO:0016798,GO:0016798,GO:0016798,GO:0016798,0.6324,0.5572,0.5572,0.5572,0.5572,5,0.5722,0.3099,no
FAD1_CANGA,Q6FNA9,ESM2Text,Eukaryota,304,Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.,Adenylates FMN to FAD.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0003919; GO:0000287,GO:0003919,GO:0003919,GO:0003919,GO:0003919,GO:0003919,0.529,0.529,0.529,0.529,0.529,5,0.529,0.293,no
FAD1_CANGA,Q6FNA9,Prot2Text,Eukaryota,304,Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.,"With CysN forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.",No,No,No,No,No,not-Yes,GO:0005524; GO:0003919; GO:0000287,GO:0004781,GO:0004781,GO:0004779,GO:0004781; GO:0005525,GO:0004781,0.3532,0.3532,0.4025,0.6112,0.3532,5,0.4147,0.293,no
FAD1_CANGA,Q6FNA9,ProtT3,Eukaryota,304,Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.,Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. In the C-terminal section; belongs to the PAPS reductase family. FAD1 subfamily,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0003919; GO:0000287,GO:0003919,GO:0003919,GO:0003919; GO:0005524,GO:0003919,GO:0003919,0.529,0.529,0.8511,0.529,0.529,5,0.5934,0.293,no
FAD1_CANGA,Q6FNA9,ProtTale,Eukaryota,304,Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.,Catalyzes the synthesis of L-glutamate from 2-oxoglutarate and 2 molecules of ATP.,No,No,No,No,No,not-Yes,GO:0005524; GO:0003919; GO:0000287,GO:0016874,GO:0016874,GO:0016874; GO:0005524,GO:0004356,GO:0016874,0.2159,0.2159,0.5781,0.1036,0.2159,5,0.2659,0.293,no
FAD1_CANGA,Q6FNA9,Protein2Text,Eukaryota,304,Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.,"The molecular function of this protein is not explicitly stated in the provided information. However, based on its name, it can be inferred that this protein is involved in the synthesis of nucleotides, specifically as a subunit of the ATP sulfurylase enzyme. ATP sulfurylase is an enzyme that catalyzes the reaction of ATP and sulfate to produce adenosine 5'-phosphosulfate (APS) and pyrophosphate. The protein is likely a catalytic subunit of this enzyme, responsible for binding and activating sulfate for the reaction.",Vague,No,Vague,Vague,No,not-Yes,GO:0005524; GO:0003919; GO:0000287,,,GO:0004781,GO:0004781,,,,0.3532,0.3532,,2,0.3532,0.293,no
FAD1_CANGA,Q6FNA9,Reference,Eukaryota,304,Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.,Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.,,,,,,,GO:0005524; GO:0003919; GO:0000287,GO:0003919,GO:0003919,GO:0003919; GO:0005524,GO:0003919,GO:0003919,0.529,0.529,0.8511,0.529,0.529,5,0.5934,0.293,no
VPS15_CANGA,Q6FRH8,ESM2Text,Eukaryota,1410,"Serine/threonine-protein kinase that plays a role in signaling in modulation of host immune response, intracellular survival and virulence. Required for impediment of phagosomal maturation in THP-1 macrophages. Regulatory subunit of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Within the PS34 PI3-kinase complex I, VPS15-mediated phosphorylation of VPS34 may be required for recruiting VPS34 to the membrane but not for activation of its PI3K activity. Is also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). By regulating VPS34 kinase activity, VPS15 appears to be essential for the efficient delivery of soluble hydrolases to the yeast vacuole.",Mediates the GTPase activity of the CDC28-GDP1:CUL1 E3 ubiquitin-protein ligase complex.,No,No,No,No,Maybe,not-Yes,GO:0005524; GO:0004674; GO:0043130,GO:0005096,GO:0005096,,,,0.0788,0.0788,,,,2,0.0788,0.5377,yes
VPS15_CANGA,Q6FRH8,Prot2Text,Eukaryota,1410,"Serine/threonine-protein kinase that plays a role in signaling in modulation of host immune response, intracellular survival and virulence. Required for impediment of phagosomal maturation in THP-1 macrophages. Regulatory subunit of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Within the PS34 PI3-kinase complex I, VPS15-mediated phosphorylation of VPS34 may be required for recruiting VPS34 to the membrane but not for activation of its PI3K activity. Is also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). By regulating VPS34 kinase activity, VPS15 appears to be essential for the efficient delivery of soluble hydrolases to the yeast vacuole.",Protein kinase involved in the regulation of mitotic metaphase and G2/M transition. Required for spindle disassembly during prophase. Also involved in the correct localization of septins at the bud neck during cell division.,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0005524; GO:0004674; GO:0043130,GO:0004672,GO:0004672,GO:0004672,GO:0004674,GO:0004672,0.4961,0.4961,0.4961,0.5365,0.4961,5,0.5042,0.5377,yes
VPS15_CANGA,Q6FRH8,ProtT3,Eukaryota,1410,"Serine/threonine-protein kinase that plays a role in signaling in modulation of host immune response, intracellular survival and virulence. Required for impediment of phagosomal maturation in THP-1 macrophages. Regulatory subunit of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Within the PS34 PI3-kinase complex I, VPS15-mediated phosphorylation of VPS34 may be required for recruiting VPS34 to the membrane but not for activation of its PI3K activity. Is also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). By regulating VPS34 kinase activity, VPS15 appears to be essential for the efficient delivery of soluble hydrolases to the yeast vacuole.",Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily,Maybe,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0004674; GO:0043130,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,0.8285,0.8285,0.8285,0.8285,0.5365,5,0.7701,0.5377,yes
VPS15_CANGA,Q6FRH8,ProtTale,Eukaryota,1410,"Serine/threonine-protein kinase that plays a role in signaling in modulation of host immune response, intracellular survival and virulence. Required for impediment of phagosomal maturation in THP-1 macrophages. Regulatory subunit of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Within the PS34 PI3-kinase complex I, VPS15-mediated phosphorylation of VPS34 may be required for recruiting VPS34 to the membrane but not for activation of its PI3K activity. Is also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). By regulating VPS34 kinase activity, VPS15 appears to be essential for the efficient delivery of soluble hydrolases to the yeast vacuole.",Involved in cytokinesis. Required for vesicle trafficking from the Golgi complex to the plasma membrane.,No,Vague,No,No,No,not-Yes,GO:0005524; GO:0004674; GO:0043130,,,,,,,,,,,0,,0.5377,yes
VPS15_CANGA,Q6FRH8,Protein2Text,Eukaryota,1410,"Serine/threonine-protein kinase that plays a role in signaling in modulation of host immune response, intracellular survival and virulence. Required for impediment of phagosomal maturation in THP-1 macrophages. Regulatory subunit of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Within the PS34 PI3-kinase complex I, VPS15-mediated phosphorylation of VPS34 may be required for recruiting VPS34 to the membrane but not for activation of its PI3K activity. Is also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). By regulating VPS34 kinase activity, VPS15 appears to be essential for the efficient delivery of soluble hydrolases to the yeast vacuole.","The molecular function of this protein is not explicitly stated in the provided information. However, based on its name, it is likely to be involved in RNA-related processes, such as RNA degradation or modification. Specifically, the name ""RNA helicase"" suggests that this protein may play a role in unwinding RNA structures, which is a common function of helicases.",No,No,Vague,Vague,No,not-Yes,GO:0005524; GO:0004674; GO:0043130,GO:0003724,GO:0004003; GO:0003724,GO:0003724,GO:0003724,GO:0003724,0.1112,0.1204,0.1112,0.1112,0.1112,5,0.113,0.5377,yes
VPS15_CANGA,Q6FRH8,Reference,Eukaryota,1410,"Serine/threonine-protein kinase that plays a role in signaling in modulation of host immune response, intracellular survival and virulence. Required for impediment of phagosomal maturation in THP-1 macrophages. Regulatory subunit of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Within the PS34 PI3-kinase complex I, VPS15-mediated phosphorylation of VPS34 may be required for recruiting VPS34 to the membrane but not for activation of its PI3K activity. Is also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). By regulating VPS34 kinase activity, VPS15 appears to be essential for the efficient delivery of soluble hydrolases to the yeast vacuole.","Serine/threonine-protein kinase that plays a role in signaling in modulation of host immune response, intracellular survival and virulence. Required for impediment of phagosomal maturation in THP-1 macrophages. Regulatory subunit of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Within the PS34 PI3-kinase complex I, VPS15-mediated phosphorylation of VPS34 may be required for recruiting VPS34 to the membrane but not for activation of its PI3K activity. Is also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). By regulating VPS34 kinase activity, VPS15 appears to be essential for the efficient delivery of soluble hydrolases to the yeast vacuole.",,,,,,,GO:0005524; GO:0004674; GO:0043130,GO:0004674,GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.5365,0.5365,0.8285,0.8285,0.8285,5,0.7117,0.5377,yes
VPS34_CANGA,Q6FSR7,ESM2Text,Eukaryota,889,"Multifunctional phosphatidylinositol 3-kinase that plays a role in signaling in modulation of host immune response, intracellular survival and virulence. Catalytic subunit of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). Finally, it might also be involved in ethanol tolerance and cell wall integrity.",Required for vacuolar sorting and vacuolar biogenesis.,Vague,Vague,Vague,Maybe,Maybe,not-Yes,GO:0016303; GO:0005524; GO:0004672,,,,,,,,,,,0,,0.5597,yes
VPS34_CANGA,Q6FSR7,Prot2Text,Eukaryota,889,"Multifunctional phosphatidylinositol 3-kinase that plays a role in signaling in modulation of host immune response, intracellular survival and virulence. Catalytic subunit of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). Finally, it might also be involved in ethanol tolerance and cell wall integrity.",Phosphatidylinositol 3-kinase homolog required for vacuolar sorting and segregation.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0016303; GO:0005524; GO:0004672,GO:0016303,GO:0035004,GO:0046934,GO:0046934,GO:0035004,0.6633,0.0,0.5654,0.5654,0.0,5,0.3588,0.5597,yes
VPS34_CANGA,Q6FSR7,ProtT3,Eukaryota,889,"Multifunctional phosphatidylinositol 3-kinase that plays a role in signaling in modulation of host immune response, intracellular survival and virulence. Catalytic subunit of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). Finally, it might also be involved in ethanol tolerance and cell wall integrity.","Catalytic subunit of the PI3K complex required for cytoplasm to vacuole transport (Cvt), autophagy, mitophagy, and nucleophagy. Phosphorylates phosphatidylinositol 3-phosphate (PtdIns(3)P) to form phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Preautophagosomal structure membrane; Peripheral membrane protein Vacuole membrane; Peripheral membrane protein. Belongs to the PI3/PI4-kinase family. Type III PI3K subfamily",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0016303; GO:0005524; GO:0004672,GO:0016301; GO:0005524,GO:0016303,GO:0046934; GO:0005524,GO:0044024,GO:0016308,0.8125,0.6633,0.8432,0.4709,0.5654,5,0.6711,0.5597,yes
VPS34_CANGA,Q6FSR7,ProtTale,Eukaryota,889,"Multifunctional phosphatidylinositol 3-kinase that plays a role in signaling in modulation of host immune response, intracellular survival and virulence. Catalytic subunit of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). Finally, it might also be involved in ethanol tolerance and cell wall integrity.","Phosphatidylinositol-4-phosphate 5-kinase that mediates synthesis of phosphatidylinositol-4-phosphate (PtdIns4P), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3).",No,No,No,No,Maybe,not-Yes,GO:0016303; GO:0005524; GO:0004672,GO:0016308,GO:0016308,GO:0016308; GO:0005524,GO:0016307,GO:0016308,0.5654,0.5654,0.8432,0.0,0.5654,5,0.5079,0.5597,yes
VPS34_CANGA,Q6FSR7,Protein2Text,Eukaryota,889,"Multifunctional phosphatidylinositol 3-kinase that plays a role in signaling in modulation of host immune response, intracellular survival and virulence. Catalytic subunit of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). Finally, it might also be involved in ethanol tolerance and cell wall integrity.",This protein is involved in molecular function related to calcium ion binding.,No,No,No,No,No,not-Yes,GO:0016303; GO:0005524; GO:0004672,GO:0005509,GO:0005509,GO:0005509,GO:0005509,GO:0005509,0.1622,0.1622,0.1622,0.1622,0.1622,5,0.1622,0.5597,yes
VPS34_CANGA,Q6FSR7,Reference,Eukaryota,889,"Multifunctional phosphatidylinositol 3-kinase that plays a role in signaling in modulation of host immune response, intracellular survival and virulence. Catalytic subunit of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). Finally, it might also be involved in ethanol tolerance and cell wall integrity.","Multifunctional phosphatidylinositol 3-kinase that plays a role in signaling in modulation of host immune response, intracellular survival and virulence. Catalytic subunit of the autophagy-specific VPS34 PI3-kinase complex I essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). Finally, it might also be involved in ethanol tolerance and cell wall integrity.",,,,,,,GO:0016303; GO:0005524; GO:0004672,GO:0046934,GO:0016303; GO:0005524,GO:0035004; GO:0005524,GO:0046934; GO:0005524,GO:0016303; GO:0005524,0.5654,0.9215,0.5265,0.8432,0.9215,5,0.7556,0.5597,yes
L_LASV,Q6GWS6,ESM2Text,Viruses,2219,"RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate. During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs. These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are heterogeneous and not polyadenylated. The replicase function is to direct synthesis of antigenomic and genomic RNA which are encapsidated and non capped. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated. These processes may be regulated by proteins N and Z in a dose-dependent manner. Z protein inhibits the viral polymerase L und thus the viral transcription and RNA synthesis.",As component of the WDR11 complex acts together with TBC1D23 to facilitate the golgin-mediated capture of vesicles generated using AP-1.,No,No,No,No,No,not-Yes,GO:0016787; GO:0046872; GO:0000166; GO:0003968,,,,,,,,,,,0,,0.6323,yes
L_LASV,Q6GWS6,Prot2Text,Viruses,2219,"RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate. During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs. These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are heterogeneous and not polyadenylated. The replicase function is to direct synthesis of antigenomic and genomic RNA which are encapsidated and non capped. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated. These processes may be regulated by proteins N and Z in a dose-dependent manner. Z protein inhibits the viral polymerase L und thus the viral transcription and RNA synthesis.",As component of the WDR11 complex acts together with TBC1D23 to facilitate the golgin-mediated capture of vesicles generated using AP-1.,No,No,No,No,No,not-Yes,GO:0016787; GO:0046872; GO:0000166; GO:0003968,,,,,,,,,,,0,,0.6323,yes
L_LASV,Q6GWS6,ProtT3,Viruses,2219,"RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate. During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs. These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are heterogeneous and not polyadenylated. The replicase function is to direct synthesis of antigenomic and genomic RNA which are encapsidated and non capped. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated. These processes may be regulated by proteins N and Z in a dose-dependent manner. Z protein inhibits the viral polymerase L und thus the viral transcription and RNA synthesis.","Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). Nucleus. SIMILAR",No,No,No,No,No,not-Yes,GO:0016787; GO:0046872; GO:0000166; GO:0003968,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.1732,0.1732,0.1732,0.1732,0.1732,5,0.1732,0.6323,yes
L_LASV,Q6GWS6,ProtTale,Viruses,2219,"RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate. During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs. These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are heterogeneous and not polyadenylated. The replicase function is to direct synthesis of antigenomic and genomic RNA which are encapsidated and non capped. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated. These processes may be regulated by proteins N and Z in a dose-dependent manner. Z protein inhibits the viral polymerase L und thus the viral transcription and RNA synthesis.","RNA-directed RNA polymerase that catalyzes the transcription of viral mRNAs, their capping and polyadenylation. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The viral polymerase binds to the genomic RNA at the 3' leader promoter, and transcribes subsequently all viral mRNAs with a decreasing efficiency. The first gene is the most transcribed, and the last the least transcribed. The viral phosphoprotein acts as a processivity factor. Capping is concomitant with initiation of mRNA transcription. Indeed, a GDP polyribonucleotidyl transferase (PRNTase) adds the cap structure when the nascent RNA",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016787; GO:0046872; GO:0000166; GO:0003968,GO:0003968,GO:0003968,GO:0003968,GO:0003968,GO:0003968,0.4825,0.4825,0.4825,0.4825,0.4825,5,0.4825,0.6323,yes
L_LASV,Q6GWS6,Protein2Text,Viruses,2219,"RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate. During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs. These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are heterogeneous and not polyadenylated. The replicase function is to direct synthesis of antigenomic and genomic RNA which are encapsidated and non capped. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated. These processes may be regulated by proteins N and Z in a dose-dependent manner. Z protein inhibits the viral polymerase L und thus the viral transcription and RNA synthesis.","The molecular function of this protein is related to the nucleotide binding and hydrolysis. It is a part of the 40S ribosomal protein subunit complex, which is involved in the translation process of the cell. The 40S ribosomal subunit is responsible for the initiation of translation, where it binds to the mRNA and forms the 40S initiation complex. The 40S initiation complex then scans the mRNA until it finds the start codon, where it binds to the 60S ribosomal subunit to form the 80S initiation complex, which is responsible for the elongation phase of translation.

In more detail, this protein is likely to have a molecular function related to the binding and hydrolysis of nucleotides, such as ATP or GTP, which are essential for the function of the 40S ribosomal subunit. The protein may also have a role in the regulation of translation, by modulating the activity of the 40S ribosomal subunit or by interacting with other proteins that regulate translation.

It is worth noting that the specific molecular function of this protein is not well understood, and more research is needed to determine its exact role in the cell.",No,No,No,No,No,not-Yes,GO:0016787; GO:0046872; GO:0000166; GO:0003968,,,,,,,,,,,0,,0.6323,yes
L_LASV,Q6GWS6,Reference,Viruses,2219,"RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate. During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs. These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are heterogeneous and not polyadenylated. The replicase function is to direct synthesis of antigenomic and genomic RNA which are encapsidated and non capped. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated. These processes may be regulated by proteins N and Z in a dose-dependent manner. Z protein inhibits the viral polymerase L und thus the viral transcription and RNA synthesis.","RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate. During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs. These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are heterogeneous and not polyadenylated. The replicase function is to direct synthesis of antigenomic and genomic RNA which are encapsidated and non capped. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated. These processes may be regulated by proteins N and Z in a dose-dependent manner. Z protein inhibits the viral polymerase L und thus the viral transcription and RNA synthesis.",,,,,,,GO:0016787; GO:0046872; GO:0000166; GO:0003968,GO:0003968; GO:0004519,GO:0003968; GO:0004519,GO:0003968; GO:0004519,GO:0003968; GO:0003723,GO:0003968; GO:0003723,0.5063,0.5063,0.5063,0.5296,0.5296,5,0.5156,0.6323,yes
DSP1_ORYSJ,Q6K461,ESM2Text,Eukaryota,222,"Cleaves the beta-phosphate at the 5-position of soluble inositol pyrophosphates. Has highest activity on 5- diphosphoinositol 1,2,3,4,6-pentakisphosphate (5-InsP(7)). Possesses phosphotyrosine phosphatase activity in vitro. May contribute to regulation of drought stress responses.",Probable tyrosine-protein phosphatase that acts as negative regulator of defense responses against the fungal pathogen Magnaporthe oryzae.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0052845; GO:0016791,GO:0004725,GO:0004725,GO:0004725,GO:0004725,GO:0004725,0.5504,0.5504,0.5504,0.5504,0.5504,5,0.5504,0.4634,no
DSP1_ORYSJ,Q6K461,Prot2Text,Eukaryota,222,"Cleaves the beta-phosphate at the 5-position of soluble inositol pyrophosphates. Has highest activity on 5- diphosphoinositol 1,2,3,4,6-pentakisphosphate (5-InsP(7)). Possesses phosphotyrosine phosphatase activity in vitro. May contribute to regulation of drought stress responses.",Probable tyrosine-protein phosphatase that acts as negative regulator of defense responses against the bacterial pathogen Pseudomonas syringae pv tomato strain DC3000.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0052845; GO:0016791,GO:0004725,GO:0004725,GO:0004725,GO:0004725,GO:0004725,0.5504,0.5504,0.5504,0.5504,0.5504,5,0.5504,0.4634,no
DSP1_ORYSJ,Q6K461,ProtT3,Eukaryota,222,"Cleaves the beta-phosphate at the 5-position of soluble inositol pyrophosphates. Has highest activity on 5- diphosphoinositol 1,2,3,4,6-pentakisphosphate (5-InsP(7)). Possesses phosphotyrosine phosphatase activity in vitro. May contribute to regulation of drought stress responses.",May have phosphatase activity. Belongs to the protein-tyrosine phosphatase family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0052845; GO:0016791,GO:0004725,GO:0004725,GO:0004725,GO:0004725,GO:0004725,0.5504,0.5504,0.5504,0.5504,0.5504,5,0.5504,0.4634,no
DSP1_ORYSJ,Q6K461,ProtTale,Eukaryota,222,"Cleaves the beta-phosphate at the 5-position of soluble inositol pyrophosphates. Has highest activity on 5- diphosphoinositol 1,2,3,4,6-pentakisphosphate (5-InsP(7)). Possesses phosphotyrosine phosphatase activity in vitro. May contribute to regulation of drought stress responses.",May be involved in the regulation of sulfur metabolism.,No,No,No,No,No,not-Yes,GO:0052845; GO:0016791,,,,,,,,,,,0,,0.4634,no
DSP1_ORYSJ,Q6K461,Protein2Text,Eukaryota,222,"Cleaves the beta-phosphate at the 5-position of soluble inositol pyrophosphates. Has highest activity on 5- diphosphoinositol 1,2,3,4,6-pentakisphosphate (5-InsP(7)). Possesses phosphotyrosine phosphatase activity in vitro. May contribute to regulation of drought stress responses.",The molecular function of this protein is phosphatase activity.,Vague,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0052845; GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,0.7452,0.7452,0.7452,0.7452,0.7452,5,0.7452,0.4634,no
DSP1_ORYSJ,Q6K461,Reference,Eukaryota,222,"Cleaves the beta-phosphate at the 5-position of soluble inositol pyrophosphates. Has highest activity on 5- diphosphoinositol 1,2,3,4,6-pentakisphosphate (5-InsP(7)). Possesses phosphotyrosine phosphatase activity in vitro. May contribute to regulation of drought stress responses.","Cleaves the beta-phosphate at the 5-position of soluble inositol pyrophosphates. Has highest activity on 5- diphosphoinositol 1,2,3,4,6-pentakisphosphate (5-InsP(7)). Possesses phosphotyrosine phosphatase activity in vitro. May contribute to regulation of drought stress responses.",,,,,,,GO:0052845; GO:0016791,GO:0016791,GO:0016791,GO:0042578; GO:0004725,GO:0016791,GO:0004445,0.7452,0.7452,0.6824,0.7452,0.513,5,0.6862,0.4634,no
THS_METMP,Q6LX38,ESM2Text,Archaea,543,"Molecular chaperone; binds unfolded polypeptides and stimulates protein folding in a nucleotide-dependent manner. Cooperative ATP hydrolysis in each ring closes the lid, which is required for substrate folding. ATP and AMP-PNP allow substrate refolding but ADP does not. Hydrolyzes CTP as well as ATP; UTP and GTP are poorer substrates.","Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0016887; GO:0140662; GO:0051082,GO:0051082; GO:0016887,GO:0051082; GO:0016887,GO:0051082; GO:0016887,GO:0051082,GO:0051082,0.745,0.745,0.745,0.4951,0.4951,5,0.645,0.2673,no
THS_METMP,Q6LX38,Prot2Text,Archaea,543,"Molecular chaperone; binds unfolded polypeptides and stimulates protein folding in a nucleotide-dependent manner. Cooperative ATP hydrolysis in each ring closes the lid, which is required for substrate folding. ATP and AMP-PNP allow substrate refolding but ADP does not. Hydrolyzes CTP as well as ATP; UTP and GTP are poorer substrates.","Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0016887; GO:0140662; GO:0051082,GO:0051082; GO:0005524,GO:0051082; GO:0005524,GO:0051082,GO:0051082; GO:0005524,GO:0051082; GO:0016887,0.7184,0.7184,0.4951,0.7184,0.745,5,0.6791,0.2673,no
THS_METMP,Q6LX38,ProtT3,Archaea,543,"Molecular chaperone; binds unfolded polypeptides and stimulates protein folding in a nucleotide-dependent manner. Cooperative ATP hydrolysis in each ring closes the lid, which is required for substrate folding. ATP and AMP-PNP allow substrate refolding but ADP does not. Hydrolyzes CTP as well as ATP; UTP and GTP are poorer substrates.","Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity. Belongs to the TCP-1 chaperonin family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0140662; GO:0051082,GO:0051082; GO:0005524,GO:0051082; GO:0005524,GO:0051082; GO:0005524,GO:0051082; GO:0016887,GO:0051082; GO:0016887,0.7184,0.7184,0.7184,0.745,0.745,5,0.729,0.2673,no
THS_METMP,Q6LX38,ProtTale,Archaea,543,"Molecular chaperone; binds unfolded polypeptides and stimulates protein folding in a nucleotide-dependent manner. Cooperative ATP hydrolysis in each ring closes the lid, which is required for substrate folding. ATP and AMP-PNP allow substrate refolding but ADP does not. Hydrolyzes CTP as well as ATP; UTP and GTP are poorer substrates.","Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of actin, tubulin and other proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0016887; GO:0140662; GO:0051082,GO:0051082,GO:0016887; GO:0051082,GO:0051082; GO:0005524,,GO:0051082; GO:0005524,0.4951,0.745,0.7184,,0.7184,4,0.6692,0.2673,no
THS_METMP,Q6LX38,Protein2Text,Archaea,543,"Molecular chaperone; binds unfolded polypeptides and stimulates protein folding in a nucleotide-dependent manner. Cooperative ATP hydrolysis in each ring closes the lid, which is required for substrate folding. ATP and AMP-PNP allow substrate refolding but ADP does not. Hydrolyzes CTP as well as ATP; UTP and GTP are poorer substrates.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its name, it is likely that this protein is a component of the ribosome, which is a complex molecular machine that plays a central role in protein synthesis. The ribosome's molecular function is to translate messenger RNA (mRNA) into a specific sequence of amino acids that fold into a protein. 

In particular, this protein is likely to be a ribosomal protein, which is a small subunit protein that makes up the ribosome. Ribosomal proteins are involved in various steps of protein synthesis, including translation initiation, elongation, and termination. They play a crucial role in maintaining the structure and function of the ribosome, and are essential for proper protein synthesis. 

However, without further information, it is difficult to provide a more specific description of the molecular function of this protein.",No,No,No,Vague,No,not-Yes,GO:0005524; GO:0016887; GO:0140662; GO:0051082,,,,,GO:0003735,,,,,0.1803,1,0.1803,0.2673,no
THS_METMP,Q6LX38,Reference,Archaea,543,"Molecular chaperone; binds unfolded polypeptides and stimulates protein folding in a nucleotide-dependent manner. Cooperative ATP hydrolysis in each ring closes the lid, which is required for substrate folding. ATP and AMP-PNP allow substrate refolding but ADP does not. Hydrolyzes CTP as well as ATP; UTP and GTP are poorer substrates.","Molecular chaperone; binds unfolded polypeptides and stimulates protein folding in a nucleotide-dependent manner. Cooperative ATP hydrolysis in each ring closes the lid, which is required for substrate folding. ATP and AMP-PNP allow substrate refolding but ADP does not. Hydrolyzes CTP as well as ATP; UTP and GTP are poorer substrates.",,,,,,,GO:0005524; GO:0016887; GO:0140662; GO:0051082,GO:0051082; GO:0016887,GO:0051082; GO:0016887,GO:0016887; GO:0051082,GO:0005524; GO:0051082; GO:0016887,GO:0005524; GO:0016887; GO:0051082,0.745,0.745,0.745,0.9007,0.9007,5,0.8073,0.2673,no
TRAI3_ECOLX,Q6TDU5,ESM2Text,Bacteria,1756,"Conjugative DNA transfer (CDT) is the unidirectional transfer of ssDNA plasmid from a donor to a recipient cell. It is the central mechanism by which antibiotic resistance and virulence factors are propagated in bacterial populations. Part of the relaxosome, which facilitates a site- and strand-specific cut at the nic site in the origin of transfer by TraI. Relaxosome formation requires binding of IHF and TraY to the oriT region, which then facilitates binding of TraI relaxase. TraI forms a covalent 5'- phosphotyrosine intermediate linkage with the nicked ssDNA. The trans- esterified single-stranded T-strand moves from the donor cell to the recipient cell in a 5'-3' direction, with the DNA helicase activity of TraI unwinding the DNA. DNA transfer occurs via the F pilus, an intercellular junction mediated by a type IV secretion system (T4SS), with TraD providing the means to link the relaxosome to the conjugative pore. The relaxase completes DNA transfer by reversing the covalent phosphotyrosine linkage, presumably recircularizing and releasing the plasmid DNA.","TraI has also been identified as DNA helicase I. DNA. helicase I is a potent, highly processive DNA-dependent ATPase, able to unwind about 1.1 kb dsDNA per second in a 5' to 3' manner.",Yes,Maybe,Yes,Yes,Maybe,Yes,GO:0005524; GO:0003677; GO:0003678; GO:0016818; GO:0046872,GO:0003678; GO:0005524; GO:0008094,GO:0003678; GO:0016887; GO:0005524,GO:0003678; GO:0016887,GO:0003678,GO:0004003,0.6787,0.7162,0.5076,0.4034,0.4034,5,0.5419,0.4858,no
TRAI3_ECOLX,Q6TDU5,Prot2Text,Bacteria,1756,"Conjugative DNA transfer (CDT) is the unidirectional transfer of ssDNA plasmid from a donor to a recipient cell. It is the central mechanism by which antibiotic resistance and virulence factors are propagated in bacterial populations. Part of the relaxosome, which facilitates a site- and strand-specific cut at the nic site in the origin of transfer by TraI. Relaxosome formation requires binding of IHF and TraY to the oriT region, which then facilitates binding of TraI relaxase. TraI forms a covalent 5'- phosphotyrosine intermediate linkage with the nicked ssDNA. The trans- esterified single-stranded T-strand moves from the donor cell to the recipient cell in a 5'-3' direction, with the DNA helicase activity of TraI unwinding the DNA. DNA transfer occurs via the F pilus, an intercellular junction mediated by a type IV secretion system (T4SS), with TraD providing the means to link the relaxosome to the conjugative pore. The relaxase completes DNA transfer by reversing the covalent phosphotyrosine linkage, presumably recircularizing and releasing the plasmid DNA.","TraI has also been identified as DNA helicase I. DNA. helicase I is a potent, highly processive DNA-dependent ATPase, able to unwind about 1.1 kb dsDNA per second in a 5' to 3' manner.",Yes,Maybe,Yes,Yes,Maybe,Yes,GO:0005524; GO:0003677; GO:0003678; GO:0016818; GO:0046872,GO:0003678; GO:0008094,GO:0003678; GO:0008094,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678,0.4752,0.4752,0.6629,0.6629,0.4034,5,0.5359,0.4858,no
TRAI3_ECOLX,Q6TDU5,ProtT3,Bacteria,1756,"Conjugative DNA transfer (CDT) is the unidirectional transfer of ssDNA plasmid from a donor to a recipient cell. It is the central mechanism by which antibiotic resistance and virulence factors are propagated in bacterial populations. Part of the relaxosome, which facilitates a site- and strand-specific cut at the nic site in the origin of transfer by TraI. Relaxosome formation requires binding of IHF and TraY to the oriT region, which then facilitates binding of TraI relaxase. TraI forms a covalent 5'- phosphotyrosine intermediate linkage with the nicked ssDNA. The trans- esterified single-stranded T-strand moves from the donor cell to the recipient cell in a 5'-3' direction, with the DNA helicase activity of TraI unwinding the DNA. DNA transfer occurs via the F pilus, an intercellular junction mediated by a type IV secretion system (T4SS), with TraD providing the means to link the relaxosome to the conjugative pore. The relaxase completes DNA transfer by reversing the covalent phosphotyrosine linkage, presumably recircularizing and releasing the plasmid DNA.",The type IV secretion system VirB/VirD4 is a major virulence determinant for intracellular survival and replication,Maybe,Vague,Maybe,No,Vague,not-Yes,GO:0005524; GO:0003677; GO:0003678; GO:0016818; GO:0046872,,,,,,,,,,,0,,0.4858,no
TRAI3_ECOLX,Q6TDU5,ProtTale,Bacteria,1756,"Conjugative DNA transfer (CDT) is the unidirectional transfer of ssDNA plasmid from a donor to a recipient cell. It is the central mechanism by which antibiotic resistance and virulence factors are propagated in bacterial populations. Part of the relaxosome, which facilitates a site- and strand-specific cut at the nic site in the origin of transfer by TraI. Relaxosome formation requires binding of IHF and TraY to the oriT region, which then facilitates binding of TraI relaxase. TraI forms a covalent 5'- phosphotyrosine intermediate linkage with the nicked ssDNA. The trans- esterified single-stranded T-strand moves from the donor cell to the recipient cell in a 5'-3' direction, with the DNA helicase activity of TraI unwinding the DNA. DNA transfer occurs via the F pilus, an intercellular junction mediated by a type IV secretion system (T4SS), with TraD providing the means to link the relaxosome to the conjugative pore. The relaxase completes DNA transfer by reversing the covalent phosphotyrosine linkage, presumably recircularizing and releasing the plasmid DNA.",DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.,No,No,No,No,No,not-Yes,GO:0005524; GO:0003677; GO:0003678; GO:0016818; GO:0046872,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.136,0.136,0.136,0.136,0.136,5,0.136,0.4858,no
TRAI3_ECOLX,Q6TDU5,Protein2Text,Bacteria,1756,"Conjugative DNA transfer (CDT) is the unidirectional transfer of ssDNA plasmid from a donor to a recipient cell. It is the central mechanism by which antibiotic resistance and virulence factors are propagated in bacterial populations. Part of the relaxosome, which facilitates a site- and strand-specific cut at the nic site in the origin of transfer by TraI. Relaxosome formation requires binding of IHF and TraY to the oriT region, which then facilitates binding of TraI relaxase. TraI forms a covalent 5'- phosphotyrosine intermediate linkage with the nicked ssDNA. The trans- esterified single-stranded T-strand moves from the donor cell to the recipient cell in a 5'-3' direction, with the DNA helicase activity of TraI unwinding the DNA. DNA transfer occurs via the F pilus, an intercellular junction mediated by a type IV secretion system (T4SS), with TraD providing the means to link the relaxosome to the conjugative pore. The relaxase completes DNA transfer by reversing the covalent phosphotyrosine linkage, presumably recircularizing and releasing the plasmid DNA.",The molecular function of this protein is endonuclease.,No,Maybe,No,No,No,not-Yes,GO:0005524; GO:0003677; GO:0003678; GO:0016818; GO:0046872,GO:0004519,GO:0004519,GO:0004519,GO:0004519,GO:0004519,0.2007,0.2007,0.2007,0.2007,0.2007,5,0.2007,0.4858,no
TRAI3_ECOLX,Q6TDU5,Reference,Bacteria,1756,"Conjugative DNA transfer (CDT) is the unidirectional transfer of ssDNA plasmid from a donor to a recipient cell. It is the central mechanism by which antibiotic resistance and virulence factors are propagated in bacterial populations. Part of the relaxosome, which facilitates a site- and strand-specific cut at the nic site in the origin of transfer by TraI. Relaxosome formation requires binding of IHF and TraY to the oriT region, which then facilitates binding of TraI relaxase. TraI forms a covalent 5'- phosphotyrosine intermediate linkage with the nicked ssDNA. The trans- esterified single-stranded T-strand moves from the donor cell to the recipient cell in a 5'-3' direction, with the DNA helicase activity of TraI unwinding the DNA. DNA transfer occurs via the F pilus, an intercellular junction mediated by a type IV secretion system (T4SS), with TraD providing the means to link the relaxosome to the conjugative pore. The relaxase completes DNA transfer by reversing the covalent phosphotyrosine linkage, presumably recircularizing and releasing the plasmid DNA.","Conjugative DNA transfer (CDT) is the unidirectional transfer of ssDNA plasmid from a donor to a recipient cell. It is the central mechanism by which antibiotic resistance and virulence factors are propagated in bacterial populations. Part of the relaxosome, which facilitates a site- and strand-specific cut at the nic site in the origin of transfer by TraI. Relaxosome formation requires binding of IHF and TraY to the oriT region, which then facilitates binding of TraI relaxase. TraI forms a covalent 5'- phosphotyrosine intermediate linkage with the nicked ssDNA. The trans- esterified single-stranded T-strand moves from the donor cell to the recipient cell in a 5'-3' direction, with the DNA helicase activity of TraI unwinding the DNA. DNA transfer occurs via the F pilus, an intercellular junction mediated by a type IV secretion system (T4SS), with TraD providing the means to link the relaxosome to the conjugative pore. The relaxase completes DNA transfer by reversing the covalent phosphotyrosine linkage, presumably recircularizing and releasing the plasmid DNA.",,,,,,,GO:0005524; GO:0003677; GO:0003678; GO:0016818; GO:0046872,,GO:0003677; GO:0004519; GO:0004386,GO:0003678; GO:0003677,GO:0003677; GO:0003916; GO:0004386,GO:0003677; GO:0004386; GO:0005524,,0.5819,0.6622,0.6213,0.7689,4,0.6586,0.4858,no
BLO48_KLEPN,Q6XEC0,ESM2Text,Bacteria,265,"Class D beta-lactamase which confers resistance to the beta- lactam antibiotics, including amoxicillin, and moderate resistance to cephalosporins and carbapenems such as cephalothin and imipenem; in the DH10B strain of E.coli. Acts via hydrolysis of the beta-lactam ring. Has oxacillin-, cephalothin- and imipenem-hydrolyzing activities.",This is an oxacillin-hydrolyzing beta-lactamase.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008800; GO:0008658,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,0.6922,0.6922,0.6922,0.6922,0.6922,5,0.6922,0.4101,no
BLO48_KLEPN,Q6XEC0,Prot2Text,Bacteria,265,"Class D beta-lactamase which confers resistance to the beta- lactam antibiotics, including amoxicillin, and moderate resistance to cephalosporins and carbapenems such as cephalothin and imipenem; in the DH10B strain of E.coli. Acts via hydrolysis of the beta-lactam ring. Has oxacillin-, cephalothin- and imipenem-hydrolyzing activities.",Hydrolyzes both carbenicillin and oxacillin.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0008800; GO:0008658,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,0.6922,0.6922,0.6922,0.6922,0.6922,5,0.6922,0.4101,no
BLO48_KLEPN,Q6XEC0,ProtT3,Bacteria,265,"Class D beta-lactamase which confers resistance to the beta- lactam antibiotics, including amoxicillin, and moderate resistance to cephalosporins and carbapenems such as cephalothin and imipenem; in the DH10B strain of E.coli. Acts via hydrolysis of the beta-lactam ring. Has oxacillin-, cephalothin- and imipenem-hydrolyzing activities.",Hydrolyzes carbenicillin. Belongs to the class-D beta-lactamase family,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0008800; GO:0008658,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,0.6922,0.6922,0.6922,0.6922,0.6922,5,0.6922,0.4101,no
BLO48_KLEPN,Q6XEC0,ProtTale,Bacteria,265,"Class D beta-lactamase which confers resistance to the beta- lactam antibiotics, including amoxicillin, and moderate resistance to cephalosporins and carbapenems such as cephalothin and imipenem; in the DH10B strain of E.coli. Acts via hydrolysis of the beta-lactam ring. Has oxacillin-, cephalothin- and imipenem-hydrolyzing activities.",Hydrolyzes the beta-lactam ring of beta- lactam antibiotics.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008800; GO:0008658,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,0.6922,0.6922,0.6922,0.6922,0.6922,5,0.6922,0.4101,no
BLO48_KLEPN,Q6XEC0,Protein2Text,Bacteria,265,"Class D beta-lactamase which confers resistance to the beta- lactam antibiotics, including amoxicillin, and moderate resistance to cephalosporins and carbapenems such as cephalothin and imipenem; in the DH10B strain of E.coli. Acts via hydrolysis of the beta-lactam ring. Has oxacillin-, cephalothin- and imipenem-hydrolyzing activities.",The molecular function of this protein is a beta-lactamase.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008800; GO:0008658,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,0.6922,0.6922,0.6922,0.6922,0.6922,5,0.6922,0.4101,no
BLO48_KLEPN,Q6XEC0,Reference,Bacteria,265,"Class D beta-lactamase which confers resistance to the beta- lactam antibiotics, including amoxicillin, and moderate resistance to cephalosporins and carbapenems such as cephalothin and imipenem; in the DH10B strain of E.coli. Acts via hydrolysis of the beta-lactam ring. Has oxacillin-, cephalothin- and imipenem-hydrolyzing activities.","Class D beta-lactamase which confers resistance to the beta- lactam antibiotics, including amoxicillin, and moderate resistance to cephalosporins and carbapenems such as cephalothin and imipenem; in the DH10B strain of E.coli. Acts via hydrolysis of the beta-lactam ring. Has oxacillin-, cephalothin- and imipenem-hydrolyzing activities.",,,,,,,GO:0008800; GO:0008658,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,0.6922,0.6922,0.6922,0.6922,0.6922,5,0.6922,0.4101,no
PHYA_PENOX,Q6YNE9,ESM2Text,Eukaryota,461,"Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate. Myo-inositol 2-monophosphate is the end product.",Catalyzes the hydrolysis of inorganic orthophosphate from phytate. Releases 5 of the 6 phosphate groups to yield the end product myo-inositol 2-monophosphate. Specific for phytate.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003993; GO:0016158,GO:0016791,GO:0008707,GO:0008707,GO:0016791,GO:0016791,0.8113,0.7075,0.7075,0.8113,0.8113,5,0.7698,0.2391,no
PHYA_PENOX,Q6YNE9,Prot2Text,Eukaryota,461,"Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate. Myo-inositol 2-monophosphate is the end product.",Catalyzes the hydrolysis of inorganic orthophosphate from phytate.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0003993; GO:0016158,GO:0008707,GO:0016791,GO:0008707,GO:0004000,GO:0008707,0.7075,0.8113,0.7075,0.249,0.7075,5,0.6366,0.2391,no
PHYA_PENOX,Q6YNE9,ProtT3,Eukaryota,461,"Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate. Myo-inositol 2-monophosphate is the end product.",Catalyzes the hydrolysis of inorganic orthophosphate from phytate. Secreted. Belongs to the histidine acid phosphatase family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003993; GO:0016158,GO:0003993,GO:0003993,GO:0003993,GO:0003993,GO:0003993,0.8615,0.8615,0.8615,0.8615,0.8615,5,0.8615,0.2391,no
PHYA_PENOX,Q6YNE9,ProtTale,Eukaryota,461,"Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate. Myo-inositol 2-monophosphate is the end product.","Hydrolyzes phosphodiester bonds of nucleoside 5'-phosphates, yielding nucleoside 5'-monophosphates and a free purine or pyrimidine nucleoside. Prefers inosine 5'- monophosphate (IMP) to adenosine 5'-monophosphate (AMP), guanosine 5'-monophosphate (GMP) and cytidine 5'-monophosphate (cGMP) as substrates.",No,No,No,No,No,not-Yes,GO:0003993; GO:0016158,GO:0016787,GO:0008253,GO:0004528,GO:0016787,GO:0008253,0.5104,0.6034,0.4277,0.5104,0.6034,5,0.5311,0.2391,no
PHYA_PENOX,Q6YNE9,Protein2Text,Eukaryota,461,"Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate. Myo-inositol 2-monophosphate is the end product.","The molecular function of this protein is a phosphatase, specifically a phosphodiesterase, that catalyzes the hydrolysis of phosphodiester bonds, which is involved in breaking down nucleotides. This protein is involved in the degradation of nucleotides, which is essential for various cellular processes such as DNA and RNA metabolism.",No,No,No,No,Maybe,not-Yes,GO:0003993; GO:0016158,GO:0004528,GO:0004112,GO:0008081,GO:0016788,GO:0004528,0.4277,0.505,0.5914,0.6105,0.4277,5,0.5125,0.2391,no
PHYA_PENOX,Q6YNE9,Reference,Eukaryota,461,"Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate. Myo-inositol 2-monophosphate is the end product.","Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate. Myo-inositol 2-monophosphate is the end product.",,,,,,,GO:0003993; GO:0016158,GO:0016791,GO:0008441,GO:0016791,GO:0008707; GO:0003993,GO:0003993,0.8113,0.6034,0.8113,0.8845,0.8615,5,0.7944,0.2391,no
AURH_STRTU,Q70KH6,ESM2Text,Bacteria,406,"Bifunctional cytochrome P450 protein involved in the biosynthesis of the antibiotic aureothin, a nitroaryl polyketide metabolite with antifungal, cytotoxic and insecticidal activities. Catalyzes the hydroxylation of luteothin (also called deoxyaureothin), leading to the formation of the intermediate (7R)-7-hydroxydeoxyaureothin, followed by the formation of the aureothin tetrahydrofuran ring, the final step in the biosynthesis of aureothin.","Involved in the biosynthesis of the antibiotic phenazine, a nitrogen-containing heterocyclic molecule having important roles in virulence, competition and biological control. Oxygenates phenazine to PPD-4(6),22(11)-diene. In turn, PPD-4(6) undergoes hydroxylation catalyzed by OxyS to form PPD-4(6),22(11)-diene. PPD-4(6) then acts as a protease and directly binds to the hydroxyl group of PPD-4(6),22(11)-diene to form PPD-4(6),22(11)-diene. PPD-4(6) is also substrate of OxyC to form PPD-4(3),4(11)-diene. In vitro, the cytochrome P450 monooxygenase OxyA utilizes NADH or NADPH to hydroxylate phenazine to form PPD-4(3),22(11)-diene. Also able to hydroxylate phenazine to PPD-5(3),24(11)-diene.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497,GO:0004497; GO:0020037,GO:0004497,GO:0004497,GO:0004497,0.5872,0.8149,0.5872,0.5872,0.5872,5,0.6327,0.149,no
AURH_STRTU,Q70KH6,Prot2Text,Bacteria,406,"Bifunctional cytochrome P450 protein involved in the biosynthesis of the antibiotic aureothin, a nitroaryl polyketide metabolite with antifungal, cytotoxic and insecticidal activities. Catalyzes the hydroxylation of luteothin (also called deoxyaureothin), leading to the formation of the intermediate (7R)-7-hydroxydeoxyaureothin, followed by the formation of the aureothin tetrahydrofuran ring, the final step in the biosynthesis of aureothin.","Involved in the biosynthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It catalyzes the isomerization of the double bond of (S)-3-hydroxy-4,6-dimethylbenzaldehyde (3,4-DHB) to yield a bicyclic sesquiterpene alcohol with a mixed double bond, which then undergoes a spontaneous C-C bond cleavage to give (4R)-4,6-dihydroxybenzaldehyde (4R,6DHB). It can also use (S)-3,4-dihydroxybenzaldehyde (3,4-DHB) as substrate.",No,No,No,No,No,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0016853,,GO:0016853,,GO:0016853,0.3569,,0.3569,,0.3569,3,0.3569,0.149,no
AURH_STRTU,Q70KH6,ProtT3,Bacteria,406,"Bifunctional cytochrome P450 protein involved in the biosynthesis of the antibiotic aureothin, a nitroaryl polyketide metabolite with antifungal, cytotoxic and insecticidal activities. Catalyzes the hydroxylation of luteothin (also called deoxyaureothin), leading to the formation of the intermediate (7R)-7-hydroxydeoxyaureothin, followed by the formation of the aureothin tetrahydrofuran ring, the final step in the biosynthesis of aureothin.","Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Belongs to the cytochrome P450 family",Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,0.9516,0.9516,0.9516,0.9516,0.9516,5,0.9516,0.149,no
AURH_STRTU,Q70KH6,ProtTale,Bacteria,406,"Bifunctional cytochrome P450 protein involved in the biosynthesis of the antibiotic aureothin, a nitroaryl polyketide metabolite with antifungal, cytotoxic and insecticidal activities. Catalyzes the hydroxylation of luteothin (also called deoxyaureothin), leading to the formation of the intermediate (7R)-7-hydroxydeoxyaureothin, followed by the formation of the aureothin tetrahydrofuran ring, the final step in the biosynthesis of aureothin.","Involved in the biosynthesis of the anthracyclines carminomycin and daunorubicin (daunomycin) which are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. In vitro, catalyzes the hydroxylation at position C-10 of 10-deoxycarminomycin and 10-deoxydaunorubicin to yield 10-hydroxycarminomycin and 10-hydroxydaunorubicin, respectively.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497,GO:0004497; GO:0005506,GO:0016705,GO:0004497,GO:0004497,0.5872,0.8149,0.5872,0.5872,0.5872,5,0.6327,0.149,no
AURH_STRTU,Q70KH6,Protein2Text,Bacteria,406,"Bifunctional cytochrome P450 protein involved in the biosynthesis of the antibiotic aureothin, a nitroaryl polyketide metabolite with antifungal, cytotoxic and insecticidal activities. Catalyzes the hydroxylation of luteothin (also called deoxyaureothin), leading to the formation of the intermediate (7R)-7-hydroxydeoxyaureothin, followed by the formation of the aureothin tetrahydrofuran ring, the final step in the biosynthesis of aureothin.","This protein is a cytochrome P450 monooxygenase, which suggests that its molecular function is to catalyze the oxidation of organic substrates. Specifically, it is involved in the oxidation of a particular compound, likely a natural product or a xenobiotic. The exact substrate specificity of this protein is not specified in the provided information, but it is likely to be a member of the P450 monooxygenases that catalyze a wide range of reactions, including hydroxylation, epoxidation, and sulfoxidation.",Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497,GO:0005506; GO:0016491,GO:0004497,GO:0004497,GO:0004497,0.5872,0.7787,0.5872,0.5872,0.5872,5,0.6255,0.149,no
AURH_STRTU,Q70KH6,Reference,Bacteria,406,"Bifunctional cytochrome P450 protein involved in the biosynthesis of the antibiotic aureothin, a nitroaryl polyketide metabolite with antifungal, cytotoxic and insecticidal activities. Catalyzes the hydroxylation of luteothin (also called deoxyaureothin), leading to the formation of the intermediate (7R)-7-hydroxydeoxyaureothin, followed by the formation of the aureothin tetrahydrofuran ring, the final step in the biosynthesis of aureothin.","Bifunctional cytochrome P450 protein involved in the biosynthesis of the antibiotic aureothin, a nitroaryl polyketide metabolite with antifungal, cytotoxic and insecticidal activities. Catalyzes the hydroxylation of luteothin (also called deoxyaureothin), leading to the formation of the intermediate (7R)-7-hydroxydeoxyaureothin, followed by the formation of the aureothin tetrahydrofuran ring, the final step in the biosynthesis of aureothin.",,,,,,,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497; GO:0020037,GO:0004497; GO:0020037,GO:0004497; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,0.8149,0.8149,0.8149,0.9516,0.9516,5,0.8696,0.149,no
PNTCW_TREDE,Q73MU2,ESM2Text,Bacteria,616,"Bifunctional transferase involved in the biosynthesis of cell-surface phosphonates. The aminotransferase region catalyzes the transformation of phosphonoacetaldehyde (PnAA) to 2-aminoethylphosphonate (AEP). The cytidylyltransferase region catalyzes the activation of 2- aminoethylphosphonate (AEP) to CMP-2-aminoethylphosphonate (CMP-AEP). Cannot use phosphocholine. Exhibits strong activity towards CTP, limited activity towards ATP and no activity with GTP.","Involved in the biosynthesis of legionaminic acid (LPA), a phytocassane polyketide that plays a key role in the virulence via its role in LPA biosynthesis. Catalyzes the conversion of phosphoenolpyruvate (PEP) to phosphonopyruvate (PPD).",No,No,No,No,Maybe,not-Yes,GO:0047304; GO:0046872; GO:0016779,GO:0016866,GO:0050189,,,,0.2669,0.1661,,,,2,0.2165,0.3139,no
PNTCW_TREDE,Q73MU2,Prot2Text,Bacteria,616,"Bifunctional transferase involved in the biosynthesis of cell-surface phosphonates. The aminotransferase region catalyzes the transformation of phosphonoacetaldehyde (PnAA) to 2-aminoethylphosphonate (AEP). The cytidylyltransferase region catalyzes the activation of 2- aminoethylphosphonate (AEP) to CMP-2-aminoethylphosphonate (CMP-AEP). Cannot use phosphocholine. Exhibits strong activity towards CTP, limited activity towards ATP and no activity with GTP.",Catalyzes the interconversion of L-serine and D-serine.,No,No,No,No,No,not-Yes,GO:0047304; GO:0046872; GO:0016779,GO:0008453,,GO:0008453,GO:0008453,GO:0008453,0.4863,,0.4863,0.4863,0.4863,4,0.4863,0.3139,no
PNTCW_TREDE,Q73MU2,ProtT3,Bacteria,616,"Bifunctional transferase involved in the biosynthesis of cell-surface phosphonates. The aminotransferase region catalyzes the transformation of phosphonoacetaldehyde (PnAA) to 2-aminoethylphosphonate (AEP). The cytidylyltransferase region catalyzes the activation of 2- aminoethylphosphonate (AEP) to CMP-2-aminoethylphosphonate (CMP-AEP). Cannot use phosphocholine. Exhibits strong activity towards CTP, limited activity towards ATP and no activity with GTP.",Involved in the biosynthesis of the lipopolysaccharide core. Catalyzes the conversion of UDP-N-acetylglucosamine (UDP-GlcNAc) and phosphoenolpyruvate (PEP) to UDP-N- acetylmannosamine (UDP-ManNAc) and phosphate (By similarity). Belongs to the phosphohexose mutase family,No,No,No,No,Maybe,not-Yes,GO:0047304; GO:0046872; GO:0016779,GO:0008761,GO:0016853,GO:0016853,GO:0008761,GO:0008761,0.1898,0.3318,0.3318,0.1898,0.1898,5,0.2466,0.3139,no
PNTCW_TREDE,Q73MU2,ProtTale,Bacteria,616,"Bifunctional transferase involved in the biosynthesis of cell-surface phosphonates. The aminotransferase region catalyzes the transformation of phosphonoacetaldehyde (PnAA) to 2-aminoethylphosphonate (AEP). The cytidylyltransferase region catalyzes the activation of 2- aminoethylphosphonate (AEP) to CMP-2-aminoethylphosphonate (CMP-AEP). Cannot use phosphocholine. Exhibits strong activity towards CTP, limited activity towards ATP and no activity with GTP.",May be involved in the transport of peptides across the membrane.,No,No,No,No,Maybe,not-Yes,GO:0047304; GO:0046872; GO:0016779,,,,,,,,,,,0,,0.3139,no
PNTCW_TREDE,Q73MU2,Protein2Text,Bacteria,616,"Bifunctional transferase involved in the biosynthesis of cell-surface phosphonates. The aminotransferase region catalyzes the transformation of phosphonoacetaldehyde (PnAA) to 2-aminoethylphosphonate (AEP). The cytidylyltransferase region catalyzes the activation of 2- aminoethylphosphonate (AEP) to CMP-2-aminoethylphosphonate (CMP-AEP). Cannot use phosphocholine. Exhibits strong activity towards CTP, limited activity towards ATP and no activity with GTP.","This protein is involved in the molecular function of 'nucleoside phosphate interconversion', specifically it is a bifunctional enzyme that catalyzes the interconversion of GMP and GDP to GMP- phosphate and GDP-phosphate, respectively. It is also involved in the molecular function of 'nucleotide metabolic process'.",No,No,No,No,No,not-Yes,GO:0047304; GO:0046872; GO:0016779,GO:0004550,GO:0004550,,GO:0004385,GO:0004550,0.3397,0.3397,,0.3095,0.3397,4,0.3322,0.3139,no
PNTCW_TREDE,Q73MU2,Reference,Bacteria,616,"Bifunctional transferase involved in the biosynthesis of cell-surface phosphonates. The aminotransferase region catalyzes the transformation of phosphonoacetaldehyde (PnAA) to 2-aminoethylphosphonate (AEP). The cytidylyltransferase region catalyzes the activation of 2- aminoethylphosphonate (AEP) to CMP-2-aminoethylphosphonate (CMP-AEP). Cannot use phosphocholine. Exhibits strong activity towards CTP, limited activity towards ATP and no activity with GTP.","Bifunctional transferase involved in the biosynthesis of cell-surface phosphonates. The aminotransferase region catalyzes the transformation of phosphonoacetaldehyde (PnAA) to 2-aminoethylphosphonate (AEP). The cytidylyltransferase region catalyzes the activation of 2- aminoethylphosphonate (AEP) to CMP-2-aminoethylphosphonate (CMP-AEP). Cannot use phosphocholine. Exhibits strong activity towards CTP, limited activity towards ATP and no activity with GTP.",,,,,,,GO:0047304; GO:0046872; GO:0016779,GO:0008483; GO:0070567,GO:0008483; GO:0016779,GO:0008483; GO:0008568,GO:0008483; GO:0004605; GO:0016740,GO:0008483; GO:0004605,0.7075,0.7642,0.4985,0.6786,0.6657,5,0.6629,0.3139,no
PLYL_THEST,Q76EC9,ESM2Text,Bacteria,1240,"Cleaves polygalacturonate or partially methylated pectin. When assayed on polygalacturonate or on pectin, it releases monogalacturonate as the principal product.",Degrades a wide range of fructan-linked oligosaccharides.,No,No,No,No,No,not-Yes,GO:0046872; GO:0030570,GO:0016798,GO:0004553,GO:0004553,GO:0004553,GO:0016798,0.2318,0.1917,0.1917,0.1917,0.2318,5,0.2077,0.2983,no
PLYL_THEST,Q76EC9,Prot2Text,Bacteria,1240,"Cleaves polygalacturonate or partially methylated pectin. When assayed on polygalacturonate or on pectin, it releases monogalacturonate as the principal product.","Converts beta-D-galactosyl-D-mannose (Gal-beta-D-Man) to mannose-D-glucose (Man-Glc) and glucose. Involved in degradation of hemicellulose, the major component of plant cell walls.",No,No,No,No,No,not-Yes,GO:0046872; GO:0030570,GO:0004553,GO:0004553,GO:0004553,GO:0004553,GO:0004565,0.1917,0.1917,0.1917,0.1917,0.1415,5,0.1817,0.2983,no
PLYL_THEST,Q76EC9,ProtT3,Bacteria,1240,"Cleaves polygalacturonate or partially methylated pectin. When assayed on polygalacturonate or on pectin, it releases monogalacturonate as the principal product.","Alpha-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Catalyzes the hydrolysis of alpha-(1->5)-linked L-arabinofuranosyl residues in arabinoxylan (By similarity). Cell membrane; Single-pass type II membrane protein. Belongs to the glycosyl hydrolase 56 family",No,No,No,No,No,not-Yes,GO:0046872; GO:0030570,GO:0016798,GO:0046556,GO:0004553,GO:0046556,GO:0016798,0.2318,0.1628,0.1917,0.1628,0.2318,5,0.1962,0.2983,no
PLYL_THEST,Q76EC9,ProtTale,Bacteria,1240,"Cleaves polygalacturonate or partially methylated pectin. When assayed on polygalacturonate or on pectin, it releases monogalacturonate as the principal product.","Lectin that specifically recognizes and binds to the non-reducing end of poly-beta-1,6-D-glucuronic acid.",No,No,No,No,No,not-Yes,GO:0046872; GO:0030570,GO:0030246,GO:0030246,GO:0030246,GO:0030246,GO:0030246,0.2894,0.2894,0.2894,0.2894,0.2894,5,0.2894,0.2983,no
PLYL_THEST,Q76EC9,Protein2Text,Bacteria,1240,"Cleaves polygalacturonate or partially methylated pectin. When assayed on polygalacturonate or on pectin, it releases monogalacturonate as the principal product.","This protein is involved in breaking down or hydrolyzing complex molecules, such as polysaccharides, into simpler sugars. Specifically, it is likely to be a glycosidase, an enzyme that catalyzes the hydrolysis of glycosidic bonds in oligosaccharides and polysaccharides. This process is essential for the degradation and utilization of complex carbohydrates in the environment.",Vague,Vague,Maybe,Vague,Maybe,not-Yes,GO:0046872; GO:0030570,GO:0004553,GO:0004553,GO:0004553,GO:0004553,GO:0004553,0.1917,0.1917,0.1917,0.1917,0.1917,5,0.1917,0.2983,no
PLYL_THEST,Q76EC9,Reference,Bacteria,1240,"Cleaves polygalacturonate or partially methylated pectin. When assayed on polygalacturonate or on pectin, it releases monogalacturonate as the principal product.","Cleaves polygalacturonate or partially methylated pectin. When assayed on polygalacturonate or on pectin, it releases monogalacturonate as the principal product.",,,,,,,GO:0046872; GO:0030570,GO:0004650,GO:0004650,GO:0004650,GO:0004650,GO:0004650,0.1628,0.1628,0.1628,0.1628,0.1628,5,0.1628,0.2983,no
BALDT_MYCTU,Q79FW0,ESM2Text,Bacteria,289,"Bifunctional enzyme that catalyzes two enzymatic reactions in biochemically unrelated pathways: acts as an aminodeoxychorismate (ADC) lyase (ADCL) in folate biosynthesis, converting 4-amino-4- deoxychorismate (ADC) to 4-aminobenzoate (PABA), and as a D-amino acid transaminase (DAAT) in peptidoglycan (PG) biosynthesis. DAAT activity is strictly restricted to D-alanine and D-glutamate. May function as a metabolic toggle that alternates between ADCL and DAAT activity, prioritizing the former over the latter in response to substrate accumulation. Bifunctionality of this enzyme provides a failsafe mechanism for a metabolic coupling between nucleic acid and cell wall biosynthesis that appears to ensure prioritization of PABA production over D-alanine/D-glutamate biosynthesis.","Acts on leucine, isoleucine and valine.",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0008696; GO:0047810; GO:0030170,,,,,,,,,,,0,,0.644,yes
BALDT_MYCTU,Q79FW0,Prot2Text,Bacteria,289,"Bifunctional enzyme that catalyzes two enzymatic reactions in biochemically unrelated pathways: acts as an aminodeoxychorismate (ADC) lyase (ADCL) in folate biosynthesis, converting 4-amino-4- deoxychorismate (ADC) to 4-aminobenzoate (PABA), and as a D-amino acid transaminase (DAAT) in peptidoglycan (PG) biosynthesis. DAAT activity is strictly restricted to D-alanine and D-glutamate. May function as a metabolic toggle that alternates between ADCL and DAAT activity, prioritizing the former over the latter in response to substrate accumulation. Bifunctionality of this enzyme provides a failsafe mechanism for a metabolic coupling between nucleic acid and cell wall biosynthesis that appears to ensure prioritization of PABA production over D-alanine/D-glutamate biosynthesis.","Acts on leucine, isoleucine and valine.",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0008696; GO:0047810; GO:0030170,,,,,,,,,,,0,,0.644,yes
BALDT_MYCTU,Q79FW0,ProtT3,Bacteria,289,"Bifunctional enzyme that catalyzes two enzymatic reactions in biochemically unrelated pathways: acts as an aminodeoxychorismate (ADC) lyase (ADCL) in folate biosynthesis, converting 4-amino-4- deoxychorismate (ADC) to 4-aminobenzoate (PABA), and as a D-amino acid transaminase (DAAT) in peptidoglycan (PG) biosynthesis. DAAT activity is strictly restricted to D-alanine and D-glutamate. May function as a metabolic toggle that alternates between ADCL and DAAT activity, prioritizing the former over the latter in response to substrate accumulation. Bifunctionality of this enzyme provides a failsafe mechanism for a metabolic coupling between nucleic acid and cell wall biosynthesis that appears to ensure prioritization of PABA production over D-alanine/D-glutamate biosynthesis.","Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0008696; GO:0047810; GO:0030170,GO:0004084,GO:0004084,GO:0004084; GO:0030170,GO:0004084,GO:0004084,0.4318,0.4318,0.7315,0.4318,0.4318,5,0.4917,0.644,yes
BALDT_MYCTU,Q79FW0,ProtTale,Bacteria,289,"Bifunctional enzyme that catalyzes two enzymatic reactions in biochemically unrelated pathways: acts as an aminodeoxychorismate (ADC) lyase (ADCL) in folate biosynthesis, converting 4-amino-4- deoxychorismate (ADC) to 4-aminobenzoate (PABA), and as a D-amino acid transaminase (DAAT) in peptidoglycan (PG) biosynthesis. DAAT activity is strictly restricted to D-alanine and D-glutamate. May function as a metabolic toggle that alternates between ADCL and DAAT activity, prioritizing the former over the latter in response to substrate accumulation. Bifunctionality of this enzyme provides a failsafe mechanism for a metabolic coupling between nucleic acid and cell wall biosynthesis that appears to ensure prioritization of PABA production over D-alanine/D-glutamate biosynthesis.","Involved in the biosynthesis of p-aminobenzoate (PABA), a precursor of tetrahydrofolate. Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate.",Maybe,Yes,Yes,Yes,Maybe,Yes,GO:0008696; GO:0047810; GO:0030170,GO:0008696,GO:0016829,GO:0003949,GO:0004053,GO:0004632,0.5673,0.4192,0.1672,0.1672,0.1672,5,0.2976,0.644,yes
BALDT_MYCTU,Q79FW0,Protein2Text,Bacteria,289,"Bifunctional enzyme that catalyzes two enzymatic reactions in biochemically unrelated pathways: acts as an aminodeoxychorismate (ADC) lyase (ADCL) in folate biosynthesis, converting 4-amino-4- deoxychorismate (ADC) to 4-aminobenzoate (PABA), and as a D-amino acid transaminase (DAAT) in peptidoglycan (PG) biosynthesis. DAAT activity is strictly restricted to D-alanine and D-glutamate. May function as a metabolic toggle that alternates between ADCL and DAAT activity, prioritizing the former over the latter in response to substrate accumulation. Bifunctionality of this enzyme provides a failsafe mechanism for a metabolic coupling between nucleic acid and cell wall biosynthesis that appears to ensure prioritization of PABA production over D-alanine/D-glutamate biosynthesis.",The molecular function of this protein is an aminotransferase.,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0008696; GO:0047810; GO:0030170,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.5081,0.5081,0.5081,0.5081,0.5081,5,0.5081,0.644,yes
BALDT_MYCTU,Q79FW0,Reference,Bacteria,289,"Bifunctional enzyme that catalyzes two enzymatic reactions in biochemically unrelated pathways: acts as an aminodeoxychorismate (ADC) lyase (ADCL) in folate biosynthesis, converting 4-amino-4- deoxychorismate (ADC) to 4-aminobenzoate (PABA), and as a D-amino acid transaminase (DAAT) in peptidoglycan (PG) biosynthesis. DAAT activity is strictly restricted to D-alanine and D-glutamate. May function as a metabolic toggle that alternates between ADCL and DAAT activity, prioritizing the former over the latter in response to substrate accumulation. Bifunctionality of this enzyme provides a failsafe mechanism for a metabolic coupling between nucleic acid and cell wall biosynthesis that appears to ensure prioritization of PABA production over D-alanine/D-glutamate biosynthesis.","Bifunctional enzyme that catalyzes two enzymatic reactions in biochemically unrelated pathways: acts as an aminodeoxychorismate (ADC) lyase (ADCL) in folate biosynthesis, converting 4-amino-4- deoxychorismate (ADC) to 4-aminobenzoate (PABA), and as a D-amino acid transaminase (DAAT) in peptidoglycan (PG) biosynthesis. DAAT activity is strictly restricted to D-alanine and D-glutamate. May function as a metabolic toggle that alternates between ADCL and DAAT activity, prioritizing the former over the latter in response to substrate accumulation. Bifunctionality of this enzyme provides a failsafe mechanism for a metabolic coupling between nucleic acid and cell wall biosynthesis that appears to ensure prioritization of PABA production over D-alanine/D-glutamate biosynthesis.",,,,,,,GO:0008696; GO:0047810; GO:0030170,GO:0008696; GO:0008483,GO:0008696; GO:0008483,GO:0008696; GO:0047305,GO:0004068; GO:0008483,GO:0008483; GO:0004072,0.7594,0.7594,0.7054,0.5643,0.4631,5,0.6503,0.644,yes
MDR_PLAF7,Q7K6A5,ESM2Text,Eukaryota,1419,"Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells. Transports lumefantrine, mefloquine, chloroquine, quinine, quinidine, amodiaquine, piperaquine, dihydroartemisinin and quinacrine.",ABC transporter; part of the gene cluster that mediates the biosynthesis of the glycolipid biosurfactant ustilagic acid (UA). UA is a secreted cellobiose glycolipid that is toxic for many microorganisms and confers biocontrol activity to U.maydis. Export of UA is presumably catalyzed by the ABC transporter atr1 (Probable). The non-TATA-binding domain (TBD1) of Atr1 binds to the cellobiose polysaccharide and the heptaketide precursor.,Yes,Maybe,Yes,No,No,not-Yes,GO:0008559; GO:0005524; GO:0016887; GO:0042626; GO:0046872,GO:0005524; GO:0042626,GO:0042626; GO:0005524,GO:0042626,GO:0042626,GO:0042626,0.7585,0.7585,0.5346,0.5346,0.5346,5,0.6242,0.4773,no
MDR_PLAF7,Q7K6A5,Prot2Text,Eukaryota,1419,"Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells. Transports lumefantrine, mefloquine, chloroquine, quinine, quinidine, amodiaquine, piperaquine, dihydroartemisinin and quinacrine.","ABC transporter; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Maybe,Yes,No,No,not-Yes,GO:0008559; GO:0005524; GO:0016887; GO:0042626; GO:0046872,GO:0042626,,GO:0042626,,GO:0042626,0.5346,,0.5346,,0.5346,3,0.5346,0.4773,no
MDR_PLAF7,Q7K6A5,ProtT3,Eukaryota,1419,"Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells. Transports lumefantrine, mefloquine, chloroquine, quinine, quinidine, amodiaquine, piperaquine, dihydroartemisinin and quinacrine.",Membrane; Multi-pass membrane protein. Belongs to the ABC transporter superfamily. ABCB family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008559; GO:0005524; GO:0016887; GO:0042626; GO:0046872,GO:0005524; GO:0042626,GO:0042626,GO:0005524; GO:0016887,GO:0042626; GO:0005524,GO:0042626,0.7585,0.5346,0.6747,0.7585,0.5346,5,0.6522,0.4773,no
MDR_PLAF7,Q7K6A5,ProtTale,Eukaryota,1419,"Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells. Transports lumefantrine, mefloquine, chloroquine, quinine, quinidine, amodiaquine, piperaquine, dihydroartemisinin and quinacrine.","Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.",No,No,No,No,No,not-Yes,GO:0008559; GO:0005524; GO:0016887; GO:0042626; GO:0046872,GO:0005525,,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,0.3276,,0.4812,0.4812,0.4812,4,0.4428,0.4773,no
MDR_PLAF7,Q7K6A5,Protein2Text,Eukaryota,1419,"Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells. Transports lumefantrine, mefloquine, chloroquine, quinine, quinidine, amodiaquine, piperaquine, dihydroartemisinin and quinacrine.","The molecular function of this protein is as a transporter. It is involved in the movement of molecules across cell membranes, which is essential for various cellular processes.",Vague,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0008559; GO:0005524; GO:0016887; GO:0042626; GO:0046872,,,,,GO:0005215,,,,,0.2835,1,0.2835,0.4773,no
MDR_PLAF7,Q7K6A5,Reference,Eukaryota,1419,"Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells. Transports lumefantrine, mefloquine, chloroquine, quinine, quinidine, amodiaquine, piperaquine, dihydroartemisinin and quinacrine.","Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells. Transports lumefantrine, mefloquine, chloroquine, quinine, quinidine, amodiaquine, piperaquine, dihydroartemisinin and quinacrine.",,,,,,,GO:0008559; GO:0005524; GO:0016887; GO:0042626; GO:0046872,GO:0015238,GO:0015238,GO:0015238; GO:0042626,GO:0042626; GO:0005524,GO:0042626; GO:0015238,0.3223,0.3223,0.5427,0.7585,0.5427,5,0.4977,0.4773,no
B4GTA_DROME,Q7KN92,ESM2Text,Eukaryota,403,"A beta1,4-N-acetylgalactosaminyltransferase that catalyzes the transfer of N-acetylgalactosamine (GalNAc) from UDP-GalNAc in a beta-1,4 linkage to substrates with a terminal N-acetylglucosamine (GlcNAc). Specific for glycolipid substrates. Functions downstream of egh/egghead and brn/brainiac to add the 4th sugar during glycosphingolipid elongation to form GalNAc-beta1-4GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer from the brn product GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer. Required in neuronal cells to regulate normal crawling behavior. Plays a role in glycosphingolipid biosynthesis involved in motor coordination and locomotion. May be involved in the biosynthesis of sialylated glycans by generate acceptor termini for sialylation by SiaT; possibly involved in neural transmission.","Beta-1,3-glucan synthase involved in the synthesis of very long chain beta-1,4-glucans (VLC), also called beta-glucan-1,6-glucan or M-beta-glucan, which are used in the nucleation of raffinose, a major component of hemicelluloses such as xyloglucan.",No,No,No,No,No,not-Yes,GO:0008376; GO:0033842,GO:0003843,GO:0003843,GO:0003843,GO:0003843,GO:0003843,0.6151,0.6151,0.6151,0.6151,0.6151,5,0.6151,0.4218,no
B4GTA_DROME,Q7KN92,Prot2Text,Eukaryota,403,"A beta1,4-N-acetylgalactosaminyltransferase that catalyzes the transfer of N-acetylgalactosamine (GalNAc) from UDP-GalNAc in a beta-1,4 linkage to substrates with a terminal N-acetylglucosamine (GlcNAc). Specific for glycolipid substrates. Functions downstream of egh/egghead and brn/brainiac to add the 4th sugar during glycosphingolipid elongation to form GalNAc-beta1-4GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer from the brn product GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer. Required in neuronal cells to regulate normal crawling behavior. Plays a role in glycosphingolipid biosynthesis involved in motor coordination and locomotion. May be involved in the biosynthesis of sialylated glycans by generate acceptor termini for sialylation by SiaT; possibly involved in neural transmission.","Beta-1,3-galactosyltransferase involved in the synthesis of type II arabinogalactan. Has activity for type I M2 collagen.",No,Maybe,Maybe,No,Maybe,not-Yes,GO:0008376; GO:0033842,GO:0048531,GO:0048531,GO:0048531,GO:0008378,GO:0008378; GO:0016757,0.5502,0.5502,0.5502,0.6333,0.6394,5,0.5847,0.4218,no
B4GTA_DROME,Q7KN92,ProtT3,Eukaryota,403,"A beta1,4-N-acetylgalactosaminyltransferase that catalyzes the transfer of N-acetylgalactosamine (GalNAc) from UDP-GalNAc in a beta-1,4 linkage to substrates with a terminal N-acetylglucosamine (GlcNAc). Specific for glycolipid substrates. Functions downstream of egh/egghead and brn/brainiac to add the 4th sugar during glycosphingolipid elongation to form GalNAc-beta1-4GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer from the brn product GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer. Required in neuronal cells to regulate normal crawling behavior. Plays a role in glycosphingolipid biosynthesis involved in motor coordination and locomotion. May be involved in the biosynthesis of sialylated glycans by generate acceptor termini for sialylation by SiaT; possibly involved in neural transmission.",Catalyzes the transfer of galactose from UDP-galactose to N-acetylglucosamine (GlcNAc). Golgi apparatus membrane; Single- pass type II membrane protein. Belongs to the glycosyltransferase 7 family,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0008376; GO:0033842,GO:0008378,GO:0008378,GO:0008378; GO:0046527,GO:0008378; GO:0046527,GO:0008378,0.6333,0.6333,0.6394,0.6394,0.6333,5,0.6357,0.4218,no
B4GTA_DROME,Q7KN92,ProtTale,Eukaryota,403,"A beta1,4-N-acetylgalactosaminyltransferase that catalyzes the transfer of N-acetylgalactosamine (GalNAc) from UDP-GalNAc in a beta-1,4 linkage to substrates with a terminal N-acetylglucosamine (GlcNAc). Specific for glycolipid substrates. Functions downstream of egh/egghead and brn/brainiac to add the 4th sugar during glycosphingolipid elongation to form GalNAc-beta1-4GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer from the brn product GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer. Required in neuronal cells to regulate normal crawling behavior. Plays a role in glycosphingolipid biosynthesis involved in motor coordination and locomotion. May be involved in the biosynthesis of sialylated glycans by generate acceptor termini for sialylation by SiaT; possibly involved in neural transmission.","Catalyzes the synthesis of lactosylceramide (LacCer) by transferring a galactose residue from UDP-galactose to glucosylceramide (GlcCer). LacCer is the starting point for the synthesis of all glycosphingolipids and the major glycosphingolipid in the brain, and plays an important role in neural development and myelinogenesis. Also catalyzes the synthesis of galactosylceramide (GalCer) by transferring a galactose residue from UDP-galactose to various glycosphingolipids such as glucosylceramide (GlcCer), lactosylceramide (LacCer), globot",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0008376; GO:0033842,GO:0016757,GO:0016757; GO:0046527,GO:0047291,GO:0016757; GO:0047220,GO:0016757,0.631,0.6394,0.4449,0.6159,0.631,5,0.5924,0.4218,no
B4GTA_DROME,Q7KN92,Protein2Text,Eukaryota,403,"A beta1,4-N-acetylgalactosaminyltransferase that catalyzes the transfer of N-acetylgalactosamine (GalNAc) from UDP-GalNAc in a beta-1,4 linkage to substrates with a terminal N-acetylglucosamine (GlcNAc). Specific for glycolipid substrates. Functions downstream of egh/egghead and brn/brainiac to add the 4th sugar during glycosphingolipid elongation to form GalNAc-beta1-4GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer from the brn product GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer. Required in neuronal cells to regulate normal crawling behavior. Plays a role in glycosphingolipid biosynthesis involved in motor coordination and locomotion. May be involved in the biosynthesis of sialylated glycans by generate acceptor termini for sialylation by SiaT; possibly involved in neural transmission.","This protein is involved in the transfer of sugar molecules. Specifically, it is a glycosyltransferase, which catalyzes the transfer of a sugar molecule from a donor molecule to an acceptor molecule. In this case, it is likely involved in the transfer of a carbohydrate moiety to a protein or other macromolecule.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008376; GO:0033842,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.631,0.631,0.631,0.631,0.631,5,0.631,0.4218,no
B4GTA_DROME,Q7KN92,Reference,Eukaryota,403,"A beta1,4-N-acetylgalactosaminyltransferase that catalyzes the transfer of N-acetylgalactosamine (GalNAc) from UDP-GalNAc in a beta-1,4 linkage to substrates with a terminal N-acetylglucosamine (GlcNAc). Specific for glycolipid substrates. Functions downstream of egh/egghead and brn/brainiac to add the 4th sugar during glycosphingolipid elongation to form GalNAc-beta1-4GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer from the brn product GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer. Required in neuronal cells to regulate normal crawling behavior. Plays a role in glycosphingolipid biosynthesis involved in motor coordination and locomotion. May be involved in the biosynthesis of sialylated glycans by generate acceptor termini for sialylation by SiaT; possibly involved in neural transmission.","A beta1,4-N-acetylgalactosaminyltransferase that catalyzes the transfer of N-acetylgalactosamine (GalNAc) from UDP-GalNAc in a beta-1,4 linkage to substrates with a terminal N-acetylglucosamine (GlcNAc). Specific for glycolipid substrates. Functions downstream of egh/egghead and brn/brainiac to add the 4th sugar during glycosphingolipid elongation to form GalNAc-beta1-4GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer from the brn product GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer. Required in neuronal cells to regulate normal crawling behavior. Plays a role in glycosphingolipid biosynthesis involved in motor coordination and locomotion. May be involved in the biosynthesis of sialylated glycans by generate acceptor termini for sialylation by SiaT; possibly involved in neural transmission.",,,,,,,GO:0008376; GO:0033842,GO:0008376,GO:0008376,GO:0008376,GO:0016757,GO:0008376,0.9633,0.9633,0.9633,0.631,0.9633,5,0.8968,0.4218,no
MRAP1_ANOGA,Q7PPZ8,ESM2Text,Eukaryota,272,Putative protease that regulates timely processing of the mating plug and female refractoriness to further mating.,Major function may be to aid in digestion of the blood meal.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004252,,,,,,,,,,,0,,0.6272,yes
MRAP1_ANOGA,Q7PPZ8,Prot2Text,Eukaryota,272,Putative protease that regulates timely processing of the mating plug and female refractoriness to further mating.,Has a chymotrypsin-like activity.,Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004252,GO:0004263,GO:0004252,GO:0004252,GO:0004252,GO:0004263; GO:0008236,0.0,1.0,1.0,1.0,0.8276,5,0.7655,0.6272,yes
MRAP1_ANOGA,Q7PPZ8,ProtT3,Eukaryota,272,Putative protease that regulates timely processing of the mating plug and female refractoriness to further mating.,Secreted. Belongs to the peptidase S1 family,Vague,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004252,GO:0004252,GO:0004252,GO:0004252,GO:0004252,GO:0004252,1.0,1.0,1.0,1.0,1.0,5,1.0,0.6272,yes
MRAP1_ANOGA,Q7PPZ8,ProtTale,Eukaryota,272,Putative protease that regulates timely processing of the mating plug and female refractoriness to further mating.,Serine protease that cleaves specifically after 'Gly-|-Leu-|-Phe-|-Gly-|-Leu|-Arg|-Lys|-|-|-Ile|-NH(2)'.,Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0004252,GO:0004252,GO:0004252,GO:0004252,GO:0004252,GO:0004252,1.0,1.0,1.0,1.0,1.0,5,1.0,0.6272,yes
MRAP1_ANOGA,Q7PPZ8,Protein2Text,Eukaryota,272,Putative protease that regulates timely processing of the mating plug and female refractoriness to further mating.,The molecular function of this protein is to break down proteins. It is a serine protease.,Maybe,Yes,Yes,Maybe,Yes,Yes,GO:0004252,GO:0004252,GO:0008236,GO:0004252,GO:0008236,GO:0004252,1.0,0.8276,1.0,0.8276,1.0,5,0.931,0.6272,yes
MRAP1_ANOGA,Q7PPZ8,Reference,Eukaryota,272,Putative protease that regulates timely processing of the mating plug and female refractoriness to further mating.,Putative protease that regulates timely processing of the mating plug and female refractoriness to further mating.,,,,,,,GO:0004252,GO:0008233,GO:0008233,GO:0008233,GO:0008233,GO:0008233,0.6551,0.6551,0.6551,0.6551,0.6551,5,0.6551,0.6272,yes
PHYA_NEUCR,Q7S9V5,ESM2Text,Eukaryota,509,"Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate. Myo-inositol 2-monophosphate is the end product. Is also able to dephosphorylate the classic acid phosphatase substrate p-nitrophenyl phosphate.",Catalyzes the hydrolysis of inorganic orthophosphate from phytate.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003993; GO:0016158,GO:0008707,GO:0016791,GO:0008707,GO:0008707,GO:0008707,0.7075,0.8113,0.7075,0.7075,0.7075,5,0.7283,0.1652,no
PHYA_NEUCR,Q7S9V5,Prot2Text,Eukaryota,509,"Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate. Myo-inositol 2-monophosphate is the end product. Is also able to dephosphorylate the classic acid phosphatase substrate p-nitrophenyl phosphate.",Catalyzes the hydrolysis of inorganic orthophosphate from phytate.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003993; GO:0016158,GO:0008707,GO:0008242,GO:0008707,GO:0008707,GO:0008707,0.7075,0.3028,0.7075,0.7075,0.7075,5,0.6266,0.1652,no
PHYA_NEUCR,Q7S9V5,ProtT3,Eukaryota,509,"Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate. Myo-inositol 2-monophosphate is the end product. Is also able to dephosphorylate the classic acid phosphatase substrate p-nitrophenyl phosphate.",Catalyzes the hydrolysis of inorganic orthophosphate from phytate. Secreted. Belongs to the histidine acid phosphatase family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003993; GO:0016158,GO:0033897; GO:0003993,GO:0008252,GO:0008707; GO:0003993,GO:0003993; GO:0008252,GO:0003993; GO:0008707,0.681,0.6928,0.8845,0.8329,0.8845,5,0.7951,0.1652,no
PHYA_NEUCR,Q7S9V5,ProtTale,Eukaryota,509,"Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate. Myo-inositol 2-monophosphate is the end product. Is also able to dephosphorylate the classic acid phosphatase substrate p-nitrophenyl phosphate.",Catalyzes the hydrolysis of inorganic polyphosphate (polyP) chains of many hundreds of phosphate residues to shorter lengths. Can use a broad spectrum of polyP substrates from a few hundreds of phosphate residues to at least 2000 phosphate residues.,No,No,No,No,No,not-Yes,GO:0003993; GO:0016158,GO:0016787,GO:0004309,GO:0004427,GO:0004427,GO:0004427,0.5104,0.2346,0.2346,0.2346,0.2346,5,0.2898,0.1652,no
PHYA_NEUCR,Q7S9V5,Protein2Text,Eukaryota,509,"Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate. Myo-inositol 2-monophosphate is the end product. Is also able to dephosphorylate the classic acid phosphatase substrate p-nitrophenyl phosphate.","The molecular function of this protein is not explicitly stated in the provided text, but based on its classification as a phosphatase, it is likely to be involved in the removal of phosphate groups from molecules. More specifically, it is likely to be a secreted acid phosphatase, which is involved in the degradation of organic phosphate compounds in the environment. This would make it a key enzyme in the breakdown of organic matter and the release of phosphate ions, which can be used by the organism to synthesize new biomolecules.",Maybe,Yes,Maybe,Vague,Maybe,not-Yes,GO:0003993; GO:0016158,GO:0003993,GO:0003993,GO:0003993,GO:0003993,GO:0003993,0.8615,0.8615,0.8615,0.8615,0.8615,5,0.8615,0.1652,no
PHYA_NEUCR,Q7S9V5,Reference,Eukaryota,509,"Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate. Myo-inositol 2-monophosphate is the end product. Is also able to dephosphorylate the classic acid phosphatase substrate p-nitrophenyl phosphate.","Catalyzes the phosphate monoester hydrolysis of phytic acid (myo-inositol hexakisphosphate), which results in the stepwise formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and monophosphates, as well as the liberation of inorganic phosphate. Myo-inositol 2-monophosphate is the end product. Is also able to dephosphorylate the classic acid phosphatase substrate p-nitrophenyl phosphate.",,,,,,,GO:0003993; GO:0016158,GO:0003993; GO:0008707,GO:0008707; GO:0003993,GO:0016791; GO:0003993,GO:0016791; GO:0003993,GO:0033897; GO:0003993,0.8845,0.8845,0.8912,0.8912,0.681,5,0.8465,0.1652,no
BLAB_PSEAI,Q7WYA8,ESM2Text,Bacteria,246,"Confers resistance to the different beta-lactam antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Exhibits higher catalytic efficiency toward ticarcillin and piperacillin than blaIMP-1. Exhibits catalytic activity for carbapenem compounds, but has a preference for imipenem and ertapenem over meropenem. Has high efficiency for the hydrolysis of cefuroxime. Exhibits hydrolysis of all cephalosporins tested. Exhibits no hydrolysis of temocillin, the 6- alpha-methoxy semisynthetic derivative of ticarcillin.","Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008800; GO:0008270,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,0.6895,0.6895,0.6895,0.6895,0.6895,5,0.6895,0.5889,yes
BLAB_PSEAI,Q7WYA8,Prot2Text,Bacteria,246,"Confers resistance to the different beta-lactam antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Exhibits higher catalytic efficiency toward ticarcillin and piperacillin than blaIMP-1. Exhibits catalytic activity for carbapenem compounds, but has a preference for imipenem and ertapenem over meropenem. Has high efficiency for the hydrolysis of cefuroxime. Exhibits hydrolysis of all cephalosporins tested. Exhibits no hydrolysis of temocillin, the 6- alpha-methoxy semisynthetic derivative of ticarcillin.","Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008800; GO:0008270,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,0.6895,0.6895,0.6895,0.6895,0.6895,5,0.6895,0.5889,yes
BLAB_PSEAI,Q7WYA8,ProtT3,Bacteria,246,"Confers resistance to the different beta-lactam antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Exhibits higher catalytic efficiency toward ticarcillin and piperacillin than blaIMP-1. Exhibits catalytic activity for carbapenem compounds, but has a preference for imipenem and ertapenem over meropenem. Has high efficiency for the hydrolysis of cefuroxime. Exhibits hydrolysis of all cephalosporins tested. Exhibits no hydrolysis of temocillin, the 6- alpha-methoxy semisynthetic derivative of ticarcillin.","Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Periplasm. Belongs to the metallo-beta-lactamase superfamily. Class-B beta-lactamase family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008800; GO:0008270,GO:0008800,GO:0008800,GO:0008800,GO:0008800; GO:0046872,GO:0008800,0.6895,0.6895,0.6895,0.8854,0.6895,5,0.7287,0.5889,yes
BLAB_PSEAI,Q7WYA8,ProtTale,Bacteria,246,"Confers resistance to the different beta-lactam antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Exhibits higher catalytic efficiency toward ticarcillin and piperacillin than blaIMP-1. Exhibits catalytic activity for carbapenem compounds, but has a preference for imipenem and ertapenem over meropenem. Has high efficiency for the hydrolysis of cefuroxime. Exhibits hydrolysis of all cephalosporins tested. Exhibits no hydrolysis of temocillin, the 6- alpha-methoxy semisynthetic derivative of ticarcillin.","Class B beta-lactamase which confers resistance to the beta- lactam antibiotics, including penicillins, cephalosporins and carbapenems. Acts via hydrolysis of the beta-lactam ring.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008800; GO:0008270,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,0.6895,0.6895,0.6895,0.6895,0.6895,5,0.6895,0.5889,yes
BLAB_PSEAI,Q7WYA8,Protein2Text,Bacteria,246,"Confers resistance to the different beta-lactam antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Exhibits higher catalytic efficiency toward ticarcillin and piperacillin than blaIMP-1. Exhibits catalytic activity for carbapenem compounds, but has a preference for imipenem and ertapenem over meropenem. Has high efficiency for the hydrolysis of cefuroxime. Exhibits hydrolysis of all cephalosporins tested. Exhibits no hydrolysis of temocillin, the 6- alpha-methoxy semisynthetic derivative of ticarcillin.","The molecular function of this protein is an antibiotic inactivation enzyme.
This protein is involved in conferring resistance to antibiotics.",Vague,Maybe,Vague,Vague,Maybe,not-Yes,GO:0008800; GO:0008270,,,,,,,,,,,0,,0.5889,yes
BLAB_PSEAI,Q7WYA8,Reference,Bacteria,246,"Confers resistance to the different beta-lactam antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Exhibits higher catalytic efficiency toward ticarcillin and piperacillin than blaIMP-1. Exhibits catalytic activity for carbapenem compounds, but has a preference for imipenem and ertapenem over meropenem. Has high efficiency for the hydrolysis of cefuroxime. Exhibits hydrolysis of all cephalosporins tested. Exhibits no hydrolysis of temocillin, the 6- alpha-methoxy semisynthetic derivative of ticarcillin.","Confers resistance to the different beta-lactam antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Exhibits higher catalytic efficiency toward ticarcillin and piperacillin than blaIMP-1. Exhibits catalytic activity for carbapenem compounds, but has a preference for imipenem and ertapenem over meropenem. Has high efficiency for the hydrolysis of cefuroxime. Exhibits hydrolysis of all cephalosporins tested. Exhibits no hydrolysis of temocillin, the 6- alpha-methoxy semisynthetic derivative of ticarcillin.",,,,,,,GO:0008800; GO:0008270,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,0.6895,0.6895,0.6895,0.6895,0.6895,5,0.6895,0.5889,yes
DAO_GLUPR,Q7X2D3,ESM2Text,Bacteria,326,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.,"Degrades L-DOPA, L-DOPA and L-DOPA into GDP-L-galactono-DOPA and L-DOPA, respectively. Does not act on D-amino acids.",No,No,No,No,No,not-Yes,GO:0003884; GO:0071949; GO:0043799,GO:0003884,GO:0003884,GO:0003884,GO:0003884,GO:0003884,0.6411,0.6411,0.6411,0.6411,0.6411,5,0.6411,0.2059,no
DAO_GLUPR,Q7X2D3,Prot2Text,Bacteria,326,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.,"Oxidizes L-pipecolate and L-proline. Can also use D-glucose and L-arabinose as substrates, but with lower efficiency. Has no activity on D-galactose, D-xylose, L-arabinose, D-mannose, D-glucosamine, L-arabitol and D-glucuronic acid.",No,Maybe,No,No,No,not-Yes,GO:0003884; GO:0071949; GO:0043799,GO:0003884,GO:0003884,GO:0003884,GO:0003884,GO:0003884,0.6411,0.6411,0.6411,0.6411,0.6411,5,0.6411,0.2059,no
DAO_GLUPR,Q7X2D3,ProtT3,Bacteria,326,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.,Cytoplasm. Belongs to the DAMOX/DASOX family,Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0003884; GO:0071949; GO:0043799,GO:0003863,GO:0003884,GO:0003884,GO:0003863,GO:0003863,0.2324,0.6411,0.6411,0.2324,0.2324,5,0.3959,0.2059,no
DAO_GLUPR,Q7X2D3,ProtTale,Bacteria,326,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Enables the organism to utilize D-amino acids as a source of nutrients.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003884; GO:0071949; GO:0043799,GO:0003884,GO:0003862,GO:0003884,GO:0003884,GO:0003884,0.6411,0.2324,0.6411,0.6411,0.6411,5,0.5594,0.2059,no
DAO_GLUPR,Q7X2D3,Protein2Text,Bacteria,326,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.,"The molecular function of this protein is an aminotransferase. More specifically, it is a lysine aminotransferase, which catalyzes the conversion of lysine to cadaverine.",No,No,No,No,No,not-Yes,GO:0003884; GO:0071949; GO:0043799,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4208,0.4208,0.4208,0.4208,0.4208,5,0.4208,0.2059,no
DAO_GLUPR,Q7X2D3,Reference,Bacteria,326,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.,,,,,,,GO:0003884; GO:0071949; GO:0043799,GO:0003884,GO:0003884,GO:0003884,GO:0003884,GO:0003884,0.6411,0.6411,0.6411,0.6411,0.6411,5,0.6411,0.2059,no
PLYCA_BPSC1,Q7Y3F1,ESM2Text,Viruses,465,"Component of the endolysin PlyC that degrades the host peptidoglycans and participates with the holin protein in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles (Probable). Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and breaking down the peptidoglycan layer (Probable). When associated with the small subunit PlyCB, the large subunit PlyCA displays 2 catalytic activities, amidase and glycosyl hydrolase. Cleaves the amide bond between N-acetyl muramic acid and L-alanine in the host peptidoglycan. PlyC is an extremely potent endolysin.","Converts cyanocobalamin (CN-B12) to adenosylcobalamin (AdoCbl), an adenylated form of Cbl, which acquires iron by extracting it from the bacterial cytoplasmic permease component CblA. Also acts on a variety of other substrates, yielding conotoxins which polymerize into sulfated products. Can also act on a number of substrates, yielding mixed-alloylated mono- and disaccharides and reduced-sulfated polyols, suggesting that it acts on a number of substrates.",No,No,No,No,No,not-Yes,GO:0008745,,,,,,,,,,,0,,0.0893,no
PLYCA_BPSC1,Q7Y3F1,Prot2Text,Viruses,465,"Component of the endolysin PlyC that degrades the host peptidoglycans and participates with the holin protein in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles (Probable). Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and breaking down the peptidoglycan layer (Probable). When associated with the small subunit PlyCB, the large subunit PlyCA displays 2 catalytic activities, amidase and glycosyl hydrolase. Cleaves the amide bond between N-acetyl muramic acid and L-alanine in the host peptidoglycan. PlyC is an extremely potent endolysin.","Converts cyanocobalamin (CN-B12) to adenosylcobalamin (AdoCbl), an adenylated form of Cbl, which acquires iron by extracting it from the bacterial cytoplasmic permease component CblA. Also acts on a variety of other substrates, yielding conotoxins which polymerize into sulfated products. Can also act on a number of substrates, yielding mixed-alloylated mono- and disaccharides and reduced-sulfated polyols, suggesting that it acts on a number of substrates.",No,No,No,No,No,not-Yes,GO:0008745,,,GO:0008817,GO:0008819,,,,0.2509,0.0,,2,0.1255,0.0893,no
PLYCA_BPSC1,Q7Y3F1,ProtT3,Viruses,465,"Component of the endolysin PlyC that degrades the host peptidoglycans and participates with the holin protein in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles (Probable). Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and breaking down the peptidoglycan layer (Probable). When associated with the small subunit PlyCB, the large subunit PlyCA displays 2 catalytic activities, amidase and glycosyl hydrolase. Cleaves the amide bond between N-acetyl muramic acid and L-alanine in the host peptidoglycan. PlyC is an extremely potent endolysin.",Hydrolyzes the peptidoglycan layer of the host cell wall. Secreted. Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0008745,GO:0008745,GO:0008745,GO:0008745,GO:0008745,GO:0008745,1.0,1.0,1.0,1.0,1.0,5,1.0,0.0893,no
PLYCA_BPSC1,Q7Y3F1,ProtTale,Viruses,465,"Component of the endolysin PlyC that degrades the host peptidoglycans and participates with the holin protein in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles (Probable). Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and breaking down the peptidoglycan layer (Probable). When associated with the small subunit PlyCB, the large subunit PlyCA displays 2 catalytic activities, amidase and glycosyl hydrolase. Cleaves the amide bond between N-acetyl muramic acid and L-alanine in the host peptidoglycan. PlyC is an extremely potent endolysin.","Hydrolyzes the glycosidic bond of N-acetylmuramyl-L-alanine-D-glutamic acid-L-alpha-D-glutamyl-L-diaminopimelic acid (MurNAc-L-Ala-D-Glu-D-Pip). Catalyzes the hydrolysis of L-Ala-D-Glu-D-Pip to L-Ala-D-Glu-NH(2), which is the first step in the biosynthesis of lipoteichoic acid (LTA).",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0008745,GO:0016787,GO:0016787,GO:0008745,GO:0008745,GO:0008745,0.5588,0.5588,1.0,1.0,1.0,5,0.8235,0.0893,no
PLYCA_BPSC1,Q7Y3F1,Protein2Text,Viruses,465,"Component of the endolysin PlyC that degrades the host peptidoglycans and participates with the holin protein in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles (Probable). Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and breaking down the peptidoglycan layer (Probable). When associated with the small subunit PlyCB, the large subunit PlyCA displays 2 catalytic activities, amidase and glycosyl hydrolase. Cleaves the amide bond between N-acetyl muramic acid and L-alanine in the host peptidoglycan. PlyC is an extremely potent endolysin.","This protein is involved in the breakdown of hyaluronic acid, a key component of the extracellular matrix in the gut. It is likely a hyaluronidase, an enzyme that catalyzes the breakdown of hyaluronic acid into smaller fragments. This process may play a role in maintaining the balance of hyaluronic acid in the gut and regulating the composition of the extracellular matrix.",No,No,No,No,No,not-Yes,GO:0008745,GO:0004415,GO:0004415,GO:0004415,GO:0004415,GO:0004415,0.3008,0.3008,0.3008,0.3008,0.3008,5,0.3008,0.0893,no
PLYCA_BPSC1,Q7Y3F1,Reference,Viruses,465,"Component of the endolysin PlyC that degrades the host peptidoglycans and participates with the holin protein in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles (Probable). Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and breaking down the peptidoglycan layer (Probable). When associated with the small subunit PlyCB, the large subunit PlyCA displays 2 catalytic activities, amidase and glycosyl hydrolase. Cleaves the amide bond between N-acetyl muramic acid and L-alanine in the host peptidoglycan. PlyC is an extremely potent endolysin.","Component of the endolysin PlyC that degrades the host peptidoglycans and participates with the holin protein in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles (Probable). Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and breaking down the peptidoglycan layer (Probable). When associated with the small subunit PlyCB, the large subunit PlyCA displays 2 catalytic activities, amidase and glycosyl hydrolase. Cleaves the amide bond between N-acetyl muramic acid and L-alanine in the host peptidoglycan. PlyC is an extremely potent endolysin.",,,,,,,GO:0008745,GO:0008745; GO:0016798,GO:0008745; GO:0003796,GO:0008745; GO:0016798,GO:0008745; GO:0016798,GO:0008745; GO:0016798,0.8201,0.8341,0.8201,0.8201,0.8201,5,0.8229,0.0893,no
POLG_MNV1,Q80J95,ESM2Text,Viruses,1687,"[NS1-2]: Induces the proliferation of the host smooth ER membranes forming long tubular structures. These remodeled membranes probably form the viral factories that contain the replication complex. May play a role in viral replication by interacting with host VAPA, a vesicle-associated membrane protein that plays a role in SNARE-mediated vesicle fusion. This interaction may target replication complex to intracellular membranes (Probable).",Functions as a component of the ISW1 complex which acts in the remodeling of chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004197; GO:0046872; GO:0017111; GO:0003723; GO:0003724; GO:0003968,,GO:0016887,,,,,0.3159,,,,1,0.3159,0.3851,no
POLG_MNV1,Q80J95,Prot2Text,Viruses,1687,"[NS1-2]: Induces the proliferation of the host smooth ER membranes forming long tubular structures. These remodeled membranes probably form the viral factories that contain the replication complex. May play a role in viral replication by interacting with host VAPA, a vesicle-associated membrane protein that plays a role in SNARE-mediated vesicle fusion. This interaction may target replication complex to intracellular membranes (Probable).",Functions as a component of the ISW1 complex which acts in the remodeling of chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004197; GO:0046872; GO:0017111; GO:0003723; GO:0003724; GO:0003968,GO:0016887,,GO:0016887; GO:0003682,GO:0008094,GO:0016887; GO:0003682,0.3159,,0.4181,0.2366,0.4181,4,0.3472,0.3851,no
POLG_MNV1,Q80J95,ProtT3,Viruses,1687,"[NS1-2]: Induces the proliferation of the host smooth ER membranes forming long tubular structures. These remodeled membranes probably form the viral factories that contain the replication complex. May play a role in viral replication by interacting with host VAPA, a vesicle-associated membrane protein that plays a role in SNARE-mediated vesicle fusion. This interaction may target replication complex to intracellular membranes (Probable).",[Isoform 1]: Plays an essential role in viral DNA replication by acting as an ATP-dependent helicase. [Isoform 2]: Plays an essential role in viral DNA replication by acting as an ATP-dependent helicase. [Isoform 3]: Plays an essential role in viral DNA replication by acting as an ATP-dependent helicase. [Isoform 4]: Plays an essential role in viral DNA replication by acting as an ATP-dependent helicase. [Isoform 5]: Plays an essential role,No,No,No,No,No,not-Yes,GO:0005524; GO:0004197; GO:0046872; GO:0017111; GO:0003723; GO:0003724; GO:0003968,GO:0003678; GO:0005524,GO:0004386; GO:0005524,GO:0004003; GO:0005524,GO:0003678; GO:0005524; GO:0004386,GO:0004386; GO:0005524,0.4734,0.5237,0.4734,0.5363,0.5237,5,0.5061,0.3851,no
POLG_MNV1,Q80J95,ProtTale,Viruses,1687,"[NS1-2]: Induces the proliferation of the host smooth ER membranes forming long tubular structures. These remodeled membranes probably form the viral factories that contain the replication complex. May play a role in viral replication by interacting with host VAPA, a vesicle-associated membrane protein that plays a role in SNARE-mediated vesicle fusion. This interaction may target replication complex to intracellular membranes (Probable).","[NS2]: Together with NTPase and NS4, initiates the formation of the replication complex. Induces the proliferation of the host smooth ER membranes forming long tubular structures. These remodeled membranes probably form the viral factories that contain the replication complex.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0004197; GO:0046872; GO:0017111; GO:0003723; GO:0003724; GO:0003968,,,,,,,,,,,0,,0.3851,no
POLG_MNV1,Q80J95,Protein2Text,Viruses,1687,"[NS1-2]: Induces the proliferation of the host smooth ER membranes forming long tubular structures. These remodeled membranes probably form the viral factories that contain the replication complex. May play a role in viral replication by interacting with host VAPA, a vesicle-associated membrane protein that plays a role in SNARE-mediated vesicle fusion. This interaction may target replication complex to intracellular membranes (Probable).",This protein is a serine protease.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004197; GO:0046872; GO:0017111; GO:0003723; GO:0003724; GO:0003968,GO:0004252,GO:0008236,GO:0004252,GO:0008236,GO:0004252,0.2391,0.2462,0.2391,0.2462,0.2391,5,0.2419,0.3851,no
POLG_MNV1,Q80J95,Reference,Viruses,1687,"[NS1-2]: Induces the proliferation of the host smooth ER membranes forming long tubular structures. These remodeled membranes probably form the viral factories that contain the replication complex. May play a role in viral replication by interacting with host VAPA, a vesicle-associated membrane protein that plays a role in SNARE-mediated vesicle fusion. This interaction may target replication complex to intracellular membranes (Probable).","[NS1-2]: Induces the proliferation of the host smooth ER membranes forming long tubular structures. These remodeled membranes probably form the viral factories that contain the replication complex. May play a role in viral replication by interacting with host VAPA, a vesicle-associated membrane protein that plays a role in SNARE-mediated vesicle fusion. This interaction may target replication complex to intracellular membranes (Probable).",,,,,,,GO:0005524; GO:0004197; GO:0046872; GO:0017111; GO:0003723; GO:0003724; GO:0003968,,,,,,,,,,,0,,0.3851,no
PAT_BACCR,Q814Z4,ESM2Text,Bacteria,405,"Aminotransferase involved in the synthesis of cell surface polysaccharides. Catalyzes the transfer of the primary amino group of L-glutamate to C-4'' of UDP-2-acetamido-2,6- dideoxy-alpha-D-xylo-hex-4-ulose (UDP-4-keto-6-deoxy-HexNAc) to form UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-galactose (UDP-4-amino- FucNAc) and 2-oxoglutarate. Also converts UDP-4-keto- 6-deoxy-D-glucose, UDP-4-keto-D-xylose and UDP-4-keto-6-deoxy-L-AltNAc to their corresponding UDP-4-amino-sugars. Is specific to L-glutamate. Marginal activity is observed with L-alanine and L-glutamine, but no activity is detected with gamma-aminobutyric acid (GABA) or L-tryptophan.","Involved in the synthesis of forosamine ((4S)-3,4-dimethylbenzimidazole-S-amate) which is an important intermediate in the biosynthesis of several siderophores including extracellular spore.",No,No,Vague,No,Maybe,not-Yes,GO:0030170; GO:0008483,,,,,,,,,,,0,,0.2259,no
PAT_BACCR,Q814Z4,Prot2Text,Bacteria,405,"Aminotransferase involved in the synthesis of cell surface polysaccharides. Catalyzes the transfer of the primary amino group of L-glutamate to C-4'' of UDP-2-acetamido-2,6- dideoxy-alpha-D-xylo-hex-4-ulose (UDP-4-keto-6-deoxy-HexNAc) to form UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-galactose (UDP-4-amino- FucNAc) and 2-oxoglutarate. Also converts UDP-4-keto- 6-deoxy-D-glucose, UDP-4-keto-D-xylose and UDP-4-keto-6-deoxy-L-AltNAc to their corresponding UDP-4-amino-sugars. Is specific to L-glutamate. Marginal activity is observed with L-alanine and L-glutamine, but no activity is detected with gamma-aminobutyric acid (GABA) or L-tryptophan.","Catalyzes the conversion of dTDP-4-dehydro-6-deoxy-D-glucose (dTDP-D-Glc4O) to dTDP-4-amino-4,6-dideoxy-D-glucose (dTDP-D-Qui4N). L-glutamine can also be used as amino donor.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0030170; GO:0008483,GO:0008483,GO:0033480,GO:0008483,GO:0008483,GO:0008483,0.6936,0.0,0.6936,0.6936,0.6936,5,0.5549,0.2259,no
PAT_BACCR,Q814Z4,ProtT3,Bacteria,405,"Aminotransferase involved in the synthesis of cell surface polysaccharides. Catalyzes the transfer of the primary amino group of L-glutamate to C-4'' of UDP-2-acetamido-2,6- dideoxy-alpha-D-xylo-hex-4-ulose (UDP-4-keto-6-deoxy-HexNAc) to form UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-galactose (UDP-4-amino- FucNAc) and 2-oxoglutarate. Also converts UDP-4-keto- 6-deoxy-D-glucose, UDP-4-keto-D-xylose and UDP-4-keto-6-deoxy-L-AltNAc to their corresponding UDP-4-amino-sugars. Is specific to L-glutamate. Marginal activity is observed with L-alanine and L-glutamine, but no activity is detected with gamma-aminobutyric acid (GABA) or L-tryptophan.",Catalyzes the conversion of UDP-4-keto-arabinose (UDP-Ara4O) to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. Belongs to the DegT/DnrJ/EryC1 family. ArnB subfamily,Maybe,Yes,Yes,Yes,Maybe,Yes,GO:0030170; GO:0008483,GO:0008483,GO:0008483; GO:0030170,GO:0008483; GO:0030170,GO:0008483; GO:0030170,GO:0008483,0.6936,1.0,1.0,1.0,0.6936,5,0.8774,0.2259,no
PAT_BACCR,Q814Z4,ProtTale,Bacteria,405,"Aminotransferase involved in the synthesis of cell surface polysaccharides. Catalyzes the transfer of the primary amino group of L-glutamate to C-4'' of UDP-2-acetamido-2,6- dideoxy-alpha-D-xylo-hex-4-ulose (UDP-4-keto-6-deoxy-HexNAc) to form UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-galactose (UDP-4-amino- FucNAc) and 2-oxoglutarate. Also converts UDP-4-keto- 6-deoxy-D-glucose, UDP-4-keto-D-xylose and UDP-4-keto-6-deoxy-L-AltNAc to their corresponding UDP-4-amino-sugars. Is specific to L-glutamate. Marginal activity is observed with L-alanine and L-glutamine, but no activity is detected with gamma-aminobutyric acid (GABA) or L-tryptophan.",Involved in the biosynthesis of L-fucose. Catalyzes the transfer of N-acetylglucosamine (GlcNAc) from ATP to L-fucose-1-phosphate (F1P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and L-fucose.,No,No,No,No,No,not-Yes,GO:0030170; GO:0008483,GO:0016757,GO:0016757,,,,0.4031,0.4031,,,,2,0.4031,0.2259,no
PAT_BACCR,Q814Z4,Protein2Text,Bacteria,405,"Aminotransferase involved in the synthesis of cell surface polysaccharides. Catalyzes the transfer of the primary amino group of L-glutamate to C-4'' of UDP-2-acetamido-2,6- dideoxy-alpha-D-xylo-hex-4-ulose (UDP-4-keto-6-deoxy-HexNAc) to form UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-galactose (UDP-4-amino- FucNAc) and 2-oxoglutarate. Also converts UDP-4-keto- 6-deoxy-D-glucose, UDP-4-keto-D-xylose and UDP-4-keto-6-deoxy-L-AltNAc to their corresponding UDP-4-amino-sugars. Is specific to L-glutamate. Marginal activity is observed with L-alanine and L-glutamine, but no activity is detected with gamma-aminobutyric acid (GABA) or L-tryptophan.","The molecular function of this protein is a transferase, specifically a beta-lactamase. It is involved in the process of breaking down beta-lactam antibiotics, such as penicillins and cephalosporins.",No,No,No,No,No,not-Yes,GO:0030170; GO:0008483,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,0.1799,0.1799,0.1799,0.1799,0.1799,5,0.1799,0.2259,no
PAT_BACCR,Q814Z4,Reference,Bacteria,405,"Aminotransferase involved in the synthesis of cell surface polysaccharides. Catalyzes the transfer of the primary amino group of L-glutamate to C-4'' of UDP-2-acetamido-2,6- dideoxy-alpha-D-xylo-hex-4-ulose (UDP-4-keto-6-deoxy-HexNAc) to form UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-galactose (UDP-4-amino- FucNAc) and 2-oxoglutarate. Also converts UDP-4-keto- 6-deoxy-D-glucose, UDP-4-keto-D-xylose and UDP-4-keto-6-deoxy-L-AltNAc to their corresponding UDP-4-amino-sugars. Is specific to L-glutamate. Marginal activity is observed with L-alanine and L-glutamine, but no activity is detected with gamma-aminobutyric acid (GABA) or L-tryptophan.","Aminotransferase involved in the synthesis of cell surface polysaccharides. Catalyzes the transfer of the primary amino group of L-glutamate to C-4'' of UDP-2-acetamido-2,6- dideoxy-alpha-D-xylo-hex-4-ulose (UDP-4-keto-6-deoxy-HexNAc) to form UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-galactose (UDP-4-amino- FucNAc) and 2-oxoglutarate. Also converts UDP-4-keto- 6-deoxy-D-glucose, UDP-4-keto-D-xylose and UDP-4-keto-6-deoxy-L-AltNAc to their corresponding UDP-4-amino-sugars. Is specific to L-glutamate. Marginal activity is observed with L-alanine and L-glutamine, but no activity is detected with gamma-aminobutyric acid (GABA) or L-tryptophan.",,,,,,,GO:0030170; GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.6936,0.6936,0.6936,0.6936,0.6936,5,0.6936,0.2259,no
PYL_BACCR,Q814Z5,ESM2Text,Bacteria,371,"ATP-grasp enzyme involved in the synthesis of cell surface polysaccharides. Catalyzes the addition of 2- oxoglutarate to the 4-amino moiety of UDP-2-acetamido-4-amino-2,4,6- trideoxy-alpha-D-galactose (UDP-4-amino-FucNAc) to form UDP-yelosamine and ADP. Is also able to ligate 2-oxoglutarate to other 4-amino-sugar derivatives to form UDP-yelose, UDP-aravonose and UDP-solosamine.",Catalyzes the transfer of the biotin moiety from ATP to the 3'-end of dihydrophenylalanine to form tetrahydrophenyl-pyrophosphate (TPP).,No,No,No,No,No,not-Yes,GO:0005524; GO:0004088; GO:0046872,,,,,,,,,,,0,,0.2899,no
PYL_BACCR,Q814Z5,Prot2Text,Bacteria,371,"ATP-grasp enzyme involved in the synthesis of cell surface polysaccharides. Catalyzes the addition of 2- oxoglutarate to the 4-amino moiety of UDP-2-acetamido-4-amino-2,4,6- trideoxy-alpha-D-galactose (UDP-4-amino-FucNAc) to form UDP-yelosamine and ADP. Is also able to ligate 2-oxoglutarate to other 4-amino-sugar derivatives to form UDP-yelose, UDP-aravonose and UDP-solosamine.",Is required for the biosynthesis of pyrrolysine. Catalyzes the ATP-dependent ligation between (3R)-3-methyl-D-ornithine and L-lysine.,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0005524; GO:0004088; GO:0046872,GO:0016874,,GO:0016874,GO:0016874,GO:0016874; GO:0016881,0.3622,,0.3622,0.3622,0.4106,4,0.3743,0.2899,no
PYL_BACCR,Q814Z5,ProtT3,Bacteria,371,"ATP-grasp enzyme involved in the synthesis of cell surface polysaccharides. Catalyzes the addition of 2- oxoglutarate to the 4-amino moiety of UDP-2-acetamido-4-amino-2,4,6- trideoxy-alpha-D-galactose (UDP-4-amino-FucNAc) to form UDP-yelosamine and ADP. Is also able to ligate 2-oxoglutarate to other 4-amino-sugar derivatives to form UDP-yelose, UDP-aravonose and UDP-solosamine.",Catalyzes the formation of N-succinyl-L-glutamate from L-glutamate and succinate semialdehyde. In the C-terminal section; belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. N-succinyl-L-glutamate synthetase subfamily,No,No,No,No,No,not-Yes,GO:0005524; GO:0004088; GO:0046872,GO:0008483; GO:0030170,GO:0008483; GO:0030170,GO:0008483; GO:0030170,GO:0008483; GO:0030170,GO:0008483,0.3447,0.3447,0.3447,0.3447,0.1596,5,0.3077,0.2899,no
PYL_BACCR,Q814Z5,ProtTale,Bacteria,371,"ATP-grasp enzyme involved in the synthesis of cell surface polysaccharides. Catalyzes the addition of 2- oxoglutarate to the 4-amino moiety of UDP-2-acetamido-4-amino-2,4,6- trideoxy-alpha-D-galactose (UDP-4-amino-FucNAc) to form UDP-yelosamine and ADP. Is also able to ligate 2-oxoglutarate to other 4-amino-sugar derivatives to form UDP-yelose, UDP-aravonose and UDP-solosamine.",Catalyzes the ATP-dependent synthesis of L-aspartyl-tRNA(Asp) from L-aspartate and tRNA(Asp). Also has an unspecific aminoacylation activity.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004088; GO:0046872,GO:0004815; GO:0005524,GO:0004815; GO:0005524,GO:0004815; GO:0005524,GO:0004815; GO:0005524,GO:0004815; GO:0005524,0.5696,0.5696,0.5696,0.5696,0.5696,5,0.5696,0.2899,no
PYL_BACCR,Q814Z5,Protein2Text,Bacteria,371,"ATP-grasp enzyme involved in the synthesis of cell surface polysaccharides. Catalyzes the addition of 2- oxoglutarate to the 4-amino moiety of UDP-2-acetamido-4-amino-2,4,6- trideoxy-alpha-D-galactose (UDP-4-amino-FucNAc) to form UDP-yelosamine and ADP. Is also able to ligate 2-oxoglutarate to other 4-amino-sugar derivatives to form UDP-yelose, UDP-aravonose and UDP-solosamine.","This protein is involved in the molecular function of catalyzing the transfer of a phosphate group to a molecule. Specifically, it is a transferase enzyme that catalyzes the transfer of a phosphate group from one molecule to another, in this case, the phosphorylation of a nucleotide. This enzyme is part of the larger class of transferases, enzymes that catalyze the transfer of a functional group from one molecule to another.",No,Vague,No,No,No,not-Yes,GO:0005524; GO:0004088; GO:0046872,GO:0016772,GO:0016301,GO:0016301,GO:0016301,GO:0016301,0.1922,0.1596,0.1596,0.1596,0.1596,5,0.1661,0.2899,no
PYL_BACCR,Q814Z5,Reference,Bacteria,371,"ATP-grasp enzyme involved in the synthesis of cell surface polysaccharides. Catalyzes the addition of 2- oxoglutarate to the 4-amino moiety of UDP-2-acetamido-4-amino-2,4,6- trideoxy-alpha-D-galactose (UDP-4-amino-FucNAc) to form UDP-yelosamine and ADP. Is also able to ligate 2-oxoglutarate to other 4-amino-sugar derivatives to form UDP-yelose, UDP-aravonose and UDP-solosamine.","ATP-grasp enzyme involved in the synthesis of cell surface polysaccharides. Catalyzes the addition of 2- oxoglutarate to the 4-amino moiety of UDP-2-acetamido-4-amino-2,4,6- trideoxy-alpha-D-galactose (UDP-4-amino-FucNAc) to form UDP-yelosamine and ADP. Is also able to ligate 2-oxoglutarate to other 4-amino-sugar derivatives to form UDP-yelose, UDP-aravonose and UDP-solosamine.",,,,,,,GO:0005524; GO:0004088; GO:0046872,GO:0016874; GO:0005524,GO:0016879; GO:0005524,GO:0016874; GO:0005524,GO:0016874; GO:0005524,GO:0016874; GO:0005524,0.6985,0.7493,0.6985,0.6985,0.6985,5,0.7087,0.2899,no
IREK_ENTFA,Q820A8,ESM2Text,Bacteria,718,"Protein kinase that plays a role in maintaining cell wall integrity. Signaling downstream of IreK modulates substrate flux through the peptidoglycan (PG) synthesis pathway, acting via phosphorylation of IreB. Involved in intrinsic cephalosporin antibiotic resistance, which requires IreK kinase activity. In part, probably promotes intrinsic antibiotic resistance by acting in concert with the two-component regulatory system CroS/CroR, via the phosphorylation of histidine sensor kinase CroS. IreK is a substrate of the cotranscribed phosphatase IreP, which suggests that they form a functional couple. May inhibit IreP phosphatase activity, at least transiently, upon kinase activation. Involved in responses to cell-envelope stressors, including oxidative and thermal. Required for both short- and long-term gastrointestinal colonization in mice.","Protein kinase that regulates many aspects of mycobacterial physiology. Is a key component of a signal transduction pathway that regulates cell growth, cell shape and cell division during biofilm formation. Also plays an important role in host cell differentiation and virulence.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0004674,GO:0004674; GO:0005524,GO:0004672,GO:0004674,GO:0004674,GO:0004672,1.0,0.6276,0.6847,0.6847,0.6276,5,0.7249,0.5139,no
IREK_ENTFA,Q820A8,Prot2Text,Bacteria,718,"Protein kinase that plays a role in maintaining cell wall integrity. Signaling downstream of IreK modulates substrate flux through the peptidoglycan (PG) synthesis pathway, acting via phosphorylation of IreB. Involved in intrinsic cephalosporin antibiotic resistance, which requires IreK kinase activity. In part, probably promotes intrinsic antibiotic resistance by acting in concert with the two-component regulatory system CroS/CroR, via the phosphorylation of histidine sensor kinase CroS. IreK is a substrate of the cotranscribed phosphatase IreP, which suggests that they form a functional couple. May inhibit IreP phosphatase activity, at least transiently, upon kinase activation. Involved in responses to cell-envelope stressors, including oxidative and thermal. Required for both short- and long-term gastrointestinal colonization in mice.","Protein kinase that regulates many aspects of mycobacterial physiology. Is a key component of a signal transduction pathway that regulates cell growth, cell shape and cell division via phosphorylation of target proteins.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0004674,GO:0004674,GO:0004672; GO:0004674,GO:0004674,GO:0004674,GO:0004674; GO:0005524,0.6847,0.7429,0.6847,0.6847,1.0,5,0.7594,0.5139,no
IREK_ENTFA,Q820A8,ProtT3,Bacteria,718,"Protein kinase that plays a role in maintaining cell wall integrity. Signaling downstream of IreK modulates substrate flux through the peptidoglycan (PG) synthesis pathway, acting via phosphorylation of IreB. Involved in intrinsic cephalosporin antibiotic resistance, which requires IreK kinase activity. In part, probably promotes intrinsic antibiotic resistance by acting in concert with the two-component regulatory system CroS/CroR, via the phosphorylation of histidine sensor kinase CroS. IreK is a substrate of the cotranscribed phosphatase IreP, which suggests that they form a functional couple. May inhibit IreP phosphatase activity, at least transiently, upon kinase activation. Involved in responses to cell-envelope stressors, including oxidative and thermal. Required for both short- and long-term gastrointestinal colonization in mice.",Belongs to the protein kinase superfamily. Ser/Thr protein kinase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5139,no
IREK_ENTFA,Q820A8,ProtTale,Bacteria,718,"Protein kinase that plays a role in maintaining cell wall integrity. Signaling downstream of IreK modulates substrate flux through the peptidoglycan (PG) synthesis pathway, acting via phosphorylation of IreB. Involved in intrinsic cephalosporin antibiotic resistance, which requires IreK kinase activity. In part, probably promotes intrinsic antibiotic resistance by acting in concert with the two-component regulatory system CroS/CroR, via the phosphorylation of histidine sensor kinase CroS. IreK is a substrate of the cotranscribed phosphatase IreP, which suggests that they form a functional couple. May inhibit IreP phosphatase activity, at least transiently, upon kinase activation. Involved in responses to cell-envelope stressors, including oxidative and thermal. Required for both short- and long-term gastrointestinal colonization in mice.",Member of the two-component regulatory system EnvE/OmpR that regulates genes involved in envelope biogenesis and outer membrane permeability. Phosphorylated EnvE (OmpR) binds directly to the promoter region of its target genes to activate transcription.,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0005524; GO:0004674,GO:0000156; GO:0003677,GO:0000156; GO:0003700,GO:0000156; GO:0003700,GO:0003700,GO:0003700,0.1482,0.1202,0.1202,0.1165,0.1165,5,0.1243,0.5139,no
IREK_ENTFA,Q820A8,Protein2Text,Bacteria,718,"Protein kinase that plays a role in maintaining cell wall integrity. Signaling downstream of IreK modulates substrate flux through the peptidoglycan (PG) synthesis pathway, acting via phosphorylation of IreB. Involved in intrinsic cephalosporin antibiotic resistance, which requires IreK kinase activity. In part, probably promotes intrinsic antibiotic resistance by acting in concert with the two-component regulatory system CroS/CroR, via the phosphorylation of histidine sensor kinase CroS. IreK is a substrate of the cotranscribed phosphatase IreP, which suggests that they form a functional couple. May inhibit IreP phosphatase activity, at least transiently, upon kinase activation. Involved in responses to cell-envelope stressors, including oxidative and thermal. Required for both short- and long-term gastrointestinal colonization in mice.","The molecular function of this protein is to act as a serine/threonine protein kinase, specifically involved in the regulation of cell wall integrity. It is a component of the cell wall integrity (CWI) signaling pathway, which plays a crucial role in maintaining cell wall integrity and responding to cell wall stress. The protein kinase domain of this protein is responsible for phosphorylating target proteins, which triggers a signaling cascade that ultimately leads to the activation of genes involved in cell wall synthesis and remodeling. This protein is also involved in the regulation of cell cycle progression and cell division. 

In more detail, this protein is a serine/threonine protein kinase that is part of the CWI signaling pathway. It is activated in response to cell wall stress, such as the presence of cell wall-perturbing agents or the loss of cell wall components. Upon activation, it phosphorylates target proteins, such as the transcription factor RIM101, which triggers a signaling cascade that ultimately leads to the activation of genes involved in cell wall synthesis and remodeling. This protein is also involved in the regulation of cell cycle progression and cell division, and its activity is regulated by the phosphorylation of its own kinase domain. 

The specific molecular functions of this protein include:

* Serine/threonine protein kinase activity: the protein kinase domain of this protein is responsible for phosphorylating target proteins, which triggers a signaling cascade that ultimately leads to the activation of genes involved in cell wall synthesis and remodeling.
* Cell wall integrity signaling: this protein is a component of the CWI signaling pathway, which plays a crucial role in maintaining cell wall integrity and responding to cell wall stress.
* Cell cycle progression and cell division regulation: this protein is involved in the regulation of cell cycle progression and cell division.
* Phosphorylation of its own kinase domain: the activity of this protein is regulated by the phosphorylation of its own kinase domain.

Overall, the molecular function of this protein is to regulate cell wall integrity and respond to cell wall stress, and to regulate cell cycle progression and cell division.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.6847,0.6847,0.6847,0.6847,0.6847,5,0.6847,0.5139,no
IREK_ENTFA,Q820A8,Reference,Bacteria,718,"Protein kinase that plays a role in maintaining cell wall integrity. Signaling downstream of IreK modulates substrate flux through the peptidoglycan (PG) synthesis pathway, acting via phosphorylation of IreB. Involved in intrinsic cephalosporin antibiotic resistance, which requires IreK kinase activity. In part, probably promotes intrinsic antibiotic resistance by acting in concert with the two-component regulatory system CroS/CroR, via the phosphorylation of histidine sensor kinase CroS. IreK is a substrate of the cotranscribed phosphatase IreP, which suggests that they form a functional couple. May inhibit IreP phosphatase activity, at least transiently, upon kinase activation. Involved in responses to cell-envelope stressors, including oxidative and thermal. Required for both short- and long-term gastrointestinal colonization in mice.","Protein kinase that plays a role in maintaining cell wall integrity. Signaling downstream of IreK modulates substrate flux through the peptidoglycan (PG) synthesis pathway, acting via phosphorylation of IreB. Involved in intrinsic cephalosporin antibiotic resistance, which requires IreK kinase activity. In part, probably promotes intrinsic antibiotic resistance by acting in concert with the two-component regulatory system CroS/CroR, via the phosphorylation of histidine sensor kinase CroS. IreK is a substrate of the cotranscribed phosphatase IreP, which suggests that they form a functional couple. May inhibit IreP phosphatase activity, at least transiently, upon kinase activation. Involved in responses to cell-envelope stressors, including oxidative and thermal. Required for both short- and long-term gastrointestinal colonization in mice.",,,,,,,GO:0005524; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5139,no
HYLB_ENTFA,Q837L8,ESM2Text,Bacteria,1004,Degrades hyaluronic acid (HA) and chondroitin sulfate (CS) A in vitro. Is not active against heparin sodium salt (HS). Involved in the pathogenesis of vancomycin-resistant E.faecalis infections. Contributes to attenuation of the lipopolysaccharide (LPS)-mediated nuclear factor (NF)-kappa-B activation assayed in the mouse RAW-Blue reporter macrophages.,"Broad-specificity glycosaminoglycan lyase, which acts in an exolytic fashion degrading the non-reducing end of the main mannose-binding linkages in the glycan chain of chondroitin sulfate and dermatan sulfate. Has a preference for poly-beta-1,4-linked N-acetylglucosamine (GlcNAc) over poly-beta-1,3-GlcNAc, and has extremely low activity towards the disaccharide mannose-containing glycans. Is not active against keratan sulfate, heparan sulfate, heparin or heparan sulfate.",Yes,Yes,Yes,No,Maybe,Yes,GO:0030246; GO:0030341; GO:0030340,,,,GO:0016829,,,,,0.517,,1,0.517,0.2797,no
HYLB_ENTFA,Q837L8,Prot2Text,Bacteria,1004,Degrades hyaluronic acid (HA) and chondroitin sulfate (CS) A in vitro. Is not active against heparin sodium salt (HS). Involved in the pathogenesis of vancomycin-resistant E.faecalis infections. Contributes to attenuation of the lipopolysaccharide (LPS)-mediated nuclear factor (NF)-kappa-B activation assayed in the mouse RAW-Blue reporter macrophages.,"Broad-specificity glycosaminoglycan lyase, which acts in an exolytic fashion degrading chondroitin sulfates and dermatan sulfate to yield only disaccharide products. Has a preference for chondroitin 4-sulfate over chondroitin 6-sulfate. Has extremely low activity against hyaluronic acid. Is not active against heparin, heparan sulfate, heparin, heparan sulfate, heparin, heparan sulfate, heparin, heparan sulfate, heparan sulfate, heparan sulfate, heparan sulfate, heparan sulfate, heparan sulfate, heparan sulfate, heparan sulfate, heparan sulfate, heparan sulfate, heparan sulfate, heparan sulfate, heparan sulfate, heparan sulfate, heparan sulfate, heparan sulfate, heparan sulfate, heparan sulfate, heparan sulfate, heparan sulfate, heparan sulfate, heparan sulfate, heparan sulfate, heparan sulf",Yes,Yes,Yes,No,Maybe,Yes,GO:0030246; GO:0030341; GO:0030340,GO:0033941,GO:0034000,GO:0016829,GO:0030208,GO:0004414,0.1477,0.5862,0.517,0.0,0.1361,5,0.2774,0.2797,no
HYLB_ENTFA,Q837L8,ProtT3,Bacteria,1004,Degrades hyaluronic acid (HA) and chondroitin sulfate (CS) A in vitro. Is not active against heparin sodium salt (HS). Involved in the pathogenesis of vancomycin-resistant E.faecalis infections. Contributes to attenuation of the lipopolysaccharide (LPS)-mediated nuclear factor (NF)-kappa-B activation assayed in the mouse RAW-Blue reporter macrophages.,Secreted. Belongs to the polysaccharide lyase 9 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0030246; GO:0030341; GO:0030340,GO:0030570,GO:0030570,GO:0030570,GO:0030570,GO:0030570,0.5862,0.5862,0.5862,0.5862,0.5862,5,0.5862,0.2797,no
HYLB_ENTFA,Q837L8,ProtTale,Bacteria,1004,Degrades hyaluronic acid (HA) and chondroitin sulfate (CS) A in vitro. Is not active against heparin sodium salt (HS). Involved in the pathogenesis of vancomycin-resistant E.faecalis infections. Contributes to attenuation of the lipopolysaccharide (LPS)-mediated nuclear factor (NF)-kappa-B activation assayed in the mouse RAW-Blue reporter macrophages.,"Degrades glycosaminoglycans (GAGs) such as chondroitin-4- sulfate, dermatan sulfate and heparan sulfate. Does not have beta-N-acetylglucosaminidase activity. Has a high preference for chondroitin-4- sulfate over dermatan sulfate and heparan sulfate. Also hydrolyzes chondroitin-6- sulfate, chondroitin-8- sulfate and chondroitin-9-sulfate. Does not have beta-N-acetylglucosaminidase activity.",Maybe,Yes,Yes,Yes,Maybe,Yes,GO:0030246; GO:0030341; GO:0030340,GO:0016798,GO:0004553,GO:0004553,GO:0016798,GO:0016798,0.2668,0.2217,0.2217,0.2668,0.2668,5,0.2488,0.2797,no
HYLB_ENTFA,Q837L8,Protein2Text,Bacteria,1004,Degrades hyaluronic acid (HA) and chondroitin sulfate (CS) A in vitro. Is not active against heparin sodium salt (HS). Involved in the pathogenesis of vancomycin-resistant E.faecalis infections. Contributes to attenuation of the lipopolysaccharide (LPS)-mediated nuclear factor (NF)-kappa-B activation assayed in the mouse RAW-Blue reporter macrophages.,"This protein is a hydrolase, which means it breaks down molecules using water. More specifically, it is a glycosidase, which is an enzyme that catalyzes the hydrolysis of glycosidic bonds.",No,Vague,Maybe,Vague,Maybe,not-Yes,GO:0030246; GO:0030341; GO:0030340,GO:0004553,GO:0016798,GO:0016798,GO:0016798,GO:0004553,0.2217,0.2668,0.2668,0.2668,0.2217,5,0.2488,0.2797,no
HYLB_ENTFA,Q837L8,Reference,Bacteria,1004,Degrades hyaluronic acid (HA) and chondroitin sulfate (CS) A in vitro. Is not active against heparin sodium salt (HS). Involved in the pathogenesis of vancomycin-resistant E.faecalis infections. Contributes to attenuation of the lipopolysaccharide (LPS)-mediated nuclear factor (NF)-kappa-B activation assayed in the mouse RAW-Blue reporter macrophages.,Degrades hyaluronic acid (HA) and chondroitin sulfate (CS) A in vitro. Is not active against heparin sodium salt (HS). Involved in the pathogenesis of vancomycin-resistant E.faecalis infections. Contributes to attenuation of the lipopolysaccharide (LPS)-mediated nuclear factor (NF)-kappa-B activation assayed in the mouse RAW-Blue reporter macrophages.,,,,,,,GO:0030246; GO:0030341; GO:0030340,GO:0004415,GO:0004415,GO:0004415,GO:0004415,GO:0004415,0.1656,0.1656,0.1656,0.1656,0.1656,5,0.1656,0.2797,no
CRTA_RUBGE,Q83YH3,ESM2Text,Bacteria,256,Involved in the biosynthesis of the carotenoids spheroidene and spirilloxanthin. Catalyzes the introduction of one keto group at the C-2 position of spheroidene and two keto groups at the C-2 and C-2' positions of spirilloxanthin.,"Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is probably used as an intermediate in the biosynthesis of menaquinone (MK, vitamin K2).",No,No,No,No,No,not-Yes,GO:0046872; GO:0043823,GO:0004506,GO:0004507,GO:0004506,GO:0004506,GO:0004506,0.4167,0.4941,0.4167,0.4167,0.4167,5,0.4322,0.2276,no
CRTA_RUBGE,Q83YH3,Prot2Text,Bacteria,256,Involved in the biosynthesis of the carotenoids spheroidene and spirilloxanthin. Catalyzes the introduction of one keto group at the C-2 position of spheroidene and two keto groups at the C-2 and C-2' positions of spirilloxanthin.,Involved in the degradation of the Pseudomonas aeruginosa quorum sensing signal molecules HHQ (2-heptyl-4-quinolone) and PQS (2-heptyl-3-hydroxy-4-quinolone) to anthranilic acid. Catalyzes the oxidative cleavage of PQS to form N-octanoylanthranilic acid and carbon monoxide.,No,No,No,No,No,not-Yes,GO:0046872; GO:0043823,GO:0051213,,GO:0051213,GO:0016702,GO:0016491,0.3353,,0.3353,0.252,0.416,4,0.3347,0.2276,no
CRTA_RUBGE,Q83YH3,ProtT3,Bacteria,256,Involved in the biosynthesis of the carotenoids spheroidene and spirilloxanthin. Catalyzes the introduction of one keto group at the C-2 position of spheroidene and two keto groups at the C-2 and C-2' positions of spirilloxanthin.,Involved in the biosynthesis of bacteriochlorophyll c (BChl c). Cell membrane; Peripheral membrane protein; Cytoplasmic side. Belongs to the BchO/ChlO family,No,No,No,No,No,not-Yes,GO:0046872; GO:0043823,,,,,,,,,,,0,,0.2276,no
CRTA_RUBGE,Q83YH3,ProtTale,Bacteria,256,Involved in the biosynthesis of the carotenoids spheroidene and spirilloxanthin. Catalyzes the introduction of one keto group at the C-2 position of spheroidene and two keto groups at the C-2 and C-2' positions of spirilloxanthin.,Catalyzes the ring opening of trans-3-hydroxy-cis-2-methylcycloprop-1-ene-1-carboxylate (MCP) to produce 3-hydroxy-2-methylpropenyl-1-phosphate (HMP-P).,No,No,No,No,No,not-Yes,GO:0046872; GO:0043823,GO:0016829,GO:0016829,,,GO:0016829,0.2671,0.2671,,,0.2671,3,0.2671,0.2276,no
CRTA_RUBGE,Q83YH3,Protein2Text,Bacteria,256,Involved in the biosynthesis of the carotenoids spheroidene and spirilloxanthin. Catalyzes the introduction of one keto group at the C-2 position of spheroidene and two keto groups at the C-2 and C-2' positions of spirilloxanthin.,"The molecular function of this protein is not explicitly stated in the provided text. However, based on its classification as a cytochrome P450 monooxygenase, it is likely involved in the oxidation of various organic substrates.",Vague,Vague,Vague,Maybe,Maybe,not-Yes,GO:0046872; GO:0043823,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.4854,0.4854,0.4854,0.4854,0.4854,5,0.4854,0.2276,no
CRTA_RUBGE,Q83YH3,Reference,Bacteria,256,Involved in the biosynthesis of the carotenoids spheroidene and spirilloxanthin. Catalyzes the introduction of one keto group at the C-2 position of spheroidene and two keto groups at the C-2 and C-2' positions of spirilloxanthin.,Involved in the biosynthesis of the carotenoids spheroidene and spirilloxanthin. Catalyzes the introduction of one keto group at the C-2 position of spheroidene and two keto groups at the C-2 and C-2' positions of spirilloxanthin.,,,,,,,GO:0046872; GO:0043823,GO:0016705,GO:0016705,GO:0016491,GO:0016705,GO:0016705,0.4854,0.4854,0.416,0.4854,0.4854,5,0.4715,0.2276,no
CDNG_BRADU,Q89Y83,ESM2Text,Bacteria,416,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (Probable). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-short CBASS system (Probable).",Circadian synthesis protein that adds a second messenger to the 3'-end of the RNA polymerase (RNAP) by a covalent mechanism and around one-third of the pre-mRNA endonuclease activity.,No,No,No,No,Yes,not-Yes,GO:0005524; GO:0106408; GO:0005525; GO:0046872,,,,,,,,,,,0,,0.5542,yes
CDNG_BRADU,Q89Y83,Prot2Text,Bacteria,416,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (Probable). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-short CBASS system (Probable).","Cyclic dinucleotide synthase that catalyzes the synthesis of c-di-GMP, has no activity with other NTP substrates.",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0106408; GO:0005525; GO:0046872,GO:0052929,GO:0052621,GO:0052621,GO:0052621,GO:0052929,0.2372,0.3316,0.3316,0.3316,0.2372,5,0.2938,0.5542,yes
CDNG_BRADU,Q89Y83,ProtT3,Bacteria,416,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (Probable). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-short CBASS system (Probable).","Cyclic dinucleotide synthase that catalyzes the synthesis of 3'3'-cGAMP (3'3'-cyclic GMP-AMP) from GTP and ATP, and 3'3'-cUMP (3'3'-cyclic UMP) from UTP and ATP. 3'3'-cGAMP and 3'3'-cUMP are second messengers that activate the cGAS-STING pathway in response to DNA and RNA viruses, respectively. Belongs to the CBASS (cyclic dinucleotide synthase) family",Yes,Yes,Maybe,Maybe,Yes,Yes,GO:0005524; GO:0106408; GO:0005525; GO:0046872,GO:0016779; GO:0005525; GO:0005524,GO:0009975,GO:0016779,GO:0061501,GO:0061501,0.8579,0.2086,0.3895,0.2887,0.2887,5,0.4067,0.5542,yes
CDNG_BRADU,Q89Y83,ProtTale,Bacteria,416,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (Probable). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-short CBASS system (Probable).","Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type I-D(GG) CBASS system.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0106408; GO:0005525; GO:0046872,GO:0016779,GO:0009975,GO:0061501,GO:0016779,GO:0016779,0.3895,0.2086,0.2887,0.3895,0.3895,5,0.3332,0.5542,yes
CDNG_BRADU,Q89Y83,Protein2Text,Bacteria,416,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (Probable). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-short CBASS system (Probable).","This protein is a restriction enzyme, which means it is involved in the defense mechanism of a cell against invading DNA from other organisms. Specifically, it is a type II restriction enzyme, which cuts DNA at a specific sequence. 
Restriction enzymes are enzymes that cleave foreign DNA at specific recognition sites, thereby protecting the cell from invading DNA. They are part of the cell's defense mechanism against invading DNA from other organisms. There are several types of restriction enzymes, including type II, which cut DNA at a specific sequence. This protein is a type II restriction enzyme.",No,No,No,No,No,not-Yes,GO:0005524; GO:0106408; GO:0005525; GO:0046872,GO:0004519,GO:0015666,GO:0009036,GO:0004519,GO:0004519,0.1403,0.0967,0.0831,0.1403,0.1403,5,0.1201,0.5542,yes
CDNG_BRADU,Q89Y83,Reference,Bacteria,416,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (Probable). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-short CBASS system (Probable).","Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (Probable). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-short CBASS system (Probable).",,,,,,,GO:0005524; GO:0106408; GO:0005525; GO:0046872,GO:0016779,GO:0016779,GO:0016779,GO:0097617,GO:0061501,0.3895,0.3895,0.3895,0.165,0.2887,5,0.3244,0.5542,yes
POLG_DWV,Q8B3M2,ESM2Text,Viruses,2893,[Capsid protein VP2]: Capsid protein that assembles with the capsid proteins VP1 and VP3 to form a pseudo-T3 icosahedral capsid of about 40 nm.,Essential for cell viability. Required for proper cell division and differentiation during postembryonic development of the embryo. May play a role in the regulation of telomere length.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004197; GO:0003723; GO:0003724; GO:0003968; GO:0005198,,,,,,,,,,,0,,0.3222,no
POLG_DWV,Q8B3M2,Prot2Text,Viruses,2893,[Capsid protein VP2]: Capsid protein that assembles with the capsid proteins VP1 and VP3 to form a pseudo-T3 icosahedral capsid of about 40 nm.,Has a role in meiosis.,No,No,Vague,No,No,not-Yes,GO:0005524; GO:0004197; GO:0003723; GO:0003724; GO:0003968; GO:0005198,,,,,,,,,,,0,,0.3222,no
POLG_DWV,Q8B3M2,ProtT3,Viruses,2893,[Capsid protein VP2]: Capsid protein that assembles with the capsid proteins VP1 and VP3 to form a pseudo-T3 icosahedral capsid of about 40 nm.,"[Capsid protein]: Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 30 nm in diameter, and consisting of 180 capsid proteins. [Capsid protein]: Virion. Belongs to the virgaviridae capsid protein family",Yes,Yes,Yes,Yes,Vague,Yes,GO:0005524; GO:0004197; GO:0003723; GO:0003724; GO:0003968; GO:0005198,,,GO:0005198,GO:0005198,GO:0005198,,,0.4064,0.4064,0.4064,3,0.4064,0.3222,no
POLG_DWV,Q8B3M2,ProtTale,Viruses,2893,[Capsid protein VP2]: Capsid protein that assembles with the capsid proteins VP1 and VP3 to form a pseudo-T3 icosahedral capsid of about 40 nm.,"[NS2]: Together with N and NS4, are required for the viral RNA-dependent RNA polymerase activity.",Maybe,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0004197; GO:0003723; GO:0003724; GO:0003968; GO:0005198,,,,,,,,,,,0,,0.3222,no
POLG_DWV,Q8B3M2,Protein2Text,Viruses,2893,[Capsid protein VP2]: Capsid protein that assembles with the capsid proteins VP1 and VP3 to form a pseudo-T3 icosahedral capsid of about 40 nm.,This protein is a subunit of the holoenzyme that catalyzes the elongation of messenger RNA chains by the stepwise addition of amino acids to their corresponding transfer RNAs.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004197; GO:0003723; GO:0003724; GO:0003968; GO:0005198,,,,,,,,,,,0,,0.3222,no
POLG_DWV,Q8B3M2,Reference,Viruses,2893,[Capsid protein VP2]: Capsid protein that assembles with the capsid proteins VP1 and VP3 to form a pseudo-T3 icosahedral capsid of about 40 nm.,[Capsid protein VP2]: Capsid protein that assembles with the capsid proteins VP1 and VP3 to form a pseudo-T3 icosahedral capsid of about 40 nm.,,,,,,,GO:0005524; GO:0004197; GO:0003723; GO:0003724; GO:0003968; GO:0005198,,,,,,,,,,,0,,0.3222,no
TRM7_MOUSE,Q8CBC7,ESM2Text,Eukaryota,324,"Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs. Requisite for faithful cytoplasmic translation. Requires THADA for methylation of the cytidine at position 32 of the anticodon loop of substrate tRNAs. Requires WDR6 for methylation of the nucleotide at position 34 of the anticodon loop of substrate tRNAs. Promotes translation efficiency of the UUU codon. Plays a role in neurogenesis. Required for expression of genes involved in neurogenesis and mitochondrial translation and energy generation. Requisite for RNA-mediated gene silencing. May modify position 32 in tRNA(Arg(ACG)), tRNA(Gln(CUG)), tRNA(Leu(UAA)), tRNA(Leu(UAG)), tRNA(Leu(AAG)), tRNA(Leu(CAG)), tRNA(Phe(GAA)), tRNA(Trp(CCA)) and tRNA(Val(AAC)), and position 34 in tRNA(Phe(GAA)), tRNA(Leu(CAA)), tRNA(Leu(UAA)), tRNA(Sec(UCA)), and tRNA(Trp(CCA)).",Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs.,Yes,Yes,Yes,Yes,Yes,Yes,GO:1904047; GO:0016423; GO:0106340; GO:0106050; GO:0008175,GO:0008173,GO:0008173,GO:0008173,GO:0008173,GO:0008173,0.6498,0.6498,0.6498,0.6498,0.6498,5,0.6498,0.6933,yes
TRM7_MOUSE,Q8CBC7,Prot2Text,Eukaryota,324,"Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs. Requisite for faithful cytoplasmic translation. Requires THADA for methylation of the cytidine at position 32 of the anticodon loop of substrate tRNAs. Requires WDR6 for methylation of the nucleotide at position 34 of the anticodon loop of substrate tRNAs. Promotes translation efficiency of the UUU codon. Plays a role in neurogenesis. Required for expression of genes involved in neurogenesis and mitochondrial translation and energy generation. Requisite for RNA-mediated gene silencing. May modify position 32 in tRNA(Arg(ACG)), tRNA(Gln(CUG)), tRNA(Leu(UAA)), tRNA(Leu(UAG)), tRNA(Leu(AAG)), tRNA(Leu(CAG)), tRNA(Phe(GAA)), tRNA(Trp(CCA)) and tRNA(Val(AAC)), and position 34 in tRNA(Phe(GAA)), tRNA(Leu(CAA)), tRNA(Leu(UAA)), tRNA(Sec(UCA)), and tRNA(Trp(CCA)).",Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs.,Yes,Yes,Yes,Yes,Yes,Yes,GO:1904047; GO:0016423; GO:0106340; GO:0106050; GO:0008175,GO:0008171,GO:0008173,GO:0008173,GO:0008173,GO:0008173,0.4366,0.6498,0.6498,0.6498,0.6498,5,0.6072,0.6933,yes
TRM7_MOUSE,Q8CBC7,ProtT3,Eukaryota,324,"Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs. Requisite for faithful cytoplasmic translation. Requires THADA for methylation of the cytidine at position 32 of the anticodon loop of substrate tRNAs. Requires WDR6 for methylation of the nucleotide at position 34 of the anticodon loop of substrate tRNAs. Promotes translation efficiency of the UUU codon. Plays a role in neurogenesis. Required for expression of genes involved in neurogenesis and mitochondrial translation and energy generation. Requisite for RNA-mediated gene silencing. May modify position 32 in tRNA(Arg(ACG)), tRNA(Gln(CUG)), tRNA(Leu(UAA)), tRNA(Leu(UAG)), tRNA(Leu(AAG)), tRNA(Leu(CAG)), tRNA(Phe(GAA)), tRNA(Trp(CCA)) and tRNA(Val(AAC)), and position 34 in tRNA(Phe(GAA)), tRNA(Leu(CAA)), tRNA(Leu(UAA)), tRNA(Sec(UCA)), and tRNA(Trp(CCA)).","S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that methylates the 2'-O-ribose of uridine 2555 in 25S ribosomal RNA. Nucleus, nucleolus. Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family. RlmM subfamily",Maybe,Maybe,Maybe,No,No,not-Yes,GO:1904047; GO:0016423; GO:0106340; GO:0106050; GO:0008175,GO:0008649,GO:0008649,GO:0008649; GO:0008757,GO:0008649; GO:0008171,GO:0008649,0.5505,0.5505,0.5648,0.559,0.5505,5,0.5551,0.6933,yes
TRM7_MOUSE,Q8CBC7,ProtTale,Eukaryota,324,"Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs. Requisite for faithful cytoplasmic translation. Requires THADA for methylation of the cytidine at position 32 of the anticodon loop of substrate tRNAs. Requires WDR6 for methylation of the nucleotide at position 34 of the anticodon loop of substrate tRNAs. Promotes translation efficiency of the UUU codon. Plays a role in neurogenesis. Required for expression of genes involved in neurogenesis and mitochondrial translation and energy generation. Requisite for RNA-mediated gene silencing. May modify position 32 in tRNA(Arg(ACG)), tRNA(Gln(CUG)), tRNA(Leu(UAA)), tRNA(Leu(UAG)), tRNA(Leu(AAG)), tRNA(Leu(CAG)), tRNA(Phe(GAA)), tRNA(Trp(CCA)) and tRNA(Val(AAC)), and position 34 in tRNA(Phe(GAA)), tRNA(Leu(CAA)), tRNA(Leu(UAA)), tRNA(Sec(UCA)), and tRNA(Trp(CCA)).",Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.,No,Maybe,No,No,No,not-Yes,GO:1904047; GO:0016423; GO:0106340; GO:0106050; GO:0008175,GO:0008649,GO:0008649,GO:0008649,GO:0008649,GO:0008649,0.5505,0.5505,0.5505,0.5505,0.5505,5,0.5505,0.6933,yes
TRM7_MOUSE,Q8CBC7,Protein2Text,Eukaryota,324,"Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs. Requisite for faithful cytoplasmic translation. Requires THADA for methylation of the cytidine at position 32 of the anticodon loop of substrate tRNAs. Requires WDR6 for methylation of the nucleotide at position 34 of the anticodon loop of substrate tRNAs. Promotes translation efficiency of the UUU codon. Plays a role in neurogenesis. Required for expression of genes involved in neurogenesis and mitochondrial translation and energy generation. Requisite for RNA-mediated gene silencing. May modify position 32 in tRNA(Arg(ACG)), tRNA(Gln(CUG)), tRNA(Leu(UAA)), tRNA(Leu(UAG)), tRNA(Leu(AAG)), tRNA(Leu(CAG)), tRNA(Phe(GAA)), tRNA(Trp(CCA)) and tRNA(Val(AAC)), and position 34 in tRNA(Phe(GAA)), tRNA(Leu(CAA)), tRNA(Leu(UAA)), tRNA(Sec(UCA)), and tRNA(Trp(CCA)).","The molecular function of this protein is a methyltransferase. Specifically, it is involved in the methylation of tRNA molecules, which is a crucial step in the processing and maturation of tRNA.",Yes,Yes,Maybe,Yes,Yes,Yes,GO:1904047; GO:0016423; GO:0106340; GO:0106050; GO:0008175,GO:0008175,GO:0008175,GO:0008175,GO:0008175,GO:0008175,0.7603,0.7603,0.7603,0.7603,0.7603,5,0.7603,0.6933,yes
TRM7_MOUSE,Q8CBC7,Reference,Eukaryota,324,"Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs. Requisite for faithful cytoplasmic translation. Requires THADA for methylation of the cytidine at position 32 of the anticodon loop of substrate tRNAs. Requires WDR6 for methylation of the nucleotide at position 34 of the anticodon loop of substrate tRNAs. Promotes translation efficiency of the UUU codon. Plays a role in neurogenesis. Required for expression of genes involved in neurogenesis and mitochondrial translation and energy generation. Requisite for RNA-mediated gene silencing. May modify position 32 in tRNA(Arg(ACG)), tRNA(Gln(CUG)), tRNA(Leu(UAA)), tRNA(Leu(UAG)), tRNA(Leu(AAG)), tRNA(Leu(CAG)), tRNA(Phe(GAA)), tRNA(Trp(CCA)) and tRNA(Val(AAC)), and position 34 in tRNA(Phe(GAA)), tRNA(Leu(CAA)), tRNA(Leu(UAA)), tRNA(Sec(UCA)), and tRNA(Trp(CCA)).","Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs. Requisite for faithful cytoplasmic translation. Requires THADA for methylation of the cytidine at position 32 of the anticodon loop of substrate tRNAs. Requires WDR6 for methylation of the nucleotide at position 34 of the anticodon loop of substrate tRNAs. Promotes translation efficiency of the UUU codon. Plays a role in neurogenesis. Required for expression of genes involved in neurogenesis and mitochondrial translation and energy generation. Requisite for RNA-mediated gene silencing. May modify position 32 in tRNA(Arg(ACG)), tRNA(Gln(CUG)), tRNA(Leu(UAA)), tRNA(Leu(UAG)), tRNA(Leu(AAG)), tRNA(Leu(CAG)), tRNA(Phe(GAA)), tRNA(Trp(CCA)) and tRNA(Val(AAC)), and position 34 in tRNA(Phe(GAA)), tRNA(Leu(CAA)), tRNA(Leu(UAA)), tRNA(Sec(UCA)), and tRNA(Trp(CCA)).",,,,,,,GO:1904047; GO:0016423; GO:0106340; GO:0106050; GO:0008175,GO:0008173; GO:0000049,GO:0008175,GO:0008175,GO:0008173,GO:0008173,0.6158,0.7603,0.7603,0.6498,0.6498,5,0.6872,0.6933,yes
COMFA_STRR6,Q8CWM9,ESM2Text,Bacteria,432,"Involved in transformation (genetic competence for DNA uptake). DNA uptake is energy dependent, this protein may provide the driving force for DNA uptake (Probable). Does not have helicase activity, translocates on single-stranded (ss)DNA in a 5'-3' direction in an ATP-dependent manner, but does not unwind double-stranded (ds)DNA (tested with 5'- and 3'-overhang dsDNA). ATP hydrolysis causes the release of ssDNA from ComFA. A ssDNA-stimulated ATPase; dsDNA does not stimulate ATPase. ATP hydrolysis causes the release of ssDNA from ComFA. ComFC has no effect on ATPase activity. Binds ssDNA but only very poorly to dsDNA in the absence of ATP. Binding to ssDNA does not require free DNA ends.",A global transcription initiation factor that binds to specific DNA sites and initiates transcription when the region becomes fully active. It can bind at a 10-bp site to a 10-bp region that contains both DNA binding and a region with RNA 3'-to-5' polarity. Part of the RadA pilus.,No,No,No,No,No,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787; GO:0046872,GO:0003700; GO:0003677,GO:0003700; GO:0003677,GO:0003700; GO:0003677,GO:0003700; GO:0003677,,0.4413,0.4413,0.4413,0.4413,,4,0.4413,0.6566,yes
COMFA_STRR6,Q8CWM9,Prot2Text,Bacteria,432,"Involved in transformation (genetic competence for DNA uptake). DNA uptake is energy dependent, this protein may provide the driving force for DNA uptake (Probable). Does not have helicase activity, translocates on single-stranded (ss)DNA in a 5'-3' direction in an ATP-dependent manner, but does not unwind double-stranded (ds)DNA (tested with 5'- and 3'-overhang dsDNA). ATP hydrolysis causes the release of ssDNA from ComFA. A ssDNA-stimulated ATPase; dsDNA does not stimulate ATPase. ATP hydrolysis causes the release of ssDNA from ComFA. ComFC has no effect on ATPase activity. Binds ssDNA but only very poorly to dsDNA in the absence of ATP. Binding to ssDNA does not require free DNA ends.",Involved in transformation (competence for DNA uptake). Required for DNA uptake but not for binding. May provide the driving force for transport of DNA through an aqueous channel.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787; GO:0046872,,,,,,,,,,,0,,0.6566,yes
COMFA_STRR6,Q8CWM9,ProtT3,Bacteria,432,"Involved in transformation (genetic competence for DNA uptake). DNA uptake is energy dependent, this protein may provide the driving force for DNA uptake (Probable). Does not have helicase activity, translocates on single-stranded (ss)DNA in a 5'-3' direction in an ATP-dependent manner, but does not unwind double-stranded (ds)DNA (tested with 5'- and 3'-overhang dsDNA). ATP hydrolysis causes the release of ssDNA from ComFA. A ssDNA-stimulated ATPase; dsDNA does not stimulate ATPase. ATP hydrolysis causes the release of ssDNA from ComFA. ComFC has no effect on ATPase activity. Binds ssDNA but only very poorly to dsDNA in the absence of ATP. Binding to ssDNA does not require free DNA ends.",Involved in chromosome segregation. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3 GTPase family. RHD3 subfamily,No,No,No,No,Vague,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787; GO:0046872,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,0.4351,0.4351,0.4351,0.4351,0.4351,5,0.4351,0.6566,yes
COMFA_STRR6,Q8CWM9,ProtTale,Bacteria,432,"Involved in transformation (genetic competence for DNA uptake). DNA uptake is energy dependent, this protein may provide the driving force for DNA uptake (Probable). Does not have helicase activity, translocates on single-stranded (ss)DNA in a 5'-3' direction in an ATP-dependent manner, but does not unwind double-stranded (ds)DNA (tested with 5'- and 3'-overhang dsDNA). ATP hydrolysis causes the release of ssDNA from ComFA. A ssDNA-stimulated ATPase; dsDNA does not stimulate ATPase. ATP hydrolysis causes the release of ssDNA from ComFA. ComFC has no effect on ATPase activity. Binds ssDNA but only very poorly to dsDNA in the absence of ATP. Binding to ssDNA does not require free DNA ends.",Involved in DNA replication.,Vague,Vague,No,Vague,Vague,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787; GO:0046872,,,,,,,,,,,0,,0.6566,yes
COMFA_STRR6,Q8CWM9,Protein2Text,Bacteria,432,"Involved in transformation (genetic competence for DNA uptake). DNA uptake is energy dependent, this protein may provide the driving force for DNA uptake (Probable). Does not have helicase activity, translocates on single-stranded (ss)DNA in a 5'-3' direction in an ATP-dependent manner, but does not unwind double-stranded (ds)DNA (tested with 5'- and 3'-overhang dsDNA). ATP hydrolysis causes the release of ssDNA from ComFA. A ssDNA-stimulated ATPase; dsDNA does not stimulate ATPase. ATP hydrolysis causes the release of ssDNA from ComFA. ComFC has no effect on ATPase activity. Binds ssDNA but only very poorly to dsDNA in the absence of ATP. Binding to ssDNA does not require free DNA ends.","This protein is an RNA polymerase subunit, which is involved in transcription. Specifically, it is a part of the DNA-dependent RNA polymerase complex, which is responsible for transcribing genetic information from DNA into RNA.",No,No,No,No,No,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787; GO:0046872,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.1557,0.1557,0.1557,0.1557,0.1557,5,0.1557,0.6566,yes
COMFA_STRR6,Q8CWM9,Reference,Bacteria,432,"Involved in transformation (genetic competence for DNA uptake). DNA uptake is energy dependent, this protein may provide the driving force for DNA uptake (Probable). Does not have helicase activity, translocates on single-stranded (ss)DNA in a 5'-3' direction in an ATP-dependent manner, but does not unwind double-stranded (ds)DNA (tested with 5'- and 3'-overhang dsDNA). ATP hydrolysis causes the release of ssDNA from ComFA. A ssDNA-stimulated ATPase; dsDNA does not stimulate ATPase. ATP hydrolysis causes the release of ssDNA from ComFA. ComFC has no effect on ATPase activity. Binds ssDNA but only very poorly to dsDNA in the absence of ATP. Binding to ssDNA does not require free DNA ends.","Involved in transformation (genetic competence for DNA uptake). DNA uptake is energy dependent, this protein may provide the driving force for DNA uptake (Probable). Does not have helicase activity, translocates on single-stranded (ss)DNA in a 5'-3' direction in an ATP-dependent manner, but does not unwind double-stranded (ds)DNA (tested with 5'- and 3'-overhang dsDNA). ATP hydrolysis causes the release of ssDNA from ComFA. A ssDNA-stimulated ATPase; dsDNA does not stimulate ATPase. ATP hydrolysis causes the release of ssDNA from ComFA. ComFC has no effect on ATPase activity. Binds ssDNA but only very poorly to dsDNA in the absence of ATP. Binding to ssDNA does not require free DNA ends.",,,,,,,GO:0043138; GO:0005524; GO:0003677; GO:0016787; GO:0046872,GO:0003697; GO:0016887; GO:0005524,GO:0016887; GO:0003697; GO:0005524,GO:0003697; GO:0016887; GO:0008094,GO:0003697; GO:0016887; GO:0005524,GO:0003697; GO:0016887; GO:0005524,0.6425,0.6425,0.5418,0.6425,0.6425,5,0.6224,0.6566,yes
LICC_STRR6,Q8DPI6,ESM2Text,Bacteria,229,"Cytidylyltransferase involved in the biosynthesis of the phosphocholine containing cell wall constituents, teichoic acid and lipoteichoic acid, which are essential for cell separation and pathogenesis. Catalyzes the activation of phosphocholine (P-Cho) to CDP-choline (CDP-Cho). Can also use phosphoethanolamine and 2-aminoethylphosphonate, with much lower efficiency. Shows lower activity with dCTP, weak activity with ATP and no activity with GTP, TTP, UTP, dATP, dGTP and dTTP.",Could be involved in the biosynthesis of a cell wall component.,Vague,Vague,Vague,Vague,No,not-Yes,GO:0004105,,,,,,,,,,,0,,0.5334,no
LICC_STRR6,Q8DPI6,Prot2Text,Bacteria,229,"Cytidylyltransferase involved in the biosynthesis of the phosphocholine containing cell wall constituents, teichoic acid and lipoteichoic acid, which are essential for cell separation and pathogenesis. Catalyzes the activation of phosphocholine (P-Cho) to CDP-choline (CDP-Cho). Can also use phosphoethanolamine and 2-aminoethylphosphonate, with much lower efficiency. Shows lower activity with dCTP, weak activity with ATP and no activity with GTP, TTP, UTP, dATP, dGTP and dTTP.","Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis.",No,No,Maybe,Maybe,No,not-Yes,GO:0004105,GO:0008879,GO:0008879,GO:0008879,GO:0008879,GO:0008879,0.6335,0.6335,0.6335,0.6335,0.6335,5,0.6335,0.5334,no
LICC_STRR6,Q8DPI6,ProtT3,Bacteria,229,"Cytidylyltransferase involved in the biosynthesis of the phosphocholine containing cell wall constituents, teichoic acid and lipoteichoic acid, which are essential for cell separation and pathogenesis. Catalyzes the activation of phosphocholine (P-Cho) to CDP-choline (CDP-Cho). Can also use phosphoethanolamine and 2-aminoethylphosphonate, with much lower efficiency. Shows lower activity with dCTP, weak activity with ATP and no activity with GTP, TTP, UTP, dATP, dGTP and dTTP.",Catalyzes the formation of UDP-N-acetylglucosamine (UDP-GlcNAc) from GlcNAc-1-P and UTP. Belongs to the UDPGP type 2 family,No,No,Maybe,Maybe,No,not-Yes,GO:0004105,GO:0003977,GO:0003977,GO:0003977,GO:0003977,GO:0003977,0.5445,0.5445,0.5445,0.5445,0.5445,5,0.5445,0.5334,no
LICC_STRR6,Q8DPI6,ProtTale,Bacteria,229,"Cytidylyltransferase involved in the biosynthesis of the phosphocholine containing cell wall constituents, teichoic acid and lipoteichoic acid, which are essential for cell separation and pathogenesis. Catalyzes the activation of phosphocholine (P-Cho) to CDP-choline (CDP-Cho). Can also use phosphoethanolamine and 2-aminoethylphosphonate, with much lower efficiency. Shows lower activity with dCTP, weak activity with ATP and no activity with GTP, TTP, UTP, dATP, dGTP and dTTP.",Bifunctional enzyme that catalyzes the enolization of D-fructose 6-phosphate to 2-keto-3-deoxy-D-gluconate (KDG) and catalyzes the condensation of acetyl-CoA with D-fructose 6-phosphate to form malonyl-CoA with the release of CoA.,No,No,No,No,No,not-Yes,GO:0004105,GO:0016829; GO:0016746,GO:0016829; GO:0016746,,,GO:0016853; GO:0016746,0.3909,0.3909,,,0.3909,3,0.3909,0.5334,no
LICC_STRR6,Q8DPI6,Protein2Text,Bacteria,229,"Cytidylyltransferase involved in the biosynthesis of the phosphocholine containing cell wall constituents, teichoic acid and lipoteichoic acid, which are essential for cell separation and pathogenesis. Catalyzes the activation of phosphocholine (P-Cho) to CDP-choline (CDP-Cho). Can also use phosphoethanolamine and 2-aminoethylphosphonate, with much lower efficiency. Shows lower activity with dCTP, weak activity with ATP and no activity with GTP, TTP, UTP, dATP, dGTP and dTTP.","The molecular function of this protein is an enzyme that catalyzes the transfer of a glucose molecule from one molecule of glucose-1-phosphate to another molecule of ADP to produce ADP-glucose, which is used as a building block for glycogen synthesis. This protein is involved in the synthesis of glycogen, a complex carbohydrate that serves as a storage form of glucose in cells. 
In more detail, this protein is a glucose-1-phosphate adenylyltransferase that catalyzes the synthesis of ADP-glucose from glucose-1-phosphate and ATP. This reaction is the rate-limiting step in glycogen biosynthesis and is essential for the synthesis of glycogen, a complex carbohydrate that serves as a storage form of glucose in cells. The protein is also involved in the regulation of glycogen synthesis by responding to changes in glucose levels in the cell.
The molecular function of this protein is critical for the regulation of glycogen synthesis and metabolism, and its activity is essential for maintaining normal blood glucose levels and preventing the development of hyperglycemia and its associated complications. 
This protein is also involved in the synthesis of glycogen in other organisms, including plants and bacteria, where it plays a critical role in energy storage and metabolism. 
The protein is also a target for the development of new drugs for the treatment of glycogen storage diseases, a group of rare genetic disorders that result from defects in glycogen synthesis or degradation. 
The protein is also involved in the regulation of glycogen synthesis in response to changes in insulin levels, and its activity is influenced by hormones such as insulin and glucagon. 
The protein is also a critical component of the glycogen storage pathway, which is essential for maintaining normal blood glucose levels and preventing the development of hyperglycemia and its associated complications. 
The protein is also involved in the synthesis of glycogen in the liver and muscles, where it plays a critical role in energy storage and metabolism. 
The protein is also a target for the development of new drugs for the treatment of metabolic disorders, such as type 2 diabetes and obesity. 
The protein is also involved in the regulation of glycogen synthesis in response to changes in glucose levels in the cell, and its activity is influenced by hormones such as insulin and glucagon. 
The protein is also a critical component of the glycogen storage pathway, which is essential for maintaining normal blood glucose levels and preventing the development of hyperglycemia and its associated complications. 
The protein is also involved in the synthesis of glyc",No,No,Maybe,No,No,not-Yes,GO:0004105,GO:0008878,GO:0008878,GO:0008878,GO:0008878,GO:0008878,0.5445,0.5445,0.5445,0.5445,0.5445,5,0.5445,0.5334,no
LICC_STRR6,Q8DPI6,Reference,Bacteria,229,"Cytidylyltransferase involved in the biosynthesis of the phosphocholine containing cell wall constituents, teichoic acid and lipoteichoic acid, which are essential for cell separation and pathogenesis. Catalyzes the activation of phosphocholine (P-Cho) to CDP-choline (CDP-Cho). Can also use phosphoethanolamine and 2-aminoethylphosphonate, with much lower efficiency. Shows lower activity with dCTP, weak activity with ATP and no activity with GTP, TTP, UTP, dATP, dGTP and dTTP.","Cytidylyltransferase involved in the biosynthesis of the phosphocholine containing cell wall constituents, teichoic acid and lipoteichoic acid, which are essential for cell separation and pathogenesis. Catalyzes the activation of phosphocholine (P-Cho) to CDP-choline (CDP-Cho). Can also use phosphoethanolamine and 2-aminoethylphosphonate, with much lower efficiency. Shows lower activity with dCTP, weak activity with ATP and no activity with GTP, TTP, UTP, dATP, dGTP and dTTP.",,,,,,,GO:0004105,GO:0004105,GO:0004105,GO:0004105,GO:0004105,GO:0004105,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5334,no
CTAA_SHEON,Q8E8P8,ESM2Text,Bacteria,330,"Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.","Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0120547; GO:0046872,GO:0008535,GO:0016491,GO:0016705,GO:0016491,,0.0,0.5125,0.4132,0.5125,,4,0.3595,0.5494,yes
CTAA_SHEON,Q8E8P8,Prot2Text,Bacteria,330,"Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.","Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0120547; GO:0046872,GO:0008535,,GO:0016705,GO:0016491,GO:0016491,0.0,,0.4132,0.5125,0.5125,4,0.3595,0.5494,yes
CTAA_SHEON,Q8E8P8,ProtT3,Bacteria,330,"Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.","Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A. Cell membrane; Multi-pass membrane protein. Belongs to the COX15/CtaA family. Type 2 subfamily",Yes,Yes,Yes,Yes,Yes,Yes,GO:0120547; GO:0046872,GO:0016705,GO:0008535,GO:0008535,GO:0016491; GO:0020037,GO:0016491,0.4132,0.0,0.0,0.4871,0.5125,5,0.2826,0.5494,yes
CTAA_SHEON,Q8E8P8,ProtTale,Bacteria,330,"Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.","Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0120547; GO:0046872,GO:0016491,GO:0008535,GO:0016491,GO:0016491,GO:0016491,0.5125,0.0,0.5125,0.5125,0.5125,5,0.41,0.5494,yes
CTAA_SHEON,Q8E8P8,Protein2Text,Bacteria,330,"Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.",The molecular function of this protein is iron-chelate dehydrogenase activity.,Vague,No,No,No,Maybe,not-Yes,GO:0120547; GO:0046872,,,,,,,,,,,0,,0.5494,yes
CTAA_SHEON,Q8E8P8,Reference,Bacteria,330,"Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.","Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.",,,,,,,GO:0120547; GO:0046872,GO:0016705,GO:0008535,GO:0004497,GO:0016491,GO:0016705,0.4132,0.0,0.4132,0.5125,0.4132,5,0.3504,0.5494,yes
CYMA_SHEON,Q8E8S0,ESM2Text,Bacteria,187,"Quinol dehydrogenase involved in several anaerobic electron transfer pathways. Acquires electrons from the membrane quinone pool and mediates their transfer to several periplasmic terminal reductases and redox shuttles, including the fumarate reductase FccA, the small tetraheme cytochrome (STC), the c-type cytochrome MtrA, the nitrate reductase NapA (either through NapB or directly), the nitrite reductase NrfA and probably also the DmsE subunit of dimethyl sulfoxide (DMSO) reductase. Required for growth on fumarate and on DMSO, and for the reduction of iron(III), manganese(IV), nitrite and nitrate. Not essential for growth on trimethylamine-N-oxide (TMAO).",Reduces thePart of the electron transfer chain of cytochrome c.,Maybe,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0009055; GO:0020037; GO:0046872; GO:0008121,,GO:0009055,,GO:0009055,,,0.5611,,0.5611,,2,0.5611,0.4493,no
CYMA_SHEON,Q8E8S0,Prot2Text,Bacteria,187,"Quinol dehydrogenase involved in several anaerobic electron transfer pathways. Acquires electrons from the membrane quinone pool and mediates their transfer to several periplasmic terminal reductases and redox shuttles, including the fumarate reductase FccA, the small tetraheme cytochrome (STC), the c-type cytochrome MtrA, the nitrate reductase NapA (either through NapB or directly), the nitrite reductase NrfA and probably also the DmsE subunit of dimethyl sulfoxide (DMSO) reductase. Required for growth on fumarate and on DMSO, and for the reduction of iron(III), manganese(IV), nitrite and nitrate. Not essential for growth on trimethylamine-N-oxide (TMAO).",Mediates electron flow from quinones to the NapAB complex.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0009055; GO:0020037; GO:0046872; GO:0008121,GO:0009055,GO:0009055,GO:0009055,GO:0009055,GO:0009055,0.5611,0.5611,0.5611,0.5611,0.5611,5,0.5611,0.4493,no
CYMA_SHEON,Q8E8S0,ProtT3,Bacteria,187,"Quinol dehydrogenase involved in several anaerobic electron transfer pathways. Acquires electrons from the membrane quinone pool and mediates their transfer to several periplasmic terminal reductases and redox shuttles, including the fumarate reductase FccA, the small tetraheme cytochrome (STC), the c-type cytochrome MtrA, the nitrate reductase NapA (either through NapB or directly), the nitrite reductase NrfA and probably also the DmsE subunit of dimethyl sulfoxide (DMSO) reductase. Required for growth on fumarate and on DMSO, and for the reduction of iron(III), manganese(IV), nitrite and nitrate. Not essential for growth on trimethylamine-N-oxide (TMAO).",Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2- (methylthio)ethanesulfonate) using coenzyme B (CoB or 7- mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of CoB and CoM (CoM-S-S-CoB). This is the final step in methanogenesis. Cell inner membrane; Single-,No,No,No,No,No,not-Yes,GO:0009055; GO:0020037; GO:0046872; GO:0008121,GO:0050524,GO:0050524,GO:0050524,GO:0050524,GO:0050524,0.1415,0.1415,0.1415,0.1415,0.1415,5,0.1415,0.4493,no
CYMA_SHEON,Q8E8S0,ProtTale,Bacteria,187,"Quinol dehydrogenase involved in several anaerobic electron transfer pathways. Acquires electrons from the membrane quinone pool and mediates their transfer to several periplasmic terminal reductases and redox shuttles, including the fumarate reductase FccA, the small tetraheme cytochrome (STC), the c-type cytochrome MtrA, the nitrate reductase NapA (either through NapB or directly), the nitrite reductase NrfA and probably also the DmsE subunit of dimethyl sulfoxide (DMSO) reductase. Required for growth on fumarate and on DMSO, and for the reduction of iron(III), manganese(IV), nitrite and nitrate. Not essential for growth on trimethylamine-N-oxide (TMAO).",Mediates electron flow from quinones to the NapAB complex.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0009055; GO:0020037; GO:0046872; GO:0008121,GO:0009055,GO:0009055,GO:0009055,GO:0009055,GO:0009055,0.5611,0.5611,0.5611,0.5611,0.5611,5,0.5611,0.4493,no
CYMA_SHEON,Q8E8S0,Protein2Text,Bacteria,187,"Quinol dehydrogenase involved in several anaerobic electron transfer pathways. Acquires electrons from the membrane quinone pool and mediates their transfer to several periplasmic terminal reductases and redox shuttles, including the fumarate reductase FccA, the small tetraheme cytochrome (STC), the c-type cytochrome MtrA, the nitrate reductase NapA (either through NapB or directly), the nitrite reductase NrfA and probably also the DmsE subunit of dimethyl sulfoxide (DMSO) reductase. Required for growth on fumarate and on DMSO, and for the reduction of iron(III), manganese(IV), nitrite and nitrate. Not essential for growth on trimethylamine-N-oxide (TMAO).",The molecular function of this protein is an electron transport chain transmembrane electron donor (oxidoreductase activity).,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0009055; GO:0020037; GO:0046872; GO:0008121,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.2342,0.2342,0.2342,0.2342,0.2342,5,0.2342,0.4493,no
CYMA_SHEON,Q8E8S0,Reference,Bacteria,187,"Quinol dehydrogenase involved in several anaerobic electron transfer pathways. Acquires electrons from the membrane quinone pool and mediates their transfer to several periplasmic terminal reductases and redox shuttles, including the fumarate reductase FccA, the small tetraheme cytochrome (STC), the c-type cytochrome MtrA, the nitrate reductase NapA (either through NapB or directly), the nitrite reductase NrfA and probably also the DmsE subunit of dimethyl sulfoxide (DMSO) reductase. Required for growth on fumarate and on DMSO, and for the reduction of iron(III), manganese(IV), nitrite and nitrate. Not essential for growth on trimethylamine-N-oxide (TMAO).","Quinol dehydrogenase involved in several anaerobic electron transfer pathways. Acquires electrons from the membrane quinone pool and mediates their transfer to several periplasmic terminal reductases and redox shuttles, including the fumarate reductase FccA, the small tetraheme cytochrome (STC), the c-type cytochrome MtrA, the nitrate reductase NapA (either through NapB or directly), the nitrite reductase NrfA and probably also the DmsE subunit of dimethyl sulfoxide (DMSO) reductase. Required for growth on fumarate and on DMSO, and for the reduction of iron(III), manganese(IV), nitrite and nitrate. Not essential for growth on trimethylamine-N-oxide (TMAO).",,,,,,,GO:0009055; GO:0020037; GO:0046872; GO:0008121,GO:0009055; GO:0016679,GO:0009055,GO:0016491,GO:0016491; GO:0009055,GO:0009055; GO:0016679,0.5136,0.5611,0.2342,0.5242,0.5136,5,0.4693,0.4493,no
YCJX_SHEON,Q8EG04,ESM2Text,Bacteria,485,Binds GTP and GDP. Has intrinsic GTPase activity. Does not hydrolyze ATP. May act as a transducer of stress responses.,Involved in the non-homologous end joining (NHEJ) DNA double-strand break repair.,No,No,No,No,No,not-Yes,GO:0003925; GO:0019003; GO:0005525; GO:0003924,,,,,,,,,,,0,,0.2296,no
YCJX_SHEON,Q8EG04,Prot2Text,Bacteria,485,Binds GTP and GDP. Has intrinsic GTPase activity. Does not hydrolyze ATP. May act as a transducer of stress responses.,Required for morphogenesis under gluconeogenic growth conditions.,No,Vague,Vague,Vague,No,not-Yes,GO:0003925; GO:0019003; GO:0005525; GO:0003924,,,,,,,,,,,0,,0.2296,no
YCJX_SHEON,Q8EG04,ProtT3,Bacteria,485,Binds GTP and GDP. Has intrinsic GTPase activity. Does not hydrolyze ATP. May act as a transducer of stress responses.,Cell inner membrane; Peripheral membrane protein; Cytoplasmic side,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0003925; GO:0019003; GO:0005525; GO:0003924,,,,,,,,,,,0,,0.2296,no
YCJX_SHEON,Q8EG04,ProtTale,Bacteria,485,Binds GTP and GDP. Has intrinsic GTPase activity. Does not hydrolyze ATP. May act as a transducer of stress responses.,Could be involved in the regulation of sporulation.,No,No,No,No,No,not-Yes,GO:0003925; GO:0019003; GO:0005525; GO:0003924,,,,,,,,,,,0,,0.2296,no
YCJX_SHEON,Q8EG04,Protein2Text,Bacteria,485,Binds GTP and GDP. Has intrinsic GTPase activity. Does not hydrolyze ATP. May act as a transducer of stress responses.,This protein is involved in the regulation of cell division.,No,Vague,Vague,Vague,No,not-Yes,GO:0003925; GO:0019003; GO:0005525; GO:0003924,,,,,,,,,,,0,,0.2296,no
YCJX_SHEON,Q8EG04,Reference,Bacteria,485,Binds GTP and GDP. Has intrinsic GTPase activity. Does not hydrolyze ATP. May act as a transducer of stress responses.,Binds GTP and GDP. Has intrinsic GTPase activity. Does not hydrolyze ATP. May act as a transducer of stress responses.,,,,,,,GO:0003925; GO:0019003; GO:0005525; GO:0003924,GO:0005525; GO:0003924,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0005525; GO:0003924,GO:0005525; GO:0003924,0.9431,0.9431,0.9431,0.9431,0.9431,5,0.9431,0.2296,no
CHIT_PLAF7,Q8I4R4,ESM2Text,Eukaryota,378,"Endochitinase that cleaves beta-1,4-linkages between tri- and tetramers of N-acetylglucosamine (GlcNAc) from penta- and hexameric chitin oligomers. Does not cleave smaller chitin oligosaccharides. Required to cross the acellular, chitin-containing peritrophic matrix (PM) which is formed around the ingested blood meal in the mosquito midgut allowing the ookinete to invade the mosquito gut epithelium.",Glucagon-like protein involved in the formation of the linkage fibrin and coagulogen.,No,No,No,No,No,not-Yes,GO:0008061; GO:0004568; GO:0008843,,,,,,,,,,,0,,0.2085,no
CHIT_PLAF7,Q8I4R4,Prot2Text,Eukaryota,378,"Endochitinase that cleaves beta-1,4-linkages between tri- and tetramers of N-acetylglucosamine (GlcNAc) from penta- and hexameric chitin oligomers. Does not cleave smaller chitin oligosaccharides. Required to cross the acellular, chitin-containing peritrophic matrix (PM) which is formed around the ingested blood meal in the mosquito midgut allowing the ookinete to invade the mosquito gut epithelium.","Beta-glucanases participate in the metabolism of beta-glucans, cell walls that are involved in cell-cell fusion during hyaluronic acid degradation. EXG2 is able to bind chitin.",No,No,No,No,No,not-Yes,GO:0008061; GO:0004568; GO:0008843,GO:0004553; GO:0008061,,GO:0004553; GO:0008061,GO:0004553,GO:0004553; GO:0008061,0.894,,0.894,0.654,0.894,4,0.834,0.2085,no
CHIT_PLAF7,Q8I4R4,ProtT3,Eukaryota,378,"Endochitinase that cleaves beta-1,4-linkages between tri- and tetramers of N-acetylglucosamine (GlcNAc) from penta- and hexameric chitin oligomers. Does not cleave smaller chitin oligosaccharides. Required to cross the acellular, chitin-containing peritrophic matrix (PM) which is formed around the ingested blood meal in the mosquito midgut allowing the ookinete to invade the mosquito gut epithelium.",Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily,Vague,Vague,Maybe,Vague,Vague,not-Yes,GO:0008061; GO:0004568; GO:0008843,GO:0004568,GO:0004568,GO:0004568,GO:0004568,GO:0004568,0.7489,0.7489,0.7489,0.7489,0.7489,5,0.7489,0.2085,no
CHIT_PLAF7,Q8I4R4,ProtTale,Eukaryota,378,"Endochitinase that cleaves beta-1,4-linkages between tri- and tetramers of N-acetylglucosamine (GlcNAc) from penta- and hexameric chitin oligomers. Does not cleave smaller chitin oligosaccharides. Required to cross the acellular, chitin-containing peritrophic matrix (PM) which is formed around the ingested blood meal in the mosquito midgut allowing the ookinete to invade the mosquito gut epithelium.","Chitinase involved in the degradation of chitin, a component of the cell wall and cell membranes.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008061; GO:0004568; GO:0008843,GO:0004568,GO:0004568,GO:0004568,GO:0004568,GO:0004568,0.7489,0.7489,0.7489,0.7489,0.7489,5,0.7489,0.2085,no
CHIT_PLAF7,Q8I4R4,Protein2Text,Eukaryota,378,"Endochitinase that cleaves beta-1,4-linkages between tri- and tetramers of N-acetylglucosamine (GlcNAc) from penta- and hexameric chitin oligomers. Does not cleave smaller chitin oligosaccharides. Required to cross the acellular, chitin-containing peritrophic matrix (PM) which is formed around the ingested blood meal in the mosquito midgut allowing the ookinete to invade the mosquito gut epithelium.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its name and the context in which it is mentioned, it can be inferred that the protein is involved in breaking down or degrading molecules, specifically in the context of hydrolysis of chitin. Chitin is a type of polysaccharide found in the cell walls of fungi, the exoskeletons of arthropods, and the scales of fish. The protein's role in breaking down chitin suggests that it may be involved in the degradation of chitin, which is a key process in various biological and ecological contexts. 

However, for a more accurate and specific answer, it would be helpful to have more information about the protein, such as its sequence, structure, and known functions. 

References:
1.  Gao, X., Li, Y., Chen, Y., Wang, W., Zhang, Y., & Zhang, X. (2020). Cloning and characterization of a chitinase gene from the medicinal fungus Cordyceps sinensis. Journal of Fungi, 6(2), 126. 
2.  Li, W., Zhang, X., & Gao, X. (2020). Molecular cloning and expression of a chitinase gene from the medicinal fungus Cordyceps sinensis. Journal of Fungi, 6(2), 125. 
3.  Zhang, X., Li, W., & Gao, X. (2020). Cloning and characterization of a chitinase gene from the medicinal fungus Cordyceps sinensis. Journal of Fungi, 6(2), 124.",Maybe,Yes,Yes,Vague,Maybe,not-Yes,GO:0008061; GO:0004568; GO:0008843,GO:0004568,GO:0004568,GO:0004568,GO:0004568,GO:0004568,0.7489,0.7489,0.7489,0.7489,0.7489,5,0.7489,0.2085,no
CHIT_PLAF7,Q8I4R4,Reference,Eukaryota,378,"Endochitinase that cleaves beta-1,4-linkages between tri- and tetramers of N-acetylglucosamine (GlcNAc) from penta- and hexameric chitin oligomers. Does not cleave smaller chitin oligosaccharides. Required to cross the acellular, chitin-containing peritrophic matrix (PM) which is formed around the ingested blood meal in the mosquito midgut allowing the ookinete to invade the mosquito gut epithelium.","Endochitinase that cleaves beta-1,4-linkages between tri- and tetramers of N-acetylglucosamine (GlcNAc) from penta- and hexameric chitin oligomers. Does not cleave smaller chitin oligosaccharides. Required to cross the acellular, chitin-containing peritrophic matrix (PM) which is formed around the ingested blood meal in the mosquito midgut allowing the ookinete to invade the mosquito gut epithelium.",,,,,,,GO:0008061; GO:0004568; GO:0008843,GO:0004568,GO:0004568,GO:0004568,GO:0004568,GO:0004568,0.7489,0.7489,0.7489,0.7489,0.7489,5,0.7489,0.2085,no
TPX2_PLAF7,Q8I5Q6,ESM2Text,Eukaryota,216,"Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively.","Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008379,GO:0051920; GO:0004601,GO:0004601,GO:0004601,GO:0051920; GO:0004601,GO:0004601; GO:0051920,0.78,0.7313,0.7313,0.78,0.78,5,0.7605,0.2284,no
TPX2_PLAF7,Q8I5Q6,Prot2Text,Eukaryota,216,"Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively.","Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008379,GO:0004601,GO:0004601; GO:0051920,GO:0004601; GO:0051920,GO:0004601,GO:0004601; GO:0051920,0.7313,0.78,0.78,0.7313,0.78,5,0.7605,0.2284,no
TPX2_PLAF7,Q8I5Q6,ProtT3,Eukaryota,216,"Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively.","Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008379,GO:0004601; GO:0051920,GO:0051920,GO:0051920,GO:0004601; GO:0051920,GO:0004601; GO:0051920,0.78,0.8044,0.8044,0.78,0.78,5,0.7898,0.2284,no
TPX2_PLAF7,Q8I5Q6,ProtTale,Eukaryota,216,"Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively.","Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008379,GO:0004601; GO:0016209,GO:0004601; GO:0016209,GO:0008379; GO:0004601,GO:0051920,GO:0004601,0.6179,0.6179,0.9104,0.8044,0.7313,5,0.7364,0.2284,no
TPX2_PLAF7,Q8I5Q6,Protein2Text,Eukaryota,216,"Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively.","The molecular function of this protein is thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. It also has a glutathione-dependent peroxidase activity. It has a glutaredoxin activity, and may be involved in the repair of oxidative stress-damaged proteins. It may also be involved in the regulation of cell growth and differentiation. It has a glutathione S-transferase activity, and may be involved in the conjugation of reduced glutathione to a wide range of exogenous and endogenous hydrophobic electrophiles. It may also be involved in the conjugation of reduced glutathione to a wide range of exogenous and endogenous hydrophobic electrophiles. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may also be involved in the regulation of cell growth and differentiation. It may",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008379,GO:0004601,GO:0004602,GO:0004601,GO:0004602,GO:0004602,0.7313,0.6262,0.7313,0.6262,0.6262,5,0.6682,0.2284,no
TPX2_PLAF7,Q8I5Q6,Reference,Eukaryota,216,"Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively.","Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively.",,,,,,,GO:0008379,GO:0004601,GO:0004601,GO:0004601; GO:0008379,GO:0004601,GO:0004601,0.7313,0.7313,0.9104,0.7313,0.7313,5,0.7671,0.2284,no
ALF1_TOXGO,Q8I8I2,ESM2Text,Eukaryota,363,"Plays a key role in glycolysis by catalyzing the cleavage of fructose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. Forms a bridge between cell surface adhesins and the actin cytoskeleton. Required for parasite invasion of host cells.","May be involved in coenzyme Q, in smooth muscle contraction.",No,No,No,No,No,not-Yes,GO:0003779; GO:0004332,,,,,,,,,,,0,,0.2154,no
ALF1_TOXGO,Q8I8I2,Prot2Text,Eukaryota,363,"Plays a key role in glycolysis by catalyzing the cleavage of fructose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. Forms a bridge between cell surface adhesins and the actin cytoskeleton. Required for parasite invasion of host cells.",Fructose-bisphosphate aldolase that plays a key role in glycolysis and gluconeogenesis.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003779; GO:0004332,GO:0004332,GO:0004332,GO:0004332,GO:0004332,GO:0004332,0.7015,0.7015,0.7015,0.7015,0.7015,5,0.7015,0.2154,no
ALF1_TOXGO,Q8I8I2,ProtT3,Eukaryota,363,"Plays a key role in glycolysis by catalyzing the cleavage of fructose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. Forms a bridge between cell surface adhesins and the actin cytoskeleton. Required for parasite invasion of host cells.",Belongs to the class I fructose-bisphosphate aldolase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0003779; GO:0004332,GO:0004332,GO:0004332,GO:0004332,GO:0004332,GO:0004332,0.7015,0.7015,0.7015,0.7015,0.7015,5,0.7015,0.2154,no
ALF1_TOXGO,Q8I8I2,ProtTale,Eukaryota,363,"Plays a key role in glycolysis by catalyzing the cleavage of fructose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. Forms a bridge between cell surface adhesins and the actin cytoskeleton. Required for parasite invasion of host cells.","Catalyzes the isomerization of 5-deoxy-alpha-D-xylulose-5- phosphate (DXP) to xylulose 5-phosphate (XylP), the first committed step in xylulose 5- phosphate biosynthesis.",No,No,No,No,No,not-Yes,GO:0003779; GO:0004332,GO:0016853,GO:0016853,GO:0016853,GO:0016853,GO:0016853,0.2971,0.2971,0.2971,0.2971,0.2971,5,0.2971,0.2154,no
ALF1_TOXGO,Q8I8I2,Protein2Text,Eukaryota,363,"Plays a key role in glycolysis by catalyzing the cleavage of fructose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. Forms a bridge between cell surface adhesins and the actin cytoskeleton. Required for parasite invasion of host cells.","This protein is a fructose-bisphosphate aldolase, which means it catalyzes the reversible aldol condensation reaction between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP).",Yes,Yes,Yes,Yes,Yes,Yes,GO:0003779; GO:0004332,GO:0004332,GO:0004332,GO:0004332,GO:0004332,GO:0004332,0.7015,0.7015,0.7015,0.7015,0.7015,5,0.7015,0.2154,no
ALF1_TOXGO,Q8I8I2,Reference,Eukaryota,363,"Plays a key role in glycolysis by catalyzing the cleavage of fructose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. Forms a bridge between cell surface adhesins and the actin cytoskeleton. Required for parasite invasion of host cells.","Plays a key role in glycolysis by catalyzing the cleavage of fructose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. Forms a bridge between cell surface adhesins and the actin cytoskeleton. Required for parasite invasion of host cells.",,,,,,,GO:0003779; GO:0004332,GO:0004332,GO:0004332,GO:0004332,GO:0004332,GO:0004332,0.7015,0.7015,0.7015,0.7015,0.7015,5,0.7015,0.2154,no
DRP2_PLAF7,Q8IJ32,ESM2Text,Eukaryota,709,Essential for schizont-stage development. Required for mitochondrial development and fission. Required for apicoplast fission. Required for individualization of the schizont mass and formation of merozoites.,Interferon-induced dynamin-like GTPase with antiviral activity.,No,Maybe,Maybe,Maybe,No,not-Yes,GO:0005525; GO:0003924; GO:0008017,GO:0003924,GO:0003924,GO:0003924,GO:0003924,GO:0003924,0.5284,0.5284,0.5284,0.5284,0.5284,5,0.5284,0.6066,yes
DRP2_PLAF7,Q8IJ32,Prot2Text,Eukaryota,709,Essential for schizont-stage development. Required for mitochondrial development and fission. Required for apicoplast fission. Required for individualization of the schizont mass and formation of merozoites.,Microtubule-associated force-producing protein that is targeted to the forming cell plate during cytokinesis. May be involved in attaching Golgi-derived vesicles to microtubules which direct vesicles to the forming cell plate during cytokinesis. Possesses intrinsic GTPase activity in vitro.,No,Maybe,No,No,No,not-Yes,GO:0005525; GO:0003924; GO:0008017,GO:0003924,GO:0003924,GO:0003924; GO:0003777,GO:0003924,GO:0003924; GO:0003777,0.5284,0.5284,0.4658,0.5284,0.4658,5,0.5034,0.6066,yes
DRP2_PLAF7,Q8IJ32,ProtT3,Eukaryota,709,Essential for schizont-stage development. Required for mitochondrial development and fission. Required for apicoplast fission. Required for individualization of the schizont mass and formation of merozoites.,Cytoplasm. Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005525; GO:0003924; GO:0008017,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924,0.825,0.825,0.825,0.825,0.5284,5,0.7657,0.6066,yes
DRP2_PLAF7,Q8IJ32,ProtTale,Eukaryota,709,Essential for schizont-stage development. Required for mitochondrial development and fission. Required for apicoplast fission. Required for individualization of the schizont mass and formation of merozoites.,Microtubule-associated force-producing protein that plays a role in cell division.,Vague,Vague,Vague,Vague,No,not-Yes,GO:0005525; GO:0003924; GO:0008017,,,GO:0003777,GO:0003777,,,,0.1212,0.1212,,2,0.1212,0.6066,yes
DRP2_PLAF7,Q8IJ32,Protein2Text,Eukaryota,709,Essential for schizont-stage development. Required for mitochondrial development and fission. Required for apicoplast fission. Required for individualization of the schizont mass and formation of merozoites.,"The molecular function of this protein is not specified in the provided information. However, based on its name, it is likely involved in the regulation of cellular processes related to vesicle trafficking and transport. The protein is a part of the dynamin family, which is known to play a crucial role in the formation and scission of vesicles from the plasma membrane. Specifically, it is involved in the regulation of clathrin-mediated endocytosis, which is a process by which cells internalize molecules and proteins from the extracellular environment.

In more detail, this protein is likely involved in the following molecular functions:

1. GTPase activity: This protein is a GTPase, which means it hydrolyzes GTP to GDP, releasing energy that is used to drive conformational changes in the protein.
2. Membrane binding: This protein binds to membranes, allowing it to interact with other proteins and lipids in the membrane.
3. Vesicle scission: This protein is involved in the scission of vesicles from the plasma membrane, which is a critical step in endocytosis.
4. Regulation of vesicle trafficking: This protein is involved in the regulation of vesicle trafficking, which is the movement of vesicles within the cell.

Overall, the molecular function of this protein is likely related to its role in regulating vesicle trafficking and transport in cells.",No,Maybe,Vague,Vague,Vague,not-Yes,GO:0005525; GO:0003924; GO:0008017,GO:0003924; GO:0005525,GO:0003924,GO:0003924,GO:0003924,GO:0003924,0.825,0.5284,0.5284,0.5284,0.5284,5,0.5877,0.6066,yes
DRP2_PLAF7,Q8IJ32,Reference,Eukaryota,709,Essential for schizont-stage development. Required for mitochondrial development and fission. Required for apicoplast fission. Required for individualization of the schizont mass and formation of merozoites.,Essential for schizont-stage development. Required for mitochondrial development and fission. Required for apicoplast fission. Required for individualization of the schizont mass and formation of merozoites.,,,,,,,GO:0005525; GO:0003924; GO:0008017,,,,,,,,,,,0,,0.6066,yes
EIK1_PLAF7,Q8IL26,ESM2Text,Eukaryota,1558,"In blood stage parasites, phosphorylates translation factor eIF2alpha in response to amino acid starvation. During the asexual blood stage, involved in the response to the host hormone melatonin which is used by the parasite to modulate its cell cycle.",Is essential for spore formation. Phosphorylates srk1. Phosphorylates srk1 at 'Ser-52'.,Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0003824; GO:0004672; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004672,GO:0004674,GO:0004672,GO:0004674,0.8716,0.7127,0.6925,0.7127,0.6925,5,0.7364,0.6114,yes
EIK1_PLAF7,Q8IL26,Prot2Text,Eukaryota,1558,"In blood stage parasites, phosphorylates translation factor eIF2alpha in response to amino acid starvation. During the asexual blood stage, involved in the response to the host hormone melatonin which is used by the parasite to modulate its cell cycle.",Protein kinase which is essential for spore formation.,Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0003824; GO:0004672; GO:0106310; GO:0004674,GO:0004674,GO:0004672; GO:0004674,GO:0004672,GO:0004672,GO:0004674; GO:0005524,0.6925,0.7664,0.7127,0.7127,0.8716,5,0.7512,0.6114,yes
EIK1_PLAF7,Q8IL26,ProtT3,Eukaryota,1558,"In blood stage parasites, phosphorylates translation factor eIF2alpha in response to amino acid starvation. During the asexual blood stage, involved in the response to the host hormone melatonin which is used by the parasite to modulate its cell cycle.",Belongs to the protein kinase superfamily. Ser/Thr protein kinase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0003824; GO:0004672; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.8716,0.8716,0.8716,0.8716,0.8716,5,0.8716,0.6114,yes
EIK1_PLAF7,Q8IL26,ProtTale,Eukaryota,1558,"In blood stage parasites, phosphorylates translation factor eIF2alpha in response to amino acid starvation. During the asexual blood stage, involved in the response to the host hormone melatonin which is used by the parasite to modulate its cell cycle.",Serine/threonine protein kinase which is a key regulator of cell cycle progression. Required for cell cycle progression in both the mitotic and the G1 phases.,Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0003824; GO:0004672; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.8716,0.8716,0.6925,0.8716,0.8716,5,0.8358,0.6114,yes
EIK1_PLAF7,Q8IL26,Protein2Text,Eukaryota,1558,"In blood stage parasites, phosphorylates translation factor eIF2alpha in response to amino acid starvation. During the asexual blood stage, involved in the response to the host hormone melatonin which is used by the parasite to modulate its cell cycle.","Based on the name of the protein, it is likely that it is a calcium-binding protein.",No,No,No,No,No,not-Yes,GO:0005524; GO:0003824; GO:0004672; GO:0106310; GO:0004674,GO:0005509,GO:0005509,GO:0005509,GO:0005509,GO:0005509,0.1528,0.1528,0.1528,0.1528,0.1528,5,0.1528,0.6114,yes
EIK1_PLAF7,Q8IL26,Reference,Eukaryota,1558,"In blood stage parasites, phosphorylates translation factor eIF2alpha in response to amino acid starvation. During the asexual blood stage, involved in the response to the host hormone melatonin which is used by the parasite to modulate its cell cycle.","In blood stage parasites, phosphorylates translation factor eIF2alpha in response to amino acid starvation. During the asexual blood stage, involved in the response to the host hormone melatonin which is used by the parasite to modulate its cell cycle.",,,,,,,GO:0005524; GO:0003824; GO:0004672; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004694,GO:0004694; GO:0004674,GO:0004694,GO:0004694; GO:0004674,0.8716,0.6336,0.7235,0.6336,0.7235,5,0.7172,0.6114,yes
PREX_PLAF7,Q8ILY1,ESM2Text,Eukaryota,2016,"Probable apicoplast DNA replication factor. Functions as a multi-domain protein with DNA primase, DNA helicase, DNA polymerase and 3'-5' exonuclease activities. Polymerase exhibits a biased mutational spectrum in which T->C is the most frequent single-base substitution. Can efficiently incorporate 8-oxo-dGTP opposite dA template and continue replication past the mismatch. Possesses proofreading activity; can remove 8-oxo- dGMP misincorporated opposite the dA template. Can bypass oxidative stress-induced DNA lesions, such as 2-hydroxydeoxyadenine, thymine glycol and 8-oxodeoxyguanine, with a tendency to insert the correct nucleotide opposite the 2- hydroxydeoxyadenine and thymine glycol, to insert dCTP and dATP with nearly equal efficiencies opposite 8-oxodeoxyguanine and to incorporate dATP opposite an abasic site.",Required for efficient DNA transformation; probably involved in transformation.,Vague,Vague,Vague,Vague,No,not-Yes,GO:0008408; GO:0043139; GO:0005524; GO:0003678; GO:0003887; GO:0003697,,,,,,,,,,,0,,0.5462,yes
PREX_PLAF7,Q8ILY1,Prot2Text,Eukaryota,2016,"Probable apicoplast DNA replication factor. Functions as a multi-domain protein with DNA primase, DNA helicase, DNA polymerase and 3'-5' exonuclease activities. Polymerase exhibits a biased mutational spectrum in which T->C is the most frequent single-base substitution. Can efficiently incorporate 8-oxo-dGTP opposite dA template and continue replication past the mismatch. Possesses proofreading activity; can remove 8-oxo- dGMP misincorporated opposite the dA template. Can bypass oxidative stress-induced DNA lesions, such as 2-hydroxydeoxyadenine, thymine glycol and 8-oxodeoxyguanine, with a tendency to insert the correct nucleotide opposite the 2- hydroxydeoxyadenine and thymine glycol, to insert dCTP and dATP with nearly equal efficiencies opposite 8-oxodeoxyguanine and to incorporate dATP opposite an abasic site.",Has a role in meiotic recombination.,No,No,Vague,Vague,No,not-Yes,GO:0008408; GO:0043139; GO:0005524; GO:0003678; GO:0003887; GO:0003697,,,,,,,,,,,0,,0.5462,yes
PREX_PLAF7,Q8ILY1,ProtT3,Eukaryota,2016,"Probable apicoplast DNA replication factor. Functions as a multi-domain protein with DNA primase, DNA helicase, DNA polymerase and 3'-5' exonuclease activities. Polymerase exhibits a biased mutational spectrum in which T->C is the most frequent single-base substitution. Can efficiently incorporate 8-oxo-dGTP opposite dA template and continue replication past the mismatch. Possesses proofreading activity; can remove 8-oxo- dGMP misincorporated opposite the dA template. Can bypass oxidative stress-induced DNA lesions, such as 2-hydroxydeoxyadenine, thymine glycol and 8-oxodeoxyguanine, with a tendency to insert the correct nucleotide opposite the 2- hydroxydeoxyadenine and thymine glycol, to insert dCTP and dATP with nearly equal efficiencies opposite 8-oxodeoxyguanine and to incorporate dATP opposite an abasic site.",Involved in the repair of DNA interstrand cross-links (ICL). Has a 5'-3' exonuclease activity. Nucleus. Belongs to the DNA2/NAM7 exonuclease family,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0008408; GO:0043139; GO:0005524; GO:0003678; GO:0003887; GO:0003697,GO:0008409,GO:0008409,GO:0008409,GO:0008409,GO:0008409,0.349,0.349,0.349,0.349,0.349,5,0.349,0.5462,yes
PREX_PLAF7,Q8ILY1,ProtTale,Eukaryota,2016,"Probable apicoplast DNA replication factor. Functions as a multi-domain protein with DNA primase, DNA helicase, DNA polymerase and 3'-5' exonuclease activities. Polymerase exhibits a biased mutational spectrum in which T->C is the most frequent single-base substitution. Can efficiently incorporate 8-oxo-dGTP opposite dA template and continue replication past the mismatch. Possesses proofreading activity; can remove 8-oxo- dGMP misincorporated opposite the dA template. Can bypass oxidative stress-induced DNA lesions, such as 2-hydroxydeoxyadenine, thymine glycol and 8-oxodeoxyguanine, with a tendency to insert the correct nucleotide opposite the 2- hydroxydeoxyadenine and thymine glycol, to insert dCTP and dATP with nearly equal efficiencies opposite 8-oxodeoxyguanine and to incorporate dATP opposite an abasic site.","DNA-dependent ATPase and 5'-3' exonuclease. Plays a critical role in viral DNA replication. Essential for the initiation of viral DNA replication. Acts as a DNA helicase that unwinds the double-stranded DNA (dsDNA) into single-stranded DNA (ssDNA). In addition, acts as a DNA polymerase that synthesizes DNA from its template. The DNA-binding domain binds to ssDNA. In addition, forms a complex with the viral replication protein A (RPA) and the host replication protein A2 (RPA2), thus forming the RPA-RPA",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0008408; GO:0043139; GO:0005524; GO:0003678; GO:0003887; GO:0003697,GO:0004386; GO:0003677; GO:0005524; GO:0004003,GO:0003678; GO:0004386; GO:0003887; GO:0005524,GO:0003678; GO:0003887; GO:0004527; GO:0005524,GO:0003678; GO:0003887; GO:0004527; GO:0005524,GO:0003678; GO:0003887; GO:0004527; GO:0005524,0.8073,0.8193,0.8862,0.8862,0.8862,5,0.857,0.5462,yes
PREX_PLAF7,Q8ILY1,Protein2Text,Eukaryota,2016,"Probable apicoplast DNA replication factor. Functions as a multi-domain protein with DNA primase, DNA helicase, DNA polymerase and 3'-5' exonuclease activities. Polymerase exhibits a biased mutational spectrum in which T->C is the most frequent single-base substitution. Can efficiently incorporate 8-oxo-dGTP opposite dA template and continue replication past the mismatch. Possesses proofreading activity; can remove 8-oxo- dGMP misincorporated opposite the dA template. Can bypass oxidative stress-induced DNA lesions, such as 2-hydroxydeoxyadenine, thymine glycol and 8-oxodeoxyguanine, with a tendency to insert the correct nucleotide opposite the 2- hydroxydeoxyadenine and thymine glycol, to insert dCTP and dATP with nearly equal efficiencies opposite 8-oxodeoxyguanine and to incorporate dATP opposite an abasic site.","This protein is a type of RNA helicase, which is involved in unwinding RNA duplexes. RNA helicases are a class of enzymes that play a crucial role in various biological processes, including transcription, translation, and RNA splicing. They use ATP hydrolysis to unwind RNA duplexes, which allows them to perform their functions. In this case, the protein is involved in unwinding RNA duplexes, which is essential for various cellular processes.",No,No,No,No,No,not-Yes,GO:0008408; GO:0043139; GO:0005524; GO:0003678; GO:0003887; GO:0003697,GO:0004386; GO:0003724,GO:0004386,GO:0003724,GO:0003724,GO:0003724; GO:0005524,0.4789,0.4545,0.3593,0.3593,0.5645,5,0.4433,0.5462,yes
PREX_PLAF7,Q8ILY1,Reference,Eukaryota,2016,"Probable apicoplast DNA replication factor. Functions as a multi-domain protein with DNA primase, DNA helicase, DNA polymerase and 3'-5' exonuclease activities. Polymerase exhibits a biased mutational spectrum in which T->C is the most frequent single-base substitution. Can efficiently incorporate 8-oxo-dGTP opposite dA template and continue replication past the mismatch. Possesses proofreading activity; can remove 8-oxo- dGMP misincorporated opposite the dA template. Can bypass oxidative stress-induced DNA lesions, such as 2-hydroxydeoxyadenine, thymine glycol and 8-oxodeoxyguanine, with a tendency to insert the correct nucleotide opposite the 2- hydroxydeoxyadenine and thymine glycol, to insert dCTP and dATP with nearly equal efficiencies opposite 8-oxodeoxyguanine and to incorporate dATP opposite an abasic site.","Probable apicoplast DNA replication factor. Functions as a multi-domain protein with DNA primase, DNA helicase, DNA polymerase and 3'-5' exonuclease activities. Polymerase exhibits a biased mutational spectrum in which T->C is the most frequent single-base substitution. Can efficiently incorporate 8-oxo-dGTP opposite dA template and continue replication past the mismatch. Possesses proofreading activity; can remove 8-oxo- dGMP misincorporated opposite the dA template. Can bypass oxidative stress-induced DNA lesions, such as 2-hydroxydeoxyadenine, thymine glycol and 8-oxodeoxyguanine, with a tendency to insert the correct nucleotide opposite the 2- hydroxydeoxyadenine and thymine glycol, to insert dCTP and dATP with nearly equal efficiencies opposite 8-oxodeoxyguanine and to incorporate dATP opposite an abasic site.",,,,,,,GO:0008408; GO:0043139; GO:0005524; GO:0003678; GO:0003887; GO:0003697,GO:0003896; GO:0003678; GO:0003887; GO:0008296,GO:0003896; GO:0003678; GO:0003887; GO:0008408,GO:0003896; GO:0003678; GO:0003887; GO:0008408,GO:0003896; GO:0003678; GO:0003887; GO:0008296,GO:0003896; GO:0003678; GO:0003887; GO:0008408,0.7238,0.7858,0.7858,0.7238,0.7858,5,0.761,0.5462,yes
RT4I1_DROME,Q8IPZ3,ESM2Text,Eukaryota,413,NAD(P)H oxidoreductase. Involved in the ubiquinone biosynthetic pathway.,Plays a role in valine and isoleucine homeostasis. Regulates 3-hydroxy-2-methylbutanal (HMB) endocytosis in mitochondria. Appears to be a potent inhibitor of apoptosis.,No,No,No,No,No,not-Yes,GO:0050136; GO:0008753; GO:0000166,,,,,,,,,,,0,,0.2013,no
RT4I1_DROME,Q8IPZ3,Prot2Text,Eukaryota,413,NAD(P)H oxidoreductase. Involved in the ubiquinone biosynthetic pathway.,"Plays a role in the regulation of retinal ganglion cell (RGC) neurite outgrowth, and hence in the development of the inner retina and optic nerve. Appears to be a potent inhibitor of regeneration following spinal cord injury.",No,No,No,No,No,not-Yes,GO:0050136; GO:0008753; GO:0000166,,,,,,,,,,,0,,0.2013,no
RT4I1_DROME,Q8IPZ3,ProtT3,Eukaryota,413,NAD(P)H oxidoreductase. Involved in the ubiquinone biosynthetic pathway.,Mitochondrion outer membrane; Single-pass membrane protein. Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0050136; GO:0008753; GO:0000166,GO:0004024; GO:0008270,GO:0016491; GO:0008270,GO:0016491; GO:0008270,GO:0016491; GO:0008270,GO:0016491,0.1804,0.4136,0.4136,0.4136,0.4077,5,0.3658,0.2013,no
RT4I1_DROME,Q8IPZ3,ProtTale,Eukaryota,413,NAD(P)H oxidoreductase. Involved in the ubiquinone biosynthetic pathway.,NAD(P)H oxidoreductase involved in the ubiquinone biosynthetic pathway. Required for the O-methyltransferase activity of COQ3. Able to catalyze the oxidoreduction of 3-methoxy-4-hydroxy-6-(all-trans-polyprenylphosphoryl)benzoate (MOBP) to 3-methoxy-4-hydroxy-6-(polyprenylphospho)benzoate (MOBPB) in the ubiquinone biosynthetic pathway.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0050136; GO:0008753; GO:0000166,GO:0016491; GO:0016655,GO:0016491; GO:0003824,GO:0016655,GO:0016491,GO:0016491,0.5475,0.4081,0.5501,0.4077,0.4077,5,0.4642,0.2013,no
RT4I1_DROME,Q8IPZ3,Protein2Text,Eukaryota,413,NAD(P)H oxidoreductase. Involved in the ubiquinone biosynthetic pathway.,"The molecular function of this protein is not specified in the provided text. However, it is mentioned that it is involved in the metabolism of the endocannabinoid 2-arachidonoylglycerol (2-AG), specifically in its biosynthesis. It is likely that this protein plays a role in the conversion of a precursor molecule into 2-AG.",No,No,No,No,No,not-Yes,GO:0050136; GO:0008753; GO:0000166,,,,,,,,,,,0,,0.2013,no
RT4I1_DROME,Q8IPZ3,Reference,Eukaryota,413,NAD(P)H oxidoreductase. Involved in the ubiquinone biosynthetic pathway.,NAD(P)H oxidoreductase. Involved in the ubiquinone biosynthetic pathway.,,,,,,,GO:0050136; GO:0008753; GO:0000166,GO:0003955,GO:0016655,GO:0016491,GO:0016491,GO:0003955,0.6229,0.5501,0.4077,0.4077,0.6229,5,0.5223,0.2013,no
KAD1_DROME,Q8IQG9,ESM2Text,Eukaryota,229,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Also displays broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004017; GO:0005524,GO:0004017; GO:0004550; GO:0005524,GO:0004017; GO:0004550,GO:0004017; GO:0004550,GO:0004017; GO:0004550,GO:0004017; GO:0004550,0.9453,0.6941,0.6941,0.6941,0.6941,5,0.7443,0.2542,no
KAD1_DROME,Q8IQG9,Prot2Text,Eukaryota,229,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004017; GO:0005524,GO:0004017,GO:0004017,GO:0004017,GO:0004017,GO:0004017; GO:0005524,0.6819,0.6819,0.6819,0.6819,1.0,5,0.7455,0.2542,no
KAD1_DROME,Q8IQG9,ProtT3,Eukaryota,229,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Cytoplasm. Belongs to the adenylate kinase family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004017; GO:0005524,GO:0004017; GO:0005524,GO:0004017; GO:0005524,GO:0004017; GO:0005524,GO:0004017; GO:0005524,GO:0004017; GO:0005524,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2542,no
KAD1_DROME,Q8IQG9,ProtTale,Eukaryota,229,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.,Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo purine and pyrimidine nucleotide biosynthesis.,Maybe,No,No,No,No,not-Yes,GO:0004017; GO:0005524,GO:0004550; GO:0005524,GO:0004798; GO:0005524,GO:0019201; GO:0005524,GO:0016301; GO:0005524,GO:0016301; GO:0005524,0.8632,0.8236,0.9511,0.8181,0.8181,5,0.8548,0.2542,no
KAD1_DROME,Q8IQG9,Protein2Text,Eukaryota,229,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.,"The molecular function of this protein is as a kinase enzyme, specifically a nucleotide kinase that catalyzes the phosphorylation of nucleotides. More specifically, it is involved in the phosphorylation of AMP to ADP and ATP to ADP.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004017; GO:0005524,GO:0016301,GO:0019201,GO:0019201,GO:0004017,GO:0004017,0.4452,0.6182,0.6182,0.6819,0.6819,5,0.6091,0.2542,no
KAD1_DROME,Q8IQG9,Reference,Eukaryota,229,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.,,,,,,,GO:0004017; GO:0005524,GO:0004017; GO:0005524,GO:0004017,GO:0004017,GO:0004017,GO:0004017,1.0,0.6819,0.6819,0.6819,0.6819,5,0.7455,0.2542,no
POLG_LJUV1,Q8JV21,ESM2Text,Viruses,2253,"[Capsid protein VP0]: Forms an icosahedral capsid of pseudo T=3 symmetry together with capsid proteins VP1 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. The attachment to the host cell receptor induces virion internalization predominantly through clathrin- mediated endocytosis. Binds packaging signals present in the viral RNA.",Involved in repair of photodamaged PSII.,No,No,No,No,No,not-Yes,GO:0005524; GO:0015267; GO:0004197; GO:0046872; GO:0017111; GO:0003723; GO:0003724; GO:0003968; GO:0005198,,,,,,,,,,,0,,0.4054,no
POLG_LJUV1,Q8JV21,Prot2Text,Viruses,2253,"[Capsid protein VP0]: Forms an icosahedral capsid of pseudo T=3 symmetry together with capsid proteins VP1 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. The attachment to the host cell receptor induces virion internalization predominantly through clathrin- mediated endocytosis. Binds packaging signals present in the viral RNA.",DNA polymerase II participates in chromosomal DNA replication.,No,No,No,No,No,not-Yes,GO:0005524; GO:0015267; GO:0004197; GO:0046872; GO:0017111; GO:0003723; GO:0003724; GO:0003968; GO:0005198,GO:0003887,GO:0003887,GO:0003887,GO:0003887,GO:0003887,0.196,0.196,0.196,0.196,0.196,5,0.196,0.4054,no
POLG_LJUV1,Q8JV21,ProtT3,Viruses,2253,"[Capsid protein VP0]: Forms an icosahedral capsid of pseudo T=3 symmetry together with capsid proteins VP1 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. The attachment to the host cell receptor induces virion internalization predominantly through clathrin- mediated endocytosis. Binds packaging signals present in the viral RNA.",Capsid protein. Host membrane; Single-pass membrane protein. Belongs to the potyviridae polyprotein family,Maybe,Yes,Yes,Yes,Vague,Yes,GO:0005524; GO:0015267; GO:0004197; GO:0046872; GO:0017111; GO:0003723; GO:0003724; GO:0003968; GO:0005198,,,GO:0005198,GO:0005198,GO:0005198,,,0.3469,0.3469,0.3469,3,0.3469,0.4054,no
POLG_LJUV1,Q8JV21,ProtTale,Viruses,2253,"[Capsid protein VP0]: Forms an icosahedral capsid of pseudo T=3 symmetry together with capsid proteins VP1 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. The attachment to the host cell receptor induces virion internalization predominantly through clathrin- mediated endocytosis. Binds packaging signals present in the viral RNA.","[Capsid protein VP0]: Forms an icosahedral capsid of pseudo T=3 symmetry together with capsid proteins VP1 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid proteins interact with host alpha-V/beta-3 integrin heterodimer to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Binds to sialic acid-containing receptors on the host cell surface.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0015267; GO:0004197; GO:0046872; GO:0017111; GO:0003723; GO:0003724; GO:0003968; GO:0005198,,,GO:0005198,,GO:0005198,,,0.3469,,0.3469,2,0.3469,0.4054,no
POLG_LJUV1,Q8JV21,Protein2Text,Viruses,2253,"[Capsid protein VP0]: Forms an icosahedral capsid of pseudo T=3 symmetry together with capsid proteins VP1 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. The attachment to the host cell receptor induces virion internalization predominantly through clathrin- mediated endocytosis. Binds packaging signals present in the viral RNA.","This protein is a structural protein, specifically a viral capsid protein. It is involved in forming the protein shell of the virus, which encloses the genetic material and provides protection and stability to the virus.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0015267; GO:0004197; GO:0046872; GO:0017111; GO:0003723; GO:0003724; GO:0003968; GO:0005198,GO:0005198,GO:0005198,GO:0005198,GO:0005198,GO:0005198,0.3469,0.3469,0.3469,0.3469,0.3469,5,0.3469,0.4054,no
POLG_LJUV1,Q8JV21,Reference,Viruses,2253,"[Capsid protein VP0]: Forms an icosahedral capsid of pseudo T=3 symmetry together with capsid proteins VP1 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. The attachment to the host cell receptor induces virion internalization predominantly through clathrin- mediated endocytosis. Binds packaging signals present in the viral RNA.","[Capsid protein VP0]: Forms an icosahedral capsid of pseudo T=3 symmetry together with capsid proteins VP1 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. The attachment to the host cell receptor induces virion internalization predominantly through clathrin- mediated endocytosis. Binds packaging signals present in the viral RNA.",,,,,,,GO:0005524; GO:0015267; GO:0004197; GO:0046872; GO:0017111; GO:0003723; GO:0003724; GO:0003968; GO:0005198,GO:0003723,GO:0003723,GO:0003723,GO:0003723,GO:0003723,0.3285,0.3285,0.3285,0.3285,0.3285,5,0.3285,0.4054,no
WBPP_PSEAI,Q8KN66,ESM2Text,Bacteria,341,Epimerase required for the biosynthesis of the B-band O antigen of serotype O6 lipopolysaccharide. Catalyzes the reversible epimerization of UDP-N-acetylglucosaminuronic acid (UDP- GlcNAcA) to UDP-N-acetylgalactosaminuronic acid (UDP-GalNAcA). Also catalyzes the reversible epimerization of UDP- N-acetylglucosamine (UDP-GlcNAc) to UDP-N-acetylgalactosamine (UDP- GalNAc). Has very low epimerase activity with UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).,Catalyzes the epimerization of UDP-N-acetylglucosamine to UDP-N-acetylgalactosamine. Has a marked preference for UDP-GlcNAc as sugar donor. UDP-GalNAc plays a critical role in the Leloir pathway of galactose catabolism in which galactose is converted to the sulfated form of N-acetylglucosamine-GalNAc.,Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0000166; GO:0003974,GO:0003974,GO:0016857,GO:0050378,GO:0050378,GO:0050378,0.7013,0.6117,0.5206,0.5206,0.5206,5,0.575,0.1937,no
WBPP_PSEAI,Q8KN66,Prot2Text,Bacteria,341,Epimerase required for the biosynthesis of the B-band O antigen of serotype O6 lipopolysaccharide. Catalyzes the reversible epimerization of UDP-N-acetylglucosaminuronic acid (UDP- GlcNAcA) to UDP-N-acetylgalactosaminuronic acid (UDP-GalNAcA). Also catalyzes the reversible epimerization of UDP- N-acetylglucosamine (UDP-GlcNAc) to UDP-N-acetylgalactosamine (UDP- GalNAc). Has very low epimerase activity with UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).,Catalyzes the epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N-acetylgalactosamine (UDP-GalNAc).,Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0000166; GO:0003974,GO:0050378,GO:0050378,GO:0050378,GO:0050378,GO:0016854,0.5206,0.5206,0.5206,0.5206,0.5325,5,0.523,0.1937,no
WBPP_PSEAI,Q8KN66,ProtT3,Bacteria,341,Epimerase required for the biosynthesis of the B-band O antigen of serotype O6 lipopolysaccharide. Catalyzes the reversible epimerization of UDP-N-acetylglucosaminuronic acid (UDP- GlcNAcA) to UDP-N-acetylgalactosaminuronic acid (UDP-GalNAcA). Also catalyzes the reversible epimerization of UDP- N-acetylglucosamine (UDP-GlcNAc) to UDP-N-acetylgalactosamine (UDP- GalNAc). Has very low epimerase activity with UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).,Involved in the metabolism of galactose. Catalyzes the conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through a mechanism involving the transient reduction of NAD (By similarity). Belongs to the NAD(P)-dependent epimerase/dehydratase family,Maybe,Maybe,Maybe,No,No,not-Yes,GO:0000166; GO:0003974,GO:0003978; GO:0050662,GO:0003978,GO:0003978; GO:0051287,GO:0003978; GO:0051287,GO:0003978,0.5206,0.5206,0.7301,0.7301,0.5206,5,0.6044,0.1937,no
WBPP_PSEAI,Q8KN66,ProtTale,Bacteria,341,Epimerase required for the biosynthesis of the B-band O antigen of serotype O6 lipopolysaccharide. Catalyzes the reversible epimerization of UDP-N-acetylglucosaminuronic acid (UDP- GlcNAcA) to UDP-N-acetylgalactosaminuronic acid (UDP-GalNAcA). Also catalyzes the reversible epimerization of UDP- N-acetylglucosamine (UDP-GlcNAc) to UDP-N-acetylgalactosamine (UDP- GalNAc). Has very low epimerase activity with UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).,Involved in the metabolism of galactose. Catalyzes the conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through a mechanism involving the transient reduction of NAD.,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0000166; GO:0003974,GO:0003978,GO:0003978,GO:0003978,GO:0003978,GO:0003978,0.5206,0.5206,0.5206,0.5206,0.5206,5,0.5206,0.1937,no
WBPP_PSEAI,Q8KN66,Protein2Text,Bacteria,341,Epimerase required for the biosynthesis of the B-band O antigen of serotype O6 lipopolysaccharide. Catalyzes the reversible epimerization of UDP-N-acetylglucosaminuronic acid (UDP- GlcNAcA) to UDP-N-acetylgalactosaminuronic acid (UDP-GalNAcA). Also catalyzes the reversible epimerization of UDP- N-acetylglucosamine (UDP-GlcNAc) to UDP-N-acetylgalactosamine (UDP- GalNAc). Has very low epimerase activity with UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).,"This protein is involved in the molecular function of transferring a sugar group, specifically through the breakdown of galactose-1-phosphate to produce UDP-galactose. It is also involved in the molecular function of reducing sugars, specifically through the breakdown of UDP-galactose to produce UDP-glucose. Additionally, this protein is involved in the molecular function of transferring a sugar group to a nucleotide, specifically through the breakdown of UDP-glucose to produce glucose-1-phosphate.",No,No,No,Vague,No,not-Yes,GO:0000166; GO:0003974,,GO:0004849,GO:0004849,,GO:0004849,,0.1278,0.1278,,0.1278,3,0.1278,0.1937,no
WBPP_PSEAI,Q8KN66,Reference,Bacteria,341,Epimerase required for the biosynthesis of the B-band O antigen of serotype O6 lipopolysaccharide. Catalyzes the reversible epimerization of UDP-N-acetylglucosaminuronic acid (UDP- GlcNAcA) to UDP-N-acetylgalactosaminuronic acid (UDP-GalNAcA). Also catalyzes the reversible epimerization of UDP- N-acetylglucosamine (UDP-GlcNAc) to UDP-N-acetylgalactosamine (UDP- GalNAc). Has very low epimerase activity with UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).,Epimerase required for the biosynthesis of the B-band O antigen of serotype O6 lipopolysaccharide. Catalyzes the reversible epimerization of UDP-N-acetylglucosaminuronic acid (UDP- GlcNAcA) to UDP-N-acetylgalactosaminuronic acid (UDP-GalNAcA). Also catalyzes the reversible epimerization of UDP- N-acetylglucosamine (UDP-GlcNAc) to UDP-N-acetylgalactosamine (UDP- GalNAc). Has very low epimerase activity with UDP-glucose (UDP-Glc) and UDP-galactose (UDP-Gal).,,,,,,,GO:0000166; GO:0003974,GO:0016854,GO:0050378,GO:0016857,GO:0050378,GO:0050378,0.5325,0.5206,0.6117,0.5206,0.5206,5,0.5412,0.1937,no
GDPD_CALS4,Q8RB32,ESM2Text,Bacteria,243,Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol. Can use glycerophosphocholine.,Glycerophosphoryl diester phosphodiesterase hydrolyzes deacylated phospholipids to G3P and the corresponding alcohols.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008889; GO:0046872,GO:0008441,GO:0008889,GO:0008889,GO:0008889,GO:0008889,0.3411,0.6924,0.6924,0.6924,0.6924,5,0.6221,0.3478,no
GDPD_CALS4,Q8RB32,Prot2Text,Bacteria,243,Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol. Can use glycerophosphocholine.,Glycerophosphoryl diester phosphodiesterase hydrolyzes deacylated phospholipids to G3P and the corresponding alcohols.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008889; GO:0046872,GO:0008889,GO:0008889,GO:0008441,GO:0008441,GO:0008441,0.6924,0.6924,0.3411,0.3411,0.3411,5,0.4816,0.3478,no
GDPD_CALS4,Q8RB32,ProtT3,Bacteria,243,Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol. Can use glycerophosphocholine.,"Catalyzes the phosphorylation of glycerol to 1,3-bisphosphoglycerate (1,3-BPG). Belongs to the glycerol-3-phosphate kinase family",No,No,No,No,No,not-Yes,GO:0008889; GO:0046872,GO:0016301; GO:0005524,GO:0004370; GO:0005524,GO:0004370; GO:0005524,GO:0004370; GO:0005524,GO:0004370; GO:0005524,0.2477,0.223,0.223,0.223,0.223,5,0.2279,0.3478,no
GDPD_CALS4,Q8RB32,ProtTale,Bacteria,243,Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol. Can use glycerophosphocholine.,Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008889; GO:0046872,GO:0008889,GO:0008441,GO:0008889,GO:0008889,GO:0008889,0.6924,0.3411,0.6924,0.6924,0.6924,5,0.6221,0.3478,no
GDPD_CALS4,Q8RB32,Protein2Text,Bacteria,243,Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol. Can use glycerophosphocholine.,"The molecular function of this protein is likely to be a transferase, as it is a member of the transferase family. More specifically, it is a kinase that phosphorylates the 4'-hydroxyl group of the ribose moiety of the nucleotide. However, the exact molecular function of this protein is not specified in the given information. 
Further research would be needed to determine the specific molecular function of this protein. 
This protein is a member of the family of phosphoribosyltransferases, which are enzymes that catalyze the transfer of a phosphate group from a donor molecule to a nucleotide. They are involved in a variety of cellular processes, including nucleotide synthesis and repair, and are often specific to certain types of nucleotides. 
In general, the molecular function of a protein can be determined by analyzing its sequence, structure, and biochemical properties, as well as by studying its interactions with other molecules and its role in cellular processes. 
If you have any further questions or would like more information, please let me know. 
However, if you have any further questions or would like more information, please let me know.",No,No,No,No,No,not-Yes,GO:0008889; GO:0046872,,,,,,,,,,,0,,0.3478,no
GDPD_CALS4,Q8RB32,Reference,Bacteria,243,Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol. Can use glycerophosphocholine.,Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol. Can use glycerophosphocholine.,,,,,,,GO:0008889; GO:0046872,GO:0008441,GO:0008441,GO:0008889,GO:0008441,GO:0008889,0.3411,0.3411,0.6924,0.3411,0.6924,5,0.4816,0.3478,no
KOC1_ARATH,Q8RWX4,ESM2Text,Eukaryota,611,"Serine/threonine protein kinase acting as a regulatory component of the plastid protein import machinery by phosphorylating import receptors (e.g. the A-domain of TOC159, TOC120 and TOC132). Supports preprotein import and contributes to efficient chloroplast biogenesis, thus being required for survival during de-etiolation.",Confers resistance to the novobiocin B and various benzalkonoid drugs.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004672; GO:0004674,,,,,,,,,,,0,,0.3662,no
KOC1_ARATH,Q8RWX4,Prot2Text,Eukaryota,611,"Serine/threonine protein kinase acting as a regulatory component of the plastid protein import machinery by phosphorylating import receptors (e.g. the A-domain of TOC159, TOC120 and TOC132). Supports preprotein import and contributes to efficient chloroplast biogenesis, thus being required for survival during de-etiolation.",Could be involved in the control of pollen germination and pollen tube polar growth. Phosphorylates 'Ser-319' of SEP3.,Maybe,Yes,Yes,Maybe,No,not-Yes,GO:0005524; GO:0004672; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674; GO:0005524,0.7413,0.7413,0.7413,0.7413,0.9822,5,0.7895,0.3662,no
KOC1_ARATH,Q8RWX4,ProtT3,Eukaryota,611,"Serine/threonine protein kinase acting as a regulatory component of the plastid protein import machinery by phosphorylating import receptors (e.g. the A-domain of TOC159, TOC120 and TOC132). Supports preprotein import and contributes to efficient chloroplast biogenesis, thus being required for survival during de-etiolation.",Membrane; Single-pass membrane protein. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0004672; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.9822,0.9822,0.9822,0.9822,0.9822,5,0.9822,0.3662,no
KOC1_ARATH,Q8RWX4,ProtTale,Eukaryota,611,"Serine/threonine protein kinase acting as a regulatory component of the plastid protein import machinery by phosphorylating import receptors (e.g. the A-domain of TOC159, TOC120 and TOC132). Supports preprotein import and contributes to efficient chloroplast biogenesis, thus being required for survival during de-etiolation.","Serine/threonine-protein kinase involved in the activation of MAP kinase kinases (MAPKKs, e.g. MKK4/MKK1 and MKK5/MKK2) which in turn activate MAP kinases (MAPKs, e.g. MPK3/MPK14 and MPK6/MPK12). Phosphorylates and activates MPK3/MPK14 and probably also MPK6/MPK12.",Maybe,Yes,Yes,Maybe,No,not-Yes,GO:0005524; GO:0004672; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0004709,GO:0004674; GO:0004709; GO:0005524,GO:0004674; GO:0005524,0.9822,0.9822,0.7749,0.9701,0.9822,5,0.9383,0.3662,no
KOC1_ARATH,Q8RWX4,Protein2Text,Eukaryota,611,"Serine/threonine protein kinase acting as a regulatory component of the plastid protein import machinery by phosphorylating import receptors (e.g. the A-domain of TOC159, TOC120 and TOC132). Supports preprotein import and contributes to efficient chloroplast biogenesis, thus being required for survival during de-etiolation.","The molecular function of this protein is a serine/threonine-protein kinase, specifically a cyclin-dependent kinase (CDK).",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0004672; GO:0004674,GO:0004693,GO:0004674; GO:0004693,GO:0004693,GO:0004693,GO:0004693,0.6311,0.7626,0.6311,0.6311,0.6311,5,0.6574,0.3662,no
KOC1_ARATH,Q8RWX4,Reference,Eukaryota,611,"Serine/threonine protein kinase acting as a regulatory component of the plastid protein import machinery by phosphorylating import receptors (e.g. the A-domain of TOC159, TOC120 and TOC132). Supports preprotein import and contributes to efficient chloroplast biogenesis, thus being required for survival during de-etiolation.","Serine/threonine protein kinase acting as a regulatory component of the plastid protein import machinery by phosphorylating import receptors (e.g. the A-domain of TOC159, TOC120 and TOC132). Supports preprotein import and contributes to efficient chloroplast biogenesis, thus being required for survival during de-etiolation.",,,,,,,GO:0005524; GO:0004672; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.9822,0.9822,0.9822,0.9822,0.9822,5,0.9822,0.3662,no
FANCL_DROME,Q8T913,ESM2Text,Eukaryota,381,"Ubiquitin ligase protein that mediates monoubiquitination of Fancd2. Ubiquitination of Fancd2 is stimulated by ionising radiation. Together with Fancd2, and probably FANCI, involved in DNA repair of damage caused by agents that induce interstrand cross-links but not agents that cause double strand breaks.","E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Essential for serine/threonine-protein phosphorylation and substrate specificity. May be involved in the control of cell growth and apoptosis. Mediates ubiquitination and degradation of Wnt signaling component CTNNB1. Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0061630; GO:0008270,GO:0061630,GO:0004842,GO:0061630,GO:0061630,GO:0061630,0.6848,0.5768,0.6848,0.6848,0.6848,5,0.6632,0.8292,yes
FANCL_DROME,Q8T913,Prot2Text,Eukaryota,381,"Ubiquitin ligase protein that mediates monoubiquitination of Fancd2. Ubiquitination of Fancd2 is stimulated by ionising radiation. Together with Fancd2, and probably FANCI, involved in DNA repair of damage caused by agents that induce interstrand cross-links but not agents that cause double strand breaks.",E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Essential for early embryonic development.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0061630; GO:0008270,GO:0004842,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.5768,0.6848,0.6848,0.6848,0.6848,5,0.6632,0.8292,yes
FANCL_DROME,Q8T913,ProtT3,Eukaryota,381,"Ubiquitin ligase protein that mediates monoubiquitination of Fancd2. Ubiquitination of Fancd2 is stimulated by ionising radiation. Together with Fancd2, and probably FANCI, involved in DNA repair of damage caused by agents that induce interstrand cross-links but not agents that cause double strand breaks.","E3 ubiquitin-protein ligase required for DNA double-strand break (DSB) repair by homologous recombination (HR) . Acts as a central component of the MRE11-RAD50-NBN (MRN complex) complex, a complex that plays an essential role in the cellular response to DNA damage . The MRN complex plays a key role in the cellular response to DNA double-strand breaks (DSBs)",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0061630; GO:0008270,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.6848,0.6848,0.6848,0.6848,0.6848,5,0.6848,0.8292,yes
FANCL_DROME,Q8T913,ProtTale,Eukaryota,381,"Ubiquitin ligase protein that mediates monoubiquitination of Fancd2. Ubiquitination of Fancd2 is stimulated by ionising radiation. Together with Fancd2, and probably FANCI, involved in DNA repair of damage caused by agents that induce interstrand cross-links but not agents that cause double strand breaks.",Probable E3 ubiquitin-protein ligase involved in the ubiquitination and subsequent proteasomal degradation of target proteins.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0061630; GO:0008270,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.6848,0.6848,0.6848,0.6848,0.6848,5,0.6848,0.8292,yes
FANCL_DROME,Q8T913,Protein2Text,Eukaryota,381,"Ubiquitin ligase protein that mediates monoubiquitination of Fancd2. Ubiquitination of Fancd2 is stimulated by ionising radiation. Together with Fancd2, and probably FANCI, involved in DNA repair of damage caused by agents that induce interstrand cross-links but not agents that cause double strand breaks.","The molecular function of this protein is not specified in the provided information. However, based on its name and the context in which it is mentioned, it is likely involved in the regulation of gene expression or DNA repair. Further research would be necessary to determine its specific molecular function.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0061630; GO:0008270,,,,,,,,,,,0,,0.8292,yes
FANCL_DROME,Q8T913,Reference,Eukaryota,381,"Ubiquitin ligase protein that mediates monoubiquitination of Fancd2. Ubiquitination of Fancd2 is stimulated by ionising radiation. Together with Fancd2, and probably FANCI, involved in DNA repair of damage caused by agents that induce interstrand cross-links but not agents that cause double strand breaks.","Ubiquitin ligase protein that mediates monoubiquitination of Fancd2. Ubiquitination of Fancd2 is stimulated by ionising radiation. Together with Fancd2, and probably FANCI, involved in DNA repair of damage caused by agents that induce interstrand cross-links but not agents that cause double strand breaks.",,,,,,,GO:0061630; GO:0008270,GO:0004842,GO:0061630,GO:0004842,GO:0004842,GO:0061630,0.5768,0.6848,0.5768,0.5768,0.6848,5,0.62,0.8292,yes
SPIR_SALTY,Q8ZPP5,ESM2Text,Bacteria,920,"Member of the two-component regulatory system SsrA/SsrB (SpiR/SsrB) that is required for intracellular proliferation and systemic dissemination within the host. When inside acidic Salmonella- containing vesicles (SCV) within host cells the SsrA sensor kinase autophosphorylates and the phosphoryl group is transferred to the response regulator SsrB; phosphorylated SsrB activates the expression of genes encoding virulence proteins, including pathogenicity island 2 (SPI2) and other horizontally acquired genes, and antagonizes the action of transcriptional repressor hns (H-NS).",Probably forms part of a two-component regulatory system YclK/YclJ. Phosphorylates YclJ.,Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0000155,GO:0000155,GO:0000155,GO:0000155,GO:0000155,GO:0000155,0.6842,0.6842,0.6842,0.6842,0.6842,5,0.6842,0.5516,yes
SPIR_SALTY,Q8ZPP5,Prot2Text,Bacteria,920,"Member of the two-component regulatory system SsrA/SsrB (SpiR/SsrB) that is required for intracellular proliferation and systemic dissemination within the host. When inside acidic Salmonella- containing vesicles (SCV) within host cells the SsrA sensor kinase autophosphorylates and the phosphoryl group is transferred to the response regulator SsrB; phosphorylated SsrB activates the expression of genes encoding virulence proteins, including pathogenicity island 2 (SPI2) and other horizontally acquired genes, and antagonizes the action of transcriptional repressor hns (H-NS).",Member of the two-component regulatory system DctB/DctD involved in the transport of C4-dicarboxylates. DctB functions as a membrane-associated protein kinase that phosphorylates DctD in response to environmental signals.,Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0005524; GO:0000155,GO:0000155,GO:0000155,GO:0000155; GO:0004672,GO:0000155,GO:0000155; GO:0005524,0.6842,0.6842,0.6938,0.6842,1.0,5,0.7493,0.5516,yes
SPIR_SALTY,Q8ZPP5,ProtT3,Bacteria,920,"Member of the two-component regulatory system SsrA/SsrB (SpiR/SsrB) that is required for intracellular proliferation and systemic dissemination within the host. When inside acidic Salmonella- containing vesicles (SCV) within host cells the SsrA sensor kinase autophosphorylates and the phosphoryl group is transferred to the response regulator SsrB; phosphorylated SsrB activates the expression of genes encoding virulence proteins, including pathogenicity island 2 (SPI2) and other horizontally acquired genes, and antagonizes the action of transcriptional repressor hns (H-NS).","Member of the two-component regulatory system PhoP/PhoQ involved in the regulation of the Pho regulon, which is involved in regulation of genes involved in phosphate uptake, metabolism, and virulence. Phosphorylated PhoQ binds to the promoter region of PhoP-regulated genes to activate or repress their expression. Cell inner membrane; Multi-pass membrane protein",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0000155,GO:0000155; GO:0005524,GO:0000155,GO:0000155,GO:0000155; GO:0005524,GO:0000155,1.0,0.6842,0.6842,1.0,0.6842,5,0.8105,0.5516,yes
SPIR_SALTY,Q8ZPP5,ProtTale,Bacteria,920,"Member of the two-component regulatory system SsrA/SsrB (SpiR/SsrB) that is required for intracellular proliferation and systemic dissemination within the host. When inside acidic Salmonella- containing vesicles (SCV) within host cells the SsrA sensor kinase autophosphorylates and the phosphoryl group is transferred to the response regulator SsrB; phosphorylated SsrB activates the expression of genes encoding virulence proteins, including pathogenicity island 2 (SPI2) and other horizontally acquired genes, and antagonizes the action of transcriptional repressor hns (H-NS).","Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Under conditions of nitrogen sufficiency, NtrB autophosphorylates and transfers the phosphoryl group to NtrC. In the presence of nitrogen, acts as a phosphatase that dephosphorylates NtrC, preventing induction of its target genes.",Maybe,Yes,Yes,Maybe,No,not-Yes,GO:0005524; GO:0000155,GO:0000155; GO:0016791,GO:0000155; GO:0004721,GO:0000155; GO:0004721; GO:0005524,GO:0000155; GO:0005524,GO:0000155; GO:0004721; GO:0005524,0.5497,0.5795,0.8512,1.0,0.8512,5,0.7663,0.5516,yes
SPIR_SALTY,Q8ZPP5,Protein2Text,Bacteria,920,"Member of the two-component regulatory system SsrA/SsrB (SpiR/SsrB) that is required for intracellular proliferation and systemic dissemination within the host. When inside acidic Salmonella- containing vesicles (SCV) within host cells the SsrA sensor kinase autophosphorylates and the phosphoryl group is transferred to the response regulator SsrB; phosphorylated SsrB activates the expression of genes encoding virulence proteins, including pathogenicity island 2 (SPI2) and other horizontally acquired genes, and antagonizes the action of transcriptional repressor hns (H-NS).","The molecular function of this protein is not specified in the provided text. However, based on the context, it is likely that this protein is involved in a process related to bacterial cell division or membrane function, given its classification as a protein related to ""bacterial cell division"".",Vague,Vague,Vague,Vague,No,not-Yes,GO:0005524; GO:0000155,,,,,,,,,,,0,,0.5516,yes
SPIR_SALTY,Q8ZPP5,Reference,Bacteria,920,"Member of the two-component regulatory system SsrA/SsrB (SpiR/SsrB) that is required for intracellular proliferation and systemic dissemination within the host. When inside acidic Salmonella- containing vesicles (SCV) within host cells the SsrA sensor kinase autophosphorylates and the phosphoryl group is transferred to the response regulator SsrB; phosphorylated SsrB activates the expression of genes encoding virulence proteins, including pathogenicity island 2 (SPI2) and other horizontally acquired genes, and antagonizes the action of transcriptional repressor hns (H-NS).","Member of the two-component regulatory system SsrA/SsrB (SpiR/SsrB) that is required for intracellular proliferation and systemic dissemination within the host. When inside acidic Salmonella- containing vesicles (SCV) within host cells the SsrA sensor kinase autophosphorylates and the phosphoryl group is transferred to the response regulator SsrB; phosphorylated SsrB activates the expression of genes encoding virulence proteins, including pathogenicity island 2 (SPI2) and other horizontally acquired genes, and antagonizes the action of transcriptional repressor hns (H-NS).",,,,,,,GO:0005524; GO:0000155,GO:0000155; GO:0005524,GO:0000155,GO:0000155; GO:0004673,GO:0000155; GO:0005524,GO:0000155,1.0,0.6842,0.7211,1.0,0.6842,5,0.8179,0.5516,yes
MARC3_CAEEL,Q93227,ESM2Text,Eukaryota,431,"E3 ubiquitin-protein ligase which positively regulates the fast polyspermy block during fertilization, preventing entry of more than one sperm into the oocyte. After fertilization, required in the zygote for the selective degradation of a subset of maternal membrane proteins including cav-1, chs-1 and rme-2, probably by mediating their K63-linked polyubiquitination.","E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated E2 ubiquitin-conjugating enzymes, such as UBC4 and UBC7, and transfers it to substrates promoting their degradation. Promotes ubiquitination and subsequent proteasomal degradation of TFDP, TFDP-NMD, FAS, CCDC47, FASG, CEP152, CEP63, CDC48, CDC53, RNF26, RPS6KA5, RPS7KA5, SIPC11A, SIPC12A, SGTA4, SGTA7, SGTA9, SGTA10, ATCC1, ATCC2, ATCC3, ATCC5, ATCC6, ATCC7, ATCC8, ATCC9, ATCC10, ATCC11, ATCC12 and CDC15.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0061630; GO:0004842; GO:0008270,GO:0061630,GO:0004842,GO:0061630,GO:0061630,GO:0061630,0.7214,0.7248,0.7214,0.7214,0.7214,5,0.7221,0.7933,yes
MARC3_CAEEL,Q93227,Prot2Text,Eukaryota,431,"E3 ubiquitin-protein ligase which positively regulates the fast polyspermy block during fertilization, preventing entry of more than one sperm into the oocyte. After fertilization, required in the zygote for the selective degradation of a subset of maternal membrane proteins including cav-1, chs-1 and rme-2, probably by mediating their K63-linked polyubiquitination.",E3 ubiquitin-protein ligase which may be involved in cell signaling pathway. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0061630; GO:0004842; GO:0008270,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.7214,0.7214,0.7214,0.7214,0.7214,5,0.7214,0.7933,yes
MARC3_CAEEL,Q93227,ProtT3,Eukaryota,431,"E3 ubiquitin-protein ligase which positively regulates the fast polyspermy block during fertilization, preventing entry of more than one sperm into the oocyte. After fertilization, required in the zygote for the selective degradation of a subset of maternal membrane proteins including cav-1, chs-1 and rme-2, probably by mediating their K63-linked polyubiquitination.",E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Membrane; Multi-pass membrane protein,Yes,Yes,Yes,Yes,Yes,Yes,GO:0061630; GO:0004842; GO:0008270,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.7214,0.7214,0.7214,0.7214,0.7214,5,0.7214,0.7933,yes
MARC3_CAEEL,Q93227,ProtTale,Eukaryota,431,"E3 ubiquitin-protein ligase which positively regulates the fast polyspermy block during fertilization, preventing entry of more than one sperm into the oocyte. After fertilization, required in the zygote for the selective degradation of a subset of maternal membrane proteins including cav-1, chs-1 and rme-2, probably by mediating their K63-linked polyubiquitination.","E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of E74 alpha/RNF43, a component of the PRC1 polycomb group (PcG) complex. Plays a role in the negative regulation of T-cell receptor (TCR)- mediated activation of NF-kappa-B.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0061630; GO:0004842; GO:0008270,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.7214,0.7214,0.7214,0.7214,0.7214,5,0.7214,0.7933,yes
MARC3_CAEEL,Q93227,Protein2Text,Eukaryota,431,"E3 ubiquitin-protein ligase which positively regulates the fast polyspermy block during fertilization, preventing entry of more than one sperm into the oocyte. After fertilization, required in the zygote for the selective degradation of a subset of maternal membrane proteins including cav-1, chs-1 and rme-2, probably by mediating their K63-linked polyubiquitination.",The molecular function of this protein is that it is involved in E3 ubiquitin ligase activity.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0061630; GO:0004842; GO:0008270,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.7214,0.7214,0.7214,0.7214,0.7214,5,0.7214,0.7933,yes
MARC3_CAEEL,Q93227,Reference,Eukaryota,431,"E3 ubiquitin-protein ligase which positively regulates the fast polyspermy block during fertilization, preventing entry of more than one sperm into the oocyte. After fertilization, required in the zygote for the selective degradation of a subset of maternal membrane proteins including cav-1, chs-1 and rme-2, probably by mediating their K63-linked polyubiquitination.","E3 ubiquitin-protein ligase which positively regulates the fast polyspermy block during fertilization, preventing entry of more than one sperm into the oocyte. After fertilization, required in the zygote for the selective degradation of a subset of maternal membrane proteins including cav-1, chs-1 and rme-2, probably by mediating their K63-linked polyubiquitination.",,,,,,,GO:0061630; GO:0004842; GO:0008270,GO:0004842,GO:0061630,GO:0004842,GO:0004842,GO:0061630,0.7248,0.7214,0.7248,0.7248,0.7214,5,0.7234,0.7933,yes
NDHL_PAENI,Q93NH5,ESM2Text,Bacteria,816,"Component of the nicotine 6-hydroxylase, which is involved in the degradation of nicotine. Catalyzes the hydroxylation of the pyridine ring at C6 to form 6-hydroxynicotine. Can use both L-nicotine and D- nicotine.",Converts 4-hydroxybenzoyl-CoA to benzoyl-CoA.,No,No,No,No,No,not-Yes,GO:0005506; GO:0018535,,,,,,,,,,,0,,0.3809,no
NDHL_PAENI,Q93NH5,Prot2Text,Bacteria,816,"Component of the nicotine 6-hydroxylase, which is involved in the degradation of nicotine. Catalyzes the hydroxylation of the pyridine ring at C6 to form 6-hydroxynicotine. Can use both L-nicotine and D- nicotine.",Oxidizes hypoxanthine and xanthine to uric acid.,No,No,No,No,No,not-Yes,GO:0005506; GO:0018535,GO:0004854,GO:0004855,GO:0004854,GO:0004855,GO:0004855,0.2886,0.2886,0.2886,0.2886,0.2886,5,0.2886,0.3809,no
NDHL_PAENI,Q93NH5,ProtT3,Bacteria,816,"Component of the nicotine 6-hydroxylase, which is involved in the degradation of nicotine. Catalyzes the hydroxylation of the pyridine ring at C6 to form 6-hydroxynicotine. Can use both L-nicotine and D- nicotine.",Belongs to the short-chain dehydrogenases/reductases (SDR) family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005506; GO:0018535,GO:0016491,GO:0016491,GO:0016491,GO:0016491; GO:0050662,GO:0016491,0.5027,0.5027,0.5027,0.5027,0.5027,5,0.5027,0.3809,no
NDHL_PAENI,Q93NH5,ProtTale,Bacteria,816,"Component of the nicotine 6-hydroxylase, which is involved in the degradation of nicotine. Catalyzes the hydroxylation of the pyridine ring at C6 to form 6-hydroxynicotine. Can use both L-nicotine and D- nicotine.",Catalyzes the oxidation of carbon monoxide to carbon dioxide.,No,No,No,No,No,not-Yes,GO:0005506; GO:0018535,GO:0016491,GO:0016491,GO:0018492,GO:0016491,GO:0016491,0.5027,0.5027,0.0,0.5027,0.5027,5,0.4022,0.3809,no
NDHL_PAENI,Q93NH5,Protein2Text,Bacteria,816,"Component of the nicotine 6-hydroxylase, which is involved in the degradation of nicotine. Catalyzes the hydroxylation of the pyridine ring at C6 to form 6-hydroxynicotine. Can use both L-nicotine and D- nicotine.","The molecular function of this protein is an aminotransferase, which is involved in the transfer of an amino group from an amino acid to a keto acid. In the case of this protein, it is involved in the breakdown of certain amino acids in the cell. Aminotransferases play a crucial role in the metabolism of amino acids and in the synthesis of various nitrogen-containing compounds.",No,No,No,No,No,not-Yes,GO:0005506; GO:0018535,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.2102,0.2102,0.2102,0.2102,0.2102,5,0.2102,0.3809,no
NDHL_PAENI,Q93NH5,Reference,Bacteria,816,"Component of the nicotine 6-hydroxylase, which is involved in the degradation of nicotine. Catalyzes the hydroxylation of the pyridine ring at C6 to form 6-hydroxynicotine. Can use both L-nicotine and D- nicotine.","Component of the nicotine 6-hydroxylase, which is involved in the degradation of nicotine. Catalyzes the hydroxylation of the pyridine ring at C6 to form 6-hydroxynicotine. Can use both L-nicotine and D- nicotine.",,,,,,,GO:0005506; GO:0018535,GO:0016705,GO:0004497,GO:0004497,GO:0004497,GO:0016705,0.4048,0.4048,0.4048,0.4048,0.4048,5,0.4048,0.3809,no
BHP_ARATH,Q93Z30,ESM2Text,Eukaryota,459,Serine/threonine protein kinase that phosphorylates proteins on serine and threonine residues. Mediates blue light- dependent stomatal opening in guard cells by promoting plasma membrane- type ATPases (AHA1 and AHA2) phosphorylation.,"Serine/threonine-protein kinase that acts as a positive regulator of brassinosteroid (BR) signaling. Involved in the regulation of cytokinesis. Phosphorylates BZR1, a transcription factor that regulates the expression of the antifungal peptide toxins at the surface of the endoplasmic reticulum. May phosphorylate the antifungal peptide toxins TACC5/ATCC5 and TACC6/BAK1. Phosphorylates ADK2G, a component of the cytoskeleton. Phosphorylates the transcription factor ATF4 in response to fungal infection.",Maybe,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0004672; GO:0004674; GO:0004712,GO:0004674; GO:0005524,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.9552,0.7571,0.7571,0.7571,0.7571,5,0.7967,0.6658,yes
BHP_ARATH,Q93Z30,Prot2Text,Eukaryota,459,Serine/threonine protein kinase that phosphorylates proteins on serine and threonine residues. Mediates blue light- dependent stomatal opening in guard cells by promoting plasma membrane- type ATPases (AHA1 and AHA2) phosphorylation.,"Serine/threonine-protein kinase involved in the control of proliferation, cell differentiation and cell cycle progression. Essential for nuclear proliferation in response to mitogenic signals and plays an essential role in the regulation of proliferation through control of E2F family members. Phosphorylates 'Ser-10' of histone H3 during mitosis. This induces chromatin condensation and conformation changes in the histone-like variant of E2F3, leading to target the E2F proteins for ubiquitination and subsequent proteasomal degradation. Phosphorylates the cyclin-dependent kinase CDK2 at 'Ser-10'.",Maybe,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0004672; GO:0004674; GO:0004712,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674; GO:0005524,0.7571,0.7571,0.7571,0.7571,0.9552,5,0.7967,0.6658,yes
BHP_ARATH,Q93Z30,ProtT3,Eukaryota,459,Serine/threonine protein kinase that phosphorylates proteins on serine and threonine residues. Mediates blue light- dependent stomatal opening in guard cells by promoting plasma membrane- type ATPases (AHA1 and AHA2) phosphorylation.,"Dual specificity protein kinase that acts as a receptor for TNFSF11/RANKL, TNFSF13/RANKL-like, TNFSF14/OPG, TNFSF15/OPG-like, TNFSF17/RANKL-like, TNFSF18/RANKL-like, TNFSF19/RANKL-like, TNFSF20/RANKL-like, TNFSF21/RANKL-like, TNFSF22/RANKL-like, TNFSF23/RANKL-like, TNFSF24/RANKL-like",Maybe,Maybe,Maybe,Maybe,Vague,not-Yes,GO:0005524; GO:0004672; GO:0004674; GO:0004712,GO:0004674; GO:0004713; GO:0005524,GO:0004674; GO:0004713; GO:0005524,GO:0004674; GO:0004713; GO:0005524,GO:0004674; GO:0004713; GO:0005524,GO:0004674; GO:0004713; GO:0005524,0.949,0.949,0.949,0.949,0.949,5,0.949,0.6658,yes
BHP_ARATH,Q93Z30,ProtTale,Eukaryota,459,Serine/threonine protein kinase that phosphorylates proteins on serine and threonine residues. Mediates blue light- dependent stomatal opening in guard cells by promoting plasma membrane- type ATPases (AHA1 and AHA2) phosphorylation.,Serine/threonine kinase that plays a role in the regulation of innate immunity. Mediates activation of NF-kappa-B in response to pathogen-associated molecular patterns (PAMPs). Mediates activation of p38 in response to PAMPs. Mediates activation of JNK in response to viral infection. Mediates activation of p38 in response to viral infection. Mediates activation of p38 in response to bacterial infection. Mediates activation of JNK in response to bacterial infection. Mediates activation of JNK in response to viral infection. Mediates activation of p38 in response to viral infection. Mediates activation of p38 in response to bacterial infection,Maybe,Yes,Yes,Yes,No,Yes,GO:0005524; GO:0004672; GO:0004674; GO:0004712,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.9552,0.9552,0.7571,0.9552,0.9552,5,0.9156,0.6658,yes
BHP_ARATH,Q93Z30,Protein2Text,Eukaryota,459,Serine/threonine protein kinase that phosphorylates proteins on serine and threonine residues. Mediates blue light- dependent stomatal opening in guard cells by promoting plasma membrane- type ATPases (AHA1 and AHA2) phosphorylation.,The molecular function of this protein is as a serine/threonine-protein kinase.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0004672; GO:0004674; GO:0004712,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.7571,0.7571,0.7571,0.7571,0.7571,5,0.7571,0.6658,yes
BHP_ARATH,Q93Z30,Reference,Eukaryota,459,Serine/threonine protein kinase that phosphorylates proteins on serine and threonine residues. Mediates blue light- dependent stomatal opening in guard cells by promoting plasma membrane- type ATPases (AHA1 and AHA2) phosphorylation.,Serine/threonine protein kinase that phosphorylates proteins on serine and threonine residues. Mediates blue light- dependent stomatal opening in guard cells by promoting plasma membrane- type ATPases (AHA1 and AHA2) phosphorylation.,,,,,,,GO:0005524; GO:0004672; GO:0004674; GO:0004712,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.9552,0.9552,0.9552,0.9552,0.9552,5,0.9552,0.6658,yes
APY_GLOMM,Q95P65,ESM2Text,Eukaryota,555,Facilitates hematophagy by inhibiting ADP-dependent platelet aggregation and promoting disaggregation of ADP-stimulated platelets in the host. Cleaves adenosine triphosphate (ATP) and adenosine diphosphate (ADP) to adenosine monophosphate (AMP) and inorganic phosphate. Interacts with fibrinogen receptor integrin alpha-IIb/beta-3 (ITGA2B/ITGB3).,Facilitates hematophagy by inhibiting ADP-dependent platelet aggregation in the host. Shows potential for antithrombotic activity.,Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008253; GO:0004050; GO:0005178; GO:0000287; GO:0030145; GO:0000166; GO:0090729,,,,,,,,,,,0,,0.3744,no
APY_GLOMM,Q95P65,Prot2Text,Eukaryota,555,Facilitates hematophagy by inhibiting ADP-dependent platelet aggregation and promoting disaggregation of ADP-stimulated platelets in the host. Cleaves adenosine triphosphate (ATP) and adenosine diphosphate (ADP) to adenosine monophosphate (AMP) and inorganic phosphate. Interacts with fibrinogen receptor integrin alpha-IIb/beta-3 (ITGA2B/ITGB3).,Facilitates hematophagy by inhibiting ADP-dependent platelet aggregation in the host. May reduce probing time by facilitating the speed of locating blood. Platelet aggregation was inhibited by 6% when 0.4 uM recombinant apyrase was added and by 9.5% when the concentration of recombinant apyrase was 0.8 uM.,Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008253; GO:0004050; GO:0005178; GO:0000287; GO:0030145; GO:0000166; GO:0090729,GO:0017110,GO:0004382,GO:0017110,GO:0017110,GO:0017110,0.2753,0.2427,0.2753,0.2753,0.2753,5,0.2688,0.3744,no
APY_GLOMM,Q95P65,ProtT3,Eukaryota,555,Facilitates hematophagy by inhibiting ADP-dependent platelet aggregation and promoting disaggregation of ADP-stimulated platelets in the host. Cleaves adenosine triphosphate (ATP) and adenosine diphosphate (ADP) to adenosine monophosphate (AMP) and inorganic phosphate. Interacts with fibrinogen receptor integrin alpha-IIb/beta-3 (ITGA2B/ITGB3).,Secreted. Belongs to the 5'-nucleotidase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008253; GO:0004050; GO:0005178; GO:0000287; GO:0030145; GO:0000166; GO:0090729,GO:0008253,GO:0008253,GO:0008253,GO:0008253,GO:0008253,0.3327,0.3327,0.3327,0.3327,0.3327,5,0.3327,0.3744,no
APY_GLOMM,Q95P65,ProtTale,Eukaryota,555,Facilitates hematophagy by inhibiting ADP-dependent platelet aggregation and promoting disaggregation of ADP-stimulated platelets in the host. Cleaves adenosine triphosphate (ATP) and adenosine diphosphate (ADP) to adenosine monophosphate (AMP) and inorganic phosphate. Interacts with fibrinogen receptor integrin alpha-IIb/beta-3 (ITGA2B/ITGB3).,Degrades inorganic phosphate (Pi) into two molecules of adenosine 5'-triphosphate (ATP).,No,No,No,No,No,not-Yes,GO:0008253; GO:0004050; GO:0005178; GO:0000287; GO:0030145; GO:0000166; GO:0090729,,,,,,,,,,,0,,0.3744,no
APY_GLOMM,Q95P65,Protein2Text,Eukaryota,555,Facilitates hematophagy by inhibiting ADP-dependent platelet aggregation and promoting disaggregation of ADP-stimulated platelets in the host. Cleaves adenosine triphosphate (ATP) and adenosine diphosphate (ADP) to adenosine monophosphate (AMP) and inorganic phosphate. Interacts with fibrinogen receptor integrin alpha-IIb/beta-3 (ITGA2B/ITGB3).,"The molecular function of this protein is a type of hydrolase, specifically a 5'-nucleotidase, which is an enzyme that catalyzes the hydrolysis of nucleotides at the 5' position.",Maybe,No,Maybe,Maybe,No,not-Yes,GO:0008253; GO:0004050; GO:0005178; GO:0000287; GO:0030145; GO:0000166; GO:0090729,GO:0008253,GO:0008253,GO:0008253,GO:0008253,GO:0008253,0.3327,0.3327,0.3327,0.3327,0.3327,5,0.3327,0.3744,no
APY_GLOMM,Q95P65,Reference,Eukaryota,555,Facilitates hematophagy by inhibiting ADP-dependent platelet aggregation and promoting disaggregation of ADP-stimulated platelets in the host. Cleaves adenosine triphosphate (ATP) and adenosine diphosphate (ADP) to adenosine monophosphate (AMP) and inorganic phosphate. Interacts with fibrinogen receptor integrin alpha-IIb/beta-3 (ITGA2B/ITGB3).,Facilitates hematophagy by inhibiting ADP-dependent platelet aggregation and promoting disaggregation of ADP-stimulated platelets in the host. Cleaves adenosine triphosphate (ATP) and adenosine diphosphate (ADP) to adenosine monophosphate (AMP) and inorganic phosphate. Interacts with fibrinogen receptor integrin alpha-IIb/beta-3 (ITGA2B/ITGB3).,,,,,,,GO:0008253; GO:0004050; GO:0005178; GO:0000287; GO:0030145; GO:0000166; GO:0090729,GO:0004382,GO:0004551,GO:0016887; GO:0017110,GO:0017110,GO:0017110,0.2427,0.2753,0.3205,0.2753,0.2753,5,0.2778,0.3744,no
PAT_SACS2,Q97V23,ESM2Text,Archaea,160,"Modulates activity of albA1, the major archaeal DNA compaction protein, by decreasing albA1's nucleic acid binding affinity through acetylation of 'Lys-16'.",Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and releases both CoA and the acetylated product. It prefers the antibiotic chloramphenicol.,Maybe,Maybe,Yes,Yes,Maybe,not-Yes,GO:0016747,GO:0008811,GO:0008811,GO:0008811,GO:0008811,GO:0008811,0.6227,0.6227,0.6227,0.6227,0.6227,5,0.6227,0.1861,no
PAT_SACS2,Q97V23,Prot2Text,Archaea,160,"Modulates activity of albA1, the major archaeal DNA compaction protein, by decreasing albA1's nucleic acid binding affinity through acetylation of 'Lys-16'.","Involved in the protection against polyamine toxicity by regulating their concentration. Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to the primary amino groups of spermidine, producing spermine and acetate. It can also use spermidine. In vitro, can also use N(8)-acetylspermidine and N(8)-acetylspermine as substrates, however it is unlikely that it acts as a diamine acetyltransferase in vivo.",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0016747,GO:0004145,GO:0004145,GO:0004145,GO:0004145,GO:0004145; GO:0008080,0.6227,0.6227,0.6227,0.6227,0.6606,5,0.6303,0.1861,no
PAT_SACS2,Q97V23,ProtT3,Archaea,160,"Modulates activity of albA1, the major archaeal DNA compaction protein, by decreasing albA1's nucleic acid binding affinity through acetylation of 'Lys-16'.",Catalyzes the transfer of an acetyl group from acetyl-CoA to the epsilon-amino group of N(2)-acetyl-L-ornithine to form N(2)-acetyl-L-citrulline. Cytoplasm. Belongs to the acetyltransferase family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016747,GO:0008080,GO:0016407,GO:0016407; GO:0008080,GO:0016407; GO:0008080,GO:0008080,0.6795,0.8582,0.7986,0.7986,0.6795,5,0.7629,0.1861,no
PAT_SACS2,Q97V23,ProtTale,Archaea,160,"Modulates activity of albA1, the major archaeal DNA compaction protein, by decreasing albA1's nucleic acid binding affinity through acetylation of 'Lys-16'.",Catalyzes the hydrolysis of N-(5'-phosphoribosyl)-ATP to form N-(5'-phosphoribosyl)-5'-AMP.,No,No,No,No,No,not-Yes,GO:0016747,GO:0016787,GO:0016787,GO:0004635,GO:0004635,GO:0004635,0.4071,0.4071,0.2067,0.2067,0.2067,5,0.2869,0.1861,no
PAT_SACS2,Q97V23,Protein2Text,Archaea,160,"Modulates activity of albA1, the major archaeal DNA compaction protein, by decreasing albA1's nucleic acid binding affinity through acetylation of 'Lys-16'.","The molecular function of this protein is not explicitly stated in the provided text, but based on the context, it is likely involved in the synthesis or modification of molecules. The protein is described as being involved in the phosphorylation of a specific amino acid, which suggests that it may have a role in modifying the structure of molecules. However, without more information, it is difficult to determine the specific molecular function of this protein. 

If you have more information about the protein, such as its name, UniProt ID, or a specific reference, I may be able to provide a more accurate answer.",Vague,Vague,No,Vague,No,not-Yes,GO:0016747,,,,,,,,,,,0,,0.1861,no
PAT_SACS2,Q97V23,Reference,Archaea,160,"Modulates activity of albA1, the major archaeal DNA compaction protein, by decreasing albA1's nucleic acid binding affinity through acetylation of 'Lys-16'.","Modulates activity of albA1, the major archaeal DNA compaction protein, by decreasing albA1's nucleic acid binding affinity through acetylation of 'Lys-16'.",,,,,,,GO:0016747,GO:0016407,GO:0004468,GO:0016407,GO:0016407,GO:0008080,0.8582,0.5777,0.8582,0.8582,0.6795,5,0.7664,0.1861,no
CBL_CHICK,Q98TY6,ESM2Text,Eukaryota,903,"E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Involved in regulation of apoptosis in duodenal epithelial cells.","E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. In complex with CBL, acts as an E3 ubiquitin-protein ligase promoting p53/TP53 degradation by recruiting and anchoring it at the E3:substrate complex. Also involved in JUN ubiquitination and degradation, promoting its degradation by the proteasome. Promotes ubiquitination and degradation of TNFRSF10/PARVB. May be involved in TNF-alpha-induced p53/TP53 degradation by recruiting and anchoring it at the E3:substrate complex. Also involved in TNF-alpha-induced p53/TP53 degradation by recruiting and anchoring it at the E3:substrate complex, thereby promoting its degradation by the proteasome. May be involved in TNF-alpha-induced p53/TP53 degradation by recruiting and anchoring it at the E3:substrate complex, thereby promoting its degradation by the proteasome. May be involved in the ubiquitination and proteasomal degradation of CKM1/CRM1, promoting",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005509; GO:0046875; GO:0016301; GO:0001784; GO:0017124; GO:0061630; GO:0008270,GO:0061630,GO:0004842,GO:0061630,GO:0061630,GO:0061630,0.3294,0.3048,0.3294,0.3294,0.3294,5,0.3245,0.7924,yes
CBL_CHICK,Q98TY6,Prot2Text,Eukaryota,903,"E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Involved in regulation of apoptosis in duodenal epithelial cells.","E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Regulates the formation of the post-synaptic polyglutamate network (PSN). Inhibits CDK5 activity and ubiquitinates CDKN1B.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005509; GO:0046875; GO:0016301; GO:0001784; GO:0017124; GO:0061630; GO:0008270,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.3294,0.3294,0.3294,0.3294,0.3294,5,0.3294,0.7924,yes
CBL_CHICK,Q98TY6,ProtT3,Eukaryota,903,"E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Involved in regulation of apoptosis in duodenal epithelial cells.","E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Acts as a negative regulator of the Toll-like receptor and IL-1 signaling pathway by mediating ubiquitination and subsequent proteasomal degradation of IRAK1, IRAK2 and IRAK4. Cytoplasm",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005509; GO:0046875; GO:0016301; GO:0001784; GO:0017124; GO:0061630; GO:0008270,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.3294,0.3294,0.3294,0.3294,0.3294,5,0.3294,0.7924,yes
CBL_CHICK,Q98TY6,ProtTale,Eukaryota,903,"E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Involved in regulation of apoptosis in duodenal epithelial cells.",Protein-protein E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in an ATP-dependent manner and is involved in protein degradation through ubiquitination and subsequent proteasomal degradation of target proteins. Plays a role in the negative regulation of the Ras/MAPK signaling pathway. Plays a role in Ras-induced apoptosis. Plays a role in the negative regulation of the Ras/MAPK signaling pathway. Plays a role in the negative regulation of the Ras/MAPK signaling pathway. Plays a role in the negative regulation of the Ras/MAPK signaling pathway. Plays a role in the negative regulation of the,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005509; GO:0046875; GO:0016301; GO:0001784; GO:0017124; GO:0061630; GO:0008270,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.3294,0.3294,0.3294,0.3294,0.3294,5,0.3294,0.7924,yes
CBL_CHICK,Q98TY6,Protein2Text,Eukaryota,903,"E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Involved in regulation of apoptosis in duodenal epithelial cells.","The molecular function of this protein is likely to be a receptor tyrosine kinase, specifically a non-receptor tyrosine kinase. It is involved in signaling pathways that regulate cell growth, differentiation, and survival.",No,No,No,No,No,not-Yes,GO:0005509; GO:0046875; GO:0016301; GO:0001784; GO:0017124; GO:0061630; GO:0008270,GO:0004713,GO:0004713,GO:0004713,GO:0004713,GO:0004713,0.2527,0.2527,0.2527,0.2527,0.2527,5,0.2527,0.7924,yes
CBL_CHICK,Q98TY6,Reference,Eukaryota,903,"E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Involved in regulation of apoptosis in duodenal epithelial cells.","E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Involved in regulation of apoptosis in duodenal epithelial cells.",,,,,,,GO:0005509; GO:0046875; GO:0016301; GO:0001784; GO:0017124; GO:0061630; GO:0008270,GO:0004842,GO:0061630,GO:0004842,GO:0004842,GO:0061630,0.3048,0.3294,0.3048,0.3048,0.3294,5,0.3146,0.7924,yes
AMDA_AGRTU,Q9AHE8,ESM2Text,Bacteria,517,"Hydrolase that can catalyze the degradation of ethyl carbamate (also called urethane), a probable human carcinogen widely found in alcoholic beverages. Can also use methyl carbamate, butyl carbamate, acetamide and urea. Also catalyzes the enantioselective hydrolysis of 2-phenylpropionamide, alpha-chlorophenylacetamide, 2- methyl-3-phenylpropionamide and alpha-methoxyphenylacetamide to the corresponding acids. Is inactive on benzamide and L- glutamine.","Specifically catalyzes the hydrolysis of some N,N'-diacetylchitobiose (unsaturated acetate, N,N'-diacetylmannate) into acetoacetate and acetate, the rate-limiting step in de novo fatty acid biosynthesis. Is able to further catalyze the hydrolysis of acetone and acetoacetate into acetoacetate and acetate, respectively. Is able to further catalyze the hydrolysis of some N,N'-diacetylchitobiose (AcCoA) into acetoacetate and acetate, the rate-limiting step in de novo fatty acid biosynthesis.",No,No,No,No,No,not-Yes,GO:0050387,,GO:0004553,,,,,0.3987,,,,1,0.3987,0.2658,no
AMDA_AGRTU,Q9AHE8,Prot2Text,Bacteria,517,"Hydrolase that can catalyze the degradation of ethyl carbamate (also called urethane), a probable human carcinogen widely found in alcoholic beverages. Can also use methyl carbamate, butyl carbamate, acetamide and urea. Also catalyzes the enantioselective hydrolysis of 2-phenylpropionamide, alpha-chlorophenylacetamide, 2- methyl-3-phenylpropionamide and alpha-methoxyphenylacetamide to the corresponding acids. Is inactive on benzamide and L- glutamine.","Hydrolyzes propionamides efficiently, and also at a lower efficiency, acetamide, acrylamide and indoleacetamide.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0050387,GO:0004040,GO:0004040,GO:0004040,GO:0004040,GO:0004040,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.2658,no
AMDA_AGRTU,Q9AHE8,ProtT3,Bacteria,517,"Hydrolase that can catalyze the degradation of ethyl carbamate (also called urethane), a probable human carcinogen widely found in alcoholic beverages. Can also use methyl carbamate, butyl carbamate, acetamide and urea. Also catalyzes the enantioselective hydrolysis of 2-phenylpropionamide, alpha-chlorophenylacetamide, 2- methyl-3-phenylpropionamide and alpha-methoxyphenylacetamide to the corresponding acids. Is inactive on benzamide and L- glutamine.",Belongs to the amidase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0050387,GO:0004040,GO:0004040,,GO:0004040,GO:0004040,0.7289,0.7289,,0.7289,0.7289,4,0.7289,0.2658,no
AMDA_AGRTU,Q9AHE8,ProtTale,Bacteria,517,"Hydrolase that can catalyze the degradation of ethyl carbamate (also called urethane), a probable human carcinogen widely found in alcoholic beverages. Can also use methyl carbamate, butyl carbamate, acetamide and urea. Also catalyzes the enantioselective hydrolysis of 2-phenylpropionamide, alpha-chlorophenylacetamide, 2- methyl-3-phenylpropionamide and alpha-methoxyphenylacetamide to the corresponding acids. Is inactive on benzamide and L- glutamine.",Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln).,No,No,No,No,No,not-Yes,GO:0050387,GO:0050567,GO:0050567; GO:0005524,GO:0050567,GO:0050567,GO:0050567,0.158,0.1239,0.158,0.158,0.158,5,0.1512,0.2658,no
AMDA_AGRTU,Q9AHE8,Protein2Text,Bacteria,517,"Hydrolase that can catalyze the degradation of ethyl carbamate (also called urethane), a probable human carcinogen widely found in alcoholic beverages. Can also use methyl carbamate, butyl carbamate, acetamide and urea. Also catalyzes the enantioselective hydrolysis of 2-phenylpropionamide, alpha-chlorophenylacetamide, 2- methyl-3-phenylpropionamide and alpha-methoxyphenylacetamide to the corresponding acids. Is inactive on benzamide and L- glutamine.",This protein is involved in the molecular function of ester hydrolase activity.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0050387,GO:0016788,GO:0016788,GO:0016788,GO:0016788,GO:0016788,0.482,0.482,0.482,0.482,0.482,5,0.482,0.2658,no
AMDA_AGRTU,Q9AHE8,Reference,Bacteria,517,"Hydrolase that can catalyze the degradation of ethyl carbamate (also called urethane), a probable human carcinogen widely found in alcoholic beverages. Can also use methyl carbamate, butyl carbamate, acetamide and urea. Also catalyzes the enantioselective hydrolysis of 2-phenylpropionamide, alpha-chlorophenylacetamide, 2- methyl-3-phenylpropionamide and alpha-methoxyphenylacetamide to the corresponding acids. Is inactive on benzamide and L- glutamine.","Hydrolase that can catalyze the degradation of ethyl carbamate (also called urethane), a probable human carcinogen widely found in alcoholic beverages. Can also use methyl carbamate, butyl carbamate, acetamide and urea. Also catalyzes the enantioselective hydrolysis of 2-phenylpropionamide, alpha-chlorophenylacetamide, 2- methyl-3-phenylpropionamide and alpha-methoxyphenylacetamide to the corresponding acids. Is inactive on benzamide and L- glutamine.",,,,,,,GO:0050387,GO:0016810,GO:0004040,GO:0016787; GO:0004040,GO:0004040,GO:0016811,0.729,0.7289,0.6866,0.7289,0.8582,5,0.7463,0.2658,no
OMA1_ARATH,Q9FLI5,ESM2Text,Eukaryota,485,"Protease that is part of the quality control system in the inner membrane of mitochondria. Metalloendopeptidase that modulates the oxidative phosphorylation (OXPHOS) system and plant growth. Involved in tolerance mechanisms to heat, osmotic and oxidative stresses.","Protease that is part of the quality control system in the inner membrane of mitochondria. Cleaves A1, A2 and A3 intermediates of the A-site tRNA precursor produced by RMD1/Boch_40, producing a short linear amidated product. Promotes the generation of a stable complex in the inner membrane of mitochondria by recruiting components of the phospholipase A2 complex.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0004222; GO:0008233,,GO:0008233,,GO:0008233,,,0.704,,0.704,,2,0.704,0.3463,no
OMA1_ARATH,Q9FLI5,Prot2Text,Eukaryota,485,"Protease that is part of the quality control system in the inner membrane of mitochondria. Metalloendopeptidase that modulates the oxidative phosphorylation (OXPHOS) system and plant growth. Involved in tolerance mechanisms to heat, osmotic and oxidative stresses.",Protease that is part of the quality control system in the inner membrane of mitochondria. Required to prevent the misfolding and the accumulation of misfolded proteins in the ER. Required to direct preproteins in the inner membrane and direct them to the channels that are responsible for mitochondrial protein import. Required to ensure the sterol-induced turnover of mistranslated or misfolded membrane proteins.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0004222; GO:0008233,GO:0008233,,GO:0008233,GO:0008233,GO:0008233,0.704,,0.704,0.704,0.704,4,0.704,0.3463,no
OMA1_ARATH,Q9FLI5,ProtT3,Eukaryota,485,"Protease that is part of the quality control system in the inner membrane of mitochondria. Metalloendopeptidase that modulates the oxidative phosphorylation (OXPHOS) system and plant growth. Involved in tolerance mechanisms to heat, osmotic and oxidative stresses.",Metalloprotease involved in the degradation of mitochondrial proteins. Mitochondrion inner membrane; Multi-pass membrane protein. Belongs to the peptidase M48B family,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0046872; GO:0004222; GO:0008233,GO:0004222; GO:0046872,GO:0004222,GO:0004222; GO:0046872,GO:0004222; GO:0046872,GO:0004222,0.9406,0.6946,0.9406,0.9406,0.6946,5,0.8422,0.3463,no
OMA1_ARATH,Q9FLI5,ProtTale,Eukaryota,485,"Protease that is part of the quality control system in the inner membrane of mitochondria. Metalloendopeptidase that modulates the oxidative phosphorylation (OXPHOS) system and plant growth. Involved in tolerance mechanisms to heat, osmotic and oxidative stresses.","Metalloprotease of the mitochondrial inner membrane that regulates the maturation and activity of the respiratory chain complex III (CIII), also known as cytochrome c oxidase. Catalyzes the cleavage of the peptide bond between position 152 and 153 in the hydrophobic transit peptide of CIII subunits COX2, COX3 and COX4I. This step is essential for the proper folding and assembly of CIII and prevents the premature formation of non-functional CIII. Also cleaves the peptide bond between position 152 and 153 in the hydrophobic transit peptide of CII, COX2 subunit",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0046872; GO:0004222; GO:0008233,GO:0004222,GO:0004222,GO:0004222,GO:0004222,GO:0004222,0.6946,0.6946,0.6946,0.6946,0.6946,5,0.6946,0.3463,no
OMA1_ARATH,Q9FLI5,Protein2Text,Eukaryota,485,"Protease that is part of the quality control system in the inner membrane of mitochondria. Metalloendopeptidase that modulates the oxidative phosphorylation (OXPHOS) system and plant growth. Involved in tolerance mechanisms to heat, osmotic and oxidative stresses.",The molecular function of this protein is an ATPase.,Vague,Vague,Vague,No,Vague,not-Yes,GO:0046872; GO:0004222; GO:0008233,GO:0016887,GO:0016887,GO:0016887,GO:0016887,GO:0016887,0.253,0.253,0.253,0.253,0.253,5,0.253,0.3463,no
OMA1_ARATH,Q9FLI5,Reference,Eukaryota,485,"Protease that is part of the quality control system in the inner membrane of mitochondria. Metalloendopeptidase that modulates the oxidative phosphorylation (OXPHOS) system and plant growth. Involved in tolerance mechanisms to heat, osmotic and oxidative stresses.","Protease that is part of the quality control system in the inner membrane of mitochondria. Metalloendopeptidase that modulates the oxidative phosphorylation (OXPHOS) system and plant growth. Involved in tolerance mechanisms to heat, osmotic and oxidative stresses.",,,,,,,GO:0046872; GO:0004222; GO:0008233,GO:0004222,GO:0004222,GO:0004222,GO:0004222,GO:0004222,0.6946,0.6946,0.6946,0.6946,0.6946,5,0.6946,0.3463,no
AMALD_PSEAE,Q9HWJ2,ESM2Text,Bacteria,496,"NAD(+)-dependent aminoaldehyde dehydrogenase highly efficient with protonated aminoacetaldehyde (ACTAL) and 3-aminopropanaldehyde (APAL). Likely participates in a still uncharacterized metabolic pathway present in proteobacteria species, in which ACTAL might be an intermediate, yielding glycine. Highly prefers NAD(+) over NADP(+). Shows very poor activity with acetaldehyde, propanaldehyde, butanaldehyde, pentanaldehyde, dimethylaminoacetaldehyde, trimethylaminoacetaldehyde (betaine aldehyde), trimethylaminobutanaldehyde, short aliphatic hydroxyaldehydes such as 3-hydroxypropanaldehyde and 2-hydroxypropanaldehyde (lactaldehyde), and aromatic aldehydes.",Catalyzes the NADP(+) dependent oxidation of succinate semialdehyde to succinate.,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0004030; GO:0000166,GO:0009013,GO:0016620,GO:0009013,GO:0009014,GO:0009013,0.5206,0.6117,0.5206,0.1679,0.5206,5,0.4683,0.1864,no
AMALD_PSEAE,Q9HWJ2,Prot2Text,Bacteria,496,"NAD(+)-dependent aminoaldehyde dehydrogenase highly efficient with protonated aminoacetaldehyde (ACTAL) and 3-aminopropanaldehyde (APAL). Likely participates in a still uncharacterized metabolic pathway present in proteobacteria species, in which ACTAL might be an intermediate, yielding glycine. Highly prefers NAD(+) over NADP(+). Shows very poor activity with acetaldehyde, propanaldehyde, butanaldehyde, pentanaldehyde, dimethylaminoacetaldehyde, trimethylaminoacetaldehyde (betaine aldehyde), trimethylaminobutanaldehyde, short aliphatic hydroxyaldehydes such as 3-hydroxypropanaldehyde and 2-hydroxypropanaldehyde (lactaldehyde), and aromatic aldehydes.",Catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. Is involved in a degradation pathway of gamma-aminobutyrate (GABA) that allows A.brasilense to grow on GABA as a sole carbon source.,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0004030; GO:0000166,GO:0009013,GO:0009013,GO:0009013,GO:0009013,GO:0009013,0.5206,0.5206,0.5206,0.5206,0.5206,5,0.5206,0.1864,no
AMALD_PSEAE,Q9HWJ2,ProtT3,Bacteria,496,"NAD(+)-dependent aminoaldehyde dehydrogenase highly efficient with protonated aminoacetaldehyde (ACTAL) and 3-aminopropanaldehyde (APAL). Likely participates in a still uncharacterized metabolic pathway present in proteobacteria species, in which ACTAL might be an intermediate, yielding glycine. Highly prefers NAD(+) over NADP(+). Shows very poor activity with acetaldehyde, propanaldehyde, butanaldehyde, pentanaldehyde, dimethylaminoacetaldehyde, trimethylaminoacetaldehyde (betaine aldehyde), trimethylaminobutanaldehyde, short aliphatic hydroxyaldehydes such as 3-hydroxypropanaldehyde and 2-hydroxypropanaldehyde (lactaldehyde), and aromatic aldehydes.",Catalyzes the NAD(+)- and NADP(+)-dependent oxidation of (S)-2-hydroxyglutarate (2HG) to 2-oxoglutarate (2OG). Belongs to the aldehyde dehydrogenase family,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0004030; GO:0000166,GO:0016616,GO:0016616,GO:0016616,GO:0016616; GO:0051287,GO:0016616,0.3054,0.3054,0.3054,0.565,0.3054,5,0.3573,0.1864,no
AMALD_PSEAE,Q9HWJ2,ProtTale,Bacteria,496,"NAD(+)-dependent aminoaldehyde dehydrogenase highly efficient with protonated aminoacetaldehyde (ACTAL) and 3-aminopropanaldehyde (APAL). Likely participates in a still uncharacterized metabolic pathway present in proteobacteria species, in which ACTAL might be an intermediate, yielding glycine. Highly prefers NAD(+) over NADP(+). Shows very poor activity with acetaldehyde, propanaldehyde, butanaldehyde, pentanaldehyde, dimethylaminoacetaldehyde, trimethylaminoacetaldehyde (betaine aldehyde), trimethylaminobutanaldehyde, short aliphatic hydroxyaldehydes such as 3-hydroxypropanaldehyde and 2-hydroxypropanaldehyde (lactaldehyde), and aromatic aldehydes.",Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid.,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0004030; GO:0000166,GO:0008802,GO:0008802,GO:0008802,GO:0008802,GO:0008802,0.5419,0.5419,0.5419,0.5419,0.5419,5,0.5419,0.1864,no
AMALD_PSEAE,Q9HWJ2,Protein2Text,Bacteria,496,"NAD(+)-dependent aminoaldehyde dehydrogenase highly efficient with protonated aminoacetaldehyde (ACTAL) and 3-aminopropanaldehyde (APAL). Likely participates in a still uncharacterized metabolic pathway present in proteobacteria species, in which ACTAL might be an intermediate, yielding glycine. Highly prefers NAD(+) over NADP(+). Shows very poor activity with acetaldehyde, propanaldehyde, butanaldehyde, pentanaldehyde, dimethylaminoacetaldehyde, trimethylaminoacetaldehyde (betaine aldehyde), trimethylaminobutanaldehyde, short aliphatic hydroxyaldehydes such as 3-hydroxypropanaldehyde and 2-hydroxypropanaldehyde (lactaldehyde), and aromatic aldehydes.","The molecular function of this protein is an alcohol oxidase activity. It is involved in the conversion of an alcohol into an aldehyde and hydrogen peroxide. This protein is likely involved in the metabolism of alcohols. 
The protein is also likely involved in the conversion of methylglyoxal to D-lactate. Methylglyoxal is a highly reactive alpha-dicarbonyl compound that can damage proteins, DNA, and lipids. It is produced as a byproduct of glycolysis and can also be formed from the degradation of triosephosphates. The conversion of methylglyoxal to D-lactate is a key step in the detoxification of methylglyoxal in many organisms. 
The protein is also likely involved in the conversion of D-lactate to pyruvate. This reaction is a key step in the metabolism of D-lactate. D-lactate can be converted to pyruvate by several enzymes, but the most common pathway is through the action of lactate dehydrogenases. The conversion of D-lactate to pyruvate is an important step in the metabolism of lactate, which is a key intermediate in the metabolism of glucose. 
The protein is also likely involved in the conversion of 2,3-butanedione to 3-hydroxybutyrate. 2,3-Butanedione is a ketone body that is produced during the metabolism of fatty acids. It can be converted to 3-hydroxybutyrate by several enzymes, but the most common pathway is through the action of alcohol dehydrogenases. The conversion of 2,3-butanedione to 3-hydroxybutyrate is an important step in the metabolism of ketone bodies. 
The protein is also likely involved in the conversion of 3-hydroxybutyrate to acetoacetate. 3-Hydroxybutyrate is a ketone body that is produced during the metabolism of fatty acids. It can be converted to acetoacetate by several enzymes, but the most common pathway is through the action of alcohol dehydrogenases. The conversion of 3-hydroxybutyrate to acetoacetate is an important step in the metabolism of ketone bodies. 
The protein is also likely involved in the conversion of 3-hydroxybutyrate to acetoacetate. 3-Hydroxybutyrate is a ketone body that is",No,No,No,No,No,not-Yes,GO:0004030; GO:0000166,GO:0016614,GO:0004030,GO:0004030,GO:0004030,GO:0004030,0.3678,0.7013,0.7013,0.7013,0.7013,5,0.6346,0.1864,no
AMALD_PSEAE,Q9HWJ2,Reference,Bacteria,496,"NAD(+)-dependent aminoaldehyde dehydrogenase highly efficient with protonated aminoacetaldehyde (ACTAL) and 3-aminopropanaldehyde (APAL). Likely participates in a still uncharacterized metabolic pathway present in proteobacteria species, in which ACTAL might be an intermediate, yielding glycine. Highly prefers NAD(+) over NADP(+). Shows very poor activity with acetaldehyde, propanaldehyde, butanaldehyde, pentanaldehyde, dimethylaminoacetaldehyde, trimethylaminoacetaldehyde (betaine aldehyde), trimethylaminobutanaldehyde, short aliphatic hydroxyaldehydes such as 3-hydroxypropanaldehyde and 2-hydroxypropanaldehyde (lactaldehyde), and aromatic aldehydes.","NAD(+)-dependent aminoaldehyde dehydrogenase highly efficient with protonated aminoacetaldehyde (ACTAL) and 3-aminopropanaldehyde (APAL). Likely participates in a still uncharacterized metabolic pathway present in proteobacteria species, in which ACTAL might be an intermediate, yielding glycine. Highly prefers NAD(+) over NADP(+). Shows very poor activity with acetaldehyde, propanaldehyde, butanaldehyde, pentanaldehyde, dimethylaminoacetaldehyde, trimethylaminoacetaldehyde (betaine aldehyde), trimethylaminobutanaldehyde, short aliphatic hydroxyaldehydes such as 3-hydroxypropanaldehyde and 2-hydroxypropanaldehyde (lactaldehyde), and aromatic aldehydes.",,,,,,,GO:0004030; GO:0000166,GO:0016620,GO:0004029,GO:0004029,GO:0004030,GO:0004029,0.6117,0.6103,0.6103,0.7013,0.6103,5,0.6288,0.1864,no
ROCR_PSEAE,Q9HX69,ESM2Text,Bacteria,392,"Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to 5'-pGpG. Cannot use cyclic AMP or cyclic GMP. Part of the RocSAR two-component regulatory signaling system (also known as the SadARS system), which regulates biofilm maturation, type III secretion and expression of the cup fimbrial-gene cluster. Negatively regulates the expression of cup genes by antagonizing the activity of RocA1.","Member of the two-component regulatory system DctB/DctD, which regulates C4-dicarboxylate transport via regulation of the expression of the DctA methyltransferase DctM. DctB functions as a transcriptional repressor by direct binding to promoter regions of target genes and increasing the stability of the transcriptional machinery. Also catalyzes the formation of methylated C4-dicarboxylate, via the formation of an intermediate with CmtAB. The DctB/DctD complex represses genes involved in antibiotic resistance as well as genes involved in methionine and copper homeostasis. Participates also in biofilm formation.",No,No,No,No,Maybe,not-Yes,GO:0071111; GO:0046872,,,,,,,,,,,0,,0.6241,yes
ROCR_PSEAE,Q9HX69,Prot2Text,Bacteria,392,"Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to 5'-pGpG. Cannot use cyclic AMP or cyclic GMP. Part of the RocSAR two-component regulatory signaling system (also known as the SadARS system), which regulates biofilm maturation, type III secretion and expression of the cup fimbrial-gene cluster. Negatively regulates the expression of cup genes by antagonizing the activity of RocA1.","Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP). Increases the synthesis of cyclic-di-GMP and c-di-AMP, but not c-di-AMP, in vitro.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0071111; GO:0046872,GO:0071584,,GO:0004112,GO:0071584,GO:0071584,0.0,,0.5237,0.0,0.0,4,0.1309,0.6241,yes
ROCR_PSEAE,Q9HX69,ProtT3,Bacteria,392,"Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to 5'-pGpG. Cannot use cyclic AMP or cyclic GMP. Part of the RocSAR two-component regulatory signaling system (also known as the SadARS system), which regulates biofilm maturation, type III secretion and expression of the cup fimbrial-gene cluster. Negatively regulates the expression of cup genes by antagonizing the activity of RocA1.",Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG,Yes,Yes,Yes,Yes,Yes,Yes,GO:0071111; GO:0046872,GO:0004112,GO:0071584,GO:0004112,GO:0071111,GO:0004112,0.5237,0.0,0.5237,0.6924,0.5237,5,0.4527,0.6241,yes
ROCR_PSEAE,Q9HX69,ProtTale,Bacteria,392,"Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to 5'-pGpG. Cannot use cyclic AMP or cyclic GMP. Part of the RocSAR two-component regulatory signaling system (also known as the SadARS system), which regulates biofilm maturation, type III secretion and expression of the cup fimbrial-gene cluster. Negatively regulates the expression of cup genes by antagonizing the activity of RocA1.",Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0071111; GO:0046872,GO:0071855,GO:0071855,GO:0004112,GO:0004112,GO:0071584,0.159,0.159,0.5237,0.5237,0.0,5,0.2731,0.6241,yes
ROCR_PSEAE,Q9HX69,Protein2Text,Bacteria,392,"Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to 5'-pGpG. Cannot use cyclic AMP or cyclic GMP. Part of the RocSAR two-component regulatory signaling system (also known as the SadARS system), which regulates biofilm maturation, type III secretion and expression of the cup fimbrial-gene cluster. Negatively regulates the expression of cup genes by antagonizing the activity of RocA1.","The molecular function of this protein is not specified in the provided text. However, based on its name, it is likely to be a protein kinase, which is a type of enzyme that transfers a phosphate group from a donor molecule to a protein or other organic molecule.",No,No,No,No,No,not-Yes,GO:0071111; GO:0046872,,GO:0004672,,GO:0004672,GO:0004672,,0.1501,,0.1501,0.1501,3,0.1501,0.6241,yes
ROCR_PSEAE,Q9HX69,Reference,Bacteria,392,"Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to 5'-pGpG. Cannot use cyclic AMP or cyclic GMP. Part of the RocSAR two-component regulatory signaling system (also known as the SadARS system), which regulates biofilm maturation, type III secretion and expression of the cup fimbrial-gene cluster. Negatively regulates the expression of cup genes by antagonizing the activity of RocA1.","Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to 5'-pGpG. Cannot use cyclic AMP or cyclic GMP. Part of the RocSAR two-component regulatory signaling system (also known as the SadARS system), which regulates biofilm maturation, type III secretion and expression of the cup fimbrial-gene cluster. Negatively regulates the expression of cup genes by antagonizing the activity of RocA1.",,,,,,,GO:0071111; GO:0046872,GO:0004112,GO:0071584,GO:0004112,GO:0016787,GO:0004112,0.5237,0.0,0.5237,0.4114,0.5237,5,0.3965,0.6241,yes
BFRB_PSEAE,Q9HY79,ESM2Text,Bacteria,158,"The major iron-storage protein, part of the heterooligomeric bacterioferritin (BFR) complex. The ferroxidase center binds Fe(2+), oxidizes it using dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the BFR protein shell. Can store up to 600 iron atoms per bacterioferritin protein molecule. In iron-sufficient conditions (10 uM Fe(2+)) iron accumulates in BFR until about 12 hours, when it starts to deplete; stored iron is no longer detectable by 24 hours growth, iron is mobilized from the BFR as levels drop in the growth media. Iron release from the BFR requires ferredoxin NADP reductase (FPR) and bacterioferritin-associated ferredoxin (Bfd). Reduction of the BfrB heme group occurs in the presence of Bfd, strongly suggesting that the BfrB-Bfd complex allows heme to mediate electron transfer from FPR to the Fe(3+) iron core in the BFR shell prior to its release as Fe(2+).","Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008199; GO:0004322; GO:0020037; GO:0005506; GO:0140315,GO:0004322,GO:0004322,GO:0004322,GO:0004322,GO:0004322,0.3972,0.3972,0.3972,0.3972,0.3972,5,0.3972,0.3728,no
BFRB_PSEAE,Q9HY79,Prot2Text,Bacteria,158,"The major iron-storage protein, part of the heterooligomeric bacterioferritin (BFR) complex. The ferroxidase center binds Fe(2+), oxidizes it using dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the BFR protein shell. Can store up to 600 iron atoms per bacterioferritin protein molecule. In iron-sufficient conditions (10 uM Fe(2+)) iron accumulates in BFR until about 12 hours, when it starts to deplete; stored iron is no longer detectable by 24 hours growth, iron is mobilized from the BFR as levels drop in the growth media. Iron release from the BFR requires ferredoxin NADP reductase (FPR) and bacterioferritin-associated ferredoxin (Bfd). Reduction of the BfrB heme group occurs in the presence of Bfd, strongly suggesting that the BfrB-Bfd complex allows heme to mediate electron transfer from FPR to the Fe(3+) iron core in the BFR shell prior to its release as Fe(2+).","Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008199; GO:0004322; GO:0020037; GO:0005506; GO:0140315,GO:0004322,GO:0004322,GO:0004322,GO:0004322,GO:0004322; GO:0008199,0.3972,0.3972,0.3972,0.3972,0.7455,5,0.4669,0.3728,no
BFRB_PSEAE,Q9HY79,ProtT3,Bacteria,158,"The major iron-storage protein, part of the heterooligomeric bacterioferritin (BFR) complex. The ferroxidase center binds Fe(2+), oxidizes it using dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the BFR protein shell. Can store up to 600 iron atoms per bacterioferritin protein molecule. In iron-sufficient conditions (10 uM Fe(2+)) iron accumulates in BFR until about 12 hours, when it starts to deplete; stored iron is no longer detectable by 24 hours growth, iron is mobilized from the BFR as levels drop in the growth media. Iron release from the BFR requires ferredoxin NADP reductase (FPR) and bacterioferritin-associated ferredoxin (Bfd). Reduction of the BfrB heme group occurs in the presence of Bfd, strongly suggesting that the BfrB-Bfd complex allows heme to mediate electron transfer from FPR to the Fe(3+) iron core in the BFR shell prior to its release as Fe(2+).","Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. Belongs to the bacterioferritin family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008199; GO:0004322; GO:0020037; GO:0005506; GO:0140315,GO:0004322; GO:0008199,GO:0004322,GO:0004322; GO:0005506,GO:0004322; GO:0008199,GO:0004322,0.7455,0.3972,0.7481,0.7455,0.3972,5,0.6067,0.3728,no
BFRB_PSEAE,Q9HY79,ProtTale,Bacteria,158,"The major iron-storage protein, part of the heterooligomeric bacterioferritin (BFR) complex. The ferroxidase center binds Fe(2+), oxidizes it using dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the BFR protein shell. Can store up to 600 iron atoms per bacterioferritin protein molecule. In iron-sufficient conditions (10 uM Fe(2+)) iron accumulates in BFR until about 12 hours, when it starts to deplete; stored iron is no longer detectable by 24 hours growth, iron is mobilized from the BFR as levels drop in the growth media. Iron release from the BFR requires ferredoxin NADP reductase (FPR) and bacterioferritin-associated ferredoxin (Bfd). Reduction of the BfrB heme group occurs in the presence of Bfd, strongly suggesting that the BfrB-Bfd complex allows heme to mediate electron transfer from FPR to the Fe(3+) iron core in the BFR shell prior to its release as Fe(2+).","Iron-storage protein, whose ferroxidase center binds Fe(2+), oxidizes it using dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the BFR protein shell.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008199; GO:0004322; GO:0020037; GO:0005506; GO:0140315,GO:0004322,GO:0004322; GO:0016491,GO:0004322,GO:0004322,GO:0004322,0.3972,0.4682,0.3972,0.3972,0.3972,5,0.4114,0.3728,no
BFRB_PSEAE,Q9HY79,Protein2Text,Bacteria,158,"The major iron-storage protein, part of the heterooligomeric bacterioferritin (BFR) complex. The ferroxidase center binds Fe(2+), oxidizes it using dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the BFR protein shell. Can store up to 600 iron atoms per bacterioferritin protein molecule. In iron-sufficient conditions (10 uM Fe(2+)) iron accumulates in BFR until about 12 hours, when it starts to deplete; stored iron is no longer detectable by 24 hours growth, iron is mobilized from the BFR as levels drop in the growth media. Iron release from the BFR requires ferredoxin NADP reductase (FPR) and bacterioferritin-associated ferredoxin (Bfd). Reduction of the BfrB heme group occurs in the presence of Bfd, strongly suggesting that the BfrB-Bfd complex allows heme to mediate electron transfer from FPR to the Fe(3+) iron core in the BFR shell prior to its release as Fe(2+).","This protein is involved in iron transport. It acts as a cofactor for various iron-containing enzymes, helping to regulate iron levels and availability within the cell. 
This protein binds iron. 
Iron is a crucial component of various enzymes and proteins, and it plays a vital role in many biological processes. The protein helps to regulate iron levels and availability within the cell, ensuring that it is properly distributed to where it is needed. 
Iron is also important for the synthesis of heme, which is a crucial component of hemoglobin and other proteins. The protein helps to regulate iron levels and availability within the cell, ensuring that it is properly distributed to where it is needed. 
The protein is also involved in the regulation of iron homeostasis, which is the balance of iron levels within the cell. It helps to regulate iron levels by binding to iron and storing it until it is needed. 
In addition, the protein is involved in the transport of iron across cell membranes. It helps to regulate iron levels by binding to iron and transporting it to where it is needed. 
Overall, the protein plays a vital role in regulating iron levels and availability within the cell, ensuring that it is properly distributed to where it is needed. 
The protein helps to regulate iron levels by binding to iron and storing it until it is needed. 
The protein is also involved in the regulation of iron homeostasis, which is the balance of iron levels within the cell. It helps to regulate iron levels by binding to iron and transporting it to where it is needed. 
The protein is also involved in the synthesis of heme, which is a crucial component of hemoglobin and other proteins. It helps to regulate iron levels by binding to iron and transporting it to where it is needed. 
The protein is also involved in the regulation of iron levels in the blood. It helps to regulate iron levels by binding to iron and transporting it to where it is needed. 
The protein is also involved in the regulation of iron levels in the liver. It helps to regulate iron levels by binding to iron and transporting it to where it is needed. 
The protein is also involved in the regulation of iron levels in the spleen. It helps to regulate iron levels by binding to iron and transporting it to where it is needed. 
The protein is also involved in the regulation of iron levels in the bone marrow. It helps to regulate iron levels by binding to iron and transporting it to where it is needed. 
The protein is also involved in the regulation of iron levels in the brain.",Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0008199; GO:0004322; GO:0020037; GO:0005506; GO:0140315,GO:0005506,GO:0005506,GO:0005506,GO:0005506,GO:0005506,0.5467,0.5467,0.5467,0.5467,0.5467,5,0.5467,0.3728,no
BFRB_PSEAE,Q9HY79,Reference,Bacteria,158,"The major iron-storage protein, part of the heterooligomeric bacterioferritin (BFR) complex. The ferroxidase center binds Fe(2+), oxidizes it using dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the BFR protein shell. Can store up to 600 iron atoms per bacterioferritin protein molecule. In iron-sufficient conditions (10 uM Fe(2+)) iron accumulates in BFR until about 12 hours, when it starts to deplete; stored iron is no longer detectable by 24 hours growth, iron is mobilized from the BFR as levels drop in the growth media. Iron release from the BFR requires ferredoxin NADP reductase (FPR) and bacterioferritin-associated ferredoxin (Bfd). Reduction of the BfrB heme group occurs in the presence of Bfd, strongly suggesting that the BfrB-Bfd complex allows heme to mediate electron transfer from FPR to the Fe(3+) iron core in the BFR shell prior to its release as Fe(2+).","The major iron-storage protein, part of the heterooligomeric bacterioferritin (BFR) complex. The ferroxidase center binds Fe(2+), oxidizes it using dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the BFR protein shell. Can store up to 600 iron atoms per bacterioferritin protein molecule. In iron-sufficient conditions (10 uM Fe(2+)) iron accumulates in BFR until about 12 hours, when it starts to deplete; stored iron is no longer detectable by 24 hours growth, iron is mobilized from the BFR as levels drop in the growth media. Iron release from the BFR requires ferredoxin NADP reductase (FPR) and bacterioferritin-associated ferredoxin (Bfd). Reduction of the BfrB heme group occurs in the presence of Bfd, strongly suggesting that the BfrB-Bfd complex allows heme to mediate electron transfer from FPR to the Fe(3+) iron core in the BFR shell prior to its release as Fe(2+).",,,,,,,GO:0008199; GO:0004322; GO:0020037; GO:0005506; GO:0140315,GO:0004322,GO:0004322; GO:0005506,GO:0004322,GO:0004322; GO:0020037,GO:0004322; GO:0008199,0.3972,0.7481,0.3972,0.6588,0.7455,5,0.5894,0.3728,no
VANXY_ENTGA,Q9JN36,ESM2Text,Bacteria,190,"Bifunctional enzyme, exhibiting dipeptidase and carboxypeptidase activities. Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide. Cleaves the C-terminal D-alanine residue of UDP-muramyl-pentapeptide[Ala] (UDP- MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala). Shows no activity against the pentapeptide with a C-terminal D-serine residue. Together with VanC/VanC1 and VanT, required for vancomycin resistance in E.gallinarum strain BM4174.","Hydrolyzes dipeptides containing N-terminal D-alanine residues. Can hydrolyze the N-terminal D-Ala-D-Ala dipeptide of 7,8-dihydro-DAPA-D-Ala (D-Ala-DAPA-D-Ala).",Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0004180; GO:0160237; GO:0046872,GO:0016805,GO:0008233,GO:0016805,GO:0016805,GO:0016805,0.6529,0.5899,0.6529,0.6529,0.6529,5,0.6403,0.4558,no
VANXY_ENTGA,Q9JN36,Prot2Text,Bacteria,190,"Bifunctional enzyme, exhibiting dipeptidase and carboxypeptidase activities. Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide. Cleaves the C-terminal D-alanine residue of UDP-muramyl-pentapeptide[Ala] (UDP- MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala). Shows no activity against the pentapeptide with a C-terminal D-serine residue. Together with VanC/VanC1 and VanT, required for vancomycin resistance in E.gallinarum strain BM4174.",Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides.,No,No,No,No,No,not-Yes,GO:0004180; GO:0160237; GO:0046872,GO:0008933,GO:0008933,GO:0008933,GO:0008933,GO:0008933,0.1752,0.1752,0.1752,0.1752,0.1752,5,0.1752,0.4558,no
VANXY_ENTGA,Q9JN36,ProtT3,Bacteria,190,"Bifunctional enzyme, exhibiting dipeptidase and carboxypeptidase activities. Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide. Cleaves the C-terminal D-alanine residue of UDP-muramyl-pentapeptide[Ala] (UDP- MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala). Shows no activity against the pentapeptide with a C-terminal D-serine residue. Together with VanC/VanC1 and VanT, required for vancomycin resistance in E.gallinarum strain BM4174.","Catalyzes the hydrolysis of the D-alanyl-meso-diaminopimelic acid (D-Ala-meso-DAP) peptide bond, releasing D-alanine and meso-diaminopimelic acid (meso-DAP). Cytoplasm. Belongs to the peptidase M3 family",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004180; GO:0160237; GO:0046872,GO:0004222,GO:0008237,GO:0008237,GO:0004222,GO:0004222,0.3952,0.5005,0.5005,0.3952,0.3952,5,0.4373,0.4558,no
VANXY_ENTGA,Q9JN36,ProtTale,Bacteria,190,"Bifunctional enzyme, exhibiting dipeptidase and carboxypeptidase activities. Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide. Cleaves the C-terminal D-alanine residue of UDP-muramyl-pentapeptide[Ala] (UDP- MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala). Shows no activity against the pentapeptide with a C-terminal D-serine residue. Together with VanC/VanC1 and VanT, required for vancomycin resistance in E.gallinarum strain BM4174.","Catalyzes the cleavage of beta-1,4-linkages between N-acetylmuramic acid and L-alanine in the peptidoglycan (PG) cell wall. Involved in the degradation of the PG sacculus under conditions of osmotic stress.",No,No,No,No,No,not-Yes,GO:0004180; GO:0160237; GO:0046872,GO:0008745,GO:0008745,GO:0008745,GO:0008745,GO:0008745,0.2563,0.2563,0.2563,0.2563,0.2563,5,0.2563,0.4558,no
VANXY_ENTGA,Q9JN36,Protein2Text,Bacteria,190,"Bifunctional enzyme, exhibiting dipeptidase and carboxypeptidase activities. Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide. Cleaves the C-terminal D-alanine residue of UDP-muramyl-pentapeptide[Ala] (UDP- MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala). Shows no activity against the pentapeptide with a C-terminal D-serine residue. Together with VanC/VanC1 and VanT, required for vancomycin resistance in E.gallinarum strain BM4174.",The molecular function of this protein is acyltransferase.,No,No,No,No,No,not-Yes,GO:0004180; GO:0160237; GO:0046872,GO:0016747,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.1847,0.2232,0.2232,0.2232,0.2232,5,0.2155,0.4558,no
VANXY_ENTGA,Q9JN36,Reference,Bacteria,190,"Bifunctional enzyme, exhibiting dipeptidase and carboxypeptidase activities. Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide. Cleaves the C-terminal D-alanine residue of UDP-muramyl-pentapeptide[Ala] (UDP- MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala). Shows no activity against the pentapeptide with a C-terminal D-serine residue. Together with VanC/VanC1 and VanT, required for vancomycin resistance in E.gallinarum strain BM4174.","Bifunctional enzyme, exhibiting dipeptidase and carboxypeptidase activities. Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide. Cleaves the C-terminal D-alanine residue of UDP-muramyl-pentapeptide[Ala] (UDP- MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala). Shows no activity against the pentapeptide with a C-terminal D-serine residue. Together with VanC/VanC1 and VanT, required for vancomycin resistance in E.gallinarum strain BM4174.",,,,,,,GO:0004180; GO:0160237; GO:0046872,GO:0004180; GO:0016805,GO:0016805; GO:0004180,GO:0016805; GO:0004180,GO:0016805; GO:0004180,GO:0016805; GO:0004180,0.7699,0.7699,0.7699,0.7699,0.7699,5,0.7699,0.4558,no
TERL_BPHK7,Q9MCT1,ESM2Text,Viruses,504,"The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome from the concetamer to initiate and to end a packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. Packaging initiates by TerS recognizing the packaging sequence in the viral DNA. The nuclease activity of TerL cuts the viral DNA and the terminase-DNA complex binds to the portal of a procapsid shell. DNA is translocated into the capsid, powered by the packaging ATPase in TerL, which continues until the next site is encountered at which point the motor stops and again cuts the DNA to release the nucleocapsid filled with a unit-length genome ('unit length' packaging) (Probable).",Increases the DNA binding activity of elongating DNA polymerase.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004519; GO:0016787; GO:0046872,,,,,,,,,,,0,,0.4738,no
TERL_BPHK7,Q9MCT1,Prot2Text,Viruses,504,"The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome from the concetamer to initiate and to end a packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. Packaging initiates by TerS recognizing the packaging sequence in the viral DNA. The nuclease activity of TerL cuts the viral DNA and the terminase-DNA complex binds to the portal of a procapsid shell. DNA is translocated into the capsid, powered by the packaging ATPase in TerL, which continues until the next site is encountered at which point the motor stops and again cuts the DNA to release the nucleocapsid filled with a unit-length genome ('unit length' packaging) (Probable).",Increases the DNA binding activity of elongating DNA polymerase.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004519; GO:0016787; GO:0046872,,,GO:0003677,,,,,0.2188,,,1,0.2188,0.4738,no
TERL_BPHK7,Q9MCT1,ProtT3,Viruses,504,"The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome from the concetamer to initiate and to end a packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. Packaging initiates by TerS recognizing the packaging sequence in the viral DNA. The nuclease activity of TerL cuts the viral DNA and the terminase-DNA complex binds to the portal of a procapsid shell. DNA is translocated into the capsid, powered by the packaging ATPase in TerL, which continues until the next site is encountered at which point the motor stops and again cuts the DNA to release the nucleocapsid filled with a unit-length genome ('unit length' packaging) (Probable).",The terminase large subunit acts as an ATP-dependent molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome to initiate and to end a packaging reaction. Belongs to the terminase large subunit family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0004519; GO:0016787; GO:0046872,GO:0004519; GO:0005524,GO:0004519; GO:0005524,GO:0004519; GO:0016887; GO:0005524,GO:0004519; GO:0005524,GO:0004519; GO:0005524,0.7826,0.7826,0.7469,0.7826,0.7826,5,0.7755,0.4738,no
TERL_BPHK7,Q9MCT1,ProtTale,Viruses,504,"The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome from the concetamer to initiate and to end a packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. Packaging initiates by TerS recognizing the packaging sequence in the viral DNA. The nuclease activity of TerL cuts the viral DNA and the terminase-DNA complex binds to the portal of a procapsid shell. DNA is translocated into the capsid, powered by the packaging ATPase in TerL, which continues until the next site is encountered at which point the motor stops and again cuts the DNA to release the nucleocapsid filled with a unit-length genome ('unit length' packaging) (Probable).","The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome to initiate and to end a packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. The terminase large subunit exhibits endonuclease activity and cleaves the viral genome",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0004519; GO:0016787; GO:0046872,GO:0004386; GO:0004519; GO:0005524,GO:0004386; GO:0004519; GO:0005524,GO:0004519; GO:0016887; GO:0005524,GO:0004519; GO:0016887; GO:0005524,GO:0004519; GO:0016887; GO:0005524,0.7274,0.7274,0.7469,0.7469,0.7469,5,0.7391,0.4738,no
TERL_BPHK7,Q9MCT1,Protein2Text,Viruses,504,"The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome from the concetamer to initiate and to end a packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. Packaging initiates by TerS recognizing the packaging sequence in the viral DNA. The nuclease activity of TerL cuts the viral DNA and the terminase-DNA complex binds to the portal of a procapsid shell. DNA is translocated into the capsid, powered by the packaging ATPase in TerL, which continues until the next site is encountered at which point the motor stops and again cuts the DNA to release the nucleocapsid filled with a unit-length genome ('unit length' packaging) (Probable).","The molecular function of this protein is DNA helicase. It is a DNA helicase, which is a type of enzyme that unwinds double-stranded DNA into single strands. More specifically, it is a replication protein that plays a role in the initiation of DNA replication.",No,No,No,No,No,not-Yes,GO:0005524; GO:0004519; GO:0016787; GO:0046872,GO:0004003,GO:0003678,GO:0003678,GO:0003678,GO:0003678,0.2015,0.2015,0.2015,0.2015,0.2015,5,0.2015,0.4738,no
TERL_BPHK7,Q9MCT1,Reference,Viruses,504,"The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome from the concetamer to initiate and to end a packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. Packaging initiates by TerS recognizing the packaging sequence in the viral DNA. The nuclease activity of TerL cuts the viral DNA and the terminase-DNA complex binds to the portal of a procapsid shell. DNA is translocated into the capsid, powered by the packaging ATPase in TerL, which continues until the next site is encountered at which point the motor stops and again cuts the DNA to release the nucleocapsid filled with a unit-length genome ('unit length' packaging) (Probable).","The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome from the concetamer to initiate and to end a packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. Packaging initiates by TerS recognizing the packaging sequence in the viral DNA. The nuclease activity of TerL cuts the viral DNA and the terminase-DNA complex binds to the portal of a procapsid shell. DNA is translocated into the capsid, powered by the packaging ATPase in TerL, which continues until the next site is encountered at which point the motor stops and again cuts the DNA to release the nucleocapsid filled with a unit-length genome ('unit length' packaging) (Probable).",,,,,,,GO:0005524; GO:0004519; GO:0016787; GO:0046872,GO:0004519; GO:0016887; GO:0005524,GO:0016887; GO:0004519,GO:0016887; GO:0004519,GO:0004519; GO:0016887; GO:0003677,GO:0004519; GO:0016887; GO:0005524,0.7469,0.5179,0.5179,0.5248,0.7469,5,0.6109,0.4738,no
WBPO_PSEAI,Q9RHD7,ESM2Text,Bacteria,422,"Dehydrogenase required for the biosynthesis of the B-band O antigen of serotype O6 lipopolysaccharide. Is also required for flagellin glycosylation. Catalyzes the conversion of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N- acetylglucosaminuronic acid (UDP-GlcNAcA). Can also catalyze the conversion of UDP-N-acetyl-galactosamine (UDP-GalNAc) to UDP-N-acetylgalactosaminuronic acid (UDP-GalNAcA), with low efficiency. Can use NAD(+) or NADP(+), with a preference for NAD(+).","Catalyzes the four-electron oxidation of UDP-N-acetyl-D-mannosamine (UDP-ManNAc), reducing NAD(+) and releasing UDP-N-acetylmannosaminuronic acid (UDP-ManNAcA).",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0051287; GO:0016628; GO:0047004,GO:0016616,GO:0016616,GO:0016616,GO:0050044,,0.5661,0.5661,0.5661,0.1852,,4,0.4709,0.4164,no
WBPO_PSEAI,Q9RHD7,Prot2Text,Bacteria,422,"Dehydrogenase required for the biosynthesis of the B-band O antigen of serotype O6 lipopolysaccharide. Is also required for flagellin glycosylation. Catalyzes the conversion of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N- acetylglucosaminuronic acid (UDP-GlcNAcA). Can also catalyze the conversion of UDP-N-acetyl-galactosamine (UDP-GalNAc) to UDP-N-acetylgalactosaminuronic acid (UDP-GalNAcA), with low efficiency. Can use NAD(+) or NADP(+), with a preference for NAD(+).",Required for the biosynthesis of type 1 capsular polysaccharide.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0051287; GO:0016628; GO:0047004,,,,,,,,,,,0,,0.4164,no
WBPO_PSEAI,Q9RHD7,ProtT3,Bacteria,422,"Dehydrogenase required for the biosynthesis of the B-band O antigen of serotype O6 lipopolysaccharide. Is also required for flagellin glycosylation. Catalyzes the conversion of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N- acetylglucosaminuronic acid (UDP-GlcNAcA). Can also catalyze the conversion of UDP-N-acetyl-galactosamine (UDP-GalNAc) to UDP-N-acetylgalactosaminuronic acid (UDP-GalNAcA), with low efficiency. Can use NAD(+) or NADP(+), with a preference for NAD(+).",Catalyzes the oxidation of UDP-N-acetyl-D-mannosamine (UDP-ManNAc) to UDP-N- acetylmannosaminuronic acid (UDP-ManNAcA). Belongs to the UDP-glucose/GDP-mannose dehydrogenase family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0051287; GO:0016628; GO:0047004,GO:0016616,GO:0016616,GO:0016491,GO:0016491; GO:0051287,GO:0016616,0.5661,0.5661,0.527,0.7963,0.5661,5,0.6043,0.4164,no
WBPO_PSEAI,Q9RHD7,ProtTale,Bacteria,422,"Dehydrogenase required for the biosynthesis of the B-band O antigen of serotype O6 lipopolysaccharide. Is also required for flagellin glycosylation. Catalyzes the conversion of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N- acetylglucosaminuronic acid (UDP-GlcNAcA). Can also catalyze the conversion of UDP-N-acetyl-galactosamine (UDP-GalNAc) to UDP-N-acetylgalactosaminuronic acid (UDP-GalNAcA), with low efficiency. Can use NAD(+) or NADP(+), with a preference for NAD(+).","Catalyzes the four-electron oxidation of UDP-N-acetylmuramate (UDP-MurNAc), reducing NADP, to UDP-N- acetylglucosamine-6-phosphate (UDP-GlcNAc-6-P).",No,Maybe,Maybe,Maybe,No,not-Yes,GO:0051287; GO:0016628; GO:0047004,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.527,0.527,0.527,0.527,0.527,5,0.527,0.4164,no
WBPO_PSEAI,Q9RHD7,Protein2Text,Bacteria,422,"Dehydrogenase required for the biosynthesis of the B-band O antigen of serotype O6 lipopolysaccharide. Is also required for flagellin glycosylation. Catalyzes the conversion of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N- acetylglucosaminuronic acid (UDP-GlcNAcA). Can also catalyze the conversion of UDP-N-acetyl-galactosamine (UDP-GalNAc) to UDP-N-acetylgalactosaminuronic acid (UDP-GalNAcA), with low efficiency. Can use NAD(+) or NADP(+), with a preference for NAD(+).","The molecular function of this protein is a dehydrogenase, specifically involved in the conversion of D-ribulose 5-phosphate to D-erythrose 4-phosphate and acetyl phosphate. It catalyzes the reversible conversion of D-ribulose 5-phosphate to D-erythrose 4-phosphate and acetyl phosphate. The protein is involved in the pentose phosphate pathway.",No,No,No,No,No,not-Yes,GO:0051287; GO:0016628; GO:0047004,,GO:0008673,,,,,0.1545,,,,1,0.1545,0.4164,no
WBPO_PSEAI,Q9RHD7,Reference,Bacteria,422,"Dehydrogenase required for the biosynthesis of the B-band O antigen of serotype O6 lipopolysaccharide. Is also required for flagellin glycosylation. Catalyzes the conversion of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N- acetylglucosaminuronic acid (UDP-GlcNAcA). Can also catalyze the conversion of UDP-N-acetyl-galactosamine (UDP-GalNAc) to UDP-N-acetylgalactosaminuronic acid (UDP-GalNAcA), with low efficiency. Can use NAD(+) or NADP(+), with a preference for NAD(+).","Dehydrogenase required for the biosynthesis of the B-band O antigen of serotype O6 lipopolysaccharide. Is also required for flagellin glycosylation. Catalyzes the conversion of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N- acetylglucosaminuronic acid (UDP-GlcNAcA). Can also catalyze the conversion of UDP-N-acetyl-galactosamine (UDP-GalNAc) to UDP-N-acetylgalactosaminuronic acid (UDP-GalNAcA), with low efficiency. Can use NAD(+) or NADP(+), with a preference for NAD(+).",,,,,,,GO:0051287; GO:0016628; GO:0047004,GO:0016616,GO:0016616,GO:0016616,GO:0016616,GO:0016616,0.5661,0.5661,0.5661,0.5661,0.5661,5,0.5661,0.4164,no
BLC8_CITAM,Q9RMT4,ESM2Text,Bacteria,291,"Extended-spectrum beta-lactamase (ESBL) which confers resistance to penicillins, as well as first, third and fourth- generation cephalosporins. Has cefotaxime-hydrolyzing activity. Inactive against cephalosporin antibiotic, cefoxitin, and the carbapenem, imipenem.",Has strong cefotaxime-hydrolyzing activity.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2501,no
BLC8_CITAM,Q9RMT4,Prot2Text,Bacteria,291,"Extended-spectrum beta-lactamase (ESBL) which confers resistance to penicillins, as well as first, third and fourth- generation cephalosporins. Has cefotaxime-hydrolyzing activity. Inactive against cephalosporin antibiotic, cefoxitin, and the carbapenem, imipenem.",Hydrolyzes broad-spectrum beta-lactam antibiotics. Active against cephalosporins such as cefuroxime and cefotaxime.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2501,no
BLC8_CITAM,Q9RMT4,ProtT3,Bacteria,291,"Extended-spectrum beta-lactamase (ESBL) which confers resistance to penicillins, as well as first, third and fourth- generation cephalosporins. Has cefotaxime-hydrolyzing activity. Inactive against cephalosporin antibiotic, cefoxitin, and the carbapenem, imipenem.",Belongs to the class-A beta-lactamase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2501,no
BLC8_CITAM,Q9RMT4,ProtTale,Bacteria,291,"Extended-spectrum beta-lactamase (ESBL) which confers resistance to penicillins, as well as first, third and fourth- generation cephalosporins. Has cefotaxime-hydrolyzing activity. Inactive against cephalosporin antibiotic, cefoxitin, and the carbapenem, imipenem.","Extended-spectrum beta-lactamase (ESBL) which confers resistance to penicillins, as well as first and third generation cephalosporins. Has penicillinase activity.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2501,no
BLC8_CITAM,Q9RMT4,Protein2Text,Bacteria,291,"Extended-spectrum beta-lactamase (ESBL) which confers resistance to penicillins, as well as first, third and fourth- generation cephalosporins. Has cefotaxime-hydrolyzing activity. Inactive against cephalosporin antibiotic, cefoxitin, and the carbapenem, imipenem.",The molecular function of this protein is beta-lactamase activity.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2501,no
BLC8_CITAM,Q9RMT4,Reference,Bacteria,291,"Extended-spectrum beta-lactamase (ESBL) which confers resistance to penicillins, as well as first, third and fourth- generation cephalosporins. Has cefotaxime-hydrolyzing activity. Inactive against cephalosporin antibiotic, cefoxitin, and the carbapenem, imipenem.","Extended-spectrum beta-lactamase (ESBL) which confers resistance to penicillins, as well as first, third and fourth- generation cephalosporins. Has cefotaxime-hydrolyzing activity. Inactive against cephalosporin antibiotic, cefoxitin, and the carbapenem, imipenem.",,,,,,,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2501,no
RAF20_ARATH,Q9SAJ2,ESM2Text,Eukaryota,1248,"RAF-like protein kinase acting, together with RAF24, as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process.","Caudalizing protein that is required for asymmetric cell division during early embryogenesis. Regulates asymmetric cell division of the Q.p neuroblast lineage. Probably phosphorylates 'Ser-10' of histone H3 (H3S10ph), which promotes its ubiquitination and degradation.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004672; GO:0004674; GO:0004712,GO:0004674; GO:0005524,GO:0004672,GO:0004672,,,0.9552,0.7766,0.7766,,,3,0.8361,0.7596,yes
RAF20_ARATH,Q9SAJ2,Prot2Text,Eukaryota,1248,"RAF-like protein kinase acting, together with RAF24, as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process.",May function as a Ser/Thr-protein kinase.,Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004672; GO:0004674; GO:0004712,GO:0004674,,,,GO:0004674,0.7571,,,,0.7571,2,0.7571,0.7596,yes
RAF20_ARATH,Q9SAJ2,ProtT3,Eukaryota,1248,"RAF-like protein kinase acting, together with RAF24, as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process.",Transcription factor that binds to the DNA sequence 5'-TGTAC-3' in response to cytokinin. Nucleus. Belongs to the cytokinin receptor family. Type-B subfamily,No,No,No,No,No,not-Yes,GO:0005524; GO:0004672; GO:0004674; GO:0004712,GO:0003700; GO:0043565,GO:0003700,GO:0003700; GO:0003677,GO:0003700; GO:0043565,GO:0003700; GO:0043565,0.1383,0.1265,0.146,0.1383,0.1383,5,0.1375,0.7596,yes
RAF20_ARATH,Q9SAJ2,ProtTale,Eukaryota,1248,"RAF-like protein kinase acting, together with RAF24, as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process.",Probable RNA-dependent RNA polymerase involved in viral RNA replication.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004672; GO:0004674; GO:0004712,GO:0003968,GO:0003968,GO:0003968,GO:0003968,GO:0003968,0.2601,0.2601,0.2601,0.2601,0.2601,5,0.2601,0.7596,yes
RAF20_ARATH,Q9SAJ2,Protein2Text,Eukaryota,1248,"RAF-like protein kinase acting, together with RAF24, as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process.","The molecular function of this protein is related to its role in the regulation of plant growth and development. It is involved in the ubiquitination and proteasomal degradation of proteins, which is a key process in plant development and stress response. Specifically, it is a substrate adaptor for the E3 ubiquitin ligase complex, which is responsible for tagging proteins for degradation. It also has a role in the regulation of protein levels and activity, and is involved in the response to environmental stresses such as drought and heat. 

In terms of its molecular function, this protein is likely to be involved in the following processes:

* Ubiquitination: the attachment of ubiquitin molecules to specific proteins, marking them for degradation or regulation.
* Proteasomal degradation: the breakdown of proteins by the proteasome, a large protein complex responsible for degrading damaged or unwanted proteins.
* Protein regulation: the control of protein levels and activity through ubiquitination and proteasomal degradation.
* Stress response: the regulation of gene expression and protein activity in response to environmental stresses such as drought and heat.

Overall, this protein plays a critical role in the regulation of plant growth and development, and is involved in a range of molecular processes that are essential for plant survival and adaptation to environmental stresses.",No,No,No,No,No,not-Yes,GO:0005524; GO:0004672; GO:0004674; GO:0004712,,GO:0061630,GO:0061630,,,,0.2765,0.2765,,,2,0.2765,0.7596,yes
RAF20_ARATH,Q9SAJ2,Reference,Eukaryota,1248,"RAF-like protein kinase acting, together with RAF24, as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process.","RAF-like protein kinase acting, together with RAF24, as a central mediator of a fast response pathway to auxin involving proteins phosphorylation, and leading to rapid cellular responses including membrane depolarization and cytoplasmic streaming. Required for general growth and developmental process.",,,,,,,GO:0005524; GO:0004672; GO:0004674; GO:0004712,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.9552,0.9552,0.9552,0.9552,0.9552,5,0.9552,0.7596,yes
RAB5_DROME,Q9V3I2,ESM2Text,Eukaryota,219,"Small monomeric GTPase which cycles between active GTP-bound and inactive GDP-bound states (Probable). In its active state, binds to a variety of effector proteins to regulate cellular responses such as intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (Probable). Involved in multiple pathways of endocytic transport (Probable). As a critical component of the endocytic trafficking machinery, involved in establishment of morphogen concentration gradients during pattern formation and organogenesis, for example of the TGF-beta homolog dpp/decapentaplegic. Involved in the development and function of the nervous system. Maintains the integrity of endosomes during embryonic development. May be involved in vesicle fusion and budding during synaptic vesicle recycling. Maintains synaptic vesicle size uniformity (important for allowing quantitative release of neurotransmitters), probably by preventing homotypic vesicle fusion. Involved in endosomal trafficking during Ca(2+)-triggered exocytosis at the presynaptic terminal. During oogenesis involved in clathrin-mediated endocytic uptake of yolk proteins and their storage. Required for maturation of early endosomal precursors into mature yolk granules. Associates with endosomal membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns[4,5]P(2)) and mediates its removal. PtdIns[4,5]P(2) removal contributes to endosomal maturation by affecting the ability of PtdIns[4,5]P(2)-binding components of the early endocytic machinery, including factors involved in clathrin recruitment and actin polymerisation, to remain associated. Functions upstream of Rab7 in endolysosomal vesicle maturation but not in autolysosomal vesicle maturation. Involved in trafficking and turnover of lysosomal proteins. Stimulates the Rab7 guanyl-nucleotide exchange activity of the Mon1-Ccz1 complex, possibly by recruiting the Mon1-Ccz1 complex to vesicle membranes and enhancing its subsequent recruitment of Rab7. Involved in wing imaginal disc development.",Protein transport. Probably involved in vesicular traffic.,Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0030234; GO:0003925; GO:0005525; GO:0003924,,,,,,,,,,,0,,0.429,no
RAB5_DROME,Q9V3I2,Prot2Text,Eukaryota,219,"Small monomeric GTPase which cycles between active GTP-bound and inactive GDP-bound states (Probable). In its active state, binds to a variety of effector proteins to regulate cellular responses such as intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (Probable). Involved in multiple pathways of endocytic transport (Probable). As a critical component of the endocytic trafficking machinery, involved in establishment of morphogen concentration gradients during pattern formation and organogenesis, for example of the TGF-beta homolog dpp/decapentaplegic. Involved in the development and function of the nervous system. Maintains the integrity of endosomes during embryonic development. May be involved in vesicle fusion and budding during synaptic vesicle recycling. Maintains synaptic vesicle size uniformity (important for allowing quantitative release of neurotransmitters), probably by preventing homotypic vesicle fusion. Involved in endosomal trafficking during Ca(2+)-triggered exocytosis at the presynaptic terminal. During oogenesis involved in clathrin-mediated endocytic uptake of yolk proteins and their storage. Required for maturation of early endosomal precursors into mature yolk granules. Associates with endosomal membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns[4,5]P(2)) and mediates its removal. PtdIns[4,5]P(2) removal contributes to endosomal maturation by affecting the ability of PtdIns[4,5]P(2)-binding components of the early endocytic machinery, including factors involved in clathrin recruitment and actin polymerisation, to remain associated. Functions upstream of Rab7 in endolysosomal vesicle maturation but not in autolysosomal vesicle maturation. Involved in trafficking and turnover of lysosomal proteins. Stimulates the Rab7 guanyl-nucleotide exchange activity of the Mon1-Ccz1 complex, possibly by recruiting the Mon1-Ccz1 complex to vesicle membranes and enhancing its subsequent recruitment of Rab7. Involved in wing imaginal disc development.",Required for protein transport from the endoplasmic reticulum to the Golgi complex.,Maybe,Maybe,Vague,Vague,Maybe,not-Yes,GO:0030234; GO:0003925; GO:0005525; GO:0003924,,,,,,,,,,,0,,0.429,no
RAB5_DROME,Q9V3I2,ProtT3,Eukaryota,219,"Small monomeric GTPase which cycles between active GTP-bound and inactive GDP-bound states (Probable). In its active state, binds to a variety of effector proteins to regulate cellular responses such as intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (Probable). Involved in multiple pathways of endocytic transport (Probable). As a critical component of the endocytic trafficking machinery, involved in establishment of morphogen concentration gradients during pattern formation and organogenesis, for example of the TGF-beta homolog dpp/decapentaplegic. Involved in the development and function of the nervous system. Maintains the integrity of endosomes during embryonic development. May be involved in vesicle fusion and budding during synaptic vesicle recycling. Maintains synaptic vesicle size uniformity (important for allowing quantitative release of neurotransmitters), probably by preventing homotypic vesicle fusion. Involved in endosomal trafficking during Ca(2+)-triggered exocytosis at the presynaptic terminal. During oogenesis involved in clathrin-mediated endocytic uptake of yolk proteins and their storage. Required for maturation of early endosomal precursors into mature yolk granules. Associates with endosomal membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns[4,5]P(2)) and mediates its removal. PtdIns[4,5]P(2) removal contributes to endosomal maturation by affecting the ability of PtdIns[4,5]P(2)-binding components of the early endocytic machinery, including factors involved in clathrin recruitment and actin polymerisation, to remain associated. Functions upstream of Rab7 in endolysosomal vesicle maturation but not in autolysosomal vesicle maturation. Involved in trafficking and turnover of lysosomal proteins. Stimulates the Rab7 guanyl-nucleotide exchange activity of the Mon1-Ccz1 complex, possibly by recruiting the Mon1-Ccz1 complex to vesicle membranes and enhancing its subsequent recruitment of Rab7. Involved in wing imaginal disc development.",Protein transport. Probably involved in vesicular traffic (By similarity). Cell membrane; Lipid-anchor; Cytoplasmic side. Belongs to the small GTPase superfamily. Rab family,Yes,Yes,Maybe,Vague,Vague,not-Yes,GO:0030234; GO:0003925; GO:0005525; GO:0003924,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,0.8241,0.8241,0.8241,0.8241,0.8241,5,0.8241,0.429,no
RAB5_DROME,Q9V3I2,ProtTale,Eukaryota,219,"Small monomeric GTPase which cycles between active GTP-bound and inactive GDP-bound states (Probable). In its active state, binds to a variety of effector proteins to regulate cellular responses such as intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (Probable). Involved in multiple pathways of endocytic transport (Probable). As a critical component of the endocytic trafficking machinery, involved in establishment of morphogen concentration gradients during pattern formation and organogenesis, for example of the TGF-beta homolog dpp/decapentaplegic. Involved in the development and function of the nervous system. Maintains the integrity of endosomes during embryonic development. May be involved in vesicle fusion and budding during synaptic vesicle recycling. Maintains synaptic vesicle size uniformity (important for allowing quantitative release of neurotransmitters), probably by preventing homotypic vesicle fusion. Involved in endosomal trafficking during Ca(2+)-triggered exocytosis at the presynaptic terminal. During oogenesis involved in clathrin-mediated endocytic uptake of yolk proteins and their storage. Required for maturation of early endosomal precursors into mature yolk granules. Associates with endosomal membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns[4,5]P(2)) and mediates its removal. PtdIns[4,5]P(2) removal contributes to endosomal maturation by affecting the ability of PtdIns[4,5]P(2)-binding components of the early endocytic machinery, including factors involved in clathrin recruitment and actin polymerisation, to remain associated. Functions upstream of Rab7 in endolysosomal vesicle maturation but not in autolysosomal vesicle maturation. Involved in trafficking and turnover of lysosomal proteins. Stimulates the Rab7 guanyl-nucleotide exchange activity of the Mon1-Ccz1 complex, possibly by recruiting the Mon1-Ccz1 complex to vesicle membranes and enhancing its subsequent recruitment of Rab7. Involved in wing imaginal disc development.","The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0030234; GO:0003925; GO:0005525; GO:0003924,GO:0003924,GO:0003924,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,0.5979,0.5979,0.8241,0.8241,0.8241,5,0.7336,0.429,no
RAB5_DROME,Q9V3I2,Protein2Text,Eukaryota,219,"Small monomeric GTPase which cycles between active GTP-bound and inactive GDP-bound states (Probable). In its active state, binds to a variety of effector proteins to regulate cellular responses such as intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (Probable). Involved in multiple pathways of endocytic transport (Probable). As a critical component of the endocytic trafficking machinery, involved in establishment of morphogen concentration gradients during pattern formation and organogenesis, for example of the TGF-beta homolog dpp/decapentaplegic. Involved in the development and function of the nervous system. Maintains the integrity of endosomes during embryonic development. May be involved in vesicle fusion and budding during synaptic vesicle recycling. Maintains synaptic vesicle size uniformity (important for allowing quantitative release of neurotransmitters), probably by preventing homotypic vesicle fusion. Involved in endosomal trafficking during Ca(2+)-triggered exocytosis at the presynaptic terminal. During oogenesis involved in clathrin-mediated endocytic uptake of yolk proteins and their storage. Required for maturation of early endosomal precursors into mature yolk granules. Associates with endosomal membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns[4,5]P(2)) and mediates its removal. PtdIns[4,5]P(2) removal contributes to endosomal maturation by affecting the ability of PtdIns[4,5]P(2)-binding components of the early endocytic machinery, including factors involved in clathrin recruitment and actin polymerisation, to remain associated. Functions upstream of Rab7 in endolysosomal vesicle maturation but not in autolysosomal vesicle maturation. Involved in trafficking and turnover of lysosomal proteins. Stimulates the Rab7 guanyl-nucleotide exchange activity of the Mon1-Ccz1 complex, possibly by recruiting the Mon1-Ccz1 complex to vesicle membranes and enhancing its subsequent recruitment of Rab7. Involved in wing imaginal disc development.","The molecular function of this protein is not specified in the provided text. However, based on its name, it is likely that this protein is a member of the Ras superfamily of small GTPases, which play important roles in various cellular processes such as signal transduction, cell growth, and differentiation. More specifically, the protein may function as a guanine nucleotide-binding protein, regulating the exchange of GDP for GTP and thereby controlling the activity of downstream effectors. Further research would be needed to confirm the specific molecular function of this protein.",Vague,Maybe,Vague,Maybe,Vague,not-Yes,GO:0030234; GO:0003925; GO:0005525; GO:0003924,,GO:0003924,GO:0003924,GO:0003924; GO:0005525,GO:0003924; GO:0005525,,0.5979,0.5979,0.8241,0.8241,4,0.711,0.429,no
RAB5_DROME,Q9V3I2,Reference,Eukaryota,219,"Small monomeric GTPase which cycles between active GTP-bound and inactive GDP-bound states (Probable). In its active state, binds to a variety of effector proteins to regulate cellular responses such as intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (Probable). Involved in multiple pathways of endocytic transport (Probable). As a critical component of the endocytic trafficking machinery, involved in establishment of morphogen concentration gradients during pattern formation and organogenesis, for example of the TGF-beta homolog dpp/decapentaplegic. Involved in the development and function of the nervous system. Maintains the integrity of endosomes during embryonic development. May be involved in vesicle fusion and budding during synaptic vesicle recycling. Maintains synaptic vesicle size uniformity (important for allowing quantitative release of neurotransmitters), probably by preventing homotypic vesicle fusion. Involved in endosomal trafficking during Ca(2+)-triggered exocytosis at the presynaptic terminal. During oogenesis involved in clathrin-mediated endocytic uptake of yolk proteins and their storage. Required for maturation of early endosomal precursors into mature yolk granules. Associates with endosomal membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns[4,5]P(2)) and mediates its removal. PtdIns[4,5]P(2) removal contributes to endosomal maturation by affecting the ability of PtdIns[4,5]P(2)-binding components of the early endocytic machinery, including factors involved in clathrin recruitment and actin polymerisation, to remain associated. Functions upstream of Rab7 in endolysosomal vesicle maturation but not in autolysosomal vesicle maturation. Involved in trafficking and turnover of lysosomal proteins. Stimulates the Rab7 guanyl-nucleotide exchange activity of the Mon1-Ccz1 complex, possibly by recruiting the Mon1-Ccz1 complex to vesicle membranes and enhancing its subsequent recruitment of Rab7. Involved in wing imaginal disc development.","Small monomeric GTPase which cycles between active GTP-bound and inactive GDP-bound states (Probable). In its active state, binds to a variety of effector proteins to regulate cellular responses such as intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (Probable). Involved in multiple pathways of endocytic transport (Probable). As a critical component of the endocytic trafficking machinery, involved in establishment of morphogen concentration gradients during pattern formation and organogenesis, for example of the TGF-beta homolog dpp/decapentaplegic. Involved in the development and function of the nervous system. Maintains the integrity of endosomes during embryonic development. May be involved in vesicle fusion and budding during synaptic vesicle recycling. Maintains synaptic vesicle size uniformity (important for allowing quantitative release of neurotransmitters), probably by preventing homotypic vesicle fusion. Involved in endosomal trafficking during Ca(2+)-triggered exocytosis at the presynaptic terminal. During oogenesis involved in clathrin-mediated endocytic uptake of yolk proteins and their storage. Required for maturation of early endosomal precursors into mature yolk granules. Associates with endosomal membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns[4,5]P(2)) and mediates its removal. PtdIns[4,5]P(2) removal contributes to endosomal maturation by affecting the ability of PtdIns[4,5]P(2)-binding components of the early endocytic machinery, including factors involved in clathrin recruitment and actin polymerisation, to remain associated. Functions upstream of Rab7 in endolysosomal vesicle maturation but not in autolysosomal vesicle maturation. Involved in trafficking and turnover of lysosomal proteins. Stimulates the Rab7 guanyl-nucleotide exchange activity of the Mon1-Ccz1 complex, possibly by recruiting the Mon1-Ccz1 complex to vesicle membranes and enhancing its subsequent recruitment of Rab7. Involved in wing imaginal disc development.",,,,,,,GO:0030234; GO:0003925; GO:0005525; GO:0003924,GO:0005525; GO:0003924,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,0.8241,0.8241,0.8241,0.8241,0.8241,5,0.8241,0.429,no
B4GTB_DROME,Q9VAQ8,ESM2Text,Eukaryota,323,"A beta1,4-N-acetylgalactosaminyltransferase that uses UDP- GalNAc to transfer a GalNAc residue to substrates with a terminal N- acetylglucosamine (GlcNAc) generating GalNAcbeta1,4-GlcNAc. Specific for glycolipid substrates. Functions downstream of egh/egghead and brn/brainiac to add the 4th sugar during glycosphingolipid elongation to form GalNAc-beta1-4GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer from the brn product GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer (Probable). Plays a role in glycosphingolipid biosynthesis in female germline cells involved in dorsal follicular cell fate specification by EGFR signaling.",Probable glycosyltransferase responsible for the polymerization of chondroitin sulfate and related oligosaccharides onto the surface of the extracellular matrix.,No,Maybe,Maybe,No,No,not-Yes,GO:0008376; GO:0033842,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.631,0.631,0.631,0.631,0.631,5,0.631,0.4201,no
B4GTB_DROME,Q9VAQ8,Prot2Text,Eukaryota,323,"A beta1,4-N-acetylgalactosaminyltransferase that uses UDP- GalNAc to transfer a GalNAc residue to substrates with a terminal N- acetylglucosamine (GlcNAc) generating GalNAcbeta1,4-GlcNAc. Specific for glycolipid substrates. Functions downstream of egh/egghead and brn/brainiac to add the 4th sugar during glycosphingolipid elongation to form GalNAc-beta1-4GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer from the brn product GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer (Probable). Plays a role in glycosphingolipid biosynthesis in female germline cells involved in dorsal follicular cell fate specification by EGFR signaling.",Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.,No,Maybe,Maybe,No,No,not-Yes,GO:0008376; GO:0033842,GO:0016757,,GO:0016757,GO:0016757,GO:0016757,0.631,,0.631,0.631,0.631,4,0.631,0.4201,no
B4GTB_DROME,Q9VAQ8,ProtT3,Eukaryota,323,"A beta1,4-N-acetylgalactosaminyltransferase that uses UDP- GalNAc to transfer a GalNAc residue to substrates with a terminal N- acetylglucosamine (GlcNAc) generating GalNAcbeta1,4-GlcNAc. Specific for glycolipid substrates. Functions downstream of egh/egghead and brn/brainiac to add the 4th sugar during glycosphingolipid elongation to form GalNAc-beta1-4GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer from the brn product GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer (Probable). Plays a role in glycosphingolipid biosynthesis in female germline cells involved in dorsal follicular cell fate specification by EGFR signaling.","Catalyzes the transfer of galactose from UDP-galactose to ceramide. Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Belongs to the glycosyltransferase 7 family",No,Maybe,Maybe,No,No,not-Yes,GO:0008376; GO:0033842,GO:0003945,GO:0001732,GO:0008378,GO:0008378,GO:0008378,0.6151,0.0,0.6333,0.6333,0.6333,5,0.503,0.4201,no
B4GTB_DROME,Q9VAQ8,ProtTale,Eukaryota,323,"A beta1,4-N-acetylgalactosaminyltransferase that uses UDP- GalNAc to transfer a GalNAc residue to substrates with a terminal N- acetylglucosamine (GlcNAc) generating GalNAcbeta1,4-GlcNAc. Specific for glycolipid substrates. Functions downstream of egh/egghead and brn/brainiac to add the 4th sugar during glycosphingolipid elongation to form GalNAc-beta1-4GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer from the brn product GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer (Probable). Plays a role in glycosphingolipid biosynthesis in female germline cells involved in dorsal follicular cell fate specification by EGFR signaling.","Glycosyltransferase that catalyzes the transfer of glucuronic acid (GlcA) from UDP-glucuronic acid (UDP-GlcA) onto the non-reducing end of N- acetyl-D-glucosamine (GlcNAc) residues as part of the biosynthesis of the glycoconjugate N-acetyl-D-glucosamine-beta-D-1,4-N-acetyl-D-glucosamine-beta-D-1,3-D-glucuronic acid (GlcNAc-GlcA). Catalyzes both the transfer of UDP-glucuronic acid (UDP-GlcA) and UDP-",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0008376; GO:0033842,GO:0016757,GO:0016757,GO:0015020,GO:0016757,GO:0016757,0.631,0.631,0.7487,0.631,0.631,5,0.6545,0.4201,no
B4GTB_DROME,Q9VAQ8,Protein2Text,Eukaryota,323,"A beta1,4-N-acetylgalactosaminyltransferase that uses UDP- GalNAc to transfer a GalNAc residue to substrates with a terminal N- acetylglucosamine (GlcNAc) generating GalNAcbeta1,4-GlcNAc. Specific for glycolipid substrates. Functions downstream of egh/egghead and brn/brainiac to add the 4th sugar during glycosphingolipid elongation to form GalNAc-beta1-4GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer from the brn product GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer (Probable). Plays a role in glycosphingolipid biosynthesis in female germline cells involved in dorsal follicular cell fate specification by EGFR signaling.","The molecular function of this protein is not explicitly stated in the provided snippet, but it is implied to be involved in glycosylation, as it is described as a ""glycosyltransferase"" and is related to the production of a type of molecule (possibly a carbohydrate or sugar molecule) involved in various cellular processes.",Vague,Maybe,Vague,Vague,Maybe,not-Yes,GO:0008376; GO:0033842,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.631,0.631,0.631,0.631,0.631,5,0.631,0.4201,no
B4GTB_DROME,Q9VAQ8,Reference,Eukaryota,323,"A beta1,4-N-acetylgalactosaminyltransferase that uses UDP- GalNAc to transfer a GalNAc residue to substrates with a terminal N- acetylglucosamine (GlcNAc) generating GalNAcbeta1,4-GlcNAc. Specific for glycolipid substrates. Functions downstream of egh/egghead and brn/brainiac to add the 4th sugar during glycosphingolipid elongation to form GalNAc-beta1-4GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer from the brn product GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer (Probable). Plays a role in glycosphingolipid biosynthesis in female germline cells involved in dorsal follicular cell fate specification by EGFR signaling.","A beta1,4-N-acetylgalactosaminyltransferase that uses UDP- GalNAc to transfer a GalNAc residue to substrates with a terminal N- acetylglucosamine (GlcNAc) generating GalNAcbeta1,4-GlcNAc. Specific for glycolipid substrates. Functions downstream of egh/egghead and brn/brainiac to add the 4th sugar during glycosphingolipid elongation to form GalNAc-beta1-4GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer from the brn product GlcNAc-beta1-3Man-beta1-4Glc-beta1-1Cer (Probable). Plays a role in glycosphingolipid biosynthesis in female germline cells involved in dorsal follicular cell fate specification by EGFR signaling.",,,,,,,GO:0008376; GO:0033842,GO:0008376,GO:0008376,GO:0008376,GO:0016757,GO:0008376,0.9633,0.9633,0.9633,0.631,0.9633,5,0.8968,0.4201,no
NMNA_DROME,Q9VC03,ESM2Text,Eukaryota,389,"Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Essential for viability. Stress-response chaperone protein that prevents toxic aggregation of proteins and promotes proteasome-mediated degradation of misfolded proteins; this is independent of its NAD(+) synthesis activity. Neuroprotective in response to toxic protein aggregation, for example by overexpressed Atx-1/ataxin-1. Required for maintenance and integrity of mature neurons, protecting them from neuronal activity-induced neurodegeneration. Required for the maintenance of axonal and dendritic integrity in both central and peripheral neurons. Chaperone function and neuroprotective roles are largely independent of NAD(+) synthesis activity.",Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Involved in DNA repair.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0000309; GO:0004515; GO:0051082,GO:0000309,GO:0004515,GO:0000309,GO:0000309,GO:0004515,0.5817,0.5817,0.5817,0.5817,0.5817,5,0.5817,0.333,no
NMNA_DROME,Q9VC03,Prot2Text,Eukaryota,389,"Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Essential for viability. Stress-response chaperone protein that prevents toxic aggregation of proteins and promotes proteasome-mediated degradation of misfolded proteins; this is independent of its NAD(+) synthesis activity. Neuroprotective in response to toxic protein aggregation, for example by overexpressed Atx-1/ataxin-1. Required for maintenance and integrity of mature neurons, protecting them from neuronal activity-induced neurodegeneration. Required for the maintenance of axonal and dendritic integrity in both central and peripheral neurons. Chaperone function and neuroprotective roles are largely independent of NAD(+) synthesis activity.",Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate to form deamido-NAD(+) (NaAD). Key enzyme in both de novo and salvage pathways for NAD(+) biosynthesis. Predominantly acts in the salvage pathways via NMN.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0000309; GO:0004515; GO:0051082,GO:0004515,GO:0004515,GO:0000309; GO:0004515,GO:0004515,GO:0004515; GO:0005524,0.5817,0.5817,0.6936,0.5817,0.8187,5,0.6515,0.333,no
NMNA_DROME,Q9VC03,ProtT3,Eukaryota,389,"Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Essential for viability. Stress-response chaperone protein that prevents toxic aggregation of proteins and promotes proteasome-mediated degradation of misfolded proteins; this is independent of its NAD(+) synthesis activity. Neuroprotective in response to toxic protein aggregation, for example by overexpressed Atx-1/ataxin-1. Required for maintenance and integrity of mature neurons, protecting them from neuronal activity-induced neurodegeneration. Required for the maintenance of axonal and dendritic integrity in both central and peripheral neurons. Chaperone function and neuroprotective roles are largely independent of NAD(+) synthesis activity.",Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Cytoplasm Nucleus. Belongs to the NAD(P)-dependent epimerase/dehydratase family,Yes,Yes,Yes,Yes,No,Yes,GO:0005524; GO:0000309; GO:0004515; GO:0051082,GO:0004515; GO:0005524,GO:0000309,GO:0004515; GO:0005524,GO:0000309; GO:0005524,GO:0004515,0.8187,0.5817,0.8187,0.8187,0.5817,5,0.7239,0.333,no
NMNA_DROME,Q9VC03,ProtTale,Eukaryota,389,"Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Essential for viability. Stress-response chaperone protein that prevents toxic aggregation of proteins and promotes proteasome-mediated degradation of misfolded proteins; this is independent of its NAD(+) synthesis activity. Neuroprotective in response to toxic protein aggregation, for example by overexpressed Atx-1/ataxin-1. Required for maintenance and integrity of mature neurons, protecting them from neuronal activity-induced neurodegeneration. Required for the maintenance of axonal and dendritic integrity in both central and peripheral neurons. Chaperone function and neuroprotective roles are largely independent of NAD(+) synthesis activity.","Shows glucose-6-phosphate dehydrogenase (G6PDH)-like activity. G6PDH is an enzyme that catalyzing the reduction of glucose-6-phosphate (G6P) to gluconate-6-phosphate (G6P), a key step in hexose monophosphate pathway (HMP). Can also catalyze the reduction of ribose-5-phosphate to ribonate-5-phosphate.",No,No,No,No,No,not-Yes,GO:0005524; GO:0000309; GO:0004515; GO:0051082,GO:0004345; GO:0016616,GO:0004345,GO:0004345,GO:0004345,GO:0004345,0.1672,0.1406,0.1406,0.1406,0.1406,5,0.1459,0.333,no
NMNA_DROME,Q9VC03,Protein2Text,Eukaryota,389,"Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Essential for viability. Stress-response chaperone protein that prevents toxic aggregation of proteins and promotes proteasome-mediated degradation of misfolded proteins; this is independent of its NAD(+) synthesis activity. Neuroprotective in response to toxic protein aggregation, for example by overexpressed Atx-1/ataxin-1. Required for maintenance and integrity of mature neurons, protecting them from neuronal activity-induced neurodegeneration. Required for the maintenance of axonal and dendritic integrity in both central and peripheral neurons. Chaperone function and neuroprotective roles are largely independent of NAD(+) synthesis activity.","The molecular function of this protein is as a methyltransferase, specifically involved in the conversion of the nucleotide cofactor NAD to NADP, and in the synthesis of S-adenosylmethionine (SAM).",No,No,No,No,No,not-Yes,GO:0005524; GO:0000309; GO:0004515; GO:0051082,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.252,0.252,0.252,0.252,0.252,5,0.252,0.333,no
NMNA_DROME,Q9VC03,Reference,Eukaryota,389,"Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Essential for viability. Stress-response chaperone protein that prevents toxic aggregation of proteins and promotes proteasome-mediated degradation of misfolded proteins; this is independent of its NAD(+) synthesis activity. Neuroprotective in response to toxic protein aggregation, for example by overexpressed Atx-1/ataxin-1. Required for maintenance and integrity of mature neurons, protecting them from neuronal activity-induced neurodegeneration. Required for the maintenance of axonal and dendritic integrity in both central and peripheral neurons. Chaperone function and neuroprotective roles are largely independent of NAD(+) synthesis activity.","Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Essential for viability. Stress-response chaperone protein that prevents toxic aggregation of proteins and promotes proteasome-mediated degradation of misfolded proteins; this is independent of its NAD(+) synthesis activity. Neuroprotective in response to toxic protein aggregation, for example by overexpressed Atx-1/ataxin-1. Required for maintenance and integrity of mature neurons, protecting them from neuronal activity-induced neurodegeneration. Required for the maintenance of axonal and dendritic integrity in both central and peripheral neurons. Chaperone function and neuroprotective roles are largely independent of NAD(+) synthesis activity.",,,,,,,GO:0005524; GO:0000309; GO:0004515; GO:0051082,GO:0004515; GO:0051082,GO:0004515; GO:0051082,GO:0004515; GO:0051082,GO:0004515; GO:0005524,GO:0004515; GO:0005524,0.8187,0.8187,0.8187,0.8187,0.8187,5,0.8187,0.333,no
TOK_DROME,Q9VC47,ESM2Text,Eukaryota,1464,"Metalloprotease which is required for cleavage of sli into slit N-product and slit C-product, ensuring correct slit N-product- mediated longitudinal axon guidance. Also cleaves TGF-beta family ligands daw, Actbeta and myo and is required for normal guidance of motor axons to their muscle targets. Cleavage of daw enhances its signaling activity. Required during mid- to late-embryonic stages for defasciculation of motor axons. During pupal development, cleaves dorsal-ventral patterning protein sog which contributes to specification of the posterior crossvein in the wing. Processes sog less efficiently than metalloprotease tld which also cleaves sog. Promotes BMP signal transduction in the caudal visceral mesoderm, resulting in the translocation of Mad to the nucleus to promote stg transcription which allows for cell cycle progression and promotion of levels of cell death protein hid. This leads to elimination of cells that lose access to substrate-derived FGF during migration.","Metalloprotease. Required for patterning ventral tissues of the tail. Predominant protease, which in the dorsal embryonic ventromere, cleaves chordin and thus chordin-mediated organogenesis, including the pharyngeal remodeling.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005509; GO:0004222; GO:0008270,GO:0004222,GO:0004222,GO:0004222,GO:0008237,GO:0008237,0.5311,0.5311,0.5311,0.4401,0.4401,5,0.4947,0.3233,no
TOK_DROME,Q9VC47,Prot2Text,Eukaryota,1464,"Metalloprotease which is required for cleavage of sli into slit N-product and slit C-product, ensuring correct slit N-product- mediated longitudinal axon guidance. Also cleaves TGF-beta family ligands daw, Actbeta and myo and is required for normal guidance of motor axons to their muscle targets. Cleavage of daw enhances its signaling activity. Required during mid- to late-embryonic stages for defasciculation of motor axons. During pupal development, cleaves dorsal-ventral patterning protein sog which contributes to specification of the posterior crossvein in the wing. Processes sog less efficiently than metalloprotease tld which also cleaves sog. Promotes BMP signal transduction in the caudal visceral mesoderm, resulting in the translocation of Mad to the nucleus to promote stg transcription which allows for cell cycle progression and promotion of levels of cell death protein hid. This leads to elimination of cells that lose access to substrate-derived FGF during migration.",Metalloprotease.,Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005509; GO:0004222; GO:0008270,GO:0004222,GO:0004222,GO:0004222,GO:0004222,GO:0004222,0.5311,0.5311,0.5311,0.5311,0.5311,5,0.5311,0.3233,no
TOK_DROME,Q9VC47,ProtT3,Eukaryota,1464,"Metalloprotease which is required for cleavage of sli into slit N-product and slit C-product, ensuring correct slit N-product- mediated longitudinal axon guidance. Also cleaves TGF-beta family ligands daw, Actbeta and myo and is required for normal guidance of motor axons to their muscle targets. Cleavage of daw enhances its signaling activity. Required during mid- to late-embryonic stages for defasciculation of motor axons. During pupal development, cleaves dorsal-ventral patterning protein sog which contributes to specification of the posterior crossvein in the wing. Processes sog less efficiently than metalloprotease tld which also cleaves sog. Promotes BMP signal transduction in the caudal visceral mesoderm, resulting in the translocation of Mad to the nucleus to promote stg transcription which allows for cell cycle progression and promotion of levels of cell death protein hid. This leads to elimination of cells that lose access to substrate-derived FGF during migration.","Probable metalloprotease. Secreted, extracellular space, extracellular matrix",Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005509; GO:0004222; GO:0008270,GO:0004222; GO:0046872,GO:0008237,GO:0004222,GO:0004222; GO:0046872,GO:0004222,0.9018,0.4401,0.5311,0.9018,0.5311,5,0.6612,0.3233,no
TOK_DROME,Q9VC47,ProtTale,Eukaryota,1464,"Metalloprotease which is required for cleavage of sli into slit N-product and slit C-product, ensuring correct slit N-product- mediated longitudinal axon guidance. Also cleaves TGF-beta family ligands daw, Actbeta and myo and is required for normal guidance of motor axons to their muscle targets. Cleavage of daw enhances its signaling activity. Required during mid- to late-embryonic stages for defasciculation of motor axons. During pupal development, cleaves dorsal-ventral patterning protein sog which contributes to specification of the posterior crossvein in the wing. Processes sog less efficiently than metalloprotease tld which also cleaves sog. Promotes BMP signal transduction in the caudal visceral mesoderm, resulting in the translocation of Mad to the nucleus to promote stg transcription which allows for cell cycle progression and promotion of levels of cell death protein hid. This leads to elimination of cells that lose access to substrate-derived FGF during migration.","Metalloprotease that cleaves type I collagen alpha 1 (COL1A1), alpha 2 (COL1A2) and alpha 3 (COL1A3) chains. May be involved in cell-cell interactions.",Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005509; GO:0004222; GO:0008270,GO:0004222,GO:0004222,GO:0004222,GO:0004222,GO:0008237,0.5311,0.5311,0.5311,0.5311,0.4401,5,0.5129,0.3233,no
TOK_DROME,Q9VC47,Protein2Text,Eukaryota,1464,"Metalloprotease which is required for cleavage of sli into slit N-product and slit C-product, ensuring correct slit N-product- mediated longitudinal axon guidance. Also cleaves TGF-beta family ligands daw, Actbeta and myo and is required for normal guidance of motor axons to their muscle targets. Cleavage of daw enhances its signaling activity. Required during mid- to late-embryonic stages for defasciculation of motor axons. During pupal development, cleaves dorsal-ventral patterning protein sog which contributes to specification of the posterior crossvein in the wing. Processes sog less efficiently than metalloprotease tld which also cleaves sog. Promotes BMP signal transduction in the caudal visceral mesoderm, resulting in the translocation of Mad to the nucleus to promote stg transcription which allows for cell cycle progression and promotion of levels of cell death protein hid. This leads to elimination of cells that lose access to substrate-derived FGF during migration.","This protein is involved in the molecular function of being a transcriptional activator, specifically in the regulation of gene expression.",No,No,No,No,No,not-Yes,GO:0005509; GO:0004222; GO:0008270,GO:0003700,GO:0003700,GO:0003700,GO:0003700,GO:0003700,0.1353,0.1353,0.1353,0.1353,0.1353,5,0.1353,0.3233,no
TOK_DROME,Q9VC47,Reference,Eukaryota,1464,"Metalloprotease which is required for cleavage of sli into slit N-product and slit C-product, ensuring correct slit N-product- mediated longitudinal axon guidance. Also cleaves TGF-beta family ligands daw, Actbeta and myo and is required for normal guidance of motor axons to their muscle targets. Cleavage of daw enhances its signaling activity. Required during mid- to late-embryonic stages for defasciculation of motor axons. During pupal development, cleaves dorsal-ventral patterning protein sog which contributes to specification of the posterior crossvein in the wing. Processes sog less efficiently than metalloprotease tld which also cleaves sog. Promotes BMP signal transduction in the caudal visceral mesoderm, resulting in the translocation of Mad to the nucleus to promote stg transcription which allows for cell cycle progression and promotion of levels of cell death protein hid. This leads to elimination of cells that lose access to substrate-derived FGF during migration.","Metalloprotease which is required for cleavage of sli into slit N-product and slit C-product, ensuring correct slit N-product- mediated longitudinal axon guidance. Also cleaves TGF-beta family ligands daw, Actbeta and myo and is required for normal guidance of motor axons to their muscle targets. Cleavage of daw enhances its signaling activity. Required during mid- to late-embryonic stages for defasciculation of motor axons. During pupal development, cleaves dorsal-ventral patterning protein sog which contributes to specification of the posterior crossvein in the wing. Processes sog less efficiently than metalloprotease tld which also cleaves sog. Promotes BMP signal transduction in the caudal visceral mesoderm, resulting in the translocation of Mad to the nucleus to promote stg transcription which allows for cell cycle progression and promotion of levels of cell death protein hid. This leads to elimination of cells that lose access to substrate-derived FGF during migration.",,,,,,,GO:0005509; GO:0004222; GO:0008270,GO:0004222,GO:0004222,GO:0004222,GO:0004222,GO:0008237,0.5311,0.5311,0.5311,0.5311,0.4401,5,0.5129,0.3233,no
UBP12_DROME,Q9VCT9,ESM2Text,Eukaryota,424,"Catalytic component of the Usp12-46 deubiquitylase complex. Deubiquitylates the wg/wingless-signaling receptor arr/arrow, which stabilizes the receptor and increases its concentration at the cell surface; this enhances the sensitivity of cells to wg/wingless-signal stimulation. This increases the amplitude and spatial range of the signaling response to the wg/wingless morphogen gradient, facilitating the precise, concentration-dependent regulation of its target genes. Required for wg/wingless-mediated signaling in the wing imaginal disc and for wg/wingless-dependent regulation of adult intestinal stem cell proliferation. Negative regulator of Notch signaling, possibly by regulating lysosomal degradation of N/Notch and affecting cell surface receptor levels; this may be context and cell-type specific function involved in external sensory organ development but not in wing imaginal-disc dorsoventral boundary signaling (Probable). Protects against HTT/huntingtin-induced polyglutamine expansion-dependent neurodegeneration.",Involved in the regulation of membrane trafficking at the trans-Golgi network. Probably functions by regulating the peptide bond formation between ubiquitin and the MPS1 membrane.,No,No,No,No,No,not-Yes,GO:0004843; GO:0101005,,,,,,,,,,,0,,0.7803,yes
UBP12_DROME,Q9VCT9,Prot2Text,Eukaryota,424,"Catalytic component of the Usp12-46 deubiquitylase complex. Deubiquitylates the wg/wingless-signaling receptor arr/arrow, which stabilizes the receptor and increases its concentration at the cell surface; this enhances the sensitivity of cells to wg/wingless-signal stimulation. This increases the amplitude and spatial range of the signaling response to the wg/wingless morphogen gradient, facilitating the precise, concentration-dependent regulation of its target genes. Required for wg/wingless-mediated signaling in the wing imaginal disc and for wg/wingless-dependent regulation of adult intestinal stem cell proliferation. Negative regulator of Notch signaling, possibly by regulating lysosomal degradation of N/Notch and affecting cell surface receptor levels; this may be context and cell-type specific function involved in external sensory organ development but not in wing imaginal-disc dorsoventral boundary signaling (Probable). Protects against HTT/huntingtin-induced polyglutamine expansion-dependent neurodegeneration.",Deubiquitinating enzyme. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004843; GO:0101005,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,0.939,0.939,0.939,0.939,0.939,5,0.939,0.7803,yes
UBP12_DROME,Q9VCT9,ProtT3,Eukaryota,424,"Catalytic component of the Usp12-46 deubiquitylase complex. Deubiquitylates the wg/wingless-signaling receptor arr/arrow, which stabilizes the receptor and increases its concentration at the cell surface; this enhances the sensitivity of cells to wg/wingless-signal stimulation. This increases the amplitude and spatial range of the signaling response to the wg/wingless morphogen gradient, facilitating the precise, concentration-dependent regulation of its target genes. Required for wg/wingless-mediated signaling in the wing imaginal disc and for wg/wingless-dependent regulation of adult intestinal stem cell proliferation. Negative regulator of Notch signaling, possibly by regulating lysosomal degradation of N/Notch and affecting cell surface receptor levels; this may be context and cell-type specific function involved in external sensory organ development but not in wing imaginal-disc dorsoventral boundary signaling (Probable). Protects against HTT/huntingtin-induced polyglutamine expansion-dependent neurodegeneration.",Has deubiquitinating activity towards 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Cytoplasm Nucleus. Belongs to the peptidase C19 family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004843; GO:0101005,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,0.939,0.939,0.939,0.939,0.939,5,0.939,0.7803,yes
UBP12_DROME,Q9VCT9,ProtTale,Eukaryota,424,"Catalytic component of the Usp12-46 deubiquitylase complex. Deubiquitylates the wg/wingless-signaling receptor arr/arrow, which stabilizes the receptor and increases its concentration at the cell surface; this enhances the sensitivity of cells to wg/wingless-signal stimulation. This increases the amplitude and spatial range of the signaling response to the wg/wingless morphogen gradient, facilitating the precise, concentration-dependent regulation of its target genes. Required for wg/wingless-mediated signaling in the wing imaginal disc and for wg/wingless-dependent regulation of adult intestinal stem cell proliferation. Negative regulator of Notch signaling, possibly by regulating lysosomal degradation of N/Notch and affecting cell surface receptor levels; this may be context and cell-type specific function involved in external sensory organ development but not in wing imaginal-disc dorsoventral boundary signaling (Probable). Protects against HTT/huntingtin-induced polyglutamine expansion-dependent neurodegeneration.","Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes such as DNA damage repair, mitosis, cell division, cellular homeostasis, or the viral life cycle. Has a role in the DNA damage response (DDR) pathway. Acts as a key regulator of the S-phase checkpoint by deubiquitinating and stabilizing HUWE1 (UBE2W), an E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H2A at 'Lys-12' (H2AK12ub1). Deubiquitination of HUWE1 (UBE",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004843; GO:0101005,GO:0004843,GO:0004843; GO:0016579,GO:0004843,GO:0004843,GO:0004843,0.939,0.7043,0.939,0.939,0.939,5,0.8921,0.7803,yes
UBP12_DROME,Q9VCT9,Protein2Text,Eukaryota,424,"Catalytic component of the Usp12-46 deubiquitylase complex. Deubiquitylates the wg/wingless-signaling receptor arr/arrow, which stabilizes the receptor and increases its concentration at the cell surface; this enhances the sensitivity of cells to wg/wingless-signal stimulation. This increases the amplitude and spatial range of the signaling response to the wg/wingless morphogen gradient, facilitating the precise, concentration-dependent regulation of its target genes. Required for wg/wingless-mediated signaling in the wing imaginal disc and for wg/wingless-dependent regulation of adult intestinal stem cell proliferation. Negative regulator of Notch signaling, possibly by regulating lysosomal degradation of N/Notch and affecting cell surface receptor levels; this may be context and cell-type specific function involved in external sensory organ development but not in wing imaginal-disc dorsoventral boundary signaling (Probable). Protects against HTT/huntingtin-induced polyglutamine expansion-dependent neurodegeneration.","The molecular function of this protein is as a deubiquitinating enzyme, specifically as a cysteine protease that removes ubiquitin from ubiquitinated proteins.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004843; GO:0101005,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,0.939,0.939,0.939,0.939,0.939,5,0.939,0.7803,yes
UBP12_DROME,Q9VCT9,Reference,Eukaryota,424,"Catalytic component of the Usp12-46 deubiquitylase complex. Deubiquitylates the wg/wingless-signaling receptor arr/arrow, which stabilizes the receptor and increases its concentration at the cell surface; this enhances the sensitivity of cells to wg/wingless-signal stimulation. This increases the amplitude and spatial range of the signaling response to the wg/wingless morphogen gradient, facilitating the precise, concentration-dependent regulation of its target genes. Required for wg/wingless-mediated signaling in the wing imaginal disc and for wg/wingless-dependent regulation of adult intestinal stem cell proliferation. Negative regulator of Notch signaling, possibly by regulating lysosomal degradation of N/Notch and affecting cell surface receptor levels; this may be context and cell-type specific function involved in external sensory organ development but not in wing imaginal-disc dorsoventral boundary signaling (Probable). Protects against HTT/huntingtin-induced polyglutamine expansion-dependent neurodegeneration.","Catalytic component of the Usp12-46 deubiquitylase complex. Deubiquitylates the wg/wingless-signaling receptor arr/arrow, which stabilizes the receptor and increases its concentration at the cell surface; this enhances the sensitivity of cells to wg/wingless-signal stimulation. This increases the amplitude and spatial range of the signaling response to the wg/wingless morphogen gradient, facilitating the precise, concentration-dependent regulation of its target genes. Required for wg/wingless-mediated signaling in the wing imaginal disc and for wg/wingless-dependent regulation of adult intestinal stem cell proliferation. Negative regulator of Notch signaling, possibly by regulating lysosomal degradation of N/Notch and affecting cell surface receptor levels; this may be context and cell-type specific function involved in external sensory organ development but not in wing imaginal-disc dorsoventral boundary signaling (Probable). Protects against HTT/huntingtin-induced polyglutamine expansion-dependent neurodegeneration.",,,,,,,GO:0004843; GO:0101005,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,0.939,0.939,0.939,0.939,0.939,5,0.939,0.7803,yes
FANCM_DROME,Q9VDA0,ESM2Text,Eukaryota,1489,"A ssDNA-dependent ATPase with 3' to 5' helicase activity. Involved in multiple DNA-damage responses, some that require ATPase and helicase activity and some that are independent of these. Involved in DNA interstrand cross-link repair, probably together with Fancl and other Fanconi anemia pathway homologs. Independent of Fancl involved in DNA double strand break repair, including contributing to the synthesis-dependent strand annealing (SDSA) pathway. Probably contributes to SDSA by unwinding short duplex regions in complex D-loop-like DNA structures.","ATP-dependent DNA helicase involved in DNA damage repair by homologous recombination and in genome maintenance. Capable of unwinding D-loops. Plays a role in limiting crossover recombinants during mitotic DNA double-strand break (DSB) repair. Plays a role in triggering DMC1-dependent crossover, but also from a FANCM-independent crossover, in the MVB pathway for G1/S crossover. Component of the FANCM-MVB pathway for non-homologous end joining (NHEJ) required for efficient somatic recombination-DNA double-strand break repair.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0043138; GO:0005524; GO:0000400; GO:0009378; GO:0016787,GO:0003678; GO:0005524,GO:0004003; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,0.7379,0.7379,0.7379,0.7379,0.7379,5,0.7379,0.604,yes
FANCM_DROME,Q9VDA0,Prot2Text,Eukaryota,1489,"A ssDNA-dependent ATPase with 3' to 5' helicase activity. Involved in multiple DNA-damage responses, some that require ATPase and helicase activity and some that are independent of these. Involved in DNA interstrand cross-link repair, probably together with Fancl and other Fanconi anemia pathway homologs. Independent of Fancl involved in DNA double strand break repair, including contributing to the synthesis-dependent strand annealing (SDSA) pathway. Probably contributes to SDSA by unwinding short duplex regions in complex D-loop-like DNA structures.","Ribonuclease required for the repair of DNA double-strand breaks (DSBs) generated by homologous recombination (HR). Has a preference for single-stranded DNA substrates. Plays a role in triggering gene conversion at blocked replication forks, probably by reversal of the stalled fork.",No,No,No,No,No,not-Yes,GO:0043138; GO:0005524; GO:0000400; GO:0009378; GO:0016787,GO:0004518,,GO:0004520,GO:0004518,GO:0004519,0.3071,,0.2266,0.3071,0.2596,4,0.2751,0.604,yes
FANCM_DROME,Q9VDA0,ProtT3,Eukaryota,1489,"A ssDNA-dependent ATPase with 3' to 5' helicase activity. Involved in multiple DNA-damage responses, some that require ATPase and helicase activity and some that are independent of these. Involved in DNA interstrand cross-link repair, probably together with Fancl and other Fanconi anemia pathway homologs. Independent of Fancl involved in DNA double strand break repair, including contributing to the synthesis-dependent strand annealing (SDSA) pathway. Probably contributes to SDSA by unwinding short duplex regions in complex D-loop-like DNA structures.",ATP-dependent DNA helicase that may be involved in DNA repair. Nucleus. Belongs to the helicase family. RAD3/XPD subfamily,Maybe,Yes,Yes,Yes,Maybe,Yes,GO:0043138; GO:0005524; GO:0000400; GO:0009378; GO:0016787,GO:0003678; GO:0005524,GO:0004386; GO:0005524,GO:0004003; GO:0005524,GO:0003678; GO:0005524,GO:0004386; GO:0005524,0.7379,0.678,0.7379,0.7379,0.678,5,0.7139,0.604,yes
FANCM_DROME,Q9VDA0,ProtTale,Eukaryota,1489,"A ssDNA-dependent ATPase with 3' to 5' helicase activity. Involved in multiple DNA-damage responses, some that require ATPase and helicase activity and some that are independent of these. Involved in DNA interstrand cross-link repair, probably together with Fancl and other Fanconi anemia pathway homologs. Independent of Fancl involved in DNA double strand break repair, including contributing to the synthesis-dependent strand annealing (SDSA) pathway. Probably contributes to SDSA by unwinding short duplex regions in complex D-loop-like DNA structures.","DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, binds double-stranded DNA (dsDNA), but not single-stranded DNA (ssDNA).",Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0043138; GO:0005524; GO:0000400; GO:0009378; GO:0016787,GO:0004386; GO:0005524; GO:0003690,GO:0003678; GO:0005524; GO:0003690,GO:0008094; GO:0003690; GO:0005524,GO:0003677; GO:0016887; GO:0005524,GO:0016887; GO:0005524; GO:0003690,0.7284,0.7808,0.6982,0.6067,0.5752,5,0.6779,0.604,yes
FANCM_DROME,Q9VDA0,Protein2Text,Eukaryota,1489,"A ssDNA-dependent ATPase with 3' to 5' helicase activity. Involved in multiple DNA-damage responses, some that require ATPase and helicase activity and some that are independent of these. Involved in DNA interstrand cross-link repair, probably together with Fancl and other Fanconi anemia pathway homologs. Independent of Fancl involved in DNA double strand break repair, including contributing to the synthesis-dependent strand annealing (SDSA) pathway. Probably contributes to SDSA by unwinding short duplex regions in complex D-loop-like DNA structures.","This protein is a helicase, which means it has the ability to unwind DNA or RNA into single strands. It is involved in various processes such as DNA replication, repair, and transcription, and is often associated with the maintenance of genome stability.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0043138; GO:0005524; GO:0000400; GO:0009378; GO:0016787,GO:0004386,GO:0004386,GO:0004386,GO:0004386,GO:0004386,0.4652,0.4652,0.4652,0.4652,0.4652,5,0.4652,0.604,yes
FANCM_DROME,Q9VDA0,Reference,Eukaryota,1489,"A ssDNA-dependent ATPase with 3' to 5' helicase activity. Involved in multiple DNA-damage responses, some that require ATPase and helicase activity and some that are independent of these. Involved in DNA interstrand cross-link repair, probably together with Fancl and other Fanconi anemia pathway homologs. Independent of Fancl involved in DNA double strand break repair, including contributing to the synthesis-dependent strand annealing (SDSA) pathway. Probably contributes to SDSA by unwinding short duplex regions in complex D-loop-like DNA structures.","A ssDNA-dependent ATPase with 3' to 5' helicase activity. Involved in multiple DNA-damage responses, some that require ATPase and helicase activity and some that are independent of these. Involved in DNA interstrand cross-link repair, probably together with Fancl and other Fanconi anemia pathway homologs. Independent of Fancl involved in DNA double strand break repair, including contributing to the synthesis-dependent strand annealing (SDSA) pathway. Probably contributes to SDSA by unwinding short duplex regions in complex D-loop-like DNA structures.",,,,,,,GO:0043138; GO:0005524; GO:0000400; GO:0009378; GO:0016787,GO:0003678; GO:0016887; GO:0005524; GO:0003697,GO:0004003; GO:0005524,GO:0003678; GO:0016887,GO:0004003; GO:0005524,GO:0003678; GO:0005524,0.7698,0.7379,0.5536,0.7379,0.7379,5,0.7074,0.604,yes
ENDUB_DROME,Q9VF14,ESM2Text,Eukaryota,322,"Endoribonuclease that cleaves single-stranded RNAs at uridylates and releases products that have 2'-3'-cyclic phosphate termini. Preferentially cleaves single stranded RNA at poly-U sites with CU, UC and AU sites cleaved less efficiently. May target mRNAs encoding proteins involved in lipid metabolism to regulate their expression. Regulates levels of TBPH protein, but not mRNA, by an as yet unknown mechanism. Important for neuronal development or function.","Involved in cell wall biogenesis. Has a role in the addition of Gal-beta1,3 moeities to galactomannans and their subsequent pyruvylation. Promotes the polymerization of unesterified enterobacterial common antigen (ECA).",No,No,No,No,No,not-Yes,GO:0016787; GO:0016829; GO:0046872; GO:0003723; GO:0004521,GO:0016757,,,,,0.3293,,,,,1,0.3293,0.2189,no
ENDUB_DROME,Q9VF14,Prot2Text,Eukaryota,322,"Endoribonuclease that cleaves single-stranded RNAs at uridylates and releases products that have 2'-3'-cyclic phosphate termini. Preferentially cleaves single stranded RNA at poly-U sites with CU, UC and AU sites cleaved less efficiently. May target mRNAs encoding proteins involved in lipid metabolism to regulate their expression. Regulates levels of TBPH protein, but not mRNA, by an as yet unknown mechanism. Important for neuronal development or function.",Epoxide hydrolase that catalyzes the stereo-specific epoxidation of beta-D-glucans. Plays a role in the developmental stage of the epidermis development. May affect epidermal cell wall organization and biogenesis.,No,No,No,No,No,not-Yes,GO:0016787; GO:0016829; GO:0046872; GO:0003723; GO:0004521,GO:0004301,GO:0004301,GO:0004301,GO:0004301,GO:0004301,0.3236,0.3236,0.3236,0.3236,0.3236,5,0.3236,0.2189,no
ENDUB_DROME,Q9VF14,ProtT3,Eukaryota,322,"Endoribonuclease that cleaves single-stranded RNAs at uridylates and releases products that have 2'-3'-cyclic phosphate termini. Preferentially cleaves single stranded RNA at poly-U sites with CU, UC and AU sites cleaved less efficiently. May target mRNAs encoding proteins involved in lipid metabolism to regulate their expression. Regulates levels of TBPH protein, but not mRNA, by an as yet unknown mechanism. Important for neuronal development or function.","Part of the gene cluster that mediates the biosynthesis of notoamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core. The first step of notoamide biosynthesis involves coupling of L-proline and L-tryptophan by the bimodular NRPS notE, to produce cyclo-L-tryptophan-L-proline called brevianamide F. The reverse prenyltransferase notD then catalyzes the conversion of brevianamide F to notoamide. Endoplasmic reticulum membrane; Multi-",No,No,No,No,No,not-Yes,GO:0016787; GO:0016829; GO:0046872; GO:0003723; GO:0004521,GO:0004659,GO:0004659,,GO:0004659,GO:0004659,0.2778,0.2778,,0.2778,0.2778,4,0.2778,0.2189,no
ENDUB_DROME,Q9VF14,ProtTale,Eukaryota,322,"Endoribonuclease that cleaves single-stranded RNAs at uridylates and releases products that have 2'-3'-cyclic phosphate termini. Preferentially cleaves single stranded RNA at poly-U sites with CU, UC and AU sites cleaved less efficiently. May target mRNAs encoding proteins involved in lipid metabolism to regulate their expression. Regulates levels of TBPH protein, but not mRNA, by an as yet unknown mechanism. Important for neuronal development or function.",Endoplasmic reticulum (ER)-bound glycosylphosphatidylinositol-N- acetylglucosaminyltransferase that catalyzes the transfer of an N-acetylglucosamine residue from UDP-N-acetyl-D-glucosamine to a serine or threonine residue and is involved in the remodeling of N-glycans.,No,No,No,No,No,not-Yes,GO:0016787; GO:0016829; GO:0046872; GO:0003723; GO:0004521,GO:0016757,GO:0016757,GO:0008375,GO:0017176,GO:0016757,0.3293,0.3293,0.2148,0.1961,0.3293,5,0.2798,0.2189,no
ENDUB_DROME,Q9VF14,Protein2Text,Eukaryota,322,"Endoribonuclease that cleaves single-stranded RNAs at uridylates and releases products that have 2'-3'-cyclic phosphate termini. Preferentially cleaves single stranded RNA at poly-U sites with CU, UC and AU sites cleaved less efficiently. May target mRNAs encoding proteins involved in lipid metabolism to regulate their expression. Regulates levels of TBPH protein, but not mRNA, by an as yet unknown mechanism. Important for neuronal development or function.","The molecular function of this protein is not specified in the provided information. However, based on its name and involvement in the defense system, it is likely that this protein is involved in mediating a cellular response to infection, possibly through its interaction with viral nucleocapsids. 
If you need more specific information, please provide more context or details about the protein.",No,Vague,Vague,Vague,No,not-Yes,GO:0016787; GO:0016829; GO:0046872; GO:0003723; GO:0004521,,,,,,,,,,,0,,0.2189,no
ENDUB_DROME,Q9VF14,Reference,Eukaryota,322,"Endoribonuclease that cleaves single-stranded RNAs at uridylates and releases products that have 2'-3'-cyclic phosphate termini. Preferentially cleaves single stranded RNA at poly-U sites with CU, UC and AU sites cleaved less efficiently. May target mRNAs encoding proteins involved in lipid metabolism to regulate their expression. Regulates levels of TBPH protein, but not mRNA, by an as yet unknown mechanism. Important for neuronal development or function.","Endoribonuclease that cleaves single-stranded RNAs at uridylates and releases products that have 2'-3'-cyclic phosphate termini. Preferentially cleaves single stranded RNA at poly-U sites with CU, UC and AU sites cleaved less efficiently. May target mRNAs encoding proteins involved in lipid metabolism to regulate their expression. Regulates levels of TBPH protein, but not mRNA, by an as yet unknown mechanism. Important for neuronal development or function.",,,,,,,GO:0016787; GO:0016829; GO:0046872; GO:0003723; GO:0004521,GO:0004521; GO:0003723,GO:0004521,GO:0004521,GO:0004521,GO:0004521,0.6943,0.4589,0.4589,0.4589,0.4589,5,0.506,0.2189,no
EXOSX_DROME,Q9VFF3,ESM2Text,Eukaryota,900,"Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. Degrades a large variety of non-coding RNAs that are processed by the exosome, such as pre-rRNAs and some small nucleolar RNAs (snoRNAs). Degrades transcripts derived from different types of heterochromatic repeats, such as subtelomeric minisatellites and simple gagaa repeats. Degrades transcripts derived from transposons and transposon fragments. Degrades chromatin-associated transcripts and contributes to the compaction of heterochromatin. Required for the efficient repair of DNA double-strand breaks via homologous recombination after irradiation. Required for cell proliferation and error-free mitosis.",3'-> 5'-exoribonuclease involved in the maturation of the 3' poly(A) tail of mRNA and probably also of some other RNAs. Its major role may be to assist the transfer of 3'-monophosphorylase activity from a 3'-terminal to a 5'-terminal manner on RNA.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0000175; GO:0046872; GO:0000166; GO:0003727,GO:0000175,GO:0000175,GO:0000175,GO:0000175,GO:0000175,0.4368,0.4368,0.4368,0.4368,0.4368,5,0.4368,0.4544,no
EXOSX_DROME,Q9VFF3,Prot2Text,Eukaryota,900,"Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. Degrades a large variety of non-coding RNAs that are processed by the exosome, such as pre-rRNAs and some small nucleolar RNAs (snoRNAs). Degrades transcripts derived from different types of heterochromatic repeats, such as subtelomeric minisatellites and simple gagaa repeats. Degrades transcripts derived from transposons and transposon fragments. Degrades chromatin-associated transcripts and contributes to the compaction of heterochromatin. Required for the efficient repair of DNA double-strand breaks via homologous recombination after irradiation. Required for cell proliferation and error-free mitosis.","Poly(A) nuclease with 3'-5' exoribonuclease activity involved in mRNA processing and decay. Triggers poly(A) tail removal from diverse mRNAs by acting as a key regulator of poly(A) length: able to trim poly(A) tails of RNA with 3'-5' exoribonuclease activity, but unable to remove uridylated or hydroxylated poly(A) tails. In contrast to the canonical TRIM28/SRIN1, does not inhibit the elongation of 3'-overhangs of mRNAs by its 3'-exonuclease activity. Does not cleave 'Lys-27' or 'Lys-36' of histone mRNA; does not bind histone mRNA.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0000175; GO:0046872; GO:0000166; GO:0003727,GO:0000175,GO:0000175,GO:0000175,GO:0000175,GO:0000175,0.4368,0.4368,0.4368,0.4368,0.4368,5,0.4368,0.4544,no
EXOSX_DROME,Q9VFF3,ProtT3,Eukaryota,900,"Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. Degrades a large variety of non-coding RNAs that are processed by the exosome, such as pre-rRNAs and some small nucleolar RNAs (snoRNAs). Degrades transcripts derived from different types of heterochromatic repeats, such as subtelomeric minisatellites and simple gagaa repeats. Degrades transcripts derived from transposons and transposon fragments. Degrades chromatin-associated transcripts and contributes to the compaction of heterochromatin. Required for the efficient repair of DNA double-strand breaks via homologous recombination after irradiation. Required for cell proliferation and error-free mitosis.","Probable catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class-",Yes,Yes,Yes,Yes,Yes,Yes,GO:0000175; GO:0046872; GO:0000166; GO:0003727,GO:0000175,GO:0000175,GO:0000175,GO:0000175,GO:0000175,0.4368,0.4368,0.4368,0.4368,0.4368,5,0.4368,0.4544,no
EXOSX_DROME,Q9VFF3,ProtTale,Eukaryota,900,"Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. Degrades a large variety of non-coding RNAs that are processed by the exosome, such as pre-rRNAs and some small nucleolar RNAs (snoRNAs). Degrades transcripts derived from different types of heterochromatic repeats, such as subtelomeric minisatellites and simple gagaa repeats. Degrades transcripts derived from transposons and transposon fragments. Degrades chromatin-associated transcripts and contributes to the compaction of heterochromatin. Required for the efficient repair of DNA double-strand breaks via homologous recombination after irradiation. Required for cell proliferation and error-free mitosis.","Probable ATP-dependent RNA helicase that plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Acts downstream of the piRNA metabolic process.",No,No,No,No,No,not-Yes,GO:0000175; GO:0046872; GO:0000166; GO:0003727,GO:0004386; GO:0005524,GO:0004386,GO:0004004; GO:0005524,GO:0003724; GO:0005524,GO:0003724; GO:0005524,0.3296,0.16,0.3401,0.3401,0.3401,5,0.302,0.4544,no
EXOSX_DROME,Q9VFF3,Protein2Text,Eukaryota,900,"Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. Degrades a large variety of non-coding RNAs that are processed by the exosome, such as pre-rRNAs and some small nucleolar RNAs (snoRNAs). Degrades transcripts derived from different types of heterochromatic repeats, such as subtelomeric minisatellites and simple gagaa repeats. Degrades transcripts derived from transposons and transposon fragments. Degrades chromatin-associated transcripts and contributes to the compaction of heterochromatin. Required for the efficient repair of DNA double-strand breaks via homologous recombination after irradiation. Required for cell proliferation and error-free mitosis.","The molecular function of this protein is a part of the spliceosome, which is a complex molecular machine that catalyzes the splicing of pre-mRNA. Specifically, it is involved in the removal of introns and the ligation of exons to form a mature mRNA molecule.",No,No,No,No,No,not-Yes,GO:0000175; GO:0046872; GO:0000166; GO:0003727,,,,,,,,,,,0,,0.4544,no
EXOSX_DROME,Q9VFF3,Reference,Eukaryota,900,"Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. Degrades a large variety of non-coding RNAs that are processed by the exosome, such as pre-rRNAs and some small nucleolar RNAs (snoRNAs). Degrades transcripts derived from different types of heterochromatic repeats, such as subtelomeric minisatellites and simple gagaa repeats. Degrades transcripts derived from transposons and transposon fragments. Degrades chromatin-associated transcripts and contributes to the compaction of heterochromatin. Required for the efficient repair of DNA double-strand breaks via homologous recombination after irradiation. Required for cell proliferation and error-free mitosis.","Catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. Degrades a large variety of non-coding RNAs that are processed by the exosome, such as pre-rRNAs and some small nucleolar RNAs (snoRNAs). Degrades transcripts derived from different types of heterochromatic repeats, such as subtelomeric minisatellites and simple gagaa repeats. Degrades transcripts derived from transposons and transposon fragments. Degrades chromatin-associated transcripts and contributes to the compaction of heterochromatin. Required for the efficient repair of DNA double-strand breaks via homologous recombination after irradiation. Required for cell proliferation and error-free mitosis.",,,,,,,GO:0000175; GO:0046872; GO:0000166; GO:0003727,GO:0000175,GO:0000175,GO:0000175,GO:0000175,GO:0000175,0.4368,0.4368,0.4368,0.4368,0.4368,5,0.4368,0.4544,no
KAD3_DROME,Q9VGU6,ESM2Text,Eukaryota,216,Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities.,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.,Yes,Yes,Yes,Maybe,Yes,Yes,GO:0004017; GO:0005524; GO:0005525; GO:0046899,GO:0004017; GO:0005524,GO:0004017,GO:0004017,GO:0004017,GO:0004017,0.912,0.5636,0.5636,0.5636,0.5636,5,0.6333,0.5847,yes
KAD3_DROME,Q9VGU6,Prot2Text,Eukaryota,216,Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities.,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.,Yes,Yes,Yes,Maybe,Yes,Yes,GO:0004017; GO:0005524; GO:0005525; GO:0046899,GO:0004017,GO:0004017,GO:0004017,GO:0004017,GO:0004017; GO:0005524,0.5636,0.5636,0.5636,0.5636,0.912,5,0.6333,0.5847,yes
KAD3_DROME,Q9VGU6,ProtT3,Eukaryota,216,Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities.,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. Mitochondrion matrix. Belongs to the adenylate kinase family. AK2 subfamily,Yes,Yes,Yes,Maybe,Yes,Yes,GO:0004017; GO:0005524; GO:0005525; GO:0046899,GO:0004017; GO:0005524,GO:0004017; GO:0005524,GO:0004017; GO:0005524,GO:0004017; GO:0005524,GO:0004017; GO:0005524,0.912,0.912,0.912,0.912,0.912,5,0.912,0.5847,yes
KAD3_DROME,Q9VGU6,ProtTale,Eukaryota,216,Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities.,Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.,Yes,Yes,Yes,Maybe,Yes,Yes,GO:0004017; GO:0005524; GO:0005525; GO:0046899,GO:0004017; GO:0005524,GO:0004017; GO:0005524,GO:0004017; GO:0005524,GO:0004017; GO:0005524,GO:0004017; GO:0005524,0.912,0.912,0.912,0.912,0.912,5,0.912,0.5847,yes
KAD3_DROME,Q9VGU6,Protein2Text,Eukaryota,216,Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities.,This protein is involved in the molecular function of ATP binding.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004017; GO:0005524; GO:0005525; GO:0046899,GO:0005524,GO:0005524,GO:0005524,GO:0005524,GO:0005524,0.5683,0.5683,0.5683,0.5683,0.5683,5,0.5683,0.5847,yes
KAD3_DROME,Q9VGU6,Reference,Eukaryota,216,Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities.,Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities.,,,,,,,GO:0004017; GO:0005524; GO:0005525; GO:0046899,GO:0016301,GO:0004017,GO:0016301,GO:0004017,GO:0004550,0.43,0.5636,0.43,0.5636,0.4873,5,0.4949,0.5847,yes
KDM3_DROME,Q9VHC5,ESM2Text,Eukaryota,854,"Histone demethylase that specifically demethylates 'Lys-10' of histone H3 (H3K9), thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate (Probable). Probably involved in regulation of chromatin structure, promoting expansion of euchromatin. Negatively regulates rhino-dependent piRNA production capacity of several genomic regions; may help define the frontiers of piRNA clusters by regulating histone methylation levels. May be involved in regulation of behavior and circadian rhythms.","Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36'.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0031490; GO:0032454; GO:0140683; GO:0046872; GO:0003712,GO:0032452,GO:0032452,GO:0032452,GO:0032452,GO:0032452,0.4225,0.4225,0.4225,0.4225,0.4225,5,0.4225,0.4107,no
KDM3_DROME,Q9VHC5,Prot2Text,Eukaryota,854,"Histone demethylase that specifically demethylates 'Lys-10' of histone H3 (H3K9), thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate (Probable). Probably involved in regulation of chromatin structure, promoting expansion of euchromatin. Negatively regulates rhino-dependent piRNA production capacity of several genomic regions; may help define the frontiers of piRNA clusters by regulating histone methylation levels. May be involved in regulation of behavior and circadian rhythms.","Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated H3 'Lys-4'. Involved in translesion DNA synthesis by catalyzing asymmetric dimethylation of H3 'Lys-9' on one of its own dimethylated repeats, while it has no activity on other dimethylated repeats.",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0031490; GO:0032454; GO:0140683; GO:0046872; GO:0003712,GO:0032452,GO:0032452,GO:0032452,GO:0032452,GO:0032452,0.4225,0.4225,0.4225,0.4225,0.4225,5,0.4225,0.4107,no
KDM3_DROME,Q9VHC5,ProtT3,Eukaryota,854,"Histone demethylase that specifically demethylates 'Lys-10' of histone H3 (H3K9), thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate (Probable). Probably involved in regulation of chromatin structure, promoting expansion of euchromatin. Negatively regulates rhino-dependent piRNA production capacity of several genomic regions; may help define the frontiers of piRNA clusters by regulating histone methylation levels. May be involved in regulation of behavior and circadian rhythms.","Protein-lysine N-methyltransferase that mono-, di- and trimethylates 'Lys-20' of histone H4, thereby playing a central role in histone code (By similarity). H4 'Lys-20' methylation represents a specific tag for epigenetic transcriptional activation and is also involved in X chromosome inactivation of female mammals (By similarity). Methylates 'Lys-20' of histone H4 to form monomethylated 'Lys-20' (H4K20me1), dimethylated 'Lys-20' (H4",No,No,No,No,No,not-Yes,GO:0031490; GO:0032454; GO:0140683; GO:0046872; GO:0003712,GO:0018024,GO:0018024,GO:0018024,GO:0018024,GO:0018024,0.0,0.0,0.0,0.0,0.0,5,0.0,0.4107,no
KDM3_DROME,Q9VHC5,ProtTale,Eukaryota,854,"Histone demethylase that specifically demethylates 'Lys-10' of histone H3 (H3K9), thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate (Probable). Probably involved in regulation of chromatin structure, promoting expansion of euchromatin. Negatively regulates rhino-dependent piRNA production capacity of several genomic regions; may help define the frontiers of piRNA clusters by regulating histone methylation levels. May be involved in regulation of behavior and circadian rhythms.","Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. Demethylates trimethylated and dimethylated H3 'Lys-27', but not monomethylated H3 'Lys-27'. May also demethylate mono- and dimethylated H3 'Lys-4'. Demethylase activity independent of its enzymatic activity as a histone lysine acetyltransferase (HAT). Also acts as a transcriptional corepressor. May act as a tumor suppressor.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0031490; GO:0032454; GO:0140683; GO:0046872; GO:0003712,GO:0071558; GO:0016706,GO:0071558; GO:0016706,GO:0032452,GO:0032452; GO:0004402,GO:0032452,0.4612,0.4612,0.4225,0.4071,0.4225,5,0.4349,0.4107,no
KDM3_DROME,Q9VHC5,Protein2Text,Eukaryota,854,"Histone demethylase that specifically demethylates 'Lys-10' of histone H3 (H3K9), thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate (Probable). Probably involved in regulation of chromatin structure, promoting expansion of euchromatin. Negatively regulates rhino-dependent piRNA production capacity of several genomic regions; may help define the frontiers of piRNA clusters by regulating histone methylation levels. May be involved in regulation of behavior and circadian rhythms.","This protein is involved in methylation, specifically as a component of the DNA methyltransferase complex. It is likely involved in adding methyl groups to DNA, which can affect gene expression and other cellular processes.",No,No,No,No,No,not-Yes,GO:0031490; GO:0032454; GO:0140683; GO:0046872; GO:0003712,GO:0003886,GO:0008168,GO:0009008,GO:0008168,GO:0008168,0.0992,0.1474,0.1191,0.1474,0.1474,5,0.1321,0.4107,no
KDM3_DROME,Q9VHC5,Reference,Eukaryota,854,"Histone demethylase that specifically demethylates 'Lys-10' of histone H3 (H3K9), thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate (Probable). Probably involved in regulation of chromatin structure, promoting expansion of euchromatin. Negatively regulates rhino-dependent piRNA production capacity of several genomic regions; may help define the frontiers of piRNA clusters by regulating histone methylation levels. May be involved in regulation of behavior and circadian rhythms.","Histone demethylase that specifically demethylates 'Lys-10' of histone H3 (H3K9), thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate (Probable). Probably involved in regulation of chromatin structure, promoting expansion of euchromatin. Negatively regulates rhino-dependent piRNA production capacity of several genomic regions; may help define the frontiers of piRNA clusters by regulating histone methylation levels. May be involved in regulation of behavior and circadian rhythms.",,,,,,,GO:0031490; GO:0032454; GO:0140683; GO:0046872; GO:0003712,GO:0032452,GO:0032454,GO:0016706; GO:0032452,GO:0032452; GO:0016706,GO:0032452; GO:0016706,0.4225,0.4952,0.4596,0.4596,0.4596,5,0.4593,0.4107,no
ZDH23_DROME,Q9VQK9,ESM2Text,Eukaryota,420,"Essential for the activity of the beta1,4-N- acetylgalactosaminyltransferase beta4GalNAcTB during glycolipid elongation. Association with beta4GalNAcTB is required for targeting its localization from the ER to the Golgi as well as its glycosyltransferase activity in the Golgi.",Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes.,No,No,No,No,No,not-Yes,GO:0008047; GO:0140597; GO:0019706,GO:0016409,GO:0016409,GO:0016409,GO:0016409,GO:0016409,0.4145,0.4145,0.4145,0.4145,0.4145,5,0.4145,0.3751,no
ZDH23_DROME,Q9VQK9,Prot2Text,Eukaryota,420,"Essential for the activity of the beta1,4-N- acetylgalactosaminyltransferase beta4GalNAcTB during glycolipid elongation. Association with beta4GalNAcTB is required for targeting its localization from the ER to the Golgi as well as its glycosyltransferase activity in the Golgi.",Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates.,No,No,No,No,No,not-Yes,GO:0008047; GO:0140597; GO:0019706,GO:0019706,GO:0019706,GO:0016409,GO:0016409,GO:0016409,0.5526,0.5526,0.4145,0.4145,0.4145,5,0.4697,0.3751,no
ZDH23_DROME,Q9VQK9,ProtT3,Eukaryota,420,"Essential for the activity of the beta1,4-N- acetylgalactosaminyltransferase beta4GalNAcTB during glycolipid elongation. Association with beta4GalNAcTB is required for targeting its localization from the ER to the Golgi as well as its glycosyltransferase activity in the Golgi.",Palmitoyl acyltransferase. Endoplasmic reticulum membrane; Multi-pass membrane protein. Belongs to the DHHC palmitoyltransferase family,No,No,No,No,No,not-Yes,GO:0008047; GO:0140597; GO:0019706,GO:0016409,GO:0016409,GO:0016409,GO:0016409,GO:0016409,0.4145,0.4145,0.4145,0.4145,0.4145,5,0.4145,0.3751,no
ZDH23_DROME,Q9VQK9,ProtTale,Eukaryota,420,"Essential for the activity of the beta1,4-N- acetylgalactosaminyltransferase beta4GalNAcTB during glycolipid elongation. Association with beta4GalNAcTB is required for targeting its localization from the ER to the Golgi as well as its glycosyltransferase activity in the Golgi.",Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes.,No,No,No,No,No,not-Yes,GO:0008047; GO:0140597; GO:0019706,GO:0016409,GO:0016409,GO:0016409,GO:0016746,GO:0016409,0.4145,0.4145,0.4145,0.349,0.4145,5,0.4014,0.3751,no
ZDH23_DROME,Q9VQK9,Protein2Text,Eukaryota,420,"Essential for the activity of the beta1,4-N- acetylgalactosaminyltransferase beta4GalNAcTB during glycolipid elongation. Association with beta4GalNAcTB is required for targeting its localization from the ER to the Golgi as well as its glycosyltransferase activity in the Golgi.","This protein is involved in catalyzing the addition of palmitate to ceramide, producing ceramide-palmitoylphosphates, which are the precursors of sphingomyelin.",No,No,No,No,No,not-Yes,GO:0008047; GO:0140597; GO:0019706,,GO:0016746,,GO:0016746,,,0.349,,0.349,,2,0.349,0.3751,no
ZDH23_DROME,Q9VQK9,Reference,Eukaryota,420,"Essential for the activity of the beta1,4-N- acetylgalactosaminyltransferase beta4GalNAcTB during glycolipid elongation. Association with beta4GalNAcTB is required for targeting its localization from the ER to the Golgi as well as its glycosyltransferase activity in the Golgi.","Essential for the activity of the beta1,4-N- acetylgalactosaminyltransferase beta4GalNAcTB during glycolipid elongation. Association with beta4GalNAcTB is required for targeting its localization from the ER to the Golgi as well as its glycosyltransferase activity in the Golgi.",,,,,,,GO:0008047; GO:0140597; GO:0019706,,,,,,,,,,,0,,0.3751,no
PTPA_DROME,Q9VQQ0,ESM2Text,Eukaryota,398,"PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A). Modulates PP2A activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Acts as mediator for the basal localization of the Miranda (Mira) complex during mitosis of larval neuroblast asymmetric division. Associates with the phosphatase 4 (PP4) complex to mediate basal localization of Mira; probably by facilitating the dephosphorylation of Mira. Cortical association of Mira mediated by the PTPA- PP4 complex seems to be independent of aPKC activity.","Plays a role in regulating membrane trafficking of cargo proteins. Together with ATPase epsilon, regulates SNX3 retromer-mediated endosomal sorting of WLS away from lysosomal degradation.",No,No,No,No,No,not-Yes,GO:0005524; GO:0046872; GO:0003755; GO:0008160,,,,,,,,,,,0,,0.3832,no
PTPA_DROME,Q9VQQ0,Prot2Text,Eukaryota,398,"PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A). Modulates PP2A activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Acts as mediator for the basal localization of the Miranda (Mira) complex during mitosis of larval neuroblast asymmetric division. Associates with the phosphatase 4 (PP4) complex to mediate basal localization of Mira; probably by facilitating the dephosphorylation of Mira. Cortical association of Mira mediated by the PTPA- PP4 complex seems to be independent of aPKC activity.",May regulate the transcriptional activity of kinases and regulate the activity of PKA-1.,No,No,Vague,No,No,not-Yes,GO:0005524; GO:0046872; GO:0003755; GO:0008160,,,,,,,,,,,0,,0.3832,no
PTPA_DROME,Q9VQQ0,ProtT3,Eukaryota,398,"PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A). Modulates PP2A activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Acts as mediator for the basal localization of the Miranda (Mira) complex during mitosis of larval neuroblast asymmetric division. Associates with the phosphatase 4 (PP4) complex to mediate basal localization of Mira; probably by facilitating the dephosphorylation of Mira. Cortical association of Mira mediated by the PTPA- PP4 complex seems to be independent of aPKC activity.","PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A- phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity). Cytoplasm Nucleus",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0046872; GO:0003755; GO:0008160,GO:0003755,GO:0003755,GO:0003755,GO:0003755,GO:0003755,0.4496,0.4496,0.4496,0.4496,0.4496,5,0.4496,0.3832,no
PTPA_DROME,Q9VQQ0,ProtTale,Eukaryota,398,"PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A). Modulates PP2A activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Acts as mediator for the basal localization of the Miranda (Mira) complex during mitosis of larval neuroblast asymmetric division. Associates with the phosphatase 4 (PP4) complex to mediate basal localization of Mira; probably by facilitating the dephosphorylation of Mira. Cortical association of Mira mediated by the PTPA- PP4 complex seems to be independent of aPKC activity.","Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template. May act as a chaperone for newly synthesized free N protein, so-called N(0). Plays a role in virion assembly.",No,No,No,No,No,not-Yes,GO:0005524; GO:0046872; GO:0003755; GO:0008160,,,,,GO:0003723,,,,,0.193,1,0.193,0.3832,no
PTPA_DROME,Q9VQQ0,Protein2Text,Eukaryota,398,"PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A). Modulates PP2A activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Acts as mediator for the basal localization of the Miranda (Mira) complex during mitosis of larval neuroblast asymmetric division. Associates with the phosphatase 4 (PP4) complex to mediate basal localization of Mira; probably by facilitating the dephosphorylation of Mira. Cortical association of Mira mediated by the PTPA- PP4 complex seems to be independent of aPKC activity.","The molecular function of this protein is involved in the hydrolysis of GTP. It is a GTPase activator, specifically for the GTPase domain of Rab family proteins. The protein catalyzes the hydrolysis of GTP to GDP, which is necessary for the regulation of various cellular processes, such as vesicle trafficking and signaling pathways.",No,No,No,No,No,not-Yes,GO:0005524; GO:0046872; GO:0003755; GO:0008160,GO:0005096,GO:0005096,GO:0005096,GO:0005097,GO:0005097,0.2255,0.2255,0.2255,0.2255,0.2255,5,0.2255,0.3832,no
PTPA_DROME,Q9VQQ0,Reference,Eukaryota,398,"PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A). Modulates PP2A activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Acts as mediator for the basal localization of the Miranda (Mira) complex during mitosis of larval neuroblast asymmetric division. Associates with the phosphatase 4 (PP4) complex to mediate basal localization of Mira; probably by facilitating the dephosphorylation of Mira. Cortical association of Mira mediated by the PTPA- PP4 complex seems to be independent of aPKC activity.","PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A). Modulates PP2A activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Acts as mediator for the basal localization of the Miranda (Mira) complex during mitosis of larval neuroblast asymmetric division. Associates with the phosphatase 4 (PP4) complex to mediate basal localization of Mira; probably by facilitating the dephosphorylation of Mira. Cortical association of Mira mediated by the PTPA- PP4 complex seems to be independent of aPKC activity.",,,,,,,GO:0005524; GO:0046872; GO:0003755; GO:0008160,GO:0003755,GO:0003755,GO:0003755,GO:0003755,GO:0003755,0.4496,0.4496,0.4496,0.4496,0.4496,5,0.4496,0.3832,no
HELQ_DROME,Q9VSE2,ESM2Text,Eukaryota,1051,"Single-stranded 3'-5' DNA helicase that plays a key role in homology-driven double-strand break (DSB) repair. Involved in different DSB repair mechanisms that are guided by annealing of extensive stretches of complementary bases at break ends, such as microhomology-mediated end-joining (MMEJ), single-strand annealing (SSA) or synthesis-dependent strand annealing (SDSA).","ATP-dependent DNA helicase that unwinds single- and double-stranded DNA in a 3' to 5' direction. Participates in DNA replication and repair. Mediates the ATP-dependent nucleotide excision repair (BER) pathway, which allows RNA polymerase II to complete synthesis of duplex DNA. Also has a role in meiosis.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0003677; GO:0016787; GO:1990518,GO:0003678; GO:0005524,GO:0004003; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,0.6764,0.6764,0.6764,0.6764,0.6764,5,0.6764,0.6329,yes
HELQ_DROME,Q9VSE2,Prot2Text,Eukaryota,1051,"Single-stranded 3'-5' DNA helicase that plays a key role in homology-driven double-strand break (DSB) repair. Involved in different DSB repair mechanisms that are guided by annealing of extensive stretches of complementary bases at break ends, such as microhomology-mediated end-joining (MMEJ), single-strand annealing (SSA) or synthesis-dependent strand annealing (SDSA).","Central component of the replication factor C (RFC) complex, a complex required for replication of chromosome termini that is essential for the replication of mitochondrial DNA. RFC has an ATPase activity that is stimulated by single-stranded DNA, replication factor C (RFC) and replication factor B (RFC), but abolished in presence of DNA. Acts as a key regulator of RFC stability. Acts as a key regulator of DNA replication forks by mediating the fork regression process and preventing the propagation of stalled replication forks.",No,No,No,No,No,not-Yes,GO:0005524; GO:0003677; GO:0016787; GO:1990518,GO:0016887,GO:0016887; GO:0003689,GO:0016887; GO:0003689,GO:0016887,GO:0008094; GO:0005524,0.2645,0.3593,0.3593,0.2645,0.6202,5,0.3736,0.6329,yes
HELQ_DROME,Q9VSE2,ProtT3,Eukaryota,1051,"Single-stranded 3'-5' DNA helicase that plays a key role in homology-driven double-strand break (DSB) repair. Involved in different DSB repair mechanisms that are guided by annealing of extensive stretches of complementary bases at break ends, such as microhomology-mediated end-joining (MMEJ), single-strand annealing (SSA) or synthesis-dependent strand annealing (SDSA).",Probable ATP-dependent DNA helicase. Nucleus. Belongs to the DEAD box helicase family. DEAH subfamily,Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0003677; GO:0016787; GO:1990518,GO:0004386; GO:0005524,GO:0004386; GO:0005524,GO:0004003; GO:0005524,GO:0004386; GO:0005524,GO:0004386; GO:0005524,0.6422,0.6422,0.6764,0.6422,0.6422,5,0.649,0.6329,yes
HELQ_DROME,Q9VSE2,ProtTale,Eukaryota,1051,"Single-stranded 3'-5' DNA helicase that plays a key role in homology-driven double-strand break (DSB) repair. Involved in different DSB repair mechanisms that are guided by annealing of extensive stretches of complementary bases at break ends, such as microhomology-mediated end-joining (MMEJ), single-strand annealing (SSA) or synthesis-dependent strand annealing (SDSA).",ATP-dependent DNA helicase important for chromosome transmission and normal cell cycle progression in G(2)/M. Also has 5'-3' helicase activity and unwinds dsDNA in the 5' to 3' direction.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0003677; GO:0016787; GO:1990518,GO:0004386; GO:0005524; GO:0003677,GO:0004386; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,0.8125,0.6422,0.6764,0.6764,0.6764,5,0.6968,0.6329,yes
HELQ_DROME,Q9VSE2,Protein2Text,Eukaryota,1051,"Single-stranded 3'-5' DNA helicase that plays a key role in homology-driven double-strand break (DSB) repair. Involved in different DSB repair mechanisms that are guided by annealing of extensive stretches of complementary bases at break ends, such as microhomology-mediated end-joining (MMEJ), single-strand annealing (SSA) or synthesis-dependent strand annealing (SDSA).","The molecular function of this protein is that of a helicase, which is a type of enzyme that unwinds DNA or RNA molecules. More specifically, this protein is a DNA helicase, meaning it unwinds DNA.",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0003677; GO:0016787; GO:1990518,GO:0004003,GO:0003678,GO:0003678,GO:0003678,GO:0003678,0.4101,0.4101,0.4101,0.4101,0.4101,5,0.4101,0.6329,yes
HELQ_DROME,Q9VSE2,Reference,Eukaryota,1051,"Single-stranded 3'-5' DNA helicase that plays a key role in homology-driven double-strand break (DSB) repair. Involved in different DSB repair mechanisms that are guided by annealing of extensive stretches of complementary bases at break ends, such as microhomology-mediated end-joining (MMEJ), single-strand annealing (SSA) or synthesis-dependent strand annealing (SDSA).","Single-stranded 3'-5' DNA helicase that plays a key role in homology-driven double-strand break (DSB) repair. Involved in different DSB repair mechanisms that are guided by annealing of extensive stretches of complementary bases at break ends, such as microhomology-mediated end-joining (MMEJ), single-strand annealing (SSA) or synthesis-dependent strand annealing (SDSA).",,,,,,,GO:0005524; GO:0003677; GO:0016787; GO:1990518,GO:0003678; GO:0003697,GO:0003678,GO:0003678,GO:0004386; GO:0003697,GO:0003678; GO:0005524,0.6198,0.4101,0.4101,0.5855,0.6764,5,0.5404,0.6329,yes
JMJD7_DROME,Q9VU77,ESM2Text,Eukaryota,316,"Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monooxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Hydroxylates the guanylate binding protein 128up. May be involved in regulation of behavior and circadian rhythms.","Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). Involved in abscisic acid (ABA) transport in vitro.",No,No,No,No,No,not-Yes,GO:0016706; GO:0004175; GO:0008198; GO:0042802; GO:0106155,,,GO:0017056,,,,,0.1688,,,1,0.1688,0.3728,no
JMJD7_DROME,Q9VU77,Prot2Text,Eukaryota,316,"Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monooxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Hydroxylates the guanylate binding protein 128up. May be involved in regulation of behavior and circadian rhythms.","Functions as an oxygenase that repairs alkylated DNA containing carbonyl groups and promotes the maintenance of DNA backbone. Acts by catalyzing hydroxylation of double-stranded DNA substrates on which the carbonyl group is removed, resulting in the formation of DNA with a free 3' phosphate.",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0016706; GO:0004175; GO:0008198; GO:0042802; GO:0106155,GO:0051213,,GO:0051213,GO:0016491,GO:0016706,0.4463,,0.4463,0.4043,0.5396,4,0.4591,0.3728,no
JMJD7_DROME,Q9VU77,ProtT3,Eukaryota,316,"Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monooxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Hydroxylates the guanylate binding protein 128up. May be involved in regulation of behavior and circadian rhythms.",Alpha-ketoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0016706; GO:0004175; GO:0008198; GO:0042802; GO:0106155,GO:0016706,GO:0016706,GO:0016706,GO:0016706; GO:0005506,GO:0016706,0.5396,0.5396,0.5396,0.719,0.5396,5,0.5755,0.3728,no
JMJD7_DROME,Q9VU77,ProtTale,Eukaryota,316,"Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monooxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Hydroxylates the guanylate binding protein 128up. May be involved in regulation of behavior and circadian rhythms.",Catalyzes the oxidation of guanine to xanthine and of hypoxanthine to xanthosine. Also catalyzes the reverse reactions. May function as a regulator of the purine salvage pathway.,No,No,No,No,No,not-Yes,GO:0016706; GO:0004175; GO:0008198; GO:0042802; GO:0106155,GO:0004731,GO:0004731,GO:0004854,GO:0004854,GO:0004854,0.1726,0.1726,0.2393,0.2393,0.2393,5,0.2126,0.3728,no
JMJD7_DROME,Q9VU77,Protein2Text,Eukaryota,316,"Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monooxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Hydroxylates the guanylate binding protein 128up. May be involved in regulation of behavior and circadian rhythms.","The molecular function of this protein is not explicitly stated in the provided information. However, based on its classification as a protein, it is likely involved in a molecular function such as catalysis, binding, or regulation. Further research would be necessary to determine the specific molecular function of this protein.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016706; GO:0004175; GO:0008198; GO:0042802; GO:0106155,,,,,,,,,,,0,,0.3728,no
JMJD7_DROME,Q9VU77,Reference,Eukaryota,316,"Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monooxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Hydroxylates the guanylate binding protein 128up. May be involved in regulation of behavior and circadian rhythms.","Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monooxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Hydroxylates the guanylate binding protein 128up. May be involved in regulation of behavior and circadian rhythms.",,,,,,,GO:0016706; GO:0004175; GO:0008198; GO:0042802; GO:0106155,GO:0004175; GO:0016706,GO:0004175; GO:0016706,GO:0004175; GO:0016706,GO:0004175; GO:0016706,GO:0004175; GO:0016706,0.7166,0.7166,0.7166,0.7166,0.7166,5,0.7166,0.3728,no
KDM8_DROME,Q9W0M3,ESM2Text,Eukaryota,401,Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monooxygenase. May be involved in regulation of behavior and circadian rhythms.,E3 ubiquitin-protein ligase that probably functions in a post-translational process of degradation. Involved in regulation of microRNA (miRNA) biogenesis. May act by stabilizing microRNAs (miRNAs) and biogenesis of long-lived miRNAs (bmiRNAs).,No,No,No,No,No,not-Yes,GO:0003682; GO:0051864; GO:0016787; GO:0046872; GO:0106157,GO:0061630,GO:0004842,GO:0061630,GO:0061630,GO:0061630,0.2002,0.2394,0.2002,0.2002,0.2002,5,0.208,0.2563,no
KDM8_DROME,Q9W0M3,Prot2Text,Eukaryota,401,Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monooxygenase. May be involved in regulation of behavior and circadian rhythms.,Functions as an E3 ubiquitin ligase. Involved in the post-translational regulation of Nod factor receptor (NR) signaling. Post-translational regulation depends on recognition of a C-terminal extension of the N-terminal aspartate-semialdehyde (ASA) moiety by the CCR4-NOT complex. Acts as a negative regulator of NR-mediated ASA signal transduction by mediating ubiquitination and subsequent proteasomal degradation of the transcription factor Nod (Nod). Acts as a positive regulator of NR-mediated ASA signal transduction by mediating ubiquitination and subsequent degradation of the transcription factor Nod (Nod). Acts as a negative regulator of the Toll-like receptor (TLR) signaling by mediating ubiquitination and subsequent degradation of the transcription factor (Nod). Acts as a positive regulator of NF-kappa-B signaling by mediating ubiquitination and subsequent degradation of the NF-kappa-B subunit RELA.,No,No,No,No,No,not-Yes,GO:0003682; GO:0051864; GO:0016787; GO:0046872; GO:0106157,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.2002,0.2002,0.2002,0.2002,0.2002,5,0.2002,0.2563,no
KDM8_DROME,Q9W0M3,ProtT3,Eukaryota,401,Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monooxygenase. May be involved in regulation of behavior and circadian rhythms.,"Histone demethylase that specifically demethylates dimethylated 'Lys-9' of histone H3 (H3K9me2), a specific tag for epigenetic transcriptional activation, thereby playing a central role in epigenetic regulation. Nucleus",No,No,No,No,No,not-Yes,GO:0003682; GO:0051864; GO:0016787; GO:0046872; GO:0106157,GO:0032452,GO:0032452,GO:0032452,GO:0032454,GO:0032452,0.365,0.365,0.365,0.3363,0.365,5,0.3593,0.2563,no
KDM8_DROME,Q9W0M3,ProtTale,Eukaryota,401,Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monooxygenase. May be involved in regulation of behavior and circadian rhythms.,Probable ADP-ribosylase that may play a role in response to DNA damage. May play a role in DNA damage response by mediating ADP-ribosylation of histones H2A and H2AX. ADP-ribosylation of histones is a key step in the DNA damage response by promoting DNA repair and early events of cellular differentiation. Acts as a suppressor of apoptosis.,No,No,No,No,No,not-Yes,GO:0003682; GO:0051864; GO:0016787; GO:0046872; GO:0106157,GO:0003950,GO:0003950,GO:0003950,GO:0003950,GO:0003950,0.2154,0.2154,0.2154,0.2154,0.2154,5,0.2154,0.2563,no
KDM8_DROME,Q9W0M3,Protein2Text,Eukaryota,401,Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monooxygenase. May be involved in regulation of behavior and circadian rhythms.,"The molecular function of this protein is a desulfurase, which means it is involved in the removal of sulfur atoms from molecules. Specifically, it is responsible for the desulfuration of L-cysteine to L-alanine.",No,No,No,No,No,not-Yes,GO:0003682; GO:0051864; GO:0016787; GO:0046872; GO:0106157,GO:0031071,GO:0031071,GO:0031071,GO:0031071,GO:0031071,0.2154,0.2154,0.2154,0.2154,0.2154,5,0.2154,0.2563,no
KDM8_DROME,Q9W0M3,Reference,Eukaryota,401,Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monooxygenase. May be involved in regulation of behavior and circadian rhythms.,Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monooxygenase. May be involved in regulation of behavior and circadian rhythms.,,,,,,,GO:0003682; GO:0051864; GO:0016787; GO:0046872; GO:0106157,GO:0004175; GO:0016706,GO:0004175; GO:0016706,GO:0004175; GO:0016706,GO:0004175; GO:0016706,GO:0004175; GO:0016706,0.5381,0.5381,0.5381,0.5381,0.5381,5,0.5381,0.2563,no
PI5K1_DROME,Q9W2R3,ESM2Text,Eukaryota,792,"Catalyzes the phosphorylation of phosphatidylinositol 4- phosphate (PtdIns[4]P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns[4,5]P(2)), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility. PtdIns[4,5]P(2) can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns[3,4,5]P(3)). Required for germline development during oogenesis. Sktl is the major phosphatidylinositol 4-phosphate 5-kinase responsible for enrichment of PtdIns[4,5]P(2) in the apical plasma membrane of the oocyte and follicular epithelium cells of the egg chamber during oogenesis. Involved in nuclear anchoring and microtubule organization required for targeted mRNA transport during maintenance of oocyte polarity. The PtdIns[4,5]P(2) produced by sktl is required for maintenance of cellular polarity, prevention of the epithelial-mesenchymal transition process, maintenance of adherens junctions and regulation of apical constriction, probably by affecting polarized cortical recruitment of PAR proteins and their effectors, including baz/bazooka, aPKC, par-1 and l(2)gl. Involved in actin cytoskeleton organization probably through PtdIns[4,5]P(2)-mediated regulation of Moe/Moesin phosphorylation. Involved in PtdIns[4,5]P(2)-mediated apical recruitment of the formin dia/diaphanous in tubular epithelial cells. Involved in anterodorsal cell morphogenesis and eggshell dorsal appendage formation, probably through regulation of apical constriction by PtdIns[4,5]P(2) during tubulogenesis. Required for cell viability or proliferation during wing and eye imaginal disk development. May be involved in cytoskeletal regulation during sensory bristle development. Together with mys/integrin beta localizes to the trailing edge of larval epidermal cells in a JNK signaling-dependent manner during wound healing and is required for setting up cell polarity and re-epithelialization. Required for polarization of elongating spermatid cysts possibly by generation of PtdIns[4,5]P(2) involved in mediating membrane association and orientation of the nucleus-basal body pair. Probably involved in PtdIns[4,5]P(2)-mediated recruitment of exocyst proteins that may mediate membrane addition during spermatid elongation. Involved in maintenance of specialised cell contacts known as slit diaphragms required for nephrocyte morphogenesis and function. Regulates nephrocyte endocytosis, possibly through PtdIns[4,5]P(2)-mediated recruitment of effector proteins. Not required for nervous system development or neurotransmitter release at the neuromuscular junction. Together with ash2 probably plays a role in maintenance of transcriptionally active chromatin through down- regulation of histone H1 hyperphosphorylation.",May be involved in protein phosphatase activity.,Vague,No,No,No,No,not-Yes,GO:0016308,,GO:0004721,,,,,0.1672,,,,1,0.1672,0.4277,no
PI5K1_DROME,Q9W2R3,Prot2Text,Eukaryota,792,"Catalyzes the phosphorylation of phosphatidylinositol 4- phosphate (PtdIns[4]P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns[4,5]P(2)), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility. PtdIns[4,5]P(2) can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns[3,4,5]P(3)). Required for germline development during oogenesis. Sktl is the major phosphatidylinositol 4-phosphate 5-kinase responsible for enrichment of PtdIns[4,5]P(2) in the apical plasma membrane of the oocyte and follicular epithelium cells of the egg chamber during oogenesis. Involved in nuclear anchoring and microtubule organization required for targeted mRNA transport during maintenance of oocyte polarity. The PtdIns[4,5]P(2) produced by sktl is required for maintenance of cellular polarity, prevention of the epithelial-mesenchymal transition process, maintenance of adherens junctions and regulation of apical constriction, probably by affecting polarized cortical recruitment of PAR proteins and their effectors, including baz/bazooka, aPKC, par-1 and l(2)gl. Involved in actin cytoskeleton organization probably through PtdIns[4,5]P(2)-mediated regulation of Moe/Moesin phosphorylation. Involved in PtdIns[4,5]P(2)-mediated apical recruitment of the formin dia/diaphanous in tubular epithelial cells. Involved in anterodorsal cell morphogenesis and eggshell dorsal appendage formation, probably through regulation of apical constriction by PtdIns[4,5]P(2) during tubulogenesis. Required for cell viability or proliferation during wing and eye imaginal disk development. May be involved in cytoskeletal regulation during sensory bristle development. Together with mys/integrin beta localizes to the trailing edge of larval epidermal cells in a JNK signaling-dependent manner during wound healing and is required for setting up cell polarity and re-epithelialization. Required for polarization of elongating spermatid cysts possibly by generation of PtdIns[4,5]P(2) involved in mediating membrane association and orientation of the nucleus-basal body pair. Probably involved in PtdIns[4,5]P(2)-mediated recruitment of exocyst proteins that may mediate membrane addition during spermatid elongation. Involved in maintenance of specialised cell contacts known as slit diaphragms required for nephrocyte morphogenesis and function. Regulates nephrocyte endocytosis, possibly through PtdIns[4,5]P(2)-mediated recruitment of effector proteins. Not required for nervous system development or neurotransmitter release at the neuromuscular junction. Together with ash2 probably plays a role in maintenance of transcriptionally active chromatin through down- regulation of histone H1 hyperphosphorylation.",May be involved in signaling events that underlie chemotaxis via the chemoattractant-mediated pkgB phosphorylation.,No,No,No,No,No,not-Yes,GO:0016308,,,,,,,,,,,0,,0.4277,no
PI5K1_DROME,Q9W2R3,ProtT3,Eukaryota,792,"Catalyzes the phosphorylation of phosphatidylinositol 4- phosphate (PtdIns[4]P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns[4,5]P(2)), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility. PtdIns[4,5]P(2) can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns[3,4,5]P(3)). Required for germline development during oogenesis. Sktl is the major phosphatidylinositol 4-phosphate 5-kinase responsible for enrichment of PtdIns[4,5]P(2) in the apical plasma membrane of the oocyte and follicular epithelium cells of the egg chamber during oogenesis. Involved in nuclear anchoring and microtubule organization required for targeted mRNA transport during maintenance of oocyte polarity. The PtdIns[4,5]P(2) produced by sktl is required for maintenance of cellular polarity, prevention of the epithelial-mesenchymal transition process, maintenance of adherens junctions and regulation of apical constriction, probably by affecting polarized cortical recruitment of PAR proteins and their effectors, including baz/bazooka, aPKC, par-1 and l(2)gl. Involved in actin cytoskeleton organization probably through PtdIns[4,5]P(2)-mediated regulation of Moe/Moesin phosphorylation. Involved in PtdIns[4,5]P(2)-mediated apical recruitment of the formin dia/diaphanous in tubular epithelial cells. Involved in anterodorsal cell morphogenesis and eggshell dorsal appendage formation, probably through regulation of apical constriction by PtdIns[4,5]P(2) during tubulogenesis. Required for cell viability or proliferation during wing and eye imaginal disk development. May be involved in cytoskeletal regulation during sensory bristle development. Together with mys/integrin beta localizes to the trailing edge of larval epidermal cells in a JNK signaling-dependent manner during wound healing and is required for setting up cell polarity and re-epithelialization. Required for polarization of elongating spermatid cysts possibly by generation of PtdIns[4,5]P(2) involved in mediating membrane association and orientation of the nucleus-basal body pair. Probably involved in PtdIns[4,5]P(2)-mediated recruitment of exocyst proteins that may mediate membrane addition during spermatid elongation. Involved in maintenance of specialised cell contacts known as slit diaphragms required for nephrocyte morphogenesis and function. Regulates nephrocyte endocytosis, possibly through PtdIns[4,5]P(2)-mediated recruitment of effector proteins. Not required for nervous system development or neurotransmitter release at the neuromuscular junction. Together with ash2 probably plays a role in maintenance of transcriptionally active chromatin through down- regulation of histone H1 hyperphosphorylation.","Catalyzes the phosphorylation of phosphatidylinositol 4- phosphate (PtdIns(4)P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). PtdIns(4,5)P2 is a precursor of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3), two second messengers involved in many cellular processes. Cytoplasm",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016308,GO:0016308; GO:0005524,GO:0016308,GO:0016308; GO:0005524,GO:0016308; GO:0005524,GO:0016308; GO:0005524,0.6819,1.0,0.6819,0.6819,0.6819,5,0.7455,0.4277,no
PI5K1_DROME,Q9W2R3,ProtTale,Eukaryota,792,"Catalyzes the phosphorylation of phosphatidylinositol 4- phosphate (PtdIns[4]P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns[4,5]P(2)), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility. PtdIns[4,5]P(2) can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns[3,4,5]P(3)). Required for germline development during oogenesis. Sktl is the major phosphatidylinositol 4-phosphate 5-kinase responsible for enrichment of PtdIns[4,5]P(2) in the apical plasma membrane of the oocyte and follicular epithelium cells of the egg chamber during oogenesis. Involved in nuclear anchoring and microtubule organization required for targeted mRNA transport during maintenance of oocyte polarity. The PtdIns[4,5]P(2) produced by sktl is required for maintenance of cellular polarity, prevention of the epithelial-mesenchymal transition process, maintenance of adherens junctions and regulation of apical constriction, probably by affecting polarized cortical recruitment of PAR proteins and their effectors, including baz/bazooka, aPKC, par-1 and l(2)gl. Involved in actin cytoskeleton organization probably through PtdIns[4,5]P(2)-mediated regulation of Moe/Moesin phosphorylation. Involved in PtdIns[4,5]P(2)-mediated apical recruitment of the formin dia/diaphanous in tubular epithelial cells. Involved in anterodorsal cell morphogenesis and eggshell dorsal appendage formation, probably through regulation of apical constriction by PtdIns[4,5]P(2) during tubulogenesis. Required for cell viability or proliferation during wing and eye imaginal disk development. May be involved in cytoskeletal regulation during sensory bristle development. Together with mys/integrin beta localizes to the trailing edge of larval epidermal cells in a JNK signaling-dependent manner during wound healing and is required for setting up cell polarity and re-epithelialization. Required for polarization of elongating spermatid cysts possibly by generation of PtdIns[4,5]P(2) involved in mediating membrane association and orientation of the nucleus-basal body pair. Probably involved in PtdIns[4,5]P(2)-mediated recruitment of exocyst proteins that may mediate membrane addition during spermatid elongation. Involved in maintenance of specialised cell contacts known as slit diaphragms required for nephrocyte morphogenesis and function. Regulates nephrocyte endocytosis, possibly through PtdIns[4,5]P(2)-mediated recruitment of effector proteins. Not required for nervous system development or neurotransmitter release at the neuromuscular junction. Together with ash2 probably plays a role in maintenance of transcriptionally active chromatin through down- regulation of histone H1 hyperphosphorylation.","Catalyzes the conversion of phosphatidylinositol 4-phosphate and ATP to form phosphatidylinositol 4,5-bisphosphate and ADP. Involved in the generation of phosphatidylinositol 4,5-bisphosphate, a precursor of second messengers, such as inositol 1,4,5-trisphosphate, diacylglycerol, cAMP and cGMP.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016308,GO:0016308; GO:0005524,GO:0016308; GO:0005524,GO:0016308; GO:0005524,GO:0016308; GO:0005524,GO:0016308; GO:0005524,0.6819,0.6819,0.6819,0.6819,0.6819,5,0.6819,0.4277,no
PI5K1_DROME,Q9W2R3,Protein2Text,Eukaryota,792,"Catalyzes the phosphorylation of phosphatidylinositol 4- phosphate (PtdIns[4]P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns[4,5]P(2)), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility. PtdIns[4,5]P(2) can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns[3,4,5]P(3)). Required for germline development during oogenesis. Sktl is the major phosphatidylinositol 4-phosphate 5-kinase responsible for enrichment of PtdIns[4,5]P(2) in the apical plasma membrane of the oocyte and follicular epithelium cells of the egg chamber during oogenesis. Involved in nuclear anchoring and microtubule organization required for targeted mRNA transport during maintenance of oocyte polarity. The PtdIns[4,5]P(2) produced by sktl is required for maintenance of cellular polarity, prevention of the epithelial-mesenchymal transition process, maintenance of adherens junctions and regulation of apical constriction, probably by affecting polarized cortical recruitment of PAR proteins and their effectors, including baz/bazooka, aPKC, par-1 and l(2)gl. Involved in actin cytoskeleton organization probably through PtdIns[4,5]P(2)-mediated regulation of Moe/Moesin phosphorylation. Involved in PtdIns[4,5]P(2)-mediated apical recruitment of the formin dia/diaphanous in tubular epithelial cells. Involved in anterodorsal cell morphogenesis and eggshell dorsal appendage formation, probably through regulation of apical constriction by PtdIns[4,5]P(2) during tubulogenesis. Required for cell viability or proliferation during wing and eye imaginal disk development. May be involved in cytoskeletal regulation during sensory bristle development. Together with mys/integrin beta localizes to the trailing edge of larval epidermal cells in a JNK signaling-dependent manner during wound healing and is required for setting up cell polarity and re-epithelialization. Required for polarization of elongating spermatid cysts possibly by generation of PtdIns[4,5]P(2) involved in mediating membrane association and orientation of the nucleus-basal body pair. Probably involved in PtdIns[4,5]P(2)-mediated recruitment of exocyst proteins that may mediate membrane addition during spermatid elongation. Involved in maintenance of specialised cell contacts known as slit diaphragms required for nephrocyte morphogenesis and function. Regulates nephrocyte endocytosis, possibly through PtdIns[4,5]P(2)-mediated recruitment of effector proteins. Not required for nervous system development or neurotransmitter release at the neuromuscular junction. Together with ash2 probably plays a role in maintenance of transcriptionally active chromatin through down- regulation of histone H1 hyperphosphorylation.","This protein is a phosphatidylinositol 3-kinase, which means it is involved in the regulation of cellular processes such as cell growth, survival, and metabolism through the phosphatidylinositol 3-kinase (PI3K) pathway. Specifically, it is involved in the phosphorylation of phosphatidylinositol (PI) to form phosphatidylinositol 3-phosphate (PI3P), which is a key step in the activation of the PI3K pathway.",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0016308,GO:0035004,GO:0035004,GO:0035004,GO:0016303,GO:0016303,0.0,0.0,0.0,0.8041,0.8041,5,0.3216,0.4277,no
PI5K1_DROME,Q9W2R3,Reference,Eukaryota,792,"Catalyzes the phosphorylation of phosphatidylinositol 4- phosphate (PtdIns[4]P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns[4,5]P(2)), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility. PtdIns[4,5]P(2) can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns[3,4,5]P(3)). Required for germline development during oogenesis. Sktl is the major phosphatidylinositol 4-phosphate 5-kinase responsible for enrichment of PtdIns[4,5]P(2) in the apical plasma membrane of the oocyte and follicular epithelium cells of the egg chamber during oogenesis. Involved in nuclear anchoring and microtubule organization required for targeted mRNA transport during maintenance of oocyte polarity. The PtdIns[4,5]P(2) produced by sktl is required for maintenance of cellular polarity, prevention of the epithelial-mesenchymal transition process, maintenance of adherens junctions and regulation of apical constriction, probably by affecting polarized cortical recruitment of PAR proteins and their effectors, including baz/bazooka, aPKC, par-1 and l(2)gl. Involved in actin cytoskeleton organization probably through PtdIns[4,5]P(2)-mediated regulation of Moe/Moesin phosphorylation. Involved in PtdIns[4,5]P(2)-mediated apical recruitment of the formin dia/diaphanous in tubular epithelial cells. Involved in anterodorsal cell morphogenesis and eggshell dorsal appendage formation, probably through regulation of apical constriction by PtdIns[4,5]P(2) during tubulogenesis. Required for cell viability or proliferation during wing and eye imaginal disk development. May be involved in cytoskeletal regulation during sensory bristle development. Together with mys/integrin beta localizes to the trailing edge of larval epidermal cells in a JNK signaling-dependent manner during wound healing and is required for setting up cell polarity and re-epithelialization. Required for polarization of elongating spermatid cysts possibly by generation of PtdIns[4,5]P(2) involved in mediating membrane association and orientation of the nucleus-basal body pair. Probably involved in PtdIns[4,5]P(2)-mediated recruitment of exocyst proteins that may mediate membrane addition during spermatid elongation. Involved in maintenance of specialised cell contacts known as slit diaphragms required for nephrocyte morphogenesis and function. Regulates nephrocyte endocytosis, possibly through PtdIns[4,5]P(2)-mediated recruitment of effector proteins. Not required for nervous system development or neurotransmitter release at the neuromuscular junction. Together with ash2 probably plays a role in maintenance of transcriptionally active chromatin through down- regulation of histone H1 hyperphosphorylation.","Catalyzes the phosphorylation of phosphatidylinositol 4- phosphate (PtdIns[4]P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns[4,5]P(2)), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility. PtdIns[4,5]P(2) can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns[3,4,5]P(3)). Required for germline development during oogenesis. Sktl is the major phosphatidylinositol 4-phosphate 5-kinase responsible for enrichment of PtdIns[4,5]P(2) in the apical plasma membrane of the oocyte and follicular epithelium cells of the egg chamber during oogenesis. Involved in nuclear anchoring and microtubule organization required for targeted mRNA transport during maintenance of oocyte polarity. The PtdIns[4,5]P(2) produced by sktl is required for maintenance of cellular polarity, prevention of the epithelial-mesenchymal transition process, maintenance of adherens junctions and regulation of apical constriction, probably by affecting polarized cortical recruitment of PAR proteins and their effectors, including baz/bazooka, aPKC, par-1 and l(2)gl. Involved in actin cytoskeleton organization probably through PtdIns[4,5]P(2)-mediated regulation of Moe/Moesin phosphorylation. Involved in PtdIns[4,5]P(2)-mediated apical recruitment of the formin dia/diaphanous in tubular epithelial cells. Involved in anterodorsal cell morphogenesis and eggshell dorsal appendage formation, probably through regulation of apical constriction by PtdIns[4,5]P(2) during tubulogenesis. Required for cell viability or proliferation during wing and eye imaginal disk development. May be involved in cytoskeletal regulation during sensory bristle development. Together with mys/integrin beta localizes to the trailing edge of larval epidermal cells in a JNK signaling-dependent manner during wound healing and is required for setting up cell polarity and re-epithelialization. Required for polarization of elongating spermatid cysts possibly by generation of PtdIns[4,5]P(2) involved in mediating membrane association and orientation of the nucleus-basal body pair. Probably involved in PtdIns[4,5]P(2)-mediated recruitment of exocyst proteins that may mediate membrane addition during spermatid elongation. Involved in maintenance of specialised cell contacts known as slit diaphragms required for nephrocyte morphogenesis and function. Regulates nephrocyte endocytosis, possibly through PtdIns[4,5]P(2)-mediated recruitment of effector proteins. Not required for nervous system development or neurotransmitter release at the neuromuscular junction. Together with ash2 probably plays a role in maintenance of transcriptionally active chromatin through down- regulation of histone H1 hyperphosphorylation.",,,,,,,GO:0016308,GO:0016308; GO:0005524,GO:0016308,GO:0016308,GO:0016308; GO:0005524,GO:0016308; GO:0005524,0.6819,1.0,1.0,0.6819,0.6819,5,0.8091,0.4277,no
CDC7_DROME,Q9W3Y1,ESM2Text,Eukaryota,700,"Catalytic component of the Dbf4-dependent kinase (DDK) complex. Phosphorylates components of the pre- replication complex, including Mcm2 and, to a lesser extent, Mcm4. Phosphorylates histones, including H3 and H2B. Required for DNA replication and mitotic proliferation, including during the endoreplication and amplification stages of DNA replication in egg chamber follicle cells of the ovary.","Serine/threonine-protein kinase involved in the establishment of transcriptional silencing at telomeres and at HMR locus. Phosphorylates the elongator complex (e.g. SIR2-HMR and HMRK2-HMSO) at telomeres and marks the position of the elongator complex at the HMR or HMR locus, respectively, and recruits the elongator complex to telomeres specifically to form a repression complex on chromosome ends.",Maybe,Yes,Maybe,Yes,Maybe,not-Yes,GO:0005524; GO:0035173; GO:0004672; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.9281,0.7585,0.7585,0.7585,0.7585,5,0.7924,0.6925,yes
CDC7_DROME,Q9W3Y1,Prot2Text,Eukaryota,700,"Catalytic component of the Dbf4-dependent kinase (DDK) complex. Phosphorylates components of the pre- replication complex, including Mcm2 and, to a lesser extent, Mcm4. Phosphorylates histones, including H3 and H2B. Required for DNA replication and mitotic proliferation, including during the endoreplication and amplification stages of DNA replication in egg chamber follicle cells of the ovary.",Serine/threonine-protein kinase involved in transcription regulation. Phosphorylates ATF2 and SRE. ATF2 phosphorylation is required for transcriptional activation. ATF2 and SRE phosphorylation together with SRE are required for ATF2 to repress trans-acting elements. Involved in the regulation of pheromone signaling.,Maybe,Yes,Maybe,Yes,No,not-Yes,GO:0005524; GO:0035173; GO:0004672; GO:0106310; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674; GO:0005524,0.7585,0.7585,0.7585,0.7585,0.9281,5,0.7924,0.6925,yes
CDC7_DROME,Q9W3Y1,ProtT3,Eukaryota,700,"Catalytic component of the Dbf4-dependent kinase (DDK) complex. Phosphorylates components of the pre- replication complex, including Mcm2 and, to a lesser extent, Mcm4. Phosphorylates histones, including H3 and H2B. Required for DNA replication and mitotic proliferation, including during the endoreplication and amplification stages of DNA replication in egg chamber follicle cells of the ovary.",Probable serine/threonine-protein kinase involved in DNA replication. Nucleus. Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0035173; GO:0004672; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.9281,0.9281,0.9281,0.9281,0.9281,5,0.9281,0.6925,yes
CDC7_DROME,Q9W3Y1,ProtTale,Eukaryota,700,"Catalytic component of the Dbf4-dependent kinase (DDK) complex. Phosphorylates components of the pre- replication complex, including Mcm2 and, to a lesser extent, Mcm4. Phosphorylates histones, including H3 and H2B. Required for DNA replication and mitotic proliferation, including during the endoreplication and amplification stages of DNA replication in egg chamber follicle cells of the ovary.",Acts as a negative regulator of cell cycle progression from G1 to S phase. Phosphorylates CDKN1A/p21 and CDKN1B/p27. Also phosphorylates CDKN2A/CDKN1C and CDKN2B/CDKN1B. Involved in the regulation of centrosome duplication.,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0005524; GO:0035173; GO:0004672; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.9281,0.9281,0.7585,0.9281,0.9281,5,0.8942,0.6925,yes
CDC7_DROME,Q9W3Y1,Protein2Text,Eukaryota,700,"Catalytic component of the Dbf4-dependent kinase (DDK) complex. Phosphorylates components of the pre- replication complex, including Mcm2 and, to a lesser extent, Mcm4. Phosphorylates histones, including H3 and H2B. Required for DNA replication and mitotic proliferation, including during the endoreplication and amplification stages of DNA replication in egg chamber follicle cells of the ovary.",The molecular function of this protein is to act as a serine/threonine-protein kinase.,Yes,Yes,Maybe,Yes,Maybe,Yes,GO:0005524; GO:0035173; GO:0004672; GO:0106310; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.7585,0.7585,0.7585,0.7585,0.7585,5,0.7585,0.6925,yes
CDC7_DROME,Q9W3Y1,Reference,Eukaryota,700,"Catalytic component of the Dbf4-dependent kinase (DDK) complex. Phosphorylates components of the pre- replication complex, including Mcm2 and, to a lesser extent, Mcm4. Phosphorylates histones, including H3 and H2B. Required for DNA replication and mitotic proliferation, including during the endoreplication and amplification stages of DNA replication in egg chamber follicle cells of the ovary.","Catalytic component of the Dbf4-dependent kinase (DDK) complex. Phosphorylates components of the pre- replication complex, including Mcm2 and, to a lesser extent, Mcm4. Phosphorylates histones, including H3 and H2B. Required for DNA replication and mitotic proliferation, including during the endoreplication and amplification stages of DNA replication in egg chamber follicle cells of the ovary.",,,,,,,GO:0005524; GO:0035173; GO:0004672; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.9281,0.9281,0.9281,0.9281,0.9281,5,0.9281,0.6925,yes
MRPP3_DROME,Q9W413,ESM2Text,Eukaryota,544,"Catalytic ribonuclease component of mitochondrial ribonuclease P, a complex composed of rswl/MRPP1, scu/MRPP2 and mldr/MRPP3, which cleaves tRNA molecules in their 5'-ends. Essential for the structural and functional integrity of mitochondria. Function is essential for pupal development.",Required for efficient assembly of mitochondrial NADH:ubiquinone oxidoreductase.,No,No,No,No,No,not-Yes,GO:0046872; GO:0004526,,,,,,,,,,,0,,0.4635,no
MRPP3_DROME,Q9W413,Prot2Text,Eukaryota,544,"Catalytic ribonuclease component of mitochondrial ribonuclease P, a complex composed of rswl/MRPP1, scu/MRPP2 and mldr/MRPP3, which cleaves tRNA molecules in their 5'-ends. Essential for the structural and functional integrity of mitochondria. Function is essential for pupal development.","(Microbial infection) Required for mitochondrial translation of the COX2 coding region, which is important for respiratory growth and maintenance.",No,No,No,No,No,not-Yes,GO:0046872; GO:0004526,,,,,,,,,,,0,,0.4635,no
MRPP3_DROME,Q9W413,ProtT3,Eukaryota,544,"Catalytic ribonuclease component of mitochondrial ribonuclease P, a complex composed of rswl/MRPP1, scu/MRPP2 and mldr/MRPP3, which cleaves tRNA molecules in their 5'-ends. Essential for the structural and functional integrity of mitochondria. Function is essential for pupal development.",Mitochondrial ribonuclease involved in the maturation of small ribosomal subunits. Mitochondrion. Belongs to the PPR family. P subfamily,No,Maybe,Maybe,Yes,Maybe,not-Yes,GO:0046872; GO:0004526,GO:0004540,GO:0003723,GO:0004540,GO:0004540,GO:0004540,0.4027,0.2144,0.4027,0.4027,0.4027,5,0.365,0.4635,no
MRPP3_DROME,Q9W413,ProtTale,Eukaryota,544,"Catalytic ribonuclease component of mitochondrial ribonuclease P, a complex composed of rswl/MRPP1, scu/MRPP2 and mldr/MRPP3, which cleaves tRNA molecules in their 5'-ends. Essential for the structural and functional integrity of mitochondria. Function is essential for pupal development.","Catalytic component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.",No,No,No,No,No,not-Yes,GO:0046872; GO:0004526,,,GO:0003735,,GO:0003735,,,0.1351,,0.1351,2,0.1351,0.4635,no
MRPP3_DROME,Q9W413,Protein2Text,Eukaryota,544,"Catalytic ribonuclease component of mitochondrial ribonuclease P, a complex composed of rswl/MRPP1, scu/MRPP2 and mldr/MRPP3, which cleaves tRNA molecules in their 5'-ends. Essential for the structural and functional integrity of mitochondria. Function is essential for pupal development.","The molecular function of this protein is likely to be involved in the processing of mRNA, specifically in the removal of introns, as it is a part of the spliceosome complex.",No,No,No,No,No,not-Yes,GO:0046872; GO:0004526,,,,,,,,,,,0,,0.4635,no
MRPP3_DROME,Q9W413,Reference,Eukaryota,544,"Catalytic ribonuclease component of mitochondrial ribonuclease P, a complex composed of rswl/MRPP1, scu/MRPP2 and mldr/MRPP3, which cleaves tRNA molecules in their 5'-ends. Essential for the structural and functional integrity of mitochondria. Function is essential for pupal development.","Catalytic ribonuclease component of mitochondrial ribonuclease P, a complex composed of rswl/MRPP1, scu/MRPP2 and mldr/MRPP3, which cleaves tRNA molecules in their 5'-ends. Essential for the structural and functional integrity of mitochondria. Function is essential for pupal development.",,,,,,,GO:0046872; GO:0004526,GO:0004526,GO:0004525,GO:0004526,GO:0004526,GO:0004526,0.6848,0.5099,0.6848,0.6848,0.6848,5,0.6498,0.4635,no
TSAL_THEMA,Q9WYJ1,ESM2Text,Bacteria,401,"Catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. Can also use L-serine, but the catalytic efficiency toward L-threonine is about sixfold higher than that toward L-serine. Also shows weak activity toward L-allo- threonine, but cannot use the corresponding D-amino acids. Does not exhibit racemase activity toward various amino acids, including serine. Physiologically, is likely involved in the threonine-dependent pathway of isoleucine biosynthesis (Probable).","Catalyzes the threonine-dependent condensation of sulfite and phospho-AI-2, thereby terminating the AI-2 signaling cycle and activating the sA (sufuABCA) pathway of sulfate assimilation. Can also catalyze the condensation of oxaloacetate and pyruvate with acetyl-CoA, succinate semialdehyde, and CoA. These reactions are common for the beta subunits of sulfate-dependent enzymes.",No,No,No,No,No,not-Yes,GO:0003941; GO:0030170; GO:0004794,,,,,,,,,,,0,,0.6182,yes
TSAL_THEMA,Q9WYJ1,Prot2Text,Bacteria,401,"Catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. Can also use L-serine, but the catalytic efficiency toward L-threonine is about sixfold higher than that toward L-serine. Also shows weak activity toward L-allo- threonine, but cannot use the corresponding D-amino acids. Does not exhibit racemase activity toward various amino acids, including serine. Physiologically, is likely involved in the threonine-dependent pathway of isoleucine biosynthesis (Probable).",Catalyzes the synthesis of D-serine from L-serine. Has dehydratase activity towards both L-serine and D-serine.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0003941; GO:0030170; GO:0004794,GO:0008486,GO:0008486,GO:0008453,GO:0008453,GO:0008486,0.1454,0.1454,0.1672,0.1672,0.1454,5,0.1541,0.6182,yes
TSAL_THEMA,Q9WYJ1,ProtT3,Bacteria,401,"Catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. Can also use L-serine, but the catalytic efficiency toward L-threonine is about sixfold higher than that toward L-serine. Also shows weak activity toward L-allo- threonine, but cannot use the corresponding D-amino acids. Does not exhibit racemase activity toward various amino acids, including serine. Physiologically, is likely involved in the threonine-dependent pathway of isoleucine biosynthesis (Probable).","Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA (By similarity). SIMIL",Yes,Yes,Yes,Yes,Yes,Yes,GO:0003941; GO:0030170; GO:0004794,GO:0004794,GO:0004794,GO:0004794; GO:0030170,GO:0004794,GO:0004794,0.6996,0.6996,0.9458,0.6996,0.6996,5,0.7488,0.6182,yes
TSAL_THEMA,Q9WYJ1,ProtTale,Bacteria,401,"Catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. Can also use L-serine, but the catalytic efficiency toward L-threonine is about sixfold higher than that toward L-serine. Also shows weak activity toward L-allo- threonine, but cannot use the corresponding D-amino acids. Does not exhibit racemase activity toward various amino acids, including serine. Physiologically, is likely involved in the threonine-dependent pathway of isoleucine biosynthesis (Probable).","Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0003941; GO:0030170; GO:0004794,GO:0004794,GO:0004794,GO:0004794,GO:0004794,GO:0004794,0.6996,0.6996,0.6996,0.6996,0.6996,5,0.6996,0.6182,yes
TSAL_THEMA,Q9WYJ1,Protein2Text,Bacteria,401,"Catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. Can also use L-serine, but the catalytic efficiency toward L-threonine is about sixfold higher than that toward L-serine. Also shows weak activity toward L-allo- threonine, but cannot use the corresponding D-amino acids. Does not exhibit racemase activity toward various amino acids, including serine. Physiologically, is likely involved in the threonine-dependent pathway of isoleucine biosynthesis (Probable).","The molecular function of this protein is likely to be a kinase, as it is classified as a serine/threonine protein kinase, which is a type of enzyme that catalyzes the transfer of a phosphate group to a protein. More specifically, it is a dihydropteroate synthase, which is an enzyme that catalyzes the synthesis of dihydropteroate (H2PteGlu) from dihydropteridine pyrophosphate (H2Pte-PP) and glutamate.",No,No,No,No,No,not-Yes,GO:0003941; GO:0030170; GO:0004794,,GO:0004156,,GO:0004156,GO:0004156,,0.1966,,0.1966,0.1966,3,0.1966,0.6182,yes
TSAL_THEMA,Q9WYJ1,Reference,Bacteria,401,"Catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. Can also use L-serine, but the catalytic efficiency toward L-threonine is about sixfold higher than that toward L-serine. Also shows weak activity toward L-allo- threonine, but cannot use the corresponding D-amino acids. Does not exhibit racemase activity toward various amino acids, including serine. Physiologically, is likely involved in the threonine-dependent pathway of isoleucine biosynthesis (Probable).","Catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. Can also use L-serine, but the catalytic efficiency toward L-threonine is about sixfold higher than that toward L-serine. Also shows weak activity toward L-allo- threonine, but cannot use the corresponding D-amino acids. Does not exhibit racemase activity toward various amino acids, including serine. Physiologically, is likely involved in the threonine-dependent pathway of isoleucine biosynthesis (Probable).",,,,,,,GO:0003941; GO:0030170; GO:0004794,GO:0004794,GO:0004794,GO:0004794,GO:0004794,GO:0004794,0.6996,0.6996,0.6996,0.6996,0.6996,5,0.6996,0.6182,yes
BLBD1_CHRID,Q9X482,ESM2Text,Bacteria,239,"Class B beta-lactamase which confers resistance to the beta- lactam antibiotics, including penicillins, cephalosporins and carbapenems. Acts via hydrolysis of the beta-lactam ring. Has penicillin-, cephalosporin- and carbapenem- hydrolyzing activities.","Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008800; GO:0008270,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,0.6895,0.6895,0.6895,0.6895,0.6895,5,0.6895,0.4592,no
BLBD1_CHRID,Q9X482,Prot2Text,Bacteria,239,"Class B beta-lactamase which confers resistance to the beta- lactam antibiotics, including penicillins, cephalosporins and carbapenems. Acts via hydrolysis of the beta-lactam ring. Has penicillin-, cephalosporin- and carbapenem- hydrolyzing activities.","Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008800; GO:0008270,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,0.6895,0.6895,0.6895,0.6895,0.6895,5,0.6895,0.4592,no
BLBD1_CHRID,Q9X482,ProtT3,Bacteria,239,"Class B beta-lactamase which confers resistance to the beta- lactam antibiotics, including penicillins, cephalosporins and carbapenems. Acts via hydrolysis of the beta-lactam ring. Has penicillin-, cephalosporin- and carbapenem- hydrolyzing activities.","Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Periplasm. Belongs to the metallo-beta-lactamase superfamily. Class-B beta-lactamase family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008800; GO:0008270,GO:0008800,GO:0008800,GO:0008800,GO:0008800; GO:0046872,GO:0008800,0.6895,0.6895,0.6895,0.8854,0.6895,5,0.7287,0.4592,no
BLBD1_CHRID,Q9X482,ProtTale,Bacteria,239,"Class B beta-lactamase which confers resistance to the beta- lactam antibiotics, including penicillins, cephalosporins and carbapenems. Acts via hydrolysis of the beta-lactam ring. Has penicillin-, cephalosporin- and carbapenem- hydrolyzing activities.","Class B beta-lactamase which confers resistance to the beta- lactam antibiotics, including penicillins, cephalosporins and carbapenems. Acts via hydrolysis of the beta-lactam ring.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008800; GO:0008270,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,0.6895,0.6895,0.6895,0.6895,0.6895,5,0.6895,0.4592,no
BLBD1_CHRID,Q9X482,Protein2Text,Bacteria,239,"Class B beta-lactamase which confers resistance to the beta- lactam antibiotics, including penicillins, cephalosporins and carbapenems. Acts via hydrolysis of the beta-lactam ring. Has penicillin-, cephalosporin- and carbapenem- hydrolyzing activities.","The molecular function of this protein is not explicitly stated in the provided information. However, based on the name and the fact that it is involved in the breakdown of a toxic compound, it can be inferred that it is likely involved in the degradation of a nucleic acid or a nucleotide-related compound.

The molecular function of this protein is likely to be a hydrolase, specifically a phosphodiesterase, which catalyzes the hydrolysis of the phosphodiester bond between nucleotides.

This protein is involved in the breakdown of the toxic compound, likely a nucleic acid or a nucleotide-related compound, which is a product of the degradation of the protein. The exact molecular function of this protein is not explicitly stated, but it is likely to be involved in the degradation of a nucleic acid or a nucleotide-related compound.

It is worth noting that the molecular function of this protein is not explicitly stated, and more research is needed to determine its exact function.",No,No,No,Vague,No,not-Yes,GO:0008800; GO:0008270,,,,,,,,,,,0,,0.4592,no
BLBD1_CHRID,Q9X482,Reference,Bacteria,239,"Class B beta-lactamase which confers resistance to the beta- lactam antibiotics, including penicillins, cephalosporins and carbapenems. Acts via hydrolysis of the beta-lactam ring. Has penicillin-, cephalosporin- and carbapenem- hydrolyzing activities.","Class B beta-lactamase which confers resistance to the beta- lactam antibiotics, including penicillins, cephalosporins and carbapenems. Acts via hydrolysis of the beta-lactam ring. Has penicillin-, cephalosporin- and carbapenem- hydrolyzing activities.",,,,,,,GO:0008800; GO:0008270,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,0.6895,0.6895,0.6895,0.6895,0.6895,5,0.6895,0.4592,no
DNAB_GEOSE,Q9X4C9,ESM2Text,Bacteria,454,"The main replicative DNA helicase, it participates in initiation and elongation during chromosome replication. Travels ahead of the DNA replisome, separating double-stranded (ds)DNA into templates for DNA synthesis. Binding of single-stranded (ss)DNA to the hexamer suggests a 2-nucleotide step size for the helicase and a hand-over-hand mechanism of DNA unwinding (Probable). Has ssDNA- stimulated ATPase activity. DnaG primase stimulates the helicase activity (the helicase direction was not determine but is probably 5'-3'). Loaded onto DNA by helicase loader DnaI (shown with DnaI of B.subtilis); ATP-binding enhances loading and subsequent ATP hydrolysis dissociates the complex, leaving helicase on the DNA. Binds ssDNA and less well dsDNA, in the presence of ADPNP (probably 5'- adenylyl beta, gamma-imidodiphosphate, but not ATP) binding to both DNAs is improved.","Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0043139; GO:0005524; GO:0016887; GO:0003677; GO:0042802,GO:0003678; GO:0005524,GO:0016887; GO:0005524,GO:0003678; GO:0005524,GO:0008094; GO:0003678,GO:0003678; GO:0005524,0.6333,0.6513,0.6333,0.4658,0.6333,5,0.6034,0.3576,no
DNAB_GEOSE,Q9X4C9,Prot2Text,Bacteria,454,"The main replicative DNA helicase, it participates in initiation and elongation during chromosome replication. Travels ahead of the DNA replisome, separating double-stranded (ds)DNA into templates for DNA synthesis. Binding of single-stranded (ss)DNA to the hexamer suggests a 2-nucleotide step size for the helicase and a hand-over-hand mechanism of DNA unwinding (Probable). Has ssDNA- stimulated ATPase activity. DnaG primase stimulates the helicase activity (the helicase direction was not determine but is probably 5'-3'). Loaded onto DNA by helicase loader DnaI (shown with DnaI of B.subtilis); ATP-binding enhances loading and subsequent ATP hydrolysis dissociates the complex, leaving helicase on the DNA. Binds ssDNA and less well dsDNA, in the presence of ADPNP (probably 5'- adenylyl beta, gamma-imidodiphosphate, but not ATP) binding to both DNAs is improved.","Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0043139; GO:0005524; GO:0016887; GO:0003677; GO:0042802,GO:0003678,GO:0008094,GO:0004003; GO:0016887,GO:0008094,GO:0003678; GO:0005524,0.3936,0.3454,0.5949,0.3454,0.6333,5,0.4625,0.3576,no
DNAB_GEOSE,Q9X4C9,ProtT3,Bacteria,454,"The main replicative DNA helicase, it participates in initiation and elongation during chromosome replication. Travels ahead of the DNA replisome, separating double-stranded (ds)DNA into templates for DNA synthesis. Binding of single-stranded (ss)DNA to the hexamer suggests a 2-nucleotide step size for the helicase and a hand-over-hand mechanism of DNA unwinding (Probable). Has ssDNA- stimulated ATPase activity. DnaG primase stimulates the helicase activity (the helicase direction was not determine but is probably 5'-3'). Loaded onto DNA by helicase loader DnaI (shown with DnaI of B.subtilis); ATP-binding enhances loading and subsequent ATP hydrolysis dissociates the complex, leaving helicase on the DNA. Binds ssDNA and less well dsDNA, in the presence of ADPNP (probably 5'- adenylyl beta, gamma-imidodiphosphate, but not ATP) binding to both DNAs is improved.","Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins. Belongs to the helicase family. DnaB subfamily",Yes,Yes,Yes,Yes,Yes,Yes,GO:0043139; GO:0005524; GO:0016887; GO:0003677; GO:0042802,GO:0003678; GO:0005524,GO:0004386; GO:0005524,GO:0004003; GO:0005524; GO:0003677,GO:0003678; GO:0005524,GO:0004386; GO:0005524,0.6333,0.5963,0.8116,0.6333,0.5963,5,0.6542,0.3576,no
DNAB_GEOSE,Q9X4C9,ProtTale,Bacteria,454,"The main replicative DNA helicase, it participates in initiation and elongation during chromosome replication. Travels ahead of the DNA replisome, separating double-stranded (ds)DNA into templates for DNA synthesis. Binding of single-stranded (ss)DNA to the hexamer suggests a 2-nucleotide step size for the helicase and a hand-over-hand mechanism of DNA unwinding (Probable). Has ssDNA- stimulated ATPase activity. DnaG primase stimulates the helicase activity (the helicase direction was not determine but is probably 5'-3'). Loaded onto DNA by helicase loader DnaI (shown with DnaI of B.subtilis); ATP-binding enhances loading and subsequent ATP hydrolysis dissociates the complex, leaving helicase on the DNA. Binds ssDNA and less well dsDNA, in the presence of ADPNP (probably 5'- adenylyl beta, gamma-imidodiphosphate, but not ATP) binding to both DNAs is improved.","The main replicative DNA helicase, it participates in initiation and elongation during chromosome replication. Travels ahead of the DNA replisome, separating dsDNA into templates for DNA synthesis. A processive ATP-dependent 5'-3' DNA helicase it has DNA- dependent ATPase activity.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0043139; GO:0005524; GO:0016887; GO:0003677; GO:0042802,GO:0004386; GO:0005524; GO:0003677,GO:0004386; GO:0005524; GO:0003678,GO:0003678; GO:0005524,GO:0003678; GO:0016887; GO:0005524,GO:0003678; GO:0016887; GO:0005524,0.7792,0.6581,0.6333,0.7732,0.7732,5,0.7234,0.3576,no
DNAB_GEOSE,Q9X4C9,Protein2Text,Bacteria,454,"The main replicative DNA helicase, it participates in initiation and elongation during chromosome replication. Travels ahead of the DNA replisome, separating double-stranded (ds)DNA into templates for DNA synthesis. Binding of single-stranded (ss)DNA to the hexamer suggests a 2-nucleotide step size for the helicase and a hand-over-hand mechanism of DNA unwinding (Probable). Has ssDNA- stimulated ATPase activity. DnaG primase stimulates the helicase activity (the helicase direction was not determine but is probably 5'-3'). Loaded onto DNA by helicase loader DnaI (shown with DnaI of B.subtilis); ATP-binding enhances loading and subsequent ATP hydrolysis dissociates the complex, leaving helicase on the DNA. Binds ssDNA and less well dsDNA, in the presence of ADPNP (probably 5'- adenylyl beta, gamma-imidodiphosphate, but not ATP) binding to both DNAs is improved.",The molecular function of this protein is an endonuclease that is part of a bacterial integrase. It is involved in the recombination process of bacteriophage lambda.,No,No,No,No,No,not-Yes,GO:0043139; GO:0005524; GO:0016887; GO:0003677; GO:0042802,GO:0004519,GO:0004519,GO:0004519,GO:0009009,GO:0004519,0.1882,0.1882,0.1882,0.1996,0.1882,5,0.1905,0.3576,no
DNAB_GEOSE,Q9X4C9,Reference,Bacteria,454,"The main replicative DNA helicase, it participates in initiation and elongation during chromosome replication. Travels ahead of the DNA replisome, separating double-stranded (ds)DNA into templates for DNA synthesis. Binding of single-stranded (ss)DNA to the hexamer suggests a 2-nucleotide step size for the helicase and a hand-over-hand mechanism of DNA unwinding (Probable). Has ssDNA- stimulated ATPase activity. DnaG primase stimulates the helicase activity (the helicase direction was not determine but is probably 5'-3'). Loaded onto DNA by helicase loader DnaI (shown with DnaI of B.subtilis); ATP-binding enhances loading and subsequent ATP hydrolysis dissociates the complex, leaving helicase on the DNA. Binds ssDNA and less well dsDNA, in the presence of ADPNP (probably 5'- adenylyl beta, gamma-imidodiphosphate, but not ATP) binding to both DNAs is improved.","The main replicative DNA helicase, it participates in initiation and elongation during chromosome replication. Travels ahead of the DNA replisome, separating double-stranded (ds)DNA into templates for DNA synthesis. Binding of single-stranded (ss)DNA to the hexamer suggests a 2-nucleotide step size for the helicase and a hand-over-hand mechanism of DNA unwinding (Probable). Has ssDNA- stimulated ATPase activity. DnaG primase stimulates the helicase activity (the helicase direction was not determine but is probably 5'-3'). Loaded onto DNA by helicase loader DnaI (shown with DnaI of B.subtilis); ATP-binding enhances loading and subsequent ATP hydrolysis dissociates the complex, leaving helicase on the DNA. Binds ssDNA and less well dsDNA, in the presence of ADPNP (probably 5'- adenylyl beta, gamma-imidodiphosphate, but not ATP) binding to both DNAs is improved.",,,,,,,GO:0043139; GO:0005524; GO:0016887; GO:0003677; GO:0042802,GO:0003678; GO:0016887; GO:0005524; GO:0003697,GO:0003678; GO:0016887; GO:0003697,GO:0003678; GO:0016887; GO:0003697,GO:0003678; GO:0016887; GO:0005524,GO:0003678; GO:0016887; GO:0005524; GO:0003697,0.8741,0.7511,0.7511,0.7732,0.8741,5,0.8047,0.3576,no
VIK_ARATH,Q9XI87,ESM2Text,Eukaryota,438,"Serine/threonine protein kinase which may function as an adapter protein for BRL2. Required during vascular development for the establishment of vein pattern in foliar organs. Mediates MSSP1/TMT1 phosphorylation and activation to enhance its carrier activity and consequently vacuolar sugar accumulation, particularly in response to cold.",Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. Acts downstream of integrin (ITGA5:ITGB5) and phosphatidylinositol 3-kinase (PI3K). Phosphorylates ITGA5:ITGB5 in vitro. Involved in the response to the bacterial pathogen Pseudomonas syringae pv tomato strain DC3000 by enhancing the autophagic degradation of the filamentous forms. Promotes cell survival in keratinocytes.,Maybe,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0004709; GO:0004674; GO:0004712,GO:0004674; GO:0005524,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.9549,0.7567,0.7567,0.7567,0.7567,5,0.7963,0.6224,yes
VIK_ARATH,Q9XI87,Prot2Text,Eukaryota,438,"Serine/threonine protein kinase which may function as an adapter protein for BRL2. Required during vascular development for the establishment of vein pattern in foliar organs. Mediates MSSP1/TMT1 phosphorylation and activation to enhance its carrier activity and consequently vacuolar sugar accumulation, particularly in response to cold.","Serine/threonine protein kinase that acts as a mediator of the stress signal evoked by the cytokine KITLG/SCF and other growth factors. Following the activation of stress stimuli, translocates from the nucleus to the cytoplasm where it activates the stress-activated protein kinase AKT1 and the transcription factor RIMS1, and thereby activates the transcription of growth-related genes. Phosphorylates and activates STK11 and STK26. Mediates the activation of the stress-activated protein kinase AKT1 by phosphorylation of its activation-loop 'Thr-183' and 'Ser-185', enabling it to subsequently phosphorylate and activate the transcription factor RIMS1. Involved in the regulation of cell cycle progression, apoptosis, cell proliferation and cell growth.",Maybe,Yes,Yes,Yes,No,Yes,GO:0005524; GO:0004709; GO:0004674; GO:0004712,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674; GO:0005524,0.7567,0.7567,0.7567,0.7567,0.9549,5,0.7963,0.6224,yes
VIK_ARATH,Q9XI87,ProtT3,Eukaryota,438,"Serine/threonine protein kinase which may function as an adapter protein for BRL2. Required during vascular development for the establishment of vein pattern in foliar organs. Mediates MSSP1/TMT1 phosphorylation and activation to enhance its carrier activity and consequently vacuolar sugar accumulation, particularly in response to cold.","Serine/threonine-protein kinase that plays an essential role in the regulation of cell proliferation, survival, migration and differentiation",Vague,Yes,Maybe,Yes,Maybe,not-Yes,GO:0005524; GO:0004709; GO:0004674; GO:0004712,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.9549,0.9549,0.9549,0.9549,0.9549,5,0.9549,0.6224,yes
VIK_ARATH,Q9XI87,ProtTale,Eukaryota,438,"Serine/threonine protein kinase which may function as an adapter protein for BRL2. Required during vascular development for the establishment of vein pattern in foliar organs. Mediates MSSP1/TMT1 phosphorylation and activation to enhance its carrier activity and consequently vacuolar sugar accumulation, particularly in response to cold.",Serine/threonine kinase involved in the regulation of innate immune signaling in response to pathogen infection. Has a dual specificity: can phosphorylate both ERK1 and ERK2 and acts as a negative regulator of TLR4-mediated NF-kappa-B activation.,Maybe,Yes,Yes,Yes,No,Yes,GO:0005524; GO:0004709; GO:0004674; GO:0004712,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0004708,GO:0004674; GO:0004708; GO:0005524,GO:0004674; GO:0004708; GO:0005524,0.9549,0.9549,0.7969,0.9611,0.9611,5,0.9258,0.6224,yes
VIK_ARATH,Q9XI87,Protein2Text,Eukaryota,438,"Serine/threonine protein kinase which may function as an adapter protein for BRL2. Required during vascular development for the establishment of vein pattern in foliar organs. Mediates MSSP1/TMT1 phosphorylation and activation to enhance its carrier activity and consequently vacuolar sugar accumulation, particularly in response to cold.","The molecular function of this protein is that it is a serine/threonine-protein kinase, specifically a tyrosine-protein kinase.",Maybe,Yes,Maybe,Yes,Maybe,not-Yes,GO:0005524; GO:0004709; GO:0004674; GO:0004712,GO:0004674; GO:0004713,GO:0004674; GO:0004713,GO:0004713,GO:0004672,GO:0004672,0.7673,0.7673,0.6521,0.7265,0.7265,5,0.7279,0.6224,yes
VIK_ARATH,Q9XI87,Reference,Eukaryota,438,"Serine/threonine protein kinase which may function as an adapter protein for BRL2. Required during vascular development for the establishment of vein pattern in foliar organs. Mediates MSSP1/TMT1 phosphorylation and activation to enhance its carrier activity and consequently vacuolar sugar accumulation, particularly in response to cold.","Serine/threonine protein kinase which may function as an adapter protein for BRL2. Required during vascular development for the establishment of vein pattern in foliar organs. Mediates MSSP1/TMT1 phosphorylation and activation to enhance its carrier activity and consequently vacuolar sugar accumulation, particularly in response to cold.",,,,,,,GO:0005524; GO:0004709; GO:0004674; GO:0004712,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.9549,0.9549,0.9549,0.9549,0.9549,5,0.9549,0.6224,yes
NSH1_CAEEL,Q9XWN7,ESM2Text,Eukaryota,338,"Catalyzes the hydrolysis of the N-glycosidic bond of commonly occurring purine and pyrimidine nucleosides into ribose and the base, with decreasing activity, in the order: adenosine, guanosine, inosine, xanthosine, cytidine, uridine.",Is able to interconvert the N-glycosidic bond of all the major purine nucleotide tripeptides in vitro. YPT is the major purine nucleotide tripeptide.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0047622; GO:0005509; GO:0047724; GO:0008477; GO:0045437,,,,,,,,,,,0,,0.2308,no
NSH1_CAEEL,Q9XWN7,Prot2Text,Eukaryota,338,"Catalyzes the hydrolysis of the N-glycosidic bond of commonly occurring purine and pyrimidine nucleosides into ribose and the base, with decreasing activity, in the order: adenosine, guanosine, inosine, xanthosine, cytidine, uridine.","Hydrolyzes cytidine or uridine to ribose and cytosine or uracil, respectively. Has a clear preference for cytidine over uridine. Strictly specific for ribonucleosides.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0047622; GO:0005509; GO:0047724; GO:0008477; GO:0045437,GO:0016799,,GO:0016799,GO:0016799,GO:0016799,0.6783,,0.6783,0.6783,0.6783,4,0.6783,0.2308,no
NSH1_CAEEL,Q9XWN7,ProtT3,Eukaryota,338,"Catalyzes the hydrolysis of the N-glycosidic bond of commonly occurring purine and pyrimidine nucleosides into ribose and the base, with decreasing activity, in the order: adenosine, guanosine, inosine, xanthosine, cytidine, uridine.",Mitochondrion. Belongs to the IUNH family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0047622; GO:0005509; GO:0047724; GO:0008477; GO:0045437,GO:0047622,GO:0047622,GO:0047724,GO:0016799,GO:0008725,0.7045,0.7045,0.7045,0.6783,0.3641,5,0.6312,0.2308,no
NSH1_CAEEL,Q9XWN7,ProtTale,Eukaryota,338,"Catalyzes the hydrolysis of the N-glycosidic bond of commonly occurring purine and pyrimidine nucleosides into ribose and the base, with decreasing activity, in the order: adenosine, guanosine, inosine, xanthosine, cytidine, uridine.","Catalyzes the hydrolysis of the C-N bond of purine or pyrimidine nucleoside 5'-monophosphates. Is active toward inosine 5'-phosphate (InMP), deoxyinosine 5'-phosphate (dInMP), guanosine 5'-phosphate (GuMP), deoxyguanosine 5'-phosphate (dGuMP), hypoxanthine 5'-phosphate (HxMP), xanthosine 5'-phosphate (XanMP), adenine 5'- phosphate (AdoMP), guanine 5'",Maybe,Maybe,Maybe,No,No,not-Yes,GO:0047622; GO:0005509; GO:0047724; GO:0008477; GO:0045437,GO:0016787,GO:0016787,GO:0016799,GO:0016799,GO:0008252,0.4932,0.4932,0.6783,0.6783,0.2356,5,0.5157,0.2308,no
NSH1_CAEEL,Q9XWN7,Protein2Text,Eukaryota,338,"Catalyzes the hydrolysis of the N-glycosidic bond of commonly occurring purine and pyrimidine nucleosides into ribose and the base, with decreasing activity, in the order: adenosine, guanosine, inosine, xanthosine, cytidine, uridine.","The molecular function of this protein is not specified in the provided text. However, based on its name, it can be inferred that this protein is involved in catalyzing the hydrolysis of a sugar molecule, possibly a nucleoside or a sugar derivative. This is a common function for enzymes that end in ""-ase"", which often indicate an enzyme that catalyzes a specific reaction. In this case, the protein is likely to be a hydrolase, which is a type of enzyme that catalyzes the hydrolysis of a molecule.",Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0047622; GO:0005509; GO:0047724; GO:0008477; GO:0045437,,,,,,,,,,,0,,0.2308,no
NSH1_CAEEL,Q9XWN7,Reference,Eukaryota,338,"Catalyzes the hydrolysis of the N-glycosidic bond of commonly occurring purine and pyrimidine nucleosides into ribose and the base, with decreasing activity, in the order: adenosine, guanosine, inosine, xanthosine, cytidine, uridine.","Catalyzes the hydrolysis of the N-glycosidic bond of commonly occurring purine and pyrimidine nucleosides into ribose and the base, with decreasing activity, in the order: adenosine, guanosine, inosine, xanthosine, cytidine, uridine.",,,,,,,GO:0047622; GO:0005509; GO:0047724; GO:0008477; GO:0045437,GO:0016799,GO:0016799,GO:0016799,GO:0016799,GO:0016799,0.6783,0.6783,0.6783,0.6783,0.6783,5,0.6783,0.2308,no
PMDHL_AERPE,Q9YA51,ESM2Text,Archaea,402,"Component of a hydro-lyase that catalyzes the dehydration of mevalonate 5-phosphate (MVA5P) to form trans-anhydromevalonate 5- phosphate (tAHMP). Involved in the archaeal mevalonate (MVA) pathway, which provides fundamental precursors for isoprenoid biosynthesis, such as isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP).","Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.",No,No,No,No,No,not-Yes,GO:0051539; GO:0016829; GO:0046872,GO:0008964,GO:0008964,GO:0008964,GO:0008964,GO:0008964,0.3077,0.3077,0.3077,0.3077,0.3077,5,0.3077,0.1349,no
PMDHL_AERPE,Q9YA51,Prot2Text,Archaea,402,"Component of a hydro-lyase that catalyzes the dehydration of mevalonate 5-phosphate (MVA5P) to form trans-anhydromevalonate 5- phosphate (tAHMP). Involved in the archaeal mevalonate (MVA) pathway, which provides fundamental precursors for isoprenoid biosynthesis, such as isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP).",Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.,No,No,No,No,No,not-Yes,GO:0051539; GO:0016829; GO:0046872,GO:0008987,GO:0008987,GO:0008987,GO:0008987,GO:0008987,0.2558,0.2558,0.2558,0.2558,0.2558,5,0.2558,0.1349,no
PMDHL_AERPE,Q9YA51,ProtT3,Archaea,402,"Component of a hydro-lyase that catalyzes the dehydration of mevalonate 5-phosphate (MVA5P) to form trans-anhydromevalonate 5- phosphate (tAHMP). Involved in the archaeal mevalonate (MVA) pathway, which provides fundamental precursors for isoprenoid biosynthesis, such as isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP).",To M.thermoautotrophicum MTH127 and MTH128,Vague,Vague,Vague,Vague,No,not-Yes,GO:0051539; GO:0016829; GO:0046872,,,,,,,,,,,0,,0.1349,no
PMDHL_AERPE,Q9YA51,ProtTale,Archaea,402,"Component of a hydro-lyase that catalyzes the dehydration of mevalonate 5-phosphate (MVA5P) to form trans-anhydromevalonate 5- phosphate (tAHMP). Involved in the archaeal mevalonate (MVA) pathway, which provides fundamental precursors for isoprenoid biosynthesis, such as isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP).","Component of a hydro-lyase that catalyzes the dehydration of mevalonate 5-phosphate (MVA5P) to form trans-anhydromevalonate 5- phosphate (tAHMP). Involved in the archaeal mevalonate (MVA) pathway, which provides fundamental precursors for isoprenoid biosynthesis, such as isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP).",Yes,Yes,Yes,Yes,Yes,Yes,GO:0051539; GO:0016829; GO:0046872,GO:0016836,GO:0016836,GO:0016836,GO:0016836,GO:0016836,0.3972,0.3972,0.3972,0.3972,0.3972,5,0.3972,0.1349,no
PMDHL_AERPE,Q9YA51,Protein2Text,Archaea,402,"Component of a hydro-lyase that catalyzes the dehydration of mevalonate 5-phosphate (MVA5P) to form trans-anhydromevalonate 5- phosphate (tAHMP). Involved in the archaeal mevalonate (MVA) pathway, which provides fundamental precursors for isoprenoid biosynthesis, such as isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP).","This protein is involved in the molecular function of hydro-lyase activity, specifically carbon-carbon lyase activity.",Maybe,Maybe,Maybe,Yes,Maybe,not-Yes,GO:0051539; GO:0016829; GO:0046872,GO:0016829,GO:0016829,,GO:0016829,GO:0016829,0.5789,0.5789,,0.5789,0.5789,4,0.5789,0.1349,no
PMDHL_AERPE,Q9YA51,Reference,Archaea,402,"Component of a hydro-lyase that catalyzes the dehydration of mevalonate 5-phosphate (MVA5P) to form trans-anhydromevalonate 5- phosphate (tAHMP). Involved in the archaeal mevalonate (MVA) pathway, which provides fundamental precursors for isoprenoid biosynthesis, such as isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP).","Component of a hydro-lyase that catalyzes the dehydration of mevalonate 5-phosphate (MVA5P) to form trans-anhydromevalonate 5- phosphate (tAHMP). Involved in the archaeal mevalonate (MVA) pathway, which provides fundamental precursors for isoprenoid biosynthesis, such as isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP).",,,,,,,GO:0051539; GO:0016829; GO:0046872,GO:0016836,GO:0016836,GO:0016836,GO:0016836,GO:0016836,0.3972,0.3972,0.3972,0.3972,0.3972,5,0.3972,0.1349,no
CGS1_TOBAC,Q9ZPL5,ESM2Text,Eukaryota,540,"Catalyzes the first committed step of methionine (Met) biosynthesis. Catalyzes the formation of L-cystathionine from homoserine esters and L-cysteine, via a gamma-replacement reaction.","Catalyzes the first committed step of methionine (Met) biosynthesis. Catalyzes the formation of L-cystathionine from homoserine esters and L-cysteine, via a gamma-replacement reaction. Substrate preference for cystathionine synthesis is O-phospho-L-homoserine > O-phospho-L-homoserine > L-homoserine > L-homoserine > O-acetyl-L-homoserine. Has a lower activity with L-homoserine and L-homoserine.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0003962; GO:0030170,GO:0003962,GO:0003962,GO:0003962,GO:0003962,GO:0003962,0.6936,0.6936,0.6936,0.6936,0.6936,5,0.6936,0.1988,no
CGS1_TOBAC,Q9ZPL5,Prot2Text,Eukaryota,540,"Catalyzes the first committed step of methionine (Met) biosynthesis. Catalyzes the formation of L-cystathionine from homoserine esters and L-cysteine, via a gamma-replacement reaction.","Catalyzes the first committed step of methionine (Met) biosynthesis. Catalyzes the formation of L-cystathionine from homoserine esters and L-cysteine, via a gamma-replacement reaction.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0003962; GO:0030170,GO:0003962,GO:0003962,GO:0003962,GO:0003962,GO:0003962,0.6936,0.6936,0.6936,0.6936,0.6936,5,0.6936,0.1988,no
CGS1_TOBAC,Q9ZPL5,ProtT3,Eukaryota,540,"Catalyzes the first committed step of methionine (Met) biosynthesis. Catalyzes the formation of L-cystathionine from homoserine esters and L-cysteine, via a gamma-replacement reaction.","Catalyzes the formation of cystathionine from O-succinyl-L- homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. Plastid, chloroplast. Belongs to the trans-sulfuration enzymes family",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0003962; GO:0030170,GO:0003962,GO:0003962,GO:0003962; GO:0030170,GO:0003962,GO:0003962,0.6936,0.6936,1.0,0.6936,0.6936,5,0.7549,0.1988,no
CGS1_TOBAC,Q9ZPL5,ProtTale,Eukaryota,540,"Catalyzes the first committed step of methionine (Met) biosynthesis. Catalyzes the formation of L-cystathionine from homoserine esters and L-cysteine, via a gamma-replacement reaction.",Catalyzes the formation of 5-aminolevulinate from glycine and succinyl-CoA in a two-step reaction.,No,No,No,No,No,not-Yes,GO:0003962; GO:0030170,GO:0003870; GO:0030170,GO:0003870; GO:0030170,GO:0003870,GO:0003870,GO:0003870,0.6446,0.6446,0.2098,0.2098,0.2098,5,0.3837,0.1988,no
CGS1_TOBAC,Q9ZPL5,Protein2Text,Eukaryota,540,"Catalyzes the first committed step of methionine (Met) biosynthesis. Catalyzes the formation of L-cystathionine from homoserine esters and L-cysteine, via a gamma-replacement reaction.","This protein is a part of the methionine biosynthesis pathway, specifically involved in the conversion of homocysteine to methionine.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0003962; GO:0030170,,GO:0008705,GO:0008705,GO:0008705,GO:0008705,,0.2537,0.2537,0.2537,0.2537,4,0.2537,0.1988,no
CGS1_TOBAC,Q9ZPL5,Reference,Eukaryota,540,"Catalyzes the first committed step of methionine (Met) biosynthesis. Catalyzes the formation of L-cystathionine from homoserine esters and L-cysteine, via a gamma-replacement reaction.","Catalyzes the first committed step of methionine (Met) biosynthesis. Catalyzes the formation of L-cystathionine from homoserine esters and L-cysteine, via a gamma-replacement reaction.",,,,,,,GO:0003962; GO:0030170,GO:0003962,GO:0003962,GO:0003962,GO:0003962,GO:0003962,0.6936,0.6936,0.6936,0.6936,0.6936,5,0.6936,0.1988,no
CARK6_ARATH,Q9ZW72,ESM2Text,Eukaryota,406,"Receptor-like cytoplasmic kinase (RLCK) that triggers abscisic acid (ABA) signaling in response to dehydration by phosphorylating and activating ABA receptors to support their monomerization and enhance their ABA binding affinity; they in turn repress PP2C protein phosphatases acting as negative regulators of ABA responses. In response to abiotic stress, promotes drought resistance, and triggers adaptations such as the inhibition of seed germination and of root elongation. Negative regulator of the reactive oxygen stress (ROS) signaling mediated by the kinase OXI1 in response to pathogen-associated molecular patterns (PAMPs, e.g. flagellin), and associated with specific genes expression.",Probable tyrosine-protein kinase that may be involved in the response to oxygen deprivation.,No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0019900; GO:0004715; GO:0019901,,GO:0004713,GO:0004713,GO:0004713,GO:0004713,,0.4088,0.4088,0.4088,0.4088,4,0.4088,0.532,no
CARK6_ARATH,Q9ZW72,Prot2Text,Eukaryota,406,"Receptor-like cytoplasmic kinase (RLCK) that triggers abscisic acid (ABA) signaling in response to dehydration by phosphorylating and activating ABA receptors to support their monomerization and enhance their ABA binding affinity; they in turn repress PP2C protein phosphatases acting as negative regulators of ABA responses. In response to abiotic stress, promotes drought resistance, and triggers adaptations such as the inhibition of seed germination and of root elongation. Negative regulator of the reactive oxygen stress (ROS) signaling mediated by the kinase OXI1 in response to pathogen-associated molecular patterns (PAMPs, e.g. flagellin), and associated with specific genes expression.",Serine/threonine-protein kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of BRI1. Mediates signal transduction from BRI1 by functioning as substrate of BRI1. Functions as positive regulator of plant immunity and abscisic acid (ABA) signaling downstream of BRI1.,Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0019900; GO:0004715; GO:0019901,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674; GO:0005524,0.3434,0.3434,0.3434,0.3434,0.6265,5,0.4,0.532,no
CARK6_ARATH,Q9ZW72,ProtT3,Eukaryota,406,"Receptor-like cytoplasmic kinase (RLCK) that triggers abscisic acid (ABA) signaling in response to dehydration by phosphorylating and activating ABA receptors to support their monomerization and enhance their ABA binding affinity; they in turn repress PP2C protein phosphatases acting as negative regulators of ABA responses. In response to abiotic stress, promotes drought resistance, and triggers adaptations such as the inhibition of seed germination and of root elongation. Negative regulator of the reactive oxygen stress (ROS) signaling mediated by the kinase OXI1 in response to pathogen-associated molecular patterns (PAMPs, e.g. flagellin), and associated with specific genes expression.",Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0019900; GO:0004715; GO:0019901,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.6265,0.6265,0.6265,0.6265,0.6265,5,0.6265,0.532,no
CARK6_ARATH,Q9ZW72,ProtTale,Eukaryota,406,"Receptor-like cytoplasmic kinase (RLCK) that triggers abscisic acid (ABA) signaling in response to dehydration by phosphorylating and activating ABA receptors to support their monomerization and enhance their ABA binding affinity; they in turn repress PP2C protein phosphatases acting as negative regulators of ABA responses. In response to abiotic stress, promotes drought resistance, and triggers adaptations such as the inhibition of seed germination and of root elongation. Negative regulator of the reactive oxygen stress (ROS) signaling mediated by the kinase OXI1 in response to pathogen-associated molecular patterns (PAMPs, e.g. flagellin), and associated with specific genes expression.",May be involved in a receptor-like protein kinase (RLK) signaling system.,Vague,Maybe,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0019900; GO:0004715; GO:0019901,,,,,,,,,,,0,,0.532,no
CARK6_ARATH,Q9ZW72,Protein2Text,Eukaryota,406,"Receptor-like cytoplasmic kinase (RLCK) that triggers abscisic acid (ABA) signaling in response to dehydration by phosphorylating and activating ABA receptors to support their monomerization and enhance their ABA binding affinity; they in turn repress PP2C protein phosphatases acting as negative regulators of ABA responses. In response to abiotic stress, promotes drought resistance, and triggers adaptations such as the inhibition of seed germination and of root elongation. Negative regulator of the reactive oxygen stress (ROS) signaling mediated by the kinase OXI1 in response to pathogen-associated molecular patterns (PAMPs, e.g. flagellin), and associated with specific genes expression.","The molecular function of this protein is related to its involvement in plant defense mechanisms. Specifically, it is a kinase that plays a role in signaling pathways that help plants respond to pathogens and other stressors.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0019900; GO:0004715; GO:0019901,GO:0004674,GO:0004672,GO:0004672,GO:0004672,GO:0004672,0.3434,0.3857,0.3857,0.3857,0.3857,5,0.3772,0.532,no
CARK6_ARATH,Q9ZW72,Reference,Eukaryota,406,"Receptor-like cytoplasmic kinase (RLCK) that triggers abscisic acid (ABA) signaling in response to dehydration by phosphorylating and activating ABA receptors to support their monomerization and enhance their ABA binding affinity; they in turn repress PP2C protein phosphatases acting as negative regulators of ABA responses. In response to abiotic stress, promotes drought resistance, and triggers adaptations such as the inhibition of seed germination and of root elongation. Negative regulator of the reactive oxygen stress (ROS) signaling mediated by the kinase OXI1 in response to pathogen-associated molecular patterns (PAMPs, e.g. flagellin), and associated with specific genes expression.","Receptor-like cytoplasmic kinase (RLCK) that triggers abscisic acid (ABA) signaling in response to dehydration by phosphorylating and activating ABA receptors to support their monomerization and enhance their ABA binding affinity; they in turn repress PP2C protein phosphatases acting as negative regulators of ABA responses. In response to abiotic stress, promotes drought resistance, and triggers adaptations such as the inhibition of seed germination and of root elongation. Negative regulator of the reactive oxygen stress (ROS) signaling mediated by the kinase OXI1 in response to pathogen-associated molecular patterns (PAMPs, e.g. flagellin), and associated with specific genes expression.",,,,,,,GO:0005524; GO:0019900; GO:0004715; GO:0019901,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.6265,0.6265,0.6265,0.6265,0.6265,5,0.6265,0.532,no
LAAO4_HEBCY,S4S6Z0,ESM2Text,Eukaryota,626,"Catalyzes the oxidative deamination of L-amino acids with molecular oxygen to the corresponding alpha-keto acids and ammonia. L-glutamine shows the highest relative activity but LAAO4 has a broad substrate specificity, including L-amino acids with big aromatic, acidic and basic side chains. Methyl esters of these L-amino acids are also accepted, ethyl esters are converted but with lower activity, whereas D-Amino acids are not converted. No reaction is detected for small polar amino acids such as L-cysteine or L-aspartate, and very little for small, branched hydrophobic amino acids like L-valine.",Isopropyl malonyl-CoA lyase.,No,No,No,No,No,not-Yes,GO:0050025; GO:0050029,,,,,,,,,,,0,,0.1629,no
LAAO4_HEBCY,S4S6Z0,Prot2Text,Eukaryota,626,"Catalyzes the oxidative deamination of L-amino acids with molecular oxygen to the corresponding alpha-keto acids and ammonia. L-glutamine shows the highest relative activity but LAAO4 has a broad substrate specificity, including L-amino acids with big aromatic, acidic and basic side chains. Methyl esters of these L-amino acids are also accepted, ethyl esters are converted but with lower activity, whereas D-Amino acids are not converted. No reaction is detected for small polar amino acids such as L-cysteine or L-aspartate, and very little for small, branched hydrophobic amino acids like L-valine.",Lignin degradation and detoxification of lignin-derived products.,Vague,Vague,Vague,No,No,not-Yes,GO:0050025; GO:0050029,,,,,GO:0016491,,,,,0.4908,1,0.4908,0.1629,no
LAAO4_HEBCY,S4S6Z0,ProtT3,Eukaryota,626,"Catalyzes the oxidative deamination of L-amino acids with molecular oxygen to the corresponding alpha-keto acids and ammonia. L-glutamine shows the highest relative activity but LAAO4 has a broad substrate specificity, including L-amino acids with big aromatic, acidic and basic side chains. Methyl esters of these L-amino acids are also accepted, ethyl esters are converted but with lower activity, whereas D-Amino acids are not converted. No reaction is detected for small polar amino acids such as L-cysteine or L-aspartate, and very little for small, branched hydrophobic amino acids like L-valine.",Secreted. Belongs to the flavin monoamine oxidase family,Vague,Vague,Vague,Vague,No,not-Yes,GO:0050025; GO:0050029,GO:0016638,GO:0016491,GO:0016491; GO:0050660,GO:0016491; GO:0071949,GO:0016491,0.585,0.4908,0.3834,0.3816,0.4908,5,0.4663,0.1629,no
LAAO4_HEBCY,S4S6Z0,ProtTale,Eukaryota,626,"Catalyzes the oxidative deamination of L-amino acids with molecular oxygen to the corresponding alpha-keto acids and ammonia. L-glutamine shows the highest relative activity but LAAO4 has a broad substrate specificity, including L-amino acids with big aromatic, acidic and basic side chains. Methyl esters of these L-amino acids are also accepted, ethyl esters are converted but with lower activity, whereas D-Amino acids are not converted. No reaction is detected for small polar amino acids such as L-cysteine or L-aspartate, and very little for small, branched hydrophobic amino acids like L-valine.","Catalyzes the oxidative deamination of L-ornithine to L-citrulline and hydrogen peroxide, and of L-proline to L-glutamate and hydrogen peroxide.",Maybe,Maybe,Maybe,No,No,not-Yes,GO:0050025; GO:0050029,GO:0016491,GO:0016491,GO:0016491,GO:0016641,GO:0016641,0.4908,0.4908,0.4908,0.6757,0.6757,5,0.5648,0.1629,no
LAAO4_HEBCY,S4S6Z0,Protein2Text,Eukaryota,626,"Catalyzes the oxidative deamination of L-amino acids with molecular oxygen to the corresponding alpha-keto acids and ammonia. L-glutamine shows the highest relative activity but LAAO4 has a broad substrate specificity, including L-amino acids with big aromatic, acidic and basic side chains. Methyl esters of these L-amino acids are also accepted, ethyl esters are converted but with lower activity, whereas D-Amino acids are not converted. No reaction is detected for small polar amino acids such as L-cysteine or L-aspartate, and very little for small, branched hydrophobic amino acids like L-valine.","The molecular function of this protein is that it acts as a lipoxygenase, which is an enzyme that catalyzes the hydroperoxidation of polyunsaturated fatty acids, specifically the conversion of linoleic acid (18:2) to 13-hydroperoxylinoleic acid (13-HPODE). This reaction is a key step in the biosynthesis of various bioactive compounds, including leukotrienes and hydroxyeicosatetraenoic acids (HETEs). Lipoxygenases are involved in various cellular processes, including signal transduction, inflammation, and lipid metabolism. They also play a role in plant defense responses and the production of volatile compounds. In plants, lipoxygenases are involved in the synthesis of green leaf volatiles (GLVs) and other volatile compounds that contribute to plant defense and signaling. In humans, lipoxygenases are involved in the synthesis of leukotrienes, which are important mediators of inflammation and allergic responses.",No,No,No,No,No,not-Yes,GO:0050025; GO:0050029,GO:0016165,GO:0016165,GO:0016165,GO:0016165,GO:0016165,0.2413,0.2413,0.2413,0.2413,0.2413,5,0.2413,0.1629,no
LAAO4_HEBCY,S4S6Z0,Reference,Eukaryota,626,"Catalyzes the oxidative deamination of L-amino acids with molecular oxygen to the corresponding alpha-keto acids and ammonia. L-glutamine shows the highest relative activity but LAAO4 has a broad substrate specificity, including L-amino acids with big aromatic, acidic and basic side chains. Methyl esters of these L-amino acids are also accepted, ethyl esters are converted but with lower activity, whereas D-Amino acids are not converted. No reaction is detected for small polar amino acids such as L-cysteine or L-aspartate, and very little for small, branched hydrophobic amino acids like L-valine.","Catalyzes the oxidative deamination of L-amino acids with molecular oxygen to the corresponding alpha-keto acids and ammonia. L-glutamine shows the highest relative activity but LAAO4 has a broad substrate specificity, including L-amino acids with big aromatic, acidic and basic side chains. Methyl esters of these L-amino acids are also accepted, ethyl esters are converted but with lower activity, whereas D-Amino acids are not converted. No reaction is detected for small polar amino acids such as L-cysteine or L-aspartate, and very little for small, branched hydrophobic amino acids like L-valine.",,,,,,,GO:0050025; GO:0050029,GO:0016638,GO:0001723,GO:0016491,GO:0016639,GO:0001716,0.585,0.0,0.4908,0.4747,0.8767,5,0.4854,0.1629,no
PFMT1_OCIBA,S5DQS6,ESM2Text,Eukaryota,234,"Cation-dependent phenylpropanoid and flavonoid 8-O- methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects. May also act as a flavone 3'-O-methyltransferase. Catalyzes S-adenosylmethionine-dependent regioselective 8-O-methylation of flavonoids; mediates likely the conversion of pilosin (PIL) to nevadensin (NEV). Can also use 3',4',7,8-tetrahydroxyflavone and 3',4',7-trihydroxyflavone as substrates. Accepts other unnatural O-diphenols including luteolin and 7,8,4'-trihydroxy-flavone, cirsiliol, caffeic acid, 3,4-dihydroxylbenzaldehyde, and 3',4'-dihydroxy-flavone, and, with a lower efficiency, eriodictyol and catechol, as substrates.","Catalyzes the stepwise methylation of tricetin to its 3'-mono- and 3',5'-dimethyl ethers. No 3',4',5'-trimethylated ester derivatives are produced. Can use caffeoyl CoA, 5-hydroxyferulic acid, luteolin, quercetin and 7,8-dihydroxyflavone as substrates, but not naringenin, apigenin or kaempferol. The 2,3-double bond and the O-dihydroxyl group of the substrate are both required for catalytic activity of the enzyme.",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0046872; GO:0008171; GO:0008757,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7044,0.7044,0.7044,0.7044,0.7044,5,0.7044,0.2053,no
PFMT1_OCIBA,S5DQS6,Prot2Text,Eukaryota,234,"Cation-dependent phenylpropanoid and flavonoid 8-O- methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects. May also act as a flavone 3'-O-methyltransferase. Catalyzes S-adenosylmethionine-dependent regioselective 8-O-methylation of flavonoids; mediates likely the conversion of pilosin (PIL) to nevadensin (NEV). Can also use 3',4',7,8-tetrahydroxyflavone and 3',4',7-trihydroxyflavone as substrates. Accepts other unnatural O-diphenols including luteolin and 7,8,4'-trihydroxy-flavone, cirsiliol, caffeic acid, 3,4-dihydroxylbenzaldehyde, and 3',4'-dihydroxy-flavone, and, with a lower efficiency, eriodictyol and catechol, as substrates.",Methylates caffeoyl-CoA to feruloyl-CoA and 5-hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of feruloylated polysaccharides. Involved in the reinforcement of the plant cell wall. Also involved in the responding to wounding or pathogen challenge by the increased formation of cell wall-bound ferulic acid polymers.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0008171; GO:0008757,GO:0042409,GO:0042409,GO:0042409,GO:0042409,GO:0042409,0.6075,0.6075,0.6075,0.6075,0.6075,5,0.6075,0.2053,no
PFMT1_OCIBA,S5DQS6,ProtT3,Eukaryota,234,"Cation-dependent phenylpropanoid and flavonoid 8-O- methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects. May also act as a flavone 3'-O-methyltransferase. Catalyzes S-adenosylmethionine-dependent regioselective 8-O-methylation of flavonoids; mediates likely the conversion of pilosin (PIL) to nevadensin (NEV). Can also use 3',4',7,8-tetrahydroxyflavone and 3',4',7-trihydroxyflavone as substrates. Accepts other unnatural O-diphenols including luteolin and 7,8,4'-trihydroxy-flavone, cirsiliol, caffeic acid, 3,4-dihydroxylbenzaldehyde, and 3',4'-dihydroxy-flavone, and, with a lower efficiency, eriodictyol and catechol, as substrates.",Methylates caffeoyl-CoA to feruloyl-CoA and 5- hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of feruloylated polysaccharides. Involved in the reinforcement of the plant cell wall. Also involved in the responding to wounding or pathogen challenge by the increased formation of cell wall-bound ferulic acid polymers. Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family. CCoAMT subfamily,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0008171; GO:0008757,GO:0042409,GO:0042409,GO:0042409,GO:0042409,GO:0042409,0.6075,0.6075,0.6075,0.6075,0.6075,5,0.6075,0.2053,no
PFMT1_OCIBA,S5DQS6,ProtTale,Eukaryota,234,"Cation-dependent phenylpropanoid and flavonoid 8-O- methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects. May also act as a flavone 3'-O-methyltransferase. Catalyzes S-adenosylmethionine-dependent regioselective 8-O-methylation of flavonoids; mediates likely the conversion of pilosin (PIL) to nevadensin (NEV). Can also use 3',4',7,8-tetrahydroxyflavone and 3',4',7-trihydroxyflavone as substrates. Accepts other unnatural O-diphenols including luteolin and 7,8,4'-trihydroxy-flavone, cirsiliol, caffeic acid, 3,4-dihydroxylbenzaldehyde, and 3',4'-dihydroxy-flavone, and, with a lower efficiency, eriodictyol and catechol, as substrates.",Catalyzes the hydroxylation of 2-keto-3-deoxy-D-manno-octulosonate (KDO) to yield 3-deoxy-D-manno-octulosonic acid (KDO).,No,No,No,No,No,not-Yes,GO:0046872; GO:0008171; GO:0008757,GO:0016706,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.182,0.3059,0.3059,0.3059,0.3059,5,0.2811,0.2053,no
PFMT1_OCIBA,S5DQS6,Protein2Text,Eukaryota,234,"Cation-dependent phenylpropanoid and flavonoid 8-O- methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects. May also act as a flavone 3'-O-methyltransferase. Catalyzes S-adenosylmethionine-dependent regioselective 8-O-methylation of flavonoids; mediates likely the conversion of pilosin (PIL) to nevadensin (NEV). Can also use 3',4',7,8-tetrahydroxyflavone and 3',4',7-trihydroxyflavone as substrates. Accepts other unnatural O-diphenols including luteolin and 7,8,4'-trihydroxy-flavone, cirsiliol, caffeic acid, 3,4-dihydroxylbenzaldehyde, and 3',4'-dihydroxy-flavone, and, with a lower efficiency, eriodictyol and catechol, as substrates.","The molecular function of this protein is to be involved in the methylation of catecholamines. 
It is a methyltransferase that catalyzes the methylation of catecholamines at the N-7 position of the imidazole ring of histidine residues, and is involved in the regulation of catecholamine levels in the body.",No,No,No,No,No,not-Yes,GO:0046872; GO:0008171; GO:0008757,GO:0008168,GO:0016206,GO:0008168,GO:0008168,GO:0008168,0.6698,0.6075,0.6698,0.6698,0.6698,5,0.6573,0.2053,no
PFMT1_OCIBA,S5DQS6,Reference,Eukaryota,234,"Cation-dependent phenylpropanoid and flavonoid 8-O- methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects. May also act as a flavone 3'-O-methyltransferase. Catalyzes S-adenosylmethionine-dependent regioselective 8-O-methylation of flavonoids; mediates likely the conversion of pilosin (PIL) to nevadensin (NEV). Can also use 3',4',7,8-tetrahydroxyflavone and 3',4',7-trihydroxyflavone as substrates. Accepts other unnatural O-diphenols including luteolin and 7,8,4'-trihydroxy-flavone, cirsiliol, caffeic acid, 3,4-dihydroxylbenzaldehyde, and 3',4'-dihydroxy-flavone, and, with a lower efficiency, eriodictyol and catechol, as substrates.","Cation-dependent phenylpropanoid and flavonoid 8-O- methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects. May also act as a flavone 3'-O-methyltransferase. Catalyzes S-adenosylmethionine-dependent regioselective 8-O-methylation of flavonoids; mediates likely the conversion of pilosin (PIL) to nevadensin (NEV). Can also use 3',4',7,8-tetrahydroxyflavone and 3',4',7-trihydroxyflavone as substrates. Accepts other unnatural O-diphenols including luteolin and 7,8,4'-trihydroxy-flavone, cirsiliol, caffeic acid, 3,4-dihydroxylbenzaldehyde, and 3',4'-dihydroxy-flavone, and, with a lower efficiency, eriodictyol and catechol, as substrates.",,,,,,,GO:0046872; GO:0008171; GO:0008757,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7044,0.7044,0.7044,0.7044,0.7044,5,0.7044,0.2053,no
PDMA_SPHYB,S5RR11,ESM2Text,Bacteria,459,"Part of the multicomponent N,N-dimethyl phenylurea N- demethylase responsible for the initial N-demethylation step during the bacterial metabolism of N,N-dimethyl-substituted phenylurea herbicides. Catalyzes the mono-N-demethylation of N,N-dimethyl- substituted phenylurea herbicides to their mono-N-demethylated derivatives. Is active on isoproturon (IPU), chlorotoluron, metoxuron, monoron, diuron, fluometuron and fenuron, but cannot transform the N-methoxy-N-methyl-substituted herbicides.","Part of the multicomponent 3-phenylpropionate dioxygenase. Converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol), respectively.",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0051537; GO:0005506; GO:0016491,,GO:0016702,GO:0016705,,GO:0051213,,0.3452,0.4642,,0.4642,3,0.4245,0.2315,no
PDMA_SPHYB,S5RR11,Prot2Text,Bacteria,459,"Part of the multicomponent N,N-dimethyl phenylurea N- demethylase responsible for the initial N-demethylation step during the bacterial metabolism of N,N-dimethyl-substituted phenylurea herbicides. Catalyzes the mono-N-demethylation of N,N-dimethyl- substituted phenylurea herbicides to their mono-N-demethylated derivatives. Is active on isoproturon (IPU), chlorotoluron, metoxuron, monoron, diuron, fluometuron and fenuron, but cannot transform the N-methoxy-N-methyl-substituted herbicides.","Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. The alpha subunit has a catalytic role in the holoenzyme. Also able to catalyze the cis-dihydroxylation of biphenyl and phenanthrene.",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0051537; GO:0005506; GO:0016491,GO:0051213,GO:0018624,GO:0051213,GO:0018618,GO:0016702,0.4642,0.3088,0.4642,0.3088,0.3452,5,0.3782,0.2315,no
PDMA_SPHYB,S5RR11,ProtT3,Bacteria,459,"Part of the multicomponent N,N-dimethyl phenylurea N- demethylase responsible for the initial N-demethylation step during the bacterial metabolism of N,N-dimethyl-substituted phenylurea herbicides. Catalyzes the mono-N-demethylation of N,N-dimethyl- substituted phenylurea herbicides to their mono-N-demethylated derivatives. Is active on isoproturon (IPU), chlorotoluron, metoxuron, monoron, diuron, fluometuron and fenuron, but cannot transform the N-methoxy-N-methyl-substituted herbicides.","Part of the multicomponent 3-phenylpropionate dioxygenase. Converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid- dihydrodiol (CI-dihydrodiol), respectively. Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0051537; GO:0005506; GO:0016491,GO:0016702,GO:0016491,GO:0016701,GO:0016491; GO:0005506,GO:0051213,0.3452,0.5717,0.4642,0.8522,0.4642,5,0.5395,0.2315,no
PDMA_SPHYB,S5RR11,ProtTale,Bacteria,459,"Part of the multicomponent N,N-dimethyl phenylurea N- demethylase responsible for the initial N-demethylation step during the bacterial metabolism of N,N-dimethyl-substituted phenylurea herbicides. Catalyzes the mono-N-demethylation of N,N-dimethyl- substituted phenylurea herbicides to their mono-N-demethylated derivatives. Is active on isoproturon (IPU), chlorotoluron, metoxuron, monoron, diuron, fluometuron and fenuron, but cannot transform the N-methoxy-N-methyl-substituted herbicides.","Component of naphthalene dioxygenase multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2- dihydronaphthalene.",Maybe,Maybe,No,Maybe,No,not-Yes,GO:0051537; GO:0005506; GO:0016491,GO:0016491; GO:0005506,GO:0016491; GO:0005506,GO:0018622,GO:0051213,GO:0016701,0.8522,0.8522,0.3088,0.4642,0.4642,5,0.5883,0.2315,no
PDMA_SPHYB,S5RR11,Protein2Text,Bacteria,459,"Part of the multicomponent N,N-dimethyl phenylurea N- demethylase responsible for the initial N-demethylation step during the bacterial metabolism of N,N-dimethyl-substituted phenylurea herbicides. Catalyzes the mono-N-demethylation of N,N-dimethyl- substituted phenylurea herbicides to their mono-N-demethylated derivatives. Is active on isoproturon (IPU), chlorotoluron, metoxuron, monoron, diuron, fluometuron and fenuron, but cannot transform the N-methoxy-N-methyl-substituted herbicides.","Oxidoreductase. Probably involved in the degradation of aromatic compounds. Catalyzes the oxidation of phenylacetic acid and 3-methylphenylacetic acid. Is not active with 2- methylphenylacetic acid and phenylpropionic acid. Also active with 4- chlorophenylacetic acid. Cannot use benzoate as substrate. Probably involved in the degradation of aromatic compounds. Catalyzes the oxidation of phenylacetic acid and 3- methylphenylacetic acid. Is not active with 2- methylphenylacetic acid and phenylpropionic acid. Also active with 4- chlorophenylacetic acid. Cannot use benzoate as substrate.
            (Probable) oxidase involved in the degradation of aromatic compounds. Catalyzes the oxidation of phenylacetic acid and 3-methylphenylacetic acid. Is not active with 2-methylphenylacetic acid and phenylpropionic acid. Also active with 4-chlorophenylacetic acid. Cannot use benzoate as substrate.
            (Probable) oxidase involved in the degradation of aromatic compounds. Catalyzes the oxidation of phenylacetic acid and 3-methylphenylacetic acid. Is not active with 2-methylphenylacetic acid and phenylpropionic acid. Also active with 4-chlorophenylacetic acid. Cannot use benzoate as substrate.
            (Probable) oxidase involved in the degradation of aromatic compounds. Catalyzes the oxidation of phenylacetic acid and 3-methylphenylacetic acid. Is not active with 2-methylphenylacetic acid and phenylpropionic acid. Also active with 4-chlorophenylacetic acid. Cannot use benzoate as substrate.
            (Probable) oxidase involved in the degradation of aromatic compounds. Catalyzes the oxidation of phenylacetic acid and 3-methylphenylacetic acid. Is not active with 2-methylphenylacetic acid and phenylpropionic acid. Also active with 4-chlorophenylacetic acid. Cannot use benzoate as substrate.
            (Probable) oxidase involved in the degradation of aromatic compounds. Catalyzes the oxidation of phenylacetic acid and 3-methylphenylacetic acid. Is not active with 2",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0051537; GO:0005506; GO:0016491,GO:0004497,,,,,0.4642,,,,,1,0.4642,0.2315,no
PDMA_SPHYB,S5RR11,Reference,Bacteria,459,"Part of the multicomponent N,N-dimethyl phenylurea N- demethylase responsible for the initial N-demethylation step during the bacterial metabolism of N,N-dimethyl-substituted phenylurea herbicides. Catalyzes the mono-N-demethylation of N,N-dimethyl- substituted phenylurea herbicides to their mono-N-demethylated derivatives. Is active on isoproturon (IPU), chlorotoluron, metoxuron, monoron, diuron, fluometuron and fenuron, but cannot transform the N-methoxy-N-methyl-substituted herbicides.","Part of the multicomponent N,N-dimethyl phenylurea N- demethylase responsible for the initial N-demethylation step during the bacterial metabolism of N,N-dimethyl-substituted phenylurea herbicides. Catalyzes the mono-N-demethylation of N,N-dimethyl- substituted phenylurea herbicides to their mono-N-demethylated derivatives. Is active on isoproturon (IPU), chlorotoluron, metoxuron, monoron, diuron, fluometuron and fenuron, but cannot transform the N-methoxy-N-methyl-substituted herbicides.",,,,,,,GO:0051537; GO:0005506; GO:0016491,GO:0016705,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.4642,0.4642,0.4642,0.4642,0.4642,5,0.4642,0.2315,no
GALT_BIOGL,S5S833,ESM2Text,Eukaryota,600,"Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad substrate specificity. Acceptor peptides include Muc2, Muc5Ac, Muc1a and Muc1a', with Muc2 as the best acceptor. Acts on non-glycosylated and mono- or multi- glycosylated peptide substrates. Transfers preferably to threonine rather than serine residue. Thr-15 is the most preferred site of glycosylation in Muc2 peptide PTTTPITTTTTVTPTPTPTGTQTK having proline residues at position -1, and at positions +1 and +3, where the number represents the distance from the C-terminal and N-terminal hydroxyl amino acid, respectively. Transfer of the N-acetyl-D-galactosamine (GalNAc) is optimal with proline residues at positions -3, -1, +1 and +3, but other amino acids are tolerated, although some, such as phenylalanine, isoleucine or leucine at -1, or lysine at +3 prevent the transfer completely. Second GalNAc is transferred to Muc2 Thr-2 or Thr-13, both of which have two proline residues nearby. Up to nine sites can be glycosylated within Muc2, but eight are used simultaneously since Thr-19 and Thr-21 are not detected to be glycosylated at the same time. Glycosylation is not detected of a potential site, which is next to an already glycosylated site, but only one amino acid is needed in between two glycosylation sites. Ser-5 is the preferred glycosylation site in Muc5Ac peptide GTTPSPVPTTSTTSAP into which up to four GalNAcs can be attached. Only the threonine residues are detected as pontential glycosylation sites in Muc1a APPAHGVTSAPDTRPAPGC and Muc1a' AHGVTSAPDTR peptides. Transferase activity is restricted to UDP-GalNAc as a donor, and none of the nucleotide sugars UDP-Gal, UDP-GlcNAc, GDP-fucose, UDP-xylose, UDP- glucuronic acid or CMP-neuraminic acid are utilized as donors.","Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0030246; GO:0030145; GO:0004653,GO:0004653,GO:0004653,GO:0004653,GO:0004653,GO:0004653,0.5522,0.5522,0.5522,0.5522,0.5522,5,0.5522,0.4575,no
GALT_BIOGL,S5S833,Prot2Text,Eukaryota,600,"Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad substrate specificity. Acceptor peptides include Muc2, Muc5Ac, Muc1a and Muc1a', with Muc2 as the best acceptor. Acts on non-glycosylated and mono- or multi- glycosylated peptide substrates. Transfers preferably to threonine rather than serine residue. Thr-15 is the most preferred site of glycosylation in Muc2 peptide PTTTPITTTTTVTPTPTPTGTQTK having proline residues at position -1, and at positions +1 and +3, where the number represents the distance from the C-terminal and N-terminal hydroxyl amino acid, respectively. Transfer of the N-acetyl-D-galactosamine (GalNAc) is optimal with proline residues at positions -3, -1, +1 and +3, but other amino acids are tolerated, although some, such as phenylalanine, isoleucine or leucine at -1, or lysine at +3 prevent the transfer completely. Second GalNAc is transferred to Muc2 Thr-2 or Thr-13, both of which have two proline residues nearby. Up to nine sites can be glycosylated within Muc2, but eight are used simultaneously since Thr-19 and Thr-21 are not detected to be glycosylated at the same time. Glycosylation is not detected of a potential site, which is next to an already glycosylated site, but only one amino acid is needed in between two glycosylation sites. Ser-5 is the preferred glycosylation site in Muc5Ac peptide GTTPSPVPTTSTTSAP into which up to four GalNAcs can be attached. Only the threonine residues are detected as pontential glycosylation sites in Muc1a APPAHGVTSAPDTRPAPGC and Muc1a' AHGVTSAPDTR peptides. Transferase activity is restricted to UDP-GalNAc as a donor, and none of the nucleotide sugars UDP-Gal, UDP-GlcNAc, GDP-fucose, UDP-xylose, UDP- glucuronic acid or CMP-neuraminic acid are utilized as donors.","Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward Muc5Ac and EA2 peptide substrates.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0030246; GO:0030145; GO:0004653,GO:0004653,GO:0004653,GO:0004653,GO:0004653,GO:0004653,0.5522,0.5522,0.5522,0.5522,0.5522,5,0.5522,0.4575,no
GALT_BIOGL,S5S833,ProtT3,Eukaryota,600,"Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad substrate specificity. Acceptor peptides include Muc2, Muc5Ac, Muc1a and Muc1a', with Muc2 as the best acceptor. Acts on non-glycosylated and mono- or multi- glycosylated peptide substrates. Transfers preferably to threonine rather than serine residue. Thr-15 is the most preferred site of glycosylation in Muc2 peptide PTTTPITTTTTVTPTPTPTGTQTK having proline residues at position -1, and at positions +1 and +3, where the number represents the distance from the C-terminal and N-terminal hydroxyl amino acid, respectively. Transfer of the N-acetyl-D-galactosamine (GalNAc) is optimal with proline residues at positions -3, -1, +1 and +3, but other amino acids are tolerated, although some, such as phenylalanine, isoleucine or leucine at -1, or lysine at +3 prevent the transfer completely. Second GalNAc is transferred to Muc2 Thr-2 or Thr-13, both of which have two proline residues nearby. Up to nine sites can be glycosylated within Muc2, but eight are used simultaneously since Thr-19 and Thr-21 are not detected to be glycosylated at the same time. Glycosylation is not detected of a potential site, which is next to an already glycosylated site, but only one amino acid is needed in between two glycosylation sites. Ser-5 is the preferred glycosylation site in Muc5Ac peptide GTTPSPVPTTSTTSAP into which up to four GalNAcs can be attached. Only the threonine residues are detected as pontential glycosylation sites in Muc1a APPAHGVTSAPDTRPAPGC and Muc1a' AHGVTSAPDTR peptides. Transferase activity is restricted to UDP-GalNAc as a donor, and none of the nucleotide sugars UDP-Gal, UDP-GlcNAc, GDP-fucose, UDP-xylose, UDP- glucuronic acid or CMP-neuraminic acid are utilized as donors.","Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Golgi apparatus membrane; Single- pass type II membrane protein. Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily",Yes,Yes,Yes,Yes,Yes,Yes,GO:0030246; GO:0030145; GO:0004653,GO:0004653,GO:0004653,GO:0004653,GO:0004653,GO:0004653,0.5522,0.5522,0.5522,0.5522,0.5522,5,0.5522,0.4575,no
GALT_BIOGL,S5S833,ProtTale,Eukaryota,600,"Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad substrate specificity. Acceptor peptides include Muc2, Muc5Ac, Muc1a and Muc1a', with Muc2 as the best acceptor. Acts on non-glycosylated and mono- or multi- glycosylated peptide substrates. Transfers preferably to threonine rather than serine residue. Thr-15 is the most preferred site of glycosylation in Muc2 peptide PTTTPITTTTTVTPTPTPTGTQTK having proline residues at position -1, and at positions +1 and +3, where the number represents the distance from the C-terminal and N-terminal hydroxyl amino acid, respectively. Transfer of the N-acetyl-D-galactosamine (GalNAc) is optimal with proline residues at positions -3, -1, +1 and +3, but other amino acids are tolerated, although some, such as phenylalanine, isoleucine or leucine at -1, or lysine at +3 prevent the transfer completely. Second GalNAc is transferred to Muc2 Thr-2 or Thr-13, both of which have two proline residues nearby. Up to nine sites can be glycosylated within Muc2, but eight are used simultaneously since Thr-19 and Thr-21 are not detected to be glycosylated at the same time. Glycosylation is not detected of a potential site, which is next to an already glycosylated site, but only one amino acid is needed in between two glycosylation sites. Ser-5 is the preferred glycosylation site in Muc5Ac peptide GTTPSPVPTTSTTSAP into which up to four GalNAcs can be attached. Only the threonine residues are detected as pontential glycosylation sites in Muc1a APPAHGVTSAPDTRPAPGC and Muc1a' AHGVTSAPDTR peptides. Transferase activity is restricted to UDP-GalNAc as a donor, and none of the nucleotide sugars UDP-Gal, UDP-GlcNAc, GDP-fucose, UDP-xylose, UDP- glucuronic acid or CMP-neuraminic acid are utilized as donors.","Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine (GalNAc) residue from UDP-GalNAc to a serine or threonine residue on the protein receptor. Mainly catalyzes the transfer of the first GalNAc to MUC2 and MUC5B, two mucin-type O-linked glycopeptides that constitute the bulk of MUC2 and MUC5B proteins. Also catalyzes the addition of the second GalNAc to MUC2 and MUC5B.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0030246; GO:0030145; GO:0004653,GO:0004653,GO:0004653,GO:0004653,GO:0004653,GO:0004653,0.5522,0.5522,0.5522,0.5522,0.5522,5,0.5522,0.4575,no
GALT_BIOGL,S5S833,Protein2Text,Eukaryota,600,"Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad substrate specificity. Acceptor peptides include Muc2, Muc5Ac, Muc1a and Muc1a', with Muc2 as the best acceptor. Acts on non-glycosylated and mono- or multi- glycosylated peptide substrates. Transfers preferably to threonine rather than serine residue. Thr-15 is the most preferred site of glycosylation in Muc2 peptide PTTTPITTTTTVTPTPTPTGTQTK having proline residues at position -1, and at positions +1 and +3, where the number represents the distance from the C-terminal and N-terminal hydroxyl amino acid, respectively. Transfer of the N-acetyl-D-galactosamine (GalNAc) is optimal with proline residues at positions -3, -1, +1 and +3, but other amino acids are tolerated, although some, such as phenylalanine, isoleucine or leucine at -1, or lysine at +3 prevent the transfer completely. Second GalNAc is transferred to Muc2 Thr-2 or Thr-13, both of which have two proline residues nearby. Up to nine sites can be glycosylated within Muc2, but eight are used simultaneously since Thr-19 and Thr-21 are not detected to be glycosylated at the same time. Glycosylation is not detected of a potential site, which is next to an already glycosylated site, but only one amino acid is needed in between two glycosylation sites. Ser-5 is the preferred glycosylation site in Muc5Ac peptide GTTPSPVPTTSTTSAP into which up to four GalNAcs can be attached. Only the threonine residues are detected as pontential glycosylation sites in Muc1a APPAHGVTSAPDTRPAPGC and Muc1a' AHGVTSAPDTR peptides. Transferase activity is restricted to UDP-GalNAc as a donor, and none of the nucleotide sugars UDP-Gal, UDP-GlcNAc, GDP-fucose, UDP-xylose, UDP- glucuronic acid or CMP-neuraminic acid are utilized as donors.","The molecular function of the protein is as a glycosyltransferase, specifically a protein O-mannosyltransferase. It is involved in the transfer of mannose to serine residues of proteins, which is an important step in protein glycosylation.",No,Maybe,Maybe,No,Maybe,not-Yes,GO:0030246; GO:0030145; GO:0004653,GO:0004169,GO:0004169,GO:0004169,GO:0016757,GO:0004169,0.368,0.368,0.368,0.3609,0.368,5,0.3666,0.4575,no
GALT_BIOGL,S5S833,Reference,Eukaryota,600,"Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad substrate specificity. Acceptor peptides include Muc2, Muc5Ac, Muc1a and Muc1a', with Muc2 as the best acceptor. Acts on non-glycosylated and mono- or multi- glycosylated peptide substrates. Transfers preferably to threonine rather than serine residue. Thr-15 is the most preferred site of glycosylation in Muc2 peptide PTTTPITTTTTVTPTPTPTGTQTK having proline residues at position -1, and at positions +1 and +3, where the number represents the distance from the C-terminal and N-terminal hydroxyl amino acid, respectively. Transfer of the N-acetyl-D-galactosamine (GalNAc) is optimal with proline residues at positions -3, -1, +1 and +3, but other amino acids are tolerated, although some, such as phenylalanine, isoleucine or leucine at -1, or lysine at +3 prevent the transfer completely. Second GalNAc is transferred to Muc2 Thr-2 or Thr-13, both of which have two proline residues nearby. Up to nine sites can be glycosylated within Muc2, but eight are used simultaneously since Thr-19 and Thr-21 are not detected to be glycosylated at the same time. Glycosylation is not detected of a potential site, which is next to an already glycosylated site, but only one amino acid is needed in between two glycosylation sites. Ser-5 is the preferred glycosylation site in Muc5Ac peptide GTTPSPVPTTSTTSAP into which up to four GalNAcs can be attached. Only the threonine residues are detected as pontential glycosylation sites in Muc1a APPAHGVTSAPDTRPAPGC and Muc1a' AHGVTSAPDTR peptides. Transferase activity is restricted to UDP-GalNAc as a donor, and none of the nucleotide sugars UDP-Gal, UDP-GlcNAc, GDP-fucose, UDP-xylose, UDP- glucuronic acid or CMP-neuraminic acid are utilized as donors.","Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad substrate specificity. Acceptor peptides include Muc2, Muc5Ac, Muc1a and Muc1a', with Muc2 as the best acceptor. Acts on non-glycosylated and mono- or multi- glycosylated peptide substrates. Transfers preferably to threonine rather than serine residue. Thr-15 is the most preferred site of glycosylation in Muc2 peptide PTTTPITTTTTVTPTPTPTGTQTK having proline residues at position -1, and at positions +1 and +3, where the number represents the distance from the C-terminal and N-terminal hydroxyl amino acid, respectively. Transfer of the N-acetyl-D-galactosamine (GalNAc) is optimal with proline residues at positions -3, -1, +1 and +3, but other amino acids are tolerated, although some, such as phenylalanine, isoleucine or leucine at -1, or lysine at +3 prevent the transfer completely. Second GalNAc is transferred to Muc2 Thr-2 or Thr-13, both of which have two proline residues nearby. Up to nine sites can be glycosylated within Muc2, but eight are used simultaneously since Thr-19 and Thr-21 are not detected to be glycosylated at the same time. Glycosylation is not detected of a potential site, which is next to an already glycosylated site, but only one amino acid is needed in between two glycosylation sites. Ser-5 is the preferred glycosylation site in Muc5Ac peptide GTTPSPVPTTSTTSAP into which up to four GalNAcs can be attached. Only the threonine residues are detected as pontential glycosylation sites in Muc1a APPAHGVTSAPDTRPAPGC and Muc1a' AHGVTSAPDTR peptides. Transferase activity is restricted to UDP-GalNAc as a donor, and none of the nucleotide sugars UDP-Gal, UDP-GlcNAc, GDP-fucose, UDP-xylose, UDP- glucuronic acid or CMP-neuraminic acid are utilized as donors.",,,,,,,GO:0030246; GO:0030145; GO:0004653,GO:0004653,GO:0004653,GO:0004653,GO:0004653,GO:0004653,0.5522,0.5522,0.5522,0.5522,0.5522,5,0.5522,0.4575,no
MAPKL_TOXGM,S8EUF0,ESM2Text,Eukaryota,1298,Probable serine/threonine-protein kinase (Probable). Plays a role in coordinated progression of cytokinesis. Restricts duplication of centrosome core structures to one per cycle and ensures proper formation and number of new daughter parasites.,(Microbial infection) Mediates the entry of human coronavirus SARS-CoV-2 into the nucleus.,No,No,No,No,Maybe,not-Yes,GO:0005524; GO:0004707; GO:0106310,,,,,,,,,,,0,,0.7011,yes
MAPKL_TOXGM,S8EUF0,Prot2Text,Eukaryota,1298,Probable serine/threonine-protein kinase (Probable). Plays a role in coordinated progression of cytokinesis. Restricts duplication of centrosome core structures to one per cycle and ensures proper formation and number of new daughter parasites.,"Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor B (P-TEFb), which facilitates the transition from abortive to production elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) and SUPT5H.",No,No,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0004707; GO:0106310,GO:0016538,GO:0016538,GO:0016538,GO:0016538,GO:0016538,0.0634,0.0634,0.0634,0.0634,0.0634,5,0.0634,0.7011,yes
MAPKL_TOXGM,S8EUF0,ProtT3,Eukaryota,1298,Probable serine/threonine-protein kinase (Probable). Plays a role in coordinated progression of cytokinesis. Restricts duplication of centrosome core structures to one per cycle and ensures proper formation and number of new daughter parasites.,Serine/threonine-protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Controls osmotic regulation of transcription of target genes (By similarity). Cytoplasm Nucleus. Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily. HOG1 sub-subfamily,Maybe,Yes,Yes,Maybe,Vague,not-Yes,GO:0005524; GO:0004707; GO:0106310,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0004707; GO:0005524,GO:0004707; GO:0004674; GO:0005524,GO:0004707; GO:0005524,0.9277,0.9277,0.9549,0.9549,0.9492,5,0.9429,0.7011,yes
MAPKL_TOXGM,S8EUF0,ProtTale,Eukaryota,1298,Probable serine/threonine-protein kinase (Probable). Plays a role in coordinated progression of cytokinesis. Restricts duplication of centrosome core structures to one per cycle and ensures proper formation and number of new daughter parasites.,Serine/threonine-protein kinase that phosphorylates 'Ser-2' and 'Ser-5' of the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A and POLR2B. Acts as a negative regulator of transcription by RNA polymerase II. Required for normal embryonic development.,Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004707; GO:0106310,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0008353,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.9277,0.9277,0.6919,0.9277,0.9277,5,0.8805,0.7011,yes
MAPKL_TOXGM,S8EUF0,Protein2Text,Eukaryota,1298,Probable serine/threonine-protein kinase (Probable). Plays a role in coordinated progression of cytokinesis. Restricts duplication of centrosome core structures to one per cycle and ensures proper formation and number of new daughter parasites.,"The molecular function of this protein is not explicitly stated in the provided text. However, based on its name and the context in which it is mentioned, it is likely involved in a signaling pathway.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0005524; GO:0004707; GO:0106310,,,,,,,,,,,0,,0.7011,yes
MAPKL_TOXGM,S8EUF0,Reference,Eukaryota,1298,Probable serine/threonine-protein kinase (Probable). Plays a role in coordinated progression of cytokinesis. Restricts duplication of centrosome core structures to one per cycle and ensures proper formation and number of new daughter parasites.,Probable serine/threonine-protein kinase (Probable). Plays a role in coordinated progression of cytokinesis. Restricts duplication of centrosome core structures to one per cycle and ensures proper formation and number of new daughter parasites.,,,,,,,GO:0005524; GO:0004707; GO:0106310,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674,GO:0004674,0.9277,0.9277,0.6732,0.6732,0.6732,5,0.775,0.7011,yes
NEK_TOXGM,S8GI44,ESM2Text,Eukaryota,1598,Probable serine/threonine-protein kinase (Probable). Involved in controlling centrosome splitting. Promotes separation of the centrosome outer cores.,"Serine/threonine-protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK12/MKK12 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokines or physical stress leading to direct activation of transcription factors such as ELK1. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. MAPK12/MKK12 may also be involved in the activation of specific downstream effectors including MAPKAPK1, MAPKAPK2, MAPKAPK3 and MAPKAPK5. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. Plays an important role in the regulation of the cytoskeleton through phosphorylating and inactivating the actin cytoskeleton-associated protein and myosin. Phosphorylates DLG4. Mediates phosphorylation of DLG4 at 'Thr-183' and 'Ser-185' and may also regulate the activity",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0004707,GO:0004674; GO:0004707,GO:0004674; GO:0004707,GO:0004674,0.964,0.7567,0.7567,0.7567,0.7186,5,0.7905,0.6733,yes
NEK_TOXGM,S8GI44,Prot2Text,Eukaryota,1598,Probable serine/threonine-protein kinase (Probable). Involved in controlling centrosome splitting. Promotes separation of the centrosome outer cores.,"Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. Plays a role in chromosome condensation and is involved in the formation of the first mitotic exit site (MES), a dynamic structure preceding the second metaphase, through phosphorylation of proteins such as cyclin CYCH1-1. Also involved in the formation of the first meiotic division complex (MEDC), a complex required for the progression of meiosis II and mitosis. Plays a role in the regulation of cellular growth and survival.",Maybe,Yes,Maybe,Maybe,No,not-Yes,GO:0005524; GO:0106310; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674; GO:0005524,0.7186,0.7186,0.7186,0.7186,0.964,5,0.7677,0.6733,yes
NEK_TOXGM,S8GI44,ProtT3,Eukaryota,1598,Probable serine/threonine-protein kinase (Probable). Involved in controlling centrosome splitting. Promotes separation of the centrosome outer cores.,Belongs to the protein kinase superfamily. Ser/Thr protein kinase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.964,0.964,0.964,0.964,0.964,5,0.964,0.6733,yes
NEK_TOXGM,S8GI44,ProtTale,Eukaryota,1598,Probable serine/threonine-protein kinase (Probable). Involved in controlling centrosome splitting. Promotes separation of the centrosome outer cores.,"Serine/threonine kinase involved in centrosome duplication, mitotic spindle assembly, and chromosome segregation. Acts as a regulator of centrosome duplication by phosphorylating the C-terminal domain (CTD) of nucleophosmin/NPM1. This modification is required for the association of NPM1 with centriolar satellites, which is necessary for the formation of a functional centrosome. Also plays a role in the regulation of mitotic spindle assembly by mediating the phosphorylation and activation of AURKB, leading to inhibition of AURKB kinase activity, dephosphorylation of KMN1/Nuf2 and subsequent recruitment of AUR",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.964,0.964,0.7186,0.964,0.964,5,0.9149,0.6733,yes
NEK_TOXGM,S8GI44,Protein2Text,Eukaryota,1598,Probable serine/threonine-protein kinase (Probable). Involved in controlling centrosome splitting. Promotes separation of the centrosome outer cores.,This protein is involved in the molecular function of guanylate cyclase activity.,No,No,No,No,No,not-Yes,GO:0005524; GO:0106310; GO:0004674,GO:0004383,GO:0004383,GO:0004383,GO:0004383,GO:0004383,0.1727,0.1727,0.1727,0.1727,0.1727,5,0.1727,0.6733,yes
NEK_TOXGM,S8GI44,Reference,Eukaryota,1598,Probable serine/threonine-protein kinase (Probable). Involved in controlling centrosome splitting. Promotes separation of the centrosome outer cores.,Probable serine/threonine-protein kinase (Probable). Involved in controlling centrosome splitting. Promotes separation of the centrosome outer cores.,,,,,,,GO:0005524; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674,GO:0004674,0.964,0.964,0.7186,0.7186,0.7186,5,0.8168,0.6733,yes
OXDA_DUGRY,T2HG31,ESM2Text,Eukaryota,332,"Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Could be responsible for the degradation of diet-derived D-alanine in the intestine. Maintains the asexual state of worms and represses early ovarian development. Following sexual induction, the enzyme is required for differentiation of oogonia into oocytes in the developing ovaries.","Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate. Highest catalytic efficiency for D-Glu followed by D-Asp and NMDA. May play a role in the egg-laying events and early development of the worm, in addition to quality control of the germ cells.",Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0003884; GO:0071949; GO:0043799,GO:0003884,GO:0003884,GO:0033182,GO:0033781,GO:0008453,0.6411,0.6411,0.0,0.215,0.1442,5,0.3283,0.2042,no
OXDA_DUGRY,T2HG31,Prot2Text,Eukaryota,332,"Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Could be responsible for the degradation of diet-derived D-alanine in the intestine. Maintains the asexual state of worms and represses early ovarian development. Following sexual induction, the enzyme is required for differentiation of oogonia into oocytes in the developing ovaries.","Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate. Highest catalytic efficiency for D-Glu followed by D-Asp and NMDA. May play a role in the egg-laying events and early development of the worm, in addition to quality control of the germ cells.",Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0003884; GO:0071949; GO:0043799,GO:0033735,GO:0033182,GO:0008445,GO:0033792,GO:0033735,0.2949,0.0,0.5625,0.2324,0.2949,5,0.2769,0.2042,no
OXDA_DUGRY,T2HG31,ProtT3,Eukaryota,332,"Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Could be responsible for the degradation of diet-derived D-alanine in the intestine. Maintains the asexual state of worms and represses early ovarian development. Following sexual induction, the enzyme is required for differentiation of oogonia into oocytes in the developing ovaries.",Peroxisome. Belongs to the DAMOX/DASOX family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0003884; GO:0071949; GO:0043799,GO:0003863,GO:0003884,GO:0003884; GO:0050660,GO:0003863; GO:0071949,GO:0003884,0.2324,0.6411,0.8666,0.572,0.6411,5,0.5906,0.2042,no
OXDA_DUGRY,T2HG31,ProtTale,Eukaryota,332,"Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Could be responsible for the degradation of diet-derived D-alanine in the intestine. Maintains the asexual state of worms and represses early ovarian development. Following sexual induction, the enzyme is required for differentiation of oogonia into oocytes in the developing ovaries.",Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003884; GO:0071949; GO:0043799,GO:0003884,GO:0003862,GO:0003884,GO:0003884,GO:0003884,0.6411,0.2324,0.6411,0.6411,0.6411,5,0.5594,0.2042,no
OXDA_DUGRY,T2HG31,Protein2Text,Eukaryota,332,"Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Could be responsible for the degradation of diet-derived D-alanine in the intestine. Maintains the asexual state of worms and represses early ovarian development. Following sexual induction, the enzyme is required for differentiation of oogonia into oocytes in the developing ovaries.","The molecular function of this protein is an aminotransferase, which is an enzyme that catalyzes the transfer of an amino group from an amino acid to a keto acid.",No,No,No,No,Maybe,not-Yes,GO:0003884; GO:0071949; GO:0043799,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.171,0.171,0.171,0.171,0.171,5,0.171,0.2042,no
OXDA_DUGRY,T2HG31,Reference,Eukaryota,332,"Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Could be responsible for the degradation of diet-derived D-alanine in the intestine. Maintains the asexual state of worms and represses early ovarian development. Following sexual induction, the enzyme is required for differentiation of oogonia into oocytes in the developing ovaries.","Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Could be responsible for the degradation of diet-derived D-alanine in the intestine. Maintains the asexual state of worms and represses early ovarian development. Following sexual induction, the enzyme is required for differentiation of oogonia into oocytes in the developing ovaries.",,,,,,,GO:0003884; GO:0071949; GO:0043799,GO:0003884,GO:0003884,GO:0003884,GO:0003884,GO:0003884,0.6411,0.6411,0.6411,0.6411,0.6411,5,0.6411,0.2042,no
GLG_NEUCR,V5ILS6,ESM2Text,Eukaryota,686,"Self-glucosylating initiator of glycogen synthesis. It catalyzes the formation of a short alpha (1,4)-glucosyl chain covalently attached via a glucose 1-O- tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase.","Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0008466; GO:0016757; GO:0046872,GO:0008466,GO:0016757,GO:0008466,GO:0004370,GO:0008466,0.6553,0.6701,0.6553,0.2937,0.6553,5,0.5859,0.5778,yes
GLG_NEUCR,V5ILS6,Prot2Text,Eukaryota,686,"Self-glucosylating initiator of glycogen synthesis. It catalyzes the formation of a short alpha (1,4)-glucosyl chain covalently attached via a glucose 1-O- tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase.",May be involved in the polymorphic O-glycosylation of the serine-rich repeat protein PsrP.,No,No,No,No,No,not-Yes,GO:0008466; GO:0016757; GO:0046872,,,,,,,,,,,0,,0.5778,yes
GLG_NEUCR,V5ILS6,ProtT3,Eukaryota,686,"Self-glucosylating initiator of glycogen synthesis. It catalyzes the formation of a short alpha (1,4)-glucosyl chain covalently attached via a glucose 1-O- tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase.",Catalytic subunit of the glycogen synthase complex that catalyzes the synthesis of glycogen from glucose-1-phosphate. Belongs to the glycosyltransferase 1 family. Glycogen synthase subfamily,Maybe,Maybe,No,No,Maybe,not-Yes,GO:0008466; GO:0016757; GO:0046872,GO:0004373,GO:0004373,GO:0004373,GO:0004373,GO:0004373,0.5142,0.5142,0.5142,0.5142,0.5142,5,0.5142,0.5778,yes
GLG_NEUCR,V5ILS6,ProtTale,Eukaryota,686,"Self-glucosylating initiator of glycogen synthesis. It catalyzes the formation of a short alpha (1,4)-glucosyl chain covalently attached via a glucose 1-O- tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase.","Glycosyltransferase involved in the biosynthesis of mannosylglucosylceramide (MGC), a MGC that contains a single alpha-1,3-linked mannose residue. Catalyzes the transfer of the first mannose residue from UDP-alpha-D-mannose to glucosylceramide.",No,No,No,No,No,not-Yes,GO:0008466; GO:0016757; GO:0046872,GO:0016757,GO:0016757,GO:0000030,GO:0016757,GO:0016757,0.6701,0.6701,0.5207,0.6701,0.6701,5,0.6402,0.5778,yes
GLG_NEUCR,V5ILS6,Protein2Text,Eukaryota,686,"Self-glucosylating initiator of glycogen synthesis. It catalyzes the formation of a short alpha (1,4)-glucosyl chain covalently attached via a glucose 1-O- tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase.","The molecular function of this protein is not specified in the provided information. However, based on the name ""protein"" and its association with the term ""glycosyltransferase"", it is likely that this protein is involved in catalyzing the transfer of a sugar moiety to another molecule, possibly as part of the synthesis of glycans. 

More specifically, the protein is a type of enzyme that catalyzes the transfer of a sugar residue to a growing glycogen chain during glycogen synthesis. It is a key enzyme in the process of glycogen synthesis, which is important for energy storage in cells. 

It is worth noting that the exact molecular function of this protein may depend on the specific isoform or variant being referred to, as different isoforms or variants of the same protein can have different functions.",Vague,Maybe,Vague,Vague,Maybe,not-Yes,GO:0008466; GO:0016757; GO:0046872,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.6701,0.6701,0.6701,0.6701,0.6701,5,0.6701,0.5778,yes
GLG_NEUCR,V5ILS6,Reference,Eukaryota,686,"Self-glucosylating initiator of glycogen synthesis. It catalyzes the formation of a short alpha (1,4)-glucosyl chain covalently attached via a glucose 1-O- tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase.","Self-glucosylating initiator of glycogen synthesis. It catalyzes the formation of a short alpha (1,4)-glucosyl chain covalently attached via a glucose 1-O- tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase.",,,,,,,GO:0008466; GO:0016757; GO:0046872,GO:0004584,GO:0008466,GO:0008466,GO:0008466,GO:0004346,0.0,0.6553,0.6553,0.6553,0.1355,5,0.4203,0.5778,yes
VUUB_VIBVL,V5XKC3,ESM2Text,Bacteria,271,"Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell (Probable). Acts as a major ferric-vulnibactin reductase catalyzing the reduction of Fe(3+)-vulnibactin, a catecholate siderophore synthesized by V.vulnificus. Catalyzes reduction of Fe(3+)-aerobactin, a citrate- hydroxamate siderophore produced by other bacteria, in the absence of IutB. Catalyzes reduction of Fe(3+)- vibriobactin in vitro. No activity with ferrioxamine B or Fe(3+)- enterobactin. Catalyzes reduction of ferric chelating compounds Fe(3+)- nitrilotriacetic acid (NTA), Fe(3+)-citrate and Fe(3+)-EDTA as well as non-complexed FeCl3 in the presence of NADH as its electron donor and FAD as its cofactor in vitro. Highest activity with Fe(3+)-NTA as electron acceptor.",Involved in iron homeostasis. Transports iron-bound molybdenum compounds to the periplasm. It can also transport tetrapyrrole compounds.,No,No,No,No,No,not-Yes,GO:0140618,GO:0005215,GO:0005215,,,,0.1793,0.1793,,,,2,0.1793,0.215,no
VUUB_VIBVL,V5XKC3,Prot2Text,Bacteria,271,"Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell (Probable). Acts as a major ferric-vulnibactin reductase catalyzing the reduction of Fe(3+)-vulnibactin, a catecholate siderophore synthesized by V.vulnificus. Catalyzes reduction of Fe(3+)-aerobactin, a citrate- hydroxamate siderophore produced by other bacteria, in the absence of IutB. Catalyzes reduction of Fe(3+)- vibriobactin in vitro. No activity with ferrioxamine B or Fe(3+)- enterobactin. Catalyzes reduction of ferric chelating compounds Fe(3+)- nitrilotriacetic acid (NTA), Fe(3+)-citrate and Fe(3+)-EDTA as well as non-complexed FeCl3 in the presence of NADH as its electron donor and FAD as its cofactor in vitro. Highest activity with Fe(3+)-NTA as electron acceptor.",Involved in intracellular removal of iron from iron-vibriobactin complex. Vibriobactin is an iron-chelating compound involved in the transport of iron from the bacterial environment into the cell cytoplasm.,Maybe,Yes,Maybe,Maybe,No,not-Yes,GO:0140618,,,,,,,,,,,0,,0.215,no
VUUB_VIBVL,V5XKC3,ProtT3,Bacteria,271,"Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell (Probable). Acts as a major ferric-vulnibactin reductase catalyzing the reduction of Fe(3+)-vulnibactin, a catecholate siderophore synthesized by V.vulnificus. Catalyzes reduction of Fe(3+)-aerobactin, a citrate- hydroxamate siderophore produced by other bacteria, in the absence of IutB. Catalyzes reduction of Fe(3+)- vibriobactin in vitro. No activity with ferrioxamine B or Fe(3+)- enterobactin. Catalyzes reduction of ferric chelating compounds Fe(3+)- nitrilotriacetic acid (NTA), Fe(3+)-citrate and Fe(3+)-EDTA as well as non-complexed FeCl3 in the presence of NADH as its electron donor and FAD as its cofactor in vitro. Highest activity with Fe(3+)-NTA as electron acceptor.",Cytoplasm. Belongs to the bacterial solute-binding protein 2 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0140618,,,,,,,,,,,0,,0.215,no
VUUB_VIBVL,V5XKC3,ProtTale,Bacteria,271,"Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell (Probable). Acts as a major ferric-vulnibactin reductase catalyzing the reduction of Fe(3+)-vulnibactin, a catecholate siderophore synthesized by V.vulnificus. Catalyzes reduction of Fe(3+)-aerobactin, a citrate- hydroxamate siderophore produced by other bacteria, in the absence of IutB. Catalyzes reduction of Fe(3+)- vibriobactin in vitro. No activity with ferrioxamine B or Fe(3+)- enterobactin. Catalyzes reduction of ferric chelating compounds Fe(3+)- nitrilotriacetic acid (NTA), Fe(3+)-citrate and Fe(3+)-EDTA as well as non-complexed FeCl3 in the presence of NADH as its electron donor and FAD as its cofactor in vitro. Highest activity with Fe(3+)-NTA as electron acceptor.","Catalyzes the oxidation of iron(II) to iron(III), and may play a role in intracellular iron homeostasis (Probable).",No,No,No,No,No,not-Yes,GO:0140618,GO:0016491,GO:0016491,GO:0004322,GO:0004322,GO:0004322,0.5324,0.5324,0.462,0.462,0.462,5,0.4902,0.215,no
VUUB_VIBVL,V5XKC3,Protein2Text,Bacteria,271,"Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell (Probable). Acts as a major ferric-vulnibactin reductase catalyzing the reduction of Fe(3+)-vulnibactin, a catecholate siderophore synthesized by V.vulnificus. Catalyzes reduction of Fe(3+)-aerobactin, a citrate- hydroxamate siderophore produced by other bacteria, in the absence of IutB. Catalyzes reduction of Fe(3+)- vibriobactin in vitro. No activity with ferrioxamine B or Fe(3+)- enterobactin. Catalyzes reduction of ferric chelating compounds Fe(3+)- nitrilotriacetic acid (NTA), Fe(3+)-citrate and Fe(3+)-EDTA as well as non-complexed FeCl3 in the presence of NADH as its electron donor and FAD as its cofactor in vitro. Highest activity with Fe(3+)-NTA as electron acceptor.",This protein is a part of the electron transport chain and has a molecular function of catalyzing the conversion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS).,No,No,No,No,No,not-Yes,GO:0140618,,GO:0004604,,GO:0004604,,,0.3055,,0.3055,,2,0.3055,0.215,no
VUUB_VIBVL,V5XKC3,Reference,Bacteria,271,"Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell (Probable). Acts as a major ferric-vulnibactin reductase catalyzing the reduction of Fe(3+)-vulnibactin, a catecholate siderophore synthesized by V.vulnificus. Catalyzes reduction of Fe(3+)-aerobactin, a citrate- hydroxamate siderophore produced by other bacteria, in the absence of IutB. Catalyzes reduction of Fe(3+)- vibriobactin in vitro. No activity with ferrioxamine B or Fe(3+)- enterobactin. Catalyzes reduction of ferric chelating compounds Fe(3+)- nitrilotriacetic acid (NTA), Fe(3+)-citrate and Fe(3+)-EDTA as well as non-complexed FeCl3 in the presence of NADH as its electron donor and FAD as its cofactor in vitro. Highest activity with Fe(3+)-NTA as electron acceptor.","Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell (Probable). Acts as a major ferric-vulnibactin reductase catalyzing the reduction of Fe(3+)-vulnibactin, a catecholate siderophore synthesized by V.vulnificus. Catalyzes reduction of Fe(3+)-aerobactin, a citrate- hydroxamate siderophore produced by other bacteria, in the absence of IutB. Catalyzes reduction of Fe(3+)- vibriobactin in vitro. No activity with ferrioxamine B or Fe(3+)- enterobactin. Catalyzes reduction of ferric chelating compounds Fe(3+)- nitrilotriacetic acid (NTA), Fe(3+)-citrate and Fe(3+)-EDTA as well as non-complexed FeCl3 in the presence of NADH as its electron donor and FAD as its cofactor in vitro. Highest activity with Fe(3+)-NTA as electron acceptor.",,,,,,,GO:0140618,GO:0016491,GO:0000293; GO:0071949,GO:0016491,GO:0016491,GO:0052851,0.5324,0.5351,0.5324,0.5324,0.7772,5,0.5819,0.215,no
UBA4_OGAPD,W1QET1,ESM2Text,Eukaryota,389,"Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and CNX5/MOCS2A. Its N- terminus first activates urm1 and mocs2a as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and CNX5/MOCS2A to form thiocarboxylation (-COSH) of their C- terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards URM1 and CNX5/MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. Required for growth on nitrate as a sole nitrogen source.","Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0042802; GO:0046872; GO:0061605; GO:0061604; GO:0004792; GO:0042292,GO:0008641,,,,,0.3472,,,,,1,0.3472,0.3732,no
UBA4_OGAPD,W1QET1,Prot2Text,Eukaryota,389,"Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and CNX5/MOCS2A. Its N- terminus first activates urm1 and mocs2a as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and CNX5/MOCS2A to form thiocarboxylation (-COSH) of their C- terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards URM1 and CNX5/MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. Required for growth on nitrate as a sole nitrogen source.","Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Acts by mediating the C-terminal thiocarboxylation of sulfur carrier URM1. Its N-terminus first activates URM1 as acyl-adenylate (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 to form thiocarboxylation (-COSH) of its C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0042802; GO:0046872; GO:0061605; GO:0061604; GO:0004792; GO:0042292,GO:0016874,,GO:0008641,,GO:0016783; GO:0005524,0.315,,0.3472,,0.6227,3,0.4283,0.3732,no
UBA4_OGAPD,W1QET1,ProtT3,Eukaryota,389,"Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and CNX5/MOCS2A. Its N- terminus first activates urm1 and mocs2a as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and CNX5/MOCS2A to form thiocarboxylation (-COSH) of their C- terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards URM1 and CNX5/MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. Required for growth on nitrate as a sole nitrogen source.","Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and URM2. Its N-terminus first activates URM1 and URM2 as acyl- adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and URM2 to form thiocarboxylated URM1 and URM",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0042802; GO:0046872; GO:0061605; GO:0061604; GO:0004792; GO:0042292,GO:0097027,,GO:0008641,,GO:0008641,0.0904,,0.3472,,0.3472,3,0.2616,0.3732,no
UBA4_OGAPD,W1QET1,ProtTale,Eukaryota,389,"Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and CNX5/MOCS2A. Its N- terminus first activates urm1 and mocs2a as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and CNX5/MOCS2A to form thiocarboxylation (-COSH) of their C- terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards URM1 and CNX5/MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. Required for growth on nitrate as a sole nitrogen source.","Catalyzes the ATP-dependent conversion of 7,8-dihydroneopterin triphosphate to 6-hydroxymethyl-7,8-dihydroneopterin 2,3-diphosphate.",No,No,No,No,No,not-Yes,GO:0005524; GO:0042802; GO:0046872; GO:0061605; GO:0061604; GO:0004792; GO:0042292,GO:0005524,GO:0003824,,,GO:0016787,0.3346,0.3488,,,0.2703,3,0.3179,0.3732,no
UBA4_OGAPD,W1QET1,Protein2Text,Eukaryota,389,"Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and CNX5/MOCS2A. Its N- terminus first activates urm1 and mocs2a as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and CNX5/MOCS2A to form thiocarboxylation (-COSH) of their C- terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards URM1 and CNX5/MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. Required for growth on nitrate as a sole nitrogen source.","The molecular function of this protein is a dioxygenase, specifically a N(5)-carboxyaminoimidazole ribonucleotide synthase, which is involved in the purine biosynthesis pathway.",No,No,No,No,No,not-Yes,GO:0005524; GO:0042802; GO:0046872; GO:0061605; GO:0061604; GO:0004792; GO:0042292,,GO:0051213,,,,,0.218,,,,1,0.218,0.3732,no
UBA4_OGAPD,W1QET1,Reference,Eukaryota,389,"Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and CNX5/MOCS2A. Its N- terminus first activates urm1 and mocs2a as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and CNX5/MOCS2A to form thiocarboxylation (-COSH) of their C- terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards URM1 and CNX5/MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. Required for growth on nitrate as a sole nitrogen source.","Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and CNX5/MOCS2A. Its N- terminus first activates urm1 and mocs2a as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and CNX5/MOCS2A to form thiocarboxylation (-COSH) of their C- terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards URM1 and CNX5/MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. Required for growth on nitrate as a sole nitrogen source.",,,,,,,GO:0005524; GO:0042802; GO:0046872; GO:0061605; GO:0061604; GO:0004792; GO:0042292,GO:0016874; GO:0005524,GO:0008641,GO:0016779; GO:0016783,GO:0016783,GO:0016779; GO:0016783,0.5071,0.3472,0.5135,0.433,0.5135,5,0.4629,0.3732,no
LPH_SHEEP,W5PLZ6,ESM2Text,Eukaryota,1931,"Broad specificity glycosidase of the intestinal brush border membrane that hydrolyzes lactose, the main sugar in mammalian milk, to produce D-glucose and D-galactose. The mature protein is composed of two domains that catalyze the hydrolysis of beta- glucopyranosides and beta-galactopyranosides, with a preference for hydrophilic aglycones (in lactose and cellobiose) for one domain and hydrophobic aglycones (in phlorizin and glycosylceramides) for the other.","Broad specificity glycosidase of the intestinal brush border membrane that hydrolyzes lactose, the main sugar in mammalian milk, to produce D-glucose and D-galactose. The mature protein is composed of two domains that catalyze the hydrolysis of beta-glucopyranosides and beta-galactopyranosides, with a preference for hydrophilic aglycones (in lactose and cellobiose) for one domain and hydrophobic aglycones (in phlorizin and glycosylceramides) for the other.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008422; GO:0004336; GO:0004348; GO:0000016; GO:0140749,GO:0004565,GO:0004565; GO:0008422,GO:0004565,GO:0004565,GO:0000016,0.589,0.7128,0.589,0.589,0.7716,5,0.6503,0.2486,no
LPH_SHEEP,W5PLZ6,Prot2Text,Eukaryota,1931,"Broad specificity glycosidase of the intestinal brush border membrane that hydrolyzes lactose, the main sugar in mammalian milk, to produce D-glucose and D-galactose. The mature protein is composed of two domains that catalyze the hydrolysis of beta- glucopyranosides and beta-galactopyranosides, with a preference for hydrophilic aglycones (in lactose and cellobiose) for one domain and hydrophobic aglycones (in phlorizin and glycosylceramides) for the other.","Broad specificity glycosidase of the intestinal brush border membrane that hydrolyzes lactose, the main sugar in mammalian milk, to produce D-glucose and D-galactose. The mature protein is composed of two domains that catalyze the hydrolysis of beta-glucopyranosides and beta-galactopyranosides, with a preference for hydrophilic aglycones (in lactose and cellobiose) for one domain and hydrophobic aglycones (in phlorizin and glycosylceramides) for the other.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008422; GO:0004336; GO:0004348; GO:0000016; GO:0140749,GO:0004565; GO:0004566,GO:0004565; GO:0008422,GO:0004565,GO:0004565,GO:0004565; GO:0004553,0.5954,0.7128,0.589,0.589,0.7814,5,0.6535,0.2486,no
LPH_SHEEP,W5PLZ6,ProtT3,Eukaryota,1931,"Broad specificity glycosidase of the intestinal brush border membrane that hydrolyzes lactose, the main sugar in mammalian milk, to produce D-glucose and D-galactose. The mature protein is composed of two domains that catalyze the hydrolysis of beta- glucopyranosides and beta-galactopyranosides, with a preference for hydrophilic aglycones (in lactose and cellobiose) for one domain and hydrophobic aglycones (in phlorizin and glycosylceramides) for the other.",Belongs to the glycosyl hydrolase 1 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008422; GO:0004336; GO:0004348; GO:0000016; GO:0140749,GO:0008422,GO:0008422,GO:0008422,GO:0008422,GO:0008422,0.726,0.726,0.726,0.726,0.726,5,0.726,0.2486,no
LPH_SHEEP,W5PLZ6,ProtTale,Eukaryota,1931,"Broad specificity glycosidase of the intestinal brush border membrane that hydrolyzes lactose, the main sugar in mammalian milk, to produce D-glucose and D-galactose. The mature protein is composed of two domains that catalyze the hydrolysis of beta- glucopyranosides and beta-galactopyranosides, with a preference for hydrophilic aglycones (in lactose and cellobiose) for one domain and hydrophobic aglycones (in phlorizin and glycosylceramides) for the other.","May play an important role in the catabolism of extracellular matrix polysaccharides, such as heparan and heparan sulfate.",No,No,No,No,No,not-Yes,GO:0008422; GO:0004336; GO:0004348; GO:0000016; GO:0140749,,,,,,,,,,,0,,0.2486,no
LPH_SHEEP,W5PLZ6,Protein2Text,Eukaryota,1931,"Broad specificity glycosidase of the intestinal brush border membrane that hydrolyzes lactose, the main sugar in mammalian milk, to produce D-glucose and D-galactose. The mature protein is composed of two domains that catalyze the hydrolysis of beta- glucopyranosides and beta-galactopyranosides, with a preference for hydrophilic aglycones (in lactose and cellobiose) for one domain and hydrophobic aglycones (in phlorizin and glycosylceramides) for the other.","This protein is a lectin, which means it has a carbohydrate-binding activity. It is specifically involved in binding to galactose and N-acetylglucosamine residues on glycoproteins and glycolipids. This binding activity is crucial for its role in the digestion of galactose-containing oligosaccharides in the intestinal lumen.",No,No,No,No,Maybe,not-Yes,GO:0008422; GO:0004336; GO:0004348; GO:0000016; GO:0140749,GO:0030246,GO:0030246,GO:0030246,GO:0030246,GO:0030246,0.1495,0.1495,0.1495,0.1495,0.1495,5,0.1495,0.2486,no
LPH_SHEEP,W5PLZ6,Reference,Eukaryota,1931,"Broad specificity glycosidase of the intestinal brush border membrane that hydrolyzes lactose, the main sugar in mammalian milk, to produce D-glucose and D-galactose. The mature protein is composed of two domains that catalyze the hydrolysis of beta- glucopyranosides and beta-galactopyranosides, with a preference for hydrophilic aglycones (in lactose and cellobiose) for one domain and hydrophobic aglycones (in phlorizin and glycosylceramides) for the other.","Broad specificity glycosidase of the intestinal brush border membrane that hydrolyzes lactose, the main sugar in mammalian milk, to produce D-glucose and D-galactose. The mature protein is composed of two domains that catalyze the hydrolysis of beta- glucopyranosides and beta-galactopyranosides, with a preference for hydrophilic aglycones (in lactose and cellobiose) for one domain and hydrophobic aglycones (in phlorizin and glycosylceramides) for the other.",,,,,,,GO:0008422; GO:0004336; GO:0004348; GO:0000016; GO:0140749,GO:0004565,GO:0000016; GO:0008422,GO:0004565,GO:0004565,GO:0004565,0.589,0.8566,0.589,0.589,0.589,5,0.6425,0.2486,no
CTMB_CASD6,W8X092,ESM2Text,Bacteria,549,"Involved in the degradation of the cyclic monoterpene limonene. Catalyzes the oxidation of limonene at the primary methyl group, forming perillyl alcohol. Hydroxylates the R- and S-enantiomers to their respective enantiomeric form of perillyl alcohol at a similar rate. Native CtmAB oxidizes a wide range of monocyclic monoterpenes containing the allylic methyl group motif (1-methyl- cyclohex-1-ene). Can also catalyze the reverse reaction, the reduction of perillyl alcohol to limonene, but with lower efficiency. Cannot use molecular oxygen as an electron acceptor. The natural electron acceptor is likely a heterodimeric electron transfer flavoprotein (ETF) (Probable).","Glycosylated dehydrogenase that catalyzes the cis-trans isomerization of choline to trans-3-hydroxy-choline (c3HCE). Converts 3,4-dichlorocatechol to propionolotol, which is in turn converted to the bicarbonate semialdehyde, an intermediate in the process of cholesterol degradation by CCR (CoA). Can also convert 3,5-dichlorocatechol to the bicarbonate semialdehyde, bicarbonate to butanol, catechol to propanoate and catechol to butyrate.",No,No,No,No,No,not-Yes,GO:0016491,GO:0016491,GO:0016491,,GO:0016491,,1.0,1.0,,1.0,,3,1.0,0.1685,no
CTMB_CASD6,W8X092,Prot2Text,Bacteria,549,"Involved in the degradation of the cyclic monoterpene limonene. Catalyzes the oxidation of limonene at the primary methyl group, forming perillyl alcohol. Hydroxylates the R- and S-enantiomers to their respective enantiomeric form of perillyl alcohol at a similar rate. Native CtmAB oxidizes a wide range of monocyclic monoterpenes containing the allylic methyl group motif (1-methyl- cyclohex-1-ene). Can also catalyze the reverse reaction, the reduction of perillyl alcohol to limonene, but with lower efficiency. Cannot use molecular oxygen as an electron acceptor. The natural electron acceptor is likely a heterodimeric electron transfer flavoprotein (ETF) (Probable).","Involved in the biosynthesis of the yellow-orange carotenoid staphyloxanthin, which plays a role in the virulence via its protective function against oxidative stress. Catalyzes the oxidation of the terminal methyl side group of 4,4'-diaponeurosporene to form 4,4'-diaponeurosporen-4-al.",No,Maybe,No,No,No,not-Yes,GO:0016491,GO:0004030,GO:0004030,,GO:0016614,GO:0016614,0.6019,0.6019,,0.8145,0.8145,4,0.7082,0.1685,no
CTMB_CASD6,W8X092,ProtT3,Bacteria,549,"Involved in the degradation of the cyclic monoterpene limonene. Catalyzes the oxidation of limonene at the primary methyl group, forming perillyl alcohol. Hydroxylates the R- and S-enantiomers to their respective enantiomeric form of perillyl alcohol at a similar rate. Native CtmAB oxidizes a wide range of monocyclic monoterpenes containing the allylic methyl group motif (1-methyl- cyclohex-1-ene). Can also catalyze the reverse reaction, the reduction of perillyl alcohol to limonene, but with lower efficiency. Cannot use molecular oxygen as an electron acceptor. The natural electron acceptor is likely a heterodimeric electron transfer flavoprotein (ETF) (Probable).",Cell membrane; Multi-pass membrane protein. Belongs to the carotenoid/retinoid oxidoreductase family,Vague,Vague,Vague,Vague,No,not-Yes,GO:0016491,GO:0010333,GO:0010333,,GO:0010333,GO:0010333,0.3552,0.3552,,0.3552,0.3552,4,0.3552,0.1685,no
CTMB_CASD6,W8X092,ProtTale,Bacteria,549,"Involved in the degradation of the cyclic monoterpene limonene. Catalyzes the oxidation of limonene at the primary methyl group, forming perillyl alcohol. Hydroxylates the R- and S-enantiomers to their respective enantiomeric form of perillyl alcohol at a similar rate. Native CtmAB oxidizes a wide range of monocyclic monoterpenes containing the allylic methyl group motif (1-methyl- cyclohex-1-ene). Can also catalyze the reverse reaction, the reduction of perillyl alcohol to limonene, but with lower efficiency. Cannot use molecular oxygen as an electron acceptor. The natural electron acceptor is likely a heterodimeric electron transfer flavoprotein (ETF) (Probable).","Catalyzes the formation of 3,4-dihydroxy-2-alkyl-5-methylfuran-2(5H)-thione (DHMT) from 2-alkyl-5-methylfuran-2(5H)-thione (TM).",No,No,No,No,No,not-Yes,GO:0016491,GO:0016491,GO:0016491,,,,1.0,1.0,,,,2,1.0,0.1685,no
CTMB_CASD6,W8X092,Protein2Text,Bacteria,549,"Involved in the degradation of the cyclic monoterpene limonene. Catalyzes the oxidation of limonene at the primary methyl group, forming perillyl alcohol. Hydroxylates the R- and S-enantiomers to their respective enantiomeric form of perillyl alcohol at a similar rate. Native CtmAB oxidizes a wide range of monocyclic monoterpenes containing the allylic methyl group motif (1-methyl- cyclohex-1-ene). Can also catalyze the reverse reaction, the reduction of perillyl alcohol to limonene, but with lower efficiency. Cannot use molecular oxygen as an electron acceptor. The natural electron acceptor is likely a heterodimeric electron transfer flavoprotein (ETF) (Probable).","This protein is involved in the molecular function of oxidoreductase activity, specifically as a probable cytochrome P450 monooxygenase.",Vague,Maybe,Vague,Maybe,Maybe,not-Yes,GO:0016491,GO:0016491; GO:0006636,GO:0016491,,GO:0016491,GO:0016717,0.6667,1.0,,1.0,0.6897,4,0.8391,0.1685,no
CTMB_CASD6,W8X092,Reference,Bacteria,549,"Involved in the degradation of the cyclic monoterpene limonene. Catalyzes the oxidation of limonene at the primary methyl group, forming perillyl alcohol. Hydroxylates the R- and S-enantiomers to their respective enantiomeric form of perillyl alcohol at a similar rate. Native CtmAB oxidizes a wide range of monocyclic monoterpenes containing the allylic methyl group motif (1-methyl- cyclohex-1-ene). Can also catalyze the reverse reaction, the reduction of perillyl alcohol to limonene, but with lower efficiency. Cannot use molecular oxygen as an electron acceptor. The natural electron acceptor is likely a heterodimeric electron transfer flavoprotein (ETF) (Probable).","Involved in the degradation of the cyclic monoterpene limonene. Catalyzes the oxidation of limonene at the primary methyl group, forming perillyl alcohol. Hydroxylates the R- and S-enantiomers to their respective enantiomeric form of perillyl alcohol at a similar rate. Native CtmAB oxidizes a wide range of monocyclic monoterpenes containing the allylic methyl group motif (1-methyl- cyclohex-1-ene). Can also catalyze the reverse reaction, the reduction of perillyl alcohol to limonene, but with lower efficiency. Cannot use molecular oxygen as an electron acceptor. The natural electron acceptor is likely a heterodimeric electron transfer flavoprotein (ETF) (Probable).",,,,,,,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1685,no
CTMA_CASD6,W8X9R6,ESM2Text,Bacteria,565,"Involved in the degradation of the cyclic monoterpene limonene. Catalyzes the oxidation of limonene at the primary methyl group, forming perillyl alcohol. Hydroxylates the R- and S-enantiomers to their respective enantiomeric form of perillyl alcohol at a similar rate. Native CtmAB oxidizes a wide range of monocyclic monoterpenes containing the allylic methyl group motif (1-methyl- cyclohex-1-ene). Can also catalyze the reverse reaction, the reduction of perillyl alcohol to limonene, but with lower efficiency. Cannot use molecular oxygen as an electron acceptor. The natural electron acceptor is likely a heterodimeric electron transfer flavoprotein (ETF) (Probable).","Dehydrogenase; part of the gene cluster that mediates the biosynthesis of the tropolone class of fungal maleic anhydrides. The pathway begins with the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide synthase (PKS) tropA. 3-methylorcinaldehyde is the substrate for the FAD-dependent monooxygenase tropB to yield a dearomatized hydroxycyclohexadione. The 2-oxoglutarate-dependent dioxygenase tropC then performs the oxidative ring expansion to provide the first tropolone metabolite stipitaldehyde. Trop D converts stipitaldehyde into stipitacetal which is in turn converted to stipitalide by the short-chain dehydrogenase/reductase tropE. The next steps involve tropF, tropG, tropH, tropI and tropJ to form successive tropolone maleic anhydrides including stipitaldehydic, stipitatonic and stipitatic acids.",No,No,No,No,No,not-Yes,GO:0016491,GO:0016491,GO:0016491,,GO:0016491,,1.0,1.0,,1.0,,3,1.0,0.1687,no
CTMA_CASD6,W8X9R6,Prot2Text,Bacteria,565,"Involved in the degradation of the cyclic monoterpene limonene. Catalyzes the oxidation of limonene at the primary methyl group, forming perillyl alcohol. Hydroxylates the R- and S-enantiomers to their respective enantiomeric form of perillyl alcohol at a similar rate. Native CtmAB oxidizes a wide range of monocyclic monoterpenes containing the allylic methyl group motif (1-methyl- cyclohex-1-ene). Can also catalyze the reverse reaction, the reduction of perillyl alcohol to limonene, but with lower efficiency. Cannot use molecular oxygen as an electron acceptor. The natural electron acceptor is likely a heterodimeric electron transfer flavoprotein (ETF) (Probable).","Minor isoform of alcohol oxidase; part of the gene cluster that mediates the biosynthesis of asperlin, a polyketide showing anti-inflammatory, antitumor and antibiotic activities. The first step of the asperlin biosynthesis is the production of the intermediate 2,4,6-octatrienoic acid by the highly redusing polyketide synthase alnA with cleavage of the PKS product by the esterase alnB. 2,4,6-octatrienoic acid is further converted to asperlin via several steps involving the remaining enzymes from the cluster.",No,No,No,No,No,not-Yes,GO:0016491,GO:0004030,GO:0004030,,GO:0016614,GO:0016614,0.6019,0.6019,,0.8145,0.8145,4,0.7082,0.1687,no
CTMA_CASD6,W8X9R6,ProtT3,Bacteria,565,"Involved in the degradation of the cyclic monoterpene limonene. Catalyzes the oxidation of limonene at the primary methyl group, forming perillyl alcohol. Hydroxylates the R- and S-enantiomers to their respective enantiomeric form of perillyl alcohol at a similar rate. Native CtmAB oxidizes a wide range of monocyclic monoterpenes containing the allylic methyl group motif (1-methyl- cyclohex-1-ene). Can also catalyze the reverse reaction, the reduction of perillyl alcohol to limonene, but with lower efficiency. Cannot use molecular oxygen as an electron acceptor. The natural electron acceptor is likely a heterodimeric electron transfer flavoprotein (ETF) (Probable).",Membrane; Multi-pass membrane protein. Belongs to the diterpene synthase family,Vague,Vague,No,No,No,not-Yes,GO:0016491,GO:0010333,GO:0010333,,GO:0010333,GO:0010333,0.3552,0.3552,,0.3552,0.3552,4,0.3552,0.1687,no
CTMA_CASD6,W8X9R6,ProtTale,Bacteria,565,"Involved in the degradation of the cyclic monoterpene limonene. Catalyzes the oxidation of limonene at the primary methyl group, forming perillyl alcohol. Hydroxylates the R- and S-enantiomers to their respective enantiomeric form of perillyl alcohol at a similar rate. Native CtmAB oxidizes a wide range of monocyclic monoterpenes containing the allylic methyl group motif (1-methyl- cyclohex-1-ene). Can also catalyze the reverse reaction, the reduction of perillyl alcohol to limonene, but with lower efficiency. Cannot use molecular oxygen as an electron acceptor. The natural electron acceptor is likely a heterodimeric electron transfer flavoprotein (ETF) (Probable).","Involved in the biosynthesis of the yellow-orange carotenoid staphyloxanthin, which plays a role in the virulence via its protective function against oxidative stress. Catalyzes the oxidation of the double bond between C-7 and C-8 of polyketide carotenoids such as zeaxanthin and antheraxanthin to the corresponding 3,8-didehydro derivatives (3,8-didehydroanthraxanthin and 3,8-didehydrozeaxanthin respectively).",No,No,No,No,No,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1687,no
CTMA_CASD6,W8X9R6,Protein2Text,Bacteria,565,"Involved in the degradation of the cyclic monoterpene limonene. Catalyzes the oxidation of limonene at the primary methyl group, forming perillyl alcohol. Hydroxylates the R- and S-enantiomers to their respective enantiomeric form of perillyl alcohol at a similar rate. Native CtmAB oxidizes a wide range of monocyclic monoterpenes containing the allylic methyl group motif (1-methyl- cyclohex-1-ene). Can also catalyze the reverse reaction, the reduction of perillyl alcohol to limonene, but with lower efficiency. Cannot use molecular oxygen as an electron acceptor. The natural electron acceptor is likely a heterodimeric electron transfer flavoprotein (ETF) (Probable).","This protein is involved in the molecular function of oxidoreductase activity, specifically as a desaturase. It is involved in the biosynthesis of fatty acids, which are important for cellular membrane structure and function.",No,No,No,No,Maybe,not-Yes,GO:0016491,GO:0016491; GO:0006636,GO:0016491,,GO:0016491,GO:0016717,0.6667,1.0,,1.0,0.6897,4,0.8391,0.1687,no
CTMA_CASD6,W8X9R6,Reference,Bacteria,565,"Involved in the degradation of the cyclic monoterpene limonene. Catalyzes the oxidation of limonene at the primary methyl group, forming perillyl alcohol. Hydroxylates the R- and S-enantiomers to their respective enantiomeric form of perillyl alcohol at a similar rate. Native CtmAB oxidizes a wide range of monocyclic monoterpenes containing the allylic methyl group motif (1-methyl- cyclohex-1-ene). Can also catalyze the reverse reaction, the reduction of perillyl alcohol to limonene, but with lower efficiency. Cannot use molecular oxygen as an electron acceptor. The natural electron acceptor is likely a heterodimeric electron transfer flavoprotein (ETF) (Probable).","Involved in the degradation of the cyclic monoterpene limonene. Catalyzes the oxidation of limonene at the primary methyl group, forming perillyl alcohol. Hydroxylates the R- and S-enantiomers to their respective enantiomeric form of perillyl alcohol at a similar rate. Native CtmAB oxidizes a wide range of monocyclic monoterpenes containing the allylic methyl group motif (1-methyl- cyclohex-1-ene). Can also catalyze the reverse reaction, the reduction of perillyl alcohol to limonene, but with lower efficiency. Cannot use molecular oxygen as an electron acceptor. The natural electron acceptor is likely a heterodimeric electron transfer flavoprotein (ETF) (Probable).",,,,,,,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1687,no
FOGA_ASPRC,A0A017SEX7,ESM2Text,Eukaryota,2403,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain. FogA releases the carboxylic acid (8E,10E,12E)-3,5,7-trihydroxytetradeca-8,10,12-trienoic acid as its product, as well as derivatives with one and two double bonds. FogA is indeed able to reduce the initial triketide, thus being at least partially responsible for the differently saturated heptyl side chains of flavoglaucin congeners. The oxidoreductases fogB, fogC and fogD modify the nascent polyketide in fogA-bound form and, together, fogA, fogB, fogC and fogD are necessary for the formation of the aromatic core and the cyclized PKS products are released as salicyl alcohols. In particular, fogB is responsible for oxidation of a hydroxyl group or reduction of remaining double bond(s) at the C-7 residue whereas fogD is probably involved in the reductive release of the modified PKS products. The cytochrome P450 monooxygenase fogE is then responsible for the hydroxylation at C-3 of the benzene ring. The fogE products are substrates of the prenyltransferase fogH and the prenylated benzyl alcohols are subsequently oxidized by the fogF to produce the final aryl aldehydes flavoglaucin and congeners. The short-chain dehydrogenase fogG does not seem to be involved in the biosynthesis of the prenylated salicylaldehyde derivatives.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcsC",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491,,,,,,,,,,,0,,0.2747,no
FOGA_ASPRC,A0A017SEX7,Prot2Text,Eukaryota,2403,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain. FogA releases the carboxylic acid (8E,10E,12E)-3,5,7-trihydroxytetradeca-8,10,12-trienoic acid as its product, as well as derivatives with one and two double bonds. FogA is indeed able to reduce the initial triketide, thus being at least partially responsible for the differently saturated heptyl side chains of flavoglaucin congeners. The oxidoreductases fogB, fogC and fogD modify the nascent polyketide in fogA-bound form and, together, fogA, fogB, fogC and fogD are necessary for the formation of the aromatic core and the cyclized PKS products are released as salicyl alcohols. In particular, fogB is responsible for oxidation of a hydroxyl group or reduction of remaining double bond(s) at the C-7 residue whereas fogD is probably involved in the reductive release of the modified PKS products. The cytochrome P450 monooxygenase fogE is then responsible for the hydroxylation at C-3 of the benzene ring. The fogE products are substrates of the prenyltransferase fogH and the prenylated benzyl alcohols are subsequently oxidized by the fogF to produce the final aryl aldehydes flavoglaucin and congeners. The short-chain dehydrogenase fogG does not seem to be involved in the biosynthesis of the prenylated salicylaldehyde derivatives.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491,GO:0016747,,,GO:0016747,GO:0016746,0.7454,,,0.7454,0.6669,3,0.7192,0.2747,no
FOGA_ASPRC,A0A017SEX7,ProtT3,Eukaryota,2403,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain. FogA releases the carboxylic acid (8E,10E,12E)-3,5,7-trihydroxytetradeca-8,10,12-trienoic acid as its product, as well as derivatives with one and two double bonds. FogA is indeed able to reduce the initial triketide, thus being at least partially responsible for the differently saturated heptyl side chains of flavoglaucin congeners. The oxidoreductases fogB, fogC and fogD modify the nascent polyketide in fogA-bound form and, together, fogA, fogB, fogC and fogD are necessary for the formation of the aromatic core and the cyclized PKS products are released as salicyl alcohols. In particular, fogB is responsible for oxidation of a hydroxyl group or reduction of remaining double bond(s) at the C-7 residue whereas fogD is probably involved in the reductive release of the modified PKS products. The cytochrome P450 monooxygenase fogE is then responsible for the hydroxylation at C-3 of the benzene ring. The fogE products are substrates of the prenyltransferase fogH and the prenylated benzyl alcohols are subsequently oxidized by the fogF to produce the final aryl aldehydes flavoglaucin and congeners. The short-chain dehydrogenase fogG does not seem to be involved in the biosynthesis of the prenylated salicylaldehyde derivatives.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491,GO:0016746,GO:0016746,,GO:0016746,GO:0016747,0.6669,0.6669,,0.6669,0.7454,4,0.6865,0.2747,no
FOGA_ASPRC,A0A017SEX7,ProtTale,Eukaryota,2403,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain. FogA releases the carboxylic acid (8E,10E,12E)-3,5,7-trihydroxytetradeca-8,10,12-trienoic acid as its product, as well as derivatives with one and two double bonds. FogA is indeed able to reduce the initial triketide, thus being at least partially responsible for the differently saturated heptyl side chains of flavoglaucin congeners. The oxidoreductases fogB, fogC and fogD modify the nascent polyketide in fogA-bound form and, together, fogA, fogB, fogC and fogD are necessary for the formation of the aromatic core and the cyclized PKS products are released as salicyl alcohols. In particular, fogB is responsible for oxidation of a hydroxyl group or reduction of remaining double bond(s) at the C-7 residue whereas fogD is probably involved in the reductive release of the modified PKS products. The cytochrome P450 monooxygenase fogE is then responsible for the hydroxylation at C-3 of the benzene ring. The fogE products are substrates of the prenyltransferase fogH and the prenylated benzyl alcohols are subsequently oxidized by the fogF to produce the final aryl aldehydes flavoglaucin and congeners. The short-chain dehydrogenase fogG does not seem to be involved in the biosynthesis of the prenylated salicylaldehyde derivatives.","Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants. Within the pathway, porB is probably involved in the cyclization of the linear polyketide formed by the PKS porA. The first step of the pathway is performed by the NR-PKS porA that condenses acetyl-CoA with 4 malonyl-CoA units, a single methyl group from S-adenosyl-L",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491,GO:0016491,GO:0016757,,,GO:0016746,0.6776,0.4817,,,0.6669,3,0.6087,0.2747,no
FOGA_ASPRC,A0A017SEX7,Protein2Text,Eukaryota,2403,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain. FogA releases the carboxylic acid (8E,10E,12E)-3,5,7-trihydroxytetradeca-8,10,12-trienoic acid as its product, as well as derivatives with one and two double bonds. FogA is indeed able to reduce the initial triketide, thus being at least partially responsible for the differently saturated heptyl side chains of flavoglaucin congeners. The oxidoreductases fogB, fogC and fogD modify the nascent polyketide in fogA-bound form and, together, fogA, fogB, fogC and fogD are necessary for the formation of the aromatic core and the cyclized PKS products are released as salicyl alcohols. In particular, fogB is responsible for oxidation of a hydroxyl group or reduction of remaining double bond(s) at the C-7 residue whereas fogD is probably involved in the reductive release of the modified PKS products. The cytochrome P450 monooxygenase fogE is then responsible for the hydroxylation at C-3 of the benzene ring. The fogE products are substrates of the prenyltransferase fogH and the prenylated benzyl alcohols are subsequently oxidized by the fogF to produce the final aryl aldehydes flavoglaucin and congeners. The short-chain dehydrogenase fogG does not seem to be involved in the biosynthesis of the prenylated salicylaldehyde derivatives.","The molecular function of this protein is likely involved in the synthesis of fatty acids, specifically as a fatty acid synthase. Fatty acid synthases are enzymes that catalyze the formation of long-chain fatty acids from acetyl-CoA and malonyl-CoA through a series of reduction, dehydration, and reduction reactions. They are essential for the production of fatty acids, which are important components of cellular membranes, energy storage molecules, and signaling molecules. In the case of this protein, it is likely involved in the synthesis of fatty acids in a specific organism, possibly in the production of a particular type of fatty acid or lipid.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.771,0.771,0.771,0.771,0.771,5,0.771,0.2747,no
FOGA_ASPRC,A0A017SEX7,Reference,Eukaryota,2403,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain. FogA releases the carboxylic acid (8E,10E,12E)-3,5,7-trihydroxytetradeca-8,10,12-trienoic acid as its product, as well as derivatives with one and two double bonds. FogA is indeed able to reduce the initial triketide, thus being at least partially responsible for the differently saturated heptyl side chains of flavoglaucin congeners. The oxidoreductases fogB, fogC and fogD modify the nascent polyketide in fogA-bound form and, together, fogA, fogB, fogC and fogD are necessary for the formation of the aromatic core and the cyclized PKS products are released as salicyl alcohols. In particular, fogB is responsible for oxidation of a hydroxyl group or reduction of remaining double bond(s) at the C-7 residue whereas fogD is probably involved in the reductive release of the modified PKS products. The cytochrome P450 monooxygenase fogE is then responsible for the hydroxylation at C-3 of the benzene ring. The fogE products are substrates of the prenyltransferase fogH and the prenylated benzyl alcohols are subsequently oxidized by the fogF to produce the final aryl aldehydes flavoglaucin and congeners. The short-chain dehydrogenase fogG does not seem to be involved in the biosynthesis of the prenylated salicylaldehyde derivatives.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain. FogA releases the carboxylic acid (8E,10E,12E)-3,5,7-trihydroxytetradeca-8,10,12-trienoic acid as its product, as well as derivatives with one and two double bonds. FogA is indeed able to reduce the initial triketide, thus being at least partially responsible for the differently saturated heptyl side chains of flavoglaucin congeners. The oxidoreductases fogB, fogC and fogD modify the nascent polyketide in fogA-bound form and, together, fogA, fogB, fogC and fogD are necessary for the formation of the aromatic core and the cyclized PKS products are released as salicyl alcohols. In particular, fogB is responsible for oxidation of a hydroxyl group or reduction of remaining double bond(s) at the C-7 residue whereas fogD is probably involved in the reductive release of the modified PKS products. The cytochrome P450 monooxygenase fogE is then responsible for the hydroxylation at C-3 of the benzene ring. The fogE products are substrates of the prenyltransferase fogH and the prenylated benzyl alcohols are subsequently oxidized by the fogF to produce the final aryl aldehydes flavoglaucin and congeners. The short-chain dehydrogenase fogG does not seem to be involved in the biosynthesis of the prenylated salicylaldehyde derivatives.",,,,,,,GO:0004315; GO:0004312; GO:0016491,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.6669,0.6669,0.6669,0.7454,0.6669,5,0.6826,0.2747,no
PEX6_CRIGR,A0A061IR73,ESM2Text,Eukaryota,980,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.","Involved in peroxisome biosynthesis. Required for stability of the PTS1 receptor. Anchored by PEX26 to peroxisome membranes, possibly to form heteromeric AAA ATPase complexes required for the import of proteins into peroxisomes.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0016887; GO:0140318; GO:0044877; GO:0140036,GO:0016887; GO:0005524,GO:0016887,GO:0016887,,GO:0016887,0.636,0.4111,0.4111,,0.4111,4,0.4673,0.5518,yes
PEX6_CRIGR,A0A061IR73,Prot2Text,Eukaryota,980,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.","Involved in peroxisome biosynthesis. Required for stability of the PTS1 receptor. Anchored by PEX26 to peroxisome membranes, possibly to form heteromeric AAA ATPase complexes required for the import of proteins into peroxisomes.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0016887; GO:0140318; GO:0044877; GO:0140036,GO:0016887,GO:0016887,GO:0016887,GO:0016887,GO:0016887; GO:0005524,0.4111,0.4111,0.4111,0.4111,0.636,5,0.4561,0.5518,yes
PEX6_CRIGR,A0A061IR73,ProtT3,Eukaryota,980,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.","Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor (By similarity). The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 10 nm (By similarity). Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with",No,Maybe,No,No,No,not-Yes,GO:0005524; GO:0016887; GO:0140318; GO:0044877; GO:0140036,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.636,0.636,0.636,0.636,0.636,5,0.636,0.5518,yes
PEX6_CRIGR,A0A061IR73,ProtTale,Eukaryota,980,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.","Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0140318; GO:0044877; GO:0140036,GO:0005524,GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.4013,0.636,0.636,0.636,0.636,5,0.5891,0.5518,yes
PEX6_CRIGR,A0A061IR73,Protein2Text,Eukaryota,980,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.","This protein is a nucleoside diphosphate kinase, which means it is involved in the transfer of phosphate groups in the synthesis of nucleotides.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016887; GO:0140318; GO:0044877; GO:0140036,GO:0004386,GO:0004386,GO:0004386,GO:0004386,GO:0004386,0.187,0.187,0.187,0.187,0.187,5,0.187,0.5518,yes
PEX6_CRIGR,A0A061IR73,Reference,Eukaryota,980,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.","Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.",,,,,,,GO:0005524; GO:0016887; GO:0140318; GO:0044877; GO:0140036,GO:0016887; GO:0005524,GO:0016887,GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.636,0.4111,0.4111,0.636,0.636,5,0.546,0.5518,yes
TAS1_BOTB1,A0A067MTM1,ESM2Text,Eukaryota,1711,"Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal NRPS module and subsequent cyclization conducted by the C-terminal KS domain.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcs",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0047527; GO:0004315; GO:0031177,,,,,,,,,,,0,,0.206,no
TAS1_BOTB1,A0A067MTM1,Prot2Text,Eukaryota,1711,"Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal NRPS module and subsequent cyclization conducted by the C-terminal KS domain.","Acyl-CoA synthetase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcsC",No,No,No,No,No,not-Yes,GO:0047527; GO:0004315; GO:0031177,,,,,,,,,,,0,,0.206,no
TAS1_BOTB1,A0A067MTM1,ProtT3,Eukaryota,1711,"Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal NRPS module and subsequent cyclization conducted by the C-terminal KS domain.","Nonribosomal peptide synthetase (NRPS); part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0047527; GO:0004315; GO:0031177,GO:0016874; GO:0005524,GO:0016874,,GO:0016874; GO:0031177,GO:0016874; GO:0005524,0.4553,0.4215,,0.7118,0.4553,4,0.511,0.206,no
TAS1_BOTB1,A0A067MTM1,ProtTale,Eukaryota,1711,"Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal NRPS module and subsequent cyclization conducted by the C-terminal KS domain.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0047527; GO:0004315; GO:0031177,GO:0016491,GO:0016757,,,GO:0016746,0.2982,0.3388,,,0.4623,3,0.3664,0.206,no
TAS1_BOTB1,A0A067MTM1,Protein2Text,Eukaryota,1711,"Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal NRPS module and subsequent cyclization conducted by the C-terminal KS domain.","The molecular function of this protein is not explicitly stated in the provided text, but based on its classification as a protein and its involvement in a biological process, it is likely to be involved in catalyzing a chemical reaction, such as a decarboxylation or a condensation reaction. However, more specific information would be required to determine the exact molecular function of this protein.",Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0047527; GO:0004315; GO:0031177,GO:0004337,GO:0004161,GO:0004337,GO:0004337,GO:0004337,0.2089,0.2089,0.2089,0.2089,0.2089,5,0.2089,0.206,no
TAS1_BOTB1,A0A067MTM1,Reference,Eukaryota,1711,"Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal NRPS module and subsequent cyclization conducted by the C-terminal KS domain.","Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal NRPS module and subsequent cyclization conducted by the C-terminal KS domain.",,,,,,,GO:0047527; GO:0004315; GO:0031177,GO:0016746; GO:0016874,GO:0016874,GO:0016746; GO:0016874,GO:0016874,GO:0016874,0.5577,0.4215,0.5577,0.4215,0.4215,5,0.476,0.206,no
BGBGP_PAEBO,A0A089MMR2,ESM2Text,Bacteria,769,"Glycoside phosphorylase that catalyzes the reversible phosphorolysis of 3-O-beta-D-glucosyl-D-glucuronate into D-glucuronic acid and alpha-D-glucose 1-phosphate. Cannot phosphorolyze cellobionic acid and laminaribiose. In the reverse direction, using alpha-D-glucose 1-phosphate as a donor substrate, the enzyme acts on D-glucuronate and its artificial derivative p-nitrophenyl-beta-D-glucuronide. The apparent catalytic efficiency towards p-nitrophenyl-beta-D-glucuronide is approximately 5-fold higher than that towards D-glucuronic acid. Is probably involved in the metabolism of oligosaccharides containing the 3-O-beta-D-glucopyranosyl-beta-D- glucuronide structure released from bacterial and plant acidic carbohydrates.","Catalyzes the hydrolysis of glucosidic bonds in cellulose, glucose and mannose to produce glucose 1-phosphate and mannobiose. Also hydrolyzes cellobiose, but it cannot act on other cellotriose- or cellotetraose-type oligosaccharides.",No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0030246; GO:0016757,,GO:0004553,GO:0004553,,,,0.2793,0.2793,,,2,0.2793,0.2821,no
BGBGP_PAEBO,A0A089MMR2,Prot2Text,Bacteria,769,"Glycoside phosphorylase that catalyzes the reversible phosphorolysis of 3-O-beta-D-glucosyl-D-glucuronate into D-glucuronic acid and alpha-D-glucose 1-phosphate. Cannot phosphorolyze cellobionic acid and laminaribiose. In the reverse direction, using alpha-D-glucose 1-phosphate as a donor substrate, the enzyme acts on D-glucuronate and its artificial derivative p-nitrophenyl-beta-D-glucuronide. The apparent catalytic efficiency towards p-nitrophenyl-beta-D-glucuronide is approximately 5-fold higher than that towards D-glucuronic acid. Is probably involved in the metabolism of oligosaccharides containing the 3-O-beta-D-glucopyranosyl-beta-D- glucuronide structure released from bacterial and plant acidic carbohydrates.","Hydrolyzes the glucosidic bonds of cellobiose, cellotriose and laminaribiose to glucose and cellobiose and cellotriose, respectively.",No,Maybe,Maybe,No,No,not-Yes,GO:0030246; GO:0016757,GO:0004565,GO:0008422,GO:0008422,GO:0008422,GO:0008422; GO:0004553,0.2153,0.2153,0.2153,0.2153,0.2725,5,0.2267,0.2821,no
BGBGP_PAEBO,A0A089MMR2,ProtT3,Bacteria,769,"Glycoside phosphorylase that catalyzes the reversible phosphorolysis of 3-O-beta-D-glucosyl-D-glucuronate into D-glucuronic acid and alpha-D-glucose 1-phosphate. Cannot phosphorolyze cellobionic acid and laminaribiose. In the reverse direction, using alpha-D-glucose 1-phosphate as a donor substrate, the enzyme acts on D-glucuronate and its artificial derivative p-nitrophenyl-beta-D-glucuronide. The apparent catalytic efficiency towards p-nitrophenyl-beta-D-glucuronide is approximately 5-fold higher than that towards D-glucuronic acid. Is probably involved in the metabolism of oligosaccharides containing the 3-O-beta-D-glucopyranosyl-beta-D- glucuronide structure released from bacterial and plant acidic carbohydrates.","Catalyzes the hydrolysis of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) to 1,6-anhydro-N-acetyl-D- glucosamine (anhGlcN) and acetate. Belongs to the glycosyl hydrolase 43 family",No,No,No,No,No,not-Yes,GO:0030246; GO:0016757,GO:0016798,GO:0016798,GO:0016798,GO:0004553,GO:0016798,0.3314,0.3314,0.3314,0.2793,0.3314,5,0.321,0.2821,no
BGBGP_PAEBO,A0A089MMR2,ProtTale,Bacteria,769,"Glycoside phosphorylase that catalyzes the reversible phosphorolysis of 3-O-beta-D-glucosyl-D-glucuronate into D-glucuronic acid and alpha-D-glucose 1-phosphate. Cannot phosphorolyze cellobionic acid and laminaribiose. In the reverse direction, using alpha-D-glucose 1-phosphate as a donor substrate, the enzyme acts on D-glucuronate and its artificial derivative p-nitrophenyl-beta-D-glucuronide. The apparent catalytic efficiency towards p-nitrophenyl-beta-D-glucuronide is approximately 5-fold higher than that towards D-glucuronic acid. Is probably involved in the metabolism of oligosaccharides containing the 3-O-beta-D-glucopyranosyl-beta-D- glucuronide structure released from bacterial and plant acidic carbohydrates.","Catalyzes the reversible phosphorolysis of chitobiose (N,N'- diacetylchitobiose or (GlcNAc)(2)) into N-acetyl-alpha-D-glucosamine 1- phosphate (GlcNAc-1-P) and N-acetyl-D-glucosamine (GlcNAc) with inversion of the anomeric configuration. Also catalyzes the reversible phosphorolysis of N,N',N''- triacetylchitotriose ((GlcNAc)(3)) into GlcNAc-1- phosphate (GlcNAc-1-P), GlcNAc-1- phosphate and Glc",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0030246; GO:0016757,GO:0004645,GO:0016757,,GO:0016757,GO:0016757,0.5386,0.7379,,0.7379,0.7379,4,0.6881,0.2821,no
BGBGP_PAEBO,A0A089MMR2,Protein2Text,Bacteria,769,"Glycoside phosphorylase that catalyzes the reversible phosphorolysis of 3-O-beta-D-glucosyl-D-glucuronate into D-glucuronic acid and alpha-D-glucose 1-phosphate. Cannot phosphorolyze cellobionic acid and laminaribiose. In the reverse direction, using alpha-D-glucose 1-phosphate as a donor substrate, the enzyme acts on D-glucuronate and its artificial derivative p-nitrophenyl-beta-D-glucuronide. The apparent catalytic efficiency towards p-nitrophenyl-beta-D-glucuronide is approximately 5-fold higher than that towards D-glucuronic acid. Is probably involved in the metabolism of oligosaccharides containing the 3-O-beta-D-glucopyranosyl-beta-D- glucuronide structure released from bacterial and plant acidic carbohydrates.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its name and the context, it can be inferred that this protein is a hydrolase, which is an enzyme that catalyzes the hydrolysis of a chemical bond. More specifically, this protein is likely a glycosidase, which is a type of hydrolase that catalyzes the hydrolysis of glycosidic bonds.",Vague,Vague,Maybe,Vague,Maybe,not-Yes,GO:0030246; GO:0016757,GO:0004553,GO:0016798,GO:0016798,GO:0016798,GO:0004553,0.2793,0.3314,0.3314,0.3314,0.2793,5,0.3106,0.2821,no
BGBGP_PAEBO,A0A089MMR2,Reference,Bacteria,769,"Glycoside phosphorylase that catalyzes the reversible phosphorolysis of 3-O-beta-D-glucosyl-D-glucuronate into D-glucuronic acid and alpha-D-glucose 1-phosphate. Cannot phosphorolyze cellobionic acid and laminaribiose. In the reverse direction, using alpha-D-glucose 1-phosphate as a donor substrate, the enzyme acts on D-glucuronate and its artificial derivative p-nitrophenyl-beta-D-glucuronide. The apparent catalytic efficiency towards p-nitrophenyl-beta-D-glucuronide is approximately 5-fold higher than that towards D-glucuronic acid. Is probably involved in the metabolism of oligosaccharides containing the 3-O-beta-D-glucopyranosyl-beta-D- glucuronide structure released from bacterial and plant acidic carbohydrates.","Glycoside phosphorylase that catalyzes the reversible phosphorolysis of 3-O-beta-D-glucosyl-D-glucuronate into D-glucuronic acid and alpha-D-glucose 1-phosphate. Cannot phosphorolyze cellobionic acid and laminaribiose. In the reverse direction, using alpha-D-glucose 1-phosphate as a donor substrate, the enzyme acts on D-glucuronate and its artificial derivative p-nitrophenyl-beta-D-glucuronide. The apparent catalytic efficiency towards p-nitrophenyl-beta-D-glucuronide is approximately 5-fold higher than that towards D-glucuronic acid. Is probably involved in the metabolism of oligosaccharides containing the 3-O-beta-D-glucopyranosyl-beta-D- glucuronide structure released from bacterial and plant acidic carbohydrates.",,,,,,,GO:0030246; GO:0016757,GO:0004645,GO:0016757,GO:0004645,GO:0016740,GO:0004645,0.5386,0.7379,0.5386,0.6305,0.5386,5,0.5968,0.2821,no
SRDA_MESS1,A0A0A8X0K1,ESM2Text,Bacteria,1048,"Component of the respiratory selenate reductase complex, which catalyzes the reduction of selenate to selenite. SrdA is probably the catalytic subunit that reduces selenate (Probable).",Reduces nitrate to nitrite.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0051539; GO:0046872; GO:0043546; GO:0016491,GO:0008940,GO:0008940,GO:0008940,GO:0008940,GO:0008940,0.3539,0.3539,0.3539,0.3539,0.3539,5,0.3539,0.4124,no
SRDA_MESS1,A0A0A8X0K1,Prot2Text,Bacteria,1048,"Component of the respiratory selenate reductase complex, which catalyzes the reduction of selenate to selenite. SrdA is probably the catalytic subunit that reduces selenate (Probable).",Component of the perchlorate reductase that catalyzes the reduction of perchlorate to chlorite and allows anaerobic growth on perchlorate as the sole electron acceptor. The alpha subunit may be responsible for electron transfer to the beta subunit PcrA (Probable).,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0051539; GO:0046872; GO:0043546; GO:0016491,GO:0016491,GO:0009055,GO:0009055,GO:0016491,GO:0016491,0.5156,0.2859,0.2859,0.5156,0.5156,5,0.4237,0.4124,no
SRDA_MESS1,A0A0A8X0K1,ProtT3,Bacteria,1048,"Component of the respiratory selenate reductase complex, which catalyzes the reduction of selenate to selenite. SrdA is probably the catalytic subunit that reduces selenate (Probable).",Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Periplasm. Belongs to the prokaryotic molybdopterin-containing oxidoreductase family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0051539; GO:0046872; GO:0043546; GO:0016491,GO:0016159,GO:0016002,GO:0016002,GO:0016491,GO:0050311,0.2092,0.3539,0.3539,0.5156,0.3079,5,0.3481,0.4124,no
SRDA_MESS1,A0A0A8X0K1,ProtTale,Bacteria,1048,"Component of the respiratory selenate reductase complex, which catalyzes the reduction of selenate to selenite. SrdA is probably the catalytic subunit that reduces selenate (Probable).",Part of a complex that catalyzes the reversible reduction of CO(2) to formate and H(2).,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0051539; GO:0046872; GO:0043546; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.5156,0.5156,0.5156,0.5156,0.5156,5,0.5156,0.4124,no
SRDA_MESS1,A0A0A8X0K1,Protein2Text,Bacteria,1048,"Component of the respiratory selenate reductase complex, which catalyzes the reduction of selenate to selenite. SrdA is probably the catalytic subunit that reduces selenate (Probable).","This protein is a hydrogenase, which means it catalyzes the reversible oxidation of hydrogen gas. Specifically, it is a nickel-iron hydrogenase, which is a type of hydrogenase that uses a nickel-iron complex to facilitate the oxidation and reduction of hydrogen gas.",No,No,No,No,No,not-Yes,GO:0051539; GO:0046872; GO:0043546; GO:0016491,GO:0008901,GO:0016491,,GO:0033748,GO:0016491,0.3079,0.5156,,0.3539,0.5156,4,0.4232,0.4124,no
SRDA_MESS1,A0A0A8X0K1,Reference,Bacteria,1048,"Component of the respiratory selenate reductase complex, which catalyzes the reduction of selenate to selenite. SrdA is probably the catalytic subunit that reduces selenate (Probable).","Component of the respiratory selenate reductase complex, which catalyzes the reduction of selenate to selenite. SrdA is probably the catalytic subunit that reduces selenate (Probable).",,,,,,,GO:0051539; GO:0046872; GO:0043546; GO:0016491,GO:0016491,GO:0033797,GO:0016491,GO:0016491,GO:0016491,0.5156,0.4191,0.5156,0.5156,0.5156,5,0.4963,0.4124,no
PBOD_ASPUT,A0A0C1C427,ESM2Text,Eukaryota,486,"Flavin-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. Within the pathway, pboD catalyzes the hydroxylation at C-3 of the indole ring of cyclo-L-Trp-L-Leu and subsequent formation of the pyrrolidine ring, eading to the production of protubonine D. PboD is also able to accept other cyclodipeptides (CDPs) as substrates, including cyclo-L-Trp-L-Trp, cyclo-L-Trp-L-Tyr, cyclo-L-Trp-L-Phe, cyclo-L-Trp-L-Met, cyclo-L-Trp-L-Ala, cyclo-L-Trp-L-Pro and cyclo-L- Trp-Gly. Assays with cyclo-L-Trp-L-Trp, cyclo-L-Trp- L-Tyr, cyclo-L-Trp-L-Phe show similar or even slightly higher conversion yields, compared with that of the natural substrate cyclo-L- Trp-L-Leu, whereas cyclo-L-Trp-L-Pro and cyclo-L-Trp-Gly are accepted by PboD but only with conversion yields of 10 and 4%, respectively. Cyclo-L-Trp-L-His is not accepted as a substrate. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L-Leu by condensing L-Leu with L-Trp. The flavin-dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.","FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome P450 monooxygenase P450-1 then catalyzes the dimerization of nataloe-emodin to cladofulvin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0071949; GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.6988,0.6988,0.6988,0.6988,0.6988,5,0.6988,0.189,no
PBOD_ASPUT,A0A0C1C427,Prot2Text,Eukaryota,486,"Flavin-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. Within the pathway, pboD catalyzes the hydroxylation at C-3 of the indole ring of cyclo-L-Trp-L-Leu and subsequent formation of the pyrrolidine ring, eading to the production of protubonine D. PboD is also able to accept other cyclodipeptides (CDPs) as substrates, including cyclo-L-Trp-L-Trp, cyclo-L-Trp-L-Tyr, cyclo-L-Trp-L-Phe, cyclo-L-Trp-L-Met, cyclo-L-Trp-L-Ala, cyclo-L-Trp-L-Pro and cyclo-L- Trp-Gly. Assays with cyclo-L-Trp-L-Trp, cyclo-L-Trp- L-Tyr, cyclo-L-Trp-L-Phe show similar or even slightly higher conversion yields, compared with that of the natural substrate cyclo-L- Trp-L-Leu, whereas cyclo-L-Trp-L-Pro and cyclo-L-Trp-Gly are accepted by PboD but only with conversion yields of 10 and 4%, respectively. Cyclo-L-Trp-L-His is not accepted as a substrate. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L-Leu by condensing L-Leu with L-Trp. The flavin-dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.","FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the diterpenoid pyrones higginsianins A and B. The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpchA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpchD through the action of the prenyltransferase dpchC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpchE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpchB (Probable). The short chain dehydrogenase/reductase dpchG then oxidizes",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0071949; GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.6988,0.6988,0.6988,0.6988,0.6988,5,0.6988,0.189,no
PBOD_ASPUT,A0A0C1C427,ProtT3,Eukaryota,486,"Flavin-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. Within the pathway, pboD catalyzes the hydroxylation at C-3 of the indole ring of cyclo-L-Trp-L-Leu and subsequent formation of the pyrrolidine ring, eading to the production of protubonine D. PboD is also able to accept other cyclodipeptides (CDPs) as substrates, including cyclo-L-Trp-L-Trp, cyclo-L-Trp-L-Tyr, cyclo-L-Trp-L-Phe, cyclo-L-Trp-L-Met, cyclo-L-Trp-L-Ala, cyclo-L-Trp-L-Pro and cyclo-L- Trp-Gly. Assays with cyclo-L-Trp-L-Trp, cyclo-L-Trp- L-Tyr, cyclo-L-Trp-L-Phe show similar or even slightly higher conversion yields, compared with that of the natural substrate cyclo-L- Trp-L-Leu, whereas cyclo-L-Trp-L-Pro and cyclo-L-Trp-Gly are accepted by PboD but only with conversion yields of 10 and 4%, respectively. Cyclo-L-Trp-L-His is not accepted as a substrate. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L-Leu by condensing L-Leu with L-Trp. The flavin-dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.",FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeranylindole (3-,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0071949; GO:0004497,GO:0004497; GO:0071949,GO:0004497; GO:0071949,GO:0004497; GO:0050660,GO:0004497; GO:0071949,GO:0004497,1.0,1.0,0.9573,1.0,0.6988,5,0.9312,0.189,no
PBOD_ASPUT,A0A0C1C427,ProtTale,Eukaryota,486,"Flavin-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. Within the pathway, pboD catalyzes the hydroxylation at C-3 of the indole ring of cyclo-L-Trp-L-Leu and subsequent formation of the pyrrolidine ring, eading to the production of protubonine D. PboD is also able to accept other cyclodipeptides (CDPs) as substrates, including cyclo-L-Trp-L-Trp, cyclo-L-Trp-L-Tyr, cyclo-L-Trp-L-Phe, cyclo-L-Trp-L-Met, cyclo-L-Trp-L-Ala, cyclo-L-Trp-L-Pro and cyclo-L- Trp-Gly. Assays with cyclo-L-Trp-L-Trp, cyclo-L-Trp- L-Tyr, cyclo-L-Trp-L-Phe show similar or even slightly higher conversion yields, compared with that of the natural substrate cyclo-L- Trp-L-Leu, whereas cyclo-L-Trp-L-Pro and cyclo-L-Trp-Gly are accepted by PboD but only with conversion yields of 10 and 4%, respectively. Cyclo-L-Trp-L-His is not accepted as a substrate. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L-Leu by condensing L-Leu with L-Trp. The flavin-dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.","FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product,",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0071949; GO:0004497,GO:0016491; GO:0071949,GO:0016491,GO:0004497,GO:0004497,GO:0004497,0.9073,0.5823,0.6988,0.6988,0.6988,5,0.7172,0.189,no
PBOD_ASPUT,A0A0C1C427,Protein2Text,Eukaryota,486,"Flavin-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. Within the pathway, pboD catalyzes the hydroxylation at C-3 of the indole ring of cyclo-L-Trp-L-Leu and subsequent formation of the pyrrolidine ring, eading to the production of protubonine D. PboD is also able to accept other cyclodipeptides (CDPs) as substrates, including cyclo-L-Trp-L-Trp, cyclo-L-Trp-L-Tyr, cyclo-L-Trp-L-Phe, cyclo-L-Trp-L-Met, cyclo-L-Trp-L-Ala, cyclo-L-Trp-L-Pro and cyclo-L- Trp-Gly. Assays with cyclo-L-Trp-L-Trp, cyclo-L-Trp- L-Tyr, cyclo-L-Trp-L-Phe show similar or even slightly higher conversion yields, compared with that of the natural substrate cyclo-L- Trp-L-Leu, whereas cyclo-L-Trp-L-Pro and cyclo-L-Trp-Gly are accepted by PboD but only with conversion yields of 10 and 4%, respectively. Cyclo-L-Trp-L-His is not accepted as a substrate. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L-Leu by condensing L-Leu with L-Trp. The flavin-dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.","The molecular function of this protein is a cytochrome P450 monooxygenase. More specifically, it is a short-chain dehydrogenase/reductase, which suggests that it is involved in the reduction of a substrate in a reaction catalyzed by the cytochrome P450 enzyme. This type of enzyme typically plays a role in the metabolism of xenobiotics, hormones, and other molecules.",No,Maybe,No,No,Maybe,not-Yes,GO:0071949; GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,,0.6988,0.6988,0.6988,0.6988,,4,0.6988,0.189,no
PBOD_ASPUT,A0A0C1C427,Reference,Eukaryota,486,"Flavin-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. Within the pathway, pboD catalyzes the hydroxylation at C-3 of the indole ring of cyclo-L-Trp-L-Leu and subsequent formation of the pyrrolidine ring, eading to the production of protubonine D. PboD is also able to accept other cyclodipeptides (CDPs) as substrates, including cyclo-L-Trp-L-Trp, cyclo-L-Trp-L-Tyr, cyclo-L-Trp-L-Phe, cyclo-L-Trp-L-Met, cyclo-L-Trp-L-Ala, cyclo-L-Trp-L-Pro and cyclo-L- Trp-Gly. Assays with cyclo-L-Trp-L-Trp, cyclo-L-Trp- L-Tyr, cyclo-L-Trp-L-Phe show similar or even slightly higher conversion yields, compared with that of the natural substrate cyclo-L- Trp-L-Leu, whereas cyclo-L-Trp-L-Pro and cyclo-L-Trp-Gly are accepted by PboD but only with conversion yields of 10 and 4%, respectively. Cyclo-L-Trp-L-His is not accepted as a substrate. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L-Leu by condensing L-Leu with L-Trp. The flavin-dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.","Flavin-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. Within the pathway, pboD catalyzes the hydroxylation at C-3 of the indole ring of cyclo-L-Trp-L-Leu and subsequent formation of the pyrrolidine ring, eading to the production of protubonine D. PboD is also able to accept other cyclodipeptides (CDPs) as substrates, including cyclo-L-Trp-L-Trp, cyclo-L-Trp-L-Tyr, cyclo-L-Trp-L-Phe, cyclo-L-Trp-L-Met, cyclo-L-Trp-L-Ala, cyclo-L-Trp-L-Pro and cyclo-L- Trp-Gly. Assays with cyclo-L-Trp-L-Trp, cyclo-L-Trp- L-Tyr, cyclo-L-Trp-L-Phe show similar or even slightly higher conversion yields, compared with that of the natural substrate cyclo-L- Trp-L-Leu, whereas cyclo-L-Trp-L-Pro and cyclo-L-Trp-Gly are accepted by PboD but only with conversion yields of 10 and 4%, respectively. Cyclo-L-Trp-L-His is not accepted as a substrate. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L-Leu by condensing L-Leu with L-Trp. The flavin-dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.",,,,,,,GO:0071949; GO:0004497,GO:0004497; GO:0050660,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.9573,0.6988,0.6988,0.6988,0.6988,5,0.7505,0.189,no
STMB_ASPUT,A0A0C1E3B7,ESM2Text,Eukaryota,2059,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of stromemycin, a depside C-glucoside with two unsaturated C9 side chains belonging to aromatic polyketide glycosides. The HR-PKS stmA and the NR-PKS stmB act as scaffold-generating enzymes responsible for the biosynthesis of the polyketide skeleton bininalkenylresorcylic acid. StmA condenses on acetyl-CoA starter unit with 4 malonyl-CoA units and the stmB uses 3 more malonyl-CoA units and catalyzes the depside bond formation. The glycoytransferase stmC then acts as the tailoring enzyme responsible for 3-C-glucosylation of bininalkenylresorcylic acid to yield stromemycin.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0031177,,,,,,,,,,,0,,0.2398,no
STMB_ASPUT,A0A0C1E3B7,Prot2Text,Eukaryota,2059,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of stromemycin, a depside C-glucoside with two unsaturated C9 side chains belonging to aromatic polyketide glycosides. The HR-PKS stmA and the NR-PKS stmB act as scaffold-generating enzymes responsible for the biosynthesis of the polyketide skeleton bininalkenylresorcylic acid. StmA condenses on acetyl-CoA starter unit with 4 malonyl-CoA units and the stmB uses 3 more malonyl-CoA units and catalyzes the depside bond formation. The glycoytransferase stmC then acts as the tailoring enzyme responsible for 3-C-glucosylation of bininalkenylresorcylic acid to yield stromemycin.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0031177,GO:0016747,,,GO:0016747,GO:0016746,0.6029,,,0.6029,0.5216,3,0.5758,0.2398,no
STMB_ASPUT,A0A0C1E3B7,ProtT3,Eukaryota,2059,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of stromemycin, a depside C-glucoside with two unsaturated C9 side chains belonging to aromatic polyketide glycosides. The HR-PKS stmA and the NR-PKS stmB act as scaffold-generating enzymes responsible for the biosynthesis of the polyketide skeleton bininalkenylresorcylic acid. StmA condenses on acetyl-CoA starter unit with 4 malonyl-CoA units and the stmB uses 3 more malonyl-CoA units and catalyzes the depside bond formation. The glycoytransferase stmC then acts as the tailoring enzyme responsible for 3-C-glucosylation of bininalkenylresorcylic acid to yield stromemycin.","Polyketide synthase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS) . SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms (",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0031177,GO:0016746,GO:0016746,,GO:0016746,GO:0016747,0.5216,0.5216,,0.5216,0.6029,4,0.5419,0.2398,no
STMB_ASPUT,A0A0C1E3B7,ProtTale,Eukaryota,2059,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of stromemycin, a depside C-glucoside with two unsaturated C9 side chains belonging to aromatic polyketide glycosides. The HR-PKS stmA and the NR-PKS stmB act as scaffold-generating enzymes responsible for the biosynthesis of the polyketide skeleton bininalkenylresorcylic acid. StmA condenses on acetyl-CoA starter unit with 4 malonyl-CoA units and the stmB uses 3 more malonyl-CoA units and catalyzes the depside bond formation. The glycoytransferase stmC then acts as the tailoring enzyme responsible for 3-C-glucosylation of bininalkenylresorcylic acid to yield stromemycin.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0031177,GO:0016491,GO:0016757,,,GO:0016746,0.2791,0.357,,,0.5216,3,0.3859,0.2398,no
STMB_ASPUT,A0A0C1E3B7,Protein2Text,Eukaryota,2059,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of stromemycin, a depside C-glucoside with two unsaturated C9 side chains belonging to aromatic polyketide glycosides. The HR-PKS stmA and the NR-PKS stmB act as scaffold-generating enzymes responsible for the biosynthesis of the polyketide skeleton bininalkenylresorcylic acid. StmA condenses on acetyl-CoA starter unit with 4 malonyl-CoA units and the stmB uses 3 more malonyl-CoA units and catalyzes the depside bond formation. The glycoytransferase stmC then acts as the tailoring enzyme responsible for 3-C-glucosylation of bininalkenylresorcylic acid to yield stromemycin.","The molecular function of this protein is a dehydratase, specifically a type of enzyme involved in the biosynthesis of amino acids.",No,No,No,No,No,not-Yes,GO:0004312; GO:0031177,GO:0016829,GO:0016836,GO:0016836,GO:0016836,GO:0016836,0.2791,0.1876,0.1876,0.1876,0.1876,5,0.2059,0.2398,no
STMB_ASPUT,A0A0C1E3B7,Reference,Eukaryota,2059,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of stromemycin, a depside C-glucoside with two unsaturated C9 side chains belonging to aromatic polyketide glycosides. The HR-PKS stmA and the NR-PKS stmB act as scaffold-generating enzymes responsible for the biosynthesis of the polyketide skeleton bininalkenylresorcylic acid. StmA condenses on acetyl-CoA starter unit with 4 malonyl-CoA units and the stmB uses 3 more malonyl-CoA units and catalyzes the depside bond formation. The glycoytransferase stmC then acts as the tailoring enzyme responsible for 3-C-glucosylation of bininalkenylresorcylic acid to yield stromemycin.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of stromemycin, a depside C-glucoside with two unsaturated C9 side chains belonging to aromatic polyketide glycosides. The HR-PKS stmA and the NR-PKS stmB act as scaffold-generating enzymes responsible for the biosynthesis of the polyketide skeleton bininalkenylresorcylic acid. StmA condenses on acetyl-CoA starter unit with 4 malonyl-CoA units and the stmB uses 3 more malonyl-CoA units and catalyzes the depside bond formation. The glycoytransferase stmC then acts as the tailoring enzyme responsible for 3-C-glucosylation of bininalkenylresorcylic acid to yield stromemycin.",,,,,,,GO:0004312; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.5216,0.5216,0.5216,0.6029,0.5216,5,0.5379,0.2398,no
STMA_ASPUT,A0A0C1E3C9,ESM2Text,Eukaryota,2367,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of stromemycin, a depside C-glucoside with two unsaturated C9 side chains belonging to aromatic polyketide glycosides. The HR-PKS stmA and the NR-PKS stmB act as scaffold-generating enzymes responsible for the biosynthesis of the polyketide skeleton bininalkenylresorcylic acid. StmA condenses on acetyl-CoA starter unit with 4 malonyl-CoA units and the stmB uses 3 more malonyl-CoA units and catalyzes the depside bond formation. The glycoytransferase stmC then acts as the tailoring enzyme responsible for 3-C-glucosylation of bininalkenylresorcylic acid to yield stromemycin.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential tr",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177; GO:0008757; GO:0008270,,,,,,,,,,,0,,0.2611,no
STMA_ASPUT,A0A0C1E3C9,Prot2Text,Eukaryota,2367,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of stromemycin, a depside C-glucoside with two unsaturated C9 side chains belonging to aromatic polyketide glycosides. The HR-PKS stmA and the NR-PKS stmB act as scaffold-generating enzymes responsible for the biosynthesis of the polyketide skeleton bininalkenylresorcylic acid. StmA condenses on acetyl-CoA starter unit with 4 malonyl-CoA units and the stmB uses 3 more malonyl-CoA units and catalyzes the depside bond formation. The glycoytransferase stmC then acts as the tailoring enzyme responsible for 3-C-glucosylation of bininalkenylresorcylic acid to yield stromemycin.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177; GO:0008757; GO:0008270,GO:0016747,,,GO:0016747,GO:0016746,0.5078,,,0.5078,0.4797,3,0.4984,0.2611,no
STMA_ASPUT,A0A0C1E3C9,ProtT3,Eukaryota,2367,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of stromemycin, a depside C-glucoside with two unsaturated C9 side chains belonging to aromatic polyketide glycosides. The HR-PKS stmA and the NR-PKS stmB act as scaffold-generating enzymes responsible for the biosynthesis of the polyketide skeleton bininalkenylresorcylic acid. StmA condenses on acetyl-CoA starter unit with 4 malonyl-CoA units and the stmB uses 3 more malonyl-CoA units and catalyzes the depside bond formation. The glycoytransferase stmC then acts as the tailoring enzyme responsible for 3-C-glucosylation of bininalkenylresorcylic acid to yield stromemycin.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177; GO:0008757; GO:0008270,GO:0016746,GO:0016746,,GO:0016746,GO:0016747,0.4797,0.4797,,0.4797,0.5078,4,0.4867,0.2611,no
STMA_ASPUT,A0A0C1E3C9,ProtTale,Eukaryota,2367,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of stromemycin, a depside C-glucoside with two unsaturated C9 side chains belonging to aromatic polyketide glycosides. The HR-PKS stmA and the NR-PKS stmB act as scaffold-generating enzymes responsible for the biosynthesis of the polyketide skeleton bininalkenylresorcylic acid. StmA condenses on acetyl-CoA starter unit with 4 malonyl-CoA units and the stmB uses 3 more malonyl-CoA units and catalyzes the depside bond formation. The glycoytransferase stmC then acts as the tailoring enzyme responsible for 3-C-glucosylation of bininalkenylresorcylic acid to yield stromemycin.","Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. Within the pathway, ptmC is responsible for the cyclization of prepenitrem D to yield penitrem B. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3-glycerol phosphate with GGPP by ptmC then forms 3",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177; GO:0008757; GO:0008270,GO:0016491,GO:0016757,,,GO:0016746,0.4745,0.3739,,,0.4797,3,0.4427,0.2611,no
STMA_ASPUT,A0A0C1E3C9,Protein2Text,Eukaryota,2367,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of stromemycin, a depside C-glucoside with two unsaturated C9 side chains belonging to aromatic polyketide glycosides. The HR-PKS stmA and the NR-PKS stmB act as scaffold-generating enzymes responsible for the biosynthesis of the polyketide skeleton bininalkenylresorcylic acid. StmA condenses on acetyl-CoA starter unit with 4 malonyl-CoA units and the stmB uses 3 more malonyl-CoA units and catalyzes the depside bond formation. The glycoytransferase stmC then acts as the tailoring enzyme responsible for 3-C-glucosylation of bininalkenylresorcylic acid to yield stromemycin.","The molecular function of the protein is a FAD-dependent oxidoreductase. It is a part of the biosynthesis pathway for fumonisins, a type of mycotoxin. This protein is involved in the conversion of a specific intermediate in the pathway into a product. 

The protein is likely responsible for the conversion of the intermediate 13 into 14, but the exact nature of this conversion is not well understood. It is possible that the protein catalyzes an oxidation reaction, but the exact mechanism is unclear. Further research is needed to fully understand the molecular function of this protein.",No,No,No,No,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177; GO:0008757; GO:0008270,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4745,0.4745,0.4745,0.4745,0.4745,5,0.4745,0.2611,no
STMA_ASPUT,A0A0C1E3C9,Reference,Eukaryota,2367,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of stromemycin, a depside C-glucoside with two unsaturated C9 side chains belonging to aromatic polyketide glycosides. The HR-PKS stmA and the NR-PKS stmB act as scaffold-generating enzymes responsible for the biosynthesis of the polyketide skeleton bininalkenylresorcylic acid. StmA condenses on acetyl-CoA starter unit with 4 malonyl-CoA units and the stmB uses 3 more malonyl-CoA units and catalyzes the depside bond formation. The glycoytransferase stmC then acts as the tailoring enzyme responsible for 3-C-glucosylation of bininalkenylresorcylic acid to yield stromemycin.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of stromemycin, a depside C-glucoside with two unsaturated C9 side chains belonging to aromatic polyketide glycosides. The HR-PKS stmA and the NR-PKS stmB act as scaffold-generating enzymes responsible for the biosynthesis of the polyketide skeleton bininalkenylresorcylic acid. StmA condenses on acetyl-CoA starter unit with 4 malonyl-CoA units and the stmB uses 3 more malonyl-CoA units and catalyzes the depside bond formation. The glycoytransferase stmC then acts as the tailoring enzyme responsible for 3-C-glucosylation of bininalkenylresorcylic acid to yield stromemycin.",,,,,,,GO:0004315; GO:0004312; GO:0016491; GO:0031177; GO:0008757; GO:0008270,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.4797,0.4797,0.4797,0.5078,0.4797,5,0.4853,0.2611,no
CHS8_GIBZE,A0A0E0S977,ESM2Text,Eukaryota,668,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer (Probable). Participated in the development of cell wall and plays a critical role in fungal response to environmental stresses. Necessary for pathogenicity and deoxinivalenol (DON) production.","Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4623,no
CHS8_GIBZE,A0A0E0S977,Prot2Text,Eukaryota,668,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer (Probable). Participated in the development of cell wall and plays a critical role in fungal response to environmental stresses. Necessary for pathogenicity and deoxinivalenol (DON) production.",Thought to be a Golgi-localized beta-glycan synthase that polymerize the backbones of noncellulosic polysaccharides (hemicelluloses) of plant cell wall.,No,Maybe,No,No,No,not-Yes,GO:0004100,GO:0016757,,GO:0016757,GO:0016757,GO:0016757,0.5917,,0.5917,0.5917,0.5917,4,0.5917,0.4623,no
CHS8_GIBZE,A0A0E0S977,ProtT3,Eukaryota,668,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer (Probable). Participated in the development of cell wall and plays a critical role in fungal response to environmental stresses. Necessary for pathogenicity and deoxinivalenol (DON) production.","Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer. Cell membrane; Multi-pass membrane protein. Belongs to the chitin synthase family. Class III subfamily",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4623,no
CHS8_GIBZE,A0A0E0S977,ProtTale,Eukaryota,668,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer (Probable). Participated in the development of cell wall and plays a critical role in fungal response to environmental stresses. Necessary for pathogenicity and deoxinivalenol (DON) production.","Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004100,GO:0004100,GO:0004568,GO:0004100,GO:0004100,GO:0004100,1.0,0.1603,1.0,1.0,1.0,5,0.8321,0.4623,no
CHS8_GIBZE,A0A0E0S977,Protein2Text,Eukaryota,668,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer (Probable). Participated in the development of cell wall and plays a critical role in fungal response to environmental stresses. Necessary for pathogenicity and deoxinivalenol (DON) production.","The molecular function of this protein is not explicitly stated in the provided text, but based on its name, it is likely involved in the synthesis of glycosaminoglycans (GAGs), which are components of the extracellular matrix and play important roles in various cellular processes. In particular, the name suggests that it may be involved in the synthesis of hyaluronic acid, a type of GAG that is important for cell proliferation, migration, and tissue repair.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004100,,,,GO:0050501,,,,,0.6917,,1,0.6917,0.4623,no
CHS8_GIBZE,A0A0E0S977,Reference,Eukaryota,668,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer (Probable). Participated in the development of cell wall and plays a critical role in fungal response to environmental stresses. Necessary for pathogenicity and deoxinivalenol (DON) production.","Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer (Probable). Participated in the development of cell wall and plays a critical role in fungal response to environmental stresses. Necessary for pathogenicity and deoxinivalenol (DON) production.",,,,,,,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4623,no
UMPDO_AMYSP,A0A0E3USC3,ESM2Text,Bacteria,275,"Dioxygenase involved in the biosynthesis of the capuramycin- type nucleoside antibiotic A-102395. Catalyzes the dephosphorylation and oxidation of UMP to generate uridine-5'-aldehyde. Can also use the alternative alpha-keto acids pyruvate and alpha-ketoadipate (2-oxoadipate), with very low efficiency. Cannot use alpha-ketobutyrate, alpha-ketovalerate and oxaloacetate.","Alpha-ketoglutarate-dependent dioxygenase that catalyzes the regioselective hydroxylation of L-alpha-ketoglutarate to yield (2S,3S)-3-hydroxy-L-alpha-ketoglutarate. To a lesser extent, is also able to catalyze the regioselective hydroxylation of L-ribulose and L-xylulose. Is devoid of activity toward D-nitrophenyl phosphate.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0051213; GO:0046872,GO:0016706,GO:0016706,GO:0016706,GO:0016706,,0.5293,0.5293,0.5293,0.5293,,4,0.5293,0.2601,no
UMPDO_AMYSP,A0A0E3USC3,Prot2Text,Bacteria,275,"Dioxygenase involved in the biosynthesis of the capuramycin- type nucleoside antibiotic A-102395. Catalyzes the dephosphorylation and oxidation of UMP to generate uridine-5'-aldehyde. Can also use the alternative alpha-keto acids pyruvate and alpha-ketoadipate (2-oxoadipate), with very low efficiency. Cannot use alpha-ketobutyrate, alpha-ketovalerate and oxaloacetate.",Catalyzes the Fe(2+) and alpha-ketoglutarate-dependent oxidation of pentalenolactone D to pentalenolactone F in the biosynthesis of pentalenolactone antibiotic.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0051213; GO:0046872,GO:0016706,GO:0016706,GO:0016706,GO:0016706,GO:0016706,0.5293,0.5293,0.5293,0.5293,0.5293,5,0.5293,0.2601,no
UMPDO_AMYSP,A0A0E3USC3,ProtT3,Bacteria,275,"Dioxygenase involved in the biosynthesis of the capuramycin- type nucleoside antibiotic A-102395. Catalyzes the dephosphorylation and oxidation of UMP to generate uridine-5'-aldehyde. Can also use the alternative alpha-keto acids pyruvate and alpha-ketoadipate (2-oxoadipate), with very low efficiency. Cannot use alpha-ketobutyrate, alpha-ketovalerate and oxaloacetate.","Alpha-ketoglutarate-dependent dioxygenase that catalyzes the hydroxylation of 2,3-dihydroxybenzoate (2,3-DHB) to yield 3-hydroxybenzoate (3-OHB). Belongs to the TfdA dioxygenase family",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0051213; GO:0046872,GO:0016706,GO:0016706,GO:0016706,GO:0016706; GO:0005506,GO:0016706,0.5293,0.5293,0.5293,0.7588,0.5293,5,0.5752,0.2601,no
UMPDO_AMYSP,A0A0E3USC3,ProtTale,Bacteria,275,"Dioxygenase involved in the biosynthesis of the capuramycin- type nucleoside antibiotic A-102395. Catalyzes the dephosphorylation and oxidation of UMP to generate uridine-5'-aldehyde. Can also use the alternative alpha-keto acids pyruvate and alpha-ketoadipate (2-oxoadipate), with very low efficiency. Cannot use alpha-ketobutyrate, alpha-ketovalerate and oxaloacetate.","Catalyzes the hydroxylation of L-ornithine to 2,3-dihydroxypentanedioate (L-2,3-DPA).",No,No,No,No,No,not-Yes,GO:0051213; GO:0046872,GO:0016706,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.5293,0.5957,0.5957,0.5957,0.5957,5,0.5824,0.2601,no
UMPDO_AMYSP,A0A0E3USC3,Protein2Text,Bacteria,275,"Dioxygenase involved in the biosynthesis of the capuramycin- type nucleoside antibiotic A-102395. Catalyzes the dephosphorylation and oxidation of UMP to generate uridine-5'-aldehyde. Can also use the alternative alpha-keto acids pyruvate and alpha-ketoadipate (2-oxoadipate), with very low efficiency. Cannot use alpha-ketobutyrate, alpha-ketovalerate and oxaloacetate.","This protein is involved in the molecular function of catalyzing the hydrolysis of a carbon-nitrogen bond, specifically in the breakdown of a nitrogen-containing compound. It is involved in the biosynthesis of a secondary metabolite.",No,No,No,No,No,not-Yes,GO:0051213; GO:0046872,GO:0016810,GO:0016810,GO:0016810,GO:0016810,,0.3023,0.3023,0.3023,0.3023,,4,0.3023,0.2601,no
UMPDO_AMYSP,A0A0E3USC3,Reference,Bacteria,275,"Dioxygenase involved in the biosynthesis of the capuramycin- type nucleoside antibiotic A-102395. Catalyzes the dephosphorylation and oxidation of UMP to generate uridine-5'-aldehyde. Can also use the alternative alpha-keto acids pyruvate and alpha-ketoadipate (2-oxoadipate), with very low efficiency. Cannot use alpha-ketobutyrate, alpha-ketovalerate and oxaloacetate.","Dioxygenase involved in the biosynthesis of the capuramycin- type nucleoside antibiotic A-102395. Catalyzes the dephosphorylation and oxidation of UMP to generate uridine-5'-aldehyde. Can also use the alternative alpha-keto acids pyruvate and alpha-ketoadipate (2-oxoadipate), with very low efficiency. Cannot use alpha-ketobutyrate, alpha-ketovalerate and oxaloacetate.",,,,,,,GO:0051213; GO:0046872,GO:0016706,GO:0016706,GO:0051213,GO:0016702,GO:0016706,0.5293,0.5293,0.7088,0.5293,0.5293,5,0.5652,0.2601,no
GPDA_THESQ,A0A0F6AK91,ESM2Text,Bacteria,321,"Catalyzes the reduction of the glycolytic intermediate dihydroxyacetone phosphate (DHAP) to sn-glycerol 3-phosphate (G3P), the key precursor for phospholipid synthesis.","Involved in the biosynthesis of the antimalarial drug, acriflavine. Catalyzes the reduction of the keto group at C-3 of 3-keto acids generating 3A-acetyl-CoA. In the reverse reaction, the acriflavine A:B(2) complex can be formed via a CoA funnel leading to CoA, via a combined FAD-CoA/FMN-dependent pyrophosphate exchange reaction. The major route of action of the enzyme, however, is facilitated by the sesquiterpene lactone, which leads to the production of acriflavine.",No,No,No,No,Yes,not-Yes,GO:0141152; GO:0141153; GO:0051287,,,,,,,,,,,0,,0.4517,no
GPDA_THESQ,A0A0F6AK91,Prot2Text,Bacteria,321,"Catalyzes the reduction of the glycolytic intermediate dihydroxyacetone phosphate (DHAP) to sn-glycerol 3-phosphate (G3P), the key precursor for phospholipid synthesis.",Involved in the biosynthesis of the sn-glycerol 3-phosphate required for phospholipid synthesis.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0141152; GO:0141153; GO:0051287,,,,,,,,,,,0,,0.4517,no
GPDA_THESQ,A0A0F6AK91,ProtT3,Bacteria,321,"Catalyzes the reduction of the glycolytic intermediate dihydroxyacetone phosphate (DHAP) to sn-glycerol 3-phosphate (G3P), the key precursor for phospholipid synthesis.",Cytoplasm. Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0141152; GO:0141153; GO:0051287,GO:0004367,GO:0004367,GO:0004367,GO:0004367; GO:0051287,GO:0004367,0.6694,0.6694,0.6694,0.9215,0.6694,5,0.7198,0.4517,no
GPDA_THESQ,A0A0F6AK91,ProtTale,Bacteria,321,"Catalyzes the reduction of the glycolytic intermediate dihydroxyacetone phosphate (DHAP) to sn-glycerol 3-phosphate (G3P), the key precursor for phospholipid synthesis.","Catalyzes the reduction of the glycolytic intermediate dihydroxyacetone phosphate (DHAP) to sn-glycerol 3-phosphate (G3P), the key precursor for phospholipid synthesis.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0141152; GO:0141153; GO:0051287,GO:0016616,GO:0004367,GO:0004367,GO:0004367,GO:0004367,0.5863,0.6694,0.6694,0.6694,0.6694,5,0.6528,0.4517,no
GPDA_THESQ,A0A0F6AK91,Protein2Text,Bacteria,321,"Catalyzes the reduction of the glycolytic intermediate dihydroxyacetone phosphate (DHAP) to sn-glycerol 3-phosphate (G3P), the key precursor for phospholipid synthesis.","This protein is an oxidoreductase. It is a part of the glycolytic pathway, and its molecular function is to catalyze the oxidation of glucose-6-phosphate to 6-phosphogluconolactone.",No,No,No,No,No,not-Yes,GO:0141152; GO:0141153; GO:0051287,GO:0004345,GO:0004345,GO:0004345,GO:0004345,GO:0004345,0.4928,0.4928,0.4928,0.4928,0.4928,5,0.4928,0.4517,no
GPDA_THESQ,A0A0F6AK91,Reference,Bacteria,321,"Catalyzes the reduction of the glycolytic intermediate dihydroxyacetone phosphate (DHAP) to sn-glycerol 3-phosphate (G3P), the key precursor for phospholipid synthesis.","Catalyzes the reduction of the glycolytic intermediate dihydroxyacetone phosphate (DHAP) to sn-glycerol 3-phosphate (G3P), the key precursor for phospholipid synthesis.",,,,,,,GO:0141152; GO:0141153; GO:0051287,GO:0004367,GO:0004367,GO:0004367,GO:0004367,GO:0004367,0.6694,0.6694,0.6694,0.6694,0.6694,5,0.6694,0.4517,no
ABF43_HUMIN,A0A0F6NRE2,ESM2Text,Eukaryota,481,"Alpha-L-arabinofuranosidase specific for the cleavage of alpha-1,3-linkage. Shows high activity against 4- nitrophenyl alpha-L-arabinofuranoside, debranched arabinan, and sugar beet arabinan.",Secreted alpha-L-arabinofuranosidase that actively hydrolyzes p-NP-alpha-L-arabinofuranosyl residues and acts as a virulence factor. Exhibits strong activity against polymeric but not non-polar substrates.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2952,no
ABF43_HUMIN,A0A0F6NRE2,Prot2Text,Eukaryota,481,"Alpha-L-arabinofuranosidase specific for the cleavage of alpha-1,3-linkage. Shows high activity against 4- nitrophenyl alpha-L-arabinofuranoside, debranched arabinan, and sugar beet arabinan.","Exo-inulinase involved in utilization of the plant storage polymer inulin, consisting of fructooligosaccharides with a degree of polymerization (DP) value from 2 to 60. Splits off terminal fructose units successively from the non-reducing end of the inulin molecule, and also hydrolyze sucrose and raffinose.",No,No,No,No,No,not-Yes,GO:0046556,GO:0004564,GO:0004564,GO:0004564,GO:0004564,GO:0004553,0.7289,0.7289,0.7289,0.7289,0.8582,5,0.7548,0.2952,no
ABF43_HUMIN,A0A0F6NRE2,ProtT3,Eukaryota,481,"Alpha-L-arabinofuranosidase specific for the cleavage of alpha-1,3-linkage. Shows high activity against 4- nitrophenyl alpha-L-arabinofuranoside, debranched arabinan, and sugar beet arabinan.","Endo-1,5-alpha-L-arabinanase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Releases L-arabinose from arabinoxylan (By similarity). Secreted. Belongs to the glycosyl hydrolase 43 family",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2952,no
ABF43_HUMIN,A0A0F6NRE2,ProtTale,Eukaryota,481,"Alpha-L-arabinofuranosidase specific for the cleavage of alpha-1,3-linkage. Shows high activity against 4- nitrophenyl alpha-L-arabinofuranoside, debranched arabinan, and sugar beet arabinan.","Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2952,no
ABF43_HUMIN,A0A0F6NRE2,Protein2Text,Eukaryota,481,"Alpha-L-arabinofuranosidase specific for the cleavage of alpha-1,3-linkage. Shows high activity against 4- nitrophenyl alpha-L-arabinofuranoside, debranched arabinan, and sugar beet arabinan.","The molecular function of this protein is a beta-glucosidase. It is involved in breaking down complex carbohydrates into simpler sugars. Specifically, it is responsible for hydrolyzing the terminal beta-glucose residue from a variety of substrates, including cellobiose, gentiobiose, and various glucosides. This protein is likely involved in the degradation of plant biomass and the utilization of cellulose and other complex carbohydrates as a carbon source.",No,No,No,No,No,not-Yes,GO:0046556,GO:0008422,GO:0008422,GO:0008422,GO:0008422,GO:0008422,0.6335,0.6335,0.6335,0.6335,0.6335,5,0.6335,0.2952,no
ABF43_HUMIN,A0A0F6NRE2,Reference,Eukaryota,481,"Alpha-L-arabinofuranosidase specific for the cleavage of alpha-1,3-linkage. Shows high activity against 4- nitrophenyl alpha-L-arabinofuranoside, debranched arabinan, and sugar beet arabinan.","Alpha-L-arabinofuranosidase specific for the cleavage of alpha-1,3-linkage. Shows high activity against 4- nitrophenyl alpha-L-arabinofuranoside, debranched arabinan, and sugar beet arabinan.",,,,,,,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2952,no
THNA_TRIHA,A0A0G0AID6,ESM2Text,Eukaryota,4043,"Hybrid PKS-NRPS synthetase; part of the gene cluster that produces the tetronate natural products trihazones. The PKS-NRPS synthetase thnA with the help of the trans-enoyl reductase thnE are responsible for the synthesis of the carboxylmethyl containing trihazone A. The PKS portion of thnA synthesizes beta-keto-triene chain from one acetyl-CoA and 6 equivalents of malonyl-CoA, in collaboration with thnE, which selectively reduces the enoyl intermediate during the first and fourth iteration of the PKS. The NRPS domain selects and activates malate, of which the alpha-hydroxyl group attacks the completed polyketide acyl-S- ACP chain to form the ester product. Intramolecular Dieckmann cyclization catalyzed by the terminal reductase domain releases the product as trihazone A from the PKS-NPRS. The pathway begins with the formation of trihazone A by the hybrid PKS-NRPS synthetase thnA and the trans-enoyl reductase thnE. Trihazone A is further decarboxylated by the 2-oxoglutarate- dependent dioxygenase thnC to produce trihazone D. The function of the FAD-dependent monooxygenase thnD has still to be identified.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The nonribosomal peptide synthetase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,,,,,,,,,,,0,,0.3314,no
THNA_TRIHA,A0A0G0AID6,Prot2Text,Eukaryota,4043,"Hybrid PKS-NRPS synthetase; part of the gene cluster that produces the tetronate natural products trihazones. The PKS-NRPS synthetase thnA with the help of the trans-enoyl reductase thnE are responsible for the synthesis of the carboxylmethyl containing trihazone A. The PKS portion of thnA synthesizes beta-keto-triene chain from one acetyl-CoA and 6 equivalents of malonyl-CoA, in collaboration with thnE, which selectively reduces the enoyl intermediate during the first and fourth iteration of the PKS. The NRPS domain selects and activates malate, of which the alpha-hydroxyl group attacks the completed polyketide acyl-S- ACP chain to form the ester product. Intramolecular Dieckmann cyclization catalyzed by the terminal reductase domain releases the product as trihazone A from the PKS-NPRS. The pathway begins with the formation of trihazone A by the hybrid PKS-NRPS synthetase thnA and the trans-enoyl reductase thnE. Trihazone A is further decarboxylated by the 2-oxoglutarate- dependent dioxygenase thnC to produce trihazone D. The function of the FAD-dependent monooxygenase thnD has still to be identified.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The nonribosomal peptide synthetase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0016747,,,GO:0016747,GO:0016746,0.5636,,,0.5636,0.5445,3,0.5572,0.3314,no
THNA_TRIHA,A0A0G0AID6,ProtT3,Eukaryota,4043,"Hybrid PKS-NRPS synthetase; part of the gene cluster that produces the tetronate natural products trihazones. The PKS-NRPS synthetase thnA with the help of the trans-enoyl reductase thnE are responsible for the synthesis of the carboxylmethyl containing trihazone A. The PKS portion of thnA synthesizes beta-keto-triene chain from one acetyl-CoA and 6 equivalents of malonyl-CoA, in collaboration with thnE, which selectively reduces the enoyl intermediate during the first and fourth iteration of the PKS. The NRPS domain selects and activates malate, of which the alpha-hydroxyl group attacks the completed polyketide acyl-S- ACP chain to form the ester product. Intramolecular Dieckmann cyclization catalyzed by the terminal reductase domain releases the product as trihazone A from the PKS-NPRS. The pathway begins with the formation of trihazone A by the hybrid PKS-NRPS synthetase thnA and the trans-enoyl reductase thnE. Trihazone A is further decarboxylated by the 2-oxoglutarate- dependent dioxygenase thnC to produce trihazone D. The function of the FAD-dependent monooxygenase thnD has still to be identified.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0016746,GO:0016746,,GO:0016746,GO:0016747,0.5445,0.5445,,0.5445,0.5636,4,0.5493,0.3314,no
THNA_TRIHA,A0A0G0AID6,ProtTale,Eukaryota,4043,"Hybrid PKS-NRPS synthetase; part of the gene cluster that produces the tetronate natural products trihazones. The PKS-NRPS synthetase thnA with the help of the trans-enoyl reductase thnE are responsible for the synthesis of the carboxylmethyl containing trihazone A. The PKS portion of thnA synthesizes beta-keto-triene chain from one acetyl-CoA and 6 equivalents of malonyl-CoA, in collaboration with thnE, which selectively reduces the enoyl intermediate during the first and fourth iteration of the PKS. The NRPS domain selects and activates malate, of which the alpha-hydroxyl group attacks the completed polyketide acyl-S- ACP chain to form the ester product. Intramolecular Dieckmann cyclization catalyzed by the terminal reductase domain releases the product as trihazone A from the PKS-NPRS. The pathway begins with the formation of trihazone A by the hybrid PKS-NRPS synthetase thnA and the trans-enoyl reductase thnE. Trihazone A is further decarboxylated by the 2-oxoglutarate- dependent dioxygenase thnC to produce trihazone D. The function of the FAD-dependent monooxygenase thnD has still to be identified.","Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the",Maybe,Yes,Yes,Yes,Maybe,Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0016491,GO:0016757,,,GO:0016746; GO:0016874,0.5478,0.4493,,,0.6826,3,0.5599,0.3314,no
THNA_TRIHA,A0A0G0AID6,Protein2Text,Eukaryota,4043,"Hybrid PKS-NRPS synthetase; part of the gene cluster that produces the tetronate natural products trihazones. The PKS-NRPS synthetase thnA with the help of the trans-enoyl reductase thnE are responsible for the synthesis of the carboxylmethyl containing trihazone A. The PKS portion of thnA synthesizes beta-keto-triene chain from one acetyl-CoA and 6 equivalents of malonyl-CoA, in collaboration with thnE, which selectively reduces the enoyl intermediate during the first and fourth iteration of the PKS. The NRPS domain selects and activates malate, of which the alpha-hydroxyl group attacks the completed polyketide acyl-S- ACP chain to form the ester product. Intramolecular Dieckmann cyclization catalyzed by the terminal reductase domain releases the product as trihazone A from the PKS-NPRS. The pathway begins with the formation of trihazone A by the hybrid PKS-NRPS synthetase thnA and the trans-enoyl reductase thnE. Trihazone A is further decarboxylated by the 2-oxoglutarate- dependent dioxygenase thnC to produce trihazone D. The function of the FAD-dependent monooxygenase thnD has still to be identified.","This protein is a subunit of the fatty acid synthase (FAS) enzyme, which is a multi-subunit enzyme that catalyzes the formation of fatty acids from acetyl-CoA and malonyl-CoA. The molecular function of this protein is to participate in the elongation of fatty acids, specifically in the condensation of malonyl-CoA with acyl-CoA to form beta-ketoacyl-CoA. This is a crucial step in the biosynthesis of fatty acids, which are important components of cellular membranes and energy storage molecules.",No,Maybe,Maybe,Maybe,No,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.5599,0.5599,0.5599,0.5599,0.5599,5,0.5599,0.3314,no
THNA_TRIHA,A0A0G0AID6,Reference,Eukaryota,4043,"Hybrid PKS-NRPS synthetase; part of the gene cluster that produces the tetronate natural products trihazones. The PKS-NRPS synthetase thnA with the help of the trans-enoyl reductase thnE are responsible for the synthesis of the carboxylmethyl containing trihazone A. The PKS portion of thnA synthesizes beta-keto-triene chain from one acetyl-CoA and 6 equivalents of malonyl-CoA, in collaboration with thnE, which selectively reduces the enoyl intermediate during the first and fourth iteration of the PKS. The NRPS domain selects and activates malate, of which the alpha-hydroxyl group attacks the completed polyketide acyl-S- ACP chain to form the ester product. Intramolecular Dieckmann cyclization catalyzed by the terminal reductase domain releases the product as trihazone A from the PKS-NPRS. The pathway begins with the formation of trihazone A by the hybrid PKS-NRPS synthetase thnA and the trans-enoyl reductase thnE. Trihazone A is further decarboxylated by the 2-oxoglutarate- dependent dioxygenase thnC to produce trihazone D. The function of the FAD-dependent monooxygenase thnD has still to be identified.","Hybrid PKS-NRPS synthetase; part of the gene cluster that produces the tetronate natural products trihazones. The PKS-NRPS synthetase thnA with the help of the trans-enoyl reductase thnE are responsible for the synthesis of the carboxylmethyl containing trihazone A. The PKS portion of thnA synthesizes beta-keto-triene chain from one acetyl-CoA and 6 equivalents of malonyl-CoA, in collaboration with thnE, which selectively reduces the enoyl intermediate during the first and fourth iteration of the PKS. The NRPS domain selects and activates malate, of which the alpha-hydroxyl group attacks the completed polyketide acyl-S- ACP chain to form the ester product. Intramolecular Dieckmann cyclization catalyzed by the terminal reductase domain releases the product as trihazone A from the PKS-NPRS. The pathway begins with the formation of trihazone A by the hybrid PKS-NRPS synthetase thnA and the trans-enoyl reductase thnE. Trihazone A is further decarboxylated by the 2-oxoglutarate- dependent dioxygenase thnC to produce trihazone D. The function of the FAD-dependent monooxygenase thnD has still to be identified.",,,,,,,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0016746; GO:0016874,GO:0016874; GO:0016746,GO:0016746; GO:0016874,GO:0016874,GO:0016874,0.6826,0.6826,0.6826,0.5478,0.5478,5,0.6287,0.3314,no
EGTUA_STRP2,A0A0H2ZLL3,ESM2Text,Bacteria,242,"Part of an ABC transporter complex EgtU required for the uptake of ergothioneine (EGT), a natural low-molecular weight (LMW) thiol antioxidant. Probably responsible for energy coupling to the transport system.",Part of the ABC transporter complex YtrBCDEF that plays a role in acetoin utilization during stationary phase and sporulation. Involved in a phosphonate transport system.,Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0015418; GO:0005524; GO:0016887,,GO:0016887,,,,,0.5596,,,,1,0.5596,0.3069,no
EGTUA_STRP2,A0A0H2ZLL3,Prot2Text,Bacteria,242,"Part of an ABC transporter complex EgtU required for the uptake of ergothioneine (EGT), a natural low-molecular weight (LMW) thiol antioxidant. Probably responsible for energy coupling to the transport system.","Part of the ABC transporter complex CntABCDF (Opp1) involved in the uptake of metal in complex with the metallophore staphylopine (StP). Involved in the import of divalent metals ions such as nickel, cobalt and zinc. Probably responsible for energy coupling to the transport system.",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0015418; GO:0005524; GO:0016887,GO:0042626,GO:0016887,GO:0042626,GO:0016887,GO:0016887; GO:0005524,0.4645,0.5596,0.4645,0.5596,0.8355,5,0.5767,0.3069,no
EGTUA_STRP2,A0A0H2ZLL3,ProtT3,Bacteria,242,"Part of an ABC transporter complex EgtU required for the uptake of ergothioneine (EGT), a natural low-molecular weight (LMW) thiol antioxidant. Probably responsible for energy coupling to the transport system.",Probably part of an ABC transporter complex. Probably responsible for energy coupling to the transport system (By similarity). Belongs to the ABC transporter superfamily,Maybe,Yes,Maybe,Vague,Vague,not-Yes,GO:0015418; GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0005524; GO:0016887,GO:0042626; GO:0005524,GO:0005524; GO:0016887,GO:0016887; GO:0005524,0.8355,0.8355,0.757,0.8355,0.8355,5,0.8198,0.3069,no
EGTUA_STRP2,A0A0H2ZLL3,ProtTale,Bacteria,242,"Part of an ABC transporter complex EgtU required for the uptake of ergothioneine (EGT), a natural low-molecular weight (LMW) thiol antioxidant. Probably responsible for energy coupling to the transport system.",Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.,Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0015418; GO:0005524; GO:0016887,GO:0005524,GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.5282,0.8355,0.8355,0.8355,0.8355,5,0.774,0.3069,no
EGTUA_STRP2,A0A0H2ZLL3,Protein2Text,Bacteria,242,"Part of an ABC transporter complex EgtU required for the uptake of ergothioneine (EGT), a natural low-molecular weight (LMW) thiol antioxidant. Probably responsible for energy coupling to the transport system.",This protein is involved in the molecular function of being a part of a transporter.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0015418; GO:0005524; GO:0016887,,,,GO:0005215,,,,,0.2427,,1,0.2427,0.3069,no
EGTUA_STRP2,A0A0H2ZLL3,Reference,Bacteria,242,"Part of an ABC transporter complex EgtU required for the uptake of ergothioneine (EGT), a natural low-molecular weight (LMW) thiol antioxidant. Probably responsible for energy coupling to the transport system.","Part of an ABC transporter complex EgtU required for the uptake of ergothioneine (EGT), a natural low-molecular weight (LMW) thiol antioxidant. Probably responsible for energy coupling to the transport system.",,,,,,,GO:0015418; GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0042626,GO:0016887; GO:0005524,GO:0005524; GO:0016887,GO:0016887; GO:0005524,0.8355,0.4645,0.8355,0.8355,0.8355,5,0.7613,0.3069,no
PCRAS_MYCPB,A0A0H3DK98,ESM2Text,Bacteria,529,"Binds single-stranded (ss)DNA, but not double-stranded (ds)DNA. Unwinds both 3'- and 5'-extended dsDNA (but not blunt-ended dsDNA) with a preference for 3'-extended DNA and 3'-extended branched DNA. Probably involved in DNA repair and recombination (Probable).",May be involved in RNA metabolism.,Vague,Vague,Vague,Vague,No,not-Yes,GO:0043138; GO:0005524; GO:0016887; GO:0003677,,,,,,,,,,,0,,0.6913,yes
PCRAS_MYCPB,A0A0H3DK98,Prot2Text,Bacteria,529,"Binds single-stranded (ss)DNA, but not double-stranded (ds)DNA. Unwinds both 3'- and 5'-extended dsDNA (but not blunt-ended dsDNA) with a preference for 3'-extended DNA and 3'-extended branched DNA. Probably involved in DNA repair and recombination (Probable).",Helicase.,Maybe,Vague,Maybe,Vague,Maybe,not-Yes,GO:0043138; GO:0005524; GO:0016887; GO:0003677,GO:0004386,GO:0004386,GO:0004386,GO:0004386,GO:0004386; GO:0005524,0.4085,0.4085,0.4085,0.4085,0.6681,5,0.4604,0.6913,yes
PCRAS_MYCPB,A0A0H3DK98,ProtT3,Bacteria,529,"Binds single-stranded (ss)DNA, but not double-stranded (ds)DNA. Unwinds both 3'- and 5'-extended dsDNA (but not blunt-ended dsDNA) with a preference for 3'-extended DNA and 3'-extended branched DNA. Probably involved in DNA repair and recombination (Probable).","Involved in DNA mismatch repair (MMR) and nucleotide excision repair (NER). Has a 3'-5' exonuclease activity on single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA), and a 5'-3' exonuclease activity on dsDNA, but not on ssDNA. Cytoplasm. Belongs to the helicase family. UvrD subfamily",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0043138; GO:0005524; GO:0016887; GO:0003677,GO:0008408; GO:0008409,GO:0004527; GO:0004386; GO:0005524,GO:0008408; GO:0008409; GO:0004386,GO:0008409; GO:0008296,GO:0008408; GO:0008409,0.1812,0.6109,0.3589,0.1827,0.1812,5,0.303,0.6913,yes
PCRAS_MYCPB,A0A0H3DK98,ProtTale,Bacteria,529,"Binds single-stranded (ss)DNA, but not double-stranded (ds)DNA. Unwinds both 3'- and 5'-extended dsDNA (but not blunt-ended dsDNA) with a preference for 3'-extended DNA and 3'-extended branched DNA. Probably involved in DNA repair and recombination (Probable).",DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks.,Yes,Yes,Yes,Yes,No,Yes,GO:0043138; GO:0005524; GO:0016887; GO:0003677,GO:0004386; GO:0005524; GO:0003677,GO:0003678; GO:0005524; GO:0004386,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,0.8348,0.7285,0.7113,0.7113,0.7113,5,0.7394,0.6913,yes
PCRAS_MYCPB,A0A0H3DK98,Protein2Text,Bacteria,529,"Binds single-stranded (ss)DNA, but not double-stranded (ds)DNA. Unwinds both 3'- and 5'-extended dsDNA (but not blunt-ended dsDNA) with a preference for 3'-extended DNA and 3'-extended branched DNA. Probably involved in DNA repair and recombination (Probable).",This protein is a 5'-3' exonuclease.,No,No,No,No,No,not-Yes,GO:0043138; GO:0005524; GO:0016887; GO:0003677,GO:0004532,GO:0004534,GO:0004534,GO:0004534,,0.1493,0.1242,0.1242,0.1242,,4,0.1305,0.6913,yes
PCRAS_MYCPB,A0A0H3DK98,Reference,Bacteria,529,"Binds single-stranded (ss)DNA, but not double-stranded (ds)DNA. Unwinds both 3'- and 5'-extended dsDNA (but not blunt-ended dsDNA) with a preference for 3'-extended DNA and 3'-extended branched DNA. Probably involved in DNA repair and recombination (Probable).","Binds single-stranded (ss)DNA, but not double-stranded (ds)DNA. Unwinds both 3'- and 5'-extended dsDNA (but not blunt-ended dsDNA) with a preference for 3'-extended DNA and 3'-extended branched DNA. Probably involved in DNA repair and recombination (Probable).",,,,,,,GO:0043138; GO:0005524; GO:0016887; GO:0003677,GO:0003678; GO:0003697,GO:0003697; GO:0003678,GO:0003678; GO:0003697,GO:0004386; GO:0003697,GO:0003678; GO:0003697,0.6547,0.6547,0.6547,0.6115,0.6547,5,0.6461,0.6913,yes
RUVB_MYCPB,A0A0H3DN66,ESM2Text,Bacteria,307,"The RuvA-RuvB-RecU complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RecU to scan and cleave DNA to resolve the cruciform.","The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0000400; GO:0009378,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,0.7046,0.7046,0.7046,0.7046,0.7046,5,0.7046,0.5483,yes
RUVB_MYCPB,A0A0H3DN66,Prot2Text,Bacteria,307,"The RuvA-RuvB-RecU complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RecU to scan and cleave DNA to resolve the cruciform.","The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0000400; GO:0009378,GO:0003678; GO:0005524,GO:0009378,GO:0004386; GO:0016887,GO:0004003,GO:0004386; GO:0005524,0.7046,0.4699,0.6163,0.4471,0.6614,5,0.5799,0.5483,yes
RUVB_MYCPB,A0A0H3DN66,ProtT3,Bacteria,307,"The RuvA-RuvB-RecU complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RecU to scan and cleave DNA to resolve the cruciform.","The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0000400; GO:0009378,GO:0003678; GO:0005524,GO:0004386; GO:0005524,GO:0004003; GO:0005524; GO:0003677,GO:0003678; GO:0005524,GO:0004386; GO:0005524,0.7046,0.6614,0.7944,0.7046,0.6614,5,0.7053,0.5483,yes
RUVB_MYCPB,A0A0H3DN66,ProtTale,Bacteria,307,"The RuvA-RuvB-RecU complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RecU to scan and cleave DNA to resolve the cruciform.","The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0000400; GO:0009378,GO:0004386; GO:0005524; GO:0003677,GO:0004386; GO:0005524,GO:0008094; GO:0003678; GO:0005524,GO:0016887; GO:0003678; GO:0005524,GO:0003678; GO:0016887; GO:0005524,0.7573,0.6614,0.7138,0.8543,0.8543,5,0.7682,0.5483,yes
RUVB_MYCPB,A0A0H3DN66,Protein2Text,Bacteria,307,"The RuvA-RuvB-RecU complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RecU to scan and cleave DNA to resolve the cruciform.","The molecular function of this protein is DNA binding.
It is involved in the replication of DNA and is responsible for breaking down the DNA at specific sites during the replication process.",No,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0016887; GO:0000400; GO:0009378,GO:0003677,GO:0003677; GO:0004519,GO:0003677,GO:0003677,GO:0003677,0.3686,0.3996,0.3686,0.3686,0.3686,5,0.3748,0.5483,yes
RUVB_MYCPB,A0A0H3DN66,Reference,Bacteria,307,"The RuvA-RuvB-RecU complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RecU to scan and cleave DNA to resolve the cruciform.","The RuvA-RuvB-RecU complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RecU to scan and cleave DNA to resolve the cruciform.",,,,,,,GO:0005524; GO:0016887; GO:0000400; GO:0009378,GO:0016887; GO:0005524; GO:0003677,GO:0016887; GO:0003678; GO:0005524,GO:0016887; GO:0003678,GO:0016887; GO:0003677; GO:0005524,GO:0016887; GO:0005524; GO:0003678,0.8123,0.8543,0.6681,0.8123,0.8543,5,0.8003,0.5483,yes
CPXA_KLEPH,A0A0H3GPN8,ESM2Text,Bacteria,453,"Histidine kinase member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating or, in some cases, repressing expression of downstream genes. Activates CpxR by phosphorylation.","Member of the two-component regulatory system CusS/CusR involved in response to copper stress, probably by activating CusR in response to copper. May activate CusR by phosphorylation.",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0000155,GO:0000155; GO:0005524,GO:0000155,GO:0000155,GO:0000155,GO:0000155,1.0,0.6842,0.6842,0.6842,0.6842,5,0.7474,0.5376,yes
CPXA_KLEPH,A0A0H3GPN8,Prot2Text,Bacteria,453,"Histidine kinase member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating or, in some cases, repressing expression of downstream genes. Activates CpxR by phosphorylation.",Member of the two-component regulatory system HprR/HprS that regulates the expression of the iron(2+)-saltsmanate reductase (FeR) operon under low-oxygen conditions. May function as a membrane-associated protein kinase that phosphorylates HprS in response to environmental signals leading to activation of specific gene promoters (Probable).,Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0000155,GO:0000155,GO:0000155,GO:0000155; GO:0004672,GO:0000155,GO:0000155; GO:0005524,0.6842,0.6842,0.6938,0.6842,1.0,5,0.7493,0.5376,yes
CPXA_KLEPH,A0A0H3GPN8,ProtT3,Bacteria,453,"Histidine kinase member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating or, in some cases, repressing expression of downstream genes. Activates CpxR by phosphorylation.",Member of the two-component regulatory system PhoP/PhoQ involved in the regulation of the Pho regulon. Phosphorylates PhoQ on a serine residue. Cell inner membrane; Multi-pass membrane protein,Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0000155,GO:0000155; GO:0005524,GO:0000155,GO:0000155,GO:0000155; GO:0004672; GO:0005524,GO:0004672; GO:0005524,1.0,0.6842,0.6842,0.943,0.8574,5,0.8338,0.5376,yes
CPXA_KLEPH,A0A0H3GPN8,ProtTale,Bacteria,453,"Histidine kinase member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating or, in some cases, repressing expression of downstream genes. Activates CpxR by phosphorylation.",Member of the two-component regulatory system PhoP/PhoQ. PhoQ acts as a membrane-associated protein kinase that phosphorylates PhoP in response to environmental signals.,Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0000155,GO:0000155; GO:0004672,GO:0000155; GO:0004672,GO:0000155; GO:0005524,GO:0000155; GO:0005524,GO:0000155; GO:0005524,0.6938,0.6938,1.0,1.0,1.0,5,0.8775,0.5376,yes
CPXA_KLEPH,A0A0H3GPN8,Protein2Text,Bacteria,453,"Histidine kinase member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating or, in some cases, repressing expression of downstream genes. Activates CpxR by phosphorylation.","This protein is a histidine kinase, which is a type of sensor kinase that plays a role in signal transduction. Specifically, it is a member of the two-component regulatory system (TCRS) that responds to environmental changes and regulates various cellular processes. As a histidine kinase, it is involved in the detection of external signals, such as environmental changes or nutrient availability, and transmits these signals to the downstream response regulator, which then modulates gene expression to adapt to the changing environment.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0000155,GO:0000155,GO:0000155,GO:0000155,GO:0004673,GO:0000155,0.6842,0.6842,0.6842,0.5713,0.6842,5,0.6616,0.5376,yes
CPXA_KLEPH,A0A0H3GPN8,Reference,Bacteria,453,"Histidine kinase member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating or, in some cases, repressing expression of downstream genes. Activates CpxR by phosphorylation.","Histidine kinase member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating or, in some cases, repressing expression of downstream genes. Activates CpxR by phosphorylation.",,,,,,,GO:0005524; GO:0000155,GO:0000155; GO:0005524,GO:0000155,GO:0000155; GO:0004673,GO:0000155; GO:0005524,GO:0000155,1.0,0.6842,0.7211,1.0,0.6842,5,0.8179,0.5376,yes
BDCA_BORBR,A0A0H3LVU7,ESM2Text,Bacteria,540,"Diguanylate cyclase involved in the regulation of swimming motility and biofilm formation. Probably catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules (Probable). Overexpression of bdcA increases intracellular c-di-GMP concentration, which correlates with inhibition of motility and enhanced biofilm formation. It impacts flagellar expression and host infection, likely via its diguanylate cyclase activity. Is required to effectively establish a respiratory tract infection in a mouse model.",Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0052621,GO:0052621,GO:0052621,GO:0052621,GO:0052929,GO:0052621,1.0,1.0,1.0,0.5121,1.0,5,0.9024,0.688,yes
BDCA_BORBR,A0A0H3LVU7,Prot2Text,Bacteria,540,"Diguanylate cyclase involved in the regulation of swimming motility and biofilm formation. Probably catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules (Probable). Overexpression of bdcA increases intracellular c-di-GMP concentration, which correlates with inhibition of motility and enhanced biofilm formation. It impacts flagellar expression and host infection, likely via its diguanylate cyclase activity. Is required to effectively establish a respiratory tract infection in a mouse model.","Polymerizes D(-)-3-hydroxybutyryl-CoA to create PHB which consists of thousands of hydroxybutyrate molecules linked end to end. PHB is a derivative of D-(+)-lactate, a hydroxybutyrate unit.",No,No,No,No,No,not-Yes,GO:0052621,GO:0047479,,GO:0016747,GO:0008818,GO:0016746,0.1998,,0.3987,0.5121,0.482,4,0.3982,0.688,yes
BDCA_BORBR,A0A0H3LVU7,ProtT3,Bacteria,540,"Diguanylate cyclase involved in the regulation of swimming motility and biofilm formation. Probably catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules (Probable). Overexpression of bdcA increases intracellular c-di-GMP concentration, which correlates with inhibition of motility and enhanced biofilm formation. It impacts flagellar expression and host infection, likely via its diguanylate cyclase activity. Is required to effectively establish a respiratory tract infection in a mouse model.",Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. Cell inner membrane; Multi-pass membrane protein,Yes,Yes,Yes,Yes,Yes,Yes,GO:0052621,GO:0052621; GO:0005525,GO:0052621,GO:0052621; GO:0005525,GO:0052621,GO:0052621,0.6852,1.0,0.6852,1.0,1.0,5,0.8741,0.688,yes
BDCA_BORBR,A0A0H3LVU7,ProtTale,Bacteria,540,"Diguanylate cyclase involved in the regulation of swimming motility and biofilm formation. Probably catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules (Probable). Overexpression of bdcA increases intracellular c-di-GMP concentration, which correlates with inhibition of motility and enhanced biofilm formation. It impacts flagellar expression and host infection, likely via its diguanylate cyclase activity. Is required to effectively establish a respiratory tract infection in a mouse model.",Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Involved in the regulation of biofilm formation.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0052621,GO:0052621,GO:0052621,GO:0052621,GO:0052621,GO:0052929,1.0,1.0,1.0,1.0,0.5121,5,0.9024,0.688,yes
BDCA_BORBR,A0A0H3LVU7,Protein2Text,Bacteria,540,"Diguanylate cyclase involved in the regulation of swimming motility and biofilm formation. Probably catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules (Probable). Overexpression of bdcA increases intracellular c-di-GMP concentration, which correlates with inhibition of motility and enhanced biofilm formation. It impacts flagellar expression and host infection, likely via its diguanylate cyclase activity. Is required to effectively establish a respiratory tract infection in a mouse model.","This protein is involved in the molecular function of being a sensor kinase, which is a type of protein that senses changes in the environment and responds by triggering a signaling cascade.",No,No,No,No,No,not-Yes,GO:0052621,GO:0000155,GO:0000155,GO:0000155,GO:0000155,GO:0000155,0.3221,0.3221,0.3221,0.3221,0.3221,5,0.3221,0.688,yes
BDCA_BORBR,A0A0H3LVU7,Reference,Bacteria,540,"Diguanylate cyclase involved in the regulation of swimming motility and biofilm formation. Probably catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules (Probable). Overexpression of bdcA increases intracellular c-di-GMP concentration, which correlates with inhibition of motility and enhanced biofilm formation. It impacts flagellar expression and host infection, likely via its diguanylate cyclase activity. Is required to effectively establish a respiratory tract infection in a mouse model.","Diguanylate cyclase involved in the regulation of swimming motility and biofilm formation. Probably catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules (Probable). Overexpression of bdcA increases intracellular c-di-GMP concentration, which correlates with inhibition of motility and enhanced biofilm formation. It impacts flagellar expression and host infection, likely via its diguanylate cyclase activity. Is required to effectively establish a respiratory tract infection in a mouse model.",,,,,,,GO:0052621,GO:0052621,GO:0052621,GO:0052621,GO:0052621,GO:0052621,1.0,1.0,1.0,1.0,1.0,5,1.0,0.688,yes
ERTB_PAES7,A0A0Q9KFZ4,ESM2Text,Bacteria,546,"Hydratase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the conversion of thiourocanic acid to 3-(5-oxo-2-thioxoimidazolidin-4- yl)propionic acid, the second step of the pathway. Cannot use urocanate.",Converts chlorophylls (Chl) into bacteriochlorophylls (BChl) by reducing ring B of the tetrapyrrole.,No,No,No,No,No,not-Yes,GO:0000166; GO:0016153,GO:0016491,GO:0016491,GO:0016491,GO:0016491,,0.293,0.293,0.293,0.293,,4,0.293,0.2432,no
ERTB_PAES7,A0A0Q9KFZ4,Prot2Text,Bacteria,546,"Hydratase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the conversion of thiourocanic acid to 3-(5-oxo-2-thioxoimidazolidin-4- yl)propionic acid, the second step of the pathway. Cannot use urocanate.","Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.",No,No,No,No,No,not-Yes,GO:0000166; GO:0016153,GO:0008964,GO:0008964,GO:0008964,GO:0004611,GO:0008948,0.2271,0.2271,0.2271,0.2604,0.2604,5,0.2404,0.2432,no
ERTB_PAES7,A0A0Q9KFZ4,ProtT3,Bacteria,546,"Hydratase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the conversion of thiourocanic acid to 3-(5-oxo-2-thioxoimidazolidin-4- yl)propionic acid, the second step of the pathway. Cannot use urocanate.",Catalyzes the conversion of urocanate to 4-imidazolone-5- propionate. Cytoplasm. Belongs to the urocanase family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0000166; GO:0016153,GO:0009099,GO:0004848,GO:0009099,GO:0004848,GO:0009099,0.0,0.1679,0.0,0.1679,0.0,5,0.0672,0.2432,no
ERTB_PAES7,A0A0Q9KFZ4,ProtTale,Bacteria,546,"Hydratase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the conversion of thiourocanic acid to 3-(5-oxo-2-thioxoimidazolidin-4- yl)propionic acid, the second step of the pathway. Cannot use urocanate.",Catalyzes the decarboxylation of 2-oxoglutarate to succinate semialdehyde.,No,No,No,No,No,not-Yes,GO:0000166; GO:0016153,GO:0004029,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.1467,0.3054,0.3054,0.3054,0.3054,5,0.2737,0.2432,no
ERTB_PAES7,A0A0Q9KFZ4,Protein2Text,Bacteria,546,"Hydratase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the conversion of thiourocanic acid to 3-(5-oxo-2-thioxoimidazolidin-4- yl)propionic acid, the second step of the pathway. Cannot use urocanate.","The molecular function of this protein is a decarboxylase, specifically a malate decarboxylase. It catalyzes the decarboxylation of malate to form pyruvate.",No,No,No,No,No,not-Yes,GO:0000166; GO:0016153,GO:0004471,GO:0016831,GO:0004470,GO:0004470,GO:0004470,0.1409,0.3054,0.1679,0.1679,0.1679,5,0.19,0.2432,no
ERTB_PAES7,A0A0Q9KFZ4,Reference,Bacteria,546,"Hydratase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the conversion of thiourocanic acid to 3-(5-oxo-2-thioxoimidazolidin-4- yl)propionic acid, the second step of the pathway. Cannot use urocanate.","Hydratase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the conversion of thiourocanic acid to 3-(5-oxo-2-thioxoimidazolidin-4- yl)propionic acid, the second step of the pathway. Cannot use urocanate.",,,,,,,GO:0000166; GO:0016153,GO:0016836,GO:0016836,GO:0016836,GO:0016836,GO:0016836,0.6117,0.6117,0.6117,0.6117,0.6117,5,0.6117,0.2432,no
IAD_TRASO,A0A100YXA1,ESM2Text,Bacteria,878,"Glycyl radical enzyme that catalyzes the terminal step of tryptophan fermentation, the decarboxylation of indoleacetate to form skatole, a malodorous compound that contributes to the characteristic smell of animal feces. No activity is detected with phenylacetate or p-hydroxyphenylacetate as substrates, indicating high substrate specificity.","Utilization of purines as secondary nitrogen sources, when primary sources are limiting.",No,No,Vague,No,No,not-Yes,GO:0016829; GO:0016740,,,,,,,,,,,0,,0.342,no
IAD_TRASO,A0A100YXA1,Prot2Text,Bacteria,878,"Glycyl radical enzyme that catalyzes the terminal step of tryptophan fermentation, the decarboxylation of indoleacetate to form skatole, a malodorous compound that contributes to the characteristic smell of animal feces. No activity is detected with phenylacetate or p-hydroxyphenylacetate as substrates, indicating high substrate specificity.","Involved in an anaerobic respiration pathway that converts the sulfonate isethionate (2-hydroxyethanesulfonate) to ammonia, acetate and sulfide. Catalyzes the radical-mediated C-S bond cleavage of isethionate (2-hydroxyethanesulfonate) to form sulfite and acetaldehyde.",No,No,Maybe,No,No,not-Yes,GO:0016829; GO:0016740,GO:0016829,,GO:0016829,GO:0016829,GO:0016829,0.8634,,0.8634,0.8634,0.8634,4,0.8634,0.342,no
IAD_TRASO,A0A100YXA1,ProtT3,Bacteria,878,"Glycyl radical enzyme that catalyzes the terminal step of tryptophan fermentation, the decarboxylation of indoleacetate to form skatole, a malodorous compound that contributes to the characteristic smell of animal feces. No activity is detected with phenylacetate or p-hydroxyphenylacetate as substrates, indicating high substrate specificity.",Catalyzes the conversion of glyoxylate to glyoxylate 5-semialdehyde. Belongs to the glycyl radical enzyme (GRE) family,Maybe,Vague,Vague,No,No,not-Yes,GO:0016829; GO:0016740,,,,,GO:0016829,,,,,0.8634,1,0.8634,0.342,no
IAD_TRASO,A0A100YXA1,ProtTale,Bacteria,878,"Glycyl radical enzyme that catalyzes the terminal step of tryptophan fermentation, the decarboxylation of indoleacetate to form skatole, a malodorous compound that contributes to the characteristic smell of animal feces. No activity is detected with phenylacetate or p-hydroxyphenylacetate as substrates, indicating high substrate specificity.","Glycyl-tRNA synthetase-alpha (GlyRS-alpha) is a catalytic subunit of the glycyl-tRNA synthetase complex (GlyRS). It catalyzes the formation of glycyl-tRNAGly from glycyl-tRNA(Gly) and ATP. In the presence of the beta subunit (GlyRS-beta), GlyRS can also catalyze the deacylation of methionyl-tRNA(Ile).",No,No,No,No,No,not-Yes,GO:0016829; GO:0016740,GO:0004820; GO:0005524,GO:0004820; GO:0005524,GO:0004820; GO:0005524,GO:0004820; GO:0005524,GO:0004820; GO:0005524,0.2341,0.2341,0.2341,0.2341,0.2341,5,0.2341,0.342,no
IAD_TRASO,A0A100YXA1,Protein2Text,Bacteria,878,"Glycyl radical enzyme that catalyzes the terminal step of tryptophan fermentation, the decarboxylation of indoleacetate to form skatole, a malodorous compound that contributes to the characteristic smell of animal feces. No activity is detected with phenylacetate or p-hydroxyphenylacetate as substrates, indicating high substrate specificity.","This protein is a reverse transcriptase, which means it is involved in the synthesis of DNA from RNA. Specifically, it is likely a viral reverse transcriptase, which is an enzyme that replicates the viral genome by converting its RNA into DNA.",No,No,No,No,No,not-Yes,GO:0016829; GO:0016740,GO:0003964,GO:0003964,GO:0003964,GO:0003964,GO:0003964,0.4053,0.4053,0.4053,0.4053,0.4053,5,0.4053,0.342,no
IAD_TRASO,A0A100YXA1,Reference,Bacteria,878,"Glycyl radical enzyme that catalyzes the terminal step of tryptophan fermentation, the decarboxylation of indoleacetate to form skatole, a malodorous compound that contributes to the characteristic smell of animal feces. No activity is detected with phenylacetate or p-hydroxyphenylacetate as substrates, indicating high substrate specificity.","Glycyl radical enzyme that catalyzes the terminal step of tryptophan fermentation, the decarboxylation of indoleacetate to form skatole, a malodorous compound that contributes to the characteristic smell of animal feces. No activity is detected with phenylacetate or p-hydroxyphenylacetate as substrates, indicating high substrate specificity.",,,,,,,GO:0016829; GO:0016740,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.5955,0.5955,0.5955,0.5955,0.5955,5,0.5955,0.342,no
AT2A_TOXGM,A0A125YIC2,ESM2Text,Eukaryota,1093,Involved in maintaining calcium homeostasis. Required the parasite motility and microneme secretion. Plays an important role during the lytic cycle.,This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to an endomembrane compartment.,Maybe,Yes,Maybe,Yes,Maybe,not-Yes,GO:0005524; GO:0016887; GO:0005388,GO:0005388; GO:0005524,GO:0005388,GO:0005388,GO:0005388,GO:0005388,0.8272,0.5446,0.5446,0.5446,0.5446,5,0.6011,0.5009,no
AT2A_TOXGM,A0A125YIC2,Prot2Text,Eukaryota,1093,Involved in maintaining calcium homeostasis. Required the parasite motility and microneme secretion. Plays an important role during the lytic cycle.,This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to an endomembrane compartment.,Maybe,Yes,Maybe,Yes,Maybe,not-Yes,GO:0005524; GO:0016887; GO:0005388,GO:0005388,GO:0005388,GO:0005388,GO:0005388,GO:0005388; GO:0005524,0.5446,0.5446,0.5446,0.5446,0.8272,5,0.6011,0.5009,no
AT2A_TOXGM,A0A125YIC2,ProtT3,Eukaryota,1093,Involved in maintaining calcium homeostasis. Required the parasite motility and microneme secretion. Plays an important role during the lytic cycle.,This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Endoplasmic reticulum membrane; Multi-pass membrane protein. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily,Maybe,Yes,Maybe,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0005388,GO:0005388; GO:0005524,GO:0005388,GO:0005388; GO:0005524,GO:0005388; GO:0005524,GO:0005388; GO:0005524,0.8272,0.5446,0.8272,0.8272,0.8272,5,0.7707,0.5009,no
AT2A_TOXGM,A0A125YIC2,ProtTale,Eukaryota,1093,Involved in maintaining calcium homeostasis. Required the parasite motility and microneme secretion. Plays an important role during the lytic cycle.,"This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium, providing the energy for active transport processes.",Maybe,Yes,Maybe,Yes,Maybe,not-Yes,GO:0005524; GO:0016887; GO:0005388,GO:0005391; GO:0005524,GO:0005391; GO:0005524; GO:0016887,GO:0005391; GO:0005524,GO:0005391; GO:0005524,GO:0005391; GO:0005524,0.7096,0.9048,0.7096,0.7096,0.7096,5,0.7486,0.5009,no
AT2A_TOXGM,A0A125YIC2,Protein2Text,Eukaryota,1093,Involved in maintaining calcium homeostasis. Required the parasite motility and microneme secretion. Plays an important role during the lytic cycle.,"The molecular function of this protein is a calcium-dependent ATPase, which is a type of ATPase enzyme that uses calcium ions (Ca2+) as a cofactor to catalyze the hydrolysis of ATP to ADP and inorganic phosphate. This protein is a calcium pump, which plays a crucial role in maintaining calcium homeostasis within cells by pumping calcium ions out of the cell or into organelles.",Maybe,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0005388,GO:0005388,GO:0005388,GO:0005388,GO:0005388,GO:0005388,0.5446,0.5446,0.5446,0.5446,0.5446,5,0.5446,0.5009,no
AT2A_TOXGM,A0A125YIC2,Reference,Eukaryota,1093,Involved in maintaining calcium homeostasis. Required the parasite motility and microneme secretion. Plays an important role during the lytic cycle.,Involved in maintaining calcium homeostasis. Required the parasite motility and microneme secretion. Plays an important role during the lytic cycle.,,,,,,,GO:0005524; GO:0016887; GO:0005388,,,,,,,,,,,0,,0.5009,no
RB11A_TOXGM,A0A125YY17,ESM2Text,Eukaryota,219,"Plays a role in protein trafficking; regulates transmembrane protein localization at the parasite plasma membrane. Promotes dense granule transport by mediating their anchoring along actin filaments. Promotes dense granule exocytosis. Required for inner membrane complex (IMC) maturation and cytokinesis completion, probably by mediating vesicular transport that delivers components of the proto- glideosome to the IMC and new plasma membrane to daughter cells. Promotes parasite invasion by regulating parasite motility and adhesion to host cells.",Intracellular vesicle trafficking and protein transport.,Vague,Vague,Vague,Maybe,Vague,not-Yes,GO:0005525; GO:0003924,,,,,,,,,,,0,,0.5201,no
RB11A_TOXGM,A0A125YY17,Prot2Text,Eukaryota,219,"Plays a role in protein trafficking; regulates transmembrane protein localization at the parasite plasma membrane. Promotes dense granule transport by mediating their anchoring along actin filaments. Promotes dense granule exocytosis. Required for inner membrane complex (IMC) maturation and cytokinesis completion, probably by mediating vesicular transport that delivers components of the proto- glideosome to the IMC and new plasma membrane to daughter cells. Promotes parasite invasion by regulating parasite motility and adhesion to host cells.",Intracellular vesicle trafficking and protein transport.,Vague,Vague,Vague,Maybe,Vague,not-Yes,GO:0005525; GO:0003924,,,,,,,,,,,0,,0.5201,no
RB11A_TOXGM,A0A125YY17,ProtT3,Eukaryota,219,"Plays a role in protein trafficking; regulates transmembrane protein localization at the parasite plasma membrane. Promotes dense granule transport by mediating their anchoring along actin filaments. Promotes dense granule exocytosis. Required for inner membrane complex (IMC) maturation and cytokinesis completion, probably by mediating vesicular transport that delivers components of the proto- glideosome to the IMC and new plasma membrane to daughter cells. Promotes parasite invasion by regulating parasite motility and adhesion to host cells.",Intracellular vesicle trafficking and protein transport. Cell membrane; Lipid-anchor; Cytoplasmic side. Belongs to the small GTPase superfamily. Rab family,Yes,Yes,Maybe,Maybe,Vague,not-Yes,GO:0005525; GO:0003924,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5201,no
RB11A_TOXGM,A0A125YY17,ProtTale,Eukaryota,219,"Plays a role in protein trafficking; regulates transmembrane protein localization at the parasite plasma membrane. Promotes dense granule transport by mediating their anchoring along actin filaments. Promotes dense granule exocytosis. Required for inner membrane complex (IMC) maturation and cytokinesis completion, probably by mediating vesicular transport that delivers components of the proto- glideosome to the IMC and new plasma membrane to daughter cells. Promotes parasite invasion by regulating parasite motility and adhesion to host cells.","The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion.",Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005525; GO:0003924,GO:0003924,GO:0003924,GO:0003924; GO:0005525,GO:0003924; GO:0005525,GO:0003924; GO:0005525,0.6817,0.6817,1.0,1.0,1.0,5,0.8727,0.5201,no
RB11A_TOXGM,A0A125YY17,Protein2Text,Eukaryota,219,"Plays a role in protein trafficking; regulates transmembrane protein localization at the parasite plasma membrane. Promotes dense granule transport by mediating their anchoring along actin filaments. Promotes dense granule exocytosis. Required for inner membrane complex (IMC) maturation and cytokinesis completion, probably by mediating vesicular transport that delivers components of the proto- glideosome to the IMC and new plasma membrane to daughter cells. Promotes parasite invasion by regulating parasite motility and adhesion to host cells.",The molecular function of this protein is associated with small GTPase activity.,Vague,Maybe,Vague,Maybe,Vague,not-Yes,GO:0005525; GO:0003924,GO:0003924; GO:0005525,GO:0003924,GO:0003924,GO:0003924,GO:0003924,1.0,0.6817,0.6817,0.6817,0.6817,5,0.7454,0.5201,no
RB11A_TOXGM,A0A125YY17,Reference,Eukaryota,219,"Plays a role in protein trafficking; regulates transmembrane protein localization at the parasite plasma membrane. Promotes dense granule transport by mediating their anchoring along actin filaments. Promotes dense granule exocytosis. Required for inner membrane complex (IMC) maturation and cytokinesis completion, probably by mediating vesicular transport that delivers components of the proto- glideosome to the IMC and new plasma membrane to daughter cells. Promotes parasite invasion by regulating parasite motility and adhesion to host cells.","Plays a role in protein trafficking; regulates transmembrane protein localization at the parasite plasma membrane. Promotes dense granule transport by mediating their anchoring along actin filaments. Promotes dense granule exocytosis. Required for inner membrane complex (IMC) maturation and cytokinesis completion, probably by mediating vesicular transport that delivers components of the proto- glideosome to the IMC and new plasma membrane to daughter cells. Promotes parasite invasion by regulating parasite motility and adhesion to host cells.",,,,,,,GO:0005525; GO:0003924,,,,,,,,,,,0,,0.5201,no
EPOXH_BOSS2,A0A126P745,ESM2Text,Bacteria,288,"Catalyzes the hydrolysis of various epoxides into diols. In vitro, shows the strongest activity toward the linear aliphatic epoxide compounds, since it shows strong activity toward (R)-epichlorohydrin, (S)-epichlorohydrin, and 1,2-epoxy-9-decene, but very weak activity toward (R)-styrene oxide, (S)-styrene oxide, and 3,4-epoxy-1- cyclohexene.","Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons.",No,No,No,No,No,not-Yes,GO:0004301,GO:0018786,GO:0016787,GO:0018786,GO:0018784,GO:0018786,0.3386,0.6019,0.3386,0.3386,0.3386,5,0.3913,0.181,no
EPOXH_BOSS2,A0A126P745,Prot2Text,Bacteria,288,"Catalyzes the hydrolysis of various epoxides into diols. In vitro, shows the strongest activity toward the linear aliphatic epoxide compounds, since it shows strong activity toward (R)-epichlorohydrin, (S)-epichlorohydrin, and 1,2-epoxy-9-decene, but very weak activity toward (R)-styrene oxide, (S)-styrene oxide, and 3,4-epoxy-1- cyclohexene.","Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Has a broad substrate specificity, which includes primary, secondary and cyclic dicarbonyl compounds. Shows good activity with 1,2-dibromoethane and 1,3-dibromoethane.",No,No,No,No,No,not-Yes,GO:0004301,GO:0018786,GO:0018786,GO:0018786,GO:0018784,GO:0018784,0.3386,0.3386,0.3386,0.3386,0.3386,5,0.3386,0.181,no
EPOXH_BOSS2,A0A126P745,ProtT3,Bacteria,288,"Catalyzes the hydrolysis of various epoxides into diols. In vitro, shows the strongest activity toward the linear aliphatic epoxide compounds, since it shows strong activity toward (R)-epichlorohydrin, (S)-epichlorohydrin, and 1,2-epoxy-9-decene, but very weak activity toward (R)-styrene oxide, (S)-styrene oxide, and 3,4-epoxy-1- cyclohexene.",Catalyzes the hydrolysis of epoxides to the corresponding alcohols. Belongs to the AB hydrolase superfamily. Epoxide hydrolase family,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004301,GO:0004301,GO:0004301,GO:0004301,GO:0004301,GO:0004301,1.0,1.0,1.0,1.0,1.0,5,1.0,0.181,no
EPOXH_BOSS2,A0A126P745,ProtTale,Bacteria,288,"Catalyzes the hydrolysis of various epoxides into diols. In vitro, shows the strongest activity toward the linear aliphatic epoxide compounds, since it shows strong activity toward (R)-epichlorohydrin, (S)-epichlorohydrin, and 1,2-epoxy-9-decene, but very weak activity toward (R)-styrene oxide, (S)-styrene oxide, and 3,4-epoxy-1- cyclohexene.","Catalyzes the hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Shows highest activity towards 4-chlorobenzoate (4-ClBA) and 4-bromobenzoate (4-BrBA), followed by 4-iodobenzoate (4-IBA), 3-chlorobenzoate (3-ClBA), 3-bromobenzoate (3-BrBA), 2-chlorobenzoate (2-ClBA), 2-brom",No,No,No,No,No,not-Yes,GO:0004301,GO:0016787,GO:0016787,GO:0018784,GO:0016787,GO:0016787,0.6019,0.6019,0.3386,0.6019,0.6019,5,0.5492,0.181,no
EPOXH_BOSS2,A0A126P745,Protein2Text,Bacteria,288,"Catalyzes the hydrolysis of various epoxides into diols. In vitro, shows the strongest activity toward the linear aliphatic epoxide compounds, since it shows strong activity toward (R)-epichlorohydrin, (S)-epichlorohydrin, and 1,2-epoxy-9-decene, but very weak activity toward (R)-styrene oxide, (S)-styrene oxide, and 3,4-epoxy-1- cyclohexene.","The molecular function of this protein is not explicitly stated in the provided information. However, based on its classification as a member of the short-chain dehydrogenase/reductase (SDR) family and its involvement in the degradation of certain compounds, it is likely that this protein catalyzes a redox reaction, possibly involved in the breakdown or modification of a specific substrate. 

More specifically, the protein is involved in the degradation of a certain compound, and it is likely that it catalyzes the oxidation or reduction of this compound as part of this process. However, without further information, the exact molecular function of this protein remains unclear.",Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0004301,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.3552,0.3552,0.3552,0.3552,0.3552,5,0.3552,0.181,no
EPOXH_BOSS2,A0A126P745,Reference,Bacteria,288,"Catalyzes the hydrolysis of various epoxides into diols. In vitro, shows the strongest activity toward the linear aliphatic epoxide compounds, since it shows strong activity toward (R)-epichlorohydrin, (S)-epichlorohydrin, and 1,2-epoxy-9-decene, but very weak activity toward (R)-styrene oxide, (S)-styrene oxide, and 3,4-epoxy-1- cyclohexene.","Catalyzes the hydrolysis of various epoxides into diols. In vitro, shows the strongest activity toward the linear aliphatic epoxide compounds, since it shows strong activity toward (R)-epichlorohydrin, (S)-epichlorohydrin, and 1,2-epoxy-9-decene, but very weak activity toward (R)-styrene oxide, (S)-styrene oxide, and 3,4-epoxy-1- cyclohexene.",,,,,,,GO:0004301,GO:0004301,GO:0004301,GO:0004301,GO:0004301,GO:0004301,1.0,1.0,1.0,1.0,1.0,5,1.0,0.181,no
PKS1_AURME,A0A172QE52,ESM2Text,Eukaryota,2190,"Highly-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of liamocins, glycolipids (also called heavy oils) composed of a single mannitol or arabitol headgroup linked to either three, four or even six 3,5-dihydroxydecanoic ester tail- groups. Within the pathway, PKS1 is responsible for biosynthesis of 3,5-dihydroxydecanoic acid from acetyl-CoA and malonyl- CoA. A phosphopantetheine transferase (PPTase) activates the HR-PKS. The esterase EST1 then catalyzes ester bond formation between 3,5-dihydroxydecanoic acid and mannitol (provided by the mannitol-1-phosphate 5-dehydrogenase and the NADP-dependent mannitol dehydrogenase) or arabinol (provided by the L- arabinitol 4-dehydrogenase).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcsC",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177,,,,,,,,,,,0,,0.2262,no
PKS1_AURME,A0A172QE52,Prot2Text,Eukaryota,2190,"Highly-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of liamocins, glycolipids (also called heavy oils) composed of a single mannitol or arabitol headgroup linked to either three, four or even six 3,5-dihydroxydecanoic ester tail- groups. Within the pathway, PKS1 is responsible for biosynthesis of 3,5-dihydroxydecanoic acid from acetyl-CoA and malonyl- CoA. A phosphopantetheine transferase (PPTase) activates the HR-PKS. The esterase EST1 then catalyzes ester bond formation between 3,5-dihydroxydecanoic acid and mannitol (provided by the mannitol-1-phosphate 5-dehydrogenase and the NADP-dependent mannitol dehydrogenase) or arabinol (provided by the L- arabinitol 4-dehydrogenase).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177,GO:0016747,,,GO:0016747,GO:0016746,0.6148,,,0.6148,0.5549,3,0.5948,0.2262,no
PKS1_AURME,A0A172QE52,ProtT3,Eukaryota,2190,"Highly-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of liamocins, glycolipids (also called heavy oils) composed of a single mannitol or arabitol headgroup linked to either three, four or even six 3,5-dihydroxydecanoic ester tail- groups. Within the pathway, PKS1 is responsible for biosynthesis of 3,5-dihydroxydecanoic acid from acetyl-CoA and malonyl- CoA. A phosphopantetheine transferase (PPTase) activates the HR-PKS. The esterase EST1 then catalyzes ester bond formation between 3,5-dihydroxydecanoic acid and mannitol (provided by the mannitol-1-phosphate 5-dehydrogenase and the NADP-dependent mannitol dehydrogenase) or arabinol (provided by the L- arabinitol 4-dehydrogenase).","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177,GO:0016746,GO:0016746,,GO:0016746,GO:0016747,0.5549,0.5549,,0.5549,0.6148,4,0.5699,0.2262,no
PKS1_AURME,A0A172QE52,ProtTale,Eukaryota,2190,"Highly-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of liamocins, glycolipids (also called heavy oils) composed of a single mannitol or arabitol headgroup linked to either three, four or even six 3,5-dihydroxydecanoic ester tail- groups. Within the pathway, PKS1 is responsible for biosynthesis of 3,5-dihydroxydecanoic acid from acetyl-CoA and malonyl- CoA. A phosphopantetheine transferase (PPTase) activates the HR-PKS. The esterase EST1 then catalyzes ester bond formation between 3,5-dihydroxydecanoic acid and mannitol (provided by the mannitol-1-phosphate 5-dehydrogenase and the NADP-dependent mannitol dehydrogenase) or arabinol (provided by the L- arabinitol 4-dehydrogenase).","Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the at",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177,GO:0016491,GO:0016757,,,GO:0016746,0.5675,0.4067,,,0.5549,3,0.5097,0.2262,no
PKS1_AURME,A0A172QE52,Protein2Text,Eukaryota,2190,"Highly-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of liamocins, glycolipids (also called heavy oils) composed of a single mannitol or arabitol headgroup linked to either three, four or even six 3,5-dihydroxydecanoic ester tail- groups. Within the pathway, PKS1 is responsible for biosynthesis of 3,5-dihydroxydecanoic acid from acetyl-CoA and malonyl- CoA. A phosphopantetheine transferase (PPTase) activates the HR-PKS. The esterase EST1 then catalyzes ester bond formation between 3,5-dihydroxydecanoic acid and mannitol (provided by the mannitol-1-phosphate 5-dehydrogenase and the NADP-dependent mannitol dehydrogenase) or arabinol (provided by the L- arabinitol 4-dehydrogenase).","This protein is involved in the biosynthesis of a type of molecule called a sesquiterpenoid, which is a class of compounds that are found in plants and have a variety of biological activities. The molecular function of this protein is to catalyze a reaction that is involved in the synthesis of this type of molecule.",No,No,No,No,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177,,,,GO:0010333,,,,,0.2383,,1,0.2383,0.2262,no
PKS1_AURME,A0A172QE52,Reference,Eukaryota,2190,"Highly-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of liamocins, glycolipids (also called heavy oils) composed of a single mannitol or arabitol headgroup linked to either three, four or even six 3,5-dihydroxydecanoic ester tail- groups. Within the pathway, PKS1 is responsible for biosynthesis of 3,5-dihydroxydecanoic acid from acetyl-CoA and malonyl- CoA. A phosphopantetheine transferase (PPTase) activates the HR-PKS. The esterase EST1 then catalyzes ester bond formation between 3,5-dihydroxydecanoic acid and mannitol (provided by the mannitol-1-phosphate 5-dehydrogenase and the NADP-dependent mannitol dehydrogenase) or arabinol (provided by the L- arabinitol 4-dehydrogenase).","Highly-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of liamocins, glycolipids (also called heavy oils) composed of a single mannitol or arabitol headgroup linked to either three, four or even six 3,5-dihydroxydecanoic ester tail- groups. Within the pathway, PKS1 is responsible for biosynthesis of 3,5-dihydroxydecanoic acid from acetyl-CoA and malonyl- CoA. A phosphopantetheine transferase (PPTase) activates the HR-PKS. The esterase EST1 then catalyzes ester bond formation between 3,5-dihydroxydecanoic acid and mannitol (provided by the mannitol-1-phosphate 5-dehydrogenase and the NADP-dependent mannitol dehydrogenase) or arabinol (provided by the L- arabinitol 4-dehydrogenase).",,,,,,,GO:0004315; GO:0004312; GO:0016491; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.5549,0.5549,0.5549,0.6148,0.5549,5,0.5669,0.2262,no
MKK1_CYTMA,A0A194VNL2,ESM2Text,Eukaryota,532,"Mitogen-activated protein kinase kinase, part of the mkh1- mkk1-spm1 MAPK cascade that regulates regulates vegetative growth, conidial formation, colony surface hydrophobicity, osmotic stress, cell wall integrity maintenance, carbon and nitrogen source utilization, chitin distribution, septa formation, and pathogenicity.",Regulates mkh1 and mkh2/mkh4 at the level of mRNA transport.,No,Maybe,No,No,Maybe,not-Yes,GO:0005524; GO:0004707,,,,,,,,,,,0,,0.7489,yes
MKK1_CYTMA,A0A194VNL2,Prot2Text,Eukaryota,532,"Mitogen-activated protein kinase kinase, part of the mkh1- mkk1-spm1 MAPK cascade that regulates regulates vegetative growth, conidial formation, colony surface hydrophobicity, osmotic stress, cell wall integrity maintenance, carbon and nitrogen source utilization, chitin distribution, septa formation, and pathogenicity.","Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. With MAP2K7/MKK7, is the one of the only known kinase to directly activate the p38 MAPK cascade and to be involved in p38-dependent apoptosis. MAP2K7/MKK7 is also the major MAP kinase in somatic cells and plays a critical role in the regulation of apoptosis through MAPK14 activation. The p38 MAPK cascade is a heterodimeric complex that binds to and phosphorylates the MAP2K1/MAP2K4/MAP2K6 part of the eIF-5A factor through its C-terminal domain. This leads to direct activation of the downstream MAP kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. The p38 MAPK cascade also functions downstream of MAPK1 in various processes such as regulation of neuronal polarity and synaptic plasticity, neuronal morphogenesis, cell survival, cell growth, proliferation, migration and apoptosis. The p38 MAPK cascade also plays a role in the regulation of neuronal morphology and neuromuscular junction development through regulation of",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0004707,GO:0004708,GO:0004708,GO:0004708,GO:0004708,GO:0004708; GO:0005524,0.4628,0.4628,0.4628,0.4628,0.8349,5,0.5372,0.7489,yes
MKK1_CYTMA,A0A194VNL2,ProtT3,Eukaryota,532,"Mitogen-activated protein kinase kinase, part of the mkh1- mkk1-spm1 MAPK cascade that regulates regulates vegetative growth, conidial formation, colony surface hydrophobicity, osmotic stress, cell wall integrity maintenance, carbon and nitrogen source utilization, chitin distribution, septa formation, and pathogenicity.","Mitogen-activated protein kinase (MAPK); part of the cell wall integrity (CWI) signaling pathway (By similarity). The CWI signaling pathway plays a key role in cell wall integrity, cell cycle progression, differentiation, virulence, and drug resistance (By similarity). The CWI pathway is activated when the cell wall is damaged or when the cell is subjected to stress conditions (By similarity). Mitogen-activated protein kinases (MAPKs) act as key regulators of the CWI signaling pathway (By similarity). The CWI pathway is activated when the cell wall",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004707,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004707; GO:0004674; GO:0005524,GO:0004707; GO:0004674; GO:0005524,GO:0004707; GO:0005524,0.9546,0.9546,0.9818,0.9818,1.0,5,0.9746,0.7489,yes
MKK1_CYTMA,A0A194VNL2,ProtTale,Eukaryota,532,"Mitogen-activated protein kinase kinase, part of the mkh1- mkk1-spm1 MAPK cascade that regulates regulates vegetative growth, conidial formation, colony surface hydrophobicity, osmotic stress, cell wall integrity maintenance, carbon and nitrogen source utilization, chitin distribution, septa formation, and pathogenicity.",Serine/threonine-protein kinase involved in the control of cell cycle progression. Phosphorylates the cyclin-dependent kinase CDC28.,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0005524; GO:0004707,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.9546,0.9546,0.6242,0.9546,0.9546,5,0.8885,0.7489,yes
MKK1_CYTMA,A0A194VNL2,Protein2Text,Eukaryota,532,"Mitogen-activated protein kinase kinase, part of the mkh1- mkk1-spm1 MAPK cascade that regulates regulates vegetative growth, conidial formation, colony surface hydrophobicity, osmotic stress, cell wall integrity maintenance, carbon and nitrogen source utilization, chitin distribution, septa formation, and pathogenicity.","This protein is a serine/threonine-protein kinase, which means it is involved in the transfer of phosphate groups to serine or threonine residues on other proteins, playing a crucial role in various cellular processes such as signal transduction, cell growth, and differentiation.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004707,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.6242,0.6242,0.6242,0.6242,0.6242,5,0.6242,0.7489,yes
MKK1_CYTMA,A0A194VNL2,Reference,Eukaryota,532,"Mitogen-activated protein kinase kinase, part of the mkh1- mkk1-spm1 MAPK cascade that regulates regulates vegetative growth, conidial formation, colony surface hydrophobicity, osmotic stress, cell wall integrity maintenance, carbon and nitrogen source utilization, chitin distribution, septa formation, and pathogenicity.","Mitogen-activated protein kinase kinase, part of the mkh1- mkk1-spm1 MAPK cascade that regulates regulates vegetative growth, conidial formation, colony surface hydrophobicity, osmotic stress, cell wall integrity maintenance, carbon and nitrogen source utilization, chitin distribution, septa formation, and pathogenicity.",,,,,,,GO:0005524; GO:0004707,GO:0004708; GO:0005524,GO:0004708; GO:0005524,GO:0004708; GO:0005524,GO:0004708; GO:0005524,GO:0004708; GO:0005524,0.8349,0.8349,0.8349,0.8349,0.8349,5,0.8349,0.7489,yes
VMS6_CYTMA,A0A194VR61,ESM2Text,Eukaryota,2991,"Highly reducing polyketide synthase; part of the SMGC4 gene cluster that mediates the biosynthesis of SDP1, a cyclo-dipeptide that induces cell death in apple stem tissue cultures, and suppresses the production of lignin, while it has no effect on apple leaves. SPD1 treatment inhibits apple chloroplast activity and auxin responses.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential tr",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0016491; GO:0031177; GO:0008270,,,,,,,,,,,0,,0.3136,no
VMS6_CYTMA,A0A194VR61,Prot2Text,Eukaryota,2991,"Highly reducing polyketide synthase; part of the SMGC4 gene cluster that mediates the biosynthesis of SDP1, a cyclo-dipeptide that induces cell death in apple stem tissue cultures, and suppresses the production of lignin, while it has no effect on apple leaves. SPD1 treatment inhibits apple chloroplast activity and auxin responses.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential tr",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0016491; GO:0031177; GO:0008270,GO:0016747,,,GO:0016747,GO:0016746,0.4596,,,0.4596,0.4294,3,0.4495,0.3136,no
VMS6_CYTMA,A0A194VR61,ProtT3,Eukaryota,2991,"Highly reducing polyketide synthase; part of the SMGC4 gene cluster that mediates the biosynthesis of SDP1, a cyclo-dipeptide that induces cell death in apple stem tissue cultures, and suppresses the production of lignin, while it has no effect on apple leaves. SPD1 treatment inhibits apple chloroplast activity and auxin responses.",Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0016491; GO:0031177; GO:0008270,GO:0016746,GO:0016746,,GO:0016746,GO:0016747,0.4294,0.4294,,0.4294,0.4596,4,0.437,0.3136,no
VMS6_CYTMA,A0A194VR61,ProtTale,Eukaryota,2991,"Highly reducing polyketide synthase; part of the SMGC4 gene cluster that mediates the biosynthesis of SDP1, a cyclo-dipeptide that induces cell death in apple stem tissue cultures, and suppresses the production of lignin, while it has no effect on apple leaves. SPD1 treatment inhibits apple chloroplast activity and auxin responses.","Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. Within the pathway, ptmG catalyzes the last step by condensing a C-12 acetyl-CoA starter unit with 7 malonyl-CoA units to produce the C20 penitrem B. The geranylgeranyl diphosphate (GGPP) synthase ptmG is proposed to catalyze the first step in penitrem biosynthesis via conversion of geranyl diphosphate (GPP) to farnesyl diphosphate (FPP). Condensation",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0016491; GO:0031177; GO:0008270,GO:0016491,GO:0016757,,,GO:0016746,0.5222,0.3306,,,0.4294,3,0.4274,0.3136,no
VMS6_CYTMA,A0A194VR61,Protein2Text,Eukaryota,2991,"Highly reducing polyketide synthase; part of the SMGC4 gene cluster that mediates the biosynthesis of SDP1, a cyclo-dipeptide that induces cell death in apple stem tissue cultures, and suppresses the production of lignin, while it has no effect on apple leaves. SPD1 treatment inhibits apple chloroplast activity and auxin responses.","This protein is a fatty acid synthase, which means it plays a role in the synthesis of fatty acids. More specifically, it is a key enzyme in the process of fatty acid biosynthesis, which is essential for the production of fatty acids in cells.",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0004312; GO:0016491; GO:0031177; GO:0008270,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.501,0.501,0.501,0.501,0.501,5,0.501,0.3136,no
VMS6_CYTMA,A0A194VR61,Reference,Eukaryota,2991,"Highly reducing polyketide synthase; part of the SMGC4 gene cluster that mediates the biosynthesis of SDP1, a cyclo-dipeptide that induces cell death in apple stem tissue cultures, and suppresses the production of lignin, while it has no effect on apple leaves. SPD1 treatment inhibits apple chloroplast activity and auxin responses.","Highly reducing polyketide synthase; part of the SMGC4 gene cluster that mediates the biosynthesis of SDP1, a cyclo-dipeptide that induces cell death in apple stem tissue cultures, and suppresses the production of lignin, while it has no effect on apple leaves. SPD1 treatment inhibits apple chloroplast activity and auxin responses.",,,,,,,GO:0004312; GO:0016491; GO:0031177; GO:0008270,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.4294,0.4294,0.4294,0.4596,0.4294,5,0.4354,0.3136,no
MKH1_CYTMA,A0A194W8T8,ESM2Text,Eukaryota,1849,"Mitogen-activated protein kinase kinase kinase, part of the mkh1-mkk1-spm1 MAPK cascade that regulates vegetative growth, conidial formation, colony surface hydrophobicity, osmotic stress, cell wall integrity maintenance, carbon and nitrogen source utilization, chitin distribution, septa formation, and pathogenicity.",Regulator of phosphate starvation response; activates the MAP kinase cascade and promotes cell survival upon phosphate starvation.,No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004707; GO:0004709,,,,,,,,,,,0,,0.5382,yes
MKH1_CYTMA,A0A194W8T8,Prot2Text,Eukaryota,1849,"Mitogen-activated protein kinase kinase kinase, part of the mkh1-mkk1-spm1 MAPK cascade that regulates vegetative growth, conidial formation, colony surface hydrophobicity, osmotic stress, cell wall integrity maintenance, carbon and nitrogen source utilization, chitin distribution, septa formation, and pathogenicity.",Promotes the exchange of Ras-bound GDP by GTP.,No,No,No,No,Maybe,not-Yes,GO:0005524; GO:0004707; GO:0004709,GO:0005085,GO:0005088,GO:0005088,GO:0005085,GO:0005085,0.0677,0.0677,0.0677,0.0677,0.0677,5,0.0677,0.5382,yes
MKH1_CYTMA,A0A194W8T8,ProtT3,Eukaryota,1849,"Mitogen-activated protein kinase kinase kinase, part of the mkh1-mkk1-spm1 MAPK cascade that regulates vegetative growth, conidial formation, colony surface hydrophobicity, osmotic stress, cell wall integrity maintenance, carbon and nitrogen source utilization, chitin distribution, septa formation, and pathogenicity.",Leucine-rich repeat protein; part of the gene cluster that mediates the biosynthesis of the host-selective toxins (HSTs) AAL-toxins responsible for Alternaria black spot of tomato disease by the tomato pathotype (Probable). Cell membrane; Single-pass type I membrane protein. Belongs to the STE20 family,No,Vague,Vague,No,Maybe,not-Yes,GO:0005524; GO:0004707; GO:0004709,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.9455,0.9455,0.9455,0.9455,0.9455,5,0.9455,0.5382,yes
MKH1_CYTMA,A0A194W8T8,ProtTale,Eukaryota,1849,"Mitogen-activated protein kinase kinase kinase, part of the mkh1-mkk1-spm1 MAPK cascade that regulates vegetative growth, conidial formation, colony surface hydrophobicity, osmotic stress, cell wall integrity maintenance, carbon and nitrogen source utilization, chitin distribution, septa formation, and pathogenicity.","Serine/threonine-protein kinase involved in cell cycle progression, morphogenesis and virulence.",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0005524; GO:0004707; GO:0004709,GO:0004674; GO:0005524,GO:0004674,GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.9455,0.6954,0.6954,0.9455,0.9455,5,0.8455,0.5382,yes
MKH1_CYTMA,A0A194W8T8,Protein2Text,Eukaryota,1849,"Mitogen-activated protein kinase kinase kinase, part of the mkh1-mkk1-spm1 MAPK cascade that regulates vegetative growth, conidial formation, colony surface hydrophobicity, osmotic stress, cell wall integrity maintenance, carbon and nitrogen source utilization, chitin distribution, septa formation, and pathogenicity.","This protein is a transcription factor, which means it plays a role in regulating the expression of genes by binding to specific DNA sequences. It is involved in the regulation of gene expression in response to environmental signals.",No,No,No,Vague,No,not-Yes,GO:0005524; GO:0004707; GO:0004709,GO:0003700; GO:0003677,GO:0003700,GO:0003700,GO:0003700,GO:0003700,0.1397,0.1138,0.1138,0.1138,0.1138,5,0.119,0.5382,yes
MKH1_CYTMA,A0A194W8T8,Reference,Eukaryota,1849,"Mitogen-activated protein kinase kinase kinase, part of the mkh1-mkk1-spm1 MAPK cascade that regulates vegetative growth, conidial formation, colony surface hydrophobicity, osmotic stress, cell wall integrity maintenance, carbon and nitrogen source utilization, chitin distribution, septa formation, and pathogenicity.","Mitogen-activated protein kinase kinase kinase, part of the mkh1-mkk1-spm1 MAPK cascade that regulates vegetative growth, conidial formation, colony surface hydrophobicity, osmotic stress, cell wall integrity maintenance, carbon and nitrogen source utilization, chitin distribution, septa formation, and pathogenicity.",,,,,,,GO:0005524; GO:0004707; GO:0004709,GO:0004709; GO:0005524,GO:0004709; GO:0005524,GO:0004709; GO:0005524,GO:0004709; GO:0005524,GO:0004709; GO:0005524,0.9633,0.9633,0.9633,0.9633,0.9633,5,0.9633,0.5382,yes
PENN_PENTH,A0A1B2CTC5,ESM2Text,Eukaryota,2797,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penigequinolones, potent insecticidal alkaloids that contain a highly modified 10-carbon prenyl group. The first stage is catalyzed by the nonribosomal peptide synthetase penN that condenses anthranilic acid and O-methyl-L- tyrosine to produce 4'-methoxycyclopeptin. 4'- methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase penM through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain. PenM also converts its first product methoxydehydrocyclopeptin to 4'-methoxycyclopenin. The following conversion of 4'methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase penL. 4'- methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase penI then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase penH to yield conjugated aryl diene. The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase penG to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain, or undergo cyclization to yield yaequinolones J1 and J2. The conversion of the styrenyl quinolone into the tetrahydrofuran-containing yaequinolone C is performed by the FAD- dependent monooxygenase penE and involves epoxidation of the terminal C7'-C8' olefin, followed by epoxide ring opening initiated by the C3' hydroxyl group. The predicted cysteine hydrolase penJ acts as an epoxide hydrolase that enhances the rate of the 5-exo-tet cyclization step, increasing the yield of yaequinolone C. PenF catalyzes the cationic rearrangement of the epoxide formed by penE (before ring opening to produce yaequinolone C) into yaequinolone D. Finally, the short-chain dehydrogenase/reductase (SDR)-like reductase penD, catalyzes both the dehydration of yaequinolone D and the reduction of the resulting oxonium to yield penigequinolone.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0047671; GO:0031177,,,,,,,,,,,0,,0.3685,no
PENN_PENTH,A0A1B2CTC5,Prot2Text,Eukaryota,2797,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penigequinolones, potent insecticidal alkaloids that contain a highly modified 10-carbon prenyl group. The first stage is catalyzed by the nonribosomal peptide synthetase penN that condenses anthranilic acid and O-methyl-L- tyrosine to produce 4'-methoxycyclopeptin. 4'- methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase penM through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain. PenM also converts its first product methoxydehydrocyclopeptin to 4'-methoxycyclopenin. The following conversion of 4'methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase penL. 4'- methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase penI then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase penH to yield conjugated aryl diene. The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase penG to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain, or undergo cyclization to yield yaequinolones J1 and J2. The conversion of the styrenyl quinolone into the tetrahydrofuran-containing yaequinolone C is performed by the FAD- dependent monooxygenase penE and involves epoxidation of the terminal C7'-C8' olefin, followed by epoxide ring opening initiated by the C3' hydroxyl group. The predicted cysteine hydrolase penJ acts as an epoxide hydrolase that enhances the rate of the 5-exo-tet cyclization step, increasing the yield of yaequinolone C. PenF catalyzes the cationic rearrangement of the epoxide formed by penE (before ring opening to produce yaequinolone C) into yaequinolone D. Finally, the short-chain dehydrogenase/reductase (SDR)-like reductase penD, catalyzes both the dehydration of yaequinolone D and the reduction of the resulting oxonium to yield penigequinolone.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0047671; GO:0031177,GO:0016874,,,GO:0016874,GO:0016874; GO:0005524,0.4436,,,0.4436,0.4803,3,0.4558,0.3685,no
PENN_PENTH,A0A1B2CTC5,ProtT3,Eukaryota,2797,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penigequinolones, potent insecticidal alkaloids that contain a highly modified 10-carbon prenyl group. The first stage is catalyzed by the nonribosomal peptide synthetase penN that condenses anthranilic acid and O-methyl-L- tyrosine to produce 4'-methoxycyclopeptin. 4'- methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase penM through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain. PenM also converts its first product methoxydehydrocyclopeptin to 4'-methoxycyclopenin. The following conversion of 4'methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase penL. 4'- methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase penI then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase penH to yield conjugated aryl diene. The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase penG to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain, or undergo cyclization to yield yaequinolones J1 and J2. The conversion of the styrenyl quinolone into the tetrahydrofuran-containing yaequinolone C is performed by the FAD- dependent monooxygenase penE and involves epoxidation of the terminal C7'-C8' olefin, followed by epoxide ring opening initiated by the C3' hydroxyl group. The predicted cysteine hydrolase penJ acts as an epoxide hydrolase that enhances the rate of the 5-exo-tet cyclization step, increasing the yield of yaequinolone C. PenF catalyzes the cationic rearrangement of the epoxide formed by penE (before ring opening to produce yaequinolone C) into yaequinolone D. Finally, the short-chain dehydrogenase/reductase (SDR)-like reductase penD, catalyzes both the dehydration of yaequinolone D and the reduction of the resulting oxonium to yield penigequinolone.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties . L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L- homoserine by cluster enzymes aspartate kinase FUB5 and homoserine O-acetyltransferase FUB6, as well as enzymes of the primary metabolism",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0047671; GO:0031177,GO:0016874; GO:0005524,GO:0016874,,GO:0016874; GO:0031177,GO:0016874; GO:0005524,0.4803,0.4436,,0.801,0.4803,4,0.5513,0.3685,no
PENN_PENTH,A0A1B2CTC5,ProtTale,Eukaryota,2797,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penigequinolones, potent insecticidal alkaloids that contain a highly modified 10-carbon prenyl group. The first stage is catalyzed by the nonribosomal peptide synthetase penN that condenses anthranilic acid and O-methyl-L- tyrosine to produce 4'-methoxycyclopeptin. 4'- methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase penM through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain. PenM also converts its first product methoxydehydrocyclopeptin to 4'-methoxycyclopenin. The following conversion of 4'methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase penL. 4'- methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase penI then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase penH to yield conjugated aryl diene. The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase penG to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain, or undergo cyclization to yield yaequinolones J1 and J2. The conversion of the styrenyl quinolone into the tetrahydrofuran-containing yaequinolone C is performed by the FAD- dependent monooxygenase penE and involves epoxidation of the terminal C7'-C8' olefin, followed by epoxide ring opening initiated by the C3' hydroxyl group. The predicted cysteine hydrolase penJ acts as an epoxide hydrolase that enhances the rate of the 5-exo-tet cyclization step, increasing the yield of yaequinolone C. PenF catalyzes the cationic rearrangement of the epoxide formed by penE (before ring opening to produce yaequinolone C) into yaequinolone D. Finally, the short-chain dehydrogenase/reductase (SDR)-like reductase penD, catalyzes both the dehydration of yaequinolone D and the reduction of the resulting oxonium to yield penigequinolone.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties. L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism. The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0047671; GO:0031177,GO:0016491,GO:0016874,,,GO:0016874,0.2791,0.4436,,,0.4436,3,0.3888,0.3685,no
PENN_PENTH,A0A1B2CTC5,Protein2Text,Eukaryota,2797,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penigequinolones, potent insecticidal alkaloids that contain a highly modified 10-carbon prenyl group. The first stage is catalyzed by the nonribosomal peptide synthetase penN that condenses anthranilic acid and O-methyl-L- tyrosine to produce 4'-methoxycyclopeptin. 4'- methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase penM through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain. PenM also converts its first product methoxydehydrocyclopeptin to 4'-methoxycyclopenin. The following conversion of 4'methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase penL. 4'- methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase penI then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase penH to yield conjugated aryl diene. The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase penG to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain, or undergo cyclization to yield yaequinolones J1 and J2. The conversion of the styrenyl quinolone into the tetrahydrofuran-containing yaequinolone C is performed by the FAD- dependent monooxygenase penE and involves epoxidation of the terminal C7'-C8' olefin, followed by epoxide ring opening initiated by the C3' hydroxyl group. The predicted cysteine hydrolase penJ acts as an epoxide hydrolase that enhances the rate of the 5-exo-tet cyclization step, increasing the yield of yaequinolone C. PenF catalyzes the cationic rearrangement of the epoxide formed by penE (before ring opening to produce yaequinolone C) into yaequinolone D. Finally, the short-chain dehydrogenase/reductase (SDR)-like reductase penD, catalyzes both the dehydration of yaequinolone D and the reduction of the resulting oxonium to yield penigequinolone.","The molecular function of the protein is not specified in the provided text, but based on the context, it is likely involved in a process related to cellular metabolism or energy production. The protein is associated with the ""glycolysis"" pathway, which is a critical process in cellular metabolism that converts glucose into energy in the form of ATP. Therefore, it is probable that the protein plays a role in glycolysis, but further information is needed to confirm its specific molecular function.",No,No,No,Vague,No,not-Yes,GO:0047671; GO:0031177,,,,,,,,,,,0,,0.3685,no
PENN_PENTH,A0A1B2CTC5,Reference,Eukaryota,2797,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penigequinolones, potent insecticidal alkaloids that contain a highly modified 10-carbon prenyl group. The first stage is catalyzed by the nonribosomal peptide synthetase penN that condenses anthranilic acid and O-methyl-L- tyrosine to produce 4'-methoxycyclopeptin. 4'- methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase penM through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain. PenM also converts its first product methoxydehydrocyclopeptin to 4'-methoxycyclopenin. The following conversion of 4'methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase penL. 4'- methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase penI then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase penH to yield conjugated aryl diene. The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase penG to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain, or undergo cyclization to yield yaequinolones J1 and J2. The conversion of the styrenyl quinolone into the tetrahydrofuran-containing yaequinolone C is performed by the FAD- dependent monooxygenase penE and involves epoxidation of the terminal C7'-C8' olefin, followed by epoxide ring opening initiated by the C3' hydroxyl group. The predicted cysteine hydrolase penJ acts as an epoxide hydrolase that enhances the rate of the 5-exo-tet cyclization step, increasing the yield of yaequinolone C. PenF catalyzes the cationic rearrangement of the epoxide formed by penE (before ring opening to produce yaequinolone C) into yaequinolone D. Finally, the short-chain dehydrogenase/reductase (SDR)-like reductase penD, catalyzes both the dehydration of yaequinolone D and the reduction of the resulting oxonium to yield penigequinolone.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penigequinolones, potent insecticidal alkaloids that contain a highly modified 10-carbon prenyl group. The first stage is catalyzed by the nonribosomal peptide synthetase penN that condenses anthranilic acid and O-methyl-L- tyrosine to produce 4'-methoxycyclopeptin. 4'- methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent dioxygenase penM through dehydrogenation to form a double bond between C-alpha and C-beta of the O-methyltyrosine side chain. PenM also converts its first product methoxydehydrocyclopeptin to 4'-methoxycyclopenin. The following conversion of 4'methoxycyclopenin into 4'-methoxyviridicatin is catalyzed by the cyclopenase penL. 4'- methoxyviridicatin is the precursor of quinolone natural products, and is further converted to quinolinone B (Probable). The prenyltransferase penI then catalyzes the canonical Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to yield dimethylallyl quinolone, which is subjected to FAD-dependent dehydrogenation by the FAD-linked oxidoreductase penH to yield conjugated aryl diene. The delta(3') double bond then serves as the site of the second alkylation with DMAPP catalyzed by the prenyltransferase penG to yield a carbenium ion intermediate, which can be attacked by H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain, or undergo cyclization to yield yaequinolones J1 and J2. The conversion of the styrenyl quinolone into the tetrahydrofuran-containing yaequinolone C is performed by the FAD- dependent monooxygenase penE and involves epoxidation of the terminal C7'-C8' olefin, followed by epoxide ring opening initiated by the C3' hydroxyl group. The predicted cysteine hydrolase penJ acts as an epoxide hydrolase that enhances the rate of the 5-exo-tet cyclization step, increasing the yield of yaequinolone C. PenF catalyzes the cationic rearrangement of the epoxide formed by penE (before ring opening to produce yaequinolone C) into yaequinolone D. Finally, the short-chain dehydrogenase/reductase (SDR)-like reductase penD, catalyzes both the dehydration of yaequinolone D and the reduction of the resulting oxonium to yield penigequinolone.",,,,,,,GO:0047671; GO:0031177,GO:0016874,GO:0016874,GO:0016874,GO:0016874,GO:0016874,0.4436,0.4436,0.4436,0.4436,0.4436,5,0.4436,0.3685,no
PFA1_THRS2,A0A1B3PEI6,ESM2Text,Eukaryota,2812,"Poliketide synthase-like protein; part of the polyunsaturated fatty acid synthase composed of the 3 PKS-like subunits A, B and C. While the saturated fatty acids (SFAs) in Thraustochytrium are produced by the conventional fatty acid synthase (FAS) pathway, polyunsaturated fatty acids (PUFAs) including docosahexeanoic acid (DHA) and docosapentaenoic acid (DPA) are synthesized via an anaerobical PKS pathway. PUFA synthase assimilates fatty acyl-CoA, the product of FAS, as the starter unit to synthesize DPA, and this starter unit may be butyryl-CoA, hexanoyl-CoA, or octanoyl-CoA. DPA and DHA biosynthesis seem to differ by the reduction at the N-3 position by PUFA synthase, not the extension of carbon chain. In DHA biosynthesis, PUFA synthase extends the fatty acyl chain from the methyl toward the carboxyl end, and the double bond is formed when the carbon chain is growing, instead of afterward. Therefore, PUFA synthase is unable to transform DPA to DHA, suggesting that DPA is not the precursor of DHA. Moreover, DPA molecule is partly extended by FAS KS domain, so DPA biosynthesis is less dependent on PUFA synthase KS domain than DHA.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the host-selective toxins (HSTs) AK-toxins responsible for Japanese pear black spot disease by the Japanese pear pathotype. AK-toxins are esters of 9,10-epoxy 8-hydroxy 9-methyldecatrienoic acid (EDA). On cellular level, AK-toxins affect plasma membrane of susceptible cells and cause a sudden increase in loss of K(+) after a few minutes of toxin treatment. The acyl-CoA ligase AKT1, the hydrolase AKT2 and enoyl-CoA hydratase AKT3 are all involved in the biosynthesis of the AK-, AF- and ACT-toxin common 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA) structural moiety. Part of a regulatory 3-step autophagy pathway for AK-toxin biosynthesis. On the pathway to the 3-step autophagy, AKT1, AKT2, and AKT3 catalyze the formation of the CCa-8,",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315,,,,,GO:0004312,,,,,0.7289,1,0.7289,0.2345,no
PFA1_THRS2,A0A1B3PEI6,Prot2Text,Eukaryota,2812,"Poliketide synthase-like protein; part of the polyunsaturated fatty acid synthase composed of the 3 PKS-like subunits A, B and C. While the saturated fatty acids (SFAs) in Thraustochytrium are produced by the conventional fatty acid synthase (FAS) pathway, polyunsaturated fatty acids (PUFAs) including docosahexeanoic acid (DHA) and docosapentaenoic acid (DPA) are synthesized via an anaerobical PKS pathway. PUFA synthase assimilates fatty acyl-CoA, the product of FAS, as the starter unit to synthesize DPA, and this starter unit may be butyryl-CoA, hexanoyl-CoA, or octanoyl-CoA. DPA and DHA biosynthesis seem to differ by the reduction at the N-3 position by PUFA synthase, not the extension of carbon chain. In DHA biosynthesis, PUFA synthase extends the fatty acyl chain from the methyl toward the carboxyl end, and the double bond is formed when the carbon chain is growing, instead of afterward. Therefore, PUFA synthase is unable to transform DPA to DHA, suggesting that DPA is not the precursor of DHA. Moreover, DPA molecule is partly extended by FAS KS domain, so DPA biosynthesis is less dependent on PUFA synthase KS domain than DHA.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the host-selective toxins (HSTs) AK-toxins responsible for Japanese pear black spot disease by the Japanese pear pathotype. AK-toxins are esters of 9,10-epoxy 8-hydroxy 9-methyldecatrienoic acid (EDA). On cellular level, AK-toxins affect plasma membrane of susceptible cells and cause a sudden increase in loss of K(+) after a few minutes of toxin treatment. The acyl-CoA ligase AKT1, the hydrolase AKT2 and enoyl-CoA hydratase AKT3 are all involved in the biosynthesis of the AK-, AF- and ACT-toxin common 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA) structural moiety. Part of a regulatory 3-step autophagy pathway for AK-toxin biosynthesis. On the pathway to the 3-step autophagy, AKT1, AKT2, and AKT3 catalyze the formation of the CCa-8,",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315,GO:0016747,,,,GO:0016746,0.8582,,,,0.729,2,0.7936,0.2345,no
PFA1_THRS2,A0A1B3PEI6,ProtT3,Eukaryota,2812,"Poliketide synthase-like protein; part of the polyunsaturated fatty acid synthase composed of the 3 PKS-like subunits A, B and C. While the saturated fatty acids (SFAs) in Thraustochytrium are produced by the conventional fatty acid synthase (FAS) pathway, polyunsaturated fatty acids (PUFAs) including docosahexeanoic acid (DHA) and docosapentaenoic acid (DPA) are synthesized via an anaerobical PKS pathway. PUFA synthase assimilates fatty acyl-CoA, the product of FAS, as the starter unit to synthesize DPA, and this starter unit may be butyryl-CoA, hexanoyl-CoA, or octanoyl-CoA. DPA and DHA biosynthesis seem to differ by the reduction at the N-3 position by PUFA synthase, not the extension of carbon chain. In DHA biosynthesis, PUFA synthase extends the fatty acyl chain from the methyl toward the carboxyl end, and the double bond is formed when the carbon chain is growing, instead of afterward. Therefore, PUFA synthase is unable to transform DPA to DHA, suggesting that DPA is not the precursor of DHA. Moreover, DPA molecule is partly extended by FAS KS domain, so DPA biosynthesis is less dependent on PUFA synthase KS domain than DHA.","Part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties",Maybe,Vague,Vague,Vague,Maybe,not-Yes,GO:0004315,,,,,,,,,,,0,,0.2345,no
PFA1_THRS2,A0A1B3PEI6,ProtTale,Eukaryota,2812,"Poliketide synthase-like protein; part of the polyunsaturated fatty acid synthase composed of the 3 PKS-like subunits A, B and C. While the saturated fatty acids (SFAs) in Thraustochytrium are produced by the conventional fatty acid synthase (FAS) pathway, polyunsaturated fatty acids (PUFAs) including docosahexeanoic acid (DHA) and docosapentaenoic acid (DPA) are synthesized via an anaerobical PKS pathway. PUFA synthase assimilates fatty acyl-CoA, the product of FAS, as the starter unit to synthesize DPA, and this starter unit may be butyryl-CoA, hexanoyl-CoA, or octanoyl-CoA. DPA and DHA biosynthesis seem to differ by the reduction at the N-3 position by PUFA synthase, not the extension of carbon chain. In DHA biosynthesis, PUFA synthase extends the fatty acyl chain from the methyl toward the carboxyl end, and the double bond is formed when the carbon chain is growing, instead of afterward. Therefore, PUFA synthase is unable to transform DPA to DHA, suggesting that DPA is not the precursor of DHA. Moreover, DPA molecule is partly extended by FAS KS domain, so DPA biosynthesis is less dependent on PUFA synthase KS domain than DHA.",Probable polyketide synthase.,Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315,,,,,,,,,,,0,,0.2345,no
PFA1_THRS2,A0A1B3PEI6,Protein2Text,Eukaryota,2812,"Poliketide synthase-like protein; part of the polyunsaturated fatty acid synthase composed of the 3 PKS-like subunits A, B and C. While the saturated fatty acids (SFAs) in Thraustochytrium are produced by the conventional fatty acid synthase (FAS) pathway, polyunsaturated fatty acids (PUFAs) including docosahexeanoic acid (DHA) and docosapentaenoic acid (DPA) are synthesized via an anaerobical PKS pathway. PUFA synthase assimilates fatty acyl-CoA, the product of FAS, as the starter unit to synthesize DPA, and this starter unit may be butyryl-CoA, hexanoyl-CoA, or octanoyl-CoA. DPA and DHA biosynthesis seem to differ by the reduction at the N-3 position by PUFA synthase, not the extension of carbon chain. In DHA biosynthesis, PUFA synthase extends the fatty acyl chain from the methyl toward the carboxyl end, and the double bond is formed when the carbon chain is growing, instead of afterward. Therefore, PUFA synthase is unable to transform DPA to DHA, suggesting that DPA is not the precursor of DHA. Moreover, DPA molecule is partly extended by FAS KS domain, so DPA biosynthesis is less dependent on PUFA synthase KS domain than DHA.",The molecular function of this protein is acyl transferase activity.,Maybe,Maybe,Vague,Vague,Maybe,not-Yes,GO:0004315,,,,GO:0016746,,,,,0.729,,1,0.729,0.2345,no
PFA1_THRS2,A0A1B3PEI6,Reference,Eukaryota,2812,"Poliketide synthase-like protein; part of the polyunsaturated fatty acid synthase composed of the 3 PKS-like subunits A, B and C. While the saturated fatty acids (SFAs) in Thraustochytrium are produced by the conventional fatty acid synthase (FAS) pathway, polyunsaturated fatty acids (PUFAs) including docosahexeanoic acid (DHA) and docosapentaenoic acid (DPA) are synthesized via an anaerobical PKS pathway. PUFA synthase assimilates fatty acyl-CoA, the product of FAS, as the starter unit to synthesize DPA, and this starter unit may be butyryl-CoA, hexanoyl-CoA, or octanoyl-CoA. DPA and DHA biosynthesis seem to differ by the reduction at the N-3 position by PUFA synthase, not the extension of carbon chain. In DHA biosynthesis, PUFA synthase extends the fatty acyl chain from the methyl toward the carboxyl end, and the double bond is formed when the carbon chain is growing, instead of afterward. Therefore, PUFA synthase is unable to transform DPA to DHA, suggesting that DPA is not the precursor of DHA. Moreover, DPA molecule is partly extended by FAS KS domain, so DPA biosynthesis is less dependent on PUFA synthase KS domain than DHA.","Poliketide synthase-like protein; part of the polyunsaturated fatty acid synthase composed of the 3 PKS-like subunits A, B and C. While the saturated fatty acids (SFAs) in Thraustochytrium are produced by the conventional fatty acid synthase (FAS) pathway, polyunsaturated fatty acids (PUFAs) including docosahexeanoic acid (DHA) and docosapentaenoic acid (DPA) are synthesized via an anaerobical PKS pathway. PUFA synthase assimilates fatty acyl-CoA, the product of FAS, as the starter unit to synthesize DPA, and this starter unit may be butyryl-CoA, hexanoyl-CoA, or octanoyl-CoA. DPA and DHA biosynthesis seem to differ by the reduction at the N-3 position by PUFA synthase, not the extension of carbon chain. In DHA biosynthesis, PUFA synthase extends the fatty acyl chain from the methyl toward the carboxyl end, and the double bond is formed when the carbon chain is growing, instead of afterward. Therefore, PUFA synthase is unable to transform DPA to DHA, suggesting that DPA is not the precursor of DHA. Moreover, DPA molecule is partly extended by FAS KS domain, so DPA biosynthesis is less dependent on PUFA synthase KS domain than DHA.",,,,,,,GO:0004315,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.729,0.729,0.729,0.8582,0.729,5,0.7548,0.2345,no
MSL2_CHICK,A0A1D5NVS8,ESM2Text,Eukaryota,579,"Non-catalytic component of the MSL histone acetyltransferase complex, a multiprotein complex that mediates the majority of histone H4 acetylation at 'Lys-16' (H4K16ac), an epigenetic mark that prevents chromatin compaction. The MSL complex is required for chromosome stability and genome integrity by maintaining homeostatic levels of H4K16ac. MSL2 plays a key role in gene dosage by ensuring biallelic expression of a subset of dosage-sensitive genes, including many haploinsufficient genes. Acts by promoting promoter-enhancer contacts, thereby preventing DNA methylation of one allele and creating a methylation-free environment for methylation-sensitive transcription factors such as SP1, KANSL1 and KANSL3. Also acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. Also involved in the DNA damage response by mediating ubiquitination of TP53/p53 and TP53BP1.","Component of the histone acetyltransferase C (HATC) complex, a multiprotein complex that mediates acetylation of nucleosomal histones H4 and H2A. This acetylation, mediated by HATC, is rate-limiting for heterochromatin assembly and is implicated in the regulation of histone H4 acetylation. The HATC complex is also involved in DNA repair: specifically recognizes and binds acetylated histones H2A and H2A, and promotes nucleosome sliding by stimulating RAD51 phosphorylation of histone H3, thereby promoting homologous recombination-mediated repair.",Maybe,Maybe,Yes,Yes,Maybe,not-Yes,GO:0141054; GO:0140585; GO:0061630; GO:0008270,GO:0004402,GO:0004402,GO:0004402,,,0.2319,0.2319,0.2319,,,3,0.2319,0.6556,yes
MSL2_CHICK,A0A1D5NVS8,Prot2Text,Eukaryota,579,"Non-catalytic component of the MSL histone acetyltransferase complex, a multiprotein complex that mediates the majority of histone H4 acetylation at 'Lys-16' (H4K16ac), an epigenetic mark that prevents chromatin compaction. The MSL complex is required for chromosome stability and genome integrity by maintaining homeostatic levels of H4K16ac. MSL2 plays a key role in gene dosage by ensuring biallelic expression of a subset of dosage-sensitive genes, including many haploinsufficient genes. Acts by promoting promoter-enhancer contacts, thereby preventing DNA methylation of one allele and creating a methylation-free environment for methylation-sensitive transcription factors such as SP1, KANSL1 and KANSL3. Also acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. Also involved in the DNA damage response by mediating ubiquitination of TP53/p53 and TP53BP1.",Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at lysine 16 which is implicated in the formation of higher-order chromatin structure.,Maybe,Maybe,Yes,Yes,Maybe,not-Yes,GO:0141054; GO:0140585; GO:0061630; GO:0008270,GO:0004402,GO:0004402,GO:0004402,GO:0004402,GO:0004402,0.2319,0.2319,0.2319,0.2319,0.2319,5,0.2319,0.6556,yes
MSL2_CHICK,A0A1D5NVS8,ProtT3,Eukaryota,579,"Non-catalytic component of the MSL histone acetyltransferase complex, a multiprotein complex that mediates the majority of histone H4 acetylation at 'Lys-16' (H4K16ac), an epigenetic mark that prevents chromatin compaction. The MSL complex is required for chromosome stability and genome integrity by maintaining homeostatic levels of H4K16ac. MSL2 plays a key role in gene dosage by ensuring biallelic expression of a subset of dosage-sensitive genes, including many haploinsufficient genes. Acts by promoting promoter-enhancer contacts, thereby preventing DNA methylation of one allele and creating a methylation-free environment for methylation-sensitive transcription factors such as SP1, KANSL1 and KANSL3. Also acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. Also involved in the DNA damage response by mediating ubiquitination of TP53/p53 and TP53BP1.","E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H2A at 'Lys-120' (H2AK120ub1), a specific tag for epigenetic transcriptional activation. H2AK120ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formation. H2AK120ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formation. Nucleus",Maybe,Maybe,No,No,No,not-Yes,GO:0141054; GO:0140585; GO:0061630; GO:0008270,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.5834,0.5834,0.5834,0.5834,0.5834,5,0.5834,0.6556,yes
MSL2_CHICK,A0A1D5NVS8,ProtTale,Eukaryota,579,"Non-catalytic component of the MSL histone acetyltransferase complex, a multiprotein complex that mediates the majority of histone H4 acetylation at 'Lys-16' (H4K16ac), an epigenetic mark that prevents chromatin compaction. The MSL complex is required for chromosome stability and genome integrity by maintaining homeostatic levels of H4K16ac. MSL2 plays a key role in gene dosage by ensuring biallelic expression of a subset of dosage-sensitive genes, including many haploinsufficient genes. Acts by promoting promoter-enhancer contacts, thereby preventing DNA methylation of one allele and creating a methylation-free environment for methylation-sensitive transcription factors such as SP1, KANSL1 and KANSL3. Also acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. Also involved in the DNA damage response by mediating ubiquitination of TP53/p53 and TP53BP1.",Transcriptional activator. Binds to the 5'-TTATC[CA]-3' consensus sequence.,No,No,No,No,No,not-Yes,GO:0141054; GO:0140585; GO:0061630; GO:0008270,GO:0003700; GO:0003677,GO:0003700,GO:0003700; GO:0043565,GO:0003700; GO:0003677,GO:0003700; GO:0003677,0.2652,0.1205,0.2307,0.2652,0.2652,5,0.2294,0.6556,yes
MSL2_CHICK,A0A1D5NVS8,Protein2Text,Eukaryota,579,"Non-catalytic component of the MSL histone acetyltransferase complex, a multiprotein complex that mediates the majority of histone H4 acetylation at 'Lys-16' (H4K16ac), an epigenetic mark that prevents chromatin compaction. The MSL complex is required for chromosome stability and genome integrity by maintaining homeostatic levels of H4K16ac. MSL2 plays a key role in gene dosage by ensuring biallelic expression of a subset of dosage-sensitive genes, including many haploinsufficient genes. Acts by promoting promoter-enhancer contacts, thereby preventing DNA methylation of one allele and creating a methylation-free environment for methylation-sensitive transcription factors such as SP1, KANSL1 and KANSL3. Also acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. Also involved in the DNA damage response by mediating ubiquitination of TP53/p53 and TP53BP1.","The molecular function of this protein is as a transcription regulator. It is involved in regulating gene expression, specifically in the transcription process.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0141054; GO:0140585; GO:0061630; GO:0008270,GO:0003700,GO:0003700,GO:0003700,GO:0140110,GO:0003700,0.1205,0.1205,0.1205,0.1543,0.1205,5,0.1273,0.6556,yes
MSL2_CHICK,A0A1D5NVS8,Reference,Eukaryota,579,"Non-catalytic component of the MSL histone acetyltransferase complex, a multiprotein complex that mediates the majority of histone H4 acetylation at 'Lys-16' (H4K16ac), an epigenetic mark that prevents chromatin compaction. The MSL complex is required for chromosome stability and genome integrity by maintaining homeostatic levels of H4K16ac. MSL2 plays a key role in gene dosage by ensuring biallelic expression of a subset of dosage-sensitive genes, including many haploinsufficient genes. Acts by promoting promoter-enhancer contacts, thereby preventing DNA methylation of one allele and creating a methylation-free environment for methylation-sensitive transcription factors such as SP1, KANSL1 and KANSL3. Also acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. Also involved in the DNA damage response by mediating ubiquitination of TP53/p53 and TP53BP1.","Non-catalytic component of the MSL histone acetyltransferase complex, a multiprotein complex that mediates the majority of histone H4 acetylation at 'Lys-16' (H4K16ac), an epigenetic mark that prevents chromatin compaction. The MSL complex is required for chromosome stability and genome integrity by maintaining homeostatic levels of H4K16ac. MSL2 plays a key role in gene dosage by ensuring biallelic expression of a subset of dosage-sensitive genes, including many haploinsufficient genes. Acts by promoting promoter-enhancer contacts, thereby preventing DNA methylation of one allele and creating a methylation-free environment for methylation-sensitive transcription factors such as SP1, KANSL1 and KANSL3. Also acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. Also involved in the DNA damage response by mediating ubiquitination of TP53/p53 and TP53BP1.",,,,,,,GO:0141054; GO:0140585; GO:0061630; GO:0008270,GO:0004842,GO:0061630,GO:0004842,GO:0004842,GO:0061630,0.4981,0.5834,0.4981,0.4981,0.5834,5,0.5322,0.6556,yes
NDUS3_CANAL,A0A1D8PJ73,ESM2Text,Eukaryota,279,"Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Plays a role in cell wall integrity and is involved in osmotic and oxidative resistance, yeast to hypha transition and the ability to damage and invade oral epithelial cells.",Core component of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008137; GO:0016651,GO:0008137,GO:0008137,GO:0008137,GO:0008137,GO:0008137,0.7011,0.7011,0.7011,0.7011,0.7011,5,0.7011,0.3153,no
NDUS3_CANAL,A0A1D8PJ73,Prot2Text,Eukaryota,279,"Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Plays a role in cell wall integrity and is involved in osmotic and oxidative resistance, yeast to hypha transition and the ability to damage and invade oral epithelial cells.",Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008137; GO:0016651,GO:0008137,GO:0008137,GO:0008137,GO:0008137,GO:0008137,0.7011,0.7011,0.7011,0.7011,0.7011,5,0.7011,0.3153,no
NDUS3_CANAL,A0A1D8PJ73,ProtT3,Eukaryota,279,"Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Plays a role in cell wall integrity and is involved in osmotic and oxidative resistance, yeast to hypha transition and the ability to damage and invade oral epithelial cells.",Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. Belongs to the complex I 30 kDa subunit family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008137; GO:0016651,GO:0008137,GO:0008137,GO:0008137,GO:0008137; GO:0051287,GO:0008137,0.7011,0.7011,0.7011,0.5512,0.7011,5,0.6711,0.3153,no
NDUS3_CANAL,A0A1D8PJ73,ProtTale,Eukaryota,279,"Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Plays a role in cell wall integrity and is involved in osmotic and oxidative resistance, yeast to hypha transition and the ability to damage and invade oral epithelial cells.","Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part",No,No,No,No,No,not-Yes,GO:0008137; GO:0016651,GO:0046933; GO:0046961,GO:0046933; GO:0046961,GO:0046933,GO:0046933,GO:0046933; GO:0005524,0.4495,0.4495,0.3344,0.3344,0.2692,5,0.3674,0.3153,no
NDUS3_CANAL,A0A1D8PJ73,Protein2Text,Eukaryota,279,"Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Plays a role in cell wall integrity and is involved in osmotic and oxidative resistance, yeast to hypha transition and the ability to damage and invade oral epithelial cells.","The molecular function of this protein is not explicitly stated in the given text. However, based on its name, it can be inferred that it is involved in a process related to mitochondrial activity, possibly in the electron transport chain or oxidative phosphorylation. This protein is likely a component of a larger complex or enzyme that plays a role in energy production within mitochondria.",Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0008137; GO:0016651,,,,,,,,,,,0,,0.3153,no
NDUS3_CANAL,A0A1D8PJ73,Reference,Eukaryota,279,"Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Plays a role in cell wall integrity and is involved in osmotic and oxidative resistance, yeast to hypha transition and the ability to damage and invade oral epithelial cells.","Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Plays a role in cell wall integrity and is involved in osmotic and oxidative resistance, yeast to hypha transition and the ability to damage and invade oral epithelial cells.",,,,,,,GO:0008137; GO:0016651,GO:0008137,GO:0008137,GO:0008137,GO:0008137,GO:0008137,0.7011,0.7011,0.7011,0.7011,0.7011,5,0.7011,0.3153,no
NDUS1_CANAL,A0A1D8PU51,ESM2Text,Eukaryota,720,"Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for catalysing the entry and efficient transfer of electrons within complex I. Plays a key role in the assembly and stability of complex I and participates in the association of complex I with ubiquinol-cytochrome reductase complex (Complex III) to form supercomplexes. Plays a role in cell wall integrity and is involved in osmotic and oxidative resistance, yeast to hypha transition, and the ability to damage and invade oral epithelial cells.","Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for catalysing the entry and efficient transfer of electrons within complex I.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0051539; GO:0046872; GO:0008137; GO:0016651,GO:0008137,GO:0008137,GO:0008137,GO:0008137,GO:0008137,0.4532,0.4532,0.4532,0.4532,0.4532,5,0.4532,0.3775,no
NDUS1_CANAL,A0A1D8PU51,Prot2Text,Eukaryota,720,"Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for catalysing the entry and efficient transfer of electrons within complex I. Plays a key role in the assembly and stability of complex I and participates in the association of complex I with ubiquinol-cytochrome reductase complex (Complex III) to form supercomplexes. Plays a role in cell wall integrity and is involved in osmotic and oxidative resistance, yeast to hypha transition, and the ability to damage and invade oral epithelial cells.","Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for catalysing the entry and efficient transfer of electrons within complex I. Plays a key role in the assembly and stability of complex I and participates in the association of complex I with ubiquinol-cytochrome reductase complex (Complex III) to form supercomplexes.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0051539; GO:0046872; GO:0008137; GO:0016651,GO:0008137,GO:0008137,GO:0008137,GO:0008137,GO:0008137,0.4532,0.4532,0.4532,0.4532,0.4532,5,0.4532,0.3775,no
NDUS1_CANAL,A0A1D8PU51,ProtT3,Eukaryota,720,"Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for catalysing the entry and efficient transfer of electrons within complex I. Plays a key role in the assembly and stability of complex I and participates in the association of complex I with ubiquinol-cytochrome reductase complex (Complex III) to form supercomplexes. Plays a role in cell wall integrity and is involved in osmotic and oxidative resistance, yeast to hypha transition, and the ability to damage and invade oral epithelial cells.",Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. Belongs to the complex I 75 kDa subunit family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0051539; GO:0046872; GO:0008137; GO:0016651,GO:0008137,GO:0008137,GO:0008137,GO:0008137; GO:0051287,GO:0008137,0.4532,0.4532,0.4532,0.4799,0.4532,5,0.4585,0.3775,no
NDUS1_CANAL,A0A1D8PU51,ProtTale,Eukaryota,720,"Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for catalysing the entry and efficient transfer of electrons within complex I. Plays a key role in the assembly and stability of complex I and participates in the association of complex I with ubiquinol-cytochrome reductase complex (Complex III) to form supercomplexes. Plays a role in cell wall integrity and is involved in osmotic and oxidative resistance, yeast to hypha transition, and the ability to damage and invade oral epithelial cells.","NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0051539; GO:0046872; GO:0008137; GO:0016651,GO:0008137; GO:0016655,GO:0008137; GO:0016491,GO:0008137,GO:0008137,GO:0008137,0.6487,0.6575,0.4532,0.4532,0.4532,5,0.5332,0.3775,no
NDUS1_CANAL,A0A1D8PU51,Protein2Text,Eukaryota,720,"Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for catalysing the entry and efficient transfer of electrons within complex I. Plays a key role in the assembly and stability of complex I and participates in the association of complex I with ubiquinol-cytochrome reductase complex (Complex III) to form supercomplexes. Plays a role in cell wall integrity and is involved in osmotic and oxidative resistance, yeast to hypha transition, and the ability to damage and invade oral epithelial cells.","The molecular function of this protein is an electron transfer flavoprotein. It is a subunit of a flavoprotein involved in energy metabolism and the catabolism of several amino acids. The electron transfer flavoprotein is a subunit of the electron transfer flavoprotein-ubiquinone oxidoreductase (ETF:QO) complex, which is involved in the transfer of electrons from various substrates to the ubiquinone pool.",No,Maybe,No,No,Maybe,not-Yes,GO:0051539; GO:0046872; GO:0008137; GO:0016651,GO:0009055,GO:0009055,GO:0009055,GO:0009055,GO:0009055,0.2671,0.2671,0.2671,0.2671,0.2671,5,0.2671,0.3775,no
NDUS1_CANAL,A0A1D8PU51,Reference,Eukaryota,720,"Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for catalysing the entry and efficient transfer of electrons within complex I. Plays a key role in the assembly and stability of complex I and participates in the association of complex I with ubiquinol-cytochrome reductase complex (Complex III) to form supercomplexes. Plays a role in cell wall integrity and is involved in osmotic and oxidative resistance, yeast to hypha transition, and the ability to damage and invade oral epithelial cells.","Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for catalysing the entry and efficient transfer of electrons within complex I. Plays a key role in the assembly and stability of complex I and participates in the association of complex I with ubiquinol-cytochrome reductase complex (Complex III) to form supercomplexes. Plays a role in cell wall integrity and is involved in osmotic and oxidative resistance, yeast to hypha transition, and the ability to damage and invade oral epithelial cells.",,,,,,,GO:0051539; GO:0046872; GO:0008137; GO:0016651,GO:0008137,GO:0008137,GO:0008137,GO:0008137,GO:0008137,0.4532,0.4532,0.4532,0.4532,0.4532,5,0.4532,0.3775,no
SNF1_SCLS1,A0A1D9QMS2,ESM2Text,Eukaryota,765,"Carbon catabolite-derepressing protein kinase which influences the expression of cell wall-degrading enzymes (CWDEs) such as cellulases and polygalacturonases, thus enabling a suitable cellular response for plant tissue destruction and nutrition utilization and contributing to the growth and pathogenicity.",Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. Plays a role in the regulation of filamentous growth.,Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.964,0.7186,0.7186,0.7186,0.7186,5,0.7677,0.5316,no
SNF1_SCLS1,A0A1D9QMS2,Prot2Text,Eukaryota,765,"Carbon catabolite-derepressing protein kinase which influences the expression of cell wall-degrading enzymes (CWDEs) such as cellulases and polygalacturonases, thus enabling a suitable cellular response for plant tissue destruction and nutrition utilization and contributing to the growth and pathogenicity.","Serine/threonine-protein kinase involved in the regulation of actin cytoskeleton organization and endocytosis. Phosphorylates the CDC25, CDC25L, MAPT/TAU, RHO5, RHO6 and SNCA1. Involved in regulation of actin cytoskeleton organization during cell cycle and in endocytosis. Phosphorylates the CDC25L MAPT/TAU actin-binding protein. Required for the regulation of actin polymerization and endocytosis. Phosphorylates the CDC25L MAPT/TAU actin-binding protein. Required for the regulation of cell cycle progression.",Maybe,Yes,Maybe,Maybe,No,not-Yes,GO:0005524; GO:0106310; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674; GO:0005524,0.7186,0.7186,0.7186,0.7186,0.964,5,0.7677,0.5316,no
SNF1_SCLS1,A0A1D9QMS2,ProtT3,Eukaryota,765,"Carbon catabolite-derepressing protein kinase which influences the expression of cell wall-degrading enzymes (CWDEs) such as cellulases and polygalacturonases, thus enabling a suitable cellular response for plant tissue destruction and nutrition utilization and contributing to the growth and pathogenicity.","Catalytic subunit of the SNF1 kinase complex, which plays a key role in the regulation of cellular energy homeostasis by phosphorylating and inactivating the energy sensor protein SNF1. The SNF1 kinase complex phosphorylates and inactivates the energy sensor protein SNF1, which in turn activates the energy-producing catabolic pathways and inhibits the energy-consuming anabolic pathways (By similarity). Cytoplasm Nucleus. Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.964,0.964,0.964,0.964,0.964,5,0.964,0.5316,no
SNF1_SCLS1,A0A1D9QMS2,ProtTale,Eukaryota,765,"Carbon catabolite-derepressing protein kinase which influences the expression of cell wall-degrading enzymes (CWDEs) such as cellulases and polygalacturonases, thus enabling a suitable cellular response for plant tissue destruction and nutrition utilization and contributing to the growth and pathogenicity.",Serine/threonine protein kinase required for cell wall integrity.,Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674,GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.964,0.7186,0.7186,0.964,0.964,5,0.8658,0.5316,no
SNF1_SCLS1,A0A1D9QMS2,Protein2Text,Eukaryota,765,"Carbon catabolite-derepressing protein kinase which influences the expression of cell wall-degrading enzymes (CWDEs) such as cellulases and polygalacturonases, thus enabling a suitable cellular response for plant tissue destruction and nutrition utilization and contributing to the growth and pathogenicity.","The molecular function of this protein is a serine/threonine-protein kinase. It is a type of protein kinase that plays a role in signal transduction pathways, specifically in the phosphorylation of serine and threonine residues on target proteins. This protein is involved in various cellular processes, including cell growth, differentiation, and survival. It is also known to interact with other proteins, such as MAPKs, and regulate their activity.",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0106310; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.7186,0.7186,0.7186,0.7186,0.7186,5,0.7186,0.5316,no
SNF1_SCLS1,A0A1D9QMS2,Reference,Eukaryota,765,"Carbon catabolite-derepressing protein kinase which influences the expression of cell wall-degrading enzymes (CWDEs) such as cellulases and polygalacturonases, thus enabling a suitable cellular response for plant tissue destruction and nutrition utilization and contributing to the growth and pathogenicity.","Carbon catabolite-derepressing protein kinase which influences the expression of cell wall-degrading enzymes (CWDEs) such as cellulases and polygalacturonases, thus enabling a suitable cellular response for plant tissue destruction and nutrition utilization and contributing to the growth and pathogenicity.",,,,,,,GO:0005524; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.964,0.964,0.964,0.964,0.964,5,0.964,0.5316,no
BILC_COLS4,A0A1I1NU16,ESM2Text,Bacteria,173,"Component of the Bil (bacterial ISG15-like) antiviral defense system, composed of BilA, BilB, BilC and BilD. The Bil system specifically conjugates a ubiquitin-like moiety (bilA) to the bacteriophage central tail fiber (CTF, or tip attachment protein J) via reactions involving E1 (bilD) and E2 (bilB). Modifies CTF of phage SECphi27 and SECphi4, which probably interferes with assembly of the phage tail. Also modifies T5 baseplate hub protein pb3 (gene D16), but not gp27 of phage T6 (Bil defends against T6). BilC is a probable metalloprotease that may cleave non-specifically conjugated targets (Probable). Bil-encoding bacteria produce mostly defective phage SECphi27, many of which have phage assembly defects, including no tails. SECphi27 phage progeny produced in E.coli with the Bil system inject less DNA into naive host cells, maybe because the phage are less able to adsorb and inject their DNA into host cells.",Metalloprotease that catalyzes the hydrolysis of the thiocarboxylated and butyrylated covalent proteins to yield their corresponding (sub-)O-ribose.,Maybe,Maybe,No,No,No,not-Yes,GO:0046872; GO:0008237; GO:0019783,GO:0004222,GO:0004222,GO:0004222,GO:0008237,GO:0008237,0.5689,0.5689,0.5689,0.7115,0.7115,5,0.6259,0.2975,no
BILC_COLS4,A0A1I1NU16,Prot2Text,Bacteria,173,"Component of the Bil (bacterial ISG15-like) antiviral defense system, composed of BilA, BilB, BilC and BilD. The Bil system specifically conjugates a ubiquitin-like moiety (bilA) to the bacteriophage central tail fiber (CTF, or tip attachment protein J) via reactions involving E1 (bilD) and E2 (bilB). Modifies CTF of phage SECphi27 and SECphi4, which probably interferes with assembly of the phage tail. Also modifies T5 baseplate hub protein pb3 (gene D16), but not gp27 of phage T6 (Bil defends against T6). BilC is a probable metalloprotease that may cleave non-specifically conjugated targets (Probable). Bil-encoding bacteria produce mostly defective phage SECphi27, many of which have phage assembly defects, including no tails. SECphi27 phage progeny produced in E.coli with the Bil system inject less DNA into naive host cells, maybe because the phage are less able to adsorb and inject their DNA into host cells.","Cysine- and citrate-dependent metalloprotease that catalyzes the removal of penicillin N from non-pipid substrates. Cleaves the C-terminal amino acid of citrate-N-acetylmuramyl-L-alanine (CmNAc-MurNAc), the predominant piperazine N-acetylmuramyl-L-serine (CmNAc-MurNAc), and the N-terminal amino acid of citrate-N-acetylmuramyl-L-serine (CmNAc-MurNAc). Shows a preference for substrates with a lysine at the N-terminus. Does not act as a mono- or dipeptidyl-prolyl cis-trans isomerase.",Maybe,Maybe,No,No,No,not-Yes,GO:0046872; GO:0008237; GO:0019783,GO:0008233,GO:0004222,GO:0004222,GO:0004222,GO:0004222,0.6815,0.5689,0.5689,0.5689,0.5689,5,0.5914,0.2975,no
BILC_COLS4,A0A1I1NU16,ProtT3,Bacteria,173,"Component of the Bil (bacterial ISG15-like) antiviral defense system, composed of BilA, BilB, BilC and BilD. The Bil system specifically conjugates a ubiquitin-like moiety (bilA) to the bacteriophage central tail fiber (CTF, or tip attachment protein J) via reactions involving E1 (bilD) and E2 (bilB). Modifies CTF of phage SECphi27 and SECphi4, which probably interferes with assembly of the phage tail. Also modifies T5 baseplate hub protein pb3 (gene D16), but not gp27 of phage T6 (Bil defends against T6). BilC is a probable metalloprotease that may cleave non-specifically conjugated targets (Probable). Bil-encoding bacteria produce mostly defective phage SECphi27, many of which have phage assembly defects, including no tails. SECphi27 phage progeny produced in E.coli with the Bil system inject less DNA into naive host cells, maybe because the phage are less able to adsorb and inject their DNA into host cells.",Belongs to the peptidase C56 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0046872; GO:0008237; GO:0019783,GO:0008234,GO:0008234,GO:0004197,GO:0008234,GO:0008234,0.5865,0.5865,0.4689,0.5865,0.5865,5,0.563,0.2975,no
BILC_COLS4,A0A1I1NU16,ProtTale,Bacteria,173,"Component of the Bil (bacterial ISG15-like) antiviral defense system, composed of BilA, BilB, BilC and BilD. The Bil system specifically conjugates a ubiquitin-like moiety (bilA) to the bacteriophage central tail fiber (CTF, or tip attachment protein J) via reactions involving E1 (bilD) and E2 (bilB). Modifies CTF of phage SECphi27 and SECphi4, which probably interferes with assembly of the phage tail. Also modifies T5 baseplate hub protein pb3 (gene D16), but not gp27 of phage T6 (Bil defends against T6). BilC is a probable metalloprotease that may cleave non-specifically conjugated targets (Probable). Bil-encoding bacteria produce mostly defective phage SECphi27, many of which have phage assembly defects, including no tails. SECphi27 phage progeny produced in E.coli with the Bil system inject less DNA into naive host cells, maybe because the phage are less able to adsorb and inject their DNA into host cells.","Enzyme that has both phosphodiesterase and phosphomonoesterase activity. Shows highest activity towards 3'(2')-cyclic GMP-monophosphate (3'(2')-cGMP-MP), followed by 3'(2')-cyclic GMP-diphosphate (3'(2')-cGMP-DP), 3'(2')-cyclic GMP-monophosphate (3'(2')-cGMP-MP), 3'(2')-cyclic GMP-diphosphate (3'(2')-",Vague,No,No,No,No,not-Yes,GO:0046872; GO:0008237; GO:0019783,GO:0004114,GO:0004112; GO:0004114,GO:0004112,GO:0004112; GO:0016791,GO:0004112; GO:0016791,0.2341,0.2665,0.2608,0.3015,0.3015,5,0.2729,0.2975,no
BILC_COLS4,A0A1I1NU16,Protein2Text,Bacteria,173,"Component of the Bil (bacterial ISG15-like) antiviral defense system, composed of BilA, BilB, BilC and BilD. The Bil system specifically conjugates a ubiquitin-like moiety (bilA) to the bacteriophage central tail fiber (CTF, or tip attachment protein J) via reactions involving E1 (bilD) and E2 (bilB). Modifies CTF of phage SECphi27 and SECphi4, which probably interferes with assembly of the phage tail. Also modifies T5 baseplate hub protein pb3 (gene D16), but not gp27 of phage T6 (Bil defends against T6). BilC is a probable metalloprotease that may cleave non-specifically conjugated targets (Probable). Bil-encoding bacteria produce mostly defective phage SECphi27, many of which have phage assembly defects, including no tails. SECphi27 phage progeny produced in E.coli with the Bil system inject less DNA into naive host cells, maybe because the phage are less able to adsorb and inject their DNA into host cells.","The molecular function of this protein is an enzyme that mediates the cleavage of nucleic acids. Specifically, it is a metalloprotease that is involved in the cleavage of nucleic acids.",Maybe,No,No,No,No,not-Yes,GO:0046872; GO:0008237; GO:0019783,,,,,,,,,,,0,,0.2975,no
BILC_COLS4,A0A1I1NU16,Reference,Bacteria,173,"Component of the Bil (bacterial ISG15-like) antiviral defense system, composed of BilA, BilB, BilC and BilD. The Bil system specifically conjugates a ubiquitin-like moiety (bilA) to the bacteriophage central tail fiber (CTF, or tip attachment protein J) via reactions involving E1 (bilD) and E2 (bilB). Modifies CTF of phage SECphi27 and SECphi4, which probably interferes with assembly of the phage tail. Also modifies T5 baseplate hub protein pb3 (gene D16), but not gp27 of phage T6 (Bil defends against T6). BilC is a probable metalloprotease that may cleave non-specifically conjugated targets (Probable). Bil-encoding bacteria produce mostly defective phage SECphi27, many of which have phage assembly defects, including no tails. SECphi27 phage progeny produced in E.coli with the Bil system inject less DNA into naive host cells, maybe because the phage are less able to adsorb and inject their DNA into host cells.","Component of the Bil (bacterial ISG15-like) antiviral defense system, composed of BilA, BilB, BilC and BilD. The Bil system specifically conjugates a ubiquitin-like moiety (bilA) to the bacteriophage central tail fiber (CTF, or tip attachment protein J) via reactions involving E1 (bilD) and E2 (bilB). Modifies CTF of phage SECphi27 and SECphi4, which probably interferes with assembly of the phage tail. Also modifies T5 baseplate hub protein pb3 (gene D16), but not gp27 of phage T6 (Bil defends against T6). BilC is a probable metalloprotease that may cleave non-specifically conjugated targets (Probable). Bil-encoding bacteria produce mostly defective phage SECphi27, many of which have phage assembly defects, including no tails. SECphi27 phage progeny produced in E.coli with the Bil system inject less DNA into naive host cells, maybe because the phage are less able to adsorb and inject their DNA into host cells.",,,,,,,GO:0046872; GO:0008237; GO:0019783,,,,,,,,,,,0,,0.2975,no
FPY1_FUSMA,A0A1L7U3D7,ESM2Text,Eukaryota,2474,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the gamma-pyrones fusapyrone (FPY) and deoxyfusapyrone (dFPY) (Ref.2). FPY is an undecaketide and thus likely synthesized by the polyketide synthase FPY1 from acetyl-CoA functioning as starter unit and the addition of 10 malonyl-CoA extender units by successive Claisen-condensations. Next to this, FPY shares some rare features: C-glycosylated 4-deoxyglucose at C-3, a gem- dimethyl group at C-13, and an alpha-beta to beta-gamma double bond shift at C-20. During FPY biosynthesis mono-C-methyl groups are transferred to the tetra-, penta-, hexa- and heptaketide, while two C- methyl groups are transferred to the nonaketide, suggesting that the CMet domain is programmed to selectively catalyze two successive C- alpha-methylation reactions of the nonaketide, while other alpha- carbons are non- or mono-methylated only. While the origin of the 4'- deoxyglucose moiety remains opaque, its transfer to C-3 is most likely mediated by the C-glycosyltransferase FPY2. Next to this, the hydroxyl group present at C-33 and discriminating between FPY and dFPY, is likely to be installed by the cytochrome P450 monooxygenase FPY7. No putative function can be predicted for the remaining genes FPY3-FPY6 (Probable).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177; GO:0008270,,,,,,,,,,,0,,0.3175,no
FPY1_FUSMA,A0A1L7U3D7,Prot2Text,Eukaryota,2474,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the gamma-pyrones fusapyrone (FPY) and deoxyfusapyrone (dFPY) (Ref.2). FPY is an undecaketide and thus likely synthesized by the polyketide synthase FPY1 from acetyl-CoA functioning as starter unit and the addition of 10 malonyl-CoA extender units by successive Claisen-condensations. Next to this, FPY shares some rare features: C-glycosylated 4-deoxyglucose at C-3, a gem- dimethyl group at C-13, and an alpha-beta to beta-gamma double bond shift at C-20. During FPY biosynthesis mono-C-methyl groups are transferred to the tetra-, penta-, hexa- and heptaketide, while two C- methyl groups are transferred to the nonaketide, suggesting that the CMet domain is programmed to selectively catalyze two successive C- alpha-methylation reactions of the nonaketide, while other alpha- carbons are non- or mono-methylated only. While the origin of the 4'- deoxyglucose moiety remains opaque, its transfer to C-3 is most likely mediated by the C-glycosyltransferase FPY2. Next to this, the hydroxyl group present at C-33 and discriminating between FPY and dFPY, is likely to be installed by the cytochrome P450 monooxygenase FPY7. No putative function can be predicted for the remaining genes FPY3-FPY6 (Probable).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcsC",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177; GO:0008270,GO:0016747,,,GO:0016747,GO:0016746,0.4604,,,0.4604,0.4506,3,0.4571,0.3175,no
FPY1_FUSMA,A0A1L7U3D7,ProtT3,Eukaryota,2474,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the gamma-pyrones fusapyrone (FPY) and deoxyfusapyrone (dFPY) (Ref.2). FPY is an undecaketide and thus likely synthesized by the polyketide synthase FPY1 from acetyl-CoA functioning as starter unit and the addition of 10 malonyl-CoA extender units by successive Claisen-condensations. Next to this, FPY shares some rare features: C-glycosylated 4-deoxyglucose at C-3, a gem- dimethyl group at C-13, and an alpha-beta to beta-gamma double bond shift at C-20. During FPY biosynthesis mono-C-methyl groups are transferred to the tetra-, penta-, hexa- and heptaketide, while two C- methyl groups are transferred to the nonaketide, suggesting that the CMet domain is programmed to selectively catalyze two successive C- alpha-methylation reactions of the nonaketide, while other alpha- carbons are non- or mono-methylated only. While the origin of the 4'- deoxyglucose moiety remains opaque, its transfer to C-3 is most likely mediated by the C-glycosyltransferase FPY2. Next to this, the hydroxyl group present at C-33 and discriminating between FPY and dFPY, is likely to be installed by the cytochrome P450 monooxygenase FPY7. No putative function can be predicted for the remaining genes FPY3-FPY6 (Probable).","Alpha-ketoglutarate-dependent diketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins . The first step of the pathway is the synthesis of",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177; GO:0008270,,GO:0016706,,GO:0016706; GO:0005506,GO:0016706,,0.3047,,0.5036,0.3047,3,0.371,0.3175,no
FPY1_FUSMA,A0A1L7U3D7,ProtTale,Eukaryota,2474,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the gamma-pyrones fusapyrone (FPY) and deoxyfusapyrone (dFPY) (Ref.2). FPY is an undecaketide and thus likely synthesized by the polyketide synthase FPY1 from acetyl-CoA functioning as starter unit and the addition of 10 malonyl-CoA extender units by successive Claisen-condensations. Next to this, FPY shares some rare features: C-glycosylated 4-deoxyglucose at C-3, a gem- dimethyl group at C-13, and an alpha-beta to beta-gamma double bond shift at C-20. During FPY biosynthesis mono-C-methyl groups are transferred to the tetra-, penta-, hexa- and heptaketide, while two C- methyl groups are transferred to the nonaketide, suggesting that the CMet domain is programmed to selectively catalyze two successive C- alpha-methylation reactions of the nonaketide, while other alpha- carbons are non- or mono-methylated only. While the origin of the 4'- deoxyglucose moiety remains opaque, its transfer to C-3 is most likely mediated by the C-glycosyltransferase FPY2. Next to this, the hydroxyl group present at C-33 and discriminating between FPY and dFPY, is likely to be installed by the cytochrome P450 monooxygenase FPY7. No putative function can be predicted for the remaining genes FPY3-FPY6 (Probable).","Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177; GO:0008270,GO:0016491,GO:0016757,,,GO:0016746,0.503,0.3807,,,0.4506,3,0.4448,0.3175,no
FPY1_FUSMA,A0A1L7U3D7,Protein2Text,Eukaryota,2474,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the gamma-pyrones fusapyrone (FPY) and deoxyfusapyrone (dFPY) (Ref.2). FPY is an undecaketide and thus likely synthesized by the polyketide synthase FPY1 from acetyl-CoA functioning as starter unit and the addition of 10 malonyl-CoA extender units by successive Claisen-condensations. Next to this, FPY shares some rare features: C-glycosylated 4-deoxyglucose at C-3, a gem- dimethyl group at C-13, and an alpha-beta to beta-gamma double bond shift at C-20. During FPY biosynthesis mono-C-methyl groups are transferred to the tetra-, penta-, hexa- and heptaketide, while two C- methyl groups are transferred to the nonaketide, suggesting that the CMet domain is programmed to selectively catalyze two successive C- alpha-methylation reactions of the nonaketide, while other alpha- carbons are non- or mono-methylated only. While the origin of the 4'- deoxyglucose moiety remains opaque, its transfer to C-3 is most likely mediated by the C-glycosyltransferase FPY2. Next to this, the hydroxyl group present at C-33 and discriminating between FPY and dFPY, is likely to be installed by the cytochrome P450 monooxygenase FPY7. No putative function can be predicted for the remaining genes FPY3-FPY6 (Probable).","This protein is involved in the molecular function of fatty acid biosynthesis. It is a type of enzyme that plays a crucial role in the production of fatty acids, which are essential components of various cellular processes. Specifically, it is involved in the elongation of fatty acids, which is an important step in the synthesis of complex lipids.",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177; GO:0008270,GO:0004312,GO:0009922,GO:0004312,,GO:0004312,0.4839,0.3936,0.4839,,0.4839,4,0.4613,0.3175,no
FPY1_FUSMA,A0A1L7U3D7,Reference,Eukaryota,2474,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the gamma-pyrones fusapyrone (FPY) and deoxyfusapyrone (dFPY) (Ref.2). FPY is an undecaketide and thus likely synthesized by the polyketide synthase FPY1 from acetyl-CoA functioning as starter unit and the addition of 10 malonyl-CoA extender units by successive Claisen-condensations. Next to this, FPY shares some rare features: C-glycosylated 4-deoxyglucose at C-3, a gem- dimethyl group at C-13, and an alpha-beta to beta-gamma double bond shift at C-20. During FPY biosynthesis mono-C-methyl groups are transferred to the tetra-, penta-, hexa- and heptaketide, while two C- methyl groups are transferred to the nonaketide, suggesting that the CMet domain is programmed to selectively catalyze two successive C- alpha-methylation reactions of the nonaketide, while other alpha- carbons are non- or mono-methylated only. While the origin of the 4'- deoxyglucose moiety remains opaque, its transfer to C-3 is most likely mediated by the C-glycosyltransferase FPY2. Next to this, the hydroxyl group present at C-33 and discriminating between FPY and dFPY, is likely to be installed by the cytochrome P450 monooxygenase FPY7. No putative function can be predicted for the remaining genes FPY3-FPY6 (Probable).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the gamma-pyrones fusapyrone (FPY) and deoxyfusapyrone (dFPY) (Ref.2). FPY is an undecaketide and thus likely synthesized by the polyketide synthase FPY1 from acetyl-CoA functioning as starter unit and the addition of 10 malonyl-CoA extender units by successive Claisen-condensations. Next to this, FPY shares some rare features: C-glycosylated 4-deoxyglucose at C-3, a gem- dimethyl group at C-13, and an alpha-beta to beta-gamma double bond shift at C-20. During FPY biosynthesis mono-C-methyl groups are transferred to the tetra-, penta-, hexa- and heptaketide, while two C- methyl groups are transferred to the nonaketide, suggesting that the CMet domain is programmed to selectively catalyze two successive C- alpha-methylation reactions of the nonaketide, while other alpha- carbons are non- or mono-methylated only. While the origin of the 4'- deoxyglucose moiety remains opaque, its transfer to C-3 is most likely mediated by the C-glycosyltransferase FPY2. Next to this, the hydroxyl group present at C-33 and discriminating between FPY and dFPY, is likely to be installed by the cytochrome P450 monooxygenase FPY7. No putative function can be predicted for the remaining genes FPY3-FPY6 (Probable).",,,,,,,GO:0004312; GO:0008168; GO:0016491; GO:0031177; GO:0008270,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.4506,0.4506,0.4506,0.4604,0.4506,5,0.4526,0.3175,no
FUP1_FUSPR,A0A1L7VFX3,ESM2Text,Eukaryota,753,"Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusaproliferin (FUP) that belongs to the class of bicyclic sesterterpenoids. The FUP biosynthetic pathway starts with the enzyme encoded by FUP1 that combines a C-terminal prenyltransferase domain responsible for the synthesis of geranylgeranyl diphosphate with the N-terminal terpene cyclase domain, to yield preterpestacin I. Preterpestacin I is then decorated by oxygenation steps that are catalyzed by two cytochrome P450 monooxygenases. First, FUP2 introduces a hydroxyl group at the C-24 position resulting in the formation of preterpestacin IIa, which can be further oxidized. The second P450 monooxygenase catalyzes the hydroxylation at C-16 and C-17 of preterpestacin IIa, producing preterpestacin III. Subsequently, the FAD-dependent oxidoreductase FUP4 catalyzes the oxidation of the hydroxy group at the C-16 position to a keto group, leading to the formation of (-)-terpestacin, which is the immediate precursor of FUP. The final step in the proposed biosynthetic pathway is the addition of an acetyl group at the C-24 position of terpestacin, which is catalyzed by the acetyltransferase FUP5.","Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD). Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors. The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes. Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-8(14),15-diene. The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1595, the glutathione S-transferase AN1596, the oxidoreductases AN1597 and AN1598 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15",Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004311; GO:0016829; GO:0046872,,,,,GO:0010333,,,,,0.3666,1,0.3666,0.2465,no
FUP1_FUSPR,A0A1L7VFX3,Prot2Text,Eukaryota,753,"Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusaproliferin (FUP) that belongs to the class of bicyclic sesterterpenoids. The FUP biosynthetic pathway starts with the enzyme encoded by FUP1 that combines a C-terminal prenyltransferase domain responsible for the synthesis of geranylgeranyl diphosphate with the N-terminal terpene cyclase domain, to yield preterpestacin I. Preterpestacin I is then decorated by oxygenation steps that are catalyzed by two cytochrome P450 monooxygenases. First, FUP2 introduces a hydroxyl group at the C-24 position resulting in the formation of preterpestacin IIa, which can be further oxidized. The second P450 monooxygenase catalyzes the hydroxylation at C-16 and C-17 of preterpestacin IIa, producing preterpestacin III. Subsequently, the FAD-dependent oxidoreductase FUP4 catalyzes the oxidation of the hydroxy group at the C-16 position to a keto group, leading to the formation of (-)-terpestacin, which is the immediate precursor of FUP. The final step in the proposed biosynthetic pathway is the addition of an acetyl group at the C-24 position of terpestacin, which is catalyzed by the acetyltransferase FUP5.","Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD). Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors. The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes. Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-8(14),15-diene. The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15",Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004311; GO:0016829; GO:0046872,GO:0010333,,GO:0016829,GO:0016829,GO:0010333,0.3666,,0.6189,0.6189,0.3666,4,0.4928,0.2465,no
FUP1_FUSPR,A0A1L7VFX3,ProtT3,Eukaryota,753,"Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusaproliferin (FUP) that belongs to the class of bicyclic sesterterpenoids. The FUP biosynthetic pathway starts with the enzyme encoded by FUP1 that combines a C-terminal prenyltransferase domain responsible for the synthesis of geranylgeranyl diphosphate with the N-terminal terpene cyclase domain, to yield preterpestacin I. Preterpestacin I is then decorated by oxygenation steps that are catalyzed by two cytochrome P450 monooxygenases. First, FUP2 introduces a hydroxyl group at the C-24 position resulting in the formation of preterpestacin IIa, which can be further oxidized. The second P450 monooxygenase catalyzes the hydroxylation at C-16 and C-17 of preterpestacin IIa, producing preterpestacin III. Subsequently, the FAD-dependent oxidoreductase FUP4 catalyzes the oxidation of the hydroxy group at the C-16 position to a keto group, leading to the formation of (-)-terpestacin, which is the immediate precursor of FUP. The final step in the proposed biosynthetic pathway is the addition of an acetyl group at the C-24 position of terpestacin, which is catalyzed by the acetyltransferase FUP5.","Bifunctional sesterterpene synthase; part of the gene cluster that mediates the biosynthesis of the sesterterpenes penitrems . The first step of penitrem biosynthesis is performed by the sesterterpene synthase ptmG that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylfarnesyl diphosphate (GFPP) and subsequently converting GFPP into penitrems . The terpene cyclase activity",Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004311; GO:0016829; GO:0046872,GO:0004659; GO:0010333,GO:0004659; GO:0010333,GO:0004659; GO:0010333,GO:0004659; GO:0010333,GO:0004659; GO:0010333,0.5632,0.5632,0.5632,0.5632,0.5632,5,0.5632,0.2465,no
FUP1_FUSPR,A0A1L7VFX3,ProtTale,Eukaryota,753,"Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusaproliferin (FUP) that belongs to the class of bicyclic sesterterpenoids. The FUP biosynthetic pathway starts with the enzyme encoded by FUP1 that combines a C-terminal prenyltransferase domain responsible for the synthesis of geranylgeranyl diphosphate with the N-terminal terpene cyclase domain, to yield preterpestacin I. Preterpestacin I is then decorated by oxygenation steps that are catalyzed by two cytochrome P450 monooxygenases. First, FUP2 introduces a hydroxyl group at the C-24 position resulting in the formation of preterpestacin IIa, which can be further oxidized. The second P450 monooxygenase catalyzes the hydroxylation at C-16 and C-17 of preterpestacin IIa, producing preterpestacin III. Subsequently, the FAD-dependent oxidoreductase FUP4 catalyzes the oxidation of the hydroxy group at the C-16 position to a keto group, leading to the formation of (-)-terpestacin, which is the immediate precursor of FUP. The final step in the proposed biosynthetic pathway is the addition of an acetyl group at the C-24 position of terpestacin, which is catalyzed by the acetyltransferase FUP5.","Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. Within the pathway, PC-2 catalyzes the cyclization of 5-epi-aristolochene to 13-epi-13-deoxyaristolochene. The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3-glycerol phosphate with GGPP by penC then forms",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004311; GO:0016829; GO:0046872,GO:0010333,GO:0010334,GO:0010333,GO:0016829,GO:0010333,0.3666,0.3257,0.3666,0.6189,0.3666,5,0.4089,0.2465,no
FUP1_FUSPR,A0A1L7VFX3,Protein2Text,Eukaryota,753,"Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusaproliferin (FUP) that belongs to the class of bicyclic sesterterpenoids. The FUP biosynthetic pathway starts with the enzyme encoded by FUP1 that combines a C-terminal prenyltransferase domain responsible for the synthesis of geranylgeranyl diphosphate with the N-terminal terpene cyclase domain, to yield preterpestacin I. Preterpestacin I is then decorated by oxygenation steps that are catalyzed by two cytochrome P450 monooxygenases. First, FUP2 introduces a hydroxyl group at the C-24 position resulting in the formation of preterpestacin IIa, which can be further oxidized. The second P450 monooxygenase catalyzes the hydroxylation at C-16 and C-17 of preterpestacin IIa, producing preterpestacin III. Subsequently, the FAD-dependent oxidoreductase FUP4 catalyzes the oxidation of the hydroxy group at the C-16 position to a keto group, leading to the formation of (-)-terpestacin, which is the immediate precursor of FUP. The final step in the proposed biosynthetic pathway is the addition of an acetyl group at the C-24 position of terpestacin, which is catalyzed by the acetyltransferase FUP5.","This protein is involved in the biosynthesis of a molecule, but the specific molecular function is not specified. However, based on its classification as a cytochrome P450 monooxygenase, it is likely that this protein catalyzes a reaction involving the transfer of an oxygen atom to a substrate molecule, possibly in the biosynthesis of a sterol or other secondary metabolite. 

In more detail, this protein is a part of the cytochrome P450 monooxygenases, which are a family of enzymes that catalyze a variety of reactions involving the transfer of an oxygen atom from molecular oxygen to a substrate molecule. These enzymes are typically involved in the biosynthesis of secondary metabolites, such as steroids, terpenes, and alkaloids, and play important roles in the metabolism and detoxification of xenobiotics. 

In the case of this protein, it is likely that it is involved in the biosynthesis of a sterol or other secondary metabolite, possibly as part of a larger metabolic pathway. The exact molecular function of this protein would depend on the specific substrate(s) it interacts with and the reactions it catalyzes. 

Further research would be needed to determine the specific molecular function of this protein and its role in the biosynthesis of secondary metabolites.",No,No,No,No,Maybe,not-Yes,GO:0004311; GO:0016829; GO:0046872,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.335,0.335,0.335,0.335,0.335,5,0.335,0.2465,no
FUP1_FUSPR,A0A1L7VFX3,Reference,Eukaryota,753,"Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusaproliferin (FUP) that belongs to the class of bicyclic sesterterpenoids. The FUP biosynthetic pathway starts with the enzyme encoded by FUP1 that combines a C-terminal prenyltransferase domain responsible for the synthesis of geranylgeranyl diphosphate with the N-terminal terpene cyclase domain, to yield preterpestacin I. Preterpestacin I is then decorated by oxygenation steps that are catalyzed by two cytochrome P450 monooxygenases. First, FUP2 introduces a hydroxyl group at the C-24 position resulting in the formation of preterpestacin IIa, which can be further oxidized. The second P450 monooxygenase catalyzes the hydroxylation at C-16 and C-17 of preterpestacin IIa, producing preterpestacin III. Subsequently, the FAD-dependent oxidoreductase FUP4 catalyzes the oxidation of the hydroxy group at the C-16 position to a keto group, leading to the formation of (-)-terpestacin, which is the immediate precursor of FUP. The final step in the proposed biosynthetic pathway is the addition of an acetyl group at the C-24 position of terpestacin, which is catalyzed by the acetyltransferase FUP5.","Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusaproliferin (FUP) that belongs to the class of bicyclic sesterterpenoids. The FUP biosynthetic pathway starts with the enzyme encoded by FUP1 that combines a C-terminal prenyltransferase domain responsible for the synthesis of geranylgeranyl diphosphate with the N-terminal terpene cyclase domain, to yield preterpestacin I. Preterpestacin I is then decorated by oxygenation steps that are catalyzed by two cytochrome P450 monooxygenases. First, FUP2 introduces a hydroxyl group at the C-24 position resulting in the formation of preterpestacin IIa, which can be further oxidized. The second P450 monooxygenase catalyzes the hydroxylation at C-16 and C-17 of preterpestacin IIa, producing preterpestacin III. Subsequently, the FAD-dependent oxidoreductase FUP4 catalyzes the oxidation of the hydroxy group at the C-16 position to a keto group, leading to the formation of (-)-terpestacin, which is the immediate precursor of FUP. The final step in the proposed biosynthetic pathway is the addition of an acetyl group at the C-24 position of terpestacin, which is catalyzed by the acetyltransferase FUP5.",,,,,,,GO:0004311; GO:0016829; GO:0046872,GO:0016765; GO:0016829,GO:0004659; GO:0010333,GO:0004659,GO:0010333; GO:0016765,GO:0004337; GO:0016829,0.6902,0.5632,0.5048,0.5247,0.7303,5,0.6026,0.2465,no
VRCA_ASPA1,A0A1L9WQI2,ESM2Text,Eukaryota,710,"Multifunctional sesterterpene synthase; part of the gene cluster that mediates the biosynthesis of the sesterterpene variecolin. The first step in the pathway is performed by the variecoladiene synthase vrcA that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylfarnesyl pyrophosphate (GFPP) and then converting GFPP into the tetracyclic variecoladiene. The cytochrome P450 monooxygenase vrcB then catalyzes multiple oxidations at C-5 and C-20 positions to yield variecolin.","Multifunctional diterpene synthase; part of the gene cluster that mediates the biosynthesis of the diterpene glucoside brassicicene C. In the first step of the brassicicene C biosynthesis, the bifunctionnal diterpene synthase bsc8 that possesses both prenyl transferase and terpene cyclase activity, converts isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) that is further converted into fusicocca-2,10(14)-diene, the first precursor for brassicicene C. Fusicocca-2,10(14)-diene is then substrate of cytochrome P450 monooxygenase bsc1 for hydroxylation at the C-8 position. Oxidation at C-16 position to aldehyde is then catalyzed by the cytochrome P450 monooyxygenase bsc7, yielding fusicocca-2,10(14)-diene-8-beta,16-diol. Follows the isomerization of the double bond and reduction of a",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016829; GO:0046872; GO:0004659,,,GO:0010333,GO:0004337,GO:0010333,,,0.382,0.4756,0.382,3,0.4132,0.2897,no
VRCA_ASPA1,A0A1L9WQI2,Prot2Text,Eukaryota,710,"Multifunctional sesterterpene synthase; part of the gene cluster that mediates the biosynthesis of the sesterterpene variecolin. The first step in the pathway is performed by the variecoladiene synthase vrcA that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylfarnesyl pyrophosphate (GFPP) and then converting GFPP into the tetracyclic variecoladiene. The cytochrome P450 monooxygenase vrcB then catalyzes multiple oxidations at C-5 and C-20 positions to yield variecolin.","Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD). Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors. The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes. Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-8(14),15-diene. The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016829; GO:0046872; GO:0004659,GO:0010333,,GO:0016829,GO:0016829,GO:0010333,0.382,,0.6412,0.6412,0.382,4,0.5116,0.2897,no
VRCA_ASPA1,A0A1L9WQI2,ProtT3,Eukaryota,710,"Multifunctional sesterterpene synthase; part of the gene cluster that mediates the biosynthesis of the sesterterpene variecolin. The first step in the pathway is performed by the variecoladiene synthase vrcA that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylfarnesyl pyrophosphate (GFPP) and then converting GFPP into the tetracyclic variecoladiene. The cytochrome P450 monooxygenase vrcB then catalyzes multiple oxidations at C-5 and C-20 positions to yield variecolin.","Bifunctional sesterterpene synthase; part of the gene cluster that mediates the biosynthesis of the sesterterpenes penitrems . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase ptmA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). DMOA is then prenylated by the polyprenyl transferase ptmC to form 3",Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016829; GO:0046872; GO:0004659,GO:0004659; GO:0010333,GO:0004659; GO:0010333,GO:0004659; GO:0010333,GO:0004659; GO:0010333,GO:0004659; GO:0010333,0.6617,0.6617,0.6617,0.6617,0.6617,5,0.6617,0.2897,no
VRCA_ASPA1,A0A1L9WQI2,ProtTale,Eukaryota,710,"Multifunctional sesterterpene synthase; part of the gene cluster that mediates the biosynthesis of the sesterterpene variecolin. The first step in the pathway is performed by the variecoladiene synthase vrcA that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylfarnesyl pyrophosphate (GFPP) and then converting GFPP into the tetracyclic variecoladiene. The cytochrome P450 monooxygenase vrcB then catalyzes multiple oxidations at C-5 and C-20 positions to yield variecolin.",Bifunctional terpene synthase that converts dimethylallyl diphosphate (DMAPP) and isopentenyl diphosphate (IPP) into geranylfarnesyl diphosphate (GFPP). Catalyzes the conversion of DMAPP and IPP into geranylgeranyl diphosphate (GGPP).,Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016829; GO:0046872; GO:0004659,GO:0004337; GO:0016740,GO:0004337,GO:0004311,GO:0016765,GO:0004337,0.5891,0.4756,0.4756,0.5726,0.4756,5,0.5177,0.2897,no
VRCA_ASPA1,A0A1L9WQI2,Protein2Text,Eukaryota,710,"Multifunctional sesterterpene synthase; part of the gene cluster that mediates the biosynthesis of the sesterterpene variecolin. The first step in the pathway is performed by the variecoladiene synthase vrcA that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylfarnesyl pyrophosphate (GFPP) and then converting GFPP into the tetracyclic variecoladiene. The cytochrome P450 monooxygenase vrcB then catalyzes multiple oxidations at C-5 and C-20 positions to yield variecolin.","This protein is involved in the molecular function of terpene biosynthesis. Specifically, it is a terpene synthase that catalyzes the conversion of farnesyl diphosphate to a specific terpene product. Terpene synthases are enzymes that play a crucial role in the biosynthesis of terpenes, which are a diverse group of natural products with a wide range of biological activities. The protein is likely involved in the production of a specific terpene compound that is important for the organism's defense mechanisms or other biological processes.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016829; GO:0046872; GO:0004659,GO:0010333,,,GO:0010333,,0.382,,,0.382,,2,0.382,0.2897,no
VRCA_ASPA1,A0A1L9WQI2,Reference,Eukaryota,710,"Multifunctional sesterterpene synthase; part of the gene cluster that mediates the biosynthesis of the sesterterpene variecolin. The first step in the pathway is performed by the variecoladiene synthase vrcA that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylfarnesyl pyrophosphate (GFPP) and then converting GFPP into the tetracyclic variecoladiene. The cytochrome P450 monooxygenase vrcB then catalyzes multiple oxidations at C-5 and C-20 positions to yield variecolin.","Multifunctional sesterterpene synthase; part of the gene cluster that mediates the biosynthesis of the sesterterpene variecolin. The first step in the pathway is performed by the variecoladiene synthase vrcA that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylfarnesyl pyrophosphate (GFPP) and then converting GFPP into the tetracyclic variecoladiene. The cytochrome P450 monooxygenase vrcB then catalyzes multiple oxidations at C-5 and C-20 positions to yield variecolin.",,,,,,,GO:0016829; GO:0046872; GO:0004659,GO:0016765; GO:0016829,GO:0004659; GO:0010333,GO:0004659,GO:0010333; GO:0016765,GO:0016765; GO:0016829,0.7682,0.6617,0.6279,0.6027,0.7682,5,0.6857,0.2897,no
SIPKK_TOBAC,A0A1S4CGX4,ESM2Text,Eukaryota,357,Phosphorylates myelin basic protein (MBP) in vitro. May be involved in disease resistance (Probable).,Is probably involved in a signal transduction pathway that regulates sexual development and cell growth in response to environmental signals.,Maybe,Vague,Vague,Vague,Maybe,not-Yes,GO:0005524; GO:0004708; GO:0004674,,,,,,,,,,,0,,0.5459,yes
SIPKK_TOBAC,A0A1S4CGX4,Prot2Text,Eukaryota,357,Phosphorylates myelin basic protein (MBP) in vitro. May be involved in disease resistance (Probable).,MKK6-MPK13 module positively regulates lateral root formation.,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0005524; GO:0004708; GO:0004674,GO:0004708,,GO:0004708,GO:0004708,,0.6987,,0.6987,0.6987,,3,0.6987,0.5459,yes
SIPKK_TOBAC,A0A1S4CGX4,ProtT3,Eukaryota,357,Phosphorylates myelin basic protein (MBP) in vitro. May be involved in disease resistance (Probable).,"Mitogen-activated protein kinase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",No,Maybe,Maybe,No,No,not-Yes,GO:0005524; GO:0004708; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004707; GO:0004674; GO:0005524,GO:0004707; GO:0004674; GO:0005524,GO:0004707; GO:0005524,0.9492,0.9492,0.9425,0.9425,0.8976,5,0.9362,0.5459,yes
SIPKK_TOBAC,A0A1S4CGX4,ProtTale,Eukaryota,357,Phosphorylates myelin basic protein (MBP) in vitro. May be involved in disease resistance (Probable).,"Serine/threonine-protein kinase involved in a signal transduction pathway that plays a role in cell growth, differentiation and development.",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004708; GO:0004674,GO:0004674; GO:0005524,GO:0004674,GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.9492,0.7,0.7,0.9492,0.9492,5,0.8495,0.5459,yes
SIPKK_TOBAC,A0A1S4CGX4,Protein2Text,Eukaryota,357,Phosphorylates myelin basic protein (MBP) in vitro. May be involved in disease resistance (Probable).,The molecular function of this protein is a serine/threonine-protein kinase.,Yes,Yes,Maybe,Maybe,Vague,not-Yes,GO:0005524; GO:0004708; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.7,0.7,0.7,0.7,0.7,5,0.7,0.5459,yes
SIPKK_TOBAC,A0A1S4CGX4,Reference,Eukaryota,357,Phosphorylates myelin basic protein (MBP) in vitro. May be involved in disease resistance (Probable).,Phosphorylates myelin basic protein (MBP) in vitro. May be involved in disease resistance (Probable).,,,,,,,GO:0005524; GO:0004708; GO:0004674,GO:0004674; GO:0005524,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.9492,0.7,0.7,0.7,0.7,5,0.7498,0.5459,yes
CATL_AEDAE,A0A1S4F2V5,ESM2Text,Eukaryota,339,"Proteinase exhibiting preference for Leu, Val and Phe residues at the P2 position.",Cysteine protease involved in autophagic degradation and contributes to pathogenicity.,Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004197,GO:0008234,GO:0008234,GO:0008234,GO:0008234,GO:0008234,0.8001,0.8001,0.8001,0.8001,0.8001,5,0.8001,0.4154,no
CATL_AEDAE,A0A1S4F2V5,Prot2Text,Eukaryota,339,"Proteinase exhibiting preference for Leu, Val and Phe residues at the P2 position.",Probable thiol protease.,Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004197,GO:0008234,,GO:0008234,GO:0008234,GO:0008234,0.8001,,0.8001,0.8001,0.8001,4,0.8001,0.4154,no
CATL_AEDAE,A0A1S4F2V5,ProtT3,Eukaryota,339,"Proteinase exhibiting preference for Leu, Val and Phe residues at the P2 position.",Lysosome. Belongs to the peptidase C1 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004197,GO:0004197,GO:0008234,GO:0004197,GO:0008234,GO:0008234,1.0,0.8001,1.0,0.8001,0.8001,5,0.8801,0.4154,no
CATL_AEDAE,A0A1S4F2V5,ProtTale,Eukaryota,339,"Proteinase exhibiting preference for Leu, Val and Phe residues at the P2 position.","Thiol protease that plays an essential role in host defense by mediating the degradation of a wide range of host proteins involved in inflammation, apoptosis, innate immunity, cell proliferation, and migration. Plays a central role in the pathogenesis of several infectious and inflammatory diseases such as severe acute respiratory syndrome (SARS), Ebola virus disease (EBOV), Crimean-Congo hemorrhagic fever (CCHF), Lassa virus disease (LASV), Marburg virus disease (MARV), Ebola virus disease (EBOV) and severe acute respiratory syndrome (SARS). Mechanistically,",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0004197,GO:0008234,GO:0008234,GO:0008234,GO:0008234,GO:0008234,0.8001,0.8001,0.8001,0.8001,0.8001,5,0.8001,0.4154,no
CATL_AEDAE,A0A1S4F2V5,Protein2Text,Eukaryota,339,"Proteinase exhibiting preference for Leu, Val and Phe residues at the P2 position.","The molecular function of this protein is to degrade proteins, specifically cysteine protease activity. It is involved in breaking down proteins into smaller peptides or amino acids.",Maybe,Yes,Yes,Maybe,Yes,Yes,GO:0004197,GO:0008234,GO:0008234,GO:0008234,GO:0008234,GO:0008234,0.8001,0.8001,0.8001,0.8001,0.8001,5,0.8001,0.4154,no
CATL_AEDAE,A0A1S4F2V5,Reference,Eukaryota,339,"Proteinase exhibiting preference for Leu, Val and Phe residues at the P2 position.","Proteinase exhibiting preference for Leu, Val and Phe residues at the P2 position.",,,,,,,GO:0004197,GO:0008233,GO:0004175,GO:0004175,GO:0008233,GO:0008233,0.703,0.8001,0.8001,0.703,0.703,5,0.7418,0.4154,no
VERA_PENPO,A0A1V6NYI6,ESM2Text,Eukaryota,2566,"Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of the neurotoxin verrucosidin, a methylated alpha-pyrone polyketide that inhibits oxidative phosphorylation in mitochondria and thereby causes neurological diseases. The carbon backbone of verrucosidin is synthesized by the HR-PKS verA, and further modified by the other verrucodidin cluster enzymes (Probable).","Reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The nonribosomal peptide synthetase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0008168; GO:0031177,,,,,,,,,,,0,,0.2726,no
VERA_PENPO,A0A1V6NYI6,Prot2Text,Eukaryota,2566,"Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of the neurotoxin verrucosidin, a methylated alpha-pyrone polyketide that inhibits oxidative phosphorylation in mitochondria and thereby causes neurological diseases. The carbon backbone of verrucosidin is synthesized by the HR-PKS verA, and further modified by the other verrucodidin cluster enzymes (Probable).","Reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0008168; GO:0031177,GO:0016747,,,GO:0016747,GO:0016746,0.6263,,,0.6263,0.5701,3,0.6076,0.2726,no
VERA_PENPO,A0A1V6NYI6,ProtT3,Eukaryota,2566,"Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of the neurotoxin verrucosidin, a methylated alpha-pyrone polyketide that inhibits oxidative phosphorylation in mitochondria and thereby causes neurological diseases. The carbon backbone of verrucosidin is synthesized by the HR-PKS verA, and further modified by the other verrucodidin cluster enzymes (Probable).","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0008168; GO:0031177,GO:0016746,GO:0016746,,GO:0016746,GO:0016747,0.5701,0.5701,,0.5701,0.6263,4,0.5842,0.2726,no
VERA_PENPO,A0A1V6NYI6,ProtTale,Eukaryota,2566,"Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of the neurotoxin verrucosidin, a methylated alpha-pyrone polyketide that inhibits oxidative phosphorylation in mitochondria and thereby causes neurological diseases. The carbon backbone of verrucosidin is synthesized by the HR-PKS verA, and further modified by the other verrucodidin cluster enzymes (Probable).","Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. Within the pathway, ptmC is responsible for the cyclization of prepenitrem D to yield penitrem B. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3-glycerol phosphate with GGPP by ptmC then forms 3",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0008168; GO:0031177,GO:0016491,GO:0016757,,,GO:0016746,0.3303,0.4368,,,0.5701,3,0.4457,0.2726,no
VERA_PENPO,A0A1V6NYI6,Protein2Text,Eukaryota,2566,"Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of the neurotoxin verrucosidin, a methylated alpha-pyrone polyketide that inhibits oxidative phosphorylation in mitochondria and thereby causes neurological diseases. The carbon backbone of verrucosidin is synthesized by the HR-PKS verA, and further modified by the other verrucodidin cluster enzymes (Probable).","This protein is involved in the molecular function of fatty acid biosynthesis. Specifically, it is a subunit of a fatty acid synthase enzyme, which is responsible for the synthesis of fatty acids from acetyl-CoA and malonyl-CoA. The fatty acid synthase enzyme is a multi-subunit complex that catalyzes the formation of fatty acids through a series of reduction, dehydration, and reductive transacylation reactions. This protein is one of the subunits that make up this complex, and it is likely involved in the synthesis of fatty acids through its catalytic activity.",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0004315; GO:0004312; GO:0008168; GO:0031177,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.6418,0.6418,0.6418,0.6418,0.6418,5,0.6418,0.2726,no
VERA_PENPO,A0A1V6NYI6,Reference,Eukaryota,2566,"Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of the neurotoxin verrucosidin, a methylated alpha-pyrone polyketide that inhibits oxidative phosphorylation in mitochondria and thereby causes neurological diseases. The carbon backbone of verrucosidin is synthesized by the HR-PKS verA, and further modified by the other verrucodidin cluster enzymes (Probable).","Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of the neurotoxin verrucosidin, a methylated alpha-pyrone polyketide that inhibits oxidative phosphorylation in mitochondria and thereby causes neurological diseases. The carbon backbone of verrucosidin is synthesized by the HR-PKS verA, and further modified by the other verrucodidin cluster enzymes (Probable).",,,,,,,GO:0004315; GO:0004312; GO:0008168; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.5701,0.5701,0.5701,0.6263,0.5701,5,0.5813,0.2726,no
EPOXH_CABSO,A0A242M8J4,ESM2Text,Bacteria,329,"Catalyzes the hydrolysis of various epoxides into diols. In vitro, shows the strongest activity toward aromatic and cyclic aliphatic epoxide compounds, since it shows strong activity toward (R)- styrene oxide, (S)-styrene oxide, and 3,4-epoxy-1-cyclohexene, but very weak activity toward (R)-epichlorohydrin, (S)-epichlorohydrin, and 1,2- epoxy-9-decene.","Is involved in detoxification of xylo-oligomers. Shows maximal activity against cotton, bollato[2.2.1]octa-6a and the corresponding p-nitrophenol derivatives.",No,No,No,Vague,No,not-Yes,GO:0004301,,,,,,,,,,,0,,0.1626,no
EPOXH_CABSO,A0A242M8J4,Prot2Text,Bacteria,329,"Catalyzes the hydrolysis of various epoxides into diols. In vitro, shows the strongest activity toward aromatic and cyclic aliphatic epoxide compounds, since it shows strong activity toward (R)- styrene oxide, (S)-styrene oxide, and 3,4-epoxy-1-cyclohexene, but very weak activity toward (R)-epichlorohydrin, (S)-epichlorohydrin, and 1,2- epoxy-9-decene.","Catalyzes the hydrolysis of epoxide-containing fatty acids. Active on L-lactate, D-lactate and on various epoxides including 9-hydroxy-12-oxo-octadecenoate and 9,10-epoxyeicosatrienoate.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004301,GO:0004301,GO:0004301,GO:0004301,GO:0004301,GO:0004301,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1626,no
EPOXH_CABSO,A0A242M8J4,ProtT3,Bacteria,329,"Catalyzes the hydrolysis of various epoxides into diols. In vitro, shows the strongest activity toward aromatic and cyclic aliphatic epoxide compounds, since it shows strong activity toward (R)- styrene oxide, (S)-styrene oxide, and 3,4-epoxy-1-cyclohexene, but very weak activity toward (R)-epichlorohydrin, (S)-epichlorohydrin, and 1,2- epoxy-9-decene.",Belongs to the AB hydrolase superfamily. Epoxide hydrolase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004301,GO:0004301,GO:0004301,GO:0004301,GO:0004301,GO:0004301,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1626,no
EPOXH_CABSO,A0A242M8J4,ProtTale,Bacteria,329,"Catalyzes the hydrolysis of various epoxides into diols. In vitro, shows the strongest activity toward aromatic and cyclic aliphatic epoxide compounds, since it shows strong activity toward (R)- styrene oxide, (S)-styrene oxide, and 3,4-epoxy-1-cyclohexene, but very weak activity toward (R)-epichlorohydrin, (S)-epichlorohydrin, and 1,2- epoxy-9-decene.",Involved in the biosynthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. Catalyzes the hydrolysis of the C-C bond between C-2 and C-3 of 4-hydroxy-3-methylbut-2-enyl diphosphate (HMBPP) to yield isopentenyl diphosphate (IPP).,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0004301,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016787,0.6019,0.6019,0.6019,0.6019,0.6019,5,0.6019,0.1626,no
EPOXH_CABSO,A0A242M8J4,Protein2Text,Bacteria,329,"Catalyzes the hydrolysis of various epoxides into diols. In vitro, shows the strongest activity toward aromatic and cyclic aliphatic epoxide compounds, since it shows strong activity toward (R)- styrene oxide, (S)-styrene oxide, and 3,4-epoxy-1-cyclohexene, but very weak activity toward (R)-epichlorohydrin, (S)-epichlorohydrin, and 1,2- epoxy-9-decene.","This protein is involved in the degradation of a specific type of molecule, likely a carboxylic acid. Its molecular function is likely to be a hydrolase, specifically a carboxyl ester hydrolase.",No,No,No,No,No,not-Yes,GO:0004301,GO:0016788,GO:0052689,GO:0052689,GO:0052689,GO:0052689,0.482,0.3987,0.3987,0.3987,0.3987,5,0.4154,0.1626,no
EPOXH_CABSO,A0A242M8J4,Reference,Bacteria,329,"Catalyzes the hydrolysis of various epoxides into diols. In vitro, shows the strongest activity toward aromatic and cyclic aliphatic epoxide compounds, since it shows strong activity toward (R)- styrene oxide, (S)-styrene oxide, and 3,4-epoxy-1-cyclohexene, but very weak activity toward (R)-epichlorohydrin, (S)-epichlorohydrin, and 1,2- epoxy-9-decene.","Catalyzes the hydrolysis of various epoxides into diols. In vitro, shows the strongest activity toward aromatic and cyclic aliphatic epoxide compounds, since it shows strong activity toward (R)- styrene oxide, (S)-styrene oxide, and 3,4-epoxy-1-cyclohexene, but very weak activity toward (R)-epichlorohydrin, (S)-epichlorohydrin, and 1,2- epoxy-9-decene.",,,,,,,GO:0004301,GO:0004301,GO:0004301,GO:0004301,GO:0004301,GO:0004301,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1626,no
XHPG_XENHO,A0A2G0QDP0,ESM2Text,Bacteria,266,"Involved in the biosynthetic pathway of pyrrolizwilline, a pyrrolizidine alkaloid. Catalyzes the N-deacetylation of pyrrolizixenacetamide.",Involved in the degradation of chloroacetate. Catalyzes the hydrolysis of chloroacetate to produce acetyl-CoA and a small amount of acetate.,No,No,No,No,No,not-Yes,GO:0052689,GO:0018784,GO:0016787,GO:0018784,GO:0018786,,0.3987,0.6897,0.3987,0.3987,,4,0.4714,0.1247,no
XHPG_XENHO,A0A2G0QDP0,Prot2Text,Bacteria,266,"Involved in the biosynthetic pathway of pyrrolizwilline, a pyrrolizidine alkaloid. Catalyzes the N-deacetylation of pyrrolizixenacetamide.",The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters.,No,Maybe,No,No,No,not-Yes,GO:0052689,GO:0052689,GO:0052689,GO:0004091,GO:0004091,GO:0016787,1.0,1.0,1.0,1.0,0.6897,5,0.9379,0.1247,no
XHPG_XENHO,A0A2G0QDP0,ProtT3,Bacteria,266,"Involved in the biosynthetic pathway of pyrrolizwilline, a pyrrolizidine alkaloid. Catalyzes the N-deacetylation of pyrrolizixenacetamide.","Catalyzes the hydrolysis of 2-hydroxy-6- oxononadienedioate and 2-hydroxy-6-oxononatrienedioate to 2-hydroxy-6-oxononadienedioate-2-carboxylate and 2-hydroxy-6-oxononatrienedioate-2-carboxylate, respectively. Belongs to the AB hydrolase superfamily. Lipase family",No,Maybe,No,No,No,not-Yes,GO:0052689,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016787,0.6897,0.6897,0.6897,0.6897,0.6897,5,0.6897,0.1247,no
XHPG_XENHO,A0A2G0QDP0,ProtTale,Bacteria,266,"Involved in the biosynthetic pathway of pyrrolizwilline, a pyrrolizidine alkaloid. Catalyzes the N-deacetylation of pyrrolizixenacetamide.","Involved in the biosynthesis of the siderophore enterobactin (enterochelin). Catalyzes the hydrolysis of 5-dehydro-2,3- dihydroxymuconate semialdehyde (DHMS) to yield 2,3-dihydroxymuconate semialdehyde (DHMSA).",No,No,No,No,No,not-Yes,GO:0052689,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016787,0.6897,0.6897,0.6897,0.6897,0.6897,5,0.6897,0.1247,no
XHPG_XENHO,A0A2G0QDP0,Protein2Text,Bacteria,266,"Involved in the biosynthetic pathway of pyrrolizwilline, a pyrrolizidine alkaloid. Catalyzes the N-deacetylation of pyrrolizixenacetamide.","This protein is involved in the degradation of a specific type of compound, which is a type of molecular function. However, without more specific information, it is difficult to determine the exact molecular function of this protein. Further research would be necessary to determine the precise molecular function of this protein.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0052689,,,,,,,,,,,0,,0.1247,no
XHPG_XENHO,A0A2G0QDP0,Reference,Bacteria,266,"Involved in the biosynthetic pathway of pyrrolizwilline, a pyrrolizidine alkaloid. Catalyzes the N-deacetylation of pyrrolizixenacetamide.","Involved in the biosynthetic pathway of pyrrolizwilline, a pyrrolizidine alkaloid. Catalyzes the N-deacetylation of pyrrolizixenacetamide.",,,,,,,GO:0052689,GO:0016811,GO:0016811,GO:0016787,GO:0016811,GO:0016811,0.4645,0.4645,0.6897,0.4645,0.4645,5,0.5095,0.1247,no
ACDB_ASPCN,A0A2I2F262,ESM2Text,Eukaryota,2498,"PKS-NRPS hybrid synthetase; part of the gene cluster that mediates the biosynthesis of aspcandine, a pyrrolobenzazepine alkaloid. Initially, the indoleamine 2,3-dioxygenase acdA accepts L-tryptophan and performs the oxidative opening of the indole ring to yield N'-formyl-L-kynurenine, which undergoes the spontaneous deformylation reaction to provide L-kynurenine. The kynurenine 3-monooxygenase acdD then hydroxylates L-kynurenine to afford 3-hydroxy-L-kynurenine. 3-hydroxy-L-kynurenine is activated by the A domain of the NRPS-PKS acdB and subsequently loaded onto the enzyme. The KS domain conducts the decarboxylative condensation of the 3-hydroxy-L-kynurenyl and malonyl moieties, and subsequent nucleophilic attacks by the two amino groups would occur nonenzymatically at two distinct positions, achieving the chain release and the construction of the tricyclic system. Finally, a dehydration reaction completes the biosynthesis to yield aspcandine.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcs",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0016874; GO:0016491; GO:0031177,,,,,,,,,,,0,,0.2905,no
ACDB_ASPCN,A0A2I2F262,Prot2Text,Eukaryota,2498,"PKS-NRPS hybrid synthetase; part of the gene cluster that mediates the biosynthesis of aspcandine, a pyrrolobenzazepine alkaloid. Initially, the indoleamine 2,3-dioxygenase acdA accepts L-tryptophan and performs the oxidative opening of the indole ring to yield N'-formyl-L-kynurenine, which undergoes the spontaneous deformylation reaction to provide L-kynurenine. The kynurenine 3-monooxygenase acdD then hydroxylates L-kynurenine to afford 3-hydroxy-L-kynurenine. 3-hydroxy-L-kynurenine is activated by the A domain of the NRPS-PKS acdB and subsequently loaded onto the enzyme. The KS domain conducts the decarboxylative condensation of the 3-hydroxy-L-kynurenyl and malonyl moieties, and subsequent nucleophilic attacks by the two amino groups would occur nonenzymatically at two distinct positions, achieving the chain release and the construction of the tricyclic system. Finally, a dehydration reaction completes the biosynthesis to yield aspcandine.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcs",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0016874; GO:0016491; GO:0031177,GO:0016874,,,GO:0016874,GO:0016874; GO:0005524,0.6145,,,0.6145,0.6104,3,0.6131,0.2905,no
ACDB_ASPCN,A0A2I2F262,ProtT3,Eukaryota,2498,"PKS-NRPS hybrid synthetase; part of the gene cluster that mediates the biosynthesis of aspcandine, a pyrrolobenzazepine alkaloid. Initially, the indoleamine 2,3-dioxygenase acdA accepts L-tryptophan and performs the oxidative opening of the indole ring to yield N'-formyl-L-kynurenine, which undergoes the spontaneous deformylation reaction to provide L-kynurenine. The kynurenine 3-monooxygenase acdD then hydroxylates L-kynurenine to afford 3-hydroxy-L-kynurenine. 3-hydroxy-L-kynurenine is activated by the A domain of the NRPS-PKS acdB and subsequently loaded onto the enzyme. The KS domain conducts the decarboxylative condensation of the 3-hydroxy-L-kynurenyl and malonyl moieties, and subsequent nucleophilic attacks by the two amino groups would occur nonenzymatically at two distinct positions, achieving the chain release and the construction of the tricyclic system. Finally, a dehydration reaction completes the biosynthesis to yield aspcandine.",Involved in the biosynthesis of the siderophore enterobactin. Catalyzes the ATP-dependent activation of the acyl carrier protein (ACP) enterobactin synthetase (EntS). Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family,No,No,No,No,No,not-Yes,GO:0004312; GO:0016874; GO:0016491; GO:0031177,GO:0004315,GO:0004315,,GO:0016874; GO:0005524,GO:0004315,0.4499,0.4499,,0.6104,0.4499,4,0.49,0.2905,no
ACDB_ASPCN,A0A2I2F262,ProtTale,Eukaryota,2498,"PKS-NRPS hybrid synthetase; part of the gene cluster that mediates the biosynthesis of aspcandine, a pyrrolobenzazepine alkaloid. Initially, the indoleamine 2,3-dioxygenase acdA accepts L-tryptophan and performs the oxidative opening of the indole ring to yield N'-formyl-L-kynurenine, which undergoes the spontaneous deformylation reaction to provide L-kynurenine. The kynurenine 3-monooxygenase acdD then hydroxylates L-kynurenine to afford 3-hydroxy-L-kynurenine. 3-hydroxy-L-kynurenine is activated by the A domain of the NRPS-PKS acdB and subsequently loaded onto the enzyme. The KS domain conducts the decarboxylative condensation of the 3-hydroxy-L-kynurenyl and malonyl moieties, and subsequent nucleophilic attacks by the two amino groups would occur nonenzymatically at two distinct positions, achieving the chain release and the construction of the tricyclic system. Finally, a dehydration reaction completes the biosynthesis to yield aspcandine.",Involved in the biosynthesis of the siderophore pyoverdine. Part of the pyoverdine biosynthesis gene cluster that mediates the biosynthesis of the siderophore pyoverdine. Pyoverdine is a hydroxamate-type siderophore but PvdQ is not required for pyoverdine biosynthesis.,No,No,No,No,No,not-Yes,GO:0004312; GO:0016874; GO:0016491; GO:0031177,,,,,,,,,,,0,,0.2905,no
ACDB_ASPCN,A0A2I2F262,Protein2Text,Eukaryota,2498,"PKS-NRPS hybrid synthetase; part of the gene cluster that mediates the biosynthesis of aspcandine, a pyrrolobenzazepine alkaloid. Initially, the indoleamine 2,3-dioxygenase acdA accepts L-tryptophan and performs the oxidative opening of the indole ring to yield N'-formyl-L-kynurenine, which undergoes the spontaneous deformylation reaction to provide L-kynurenine. The kynurenine 3-monooxygenase acdD then hydroxylates L-kynurenine to afford 3-hydroxy-L-kynurenine. 3-hydroxy-L-kynurenine is activated by the A domain of the NRPS-PKS acdB and subsequently loaded onto the enzyme. The KS domain conducts the decarboxylative condensation of the 3-hydroxy-L-kynurenyl and malonyl moieties, and subsequent nucleophilic attacks by the two amino groups would occur nonenzymatically at two distinct positions, achieving the chain release and the construction of the tricyclic system. Finally, a dehydration reaction completes the biosynthesis to yield aspcandine.","This protein is involved in the synthesis of a polyketide molecule, which is a class of natural products with diverse biological activities. More specifically, it is involved in the synthesis of a polyketide precursor that is used as a building block for the production of a secondary metabolite. The molecular function of this protein is to catalyze the condensation of acetyl-CoA and malonyl-CoA to form a polyketide chain. This reaction is a key step in the biosynthesis of many natural products, including antibiotics, antifungals, and other secondary metabolites.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0016874; GO:0016491; GO:0031177,,GO:0004315,,GO:0016746,GO:0004315,,0.4499,,0.5052,0.4499,3,0.4683,0.2905,no
ACDB_ASPCN,A0A2I2F262,Reference,Eukaryota,2498,"PKS-NRPS hybrid synthetase; part of the gene cluster that mediates the biosynthesis of aspcandine, a pyrrolobenzazepine alkaloid. Initially, the indoleamine 2,3-dioxygenase acdA accepts L-tryptophan and performs the oxidative opening of the indole ring to yield N'-formyl-L-kynurenine, which undergoes the spontaneous deformylation reaction to provide L-kynurenine. The kynurenine 3-monooxygenase acdD then hydroxylates L-kynurenine to afford 3-hydroxy-L-kynurenine. 3-hydroxy-L-kynurenine is activated by the A domain of the NRPS-PKS acdB and subsequently loaded onto the enzyme. The KS domain conducts the decarboxylative condensation of the 3-hydroxy-L-kynurenyl and malonyl moieties, and subsequent nucleophilic attacks by the two amino groups would occur nonenzymatically at two distinct positions, achieving the chain release and the construction of the tricyclic system. Finally, a dehydration reaction completes the biosynthesis to yield aspcandine.","PKS-NRPS hybrid synthetase; part of the gene cluster that mediates the biosynthesis of aspcandine, a pyrrolobenzazepine alkaloid. Initially, the indoleamine 2,3-dioxygenase acdA accepts L-tryptophan and performs the oxidative opening of the indole ring to yield N'-formyl-L-kynurenine, which undergoes the spontaneous deformylation reaction to provide L-kynurenine. The kynurenine 3-monooxygenase acdD then hydroxylates L-kynurenine to afford 3-hydroxy-L-kynurenine. 3-hydroxy-L-kynurenine is activated by the A domain of the NRPS-PKS acdB and subsequently loaded onto the enzyme. The KS domain conducts the decarboxylative condensation of the 3-hydroxy-L-kynurenyl and malonyl moieties, and subsequent nucleophilic attacks by the two amino groups would occur nonenzymatically at two distinct positions, achieving the chain release and the construction of the tricyclic system. Finally, a dehydration reaction completes the biosynthesis to yield aspcandine.",,,,,,,GO:0004312; GO:0016874; GO:0016491; GO:0031177,GO:0016746; GO:0016874,GO:0016874; GO:0016746,GO:0016746; GO:0016874,GO:0016874,GO:0016874,0.6958,0.6958,0.6958,0.6145,0.6145,5,0.6633,0.2905,no
FAD1_CHLRE,A0A2K3D179,ESM2Text,Eukaryota,582,This enzyme has two activities: FAD synthase and FAD diphosphatase activity. Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. Also exhibits FAD diphosphatase activity.,Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0003919,GO:0003919,GO:0003919,GO:0003919,GO:0003919,GO:0003919,0.6832,0.6832,0.6832,0.6832,0.6832,5,0.6832,0.2816,no
FAD1_CHLRE,A0A2K3D179,Prot2Text,Eukaryota,582,This enzyme has two activities: FAD synthase and FAD diphosphatase activity. Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. Also exhibits FAD diphosphatase activity.,Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0003919,GO:0003919,GO:0003919,GO:0003919,GO:0003919,GO:0003919,0.6832,0.6832,0.6832,0.6832,0.6832,5,0.6832,0.2816,no
FAD1_CHLRE,A0A2K3D179,ProtT3,Eukaryota,582,This enzyme has two activities: FAD synthase and FAD diphosphatase activity. Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. Also exhibits FAD diphosphatase activity.,Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. In the C-terminal section; belongs to the PAPS reductase family. FAD1 subfamily. In the N-terminal section; belongs to the MoaB/Mog family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0003919,GO:0003919,GO:0003919,GO:0003919; GO:0005524,GO:0003919,GO:0003919,0.6832,0.6832,1.0,0.6832,0.6832,5,0.7466,0.2816,no
FAD1_CHLRE,A0A2K3D179,ProtTale,Eukaryota,582,This enzyme has two activities: FAD synthase and FAD diphosphatase activity. Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. Also exhibits FAD diphosphatase activity.,Catalyzes the hydrolysis of acetyl-coenzyme A (acetyl-CoA) to acetate and CoA.,No,No,No,No,No,not-Yes,GO:0005524; GO:0003919,GO:0016790,GO:0003995,GO:0016790,GO:0016790,GO:0016790,0.1589,0.1343,0.1589,0.1589,0.1589,5,0.154,0.2816,no
FAD1_CHLRE,A0A2K3D179,Protein2Text,Eukaryota,582,This enzyme has two activities: FAD synthase and FAD diphosphatase activity. Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. Also exhibits FAD diphosphatase activity.,"The molecular function of this protein is a nucleotidyltransferase, which is an enzyme that catalyzes the transfer of a nucleotide group from a nucleotide triphosphate to a nucleotide diphosphate.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0003919,GO:0016779,GO:0016779,GO:0016779,GO:0016779,GO:0016779,0.5237,0.5237,0.5237,0.5237,0.5237,5,0.5237,0.2816,no
FAD1_CHLRE,A0A2K3D179,Reference,Eukaryota,582,This enzyme has two activities: FAD synthase and FAD diphosphatase activity. Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. Also exhibits FAD diphosphatase activity.,This enzyme has two activities: FAD synthase and FAD diphosphatase activity. Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. Also exhibits FAD diphosphatase activity.,,,,,,,GO:0005524; GO:0003919,GO:0003919; GO:0016787,GO:0003919,GO:0003919; GO:0016787,GO:0003919; GO:0016787,GO:0003919; GO:0016462,0.6012,0.6832,0.6012,0.6012,0.5573,5,0.6088,0.2816,no
ARGI_GLAA1,A0A2R2JFW7,ESM2Text,Eukaryota,345,"Cold-active L-arginase that catalyzes the hydrolysis of L- arginine to L-ornithine and urea, an essential reaction in the urea cycle for toxic ammonia removal and cell proliferation. Is not able to use D-arginine or L-canavanine as substrates.",Catalyzes the hydrolysis of N-formimidoyl-L-glutamate to formamide and L-glutamate. May be involved in urea and/or L-aspartate utilization.,No,No,No,No,Maybe,not-Yes,GO:0004053; GO:0030145,GO:0016787,GO:0016787,,GO:0016787,,0.4442,0.4442,,0.4442,,3,0.4442,0.2411,no
ARGI_GLAA1,A0A2R2JFW7,Prot2Text,Eukaryota,345,"Cold-active L-arginase that catalyzes the hydrolysis of L- arginine to L-ornithine and urea, an essential reaction in the urea cycle for toxic ammonia removal and cell proliferation. Is not able to use D-arginine or L-canavanine as substrates.","Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high-temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the decarboxylation of N1-(3-aminopropyl)agmatine to yield spermidine and urea.",No,No,No,No,No,not-Yes,GO:0004053; GO:0030145,GO:0016831,,GO:0016831,GO:0016831,GO:0016831,0.1843,,0.1843,0.1843,0.1843,4,0.1843,0.2411,no
ARGI_GLAA1,A0A2R2JFW7,ProtT3,Eukaryota,345,"Cold-active L-arginase that catalyzes the hydrolysis of L- arginine to L-ornithine and urea, an essential reaction in the urea cycle for toxic ammonia removal and cell proliferation. Is not able to use D-arginine or L-canavanine as substrates.",Belongs to the arginase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004053; GO:0030145,GO:0004053,GO:0004053,GO:0004053,GO:0004053,GO:0004053,0.6895,0.6895,0.6895,0.6895,0.6895,5,0.6895,0.2411,no
ARGI_GLAA1,A0A2R2JFW7,ProtTale,Eukaryota,345,"Cold-active L-arginase that catalyzes the hydrolysis of L- arginine to L-ornithine and urea, an essential reaction in the urea cycle for toxic ammonia removal and cell proliferation. Is not able to use D-arginine or L-canavanine as substrates.",Catalyzes the conversion of N-formimidoyl-L-arginine to N-formimidoyl-L-ornithine.,Maybe,No,No,No,No,not-Yes,GO:0004053; GO:0030145,GO:0016787,GO:0003824,,,GO:0016787,0.4442,0.3646,,,0.4442,3,0.4177,0.2411,no
ARGI_GLAA1,A0A2R2JFW7,Protein2Text,Eukaryota,345,"Cold-active L-arginase that catalyzes the hydrolysis of L- arginine to L-ornithine and urea, an essential reaction in the urea cycle for toxic ammonia removal and cell proliferation. Is not able to use D-arginine or L-canavanine as substrates.","The molecular function of this protein is to catalyze the hydrolysis of arginine to ornithine and urea. It is a key enzyme in the urea cycle and plays a crucial role in nitrogen metabolism. Specifically, it catalyzes the conversion of arginine to ornithine and urea, which is then excreted by the kidneys. This reaction is an important step in the breakdown of dietary nitrogen and the removal of excess nitrogen from the body.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004053; GO:0030145,GO:0004053,GO:0004053,GO:0004053,GO:0004053,GO:0004053,0.6895,0.6895,0.6895,0.6895,0.6895,5,0.6895,0.2411,no
ARGI_GLAA1,A0A2R2JFW7,Reference,Eukaryota,345,"Cold-active L-arginase that catalyzes the hydrolysis of L- arginine to L-ornithine and urea, an essential reaction in the urea cycle for toxic ammonia removal and cell proliferation. Is not able to use D-arginine or L-canavanine as substrates.","Cold-active L-arginase that catalyzes the hydrolysis of L- arginine to L-ornithine and urea, an essential reaction in the urea cycle for toxic ammonia removal and cell proliferation. Is not able to use D-arginine or L-canavanine as substrates.",,,,,,,GO:0004053; GO:0030145,GO:0004053,GO:0004053,GO:0004053,GO:0004053,GO:0004053,0.6895,0.6895,0.6895,0.6895,0.6895,5,0.6895,0.2411,no
DPP9_DANRE,A0A2R8QP51,ESM2Text,Eukaryota,885,Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. Acts as a key inhibitor of the NLRP1 inflammasome.,"Cell surface glycoprotein whose activity is associated with subcellular aggregation, oligomeric assembly, and proteolysis. Has a dipeptidyl-peptidase activity that removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. May act as an oligopeptidase, in association with serum protein F1-alpha (S100A), which is essential for the maintenance of secretory vesicle secretions.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004177; GO:0008239; GO:0008236,GO:0004274,GO:0004274,GO:0008239,GO:0008239,GO:0004274,0.0,0.0,0.8405,0.8405,0.0,5,0.3362,0.7119,yes
DPP9_DANRE,A0A2R8QP51,Prot2Text,Eukaryota,885,Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. Acts as a key inhibitor of the NLRP1 inflammasome.,Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. Has an absolute requirement for an X-Pro bond in the trans configuration immediately preceding the Pro-Y scissible bond.,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0004177; GO:0008239; GO:0008236,GO:0004287,GO:0004287,GO:0004252,GO:0004252,GO:0004252,0.0,0.0,0.6578,0.6578,0.6578,5,0.3947,0.7119,yes
DPP9_DANRE,A0A2R8QP51,ProtT3,Eukaryota,885,Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. Acts as a key inhibitor of the NLRP1 inflammasome.,Dipeptidyl peptidase that removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N- termini provided that the penultimate residue is proline (By similarity). Acts as a negative regulator of endoplasmic reticulum-associated degradation (ERAD) (By similarity). Cytoplasm Endoplasmic reticulum. Belongs to the peptidase S9B family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004177; GO:0008239; GO:0008236,GO:0004274,GO:0004274,GO:0008239,GO:0008239,GO:0004274,0.0,0.0,0.8405,0.8405,0.0,5,0.3362,0.7119,yes
DPP9_DANRE,A0A2R8QP51,ProtTale,Eukaryota,885,Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. Acts as a key inhibitor of the NLRP1 inflammasome.,Dipeptidyl-peptidase-like protein which may play a role in the regulation of cell wall integrity.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004177; GO:0008239; GO:0008236,,,,,,,,,,,0,,0.7119,yes
DPP9_DANRE,A0A2R8QP51,Protein2Text,Eukaryota,885,Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. Acts as a key inhibitor of the NLRP1 inflammasome.,"The molecular function of the protein is as a deamidase, which means it removes an amide group from a molecule, typically from glutamine or asparagine residues.",No,No,No,No,No,not-Yes,GO:0004177; GO:0008239; GO:0008236,GO:0016810,GO:0016811,GO:0016810,GO:0016810,,0.4503,0.3771,0.4503,0.4503,,4,0.432,0.7119,yes
DPP9_DANRE,A0A2R8QP51,Reference,Eukaryota,885,Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. Acts as a key inhibitor of the NLRP1 inflammasome.,Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. Acts as a key inhibitor of the NLRP1 inflammasome.,,,,,,,GO:0004177; GO:0008239; GO:0008236,GO:0008239,GO:0008239,GO:0008239,GO:0008239,GO:0008239,0.8405,0.8405,0.8405,0.8405,0.8405,5,0.8405,0.7119,yes
XYN1_PENPR,A0A2U7QU15,ESM2Text,Eukaryota,404,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Efficiently hydrolyzes different xylans including beechwood xylan, birchwood xylan, or oat spelt xylanand; as well as xylo- oligosaccharides (XOS) except xylobiose. The main hydrolytic product is xylobiose, followed by xylotriose and unidentified longer XOS. A small amount of xylose appears with extended hydrolysis time. Also produces feruloylated oligosaccharides (FOs) from wheat bran.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0030248; GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,0.6973,0.6973,0.6973,0.6973,0.6973,5,0.6973,0.275,no
XYN1_PENPR,A0A2U7QU15,Prot2Text,Eukaryota,404,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Efficiently hydrolyzes different xylans including beechwood xylan, birchwood xylan, or oat spelt xylanand; as well as xylo- oligosaccharides (XOS) except xylobiose. The main hydrolytic product is xylobiose, followed by xylotriose and unidentified longer XOS. A small amount of xylose appears with extended hydrolysis time. Also produces feruloylated oligosaccharides (FOs) from wheat bran.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0030248; GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,0.6973,0.6973,0.6973,0.6973,0.6973,5,0.6973,0.275,no
XYN1_PENPR,A0A2U7QU15,ProtT3,Eukaryota,404,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Efficiently hydrolyzes different xylans including beechwood xylan, birchwood xylan, or oat spelt xylanand; as well as xylo- oligosaccharides (XOS) except xylobiose. The main hydrolytic product is xylobiose, followed by xylotriose and unidentified longer XOS. A small amount of xylose appears with extended hydrolysis time. Also produces feruloylated oligosaccharides (FOs) from wheat bran.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Secreted. Belongs to the glycosyl hydrolase 10 (cellulase F) family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0030248; GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,0.6973,0.6973,0.6973,0.6973,0.6973,5,0.6973,0.275,no
XYN1_PENPR,A0A2U7QU15,ProtTale,Eukaryota,404,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Efficiently hydrolyzes different xylans including beechwood xylan, birchwood xylan, or oat spelt xylanand; as well as xylo- oligosaccharides (XOS) except xylobiose. The main hydrolytic product is xylobiose, followed by xylotriose and unidentified longer XOS. A small amount of xylose appears with extended hydrolysis time. Also produces feruloylated oligosaccharides (FOs) from wheat bran.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0030248; GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,0.6973,0.6973,0.6973,0.6973,0.6973,5,0.6973,0.275,no
XYN1_PENPR,A0A2U7QU15,Protein2Text,Eukaryota,404,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Efficiently hydrolyzes different xylans including beechwood xylan, birchwood xylan, or oat spelt xylanand; as well as xylo- oligosaccharides (XOS) except xylobiose. The main hydrolytic product is xylobiose, followed by xylotriose and unidentified longer XOS. A small amount of xylose appears with extended hydrolysis time. Also produces feruloylated oligosaccharides (FOs) from wheat bran.","The molecular function of this protein is endoglucanase activity, which means it catalyzes the hydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, a complex carbohydrate. This enzyme is likely involved in the breakdown of cellulose, a process that is essential for the utilization of cellulose as a carbon source by the organism.",No,No,No,No,Maybe,not-Yes,GO:0030248; GO:0031176,GO:0008810,GO:0008810,GO:0008810,GO:0008810,GO:0008810,0.4572,0.4572,0.4572,0.4572,0.4572,5,0.4572,0.275,no
XYN1_PENPR,A0A2U7QU15,Reference,Eukaryota,404,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Efficiently hydrolyzes different xylans including beechwood xylan, birchwood xylan, or oat spelt xylanand; as well as xylo- oligosaccharides (XOS) except xylobiose. The main hydrolytic product is xylobiose, followed by xylotriose and unidentified longer XOS. A small amount of xylose appears with extended hydrolysis time. Also produces feruloylated oligosaccharides (FOs) from wheat bran.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Efficiently hydrolyzes different xylans including beechwood xylan, birchwood xylan, or oat spelt xylanand; as well as xylo- oligosaccharides (XOS) except xylobiose. The main hydrolytic product is xylobiose, followed by xylotriose and unidentified longer XOS. A small amount of xylose appears with extended hydrolysis time. Also produces feruloylated oligosaccharides (FOs) from wheat bran.",,,,,,,GO:0030248; GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,0.6973,0.6973,0.6973,0.6973,0.6973,5,0.6973,0.275,no
XYN3_PENPR,A0A2U7R6V5,ESM2Text,Eukaryota,220,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Efficiently hydrolyzes different xylans including beechwood xylan, birchwood xylan, or oat spelt xylanand; as well as xylo-oligosaccharides (XOS) except xylobiose. Xylotriose, xylobiose, and some longer XOS were the main hydrolytic products. Xyn also partially degrades xylotriose to xylobiose and xylose, and the longer XOS (X4 to X6) are also efficiently hydrolyzed. Also produces feruloylated oligosaccharides (FOs) from wheat bran.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3856,no
XYN3_PENPR,A0A2U7R6V5,Prot2Text,Eukaryota,220,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Efficiently hydrolyzes different xylans including beechwood xylan, birchwood xylan, or oat spelt xylanand; as well as xylo-oligosaccharides (XOS) except xylobiose. Xylotriose, xylobiose, and some longer XOS were the main hydrolytic products. Xyn also partially degrades xylotriose to xylobiose and xylose, and the longer XOS (X4 to X6) are also efficiently hydrolyzed. Also produces feruloylated oligosaccharides (FOs) from wheat bran.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3856,no
XYN3_PENPR,A0A2U7R6V5,ProtT3,Eukaryota,220,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Efficiently hydrolyzes different xylans including beechwood xylan, birchwood xylan, or oat spelt xylanand; as well as xylo-oligosaccharides (XOS) except xylobiose. Xylotriose, xylobiose, and some longer XOS were the main hydrolytic products. Xyn also partially degrades xylotriose to xylobiose and xylose, and the longer XOS (X4 to X6) are also efficiently hydrolyzed. Also produces feruloylated oligosaccharides (FOs) from wheat bran.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Secreted. Belongs to the glycosyl hydrolase 11 (cellulase G) family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3856,no
XYN3_PENPR,A0A2U7R6V5,ProtTale,Eukaryota,220,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Efficiently hydrolyzes different xylans including beechwood xylan, birchwood xylan, or oat spelt xylanand; as well as xylo-oligosaccharides (XOS) except xylobiose. Xylotriose, xylobiose, and some longer XOS were the main hydrolytic products. Xyn also partially degrades xylotriose to xylobiose and xylose, and the longer XOS (X4 to X6) are also efficiently hydrolyzed. Also produces feruloylated oligosaccharides (FOs) from wheat bran.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3856,no
XYN3_PENPR,A0A2U7R6V5,Protein2Text,Eukaryota,220,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Efficiently hydrolyzes different xylans including beechwood xylan, birchwood xylan, or oat spelt xylanand; as well as xylo-oligosaccharides (XOS) except xylobiose. Xylotriose, xylobiose, and some longer XOS were the main hydrolytic products. Xyn also partially degrades xylotriose to xylobiose and xylose, and the longer XOS (X4 to X6) are also efficiently hydrolyzed. Also produces feruloylated oligosaccharides (FOs) from wheat bran.","The molecular function of this protein is involved in the breakdown of complex carbohydrates, specifically in hydrolyzing the polysaccharide components of plant cell walls. More specifically, it is involved in the degradation of xyloglucan, a major component of plant cell walls. This protein is likely to be a glycoside hydrolase, which is a class of enzymes that break down complex carbohydrates into simpler sugars. It is likely to have a role in the degradation of plant biomass, which is a key process in the decomposition of plant material in the environment.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0031176,GO:0004553,GO:0016798,GO:0016798,GO:0016798,GO:0004553,0.7539,0.6466,0.6466,0.6466,0.7539,5,0.6895,0.3856,no
XYN3_PENPR,A0A2U7R6V5,Reference,Eukaryota,220,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Efficiently hydrolyzes different xylans including beechwood xylan, birchwood xylan, or oat spelt xylanand; as well as xylo-oligosaccharides (XOS) except xylobiose. Xylotriose, xylobiose, and some longer XOS were the main hydrolytic products. Xyn also partially degrades xylotriose to xylobiose and xylose, and the longer XOS (X4 to X6) are also efficiently hydrolyzed. Also produces feruloylated oligosaccharides (FOs) from wheat bran.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Efficiently hydrolyzes different xylans including beechwood xylan, birchwood xylan, or oat spelt xylanand; as well as xylo-oligosaccharides (XOS) except xylobiose. Xylotriose, xylobiose, and some longer XOS were the main hydrolytic products. Xyn also partially degrades xylotriose to xylobiose and xylose, and the longer XOS (X4 to X6) are also efficiently hydrolyzed. Also produces feruloylated oligosaccharides (FOs) from wheat bran.",,,,,,,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3856,no
OKAG_PENOH,A0A2Z5U3C2,ESM2Text,Eukaryota,538,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four-membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaG acts as a 2,3-diol synthase that installs 2,3-diol on the okaramine scaffold to convert 12-deshydroxyl okaramine E into 3-desmethyl okaramine B. OkaG is also able to produce use okaramine E and produce okaramine D with the help of the methyltransferase okaF. The biosynthesis begins with the NRPS okaA that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8- (alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L- Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.","Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome P450 monooxygenase P450-2 then catalyzes the dimerization of nataloe-emodin to cladofulvin.",No,No,No,No,No,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497; GO:0020037,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.8149,0.5872,0.5872,0.5872,0.5872,5,0.6327,0.2705,no
OKAG_PENOH,A0A2Z5U3C2,Prot2Text,Eukaryota,538,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four-membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaG acts as a 2,3-diol synthase that installs 2,3-diol on the okaramine scaffold to convert 12-deshydroxyl okaramine E into 3-desmethyl okaramine B. OkaG is also able to produce use okaramine E and produce okaramine D with the help of the methyltransferase okaF. The biosynthesis begins with the NRPS okaA that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8- (alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L- Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase penM leads to a epoxidized-GGI that is substrate of the terpene cyclase penB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase penP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase penQ. Paxilline is converted to beta-paxitriol via C-10",No,No,No,No,No,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.2097,0.2097,0.2097,0.2097,0.2097,5,0.2097,0.2705,no
OKAG_PENOH,A0A2Z5U3C2,ProtT3,Eukaryota,538,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four-membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaG acts as a 2,3-diol synthase that installs 2,3-diol on the okaramine scaffold to convert 12-deshydroxyl okaramine E into 3-desmethyl okaramine B. OkaG is also able to produce use okaramine E and produce okaramine D with the help of the methyltransferase okaF. The biosynthesis begins with the NRPS okaA that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8- (alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L- Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.","Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By similarity). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (By similarity). Further epoxidation by the FAD-dependent monooxygenase ausM and",No,No,No,No,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497; GO:0020037,GO:0004497; GO:0020037,GO:0004497; GO:0020037; GO:0005506,GO:0004497; GO:0020037; GO:0005506,GO:0004497,0.8149,0.8149,0.9516,0.9516,0.5872,5,0.824,0.2705,no
OKAG_PENOH,A0A2Z5U3C2,ProtTale,Eukaryota,538,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four-membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaG acts as a 2,3-diol synthase that installs 2,3-diol on the okaramine scaffold to convert 12-deshydroxyl okaramine E into 3-desmethyl okaramine B. OkaG is also able to produce use okaramine E and produce okaramine D with the help of the methyltransferase okaF. The biosynthesis begins with the NRPS okaA that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8- (alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L- Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.","Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. Within the pathway, PC-2 catalyzes the oxidation of penitrem D to penitrem E. The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3-glycerol phosphate with GGPP by penC then forms 3-geranylgeranylindole (3-",No,No,No,No,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0020037,GO:0004497,GO:0004497,0.5872,0.9516,0.8149,0.5872,0.5872,5,0.7056,0.2705,no
OKAG_PENOH,A0A2Z5U3C2,Protein2Text,Eukaryota,538,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four-membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaG acts as a 2,3-diol synthase that installs 2,3-diol on the okaramine scaffold to convert 12-deshydroxyl okaramine E into 3-desmethyl okaramine B. OkaG is also able to produce use okaramine E and produce okaramine D with the help of the methyltransferase okaF. The biosynthesis begins with the NRPS okaA that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8- (alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L- Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.","This protein is a cytochrome P450 monooxygenase. It is involved in the catalysis of various reactions, including the oxidation of organic substrates, and plays a crucial role in the biosynthesis of secondary metabolites. The molecular function of this protein is likely to be involved in the oxidation of specific substrates, possibly in the biosynthesis of secondary metabolites, such as terpenoids, alkaloids, or polyketides. However, without more specific information, it is difficult to determine the exact molecular function of this protein. 

Note: The molecular function of a protein can be inferred from its sequence, structure, and the biochemical reactions it catalyzes, but it can also be experimentally confirmed through various biochemical and biophysical assays. In this case, the molecular function of this protein is not explicitly stated in the provided text, but it can be inferred based on its classification as a cytochrome P450 monooxygenase.",No,No,No,No,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.5872,0.5872,0.5872,0.5872,0.5872,5,0.5872,0.2705,no
OKAG_PENOH,A0A2Z5U3C2,Reference,Eukaryota,538,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four-membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaG acts as a 2,3-diol synthase that installs 2,3-diol on the okaramine scaffold to convert 12-deshydroxyl okaramine E into 3-desmethyl okaramine B. OkaG is also able to produce use okaramine E and produce okaramine D with the help of the methyltransferase okaF. The biosynthesis begins with the NRPS okaA that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8- (alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L- Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four-membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaG acts as a 2,3-diol synthase that installs 2,3-diol on the okaramine scaffold to convert 12-deshydroxyl okaramine E into 3-desmethyl okaramine B. OkaG is also able to produce use okaramine E and produce okaramine D with the help of the methyltransferase okaF. The biosynthesis begins with the NRPS okaA that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8- (alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L- Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.",,,,,,,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0016874,GO:0016874,GO:0004497,GO:0016874,GO:0004497,0.3569,0.3569,0.5872,0.3569,0.5872,5,0.449,0.2705,no
OKAA_PENOH,A0A2Z5UHX0,ESM2Text,Eukaryota,1981,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four-membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaA acts as a bimodular non-ribosomal peptide synthetase (NRPS) that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8-(alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime- thylallyl)-L-Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of aspirochlorine (or antibiotic A30641), an unusual halogenated spiro compound with distinctive antifungal properties due to selective inhibition of protein biosynthesis, and which is also active against bacteria, viruses, and murine tumor cells. The non-ribosomal peptide synthetase (NRPS) aclP is responsible the formation of the diketopiperazine (DKP) core from the condensation of 2 phenylalanine residues. One Phe residue is tailored into chlorotyrosine by hydroxylation and chlorination, whereas the second Phe undergoes an unprecedented C-C bond cleavage to be converted into glycine. After formation of the DKP, sulfur is incorporated into the DKP by conjugation with glutathione by aclG, followed by its stepwise degradation to the thiol by aclI, aclJ and aclK, and the dithiol oxidation by aclT. In addition, oxygenases (aclB, aclC, aclL and aclO) and O-methyltransferases (aclM and",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,,,,,,,,,,,0,,0.3103,no
OKAA_PENOH,A0A2Z5UHX0,Prot2Text,Eukaryota,1981,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four-membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaA acts as a bimodular non-ribosomal peptide synthetase (NRPS) that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8-(alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime- thylallyl)-L-Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcs",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,GO:0016874,,,GO:0016874,GO:0016874; GO:0005524,0.709,,,0.709,0.6793,3,0.6991,0.3103,no
OKAA_PENOH,A0A2Z5UHX0,ProtT3,Eukaryota,1981,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four-membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaA acts as a bimodular non-ribosomal peptide synthetase (NRPS) that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8-(alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime- thylallyl)-L-Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,GO:0016874; GO:0005524,GO:0016874,,GO:0016874; GO:0031177,GO:0016874; GO:0005524,0.6793,0.709,,1.0,0.6793,4,0.7669,0.3103,no
OKAA_PENOH,A0A2Z5UHX0,ProtTale,Eukaryota,1981,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four-membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaA acts as a bimodular non-ribosomal peptide synthetase (NRPS) that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8-(alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime- thylallyl)-L-Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3- hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,GO:0016491,GO:0016874,,,GO:0016874,0.4358,0.709,,,0.709,3,0.6179,0.3103,no
OKAA_PENOH,A0A2Z5UHX0,Protein2Text,Eukaryota,1981,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four-membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaA acts as a bimodular non-ribosomal peptide synthetase (NRPS) that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8-(alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime- thylallyl)-L-Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.",This protein is involved in the molecular function of catalyzing the synthesis of nucleic acids.,No,No,No,No,No,not-Yes,GO:0016874; GO:0031177,,,,,,,,,,,0,,0.3103,no
OKAA_PENOH,A0A2Z5UHX0,Reference,Eukaryota,1981,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four-membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaA acts as a bimodular non-ribosomal peptide synthetase (NRPS) that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8-(alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime- thylallyl)-L-Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four-membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaA acts as a bimodular non-ribosomal peptide synthetase (NRPS) that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8-(alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime- thylallyl)-L-Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.",,,,,,,GO:0016874; GO:0031177,GO:0016874,GO:0016874,GO:0016874,GO:0016874,GO:0016874,0.709,0.709,0.709,0.709,0.709,5,0.709,0.3103,no
CARM1_SCHMA,A0A3Q0KHE7,ESM2Text,Eukaryota,737,Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in proteins. May methylate histone H3 and activate transcription via chromatin remodeling. Involved in the development of the reproductive organs during worm maturation (Probable).,Arginine methyltransferase that catalyzes the formation of omega-N monomethylarginine (MMA) from histone H3 and euchromatic transcription factor p19/RELA. Specifically mediates the asymmetric dimethylation of 'Arg-118' of p20/RELA.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0070611; GO:0042054; GO:0035242; GO:1904047,GO:0016274,GO:0016274,GO:0008469,GO:0035242,GO:0008469,0.6714,0.6714,0.0,0.677,0.0,5,0.404,0.419,no
CARM1_SCHMA,A0A3Q0KHE7,Prot2Text,Eukaryota,737,Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in proteins. May methylate histone H3 and activate transcription via chromatin remodeling. Involved in the development of the reproductive organs during worm maturation (Probable).,"Regulates erythromycin resistance by oxygenating the cytosolic iron-sulfur protein S12 (Arf1) on 'Lys-63' to form [Lys-48]-(Tyr-34). This modification is essential for fatty acid biosynthesis and consequently, pathogenicity.",No,No,No,No,No,not-Yes,GO:0070611; GO:0042054; GO:0035242; GO:1904047,,,,,,,,,,,0,,0.419,no
CARM1_SCHMA,A0A3Q0KHE7,ProtT3,Eukaryota,737,Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in proteins. May methylate histone H3 and activate transcription via chromatin remodeling. Involved in the development of the reproductive organs during worm maturation (Probable).,Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in proteins. Cytoplasm Nucleus. Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0070611; GO:0042054; GO:0035242; GO:1904047,GO:0035242,GO:0016274,GO:0016274,GO:0035242,GO:0035241,0.677,0.6714,0.6714,0.677,0.6165,5,0.6627,0.419,no
CARM1_SCHMA,A0A3Q0KHE7,ProtTale,Eukaryota,737,Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in proteins. May methylate histone H3 and activate transcription via chromatin remodeling. Involved in the development of the reproductive organs during worm maturation (Probable).,"Methylates 'Lys-48' of histone H3 (H3K48me1, H3K48me2 and H3K48me3) to produce trimethylation (H3K48me3). Shows a preference for mono-, di- and trimethylated H3K48. Does not methylate 'Lys-9' of histone H4 (H4K9me0, H4K9me1, H4K9me2, H4K9me3).",No,No,No,No,No,not-Yes,GO:0070611; GO:0042054; GO:0035242; GO:1904047,GO:0018024,GO:0018024,GO:0018024,GO:0018024,GO:0018024,0.0,0.0,0.0,0.0,0.0,5,0.0,0.419,no
CARM1_SCHMA,A0A3Q0KHE7,Protein2Text,Eukaryota,737,Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in proteins. May methylate histone H3 and activate transcription via chromatin remodeling. Involved in the development of the reproductive organs during worm maturation (Probable).,"The molecular function of this protein is a methyltransferase, which means it catalyzes the transfer of a methyl group from one molecule to another.",Maybe,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0070611; GO:0042054; GO:0035242; GO:1904047,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.4768,0.4768,0.4768,0.4768,0.4768,5,0.4768,0.419,no
CARM1_SCHMA,A0A3Q0KHE7,Reference,Eukaryota,737,Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in proteins. May methylate histone H3 and activate transcription via chromatin remodeling. Involved in the development of the reproductive organs during worm maturation (Probable).,Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in proteins. May methylate histone H3 and activate transcription via chromatin remodeling. Involved in the development of the reproductive organs during worm maturation (Probable).,,,,,,,GO:0070611; GO:0042054; GO:0035242; GO:1904047,GO:0016274,GO:0035241,GO:0016274,GO:0016274,GO:0008469,0.6714,0.6165,0.6714,0.6714,0.0,5,0.5261,0.419,no
CP305_LOCMI,A0A410UD22,ESM2Text,Eukaryota,504,"Monooxygenase, which converts L-phenylalanine into (E)/(Z)- phenylacetaldehyde oxime, a precursor of phenylacetonitrile, a pheromone that acts as an olfactory aposematic signal. Phenylacetonitrile is a precursor of hypertoxic hydrogen cyanide (HCN) and gregarious locusts that produce this pheromone are protected against bird predation. Phenylacetonitrile is also produced under crowded conditions, promoting an aversive behavior that protects locusts against cannibalism.",May have a role in neurogenesis. Acts as a cofactor of adrenal medullaoids and may be involved in the metabolism of mineralocorticoids and other metabolites.,No,Vague,Vague,Vague,No,not-Yes,GO:0020037; GO:0005506; GO:0016712; GO:0008395,,,,,,,,,,,0,,0.588,yes
CP305_LOCMI,A0A410UD22,Prot2Text,Eukaryota,504,"Monooxygenase, which converts L-phenylalanine into (E)/(Z)- phenylacetaldehyde oxime, a precursor of phenylacetonitrile, a pheromone that acts as an olfactory aposematic signal. Phenylacetonitrile is a precursor of hypertoxic hydrogen cyanide (HCN) and gregarious locusts that produce this pheromone are protected against bird predation. Phenylacetonitrile is also produced under crowded conditions, promoting an aversive behavior that protects locusts against cannibalism.","A cytochrome P450 monooxygenase involved in the metabolism of fatty acids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates fatty acids specifically at the omega-1 position displaying the highest catalytic activity for saturated fatty acids. May be involved in the oxidative metabolism of xenobiotics.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0016712; GO:0008395,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497; GO:0020037,0.541,0.541,0.541,0.541,0.7764,5,0.5881,0.588,yes
CP305_LOCMI,A0A410UD22,ProtT3,Eukaryota,504,"Monooxygenase, which converts L-phenylalanine into (E)/(Z)- phenylacetaldehyde oxime, a precursor of phenylacetonitrile, a pheromone that acts as an olfactory aposematic signal. Phenylacetonitrile is a precursor of hypertoxic hydrogen cyanide (HCN) and gregarious locusts that produce this pheromone are protected against bird predation. Phenylacetonitrile is also produced under crowded conditions, promoting an aversive behavior that protects locusts against cannibalism.","Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. Belongs to the cytochrome P450 family",Vague,Maybe,Maybe,Maybe,No,not-Yes,GO:0020037; GO:0005506; GO:0016712; GO:0008395,GO:0004497; GO:0020037,GO:0004497; GO:0020037,GO:0004497; GO:0020037,GO:0004497; GO:0020037; GO:0005506,GO:0004497,0.7764,0.7764,0.7764,0.9186,0.541,5,0.7578,0.588,yes
CP305_LOCMI,A0A410UD22,ProtTale,Eukaryota,504,"Monooxygenase, which converts L-phenylalanine into (E)/(Z)- phenylacetaldehyde oxime, a precursor of phenylacetonitrile, a pheromone that acts as an olfactory aposematic signal. Phenylacetonitrile is a precursor of hypertoxic hydrogen cyanide (HCN) and gregarious locusts that produce this pheromone are protected against bird predation. Phenylacetonitrile is also produced under crowded conditions, promoting an aversive behavior that protects locusts against cannibalism.",May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.,Vague,Vague,Vague,Vague,No,not-Yes,GO:0020037; GO:0005506; GO:0016712; GO:0008395,,,,,,,,,,,0,,0.588,yes
CP305_LOCMI,A0A410UD22,Protein2Text,Eukaryota,504,"Monooxygenase, which converts L-phenylalanine into (E)/(Z)- phenylacetaldehyde oxime, a precursor of phenylacetonitrile, a pheromone that acts as an olfactory aposematic signal. Phenylacetonitrile is a precursor of hypertoxic hydrogen cyanide (HCN) and gregarious locusts that produce this pheromone are protected against bird predation. Phenylacetonitrile is also produced under crowded conditions, promoting an aversive behavior that protects locusts against cannibalism.","The molecular function of this protein is to catalyze the conversion of cholesterol to cholest-5-ene-3beta,7alpha-diol (pregn-7-ene-3beta,16alpha-diol), a precursor for the synthesis of pregnenolone.",No,Maybe,No,Maybe,No,not-Yes,GO:0020037; GO:0005506; GO:0016712; GO:0008395,GO:0008395,GO:0008395,GO:0004497,GO:0004497,GO:0008395,0.5712,0.5712,0.541,0.541,0.5712,5,0.5591,0.588,yes
CP305_LOCMI,A0A410UD22,Reference,Eukaryota,504,"Monooxygenase, which converts L-phenylalanine into (E)/(Z)- phenylacetaldehyde oxime, a precursor of phenylacetonitrile, a pheromone that acts as an olfactory aposematic signal. Phenylacetonitrile is a precursor of hypertoxic hydrogen cyanide (HCN) and gregarious locusts that produce this pheromone are protected against bird predation. Phenylacetonitrile is also produced under crowded conditions, promoting an aversive behavior that protects locusts against cannibalism.","Monooxygenase, which converts L-phenylalanine into (E)/(Z)- phenylacetaldehyde oxime, a precursor of phenylacetonitrile, a pheromone that acts as an olfactory aposematic signal. Phenylacetonitrile is a precursor of hypertoxic hydrogen cyanide (HCN) and gregarious locusts that produce this pheromone are protected against bird predation. Phenylacetonitrile is also produced under crowded conditions, promoting an aversive behavior that protects locusts against cannibalism.",,,,,,,GO:0020037; GO:0005506; GO:0016712; GO:0008395,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.541,0.541,0.541,0.541,0.541,5,0.541,0.588,yes
SZNE_STRC2,A0A411EW25,ESM2Text,Bacteria,361,"Involved in the biosynthesis of the glucosamine-nitrosourea antibiotic streptozotocin (SZN). Catalyzes the conversion of L-arginine to N(omega)-methyl-L-arginine (L-NMA), using S-adenosyl-L-methionine (SAM) as a methyl donor.","Specifically methylates the N(7) position of guanidinoacetate adenine dinucleotide (AAD) and tRNA(A). Confers resistance to various aminoglycosides, including gentamicin and kanamycin. Methylation is not dependent on pH and the absence of AAD.",No,No,No,No,Maybe,not-Yes,GO:0042054; GO:0016274,,GO:0008168,GO:0008168,GO:0008168,,,0.6169,0.6169,0.6169,,3,0.6169,0.3703,no
SZNE_STRC2,A0A411EW25,Prot2Text,Bacteria,361,"Involved in the biosynthesis of the glucosamine-nitrosourea antibiotic streptozotocin (SZN). Catalyzes the conversion of L-arginine to N(omega)-methyl-L-arginine (L-NMA), using S-adenosyl-L-methionine (SAM) as a methyl donor.","Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins. In vitro, methylates histone H3 at 'Arg-17' and 'Lys-36' using S-adenosyl L-methionine as methyl donor.",Maybe,Yes,Yes,Yes,Maybe,Yes,GO:0042054; GO:0016274,GO:0008469,GO:0035242,GO:0008469,GO:0016274,GO:0008469,0.0,0.8086,0.0,0.8722,0.0,5,0.3362,0.3703,no
SZNE_STRC2,A0A411EW25,ProtT3,Bacteria,361,"Involved in the biosynthesis of the glucosamine-nitrosourea antibiotic streptozotocin (SZN). Catalyzes the conversion of L-arginine to N(omega)-methyl-L-arginine (L-NMA), using S-adenosyl-L-methionine (SAM) as a methyl donor.",Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA). Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT7 subfamily,Maybe,Yes,Yes,Yes,Maybe,Yes,GO:0042054; GO:0016274,GO:0035241,GO:0016274,GO:0016274,GO:0035241,GO:0035242,0.8086,0.8722,0.8722,0.8086,0.8086,5,0.834,0.3703,no
SZNE_STRC2,A0A411EW25,ProtTale,Bacteria,361,"Involved in the biosynthesis of the glucosamine-nitrosourea antibiotic streptozotocin (SZN). Catalyzes the conversion of L-arginine to N(omega)-methyl-L-arginine (L-NMA), using S-adenosyl-L-methionine (SAM) as a methyl donor.",Arginine methyltransferase which methylates the guanidine group of S-adenosyl-L- arginine (AdoMet) to form N(omega)-monomethylarginine (MMA). In vitro also methylates S-adenosyl-L-homocysteine (AdoHcy) to produce N(6)- dimethylarginine (DMA). Not involved in the regulation of polyamine biosynthesis.,No,No,No,No,No,not-Yes,GO:0042054; GO:0016274,GO:0016274,GO:0016274,GO:0016274,GO:0016274,GO:0008276,0.8722,0.8722,0.8722,0.8722,0.8009,5,0.8579,0.3703,no
SZNE_STRC2,A0A411EW25,Protein2Text,Bacteria,361,"Involved in the biosynthesis of the glucosamine-nitrosourea antibiotic streptozotocin (SZN). Catalyzes the conversion of L-arginine to N(omega)-methyl-L-arginine (L-NMA), using S-adenosyl-L-methionine (SAM) as a methyl donor.","The molecular function of this protein is as a monoamine oxidase, specifically a spermine oxidase. It catalyzes the oxidative deamination of spermine and spermidine to 3-aminopropylamine and 4-aminobutylamine, respectively.",No,No,No,No,No,not-Yes,GO:0042054; GO:0016274,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016641,0.2762,0.2762,0.2762,0.2762,0.1945,5,0.2599,0.3703,no
SZNE_STRC2,A0A411EW25,Reference,Bacteria,361,"Involved in the biosynthesis of the glucosamine-nitrosourea antibiotic streptozotocin (SZN). Catalyzes the conversion of L-arginine to N(omega)-methyl-L-arginine (L-NMA), using S-adenosyl-L-methionine (SAM) as a methyl donor.","Involved in the biosynthesis of the glucosamine-nitrosourea antibiotic streptozotocin (SZN). Catalyzes the conversion of L-arginine to N(omega)-methyl-L-arginine (L-NMA), using S-adenosyl-L-methionine (SAM) as a methyl donor.",,,,,,,GO:0042054; GO:0016274,GO:0008757,GO:0008757,GO:0008168,GO:0008168,GO:0016741,0.6079,0.6079,0.6169,0.6169,0.5291,5,0.5957,0.3703,no
STE11_CYTCH,A0A423V942,ESM2Text,Eukaryota,820,"Mitogen-activated protein kinase; part of the Ste11-Ste7-Pmk1 complex that receives signals transmitted by upstream Ste50 and transmits signals to downstream Ste12, which regulates hydrolase, effectors and other genes to promote virulence.","Serine/threonine-protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK11 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. MAPK11 is one of the less studied p38 MAPK. Some of the targets are downstream kinases such as MAPKAPK2, which are activated through phosphorylation and further phosphorylate additional targets. Involved in the regulation of cell polarity and actin organization.",Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0004707; GO:0004709,GO:0004709; GO:0005524,GO:0004709,GO:0004709,GO:0004709,GO:0004709,0.9633,0.7164,0.7164,0.7164,0.7164,5,0.7658,0.5873,yes
STE11_CYTCH,A0A423V942,Prot2Text,Eukaryota,820,"Mitogen-activated protein kinase; part of the Ste11-Ste7-Pmk1 complex that receives signals transmitted by upstream Ste50 and transmits signals to downstream Ste12, which regulates hydrolase, effectors and other genes to promote virulence.","Mitogen-activated protein kinase kinase kinase; part of the MST11-MST7-PMK1 MAP kinase (MAPK) cascade that is essential for appressorium formation, penetration and invasive growth. The MST11-MST7-PMK1 MAP kinase cascade transduces signals from the cell surface sensors MDB2 and SHO1 that recognize various surface signals such as surface hydrophobicity, cutin monomers, and rice leaf waxes. MST7 acts as the upstream MAPKK that directly phosphorylates MAPKK MST1 (Probable).",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0004707; GO:0004709,GO:0004708,GO:0004708,GO:0004708,GO:0004708,GO:0004708; GO:0005524,0.5146,0.5146,0.5146,0.5146,0.8019,5,0.5721,0.5873,yes
STE11_CYTCH,A0A423V942,ProtT3,Eukaryota,820,"Mitogen-activated protein kinase; part of the Ste11-Ste7-Pmk1 complex that receives signals transmitted by upstream Ste50 and transmits signals to downstream Ste12, which regulates hydrolase, effectors and other genes to promote virulence.",Mitogen-activated protein kinase kinase kinase (MAPKKK); part of the MAP kinase kinase (MAPKKK) complex MKK1-MKK2-MKK3 (By similarity). The MKK1-MKK2-MKK3 complex phosphorylates and activates the MAP kinase kinases MKK1 and MKK2 (By similarity). The MKK1-MKK2-MKK3 complex also phosphorylates and activates the MAP kinase kinases MKK4 and MKK5 (By similarity). The MKK1-MKK2-MKK3 complex is,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0004707; GO:0004709,GO:0004709; GO:0005524,GO:0004709; GO:0005524,GO:0004709; GO:0005524,GO:0004709; GO:0005524,GO:0004709; GO:0005524,0.9633,0.9633,0.9633,0.9633,0.9633,5,0.9633,0.5873,yes
STE11_CYTCH,A0A423V942,ProtTale,Eukaryota,820,"Mitogen-activated protein kinase; part of the Ste11-Ste7-Pmk1 complex that receives signals transmitted by upstream Ste50 and transmits signals to downstream Ste12, which regulates hydrolase, effectors and other genes to promote virulence.",Involved in the activation of a MAP kinase cascade that is required for cell cycle G2/M transition.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004707; GO:0004709,,,,,,,,,,,0,,0.5873,yes
STE11_CYTCH,A0A423V942,Protein2Text,Eukaryota,820,"Mitogen-activated protein kinase; part of the Ste11-Ste7-Pmk1 complex that receives signals transmitted by upstream Ste50 and transmits signals to downstream Ste12, which regulates hydrolase, effectors and other genes to promote virulence.","The molecular function of this protein is to act as a guanine nucleotide exchange factor (GEF), which is a type of protein that promotes the exchange of GDP for GTP on G-protein alpha subunits. This protein is involved in regulating various cellular processes, including cell growth, differentiation, and survival, by modulating the activity of G-protein signaling pathways.",No,No,No,No,No,not-Yes,GO:0005524; GO:0004707; GO:0004709,GO:0004708,GO:0004708,GO:0004708,GO:0004708,GO:0004708,0.5146,0.5146,0.5146,0.5146,0.5146,5,0.5146,0.5873,yes
STE11_CYTCH,A0A423V942,Reference,Eukaryota,820,"Mitogen-activated protein kinase; part of the Ste11-Ste7-Pmk1 complex that receives signals transmitted by upstream Ste50 and transmits signals to downstream Ste12, which regulates hydrolase, effectors and other genes to promote virulence.","Mitogen-activated protein kinase; part of the Ste11-Ste7-Pmk1 complex that receives signals transmitted by upstream Ste50 and transmits signals to downstream Ste12, which regulates hydrolase, effectors and other genes to promote virulence.",,,,,,,GO:0005524; GO:0004707; GO:0004709,GO:0004707; GO:0005524,GO:0004707; GO:0005524,GO:0004707; GO:0005524,GO:0004707; GO:0005524,GO:0004707; GO:0005524,0.9633,0.9633,0.9633,0.9633,0.9633,5,0.9633,0.5873,yes
STE7_CYTCH,A0A423VZH2,ESM2Text,Eukaryota,419,"Mitogen-activated protein kinase; part of the Ste11-Ste7-Pmk1 complex that receives signals transmitted by upstream Ste50 and transmits signals to downstream Ste12, which regulates hydrolase, effectors and other genes to promote virulence.",Mitogen-activated protein kinase kinase kinase (MAPK) component of the MAP kinase signal transduction pathway that is essential for cell wall integrity and maintenance of cell wall integrity.,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0004674; GO:0004712,GO:0004709; GO:0005524,GO:0004709,GO:0004709,GO:0004709,GO:0004709,0.9128,0.6533,0.6533,0.6533,0.6533,5,0.7052,0.6364,yes
STE7_CYTCH,A0A423VZH2,Prot2Text,Eukaryota,419,"Mitogen-activated protein kinase; part of the Ste11-Ste7-Pmk1 complex that receives signals transmitted by upstream Ste50 and transmits signals to downstream Ste12, which regulates hydrolase, effectors and other genes to promote virulence.","Mitogen-activated protein kinase kinase; part of the MST11-MST7-PMK1 MAP kinase (MAPK) cascade that is essential for appressorium formation, penetration and invasive growth. Central regulator of appressorium development that acts downstream of the cAMP signal. The MST11-MST7-PMK1 MAP kinase cascade transduces signals from the cell surface sensors MDB2 and SHO1 that recognize various surface signals such as surface hydrophobicity, cutin monomers, and rice leaf waxes. MST7 acts as the upstream MAPKK that directly phosphorylates MAP kinase PMK1.",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0004674; GO:0004712,GO:0004708,GO:0004708,GO:0004708,GO:0004708,GO:0004708; GO:0005524,0.6533,0.6533,0.6533,0.6533,0.9128,5,0.7052,0.6364,yes
STE7_CYTCH,A0A423VZH2,ProtT3,Eukaryota,419,"Mitogen-activated protein kinase; part of the Ste11-Ste7-Pmk1 complex that receives signals transmitted by upstream Ste50 and transmits signals to downstream Ste12, which regulates hydrolase, effectors and other genes to promote virulence.","Mitogen-activated protein kinase kinase kinase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",No,Maybe,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0004674; GO:0004712,GO:0004709; GO:0005524,GO:0004709; GO:0005524,GO:0004709; GO:0005524,GO:0004709; GO:0005524,GO:0004709; GO:0005524,0.9128,0.9128,0.9128,0.9128,0.9128,5,0.9128,0.6364,yes
STE7_CYTCH,A0A423VZH2,ProtTale,Eukaryota,419,"Mitogen-activated protein kinase; part of the Ste11-Ste7-Pmk1 complex that receives signals transmitted by upstream Ste50 and transmits signals to downstream Ste12, which regulates hydrolase, effectors and other genes to promote virulence.","Serine/threonine-protein kinase involved in the regulation of cell polarity and cell growth. Acts as a positive regulator of septin ring formation at the mother-bud junction (MBJ), probably by acting downstream of the MAP kinase pathway.",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0005524; GO:0004674; GO:0004712,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.964,0.964,0.7186,0.964,0.964,5,0.9149,0.6364,yes
STE7_CYTCH,A0A423VZH2,Protein2Text,Eukaryota,419,"Mitogen-activated protein kinase; part of the Ste11-Ste7-Pmk1 complex that receives signals transmitted by upstream Ste50 and transmits signals to downstream Ste12, which regulates hydrolase, effectors and other genes to promote virulence.",The molecular function of this protein is a MAPK kinase.,Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004674; GO:0004712,GO:0004708,GO:0004708,GO:0004708,GO:0004708,GO:0004708,0.6533,0.6533,0.6533,0.6533,0.6533,5,0.6533,0.6364,yes
STE7_CYTCH,A0A423VZH2,Reference,Eukaryota,419,"Mitogen-activated protein kinase; part of the Ste11-Ste7-Pmk1 complex that receives signals transmitted by upstream Ste50 and transmits signals to downstream Ste12, which regulates hydrolase, effectors and other genes to promote virulence.","Mitogen-activated protein kinase; part of the Ste11-Ste7-Pmk1 complex that receives signals transmitted by upstream Ste50 and transmits signals to downstream Ste12, which regulates hydrolase, effectors and other genes to promote virulence.",,,,,,,GO:0005524; GO:0004674; GO:0004712,GO:0004707; GO:0005524,GO:0004707; GO:0005524,GO:0004707; GO:0005524,GO:0004707; GO:0005524,GO:0004707; GO:0005524,0.9128,0.9128,0.9128,0.9128,0.9128,5,0.9128,0.6364,yes
PERA_METMF,A0A455ZJD4,ESM2Text,Eukaryota,2799,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. The single multifunctional NRPS ppzA is responsible for the biosynthesis of peramine. The condensation domain of ppzA is proposed to catalyze formation of a peptide bond between 1-pyrroline-5-carboxylate and arginine. The methylation domain of ppzA would catalyze the N-methylation of the alpha-amino group of arginine. The reductase domain is proposed to be responsible for reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. This final oxidation to give the pyrrole functionality may be spontaneous. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8-hydroxyperamine whereas ppzD converts L-proline into trans- 4-hydroxy-L-proline, a precursor of peramine biosynthesis.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of aspirochlorine (or antibiotic A30641), an unusual halogenated spiro compound with distinctive antifungal properties due to selective inhibition of protein biosynthesis, and which is also active against bacteria, viruses, and murine tumor cells. The non-ribosomal peptide synthetase (NRPS) aclP is responsible the formation of the diketopiperazine (DKP) core from the condensation of 2 phenylalanine residues. One Phe residue is tailored into chlorotyrosine by hydroxylation and chlorination, whereas the second Phe undergoes an unprecedented C-C bond cleavage to be converted into glycine. After formation of the DKP, sulfur is incorporated into the DKP by conjugation with glutathione by aclG, followed by its stepwise degradation to the thiol by aclI, aclJ and aclK, and the dithiol oxidation by aclT. In addition, oxygenases (aclB, aclC, aclL and aclO) and O-methyltransferases (aclM and",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0008168; GO:0031177,,,,,,,,,,,0,,0.2936,no
PERA_METMF,A0A455ZJD4,Prot2Text,Eukaryota,2799,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. The single multifunctional NRPS ppzA is responsible for the biosynthesis of peramine. The condensation domain of ppzA is proposed to catalyze formation of a peptide bond between 1-pyrroline-5-carboxylate and arginine. The methylation domain of ppzA would catalyze the N-methylation of the alpha-amino group of arginine. The reductase domain is proposed to be responsible for reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. This final oxidation to give the pyrrole functionality may be spontaneous. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8-hydroxyperamine whereas ppzD converts L-proline into trans- 4-hydroxy-L-proline, a precursor of peramine biosynthesis.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of aspirochlorine (or antibiotic A30641), an unusual halogenated spiro compound with distinctive antifungal properties due to selective inhibition of protein biosynthesis, and which is also active against bacteria, viruses, and murine tumor cells. The non-ribosomal peptide synthetase (NRPS) aclP is responsible the formation of the diketopiperazine (DKP) core from the condensation of 2 phenylalanine residues. One Phe residue is tailored into chlorotyrosine by hydroxylation and chlorination, whereas the second Phe undergoes an unprecedented C-C bond cleavage to be converted into glycine. After formation of the DKP, sulfur is incorporated into the DKP by conjugation with glutathione by aclG, followed by its stepwise degradation to the thiol by aclI, aclJ and aclK, and the dithiol oxidation by aclT. In addition, oxygenases (aclB, aclC, aclL and aclO) and O-methyltransferases (aclM and",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0008168; GO:0031177,GO:0016874,,,GO:0016874,GO:0016874; GO:0005524,0.6335,,,0.6335,0.6249,3,0.6306,0.2936,no
PERA_METMF,A0A455ZJD4,ProtT3,Eukaryota,2799,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. The single multifunctional NRPS ppzA is responsible for the biosynthesis of peramine. The condensation domain of ppzA is proposed to catalyze formation of a peptide bond between 1-pyrroline-5-carboxylate and arginine. The methylation domain of ppzA would catalyze the N-methylation of the alpha-amino group of arginine. The reductase domain is proposed to be responsible for reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. This final oxidation to give the pyrrole functionality may be spontaneous. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8-hydroxyperamine whereas ppzD converts L-proline into trans- 4-hydroxy-L-proline, a precursor of peramine biosynthesis.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties . L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L- homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O- acetyltransferase FUB4, as well as enzymes of the primary metabolism",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0008168; GO:0031177,GO:0016874; GO:0005524,GO:0016874,,GO:0016874; GO:0031177,GO:0016874; GO:0005524,0.6249,0.6335,,0.8814,0.6249,4,0.6912,0.2936,no
PERA_METMF,A0A455ZJD4,ProtTale,Eukaryota,2799,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. The single multifunctional NRPS ppzA is responsible for the biosynthesis of peramine. The condensation domain of ppzA is proposed to catalyze formation of a peptide bond between 1-pyrroline-5-carboxylate and arginine. The methylation domain of ppzA would catalyze the N-methylation of the alpha-amino group of arginine. The reductase domain is proposed to be responsible for reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. This final oxidation to give the pyrrole functionality may be spontaneous. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8-hydroxyperamine whereas ppzD converts L-proline into trans- 4-hydroxy-L-proline, a precursor of peramine biosynthesis.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS). SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms. These initial steps feature the priming of an unusual benzoic acid starter unit onto",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0008168; GO:0031177,GO:0016491,GO:0016874,,,GO:0016874,0.4286,0.6335,,,0.6335,3,0.5652,0.2936,no
PERA_METMF,A0A455ZJD4,Protein2Text,Eukaryota,2799,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. The single multifunctional NRPS ppzA is responsible for the biosynthesis of peramine. The condensation domain of ppzA is proposed to catalyze formation of a peptide bond between 1-pyrroline-5-carboxylate and arginine. The methylation domain of ppzA would catalyze the N-methylation of the alpha-amino group of arginine. The reductase domain is proposed to be responsible for reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. This final oxidation to give the pyrrole functionality may be spontaneous. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8-hydroxyperamine whereas ppzD converts L-proline into trans- 4-hydroxy-L-proline, a precursor of peramine biosynthesis.","This protein is involved in the synthesis of a specific type of molecule, likely a non-proteinogenic amino acid. The exact molecular function is not specified in the provided text, but it is likely involved in the production of a molecule that is used by a microorganism to grow or survive.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0016874; GO:0008168; GO:0031177,,,,,,,,,,,0,,0.2936,no
PERA_METMF,A0A455ZJD4,Reference,Eukaryota,2799,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. The single multifunctional NRPS ppzA is responsible for the biosynthesis of peramine. The condensation domain of ppzA is proposed to catalyze formation of a peptide bond between 1-pyrroline-5-carboxylate and arginine. The methylation domain of ppzA would catalyze the N-methylation of the alpha-amino group of arginine. The reductase domain is proposed to be responsible for reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. This final oxidation to give the pyrrole functionality may be spontaneous. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8-hydroxyperamine whereas ppzD converts L-proline into trans- 4-hydroxy-L-proline, a precursor of peramine biosynthesis.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. The single multifunctional NRPS ppzA is responsible for the biosynthesis of peramine. The condensation domain of ppzA is proposed to catalyze formation of a peptide bond between 1-pyrroline-5-carboxylate and arginine. The methylation domain of ppzA would catalyze the N-methylation of the alpha-amino group of arginine. The reductase domain is proposed to be responsible for reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. This final oxidation to give the pyrrole functionality may be spontaneous. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8-hydroxyperamine whereas ppzD converts L-proline into trans- 4-hydroxy-L-proline, a precursor of peramine biosynthesis.",,,,,,,GO:0016874; GO:0008168; GO:0031177,GO:0016874,GO:0016874,GO:0016874,GO:0016874,GO:0016874,0.6335,0.6335,0.6335,0.6335,0.6335,5,0.6335,0.2936,no
COBC_RHIML,A0A499W357,ESM2Text,Bacteria,333,"Decarboxylates L-threonine-O-3-phosphate to yield (R)-1- amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.","Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0030170; GO:0048472,GO:0016831,GO:0016831,GO:0016831,GO:0016831,,0.599,0.599,0.599,0.599,,4,0.599,0.1562,no
COBC_RHIML,A0A499W357,Prot2Text,Bacteria,333,"Decarboxylates L-threonine-O-3-phosphate to yield (R)-1- amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.","Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0030170; GO:0048472,GO:0016831,,GO:0016831,GO:0008497,GO:0016831,0.599,,0.599,0.1164,0.599,4,0.4783,0.1562,no
COBC_RHIML,A0A499W357,ProtT3,Bacteria,333,"Decarboxylates L-threonine-O-3-phosphate to yield (R)-1- amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.","Involved in the biosynthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL- diaminopimelate. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. LL-diaminopimelate aminotransferase subfamily",No,No,No,No,No,not-Yes,GO:0030170; GO:0048472,GO:0008483; GO:0030170,GO:0008483; GO:0030170,GO:0070546; GO:0030170,GO:0008483; GO:0030170,GO:0008483,0.6176,0.6176,0.6898,0.6176,0.1838,5,0.5453,0.1562,no
COBC_RHIML,A0A499W357,ProtTale,Bacteria,333,"Decarboxylates L-threonine-O-3-phosphate to yield (R)-1- amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.",Transforms glucosamine-6-phosphate to fructose-6-phosphate.,No,No,No,No,No,not-Yes,GO:0030170; GO:0048472,GO:0004342,GO:0016853,GO:0004342,GO:0004342,GO:0004342,0.1563,0.2761,0.1563,0.1563,0.1563,5,0.1803,0.1562,no
COBC_RHIML,A0A499W357,Protein2Text,Bacteria,333,"Decarboxylates L-threonine-O-3-phosphate to yield (R)-1- amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.","The molecular function of this protein is an aminotransferase that catalyzes the transfer of an amino group from an amino acid to a keto acid, specifically in the biosynthesis of L-lysine.",No,No,No,No,No,not-Yes,GO:0030170; GO:0048472,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.1838,0.1838,0.1838,0.1838,0.1838,5,0.1838,0.1562,no
COBC_RHIML,A0A499W357,Reference,Bacteria,333,"Decarboxylates L-threonine-O-3-phosphate to yield (R)-1- amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.","Decarboxylates L-threonine-O-3-phosphate to yield (R)-1- amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.",,,,,,,GO:0030170; GO:0048472,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.599,0.599,0.599,0.599,0.599,5,0.599,0.1562,no
CDPK6_PLABA,A0A509ALV6,ESM2Text,Eukaryota,1482,"Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels. In sporozoites, probably involved in the secretion of the cysteine protease that cleaves circumsporozoite protein CSP, thereby exposing CSP TSR domain, which binds with high affinity to highly sulfated heparan sulfate proteoglycans (HSPGs), resulting in productive invasion of the host hepatocytes.","Chromatin reader component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Acts as a regulator of gene expression during meiosis. Required for the formation of the contractile ring around the spindle pole body during meiosis, and for the ring assembly.",No,No,No,No,Maybe,not-Yes,GO:0005524; GO:0005509; GO:0004674,,,,,,,,,,,0,,0.4927,no
CDPK6_PLABA,A0A509ALV6,Prot2Text,Eukaryota,1482,"Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels. In sporozoites, probably involved in the secretion of the cysteine protease that cleaves circumsporozoite protein CSP, thereby exposing CSP TSR domain, which binds with high affinity to highly sulfated heparan sulfate proteoglycans (HSPGs), resulting in productive invasion of the host hepatocytes.",Protein with a role in sporulation.,No,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0005509; GO:0004674,,,,,,,,,,,0,,0.4927,no
CDPK6_PLABA,A0A509ALV6,ProtT3,Eukaryota,1482,"Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels. In sporozoites, probably involved in the secretion of the cysteine protease that cleaves circumsporozoite protein CSP, thereby exposing CSP TSR domain, which binds with high affinity to highly sulfated heparan sulfate proteoglycans (HSPGs), resulting in productive invasion of the host hepatocytes.","Involved in the regulation of the cell cycle. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Belongs to the SIP1 family",No,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0005509; GO:0004674,,,,,,,,,,,0,,0.4927,no
CDPK6_PLABA,A0A509ALV6,ProtTale,Eukaryota,1482,"Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels. In sporozoites, probably involved in the secretion of the cysteine protease that cleaves circumsporozoite protein CSP, thereby exposing CSP TSR domain, which binds with high affinity to highly sulfated heparan sulfate proteoglycans (HSPGs), resulting in productive invasion of the host hepatocytes.","Serine/threonine protein kinase involved in the regulation of calcium-dependent processes such as gametogenesis, ookinete formation and fertilization.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0005509; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.8511,0.8511,0.5312,0.8511,0.8511,5,0.7871,0.4927,no
CDPK6_PLABA,A0A509ALV6,Protein2Text,Eukaryota,1482,"Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels. In sporozoites, probably involved in the secretion of the cysteine protease that cleaves circumsporozoite protein CSP, thereby exposing CSP TSR domain, which binds with high affinity to highly sulfated heparan sulfate proteoglycans (HSPGs), resulting in productive invasion of the host hepatocytes.",The molecular function of this protein is an ATP-dependent RNA helicase.,No,No,No,No,Vague,not-Yes,GO:0005524; GO:0005509; GO:0004674,GO:0004386; GO:0005524,GO:0004004,GO:0003724,GO:0004004,GO:0004004,0.5283,0.1068,0.1068,0.1068,0.1068,5,0.1911,0.4927,no
CDPK6_PLABA,A0A509ALV6,Reference,Eukaryota,1482,"Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels. In sporozoites, probably involved in the secretion of the cysteine protease that cleaves circumsporozoite protein CSP, thereby exposing CSP TSR domain, which binds with high affinity to highly sulfated heparan sulfate proteoglycans (HSPGs), resulting in productive invasion of the host hepatocytes.","Calcium-dependent protein kinase which acts as a sensor and effector of intracellular Ca(2+) levels. In sporozoites, probably involved in the secretion of the cysteine protease that cleaves circumsporozoite protein CSP, thereby exposing CSP TSR domain, which binds with high affinity to highly sulfated heparan sulfate proteoglycans (HSPGs), resulting in productive invasion of the host hepatocytes.",,,,,,,GO:0005524; GO:0005509; GO:0004674,GO:0004674; GO:0005524; GO:0005509,GO:0004674; GO:0005524; GO:0005509,GO:0004674; GO:0005509; GO:0005524,GO:0004674; GO:0005509; GO:0005524,GO:0004674; GO:0005509; GO:0005524,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4927,no
BHPC1_PLABA,A0A509APV9,ESM2Text,Eukaryota,519,Cysteine protease. Required for host hepatocyte-derived merozoite infectivity and to a lesser extent for host erythrocyte-derived merozoite infectivity.,Probably degrades erythrocyte hemoglobin.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008234,GO:0008233,GO:0008233,,GO:0008233,,0.871,0.871,,0.871,,3,0.871,0.4149,no
BHPC1_PLABA,A0A509APV9,Prot2Text,Eukaryota,519,Cysteine protease. Required for host hepatocyte-derived merozoite infectivity and to a lesser extent for host erythrocyte-derived merozoite infectivity.,Probably degrades erythrocyte hemoglobin.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008234,GO:0008233,,GO:0008233,GO:0008233,GO:0008233,0.871,,0.871,0.871,0.871,4,0.871,0.4149,no
BHPC1_PLABA,A0A509APV9,ProtT3,Eukaryota,519,Cysteine protease. Required for host hepatocyte-derived merozoite infectivity and to a lesser extent for host erythrocyte-derived merozoite infectivity.,Belongs to the peptidase C1 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008234,GO:0004197,GO:0008234,GO:0004197,GO:0008234,GO:0008234,0.8001,1.0,0.8001,1.0,1.0,5,0.92,0.4149,no
BHPC1_PLABA,A0A509APV9,ProtTale,Eukaryota,519,Cysteine protease. Required for host hepatocyte-derived merozoite infectivity and to a lesser extent for host erythrocyte-derived merozoite infectivity.,Cysteine protease that catalyzes the cleavage of a peptide chain between two amino acids with a side chain that is smaller than the other one.,Maybe,Yes,Yes,Yes,Maybe,Yes,GO:0008234,GO:0008234,GO:0008234,GO:0008234,GO:0008234,GO:0008234,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4149,no
BHPC1_PLABA,A0A509APV9,Protein2Text,Eukaryota,519,Cysteine protease. Required for host hepatocyte-derived merozoite infectivity and to a lesser extent for host erythrocyte-derived merozoite infectivity.,"This protein is involved in proteolysis, which is the breakdown of proteins into smaller peptides or amino acids. More specifically, it is involved in the cleavage of proteins in the cell, which is an important step in various cellular processes such as protein turnover, signaling, and cell differentiation.",Maybe,Maybe,Maybe,Vague,Yes,not-Yes,GO:0008234,GO:0008233,GO:0008233,GO:0008233,GO:0008233,GO:0008233,0.871,0.871,0.871,0.871,0.871,5,0.871,0.4149,no
BHPC1_PLABA,A0A509APV9,Reference,Eukaryota,519,Cysteine protease. Required for host hepatocyte-derived merozoite infectivity and to a lesser extent for host erythrocyte-derived merozoite infectivity.,Cysteine protease. Required for host hepatocyte-derived merozoite infectivity and to a lesser extent for host erythrocyte-derived merozoite infectivity.,,,,,,,GO:0008234,GO:0008234,GO:0008234,GO:0008234,GO:0008234,GO:0008234,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4149,no
UIS2_PLABA,A0A509AQ20,ESM2Text,Eukaryota,1322,"Protein phosphatase which dephosphorylates 'Ser-59' of translation factor eIF2alpha during the liver stage, thus enabling protein translation.","Metalloprotease, which cleaves specifically after arginine or lysine residues.",No,No,No,No,No,not-Yes,GO:0046872; GO:0004722,GO:0004222,GO:0004222,GO:0004222,GO:0008237,GO:0008237,0.2625,0.2625,0.2625,0.3267,0.3267,5,0.2882,0.5761,yes
UIS2_PLABA,A0A509AQ20,Prot2Text,Eukaryota,1322,"Protein phosphatase which dephosphorylates 'Ser-59' of translation factor eIF2alpha during the liver stage, thus enabling protein translation.",Seems to play a role in the degradation of the storage polymer of cytoplasmic proteins. Its overall degradation activity is required for cell growth.,No,No,No,Vague,No,not-Yes,GO:0046872; GO:0004722,,,,,GO:0008233,,,,,0.3813,1,0.3813,0.5761,yes
UIS2_PLABA,A0A509AQ20,ProtT3,Eukaryota,1322,"Protein phosphatase which dephosphorylates 'Ser-59' of translation factor eIF2alpha during the liver stage, thus enabling protein translation.",Plays a role in merozoite invasion of erythrocytes. Membrane; Single-pass type I membrane protein. Belongs to the hemagglutinin-like family,No,No,Vague,No,No,not-Yes,GO:0046872; GO:0004722,,,,,,,,,,,0,,0.5761,yes
UIS2_PLABA,A0A509AQ20,ProtTale,Eukaryota,1322,"Protein phosphatase which dephosphorylates 'Ser-59' of translation factor eIF2alpha during the liver stage, thus enabling protein translation.","Phosphatidylinositol-4,5-bisphosphate (PtdIns-4,5-bisP) phosphatase that hydrolyzes PtdIns-4,5-bisphosphate to produce phosphatidylinositol-4-phosphate (PtdIns-4-phosphate) and diphosphate.",No,No,No,No,No,not-Yes,GO:0046872; GO:0004722,GO:0016791,GO:0016791,GO:0004439,GO:0004439,GO:0004439,0.5143,0.5143,0.3018,0.3018,0.3018,5,0.3868,0.5761,yes
UIS2_PLABA,A0A509AQ20,Protein2Text,Eukaryota,1322,"Protein phosphatase which dephosphorylates 'Ser-59' of translation factor eIF2alpha during the liver stage, thus enabling protein translation.","This protein is a component of the vacuolar ATPase complex, which is a proton pump that helps to regulate the pH of the cell. It is likely involved in the transport of protons across the cell membrane.",No,No,No,No,No,not-Yes,GO:0046872; GO:0004722,GO:0046961,GO:0046961,GO:0046961,GO:0046961,GO:0046961,0.0577,0.0577,0.0577,0.0577,0.0577,5,0.0577,0.5761,yes
UIS2_PLABA,A0A509AQ20,Reference,Eukaryota,1322,"Protein phosphatase which dephosphorylates 'Ser-59' of translation factor eIF2alpha during the liver stage, thus enabling protein translation.","Protein phosphatase which dephosphorylates 'Ser-59' of translation factor eIF2alpha during the liver stage, thus enabling protein translation.",,,,,,,GO:0046872; GO:0004722,GO:0004722,GO:0004722,GO:0004722,GO:0004722,GO:0004722,0.6942,0.6942,0.6942,0.6942,0.6942,5,0.6942,0.5761,yes
AGA86_WENAE,A0A516RTC5,ESM2Text,Bacteria,735,"Endohydrolase that cleaves the beta-1,4 glycosidic bond between beta-D-galactopyranose-6-sulfate (G6S) and 3,6-anhydro-alpha-L- galactopyranose (LA) unit of funoran, a polysaccharide produced by red algae of the genus Gloiopeltis. It releases the disaccharide LA-G6S as the predominant end product. Also acts as a random endo-acting beta-agarase, which can hydrolyze agarose tetrasaccharides and hexasaccharides, and produces disaccharides as smallest products. Besides typical agarose oligosaccharides, it can use methylated galactoses. The enzyme exhibits higher catalytic efficiency towards agarose, but binds funoran preferentially. Has no activity on porphyran.","Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Acts only on small linear 1,5-alpha-linked L-arabinofuranosyl oligosaccharides.",No,No,No,No,No,not-Yes,GO:0033916,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.3449,no
AGA86_WENAE,A0A516RTC5,Prot2Text,Bacteria,735,"Endohydrolase that cleaves the beta-1,4 glycosidic bond between beta-D-galactopyranose-6-sulfate (G6S) and 3,6-anhydro-alpha-L- galactopyranose (LA) unit of funoran, a polysaccharide produced by red algae of the genus Gloiopeltis. It releases the disaccharide LA-G6S as the predominant end product. Also acts as a random endo-acting beta-agarase, which can hydrolyze agarose tetrasaccharides and hexasaccharides, and produces disaccharides as smallest products. Besides typical agarose oligosaccharides, it can use methylated galactoses. The enzyme exhibits higher catalytic efficiency towards agarose, but binds funoran preferentially. Has no activity on porphyran.","Glycoside hydrolase that exhibits an enzymatic activity toward arabinoxylan, a major component of plant hemicellulose. Acts by cleaving the beta-1,4-linked arabinofuranosyl residues from the non-reducing end of the arabinoxylan polymer, generating oligosaccharides that have unsaturated alpha-1,4-linked arabinofuranose residues.",No,No,No,No,No,not-Yes,GO:0033916,GO:0046556,,GO:0004553,GO:0004553,GO:0004553,0.7289,,0.8582,0.8582,0.8582,4,0.8259,0.3449,no
AGA86_WENAE,A0A516RTC5,ProtT3,Bacteria,735,"Endohydrolase that cleaves the beta-1,4 glycosidic bond between beta-D-galactopyranose-6-sulfate (G6S) and 3,6-anhydro-alpha-L- galactopyranose (LA) unit of funoran, a polysaccharide produced by red algae of the genus Gloiopeltis. It releases the disaccharide LA-G6S as the predominant end product. Also acts as a random endo-acting beta-agarase, which can hydrolyze agarose tetrasaccharides and hexasaccharides, and produces disaccharides as smallest products. Besides typical agarose oligosaccharides, it can use methylated galactoses. The enzyme exhibits higher catalytic efficiency towards agarose, but binds funoran preferentially. Has no activity on porphyran.","Alpha-L-arabinofuranosidase involved in the degradation of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Catalyzes the endohydrolysis of alpha-(1->5)-L-arabinofuranosyl bonds in L-arabinofuranosyl oligosaccharides (By similarity). Secreted. Belongs to the glycosyl hydrolase 43 family",No,No,No,No,No,not-Yes,GO:0033916,GO:0046556,GO:0046556,GO:0046556,GO:0046556; GO:0004553,GO:0046556,0.7289,0.7289,0.7289,0.8151,0.7289,5,0.7461,0.3449,no
AGA86_WENAE,A0A516RTC5,ProtTale,Bacteria,735,"Endohydrolase that cleaves the beta-1,4 glycosidic bond between beta-D-galactopyranose-6-sulfate (G6S) and 3,6-anhydro-alpha-L- galactopyranose (LA) unit of funoran, a polysaccharide produced by red algae of the genus Gloiopeltis. It releases the disaccharide LA-G6S as the predominant end product. Also acts as a random endo-acting beta-agarase, which can hydrolyze agarose tetrasaccharides and hexasaccharides, and produces disaccharides as smallest products. Besides typical agarose oligosaccharides, it can use methylated galactoses. The enzyme exhibits higher catalytic efficiency towards agarose, but binds funoran preferentially. Has no activity on porphyran.","Endohydrolysis of the glucosidic linkages in beta-1,3-glucan.",No,No,No,No,No,not-Yes,GO:0033916,GO:0016798,GO:0004553,GO:0042973,GO:0042973,GO:0042973,0.729,0.8582,0.5618,0.5618,0.5618,5,0.6545,0.3449,no
AGA86_WENAE,A0A516RTC5,Protein2Text,Bacteria,735,"Endohydrolase that cleaves the beta-1,4 glycosidic bond between beta-D-galactopyranose-6-sulfate (G6S) and 3,6-anhydro-alpha-L- galactopyranose (LA) unit of funoran, a polysaccharide produced by red algae of the genus Gloiopeltis. It releases the disaccharide LA-G6S as the predominant end product. Also acts as a random endo-acting beta-agarase, which can hydrolyze agarose tetrasaccharides and hexasaccharides, and produces disaccharides as smallest products. Besides typical agarose oligosaccharides, it can use methylated galactoses. The enzyme exhibits higher catalytic efficiency towards agarose, but binds funoran preferentially. Has no activity on porphyran.","The molecular function of this protein is to catalyze the hydrolysis of cellulose, a type of polysaccharide found in plant cell walls. More specifically, it is a beta-glucosidase, which breaks down the beta-1,4-glycosidic bonds in cellulose into glucose. This process is an important step in the degradation of cellulose, which is a major component of plant biomass. The protein is likely involved in the breakdown of cellulose in the gut of organisms that consume plant material.",No,No,No,No,No,not-Yes,GO:0033916,GO:0008422,GO:0008422,GO:0008422,GO:0008422,GO:0008422,0.6335,0.6335,0.6335,0.6335,0.6335,5,0.6335,0.3449,no
AGA86_WENAE,A0A516RTC5,Reference,Bacteria,735,"Endohydrolase that cleaves the beta-1,4 glycosidic bond between beta-D-galactopyranose-6-sulfate (G6S) and 3,6-anhydro-alpha-L- galactopyranose (LA) unit of funoran, a polysaccharide produced by red algae of the genus Gloiopeltis. It releases the disaccharide LA-G6S as the predominant end product. Also acts as a random endo-acting beta-agarase, which can hydrolyze agarose tetrasaccharides and hexasaccharides, and produces disaccharides as smallest products. Besides typical agarose oligosaccharides, it can use methylated galactoses. The enzyme exhibits higher catalytic efficiency towards agarose, but binds funoran preferentially. Has no activity on porphyran.","Endohydrolase that cleaves the beta-1,4 glycosidic bond between beta-D-galactopyranose-6-sulfate (G6S) and 3,6-anhydro-alpha-L- galactopyranose (LA) unit of funoran, a polysaccharide produced by red algae of the genus Gloiopeltis. It releases the disaccharide LA-G6S as the predominant end product. Also acts as a random endo-acting beta-agarase, which can hydrolyze agarose tetrasaccharides and hexasaccharides, and produces disaccharides as smallest products. Besides typical agarose oligosaccharides, it can use methylated galactoses. The enzyme exhibits higher catalytic efficiency towards agarose, but binds funoran preferentially. Has no activity on porphyran.",,,,,,,GO:0033916,GO:0016798,GO:0004553,GO:0004553,GO:0004553,GO:0004553,0.729,0.8582,0.8582,0.8582,0.8582,5,0.8324,0.3449,no
IDH1_PSYS3,A0A5A4WIX0,ESM2Text,Bacteria,419,Catalyzes the oxidative decarboxylation of isocitrate to 2- oxoglutarate and carbon dioxide with the concomitant reduction of NADP(+). Cannot use NAD(+).,The complex from the organism is particularly stable to disruption and remains functional after 6 hrs at 55 degrees Celsius.,Vague,Vague,Vague,Vague,Yes,not-Yes,GO:0004450; GO:0000287; GO:0051287,,,,,,,,,,,0,,0.4033,no
IDH1_PSYS3,A0A5A4WIX0,Prot2Text,Bacteria,419,Catalyzes the oxidative decarboxylation of isocitrate to 2- oxoglutarate and carbon dioxide with the concomitant reduction of NADP(+). Cannot use NAD(+).,Performs an essential role in the oxidative function of the citric acid cycle.,Vague,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0004450; GO:0000287; GO:0051287,,,,,,,,,,,0,,0.4033,no
IDH1_PSYS3,A0A5A4WIX0,ProtT3,Bacteria,419,Catalyzes the oxidative decarboxylation of isocitrate to 2- oxoglutarate and carbon dioxide with the concomitant reduction of NADP(+). Cannot use NAD(+).,Belongs to the isocitrate and isopropylmalate dehydrogenases family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004450; GO:0000287; GO:0051287,GO:0016616,,,GO:0016616,GO:0004449,0.4208,,,0.4208,0.4052,3,0.4156,0.4033,no
IDH1_PSYS3,A0A5A4WIX0,ProtTale,Bacteria,419,Catalyzes the oxidative decarboxylation of isocitrate to 2- oxoglutarate and carbon dioxide with the concomitant reduction of NADP(+). Cannot use NAD(+).,Catalyzes the oxidative decarboxylation of isocitrate to 2- oxoglutarate and carbon dioxide with the concomitant reduction of NADP(+).,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004450; GO:0000287; GO:0051287,GO:0004450; GO:0000166,GO:0004450; GO:0016616,GO:0004450,GO:0004450,GO:0004450,0.7594,0.5858,0.5318,0.5318,0.5318,5,0.5881,0.4033,no
IDH1_PSYS3,A0A5A4WIX0,Protein2Text,Bacteria,419,Catalyzes the oxidative decarboxylation of isocitrate to 2- oxoglutarate and carbon dioxide with the concomitant reduction of NADP(+). Cannot use NAD(+).,"The molecular function of this protein is a dehydrogenase. Specifically, it catalyzes the oxidation of 3-phospho-D-glycerate to 3-phospho-2-oxopropionate, and uses the reducing equivalent in the form of NAD+ to NADH.",No,No,No,No,No,not-Yes,GO:0004450; GO:0000287; GO:0051287,GO:0016616,GO:0004617,GO:0004617,GO:0004617,GO:0004617,0.4208,0.3537,0.3537,0.3537,0.3537,5,0.3671,0.4033,no
IDH1_PSYS3,A0A5A4WIX0,Reference,Bacteria,419,Catalyzes the oxidative decarboxylation of isocitrate to 2- oxoglutarate and carbon dioxide with the concomitant reduction of NADP(+). Cannot use NAD(+).,Catalyzes the oxidative decarboxylation of isocitrate to 2- oxoglutarate and carbon dioxide with the concomitant reduction of NADP(+). Cannot use NAD(+).,,,,,,,GO:0004450; GO:0000287; GO:0051287,GO:0004450,GO:0004450,GO:0004450,GO:0004450,GO:0004450,0.5318,0.5318,0.5318,0.5318,0.5318,5,0.5318,0.4033,no
PNAE1_TABIB,A0A5B8X840,ESM2Text,Eukaryota,263,"Hydrolase involved in iboga and aspidosperma monoterpenoid indole alkaloids (MIAs, e.g. ibogaine, coronaridine and voacangine) biosynthesis pathway from 19E-geissoschizine, psychoactive compounds likely to be used in the treatment of opioid dependence as anti- addiction agents. Catalyzes the conversion of (-)- voacangine to de-ester-(-)-voacangine which spontaneously converts to (-)-ibogaine on heating. May also convert (-)- coronaridine to de-ester-(-)-coronaridine, but spontaneous conversion to (-)-ibogamine is not observed.","Methylesterase shown to have carboxylesterase activity, methyl indole-3-acetic acid (MeIAA) esterase activity and methyl jasmonate (MeJA) esterase activity in vitro.",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0016787; GO:0080030; GO:0080032; GO:0080031,GO:0004091,GO:0004091,GO:0004091,GO:0004091,GO:0004091,0.8245,0.8245,0.8245,0.8245,0.8245,5,0.8245,0.1569,no
PNAE1_TABIB,A0A5B8X840,Prot2Text,Eukaryota,263,"Hydrolase involved in iboga and aspidosperma monoterpenoid indole alkaloids (MIAs, e.g. ibogaine, coronaridine and voacangine) biosynthesis pathway from 19E-geissoschizine, psychoactive compounds likely to be used in the treatment of opioid dependence as anti- addiction agents. Catalyzes the conversion of (-)- voacangine to de-ester-(-)-voacangine which spontaneously converts to (-)-ibogaine on heating. May also convert (-)- coronaridine to de-ester-(-)-coronaridine, but spontaneous conversion to (-)-ibogamine is not observed.","Methylesterase shown to have carboxylesterase activity, methyl indole-3-acetic acid (MeIAA) esterase activity, methyl salicylate (MeSA) esterase activity and methyl jasmonate (MeJA) esterase activity in vitro.",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0016787; GO:0080030; GO:0080032; GO:0080031,GO:0004091,GO:0052689,GO:0004091,GO:0004091,GO:0004091,0.8245,0.8245,0.8245,0.8245,0.8245,5,0.8245,0.1569,no
PNAE1_TABIB,A0A5B8X840,ProtT3,Eukaryota,263,"Hydrolase involved in iboga and aspidosperma monoterpenoid indole alkaloids (MIAs, e.g. ibogaine, coronaridine and voacangine) biosynthesis pathway from 19E-geissoschizine, psychoactive compounds likely to be used in the treatment of opioid dependence as anti- addiction agents. Catalyzes the conversion of (-)- voacangine to de-ester-(-)-voacangine which spontaneously converts to (-)-ibogaine on heating. May also convert (-)- coronaridine to de-ester-(-)-coronaridine, but spontaneous conversion to (-)-ibogamine is not observed.",Methylesterase. Belongs to the AB hydrolase superfamily. Methylesterase family,Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0016787; GO:0080030; GO:0080032; GO:0080031,GO:0016788,GO:0016788,GO:0016788,GO:0016788,GO:0016788,0.7632,0.7632,0.7632,0.7632,0.7632,5,0.7632,0.1569,no
PNAE1_TABIB,A0A5B8X840,ProtTale,Eukaryota,263,"Hydrolase involved in iboga and aspidosperma monoterpenoid indole alkaloids (MIAs, e.g. ibogaine, coronaridine and voacangine) biosynthesis pathway from 19E-geissoschizine, psychoactive compounds likely to be used in the treatment of opioid dependence as anti- addiction agents. Catalyzes the conversion of (-)- voacangine to de-ester-(-)-voacangine which spontaneously converts to (-)-ibogaine on heating. May also convert (-)- coronaridine to de-ester-(-)-coronaridine, but spontaneous conversion to (-)-ibogamine is not observed.","Hydrolase; part of the gene cluster that mediates the biosynthesis of gramillins A and B, bicyclic lipopeptides that induce cell death in maize leaves but not in wheat leaves. The nonribosomal peptide synthetase GRA1 incorporates respectively a glutamic adic (Glu), a leucine (Leu), a serine (Ser), a hydroxyglutamine (HOGln), a 2-amino decanoic acid, and 2 cysteins (CysB and CysA) (Probable). The biosynthesis of 2-amino decanoic acid incorporated in gramillins could be initiated",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0016787; GO:0080030; GO:0080032; GO:0080031,GO:0016787,GO:0016787,,,GO:0016787,0.7611,0.7611,,,0.7611,3,0.7611,0.1569,no
PNAE1_TABIB,A0A5B8X840,Protein2Text,Eukaryota,263,"Hydrolase involved in iboga and aspidosperma monoterpenoid indole alkaloids (MIAs, e.g. ibogaine, coronaridine and voacangine) biosynthesis pathway from 19E-geissoschizine, psychoactive compounds likely to be used in the treatment of opioid dependence as anti- addiction agents. Catalyzes the conversion of (-)- voacangine to de-ester-(-)-voacangine which spontaneously converts to (-)-ibogaine on heating. May also convert (-)- coronaridine to de-ester-(-)-coronaridine, but spontaneous conversion to (-)-ibogamine is not observed.","The molecular function of this protein is not explicitly stated in the provided text. However, based on the name ""O-methyltransferase"", it can be inferred that this protein is involved in the transfer of a methyl group to another molecule, likely as part of a metabolic or biosynthetic pathway.",No,No,No,No,No,not-Yes,GO:0016787; GO:0080030; GO:0080032; GO:0080031,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.262,0.262,0.262,0.262,0.262,5,0.262,0.1569,no
PNAE1_TABIB,A0A5B8X840,Reference,Eukaryota,263,"Hydrolase involved in iboga and aspidosperma monoterpenoid indole alkaloids (MIAs, e.g. ibogaine, coronaridine and voacangine) biosynthesis pathway from 19E-geissoschizine, psychoactive compounds likely to be used in the treatment of opioid dependence as anti- addiction agents. Catalyzes the conversion of (-)- voacangine to de-ester-(-)-voacangine which spontaneously converts to (-)-ibogaine on heating. May also convert (-)- coronaridine to de-ester-(-)-coronaridine, but spontaneous conversion to (-)-ibogamine is not observed.","Hydrolase involved in iboga and aspidosperma monoterpenoid indole alkaloids (MIAs, e.g. ibogaine, coronaridine and voacangine) biosynthesis pathway from 19E-geissoschizine, psychoactive compounds likely to be used in the treatment of opioid dependence as anti- addiction agents. Catalyzes the conversion of (-)- voacangine to de-ester-(-)-voacangine which spontaneously converts to (-)-ibogaine on heating. May also convert (-)- coronaridine to de-ester-(-)-coronaridine, but spontaneous conversion to (-)-ibogamine is not observed.",,,,,,,GO:0016787; GO:0080030; GO:0080032; GO:0080031,GO:0016788,GO:0004091,GO:0016788,GO:0016788,GO:0016788,0.7632,0.8245,0.7632,0.7632,0.7632,5,0.7755,0.1569,no
PNMT_MACMU,A0A5F8AH41,ESM2Text,Eukaryota,282,"Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L- methionine as the methyl donor. Other substrates include phenylethanolamine, octopamine and normetanephrine.",N-methyltransferase that mediates the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.,No,Maybe,No,No,No,not-Yes,GO:0004603,GO:0008176,GO:0008176,GO:0008176,GO:0008176,GO:0008176,0.4696,0.4696,0.4696,0.4696,0.4696,5,0.4696,0.4276,no
PNMT_MACMU,A0A5F8AH41,Prot2Text,Eukaryota,282,"Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L- methionine as the methyl donor. Other substrates include phenylethanolamine, octopamine and normetanephrine.","Thiol S-methyltransferase involved in the synthesis of dothistromin (N-DM-1). Also able to mediate the conversion of N-DM-1 to dothistromin, suggesting that the sulfur atoms of dothistromin formed by its thiol-specific S-methyltransferase domain rather than its protein-thiol reductase activity.",No,Maybe,No,No,No,not-Yes,GO:0004603,GO:0008172,,GO:0008168,GO:0008172,GO:0008168,0.5735,,0.6795,0.5735,0.6795,4,0.6265,0.4276,no
PNMT_MACMU,A0A5F8AH41,ProtT3,Eukaryota,282,"Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L- methionine as the methyl donor. Other substrates include phenylethanolamine, octopamine and normetanephrine.","Catalyzes the transmethylation of polyamines such as putrescine, spermidine and spermine into N(1)-methylputrescine, N(1)-methylspermidine and N(1)-methylspermine, respectively, using S-adenosyl-L-methionine (SAM) as the methyl donor (By similarity). Also catalyzes the N(1),N(1)-dimethylation of polyamines such as N(1),N(1)-dimethylputrescine, N(1),N(1)-dimethylsper",No,Maybe,Maybe,No,No,not-Yes,GO:0004603,GO:0008170,GO:0008170,GO:0008757,GO:0008170,GO:0008170,0.7867,0.7867,0.7867,0.7867,0.7867,5,0.7867,0.4276,no
PNMT_MACMU,A0A5F8AH41,ProtTale,Eukaryota,282,"Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L- methionine as the methyl donor. Other substrates include phenylethanolamine, octopamine and normetanephrine.",Catalyzes the N-methylation of polyamines such as spermine and spermidine. Plays an important role in the regulation of cellular polyamine levels.,No,Maybe,Maybe,No,No,not-Yes,GO:0004603,GO:0008170,GO:0008170,GO:0008170,GO:0008170,GO:0008170,0.7867,0.7867,0.7867,0.7867,0.7867,5,0.7867,0.4276,no
PNMT_MACMU,A0A5F8AH41,Protein2Text,Eukaryota,282,"Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L- methionine as the methyl donor. Other substrates include phenylethanolamine, octopamine and normetanephrine.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its name, it is likely that this protein is involved in the methylation of a molecule, specifically tyramine. This suggests that its molecular function is as a methyltransferase, catalyzing the transfer of a methyl group from S-adenosylmethionine to tyramine.",Maybe,Maybe,Maybe,Vague,No,not-Yes,GO:0004603,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008168,0.5735,0.5735,0.5735,0.5735,0.6795,5,0.5947,0.4276,no
PNMT_MACMU,A0A5F8AH41,Reference,Eukaryota,282,"Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L- methionine as the methyl donor. Other substrates include phenylethanolamine, octopamine and normetanephrine.","Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L- methionine as the methyl donor. Other substrates include phenylethanolamine, octopamine and normetanephrine.",,,,,,,GO:0004603,GO:0003468,GO:0004603,GO:0004603,GO:0003868,GO:0003468,0.0,1.0,1.0,0.1461,0.0,5,0.4292,0.4276,no
RN123_RABIT,A0A5F9C6I2,ESM2Text,Eukaryota,1314,"Catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Promotes the ubiquitination and proteasome-mediated degradation of CDKN1B which is the cyclin- dependent kinase inhibitor at the G0-G1 transition of the cell cycle. Also acts as a key regulator of the NF-kappa-B signaling by promoting maturation of the NFKB1 component of NF-kappa-B. Acts by catalyzing ubiquitination of the NFKB1 p105 precursor, leading to limited proteasomal degradation of NFKB1 p105 and generation of the active NFKB1 p50 subunit. Functions also as an inhibitor of innate antiviral signaling mediated by RIGI and IFIH1 independently of its E3 ligase activity. Interacts with the N-terminal CARD domains of RIGI and IFIH1 and competes with the downstream adapter MAVS.",Catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Promotes the ubiquitination and proteasome-mediated degradation of CDKN1B which is the cyclin-dependent kinase inhibitor at the G0-G1 transition of the cell cycle. Functions also as an inhibitor of innate antiviral signaling mediated by DDX58 and IFIH1 independently of its E3 ligase activity. Interacts with the N-terminal CARD domains of DDX58 and IFIH1 and competes with the downstream adapter MAVS.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0061630; GO:0008270,GO:0061630,GO:0004842,GO:0061630,GO:0061630,GO:0061630,0.6848,0.5768,0.6848,0.6848,0.6848,5,0.6632,0.5976,yes
RN123_RABIT,A0A5F9C6I2,Prot2Text,Eukaryota,1314,"Catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Promotes the ubiquitination and proteasome-mediated degradation of CDKN1B which is the cyclin- dependent kinase inhibitor at the G0-G1 transition of the cell cycle. Also acts as a key regulator of the NF-kappa-B signaling by promoting maturation of the NFKB1 component of NF-kappa-B. Acts by catalyzing ubiquitination of the NFKB1 p105 precursor, leading to limited proteasomal degradation of NFKB1 p105 and generation of the active NFKB1 p50 subunit. Functions also as an inhibitor of innate antiviral signaling mediated by RIGI and IFIH1 independently of its E3 ligase activity. Interacts with the N-terminal CARD domains of RIGI and IFIH1 and competes with the downstream adapter MAVS.",Catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Promotes the ubiquitination and proteasome-mediated degradation of CDKN1B which is the cyclin-dependent kinase inhibitor at the G0-G1 transition of the cell cycle. Functions also as an inhibitor of innate antiviral signaling mediated by DDX58 and IFIH1 independently of its E3 ligase activity. Interacts with the N-terminal CARD domains of DDX58 and IFIH1 and competes with the downstream adapter MAVS.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0061630; GO:0008270,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.6848,0.6848,0.6848,0.6848,0.6848,5,0.6848,0.5976,yes
RN123_RABIT,A0A5F9C6I2,ProtT3,Eukaryota,1314,"Catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Promotes the ubiquitination and proteasome-mediated degradation of CDKN1B which is the cyclin- dependent kinase inhibitor at the G0-G1 transition of the cell cycle. Also acts as a key regulator of the NF-kappa-B signaling by promoting maturation of the NFKB1 component of NF-kappa-B. Acts by catalyzing ubiquitination of the NFKB1 p105 precursor, leading to limited proteasomal degradation of NFKB1 p105 and generation of the active NFKB1 p50 subunit. Functions also as an inhibitor of innate antiviral signaling mediated by RIGI and IFIH1 independently of its E3 ligase activity. Interacts with the N-terminal CARD domains of RIGI and IFIH1 and competes with the downstream adapter MAVS.","Plays an important role in the regulation of cell migration. Acts as a GTPase-activating protein (GAP) for RAB11A, RAB11B, RAB35 and RAB5A (By similarity). Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, spindle pole Cytoplasm, cytoskeleton, spindle pole, centriole Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite Cytoplasm, cytoskeleton, spindle pole, kinetochore Cytoplasm, cytoskeleton, spindle Note=Colocalizes with RAB11",No,No,No,No,No,not-Yes,GO:0061630; GO:0008270,GO:0005096,GO:0005097,GO:0005096,GO:0005097,GO:0005096,0.0655,0.0655,0.0655,0.0655,0.0655,5,0.0655,0.5976,yes
RN123_RABIT,A0A5F9C6I2,ProtTale,Eukaryota,1314,"Catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Promotes the ubiquitination and proteasome-mediated degradation of CDKN1B which is the cyclin- dependent kinase inhibitor at the G0-G1 transition of the cell cycle. Also acts as a key regulator of the NF-kappa-B signaling by promoting maturation of the NFKB1 component of NF-kappa-B. Acts by catalyzing ubiquitination of the NFKB1 p105 precursor, leading to limited proteasomal degradation of NFKB1 p105 and generation of the active NFKB1 p50 subunit. Functions also as an inhibitor of innate antiviral signaling mediated by RIGI and IFIH1 independently of its E3 ligase activity. Interacts with the N-terminal CARD domains of RIGI and IFIH1 and competes with the downstream adapter MAVS.",E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in the regulation of synaptic vesicle recycling.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0061630; GO:0008270,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.6848,0.6848,0.6848,0.6848,0.6848,5,0.6848,0.5976,yes
RN123_RABIT,A0A5F9C6I2,Protein2Text,Eukaryota,1314,"Catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Promotes the ubiquitination and proteasome-mediated degradation of CDKN1B which is the cyclin- dependent kinase inhibitor at the G0-G1 transition of the cell cycle. Also acts as a key regulator of the NF-kappa-B signaling by promoting maturation of the NFKB1 component of NF-kappa-B. Acts by catalyzing ubiquitination of the NFKB1 p105 precursor, leading to limited proteasomal degradation of NFKB1 p105 and generation of the active NFKB1 p50 subunit. Functions also as an inhibitor of innate antiviral signaling mediated by RIGI and IFIH1 independently of its E3 ligase activity. Interacts with the N-terminal CARD domains of RIGI and IFIH1 and competes with the downstream adapter MAVS.","The molecular function of this protein is not explicitly stated in the provided information. However, based on its name, it is likely involved in vesicular transport, as the name suggests it may be a component of a vesicle. 

A more detailed search of the protein's name in scientific databases reveals that this protein is a guanine nucleotide exchange factor (GEF), specifically a GEF that interacts with the small GTPase Rab5. Rab5 is a key regulator of endocytosis and vesicular trafficking. 

Therefore, the molecular function of this protein is likely to be a GEF that regulates the activity of Rab5, promoting its interaction with GTP and facilitating its role in endocytosis and vesicular trafficking.",No,No,No,Vague,No,not-Yes,GO:0061630; GO:0008270,GO:0005085,GO:0005085,GO:0005085,GO:0005085,GO:0005085,0.0692,0.0692,0.0692,0.0692,0.0692,5,0.0692,0.5976,yes
RN123_RABIT,A0A5F9C6I2,Reference,Eukaryota,1314,"Catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Promotes the ubiquitination and proteasome-mediated degradation of CDKN1B which is the cyclin- dependent kinase inhibitor at the G0-G1 transition of the cell cycle. Also acts as a key regulator of the NF-kappa-B signaling by promoting maturation of the NFKB1 component of NF-kappa-B. Acts by catalyzing ubiquitination of the NFKB1 p105 precursor, leading to limited proteasomal degradation of NFKB1 p105 and generation of the active NFKB1 p50 subunit. Functions also as an inhibitor of innate antiviral signaling mediated by RIGI and IFIH1 independently of its E3 ligase activity. Interacts with the N-terminal CARD domains of RIGI and IFIH1 and competes with the downstream adapter MAVS.","Catalytic subunit of the KPC complex that acts as E3 ubiquitin-protein ligase. Promotes the ubiquitination and proteasome-mediated degradation of CDKN1B which is the cyclin- dependent kinase inhibitor at the G0-G1 transition of the cell cycle. Also acts as a key regulator of the NF-kappa-B signaling by promoting maturation of the NFKB1 component of NF-kappa-B. Acts by catalyzing ubiquitination of the NFKB1 p105 precursor, leading to limited proteasomal degradation of NFKB1 p105 and generation of the active NFKB1 p50 subunit. Functions also as an inhibitor of innate antiviral signaling mediated by RIGI and IFIH1 independently of its E3 ligase activity. Interacts with the N-terminal CARD domains of RIGI and IFIH1 and competes with the downstream adapter MAVS.",,,,,,,GO:0061630; GO:0008270,GO:0004842,GO:0061630,GO:0004842,GO:0004842,GO:0061630,0.5768,0.6848,0.5768,0.5768,0.6848,5,0.62,0.5976,yes
VVIA_VIRVR,A0A6A6H402,ESM2Text,Eukaryota,293,"Prenyltransferase that exclusively uses vviB-synthesized drim-8-ene diphosphate (cyclo-farnesyl diphosphate) as the native prenyl donor to catalyze the prenylation of D-mannitol on C-3'-OH to produce sporulositol A. Moreover, when the native substrate D-mannitol is replaced by other C6 saccharide polyols (D- sorbitol or D-galactitol), vviA is able to transfer drim-8-ene diphosphate to each C6 saccharide polyols with low yields, showing a broad substrate tolerance toward C6 saccharide polyols. However, the C5 to C3 saccharide polyols such as C5 xylitol, C4 erythritol or C3 glycerol are not recognized by vviA.","Fatty acid elongase; part of the gene cluster that mediates the biosynthesis of echinocandin B, a fungal lipidated cyclic hexadepsipeptide that acts as an antifungal agent. Linoleoyl-CoA epoxide is the preferred substrate, but it can also be used with a wide range of other CoA esters as well as benzylCoA. The fatty acid synthase epsilonA is responsible for the production of the fatty acid coenzyme A (CoA), while the methyltransferase epsilonB is involved in the second step. CoA-CoA is then methylated by the methyltransferase epsilonC, followed by ester bond formation between the carboxyl end of the fatty acid and a beta-lactam ring. A last step of echinocandin biosynthesis is ester cyclization to form dihydropin.",No,No,No,No,No,not-Yes,GO:0016740,GO:0009922,GO:0016747,GO:0009922,GO:0009922,GO:0009922,0.6019,0.6897,0.6019,0.6019,0.6019,5,0.6195,0.2554,no
VVIA_VIRVR,A0A6A6H402,Prot2Text,Eukaryota,293,"Prenyltransferase that exclusively uses vviB-synthesized drim-8-ene diphosphate (cyclo-farnesyl diphosphate) as the native prenyl donor to catalyze the prenylation of D-mannitol on C-3'-OH to produce sporulositol A. Moreover, when the native substrate D-mannitol is replaced by other C6 saccharide polyols (D- sorbitol or D-galactitol), vviA is able to transfer drim-8-ene diphosphate to each C6 saccharide polyols with low yields, showing a broad substrate tolerance toward C6 saccharide polyols. However, the C5 to C3 saccharide polyols such as C5 xylitol, C4 erythritol or C3 glycerol are not recognized by vviA.",Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Catalyzes the conversion of tetra- and penta-methyl phytoalexins to their corresponding methyl esters.,Maybe,Maybe,No,Maybe,No,not-Yes,GO:0016740,GO:0008168,GO:0008171,GO:0008171,GO:0008168,GO:0008171,0.6897,0.6019,0.6019,0.6897,0.6019,5,0.637,0.2554,no
VVIA_VIRVR,A0A6A6H402,ProtT3,Eukaryota,293,"Prenyltransferase that exclusively uses vviB-synthesized drim-8-ene diphosphate (cyclo-farnesyl diphosphate) as the native prenyl donor to catalyze the prenylation of D-mannitol on C-3'-OH to produce sporulositol A. Moreover, when the native substrate D-mannitol is replaced by other C6 saccharide polyols (D- sorbitol or D-galactitol), vviA is able to transfer drim-8-ene diphosphate to each C6 saccharide polyols with low yields, showing a broad substrate tolerance toward C6 saccharide polyols. However, the C5 to C3 saccharide polyols such as C5 xylitol, C4 erythritol or C3 glycerol are not recognized by vviA.",Membrane; Multi-pass membrane protein,Vague,Vague,Vague,Vague,No,not-Yes,GO:0016740,,,,,,,,,,,0,,0.2554,no
VVIA_VIRVR,A0A6A6H402,ProtTale,Eukaryota,293,"Prenyltransferase that exclusively uses vviB-synthesized drim-8-ene diphosphate (cyclo-farnesyl diphosphate) as the native prenyl donor to catalyze the prenylation of D-mannitol on C-3'-OH to produce sporulositol A. Moreover, when the native substrate D-mannitol is replaced by other C6 saccharide polyols (D- sorbitol or D-galactitol), vviA is able to transfer drim-8-ene diphosphate to each C6 saccharide polyols with low yields, showing a broad substrate tolerance toward C6 saccharide polyols. However, the C5 to C3 saccharide polyols such as C5 xylitol, C4 erythritol or C3 glycerol are not recognized by vviA.",Catalyzes the condensation of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) to yield geranyl diphosphate (GPP). May be able to use a mixture of IPP and DMAPP as the substrate.,Maybe,Maybe,Maybe,No,No,not-Yes,GO:0016740,GO:0004337,GO:0004337,GO:0004161,GO:0004337,GO:0004337,0.5381,0.5381,0.5381,0.5381,0.5381,5,0.5381,0.2554,no
VVIA_VIRVR,A0A6A6H402,Protein2Text,Eukaryota,293,"Prenyltransferase that exclusively uses vviB-synthesized drim-8-ene diphosphate (cyclo-farnesyl diphosphate) as the native prenyl donor to catalyze the prenylation of D-mannitol on C-3'-OH to produce sporulositol A. Moreover, when the native substrate D-mannitol is replaced by other C6 saccharide polyols (D- sorbitol or D-galactitol), vviA is able to transfer drim-8-ene diphosphate to each C6 saccharide polyols with low yields, showing a broad substrate tolerance toward C6 saccharide polyols. However, the C5 to C3 saccharide polyols such as C5 xylitol, C4 erythritol or C3 glycerol are not recognized by vviA.","This protein is involved in the transfer of molecular groups or molecules, specifically in the transfer of sterol groups.",No,No,Vague,Vague,No,not-Yes,GO:0016740,,,,,,,,,,,0,,0.2554,no
VVIA_VIRVR,A0A6A6H402,Reference,Eukaryota,293,"Prenyltransferase that exclusively uses vviB-synthesized drim-8-ene diphosphate (cyclo-farnesyl diphosphate) as the native prenyl donor to catalyze the prenylation of D-mannitol on C-3'-OH to produce sporulositol A. Moreover, when the native substrate D-mannitol is replaced by other C6 saccharide polyols (D- sorbitol or D-galactitol), vviA is able to transfer drim-8-ene diphosphate to each C6 saccharide polyols with low yields, showing a broad substrate tolerance toward C6 saccharide polyols. However, the C5 to C3 saccharide polyols such as C5 xylitol, C4 erythritol or C3 glycerol are not recognized by vviA.","Prenyltransferase that exclusively uses vviB-synthesized drim-8-ene diphosphate (cyclo-farnesyl diphosphate) as the native prenyl donor to catalyze the prenylation of D-mannitol on C-3'-OH to produce sporulositol A. Moreover, when the native substrate D-mannitol is replaced by other C6 saccharide polyols (D- sorbitol or D-galactitol), vviA is able to transfer drim-8-ene diphosphate to each C6 saccharide polyols with low yields, showing a broad substrate tolerance toward C6 saccharide polyols. However, the C5 to C3 saccharide polyols such as C5 xylitol, C4 erythritol or C3 glycerol are not recognized by vviA.",,,,,,,GO:0016740,GO:0016765,GO:0004659,GO:0004659,GO:0016765,GO:0016765,0.8145,0.6897,0.6897,0.8145,0.8145,5,0.7646,0.2554,no
CREL1_XENTR,A0A6I8RMG7,ESM2Text,Eukaryota,410,Protein disulfide isomerase. Promotes the localization of acetylcholine receptors (AChRs) to the plasma membrane.,Subunit of the peripheral V1 complex of vacuolar ATPase. May have a role in antigen receptor (AR) autophagy.,No,No,No,No,No,not-Yes,GO:0005509; GO:0003756,GO:0046961,GO:0016887,GO:0046961,,GO:0046961,0.0612,0.1546,0.0612,,0.0612,4,0.0846,0.4997,no
CREL1_XENTR,A0A6I8RMG7,Prot2Text,Eukaryota,410,Protein disulfide isomerase. Promotes the localization of acetylcholine receptors (AChRs) to the plasma membrane.,Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Mediates the endocytosis of the KCNMA1 channel and the subsequent transactivation of the downstream calcium ions. Has a role in angiogenesis and in the development of cardiac hypertrophy and hypertrophy.,No,No,No,No,No,not-Yes,GO:0005509; GO:0003756,,,GO:0015459,GO:0015459,GO:0015459,,,0.0909,0.0909,0.0909,3,0.0909,0.4997,no
CREL1_XENTR,A0A6I8RMG7,ProtT3,Eukaryota,410,Protein disulfide isomerase. Promotes the localization of acetylcholine receptors (AChRs) to the plasma membrane.,Calcium-regulated proprotein convertase involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins in the endoplasmic reticulum (ER) lumen (By similarity). Catalyzes the cleavage of the C-terminal peptide from nascent proteins that are misfolded in the ER lumen (By similarity). Endoplasmic reticulum membrane; Single-pass type II membrane protein. Belongs to the CCP1 family,No,No,No,No,No,not-Yes,GO:0005509; GO:0003756,GO:0004252,GO:0008233,GO:0004252; GO:0005509,GO:0004175,GO:0004252,0.2229,0.3342,0.6518,0.2912,0.2229,5,0.3446,0.4997,no
CREL1_XENTR,A0A6I8RMG7,ProtTale,Eukaryota,410,Protein disulfide isomerase. Promotes the localization of acetylcholine receptors (AChRs) to the plasma membrane.,Acts as a ligand for integrin alpha-V/beta-3 (ITGA-V:ITGB-3) and integrin alpha-V/beta-5 (ITGA-V:ITGB-5). May play a role in angiogenesis.,No,No,No,No,No,not-Yes,GO:0005509; GO:0003756,,,,,,,,,,,0,,0.4997,no
CREL1_XENTR,A0A6I8RMG7,Protein2Text,Eukaryota,410,Protein disulfide isomerase. Promotes the localization of acetylcholine receptors (AChRs) to the plasma membrane.,"The molecular function of this protein is not explicitly stated in the provided text. However, based on the information that it is involved in a signaling pathway and has a role in regulating the behavior of other proteins, it is likely that the protein is involved in protein-protein interactions and possibly in signal transduction. 

However, according to the UniProt database, this protein is involved in the following molecular functions:

* Glycosaminoglycan binding: It is involved in the binding of glycosaminoglycans, which are carbohydrate molecules that are attached to proteins or lipids and play a crucial role in various biological processes.
* Protein homooligomerization: It is involved in the formation of homooligomers, which are complexes of multiple copies of the same protein.
* Protein binding: It is involved in the binding of other proteins, which suggests that it may play a role in protein-protein interactions.

Please note that this information is based on external sources and may not be comprehensive or up-to-date.",No,Vague,Vague,Vague,No,not-Yes,GO:0005509; GO:0003756,,,,GO:0005539,GO:0005539,,,,0.2117,0.2117,2,0.2117,0.4997,no
CREL1_XENTR,A0A6I8RMG7,Reference,Eukaryota,410,Protein disulfide isomerase. Promotes the localization of acetylcholine receptors (AChRs) to the plasma membrane.,Protein disulfide isomerase. Promotes the localization of acetylcholine receptors (AChRs) to the plasma membrane.,,,,,,,GO:0005509; GO:0003756,GO:0003756,GO:0003756,GO:0003756,GO:0003756,GO:0003756,0.6958,0.6958,0.6958,0.6958,0.6958,5,0.6958,0.4997,no
CGLR_FRAOC,A0A6J1SUS3,ESM2Text,Eukaryota,431,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Transcription elongation factor component of the PET complex, a multiprotein complex involved in autophagy. The PET complex increases the DNA-binding affinity of the autophagy apparatus and increases the processivity of autophagy by inhibiting autophagosome formation. Required for maintenance of steady-state levels of ATG9 and ULK1 at the pre-autophagosomal structure (PAS) and the normal mitophagy response. The PET complex acts at the PAS to stimulate autophagosome formation: the complex associates with ATG9 at the PAS, and acts by enhancing ATG9-mediated phosphorylation of LCFAs and subsequent activation of pre-autophagosomal structure. The PET complex is required for maintenance of cell morphology and motility.",No,No,No,No,No,not-Yes,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,GO:0052621,GO:0052621,GO:0052621,GO:0052929,GO:0052621,0.2426,0.2426,0.2426,0.1747,0.2426,5,0.229,0.6228,yes
CGLR_FRAOC,A0A6J1SUS3,Prot2Text,Eukaryota,431,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",TnsABC + TnsD promote high-frequency insertion of Tn7 into a specific target site known as att-Tn7 whereas TnsABC + TnsE promote low-frequency insertion into many different sites.,No,No,No,No,No,not-Yes,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,,,,,,,,,,,0,,0.6228,yes
CGLR_FRAOC,A0A6J1SUS3,ProtT3,Eukaryota,431,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity (By similarity). Acts by mediating formation of 2',3'-cGAMP, a second messenger that binds to and activates cGAS (By similarity). 2',3'-cGAMP acts as a second messenger that binds to and activates cGAS, leading to production of cyclic GMP-AMP (2',3'-cGAMP), a second messenger that binds to",Yes,Yes,Yes,Yes,Yes,Yes,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,GO:0061501; GO:0005524; GO:0005525,GO:0009975,GO:0016779; GO:0005525; GO:0005524,GO:0061501,GO:0061501,0.7329,0.1946,0.6782,0.3401,0.3401,5,0.4572,0.6228,yes
CGLR_FRAOC,A0A6J1SUS3,ProtTale,Eukaryota,431,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Synthesizes 2',3'-cGAMP in a two-step reaction through production of the linear intermediate pppA(2'-5')pG. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of",Yes,Yes,Yes,Yes,Yes,Yes,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,GO:0016779; GO:0003725,GO:0009975; GO:0003690,GO:0061501; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,0.5219,0.464,0.5835,0.5219,0.5219,5,0.5226,0.6228,yes
CGLR_FRAOC,A0A6J1SUS3,Protein2Text,Eukaryota,431,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","The molecular function of this protein is a cytoplasmic sensor of double-stranded RNA (dsRNA) and it is involved in antiviral immunity. It plays a crucial role in recognizing dsRNA produced by viruses and triggering the innate immune response. Specifically, it acts as a guanylate-binding protein (GBP) that binds to dsRNA and activates downstream signaling pathways to induce antiviral activity.",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,GO:0003725,GO:0003676,GO:0003676,,,0.3942,0.4583,0.4583,,,3,0.4369,0.6228,yes
CGLR_FRAOC,A0A6J1SUS3,Reference,Eukaryota,431,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",,,,,,,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,GO:0016779; GO:0003725,GO:0061501; GO:0003725,GO:0016779; GO:0003725,GO:0097617; GO:0003725,GO:0061501; GO:0003725,0.5219,0.5835,0.5219,0.4071,0.5835,5,0.5236,0.6228,yes
CDND_SALEB,A0A728KSL7,ESM2Text,Bacteria,381,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (Probable). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection (Probable).","Cyclic dinucleotide synthase that catalyzes the synthesis of c-di-GMP, has no activity with other NTP substrates.",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005525; GO:0046872; GO:0016779,GO:0052621,GO:0052621,GO:0052621,GO:0052929,GO:0052621,0.4652,0.4652,0.4652,0.3293,0.4652,5,0.438,0.5505,yes
CDND_SALEB,A0A728KSL7,Prot2Text,Bacteria,381,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (Probable). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection (Probable).","Cyclic dinucleotide synthase that catalyzes the synthesis of c-di-GMP, has no activity with other NTP substrates.",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005525; GO:0046872; GO:0016779,GO:0052929,GO:0052621,GO:0052621,GO:0052621,GO:0052929,0.3293,0.4652,0.4652,0.4652,0.3293,5,0.4108,0.5505,yes
CDND_SALEB,A0A728KSL7,ProtT3,Bacteria,381,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (Probable). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection (Probable).","CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection (By similarity). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005525; GO:0046872; GO:0016779,GO:0016779,GO:0009975,GO:0016779,GO:0016779,GO:0016779,0.542,0.2648,0.542,0.542,0.542,5,0.4866,0.5505,yes
CDND_SALEB,A0A728KSL7,ProtTale,Bacteria,381,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (Probable). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection (Probable).","Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type I-D(GG) CBASS system.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005525; GO:0046872; GO:0016779,GO:0016779,GO:0009975,GO:0061501,GO:0016779,GO:0016779,0.542,0.2648,0.4086,0.542,0.542,5,0.4599,0.5505,yes
CDND_SALEB,A0A728KSL7,Protein2Text,Bacteria,381,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (Probable). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection (Probable).","This protein is a DNA helicase, which is a type of enzyme that plays a crucial role in DNA replication and repair. Specifically, it is involved in unwinding double-stranded DNA into single strands, allowing other enzymes to access the DNA and perform their functions. The molecular function of this protein is to unwind DNA, which is essential for various cellular processes such as DNA replication, repair, and transcription. 

In more detail, the protein has the ability to unwind DNA in an ATP-dependent manner, which means that it requires energy from ATP to perform its function. This protein is also known to have a preference for DNA with a specific structure, such as DNA with a forked or branched structure. The molecular function of this protein is critical for maintaining genome stability and ensuring proper DNA replication and repair. 

It's worth noting that the specific molecular function of this protein may vary depending on the organism and the context in which it is expressed. However, in general, this protein plays a crucial role in DNA metabolism and is essential for maintaining genome stability.",No,No,No,No,No,not-Yes,GO:0005525; GO:0046872; GO:0016779,GO:0004003; GO:0005524,GO:0003678,GO:0003678,GO:0003678,GO:0003678,0.4303,0.1262,0.1262,0.1262,0.1262,5,0.187,0.5505,yes
CDND_SALEB,A0A728KSL7,Reference,Bacteria,381,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (Probable). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection (Probable).","Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system (Probable). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection (Probable).",,,,,,,GO:0005525; GO:0046872; GO:0016779,GO:0016779,GO:0016779,GO:0016779,GO:0097617,GO:0061501,0.542,0.542,0.542,0.1864,0.4086,5,0.4442,0.5505,yes
IDI_CANSA,A0A7C9FSB8,ESM2Text,Eukaryota,287,"Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).","Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004452; GO:0046872,GO:0004452,GO:0004452,GO:0004452,GO:0004452,GO:0004452,0.6963,0.6963,0.6963,0.6963,0.6963,5,0.6963,0.1115,no
IDI_CANSA,A0A7C9FSB8,Prot2Text,Eukaryota,287,"Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).","Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004452; GO:0046872,GO:0004452,GO:0004452,GO:0004452,GO:0004452,GO:0004452,0.6963,0.6963,0.6963,0.6963,0.6963,5,0.6963,0.1115,no
IDI_CANSA,A0A7C9FSB8,ProtT3,Eukaryota,287,"Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).","Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Plastid, chloroplast. Belongs to the IPP isomerase type 1 family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004452; GO:0046872,GO:0004452,GO:0004452,GO:0004452,GO:0004452,GO:0004452,0.6963,0.6963,0.6963,0.6963,0.6963,5,0.6963,0.1115,no
IDI_CANSA,A0A7C9FSB8,ProtTale,Eukaryota,287,"Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).","Catalyzes the hydrolysis of a carbon-carbon bond at an alpha-position of an acyl group in an acyl-CoA ester, leading to the formation of free fatty acids and acetoacetyl-CoA.",No,No,No,No,No,not-Yes,GO:0004452; GO:0046872,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016787,0.2894,0.2894,0.2894,0.2894,0.2894,5,0.2894,0.1115,no
IDI_CANSA,A0A7C9FSB8,Protein2Text,Eukaryota,287,"Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).","The molecular function of this protein is a methyltransferase, specifically a 2,3-dimethylxanthine methyltransferase.",No,No,No,No,No,not-Yes,GO:0004452; GO:0046872,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.1917,0.1917,0.1917,0.1917,0.1917,5,0.1917,0.1115,no
IDI_CANSA,A0A7C9FSB8,Reference,Eukaryota,287,"Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).","Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).",,,,,,,GO:0004452; GO:0046872,GO:0004452,GO:0004452,GO:0004452,GO:0004452,GO:0004452,0.6963,0.6963,0.6963,0.6963,0.6963,5,0.6963,0.1115,no
HDR_CANSA,A0A7J6F8C5,ESM2Text,Eukaryota,464,Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that converts 1-hydroxy-2-methyl-2-(E)-butenyl 4- diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Is essential for chloroplast development.,Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Is essential for chloroplast development.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0051539; GO:0051745; GO:0046872,GO:0051745,GO:0016491,GO:0051745,GO:0051745,GO:0051745,0.5444,0.3799,0.5444,0.5444,0.5444,5,0.5115,0.2011,no
HDR_CANSA,A0A7J6F8C5,Prot2Text,Eukaryota,464,Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that converts 1-hydroxy-2-methyl-2-(E)-butenyl 4- diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Is essential for chloroplast development.,Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Is essential for chloroplast development.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0051539; GO:0051745; GO:0046872,GO:0046429,GO:0046429,GO:0051745,GO:0051745,GO:0051745,0.4089,0.4089,0.5444,0.5444,0.5444,5,0.4902,0.2011,no
HDR_CANSA,A0A7J6F8C5,ProtT3,Eukaryota,464,Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that converts 1-hydroxy-2-methyl-2-(E)-butenyl 4- diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Is essential for chloroplast development.,"Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. Plastid, chloroplast. Belongs to the IspH family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0051539; GO:0051745; GO:0046872,GO:0046429,GO:0046429,GO:0046429,GO:0046429,GO:0046429,0.4089,0.4089,0.4089,0.4089,0.4089,5,0.4089,0.2011,no
HDR_CANSA,A0A7J6F8C5,ProtTale,Eukaryota,464,Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that converts 1-hydroxy-2-methyl-2-(E)-butenyl 4- diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Is essential for chloroplast development.,"N(6)-(pyridoxal phosphate)-L-lysine reductase (PLPR) that catalyzes the NADPH-dependent reduction of N(6)- (pyridoxal phosphate)-L-lysine to form N(6)-(pyridoxal phosphate)-L-lysine mononucleotide, the first step of de novo lysine biosynthesis.",No,No,No,No,No,not-Yes,GO:0051539; GO:0051745; GO:0046872,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.3799,0.3799,0.3799,0.3799,0.3799,5,0.3799,0.2011,no
HDR_CANSA,A0A7J6F8C5,Protein2Text,Eukaryota,464,Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that converts 1-hydroxy-2-methyl-2-(E)-butenyl 4- diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Is essential for chloroplast development.,"The molecular function of the protein is a cysteine desulfurase, which catalyzes the removal of sulfur from cysteine to produce 2-aminoadipate semialdehyde and elemental sulfur. This process is essential for the biosynthesis of cofactors such as iron-sulfur clusters and molybdenum cofactor.",No,No,No,No,No,not-Yes,GO:0051539; GO:0051745; GO:0046872,GO:0031071,GO:0031071,GO:0031071,GO:0031071,GO:0031071,0.1443,0.1443,0.1443,0.1443,0.1443,5,0.1443,0.2011,no
HDR_CANSA,A0A7J6F8C5,Reference,Eukaryota,464,Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that converts 1-hydroxy-2-methyl-2-(E)-butenyl 4- diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Is essential for chloroplast development.,Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that converts 1-hydroxy-2-methyl-2-(E)-butenyl 4- diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Is essential for chloroplast development.,,,,,,,GO:0051539; GO:0051745; GO:0046872,GO:0051745,GO:0051745,GO:0016491,GO:0016491,GO:0016491,0.5444,0.5444,0.3799,0.3799,0.3799,5,0.4457,0.2011,no
ATG4_TOXGO,A0A7J6K805,ESM2Text,Eukaryota,3753,"Putative peptidase that may process C-terminus of ATG8, possibly to regulate ATG8 membrane association. Required for apicoplast biogenesis. Required for maintaining mitochondrial network integrity. Plays a role in intracellular multiplication of tachyzoites.",Involved in the regulation of mitochondrial morphology and distribution. May act as negative regulator of NADPH oxidase.,No,No,Vague,Vague,No,not-Yes,GO:0004197; GO:0019786,,,,,,,,,,,0,,0.7736,yes
ATG4_TOXGO,A0A7J6K805,Prot2Text,Eukaryota,3753,"Putative peptidase that may process C-terminus of ATG8, possibly to regulate ATG8 membrane association. Required for apicoplast biogenesis. Required for maintaining mitochondrial network integrity. Plays a role in intracellular multiplication of tachyzoites.",Involved in the regulation of mitochondrial morphology and distribution. May act as negative regulator of NADPH oxidase.,No,No,Vague,Vague,No,not-Yes,GO:0004197; GO:0019786,,,,,,,,,,,0,,0.7736,yes
ATG4_TOXGO,A0A7J6K805,ProtT3,Eukaryota,3753,"Putative peptidase that may process C-terminus of ATG8, possibly to regulate ATG8 membrane association. Required for apicoplast biogenesis. Required for maintaining mitochondrial network integrity. Plays a role in intracellular multiplication of tachyzoites.",Cytoplasm Nucleus,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004197; GO:0019786,,,,,,,,,,,0,,0.7736,yes
ATG4_TOXGO,A0A7J6K805,ProtTale,Eukaryota,3753,"Putative peptidase that may process C-terminus of ATG8, possibly to regulate ATG8 membrane association. Required for apicoplast biogenesis. Required for maintaining mitochondrial network integrity. Plays a role in intracellular multiplication of tachyzoites.",Essential component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup98-Nup107-160 subcomplex may play a role in stress response.,No,No,No,No,No,not-Yes,GO:0004197; GO:0019786,,,,,,,,,,,0,,0.7736,yes
ATG4_TOXGO,A0A7J6K805,Protein2Text,Eukaryota,3753,"Putative peptidase that may process C-terminus of ATG8, possibly to regulate ATG8 membrane association. Required for apicoplast biogenesis. Required for maintaining mitochondrial network integrity. Plays a role in intracellular multiplication of tachyzoites.","This protein is a transcriptional regulator, which means it helps control the activity of genes by binding to specific DNA sequences and recruiting other proteins to regulate gene expression.",No,No,No,No,No,not-Yes,GO:0004197; GO:0019786,GO:0003700; GO:0003677,GO:0003700,GO:0003700,GO:0003700,GO:0003700,0.1637,0.1674,0.1674,0.1674,0.1674,5,0.1667,0.7736,yes
ATG4_TOXGO,A0A7J6K805,Reference,Eukaryota,3753,"Putative peptidase that may process C-terminus of ATG8, possibly to regulate ATG8 membrane association. Required for apicoplast biogenesis. Required for maintaining mitochondrial network integrity. Plays a role in intracellular multiplication of tachyzoites.","Putative peptidase that may process C-terminus of ATG8, possibly to regulate ATG8 membrane association. Required for apicoplast biogenesis. Required for maintaining mitochondrial network integrity. Plays a role in intracellular multiplication of tachyzoites.",,,,,,,GO:0004197; GO:0019786,GO:0008233,,,GO:0008233,GO:0008233,0.7233,,,0.7233,0.7233,3,0.7233,0.7736,yes
ADHB_ASPFN,A0A7U2MMF3,ESM2Text,Eukaryota,428,"Zinc-type alcohol dehydrogenase involved in development, secondary metabolism, pathogenicity, and stress response. Specifically controls the formation of sclerotia and the biosynthesis of aflatoxin. Contribute to seed colonization of A flavus on host maize seed.","Oxidizes primary as well as secondary alcohols. Allows the use of a wide range of primary alcohols as primary alcohols. Highest catalytic efficiency for racemic primary alcohols is 50% in the presence of NADP(+). Can also catalyze the reverse reaction, i.e. the NADPH-dependent reduction of 5-keto-4-ene-3-beta-ol to yield trans-2,4-didehydro-L-proline.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004022; GO:0008270,GO:0016614,GO:0016614,GO:0016614,GO:0016614,,0.4649,0.4649,0.4649,0.4649,,4,0.4649,0.1673,no
ADHB_ASPFN,A0A7U2MMF3,Prot2Text,Eukaryota,428,"Zinc-type alcohol dehydrogenase involved in development, secondary metabolism, pathogenicity, and stress response. Specifically controls the formation of sclerotia and the biosynthesis of aflatoxin. Contribute to seed colonization of A flavus on host maize seed.",Alcohol dehydrogenase. Oxidizes primary as well as secondary alcohols. Ethanol is a very poor substrate.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004022; GO:0008270,GO:0004022,GO:0004022,GO:0004022,GO:0004022,GO:0004022,0.6861,0.6861,0.6861,0.6861,0.6861,5,0.6861,0.1673,no
ADHB_ASPFN,A0A7U2MMF3,ProtT3,Eukaryota,428,"Zinc-type alcohol dehydrogenase involved in development, secondary metabolism, pathogenicity, and stress response. Specifically controls the formation of sclerotia and the biosynthesis of aflatoxin. Contribute to seed colonization of A flavus on host maize seed.",Cytoplasm. Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004022; GO:0008270,GO:0004024; GO:0008270,GO:0016491; GO:0008270,GO:0016491; GO:0008270,GO:0016491; GO:0008270,GO:0016491,0.6861,0.7691,0.7691,0.7691,0.4017,5,0.679,0.1673,no
ADHB_ASPFN,A0A7U2MMF3,ProtTale,Eukaryota,428,"Zinc-type alcohol dehydrogenase involved in development, secondary metabolism, pathogenicity, and stress response. Specifically controls the formation of sclerotia and the biosynthesis of aflatoxin. Contribute to seed colonization of A flavus on host maize seed.","Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Can utilize both NAD(+) and NADP(+) as electron acceptor. Is involved in a degradation pathway of D-glucose that does not involve intermediate formation of fructose 1,6-bisphosphate.",No,No,No,No,No,not-Yes,GO:0004022; GO:0008270,GO:0004345; GO:0016616,GO:0004345; GO:0016616,GO:0016614,GO:0016616,GO:0016614,0.5559,0.5559,0.4649,0.53,0.4649,5,0.5143,0.1673,no
ADHB_ASPFN,A0A7U2MMF3,Protein2Text,Eukaryota,428,"Zinc-type alcohol dehydrogenase involved in development, secondary metabolism, pathogenicity, and stress response. Specifically controls the formation of sclerotia and the biosynthesis of aflatoxin. Contribute to seed colonization of A flavus on host maize seed.","The molecular function of this protein is an oxidoreductase activity, specifically a zinc-dependent alcohol dehydrogenase activity. It catalyzes the oxidation of primary and secondary alcohols to their corresponding aldehydes or ketones, using NAD+ as the electron acceptor.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004022; GO:0008270,GO:0004024,GO:0004024,GO:0004024,GO:0004024,GO:0004024,0.0,0.0,0.0,0.0,0.0,5,0.0,0.1673,no
ADHB_ASPFN,A0A7U2MMF3,Reference,Eukaryota,428,"Zinc-type alcohol dehydrogenase involved in development, secondary metabolism, pathogenicity, and stress response. Specifically controls the formation of sclerotia and the biosynthesis of aflatoxin. Contribute to seed colonization of A flavus on host maize seed.","Zinc-type alcohol dehydrogenase involved in development, secondary metabolism, pathogenicity, and stress response. Specifically controls the formation of sclerotia and the biosynthesis of aflatoxin. Contribute to seed colonization of A flavus on host maize seed.",,,,,,,GO:0004022; GO:0008270,GO:0004024,GO:0004024,GO:0004024,GO:0004024,GO:0016616; GO:0008270,0.0,0.0,0.0,0.0,0.8769,5,0.1754,0.1673,no
CDNB_BACFG,A0A853PXE5,ESM2Text,Bacteria,341,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system (Probable).",Exonuclease which shows higher activity towards intronless RNA substrates than RNA oligonucleotides. Has a higher activity towards DNA oligonucleotides than double-stranded DNA. Involved in the activation of the classical pathway of the complement and repair of double-stranded DNA breaks.,No,No,No,No,No,not-Yes,GO:0140701; GO:0005524; GO:0005525; GO:0046872,GO:0004532,GO:0004527,GO:0004527,GO:0004527,,0.0836,0.1092,0.1092,0.1092,,4,0.1028,0.4994,no
CDNB_BACFG,A0A853PXE5,Prot2Text,Bacteria,341,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system (Probable).","Cyclic dinucleotide synthase that catalyzes the synthesis of 3'3'-cyclic GMP-AMP (cGAMP) from GTP and ATP, and of c-di-AMP and c-di-GMP, that are second messengers for cell signal transduction.",Yes,Yes,Yes,Maybe,Maybe,Yes,GO:0140701; GO:0005524; GO:0005525; GO:0046872,GO:0061501,,GO:0061501,GO:0061501,GO:0016779,0.3341,,0.3341,0.3341,0.3478,4,0.3375,0.4994,no
CDNB_BACFG,A0A853PXE5,ProtT3,Bacteria,341,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system (Probable).","CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type III-A(C) CBASS system (By similarity). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate",Yes,Yes,Yes,Yes,Yes,Yes,GO:0140701; GO:0005524; GO:0005525; GO:0046872,GO:0016779,GO:0009975,GO:0016779,GO:0016779,GO:0016779,0.3478,0.1935,0.3478,0.3478,0.3478,5,0.3169,0.4994,no
CDNB_BACFG,A0A853PXE5,ProtTale,Bacteria,341,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system (Probable).","Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type I-D(GG) CBASS system.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0140701; GO:0005524; GO:0005525; GO:0046872,GO:0016779,GO:0009975,GO:0061501,GO:0016779,GO:0016779,0.3478,0.1935,0.3341,0.3478,0.3478,5,0.3142,0.4994,no
CDNB_BACFG,A0A853PXE5,Protein2Text,Bacteria,341,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system (Probable).","This protein is a viral endonuclease, which means it is involved in the cleavage of DNA. Specifically, it is a restriction enzyme that recognizes and cleaves a particular sequence of DNA. It is also involved in the replication of viral DNA. 
In more detail, the molecular function of this protein is to cleave DNA at specific recognition sites, which helps to control the replication of viral DNA. This is an important function for the virus, as it allows the virus to take control of the host cell's DNA replication machinery and produce new viral DNA for infection of other cells. The protein works by binding to a specific sequence of DNA and cutting the DNA at that site, resulting in the release of a fragment of DNA. This fragment can then be used by the virus to replicate its DNA and produce new viral particles.",No,No,No,No,No,not-Yes,GO:0140701; GO:0005524; GO:0005525; GO:0046872,GO:0004519,GO:0004519,GO:0004519,GO:0004519,GO:0004519,0.1289,0.1289,0.1289,0.1289,0.1289,5,0.1289,0.4994,no
CDNB_BACFG,A0A853PXE5,Reference,Bacteria,341,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system (Probable).","Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(GA) CBASS system (Probable).",,,,,,,GO:0140701; GO:0005524; GO:0005525; GO:0046872,GO:0016779,GO:0016779,GO:0016779,GO:0097617,GO:0061501,0.3478,0.3478,0.3478,0.1612,0.3341,5,0.3077,0.4994,no
GUN5_MICS2,A0A8A1G1R1,ESM2Text,Bacteria,514,"Endoglucanase that exhibits highest activity toward barley beta-glucan, lower activity toward carboxymethyl cellulose (CMC-Na), and marginal activity toward laminarin and xylan.","Inhibits endo-1,4-beta-glucanase and is thought to be involved in the degradation of cellulose. Has also no activity toward cellobiose and mannobiose.",Maybe,No,No,No,Maybe,not-Yes,GO:0030246; GO:0008810,GO:0004857,,,,GO:0004857,0.1616,,,,0.1616,2,0.1616,0.2514,no
GUN5_MICS2,A0A8A1G1R1,Prot2Text,Bacteria,514,"Endoglucanase that exhibits highest activity toward barley beta-glucan, lower activity toward carboxymethyl cellulose (CMC-Na), and marginal activity toward laminarin and xylan.","Hydrolyzes 1,4-beta linked polysaccharide backbones of mannans. Does not hydrolyze carboxymethylcellulose (CMC).",No,No,No,No,No,not-Yes,GO:0030246; GO:0008810,GO:0016985,GO:0016985,GO:0016985,GO:0016985,GO:0016985,0.4174,0.4174,0.4174,0.4174,0.4174,5,0.4174,0.2514,no
GUN5_MICS2,A0A8A1G1R1,ProtT3,Bacteria,514,"Endoglucanase that exhibits highest activity toward barley beta-glucan, lower activity toward carboxymethyl cellulose (CMC-Na), and marginal activity toward laminarin and xylan.",Belongs to the glycosyl hydrolase 5 (cellulase A) family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0030246; GO:0008810,GO:0008810,GO:0008810,GO:0008810,GO:0008810,GO:0008810,0.7193,0.7193,0.7193,0.7193,0.7193,5,0.7193,0.2514,no
GUN5_MICS2,A0A8A1G1R1,ProtTale,Bacteria,514,"Endoglucanase that exhibits highest activity toward barley beta-glucan, lower activity toward carboxymethyl cellulose (CMC-Na), and marginal activity toward laminarin and xylan.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.",No,No,No,No,No,not-Yes,GO:0030246; GO:0008810,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,0.4694,0.4694,0.4694,0.4694,0.4694,5,0.4694,0.2514,no
GUN5_MICS2,A0A8A1G1R1,Protein2Text,Bacteria,514,"Endoglucanase that exhibits highest activity toward barley beta-glucan, lower activity toward carboxymethyl cellulose (CMC-Na), and marginal activity toward laminarin and xylan.","The molecular function of this protein is not explicitly stated in the provided text, but based on its name and the context in which it is mentioned, it can be inferred that it is a glycosyl hydrolase, which is an enzyme that breaks down complex carbohydrates into simpler sugars. More specifically, it is likely a beta-glucosidase, which is an enzyme that catalyzes the hydrolysis of beta-glucosidic linkages in complex carbohydrates. However, this is a generalization and the specific molecular function of this protein would require further research to determine. 
In the provided text, it is stated that this protein is involved in breaking down cellulose, which is a complex carbohydrate that consists of beta-glucosidic linkages. This suggests that it is a beta-glucosidase, but this is not explicitly stated. 

If you need more information, please let me know.",Vague,Maybe,Vague,Vague,Maybe,not-Yes,GO:0030246; GO:0008810,GO:0008422,GO:0008422,GO:0008422,GO:0008422,GO:0008422,0.4694,0.4694,0.4694,0.4694,0.4694,5,0.4694,0.2514,no
GUN5_MICS2,A0A8A1G1R1,Reference,Bacteria,514,"Endoglucanase that exhibits highest activity toward barley beta-glucan, lower activity toward carboxymethyl cellulose (CMC-Na), and marginal activity toward laminarin and xylan.","Endoglucanase that exhibits highest activity toward barley beta-glucan, lower activity toward carboxymethyl cellulose (CMC-Na), and marginal activity toward laminarin and xylan.",,,,,,,GO:0030246; GO:0008810,GO:0008810,GO:0008810,GO:0008810,GO:0008810,GO:0008810,0.7193,0.7193,0.7193,0.7193,0.7193,5,0.7193,0.2514,no
ISRA_AMPFL,A0A8B0M7B9,ESM2Text,Eukaryota,7398,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. IsrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1. The adenylation domains (A domains) A2-A6 in isrA then select glycine, D-valine, D-leucine, L- alanine, and L-valine, respectively. IsrA is responsible for the biosynthesis of at least 7 different ISRs: felinotoxin G, isariins A, B, E, G1, G2, and nodupetide. The different length of the polyketide moieties in ISRs suggests the substrate promiscuities of isrB and isrC. The presence of an epimerization (E) domain in module 4 and the absence of methyltransferase (MT) domains in modules 5 and 6 are consistent with the three adjacent D-leucine, L-alanine, and L-valine residues in ISRs. The replacement of the L-alanine residue in felinotoxin G and isariin G2 by the L-valine residue in isariins A, B and G1 at corresponding positions may be attributed to the substrate promiscuity of A-6 domain in module 6.","Part of the gene cluster that mediates the biosynthesis of the mycotoxin cyclochlorotine, a hepatotoxic and carcinogenic cyclic chlorinated pentapeptide. Cyclochlorotine is formed by the nonproteinogenic amino acids L-2-aminobutyrate (2Abu), L-beta-phenylalanine (beta-Phe), the unique L-cis-3,4-dichloroproline Pro(Cl(2)) and two L-serines (Ser). The condensation of the 5 building blocks is performed by the cyclochlorotine synthetase cctN, a nonribosomal peptide synthetase. The assembled linear pentapeptide is then assumed to be released through cyclization by the terminal condensation-like domain of cctN. Incorporation of the alternative substrates allo-threonine or alanine by the domains A3 or A1 respectively may lead to the production of the variants hydroxy-cyclochlorotine and deoxy-cyclochlorotine, respectively. CctP probably acts as a phenylalanine aminomutase and provides the uncommon building block beta-Phe. The beta",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,,,,,,,,,,,0,,0.4682,no
ISRA_AMPFL,A0A8B0M7B9,Prot2Text,Eukaryota,7398,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. IsrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1. The adenylation domains (A domains) A2-A6 in isrA then select glycine, D-valine, D-leucine, L- alanine, and L-valine, respectively. IsrA is responsible for the biosynthesis of at least 7 different ISRs: felinotoxin G, isariins A, B, E, G1, G2, and nodupetide. The different length of the polyketide moieties in ISRs suggests the substrate promiscuities of isrB and isrC. The presence of an epimerization (E) domain in module 4 and the absence of methyltransferase (MT) domains in modules 5 and 6 are consistent with the three adjacent D-leucine, L-alanine, and L-valine residues in ISRs. The replacement of the L-alanine residue in felinotoxin G and isariin G2 by the L-valine residue in isariins A, B and G1 at corresponding positions may be attributed to the substrate promiscuity of A-6 domain in module 6.","Part of the gene cluster that mediates the biosynthesis of the mycotoxin cyclochlorotine, a hepatotoxic and carcinogenic cyclic chlorinated pentapeptide. Cyclochlorotine is formed by the nonproteinogenic amino acids L-2-aminobutyrate (2Abu), L-beta-phenylalanine (beta-Phe), the unique L-cis-3,4-dichloroproline Pro(Cl(2)) and two L-serines (Ser). The condensation of the 5 building blocks is performed by the cyclochlorotine synthetase cctN, a nonribosomal peptide synthetase. The assembled linear pentapeptide is then assumed to be released through cyclization by the terminal condensation-like domain of cctN. Incorporation of the alternative substrates allo-threonine or alanine by the domains A3 or A1 respectively may lead to the production of the variants hydroxy-cyclochlorotine and deoxy-cyclochlorotine, respectively. CctP probably acts as a phenylalanine aminomutase and provides the uncommon building block beta-Phe. The beta",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,,,,,,,,,,,0,,0.4682,no
ISRA_AMPFL,A0A8B0M7B9,ProtT3,Eukaryota,7398,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. IsrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1. The adenylation domains (A domains) A2-A6 in isrA then select glycine, D-valine, D-leucine, L- alanine, and L-valine, respectively. IsrA is responsible for the biosynthesis of at least 7 different ISRs: felinotoxin G, isariins A, B, E, G1, G2, and nodupetide. The different length of the polyketide moieties in ISRs suggests the substrate promiscuities of isrB and isrC. The presence of an epimerization (E) domain in module 4 and the absence of methyltransferase (MT) domains in modules 5 and 6 are consistent with the three adjacent D-leucine, L-alanine, and L-valine residues in ISRs. The replacement of the L-alanine residue in felinotoxin G and isariin G2 by the L-valine residue in isariins A, B and G1 at corresponding positions may be attributed to the substrate promiscuity of A-6 domain in module 6.","P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of austinol, a fungal meroterpenoid . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA . 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN . Further epoxidation",No,No,No,No,No,not-Yes,GO:0016874; GO:0031177,GO:0004497; GO:0020037,GO:0004497; GO:0020037,GO:0004497; GO:0020037,GO:0004497; GO:0020037; GO:0005506,GO:0004497,0.3606,0.3606,0.3606,0.3753,0.3561,5,0.3626,0.4682,no
ISRA_AMPFL,A0A8B0M7B9,ProtTale,Eukaryota,7398,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. IsrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1. The adenylation domains (A domains) A2-A6 in isrA then select glycine, D-valine, D-leucine, L- alanine, and L-valine, respectively. IsrA is responsible for the biosynthesis of at least 7 different ISRs: felinotoxin G, isariins A, B, E, G1, G2, and nodupetide. The different length of the polyketide moieties in ISRs suggests the substrate promiscuities of isrB and isrC. The presence of an epimerization (E) domain in module 4 and the absence of methyltransferase (MT) domains in modules 5 and 6 are consistent with the three adjacent D-leucine, L-alanine, and L-valine residues in ISRs. The replacement of the L-alanine residue in felinotoxin G and isariin G2 by the L-valine residue in isariins A, B and G1 at corresponding positions may be attributed to the substrate promiscuity of A-6 domain in module 6.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS). SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms. These initial steps feature the priming of an unusual benzoic acid starter unit onto",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,GO:0016491,GO:0016874,,,GO:0016874,0.4358,0.709,,,0.709,3,0.6179,0.4682,no
ISRA_AMPFL,A0A8B0M7B9,Protein2Text,Eukaryota,7398,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. IsrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1. The adenylation domains (A domains) A2-A6 in isrA then select glycine, D-valine, D-leucine, L- alanine, and L-valine, respectively. IsrA is responsible for the biosynthesis of at least 7 different ISRs: felinotoxin G, isariins A, B, E, G1, G2, and nodupetide. The different length of the polyketide moieties in ISRs suggests the substrate promiscuities of isrB and isrC. The presence of an epimerization (E) domain in module 4 and the absence of methyltransferase (MT) domains in modules 5 and 6 are consistent with the three adjacent D-leucine, L-alanine, and L-valine residues in ISRs. The replacement of the L-alanine residue in felinotoxin G and isariin G2 by the L-valine residue in isariins A, B and G1 at corresponding positions may be attributed to the substrate promiscuity of A-6 domain in module 6.","This protein is a structural component of the virus, specifically a capsid protein, which forms the protein shell that encloses the viral genome.",No,No,No,No,No,not-Yes,GO:0016874; GO:0031177,GO:0005198,GO:0005198,GO:0005198,GO:0005198,GO:0005198,0.2783,0.2783,0.2783,0.2783,0.2783,5,0.2783,0.4682,no
ISRA_AMPFL,A0A8B0M7B9,Reference,Eukaryota,7398,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. IsrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1. The adenylation domains (A domains) A2-A6 in isrA then select glycine, D-valine, D-leucine, L- alanine, and L-valine, respectively. IsrA is responsible for the biosynthesis of at least 7 different ISRs: felinotoxin G, isariins A, B, E, G1, G2, and nodupetide. The different length of the polyketide moieties in ISRs suggests the substrate promiscuities of isrB and isrC. The presence of an epimerization (E) domain in module 4 and the absence of methyltransferase (MT) domains in modules 5 and 6 are consistent with the three adjacent D-leucine, L-alanine, and L-valine residues in ISRs. The replacement of the L-alanine residue in felinotoxin G and isariin G2 by the L-valine residue in isariins A, B and G1 at corresponding positions may be attributed to the substrate promiscuity of A-6 domain in module 6.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. IsrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1. The adenylation domains (A domains) A2-A6 in isrA then select glycine, D-valine, D-leucine, L- alanine, and L-valine, respectively. IsrA is responsible for the biosynthesis of at least 7 different ISRs: felinotoxin G, isariins A, B, E, G1, G2, and nodupetide. The different length of the polyketide moieties in ISRs suggests the substrate promiscuities of isrB and isrC. The presence of an epimerization (E) domain in module 4 and the absence of methyltransferase (MT) domains in modules 5 and 6 are consistent with the three adjacent D-leucine, L-alanine, and L-valine residues in ISRs. The replacement of the L-alanine residue in felinotoxin G and isariin G2 by the L-valine residue in isariins A, B and G1 at corresponding positions may be attributed to the substrate promiscuity of A-6 domain in module 6.",,,,,,,GO:0016874; GO:0031177,GO:0016874,GO:0016874,GO:0016874,GO:0016874,GO:0016874,0.709,0.709,0.709,0.709,0.709,5,0.709,0.4682,no
CHI52_PAEXY,A0A8G1A3Q5,ESM2Text,Bacteria,523,"Acidic chitinase that displays a broad substrate specificity, showing the highest specific activity toward colloidal chitin, followed by ethylene glycol chitin and ball milled chitin, but exhibits no activity toward powdery chitin and chitosan. Hydrolyzes colloidal chitin and chitooligosaccharides with degree of polymerization 2-5 to release mainly N-acetyl chitobiose. Displays inhibition effects on the growth of some phytopathogenic fungi, including Alternaria alstroemeriae, Botrytis cinerea, Rhizoctonia solani, Sclerotinia sclerotiorum and Valsa mali.","Xylanase 1 is specific for high-hydroxylaminobenzene. The Xylobiose subunit penetrates into the cell membrane and is thought to anchor the enzyme to the cell membrane, where it exerts its enzymatic activity.",No,No,No,No,Maybe,not-Yes,GO:0030246; GO:0008061; GO:0008843,,GO:0031176,,,,,0.3356,,,,1,0.3356,0.373,no
CHI52_PAEXY,A0A8G1A3Q5,Prot2Text,Bacteria,523,"Acidic chitinase that displays a broad substrate specificity, showing the highest specific activity toward colloidal chitin, followed by ethylene glycol chitin and ball milled chitin, but exhibits no activity toward powdery chitin and chitosan. Hydrolyzes colloidal chitin and chitooligosaccharides with degree of polymerization 2-5 to release mainly N-acetyl chitobiose. Displays inhibition effects on the growth of some phytopathogenic fungi, including Alternaria alstroemeriae, Botrytis cinerea, Rhizoctonia solani, Sclerotinia sclerotiorum and Valsa mali.","Degrades chitin, chitotriose and chitobiose. Has weak activity against chitotetraose, chitopentaose, and chitin. Hydrolyzes glucosidic bonds with inversion of anomeric configuration.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0030246; GO:0008061; GO:0008843,GO:0004568,GO:0004568,GO:0004568,GO:0004568,GO:0004568,0.5056,0.5056,0.5056,0.5056,0.5056,5,0.5056,0.373,no
CHI52_PAEXY,A0A8G1A3Q5,ProtT3,Bacteria,523,"Acidic chitinase that displays a broad substrate specificity, showing the highest specific activity toward colloidal chitin, followed by ethylene glycol chitin and ball milled chitin, but exhibits no activity toward powdery chitin and chitosan. Hydrolyzes colloidal chitin and chitooligosaccharides with degree of polymerization 2-5 to release mainly N-acetyl chitobiose. Displays inhibition effects on the growth of some phytopathogenic fungi, including Alternaria alstroemeriae, Botrytis cinerea, Rhizoctonia solani, Sclerotinia sclerotiorum and Valsa mali.",Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily,Vague,Vague,Maybe,Vague,Vague,not-Yes,GO:0030246; GO:0008061; GO:0008843,GO:0004568,GO:0004568,GO:0004568,GO:0004568,GO:0004568,0.5056,0.5056,0.5056,0.5056,0.5056,5,0.5056,0.373,no
CHI52_PAEXY,A0A8G1A3Q5,ProtTale,Bacteria,523,"Acidic chitinase that displays a broad substrate specificity, showing the highest specific activity toward colloidal chitin, followed by ethylene glycol chitin and ball milled chitin, but exhibits no activity toward powdery chitin and chitosan. Hydrolyzes colloidal chitin and chitooligosaccharides with degree of polymerization 2-5 to release mainly N-acetyl chitobiose. Displays inhibition effects on the growth of some phytopathogenic fungi, including Alternaria alstroemeriae, Botrytis cinerea, Rhizoctonia solani, Sclerotinia sclerotiorum and Valsa mali.","Cleaves beta-1,4-glucosidic linkages.",No,No,No,No,No,not-Yes,GO:0030246; GO:0008061; GO:0008843,GO:0016798,GO:0004553,GO:0004553,GO:0004553,GO:0008810,0.42,0.4587,0.4587,0.4587,0.3878,5,0.4368,0.373,no
CHI52_PAEXY,A0A8G1A3Q5,Protein2Text,Bacteria,523,"Acidic chitinase that displays a broad substrate specificity, showing the highest specific activity toward colloidal chitin, followed by ethylene glycol chitin and ball milled chitin, but exhibits no activity toward powdery chitin and chitosan. Hydrolyzes colloidal chitin and chitooligosaccharides with degree of polymerization 2-5 to release mainly N-acetyl chitobiose. Displays inhibition effects on the growth of some phytopathogenic fungi, including Alternaria alstroemeriae, Botrytis cinerea, Rhizoctonia solani, Sclerotinia sclerotiorum and Valsa mali.","The molecular function of this protein is likely to be a lyase enzyme, specifically a glycoside hydrolase. It is involved in breaking down glycosidic bonds in polysaccharides, which are complex carbohydrates found in plant cell walls and other biomolecules. More specifically, it is a type of lyase that catalyzes the hydrolysis of glycosidic bonds using a covalent enzyme-substrate intermediate. The exact function of this protein would depend on the specific type of glycosidic bond it catalyzes, such as breaking down cellulose, hemicellulose, or pectin. However, without more information, it is difficult to determine the exact molecular function of this protein.",Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0030246; GO:0008061; GO:0008843,GO:0004553,GO:0016798,GO:0016798,GO:0016798,GO:0004553,0.4587,0.42,0.42,0.42,0.4587,5,0.4355,0.373,no
CHI52_PAEXY,A0A8G1A3Q5,Reference,Bacteria,523,"Acidic chitinase that displays a broad substrate specificity, showing the highest specific activity toward colloidal chitin, followed by ethylene glycol chitin and ball milled chitin, but exhibits no activity toward powdery chitin and chitosan. Hydrolyzes colloidal chitin and chitooligosaccharides with degree of polymerization 2-5 to release mainly N-acetyl chitobiose. Displays inhibition effects on the growth of some phytopathogenic fungi, including Alternaria alstroemeriae, Botrytis cinerea, Rhizoctonia solani, Sclerotinia sclerotiorum and Valsa mali.","Acidic chitinase that displays a broad substrate specificity, showing the highest specific activity toward colloidal chitin, followed by ethylene glycol chitin and ball milled chitin, but exhibits no activity toward powdery chitin and chitosan. Hydrolyzes colloidal chitin and chitooligosaccharides with degree of polymerization 2-5 to release mainly N-acetyl chitobiose. Displays inhibition effects on the growth of some phytopathogenic fungi, including Alternaria alstroemeriae, Botrytis cinerea, Rhizoctonia solani, Sclerotinia sclerotiorum and Valsa mali.",,,,,,,GO:0030246; GO:0008061; GO:0008843,GO:0004568,GO:0004568,GO:0004568,GO:0004568,GO:0004568,0.5056,0.5056,0.5056,0.5056,0.5056,5,0.5056,0.373,no
CGCS_COLGL,A0A8H4CUY8,ESM2Text,Eukaryota,760,"Bifunctional terpene synthase that converts dimethylallyl diphosphate (DMAPP) and isopentenyl diphosphate (IPP) into colleterpenol as a single product. The C-terminal prenyltransferase (PT) domain of CgCS catalyzes formation of hexaprenyl diphosphate (HexPP), whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of HexPP to colleterpenol.","Bifunctional enzyme that catalyzes the sequential condensation of isopentenyl pyrophosphate (IPP) with geranylgeranyl diphosphate (GGPP) to form geranylgeranyl pyrophosphate (GGPP), and the isoprenoid-microsphingoid cyclic dihydroxyl (HIP) with GGPP to form myrcene. GGPP is a precursor for the C20 alkaloid bicyclic diterpene dimycocerosate (DIM A).",Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016829; GO:0046872; GO:0004659,,GO:0016765,,,,,0.5726,,,,1,0.5726,0.2366,no
CGCS_COLGL,A0A8H4CUY8,Prot2Text,Eukaryota,760,"Bifunctional terpene synthase that converts dimethylallyl diphosphate (DMAPP) and isopentenyl diphosphate (IPP) into colleterpenol as a single product. The C-terminal prenyltransferase (PT) domain of CgCS catalyzes formation of hexaprenyl diphosphate (HexPP), whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of HexPP to colleterpenol.","Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of the diterpenoid pyrones subglutinols A and B. The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpasA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpasD through the action of the prenyltransferase dpasC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpasE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpasB (Probable). The short chain dehydrogenase/reductase dpasF is then involved in tetrah",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016829; GO:0046872; GO:0004659,GO:0004311,GO:0004337,GO:0004311,GO:0004337,GO:0004337,0.4756,0.4756,0.4756,0.4756,0.4756,5,0.4756,0.2366,no
CGCS_COLGL,A0A8H4CUY8,ProtT3,Eukaryota,760,"Bifunctional terpene synthase that converts dimethylallyl diphosphate (DMAPP) and isopentenyl diphosphate (IPP) into colleterpenol as a single product. The C-terminal prenyltransferase (PT) domain of CgCS catalyzes formation of hexaprenyl diphosphate (HexPP), whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of HexPP to colleterpenol.","Bifunctional sesterterpene synthase; part of the gene cluster that mediates the biosynthesis of the sesterterpenes penitrems . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase ptmA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). DMOA is then prenylated by the polyprenyl transferase ptmC to form 3",Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016829; GO:0046872; GO:0004659,GO:0004659; GO:0010333,GO:0004659; GO:0010333,GO:0004659; GO:0010333,GO:0004659; GO:0010333,GO:0004659; GO:0010333,0.6617,0.6617,0.6617,0.6617,0.6617,5,0.6617,0.2366,no
CGCS_COLGL,A0A8H4CUY8,ProtTale,Eukaryota,760,"Bifunctional terpene synthase that converts dimethylallyl diphosphate (DMAPP) and isopentenyl diphosphate (IPP) into colleterpenol as a single product. The C-terminal prenyltransferase (PT) domain of CgCS catalyzes formation of hexaprenyl diphosphate (HexPP), whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of HexPP to colleterpenol.","Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD). Within the cluster, the alpha-amyrin synthase alpha-AS is responsible for the formation of pimara-8(14),15-diene from farnesyl diphosphate (FPP). The next step is the oxidation of pimara-8(14),15-diene by the oxidase PDO to yield pimara-8(14),1",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016829; GO:0046872; GO:0004659,GO:0010333,GO:0010334,GO:0010333,GO:0016829,GO:0010333,0.382,0.34,0.382,0.6412,0.382,5,0.4254,0.2366,no
CGCS_COLGL,A0A8H4CUY8,Protein2Text,Eukaryota,760,"Bifunctional terpene synthase that converts dimethylallyl diphosphate (DMAPP) and isopentenyl diphosphate (IPP) into colleterpenol as a single product. The C-terminal prenyltransferase (PT) domain of CgCS catalyzes formation of hexaprenyl diphosphate (HexPP), whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of HexPP to colleterpenol.","This protein is involved in the biosynthesis of terpenes, specifically a class of compounds called sesquiterpenes. More specifically, it is a sesquiterpene synthase, which means it catalyzes the conversion of farnesyl diphosphate (FPP) into sesquiterpenes. Sesquiterpenes are a type of natural product that have a wide range of biological activities and are found in many organisms, including plants, fungi, and bacteria. They play important roles in various processes such as defense against pathogens, signaling, and stress responses. In the case of this protein, it is likely involved in the production of sesquiterpenes that play a role in the plant's defense against pathogens or other environmental stresses.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016829; GO:0046872; GO:0004659,GO:0010333,GO:0016829,,GO:0010333,GO:0010333,0.382,0.6412,,0.382,0.382,4,0.4468,0.2366,no
CGCS_COLGL,A0A8H4CUY8,Reference,Eukaryota,760,"Bifunctional terpene synthase that converts dimethylallyl diphosphate (DMAPP) and isopentenyl diphosphate (IPP) into colleterpenol as a single product. The C-terminal prenyltransferase (PT) domain of CgCS catalyzes formation of hexaprenyl diphosphate (HexPP), whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of HexPP to colleterpenol.","Bifunctional terpene synthase that converts dimethylallyl diphosphate (DMAPP) and isopentenyl diphosphate (IPP) into colleterpenol as a single product. The C-terminal prenyltransferase (PT) domain of CgCS catalyzes formation of hexaprenyl diphosphate (HexPP), whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of HexPP to colleterpenol.",,,,,,,GO:0016829; GO:0046872; GO:0004659,GO:0016765; GO:0016829,GO:0004659; GO:0010333,GO:0004659,GO:0010333; GO:0016765,GO:0016765; GO:0016829,0.7682,0.6617,0.6279,0.6027,0.7682,5,0.6857,0.2366,no
FANCJ_XENLA,A0A8J1M587,ESM2Text,Eukaryota,1231,"DNA-dependent helicase and 5' to 3' DNA helicase required for the maintenance of chromosomal stability. Involved in the repair of DNA double-strand breaks by homologous recombination. Involved in the repair of abasic sites at replication forks by promoting the degradation of DNA-protein cross-links: acts by catalyzing unfolding of HMCES DNA-protein cross-link via its helicase activity, exposing the underlying DNA and enabling cleavage of the DNA- protein adduct by the SPRTN metalloprotease.",ATP-dependent DNA helicase implicated in DNA repair and the maintenance of genomic stability. Acts as an anti-recombinase to counteract toxic recombination and limit crossover during meiosis. Regulates meiotic recombination by physically dissociating strand invasion events and thereby promotes noncrossover repair by meiotic synthesis dependent strand annealing (SDSA) as well as disassembly of D loop recombination intermediates.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0051539; GO:0043139; GO:0005524; GO:0003677; GO:0016818; GO:0046872,GO:0003678; GO:0005524,GO:0004003; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,0.5871,0.5871,0.5871,0.5871,0.5871,5,0.5871,0.4426,no
FANCJ_XENLA,A0A8J1M587,Prot2Text,Eukaryota,1231,"DNA-dependent helicase and 5' to 3' DNA helicase required for the maintenance of chromosomal stability. Involved in the repair of DNA double-strand breaks by homologous recombination. Involved in the repair of abasic sites at replication forks by promoting the degradation of DNA-protein cross-links: acts by catalyzing unfolding of HMCES DNA-protein cross-link via its helicase activity, exposing the underlying DNA and enabling cleavage of the DNA- protein adduct by the SPRTN metalloprotease.",ATP-dependent DNA helicase implicated in DNA repair and the maintenance of genomic stability. Acts as an anti-recombinase to counteract toxic recombination and limit crossover during meiosis. Regulates meiotic recombination and crossover homeostasis by physically dissociating strand invasion events and thereby promotes noncrossover repair by meiotic synthesis dependent strand annealing (SDSA) as well as disassembly of D loop recombination intermediates.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0051539; GO:0043139; GO:0005524; GO:0003677; GO:0016818; GO:0046872,GO:0003678; GO:0005524,GO:0003678,GO:0004003,GO:0004003,GO:0003678; GO:0005524,0.5871,0.3362,0.3362,0.3362,0.5871,5,0.4366,0.4426,no
FANCJ_XENLA,A0A8J1M587,ProtT3,Eukaryota,1231,"DNA-dependent helicase and 5' to 3' DNA helicase required for the maintenance of chromosomal stability. Involved in the repair of DNA double-strand breaks by homologous recombination. Involved in the repair of abasic sites at replication forks by promoting the degradation of DNA-protein cross-links: acts by catalyzing unfolding of HMCES DNA-protein cross-link via its helicase activity, exposing the underlying DNA and enabling cleavage of the DNA- protein adduct by the SPRTN metalloprotease.","ATP-dependent 3'-5' DNA helicase involved in DNA repair and the maintenance of genomic stability. Acts as an anti-recombinase to counteract toxic recombination and limit crossover during meiosis. Regulates meiotic double-strand break (DSB) formation and repair, meiotic recombination and crossover homeostasis, and crossover interference during meiosis. Regulates meiotic DSB formation and repair, meiotic recombination and crossover homeostasis, and crossover interference during meiosis. Nucleus. Nucleus. Belongs to the helicase family. RAD3/XPD subfamily",Maybe,Yes,Yes,Maybe,Yes,Yes,GO:0051539; GO:0043139; GO:0005524; GO:0003677; GO:0016818; GO:0046872,GO:0003678; GO:0005524,GO:0004386; GO:0005524,GO:0004003; GO:0005524,GO:0003678; GO:0005524,GO:0004386; GO:0005524,0.5871,0.553,0.5871,0.5871,0.553,5,0.5735,0.4426,no
FANCJ_XENLA,A0A8J1M587,ProtTale,Eukaryota,1231,"DNA-dependent helicase and 5' to 3' DNA helicase required for the maintenance of chromosomal stability. Involved in the repair of DNA double-strand breaks by homologous recombination. Involved in the repair of abasic sites at replication forks by promoting the degradation of DNA-protein cross-links: acts by catalyzing unfolding of HMCES DNA-protein cross-link via its helicase activity, exposing the underlying DNA and enabling cleavage of the DNA- protein adduct by the SPRTN metalloprotease.",A probable ATP-dependent DNA helicase implicated in DNA repair and the maintenance of genomic stability. Acts as an anti- recombinase to counteract toxic recombination and limit crossover during meiosis. Regulates meiotic recombination and crossover homeostasis by physically dissociating strand invasion events and thereby promotes noncrossover repair by meiotic synthesis dependent strand annealing (SDSA) as well as disassembly of D loop recombination intermediates.,Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0051539; GO:0043139; GO:0005524; GO:0003677; GO:0016818; GO:0046872,GO:0004386; GO:0005524; GO:0003677,GO:0004386; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,0.7046,0.553,0.5871,0.5871,0.5871,5,0.6038,0.4426,no
FANCJ_XENLA,A0A8J1M587,Protein2Text,Eukaryota,1231,"DNA-dependent helicase and 5' to 3' DNA helicase required for the maintenance of chromosomal stability. Involved in the repair of DNA double-strand breaks by homologous recombination. Involved in the repair of abasic sites at replication forks by promoting the degradation of DNA-protein cross-links: acts by catalyzing unfolding of HMCES DNA-protein cross-link via its helicase activity, exposing the underlying DNA and enabling cleavage of the DNA- protein adduct by the SPRTN metalloprotease.","This protein is involved in DNA repair, specifically in the removal of DNA lesions caused by replication stress. It has helicase activity, which allows it to unwind DNA and access the lesions for repair.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0051539; GO:0043139; GO:0005524; GO:0003677; GO:0016818; GO:0046872,GO:0004386; GO:0005524,GO:0004386,GO:0003678,GO:0003678,GO:0003678,0.553,0.31,0.3362,0.3362,0.3362,5,0.3743,0.4426,no
FANCJ_XENLA,A0A8J1M587,Reference,Eukaryota,1231,"DNA-dependent helicase and 5' to 3' DNA helicase required for the maintenance of chromosomal stability. Involved in the repair of DNA double-strand breaks by homologous recombination. Involved in the repair of abasic sites at replication forks by promoting the degradation of DNA-protein cross-links: acts by catalyzing unfolding of HMCES DNA-protein cross-link via its helicase activity, exposing the underlying DNA and enabling cleavage of the DNA- protein adduct by the SPRTN metalloprotease.","DNA-dependent helicase and 5' to 3' DNA helicase required for the maintenance of chromosomal stability. Involved in the repair of DNA double-strand breaks by homologous recombination. Involved in the repair of abasic sites at replication forks by promoting the degradation of DNA-protein cross-links: acts by catalyzing unfolding of HMCES DNA-protein cross-link via its helicase activity, exposing the underlying DNA and enabling cleavage of the DNA- protein adduct by the SPRTN metalloprotease.",,,,,,,GO:0051539; GO:0043139; GO:0005524; GO:0003677; GO:0016818; GO:0046872,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678,GO:0003678; GO:0005524,GO:0003678; GO:0005524,0.5871,0.5871,0.3362,0.5871,0.5871,5,0.5369,0.4426,no
TMX3A_DANRE,A0A8M1N5Y4,ESM2Text,Eukaryota,437,"Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase. Acts as a regulator of endoplasmic reticulum-mitochondria contact sites via its ability to regulate redox signals.","Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0003756,GO:0003756,GO:0003756,GO:0003756,GO:0003756,GO:0003756,1.0,1.0,1.0,1.0,1.0,5,1.0,0.6833,yes
TMX3A_DANRE,A0A8M1N5Y4,Prot2Text,Eukaryota,437,"Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase. Acts as a regulator of endoplasmic reticulum-mitochondria contact sites via its ability to regulate redox signals.","Acts as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0003756,GO:0003756,GO:0003756,GO:0003756,GO:0003756,GO:0003756,1.0,1.0,1.0,1.0,1.0,5,1.0,0.6833,yes
TMX3A_DANRE,A0A8M1N5Y4,ProtT3,Eukaryota,437,"Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase. Acts as a regulator of endoplasmic reticulum-mitochondria contact sites via its ability to regulate redox signals.",Probable disulfide isomerase. Endoplasmic reticulum membrane; Single-pass membrane protein. Belongs to the protein disulfide isomerase family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003756,GO:0003756,GO:0003756,GO:0003756,GO:0003756,GO:0003756,1.0,1.0,1.0,1.0,1.0,5,1.0,0.6833,yes
TMX3A_DANRE,A0A8M1N5Y4,ProtTale,Eukaryota,437,"Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase. Acts as a regulator of endoplasmic reticulum-mitochondria contact sites via its ability to regulate redox signals.","Acts as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0003756,GO:0003756,GO:0003756,GO:0003756,GO:0003756,GO:0003756,1.0,1.0,1.0,1.0,1.0,5,1.0,0.6833,yes
TMX3A_DANRE,A0A8M1N5Y4,Protein2Text,Eukaryota,437,"Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase. Acts as a regulator of endoplasmic reticulum-mitochondria contact sites via its ability to regulate redox signals.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its classification as a protein involved in a disease, it is likely that it plays a role in molecular processes such as cell signaling, protein-protein interactions, or enzyme activity. Further research would be needed to determine its specific molecular function.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0003756,,,,,,,,,,,0,,0.6833,yes
TMX3A_DANRE,A0A8M1N5Y4,Reference,Eukaryota,437,"Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase. Acts as a regulator of endoplasmic reticulum-mitochondria contact sites via its ability to regulate redox signals.","Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase. Acts as a regulator of endoplasmic reticulum-mitochondria contact sites via its ability to regulate redox signals.",,,,,,,GO:0003756,GO:0003756,GO:0003756,GO:0003756,GO:0003756,GO:0003756,1.0,1.0,1.0,1.0,1.0,5,1.0,0.6833,yes
PNLTA_PENCI,A0A9W9TFE0,ESM2Text,Eukaryota,3920,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of penicilactam A, a fungal alkaloid featuring a rare 5-oxaindolizidine scaffold. This pathway ultilizes the hybrid polyketide synthase-nonribosomal peptide synthetase (PKS-NRPS) pnltA to assemble the prolinol-containing precursor scalusamide A. The polyketide moity is synthesized by the PKS part of pnltA by condensing one acetyl-CoA starter unit and 4 malonyl- CoA elongation units, with one methylation reaction. The D-prolinol moiety in scalusamide A, despite pnltA's lack of epimerization domains, implies selective recruitment of D-proline by the adenylation (A) domain. The pnltA reductase (R) domain mediates reductive release of scalusamide A. PlntA lacks an enyol reductase domain and the trans- enoyl reductase pnltB is essential for the production of scalusamide A by pnltA. The multifunctional cytochrome P450 enzyme pnltC then orchestrates two mechanistically distinct reactions: radical-mediated C-C bond cleavage followed by iminium-driven cyclization to convert scalusamide A into penicilactam A.","Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcs",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0031177,,,,,,,,,,,0,,0.2969,no
PNLTA_PENCI,A0A9W9TFE0,Prot2Text,Eukaryota,3920,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of penicilactam A, a fungal alkaloid featuring a rare 5-oxaindolizidine scaffold. This pathway ultilizes the hybrid polyketide synthase-nonribosomal peptide synthetase (PKS-NRPS) pnltA to assemble the prolinol-containing precursor scalusamide A. The polyketide moity is synthesized by the PKS part of pnltA by condensing one acetyl-CoA starter unit and 4 malonyl- CoA elongation units, with one methylation reaction. The D-prolinol moiety in scalusamide A, despite pnltA's lack of epimerization domains, implies selective recruitment of D-proline by the adenylation (A) domain. The pnltA reductase (R) domain mediates reductive release of scalusamide A. PlntA lacks an enyol reductase domain and the trans- enoyl reductase pnltB is essential for the production of scalusamide A by pnltA. The multifunctional cytochrome P450 enzyme pnltC then orchestrates two mechanistically distinct reactions: radical-mediated C-C bond cleavage followed by iminium-driven cyclization to convert scalusamide A into penicilactam A.","Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcs",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0031177,GO:0016747,,,GO:0016747,GO:0016746,0.5897,,,0.5897,0.5552,3,0.5782,0.2969,no
PNLTA_PENCI,A0A9W9TFE0,ProtT3,Eukaryota,3920,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of penicilactam A, a fungal alkaloid featuring a rare 5-oxaindolizidine scaffold. This pathway ultilizes the hybrid polyketide synthase-nonribosomal peptide synthetase (PKS-NRPS) pnltA to assemble the prolinol-containing precursor scalusamide A. The polyketide moity is synthesized by the PKS part of pnltA by condensing one acetyl-CoA starter unit and 4 malonyl- CoA elongation units, with one methylation reaction. The D-prolinol moiety in scalusamide A, despite pnltA's lack of epimerization domains, implies selective recruitment of D-proline by the adenylation (A) domain. The pnltA reductase (R) domain mediates reductive release of scalusamide A. PlntA lacks an enyol reductase domain and the trans- enoyl reductase pnltB is essential for the production of scalusamide A by pnltA. The multifunctional cytochrome P450 enzyme pnltC then orchestrates two mechanistically distinct reactions: radical-mediated C-C bond cleavage followed by iminium-driven cyclization to convert scalusamide A into penicilactam A.",Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0031177,GO:0016746,GO:0016746,,GO:0016746,GO:0016747,0.5552,0.5552,,0.5552,0.5897,4,0.5638,0.2969,no
PNLTA_PENCI,A0A9W9TFE0,ProtTale,Eukaryota,3920,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of penicilactam A, a fungal alkaloid featuring a rare 5-oxaindolizidine scaffold. This pathway ultilizes the hybrid polyketide synthase-nonribosomal peptide synthetase (PKS-NRPS) pnltA to assemble the prolinol-containing precursor scalusamide A. The polyketide moity is synthesized by the PKS part of pnltA by condensing one acetyl-CoA starter unit and 4 malonyl- CoA elongation units, with one methylation reaction. The D-prolinol moiety in scalusamide A, despite pnltA's lack of epimerization domains, implies selective recruitment of D-proline by the adenylation (A) domain. The pnltA reductase (R) domain mediates reductive release of scalusamide A. PlntA lacks an enyol reductase domain and the trans- enoyl reductase pnltB is essential for the production of scalusamide A by pnltA. The multifunctional cytochrome P450 enzyme pnltC then orchestrates two mechanistically distinct reactions: radical-mediated C-C bond cleavage followed by iminium-driven cyclization to convert scalusamide A into penicilactam A.","Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the",Maybe,Yes,Yes,Yes,Maybe,Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0031177,GO:0016491,GO:0016757,,,GO:0016746; GO:0016874,0.4041,0.4441,,,0.6958,3,0.5147,0.2969,no
PNLTA_PENCI,A0A9W9TFE0,Protein2Text,Eukaryota,3920,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of penicilactam A, a fungal alkaloid featuring a rare 5-oxaindolizidine scaffold. This pathway ultilizes the hybrid polyketide synthase-nonribosomal peptide synthetase (PKS-NRPS) pnltA to assemble the prolinol-containing precursor scalusamide A. The polyketide moity is synthesized by the PKS part of pnltA by condensing one acetyl-CoA starter unit and 4 malonyl- CoA elongation units, with one methylation reaction. The D-prolinol moiety in scalusamide A, despite pnltA's lack of epimerization domains, implies selective recruitment of D-proline by the adenylation (A) domain. The pnltA reductase (R) domain mediates reductive release of scalusamide A. PlntA lacks an enyol reductase domain and the trans- enoyl reductase pnltB is essential for the production of scalusamide A by pnltA. The multifunctional cytochrome P450 enzyme pnltC then orchestrates two mechanistically distinct reactions: radical-mediated C-C bond cleavage followed by iminium-driven cyclization to convert scalusamide A into penicilactam A.",This protein is a component of a type IV secretion system. The type IV secretion system is a complex structure that functions as a molecular injector. It is used by some bacteria to deliver effector proteins into the cytosol of eukaryotic cells. The protein is involved in the translocation of effector proteins.,No,No,No,No,No,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0031177,,,,,,,,,,,0,,0.2969,no
PNLTA_PENCI,A0A9W9TFE0,Reference,Eukaryota,3920,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of penicilactam A, a fungal alkaloid featuring a rare 5-oxaindolizidine scaffold. This pathway ultilizes the hybrid polyketide synthase-nonribosomal peptide synthetase (PKS-NRPS) pnltA to assemble the prolinol-containing precursor scalusamide A. The polyketide moity is synthesized by the PKS part of pnltA by condensing one acetyl-CoA starter unit and 4 malonyl- CoA elongation units, with one methylation reaction. The D-prolinol moiety in scalusamide A, despite pnltA's lack of epimerization domains, implies selective recruitment of D-proline by the adenylation (A) domain. The pnltA reductase (R) domain mediates reductive release of scalusamide A. PlntA lacks an enyol reductase domain and the trans- enoyl reductase pnltB is essential for the production of scalusamide A by pnltA. The multifunctional cytochrome P450 enzyme pnltC then orchestrates two mechanistically distinct reactions: radical-mediated C-C bond cleavage followed by iminium-driven cyclization to convert scalusamide A into penicilactam A.","Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of penicilactam A, a fungal alkaloid featuring a rare 5-oxaindolizidine scaffold. This pathway ultilizes the hybrid polyketide synthase-nonribosomal peptide synthetase (PKS-NRPS) pnltA to assemble the prolinol-containing precursor scalusamide A. The polyketide moity is synthesized by the PKS part of pnltA by condensing one acetyl-CoA starter unit and 4 malonyl- CoA elongation units, with one methylation reaction. The D-prolinol moiety in scalusamide A, despite pnltA's lack of epimerization domains, implies selective recruitment of D-proline by the adenylation (A) domain. The pnltA reductase (R) domain mediates reductive release of scalusamide A. PlntA lacks an enyol reductase domain and the trans- enoyl reductase pnltB is essential for the production of scalusamide A by pnltA. The multifunctional cytochrome P450 enzyme pnltC then orchestrates two mechanistically distinct reactions: radical-mediated C-C bond cleavage followed by iminium-driven cyclization to convert scalusamide A into penicilactam A.",,,,,,,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0031177,GO:0016746; GO:0016874,GO:0016874; GO:0016746,GO:0016746; GO:0016874,GO:0016874,GO:0016874,0.6958,0.6958,0.6958,0.5407,0.5407,5,0.6338,0.2969,no
MURE_DREDA,A0AAD6J5K1,ESM2Text,Eukaryota,522,"Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of cell-wall peptidoglycan. Plays a role in carnivorism. Originally involved in bacterial peptidoglycan biosynthesis, may repurpose GlcNAc metabolism to modify trap-specific cell wall components as the cell wall of the nematode traps appear different from that of the hyphae.",Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0016881; GO:0005524,GO:0008765,GO:0008765,GO:0008764,GO:0008765,GO:0008765,0.5906,0.5906,0.5906,0.5906,0.5906,5,0.5906,0.5644,yes
MURE_DREDA,A0AAD6J5K1,Prot2Text,Eukaryota,522,"Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of cell-wall peptidoglycan. Plays a role in carnivorism. Originally involved in bacterial peptidoglycan biosynthesis, may repurpose GlcNAc metabolism to modify trap-specific cell wall components as the cell wall of the nematode traps appear different from that of the hyphae.",Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0016881; GO:0005524,GO:0008765,GO:0008765,GO:0008765,GO:0008765,GO:0008765,0.5906,0.5906,0.5906,0.5906,0.5906,5,0.5906,0.5644,yes
MURE_DREDA,A0AAD6J5K1,ProtT3,Eukaryota,522,"Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of cell-wall peptidoglycan. Plays a role in carnivorism. Originally involved in bacterial peptidoglycan biosynthesis, may repurpose GlcNAc metabolism to modify trap-specific cell wall components as the cell wall of the nematode traps appear different from that of the hyphae.",Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Cytoplasm. Belongs to the MurCDEF family. MurE subfamily,Yes,Yes,Yes,Yes,Yes,Yes,GO:0016881; GO:0005524,GO:0008764; GO:0005524,GO:0008765,GO:0008765; GO:0005524,GO:0008765; GO:0005524,GO:0008765; GO:0005524,0.9291,0.5906,0.9291,0.9291,0.9291,5,0.8614,0.5644,yes
MURE_DREDA,A0AAD6J5K1,ProtTale,Eukaryota,522,"Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of cell-wall peptidoglycan. Plays a role in carnivorism. Originally involved in bacterial peptidoglycan biosynthesis, may repurpose GlcNAc metabolism to modify trap-specific cell wall components as the cell wall of the nematode traps appear different from that of the hyphae.",Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0016881; GO:0005524,GO:0008765,GO:0008765,GO:0008765; GO:0005524,GO:0008765,GO:0008765; GO:0005524,0.5906,0.5906,0.9291,0.5906,0.9291,5,0.726,0.5644,yes
MURE_DREDA,A0AAD6J5K1,Protein2Text,Eukaryota,522,"Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of cell-wall peptidoglycan. Plays a role in carnivorism. Originally involved in bacterial peptidoglycan biosynthesis, may repurpose GlcNAc metabolism to modify trap-specific cell wall components as the cell wall of the nematode traps appear different from that of the hyphae.","The molecular function of this protein is a GTase (glycosyltransferase) enzyme, specifically a peptide transferase. It is involved in the synthesis of lipid-linked oligosaccharides (LLO) by catalyzing the transfer of a GlcNAc moiety from UDP-GlcNAc to the lipid-linked oligosaccharide precursor.",No,No,No,No,No,not-Yes,GO:0016881; GO:0005524,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.2435,0.2435,0.2435,0.2435,0.2435,5,0.2435,0.5644,yes
MURE_DREDA,A0AAD6J5K1,Reference,Eukaryota,522,"Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of cell-wall peptidoglycan. Plays a role in carnivorism. Originally involved in bacterial peptidoglycan biosynthesis, may repurpose GlcNAc metabolism to modify trap-specific cell wall components as the cell wall of the nematode traps appear different from that of the hyphae.","Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of cell-wall peptidoglycan. Plays a role in carnivorism. Originally involved in bacterial peptidoglycan biosynthesis, may repurpose GlcNAc metabolism to modify trap-specific cell wall components as the cell wall of the nematode traps appear different from that of the hyphae.",,,,,,,GO:0016881; GO:0005524,GO:0008765; GO:0005524,GO:0008764,GO:0008765; GO:0005524,GO:0008765,GO:0008765; GO:0005524,0.9291,0.5906,0.9291,0.5906,0.9291,5,0.7937,0.5644,yes
LENB_ASPLE,A0AAN4PAE6,ESM2Text,Eukaryota,722,"Phenylalanine ammonia-lyase; part of the gene cluster that mediates the biosynthesis of the ergot alkaloids lentopeptins A and B. Within the pathway, lenB provides the cinnamic acid starter unit for the synthesis of the N-acyldiketopiperazine intermediate by the NRPS lenA. Cinnamic acid is condensed with the Ala-Val-Ala peptide chain by lenA which leads to the N-acyldiketopiperazine intermediate which in turn is converted into lentopeptins A and B by the cytochrome P450 monooxygenase lenC.","Amino acid transporter that mediates the uptake of monodehydro-L-tryptophan (DMT) into mitochondria. DMT is an essential neurotransmitter that orchestrates neuronal activity and animal behavior in response to sensory neuron input. Required for maintaining the neuromuscular junction (NMJ) state that is essential for normal synchronous and synchronous locomotion. Also required to maintain a normal synchronous synchrony of locomotor activity in the presence of external light. In darkness, its toxicity is neutralized by the presence of the major fluorescent protein DMT-Amino-gamma (DAMP-Amino-DAMP). Preferentially binds L-tryptophan.",No,No,No,No,Maybe,not-Yes,GO:0045548,,GO:0015171,,GO:0015171,,,0.1264,,0.1264,,2,0.1264,0.488,no
LENB_ASPLE,A0AAN4PAE6,Prot2Text,Eukaryota,722,"Phenylalanine ammonia-lyase; part of the gene cluster that mediates the biosynthesis of the ergot alkaloids lentopeptins A and B. Within the pathway, lenB provides the cinnamic acid starter unit for the synthesis of the N-acyldiketopiperazine intermediate by the NRPS lenA. Cinnamic acid is condensed with the Ala-Val-Ala peptide chain by lenA which leads to the N-acyldiketopiperazine intermediate which in turn is converted into lentopeptins A and B by the cytochrome P450 monooxygenase lenC.","Phenylalanine aminomutase that catalyzes the rearrangement of L-phenylalanine to R-beta-phenylalanine. Catalyzes the first committed step in the biosynthesis of the side chain of the alkaloid taxol (paclitaxel), a widely-used compound with antitumor activity. Also has low phenylalanine ammonia-lyase activity and can catalyze the amination of trans-cinnamate.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0045548,GO:0050031,,GO:0045548,GO:0016866,GO:0016866,0.1998,,1.0,0.2845,0.2845,4,0.4422,0.488,no
LENB_ASPLE,A0AAN4PAE6,ProtT3,Eukaryota,722,"Phenylalanine ammonia-lyase; part of the gene cluster that mediates the biosynthesis of the ergot alkaloids lentopeptins A and B. Within the pathway, lenB provides the cinnamic acid starter unit for the synthesis of the N-acyldiketopiperazine intermediate by the NRPS lenA. Cinnamic acid is condensed with the Ala-Val-Ala peptide chain by lenA which leads to the N-acyldiketopiperazine intermediate which in turn is converted into lentopeptins A and B by the cytochrome P450 monooxygenase lenC.","Catalyzes the non-oxidative deamination of L-phenylalanine to form trans-cinnamic acid and ammonia, and of L-tyrosine to form trans-cinnamic aldehyde and ammonia. Cytoplasm. Belongs to the PAL/histidase family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0045548,GO:0045548,GO:0045548,GO:0045548,GO:0045548,GO:0045548,1.0,1.0,1.0,1.0,1.0,5,1.0,0.488,no
LENB_ASPLE,A0AAN4PAE6,ProtTale,Eukaryota,722,"Phenylalanine ammonia-lyase; part of the gene cluster that mediates the biosynthesis of the ergot alkaloids lentopeptins A and B. Within the pathway, lenB provides the cinnamic acid starter unit for the synthesis of the N-acyldiketopiperazine intermediate by the NRPS lenA. Cinnamic acid is condensed with the Ala-Val-Ala peptide chain by lenA which leads to the N-acyldiketopiperazine intermediate which in turn is converted into lentopeptins A and B by the cytochrome P450 monooxygenase lenC.","Phenylalanine ammonia-lyase; part of the gene cluster that mediates the biosynthesis of sordarin and hypoxysordarin, glycoside antibiotics with a unique tetracyclic diterpene aglycone structure. First, the geranylgeranyl diphosphate synthase sdnC constructs GGDP from farnesyl diphosphate and isopentenyl diphosphate. The diterpene cyclase sdnA then catalyzes the cyclization of GGDP to afford cycloaraneosene. Cycloaraneosene is then hydroxylated four times by the putative cytochrome P450 monooxygenases sdnB, sdnE, sdnF and s",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0045548,GO:0045548,GO:0045548,GO:0045548,GO:0045548,GO:0045548,1.0,1.0,1.0,1.0,1.0,5,1.0,0.488,no
LENB_ASPLE,A0AAN4PAE6,Protein2Text,Eukaryota,722,"Phenylalanine ammonia-lyase; part of the gene cluster that mediates the biosynthesis of the ergot alkaloids lentopeptins A and B. Within the pathway, lenB provides the cinnamic acid starter unit for the synthesis of the N-acyldiketopiperazine intermediate by the NRPS lenA. Cinnamic acid is condensed with the Ala-Val-Ala peptide chain by lenA which leads to the N-acyldiketopiperazine intermediate which in turn is converted into lentopeptins A and B by the cytochrome P450 monooxygenase lenC.","The molecular function of this protein is likely to be involved in the biosynthesis of plant growth regulators, such as phenylpropanoids and alkaloids, which are important for plant defense and development. This protein is a type of aminotransferase, which catalyzes the transfer of an amino group from an amino acid to a keto acid, playing a crucial role in the biosynthesis of these important compounds.",Vague,Vague,No,Vague,No,not-Yes,GO:0045548,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.2353,0.2353,0.2353,0.2353,0.2353,5,0.2353,0.488,no
LENB_ASPLE,A0AAN4PAE6,Reference,Eukaryota,722,"Phenylalanine ammonia-lyase; part of the gene cluster that mediates the biosynthesis of the ergot alkaloids lentopeptins A and B. Within the pathway, lenB provides the cinnamic acid starter unit for the synthesis of the N-acyldiketopiperazine intermediate by the NRPS lenA. Cinnamic acid is condensed with the Ala-Val-Ala peptide chain by lenA which leads to the N-acyldiketopiperazine intermediate which in turn is converted into lentopeptins A and B by the cytochrome P450 monooxygenase lenC.","Phenylalanine ammonia-lyase; part of the gene cluster that mediates the biosynthesis of the ergot alkaloids lentopeptins A and B. Within the pathway, lenB provides the cinnamic acid starter unit for the synthesis of the N-acyldiketopiperazine intermediate by the NRPS lenA. Cinnamic acid is condensed with the Ala-Val-Ala peptide chain by lenA which leads to the N-acyldiketopiperazine intermediate which in turn is converted into lentopeptins A and B by the cytochrome P450 monooxygenase lenC.",,,,,,,GO:0045548,GO:0045548,GO:0045548,GO:0045548,GO:0045548,GO:0045548,1.0,1.0,1.0,1.0,1.0,5,1.0,0.488,no
LENA_ASPLE,A0AAN4PB13,ESM2Text,Eukaryota,4650,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the ergot alkaloids lentopeptins A and B. Within the pathway, lenA catalyzes the biosynthesis of the Ala-Val-Ala peptide chain, including a cinnamic acid moiety as the starting unit. The release of the peptide from the enzyme is accomplished via a cyclization reaction catalyzed by the terminal condensation-like (Ct) domain of lenA to form the N- acyldiketopiperazine intermediate. The reaction appears to proceed through a nucleophilic attack on the carbonyl carbon by a lone electron pair of the valine amide nitrogen. The phenylalanine ammonia-lyase lenB provides the starter unit for the synthesis of the N-acyldiketopiperazine intermediate by the NRPS lenA, while the cytochrome P450 monooxygenase lenC is involved in the post-NRPS oxidative modification steps to form lentopeptins A and B.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the benzazepine alkaloid nanangelenin A which contains an unprecedented 3,4-dihydro-1-benzazepine-2,5-dione-N-prenyl-N-acetoxy-anthranilamide scaffold. The first step of nanangelenin biosynthesis is catalyzed by the indoleamine 2,3-dioxygenase nanC which produces N-formyl-kynurenine through the catabolism of tryptophan. The two-module NRPS nanA then utilizes anthranilate (Ant) and L-kynurenine (L-Kyn) to assemble the dipeptide product nanangelenin B. The first adenylation domain of nanA (A1) loads anthranilate onto the T1 domain, while A2 loads kynurenine, generated through spontaneous nonenzymatic deformylation of the nanC-supplied N-formyl-kynurenine. The peptide bond formation between the tethered amino acids is catalyzed by the first condensation",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,,,,,,,,,,,0,,0.372,no
LENA_ASPLE,A0AAN4PB13,Prot2Text,Eukaryota,4650,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the ergot alkaloids lentopeptins A and B. Within the pathway, lenA catalyzes the biosynthesis of the Ala-Val-Ala peptide chain, including a cinnamic acid moiety as the starting unit. The release of the peptide from the enzyme is accomplished via a cyclization reaction catalyzed by the terminal condensation-like (Ct) domain of lenA to form the N- acyldiketopiperazine intermediate. The reaction appears to proceed through a nucleophilic attack on the carbonyl carbon by a lone electron pair of the valine amide nitrogen. The phenylalanine ammonia-lyase lenB provides the starter unit for the synthesis of the N-acyldiketopiperazine intermediate by the NRPS lenA, while the cytochrome P450 monooxygenase lenC is involved in the post-NRPS oxidative modification steps to form lentopeptins A and B.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the benzazepine alkaloid nanangelenin A which contains an unprecedented 3,4-dihydro-1-benzazepine-2,5-dione-N-prenyl-N-acetoxy-anthranilamide scaffold. The first step of nanangelenin biosynthesis is catalyzed by the indoleamine 2,3-dioxygenase nanC which produces N-formyl-kynurenine through the catabolism of tryptophan. The two-module NRPS nanA then utilizes anthranilate (Ant) and L-kynurenine (L-Kyn) to assemble the dipeptide product nanangelenin B. The first adenylation domain of nanA (A1) loads anthranilate onto the T1 domain, while A2 loads kynurenine, generated through spontaneous nonenzymatic deformylation of the nanC-supplied N-formyl-kynurenine. The peptide bond formation between the tethered amino acids is catalyzed by the first condensation",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,GO:0016874,,,GO:0016874,GO:0016874; GO:0005524,0.709,,,0.709,0.6793,3,0.6991,0.372,no
LENA_ASPLE,A0AAN4PB13,ProtT3,Eukaryota,4650,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the ergot alkaloids lentopeptins A and B. Within the pathway, lenA catalyzes the biosynthesis of the Ala-Val-Ala peptide chain, including a cinnamic acid moiety as the starting unit. The release of the peptide from the enzyme is accomplished via a cyclization reaction catalyzed by the terminal condensation-like (Ct) domain of lenA to form the N- acyldiketopiperazine intermediate. The reaction appears to proceed through a nucleophilic attack on the carbonyl carbon by a lone electron pair of the valine amide nitrogen. The phenylalanine ammonia-lyase lenB provides the starter unit for the synthesis of the N-acyldiketopiperazine intermediate by the NRPS lenA, while the cytochrome P450 monooxygenase lenC is involved in the post-NRPS oxidative modification steps to form lentopeptins A and B.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties . L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L- homoserine by cluster enzymes aspartate kinase FUB5 and homoserine O-acetyltransferase FUB6, as well as enzymes of the primary metabolism",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,GO:0016874; GO:0005524,GO:0016874,,GO:0016874; GO:0031177,GO:0016874; GO:0005524,0.6793,0.709,,1.0,0.6793,4,0.7669,0.372,no
LENA_ASPLE,A0AAN4PB13,ProtTale,Eukaryota,4650,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the ergot alkaloids lentopeptins A and B. Within the pathway, lenA catalyzes the biosynthesis of the Ala-Val-Ala peptide chain, including a cinnamic acid moiety as the starting unit. The release of the peptide from the enzyme is accomplished via a cyclization reaction catalyzed by the terminal condensation-like (Ct) domain of lenA to form the N- acyldiketopiperazine intermediate. The reaction appears to proceed through a nucleophilic attack on the carbonyl carbon by a lone electron pair of the valine amide nitrogen. The phenylalanine ammonia-lyase lenB provides the starter unit for the synthesis of the N-acyldiketopiperazine intermediate by the NRPS lenA, while the cytochrome P450 monooxygenase lenC is involved in the post-NRPS oxidative modification steps to form lentopeptins A and B.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,GO:0016491,GO:0016874,,,GO:0016874,0.4358,0.709,,,0.709,3,0.6179,0.372,no
LENA_ASPLE,A0AAN4PB13,Protein2Text,Eukaryota,4650,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the ergot alkaloids lentopeptins A and B. Within the pathway, lenA catalyzes the biosynthesis of the Ala-Val-Ala peptide chain, including a cinnamic acid moiety as the starting unit. The release of the peptide from the enzyme is accomplished via a cyclization reaction catalyzed by the terminal condensation-like (Ct) domain of lenA to form the N- acyldiketopiperazine intermediate. The reaction appears to proceed through a nucleophilic attack on the carbonyl carbon by a lone electron pair of the valine amide nitrogen. The phenylalanine ammonia-lyase lenB provides the starter unit for the synthesis of the N-acyldiketopiperazine intermediate by the NRPS lenA, while the cytochrome P450 monooxygenase lenC is involved in the post-NRPS oxidative modification steps to form lentopeptins A and B.","This protein is a component of the 3'-5' exonuclease complex which is required for normal mitochondrial DNA (mtDNA) replication and degradation. It may be involved in the regulation of mtDNA replication, or may play a role in the maintenance of mtDNA stability. May have a role in the regulation of mtDNA replication, or in the maintenance of mtDNA stability. May play a role in the regulation of mtDNA replication, or in the maintenance of mtDNA stability. May play a role in the regulation of mtDNA replication, or in the maintenance of mtDNA stability. May play a role in the regulation of mtDNA replication, or in the maintenance of mtDNA stability. May play a role in the regulation of mtDNA replication, or in the maintenance of mtDNA stability. May play a role in the regulation of mtDNA replication, or in the maintenance of mtDNA stability. May play a role in the regulation of mtDNA replication, or in the maintenance of mtDNA stability. May play a role in the regulation of mtDNA replication, or in the maintenance of mtDNA stability. May play a role in the regulation of mtDNA replication, or in the maintenance of mtDNA stability. May play a role in the regulation of mtDNA replication, or in the maintenance of mtDNA stability. May play a role in the regulation of mtDNA replication, or in the maintenance of mtDNA stability. May play a role in the regulation of mtDNA replication, or in the maintenance of mtDNA stability. May play a role in the regulation of mtDNA replication, or in the maintenance of mtDNA stability. May play a role in the regulation of mtDNA replication, or in the maintenance of mtDNA stability. May play a role in the regulation of mtDNA replication, or in the maintenance of mtDNA stability. May play a role in the regulation of mtDNA replication, or in the maintenance of mtDNA stability. May play a role in the regulation of mtDNA replication, or in the maintenance of mtDNA stability. May play a role in the regulation of mtDNA replication, or in the maintenance of mtDNA stability. May play a role in the regulation of mtDNA replication, or in the maintenance of mtDNA stability. May play a role in the regulation of mtDNA replication, or in the maintenance of mtDNA stability. May play a role in the regulation of mtDNA replication, or in the maintenance of mtDNA stability. May play a role in the regulation of mtDNA replication, or in the",No,No,No,No,No,not-Yes,GO:0016874; GO:0031177,GO:0004532,GO:0008408,GO:0008408,GO:0008408,GO:0008408,0.1881,0.2237,0.2237,0.2237,0.2237,5,0.2166,0.372,no
LENA_ASPLE,A0AAN4PB13,Reference,Eukaryota,4650,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the ergot alkaloids lentopeptins A and B. Within the pathway, lenA catalyzes the biosynthesis of the Ala-Val-Ala peptide chain, including a cinnamic acid moiety as the starting unit. The release of the peptide from the enzyme is accomplished via a cyclization reaction catalyzed by the terminal condensation-like (Ct) domain of lenA to form the N- acyldiketopiperazine intermediate. The reaction appears to proceed through a nucleophilic attack on the carbonyl carbon by a lone electron pair of the valine amide nitrogen. The phenylalanine ammonia-lyase lenB provides the starter unit for the synthesis of the N-acyldiketopiperazine intermediate by the NRPS lenA, while the cytochrome P450 monooxygenase lenC is involved in the post-NRPS oxidative modification steps to form lentopeptins A and B.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the ergot alkaloids lentopeptins A and B. Within the pathway, lenA catalyzes the biosynthesis of the Ala-Val-Ala peptide chain, including a cinnamic acid moiety as the starting unit. The release of the peptide from the enzyme is accomplished via a cyclization reaction catalyzed by the terminal condensation-like (Ct) domain of lenA to form the N- acyldiketopiperazine intermediate. The reaction appears to proceed through a nucleophilic attack on the carbonyl carbon by a lone electron pair of the valine amide nitrogen. The phenylalanine ammonia-lyase lenB provides the starter unit for the synthesis of the N-acyldiketopiperazine intermediate by the NRPS lenA, while the cytochrome P450 monooxygenase lenC is involved in the post-NRPS oxidative modification steps to form lentopeptins A and B.",,,,,,,GO:0016874; GO:0031177,GO:0016874,GO:0016874,GO:0016874,GO:0016874,GO:0016874,0.709,0.709,0.709,0.709,0.709,5,0.709,0.372,no
CSL1_SAPOF,A0AAW1HA02,ESM2Text,Eukaryota,698,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. Glycosyltransferase that mediates the conversion of quillaic acid (QA) to QA-mono via the initiation of the C-3 sugar chain.",Thought to be a Golgi-localized beta-glycan synthase that polymerize the backbones of noncellulosic polysaccharides (hemicelluloses) of plant cell wall.,No,No,No,Maybe,No,not-Yes,GO:0016760; GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.8347,0.8347,0.8347,0.8347,0.8347,5,0.8347,0.3726,no
CSL1_SAPOF,A0AAW1HA02,Prot2Text,Eukaryota,698,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. Glycosyltransferase that mediates the conversion of quillaic acid (QA) to QA-mono via the initiation of the C-3 sugar chain.",Thought to be a Golgi-localized beta-glycan synthase that polymerize the backbones of noncellulosic polysaccharides (hemicelluloses) of plant cell wall.,No,No,No,Maybe,No,not-Yes,GO:0016760; GO:0016757,GO:0016757,,GO:0016757,GO:0016757,GO:0016757,0.8347,,0.8347,0.8347,0.8347,4,0.8347,0.3726,no
CSL1_SAPOF,A0AAW1HA02,ProtT3,Eukaryota,698,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. Glycosyltransferase that mediates the conversion of quillaic acid (QA) to QA-mono via the initiation of the C-3 sugar chain.",Thought to be a Golgi-localized beta-glycan synthase that polymerize the backbones of noncellulosic polysaccharides (hemicelluloses) of plant cell wall. Golgi apparatus membrane; Multi- pass membrane protein. Belongs to the glycosyltransferase 2 family. Plant cellulose synthase-like B subfamily,No,No,Maybe,Maybe,Maybe,not-Yes,GO:0016760; GO:0016757,GO:0016757,GO:0016757,GO:0016759,GO:0016757,GO:0016757,0.8347,0.8347,0.7171,0.8347,0.8347,5,0.8112,0.3726,no
CSL1_SAPOF,A0AAW1HA02,ProtTale,Eukaryota,698,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. Glycosyltransferase that mediates the conversion of quillaic acid (QA) to QA-mono via the initiation of the C-3 sugar chain.",Thought to be a Golgi-localized beta-glycan synthase that polymerize the backbones of noncellulosic polysaccharides (hemicelluloses) of plant cell wall.,No,No,No,Maybe,Maybe,not-Yes,GO:0016760; GO:0016757,GO:0016757,GO:0016757,,,,0.8347,0.8347,,,,2,0.8347,0.3726,no
CSL1_SAPOF,A0AAW1HA02,Protein2Text,Eukaryota,698,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. Glycosyltransferase that mediates the conversion of quillaic acid (QA) to QA-mono via the initiation of the C-3 sugar chain.","The molecular function of this protein is to catalyze the synthesis of cellulose, a type of complex carbohydrate.",No,No,No,Maybe,No,not-Yes,GO:0016760; GO:0016757,GO:0016760,GO:0016760,GO:0016760,GO:0016760,GO:0016760,0.8347,0.8347,0.8347,0.8347,0.8347,5,0.8347,0.3726,no
CSL1_SAPOF,A0AAW1HA02,Reference,Eukaryota,698,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. Glycosyltransferase that mediates the conversion of quillaic acid (QA) to QA-mono via the initiation of the C-3 sugar chain.","Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. Glycosyltransferase that mediates the conversion of quillaic acid (QA) to QA-mono via the initiation of the C-3 sugar chain.",,,,,,,GO:0016760; GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.8347,0.8347,0.8347,0.8347,0.8347,5,0.8347,0.3726,no
GH1_SAPOF,A0AAW1I778,ESM2Text,Eukaryota,449,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. Beta-glycosidase that catalyzes the transfer of a modified glucose moiety to QA-triFRXX to produce QA-triF(Q)RXX via the elongation of the C-28 sugar chain with a D-quinovose.","Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl beta-D-mannoside, p-nitrophenyl beta-D-galactoside, p-nitrophenyl beta-D-xyloside, p-nitrophenyl beta-D-fucoside, p-nitrophenyl beta-L-arabinoside, p-nitrophenyl beta-D-xyloside, p-nitrophenyl beta-L-arabino-lactoside, p-nitrophenyl beta-D-glucoside, p-nitrophenyl beta-D-mannobiose, cellobiose, syringin, scopoletin and furan-A.",Maybe,Maybe,No,Maybe,No,not-Yes,GO:0008422; GO:0016757; GO:0016798,GO:0004553,GO:0008422,GO:0008422,GO:0008422,GO:0008422,0.6914,0.7247,0.7247,0.7247,0.7247,5,0.718,0.2078,no
GH1_SAPOF,A0AAW1I778,Prot2Text,Eukaryota,449,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. Beta-glycosidase that catalyzes the transfer of a modified glucose moiety to QA-triFRXX to produce QA-triF(Q)RXX via the elongation of the C-28 sugar chain with a D-quinovose.","Glucosidase specifically involved in alkaloid biosynthesis leading to the accumulation of several alkaloids, including ajmaline, an important plant-derived pharmaceutical used in the therapy of heart disorders.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008422; GO:0016757; GO:0016798,GO:0004553,GO:0008422,GO:0004553,GO:0004553,GO:0015926,0.6914,0.7247,0.6914,0.6914,0.6879,5,0.6974,0.2078,no
GH1_SAPOF,A0AAW1I778,ProtT3,Eukaryota,449,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. Beta-glycosidase that catalyzes the transfer of a modified glucose moiety to QA-triFRXX to produce QA-triF(Q)RXX via the elongation of the C-28 sugar chain with a D-quinovose.",Belongs to the glycosyl hydrolase 1 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008422; GO:0016757; GO:0016798,GO:0008422,GO:0008422,GO:0008422,GO:0008422,GO:0008422,0.7247,0.7247,0.7247,0.7247,0.7247,5,0.7247,0.2078,no
GH1_SAPOF,A0AAW1I778,ProtTale,Eukaryota,449,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. Beta-glycosidase that catalyzes the transfer of a modified glucose moiety to QA-triFRXX to produce QA-triF(Q)RXX via the elongation of the C-28 sugar chain with a D-quinovose.","Hydrolyzes p-nitrophenyl-beta-D-glucoside, p-nitrophenyl-beta-D-galactoside, p-nitrophenyl-beta-D-xyloside and p-nitrophenyl-beta-D-mannoside. Does not hydrolyze p-nitrophenyl-beta-D-fucoside, p-nitrophenyl-beta-D-glucopyranoside, p-nitrophenyl-beta-D-glucuronide, p-nitrophenyl-beta-D-xyloside, p-nitrophenyl-beta-D-galactoside, p-nitrophenyl-beta-D-arabinoside, p-nitrophenyl-beta-D-xyl",Maybe,Maybe,No,Maybe,No,not-Yes,GO:0008422; GO:0016757; GO:0016798,GO:0016798,GO:0004553,GO:0008422,GO:0008422,GO:0008422,0.7592,0.6914,0.7247,0.7247,0.7247,5,0.7249,0.2078,no
GH1_SAPOF,A0AAW1I778,Protein2Text,Eukaryota,449,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. Beta-glycosidase that catalyzes the transfer of a modified glucose moiety to QA-triFRXX to produce QA-triF(Q)RXX via the elongation of the C-28 sugar chain with a D-quinovose.","The molecular function of this protein is to catalyze the hydrolysis of the glycosidic bond in various substrates, such as flavonoids and other polyphenolic compounds. It has been shown to have activity against a range of substrates, including flavonols, flavanols, and anthocyanidins. This protein is likely involved in the breakdown and degradation of these compounds in the plant, and may also play a role in the regulation of their levels in the plant.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008422; GO:0016757; GO:0016798,GO:0004553,GO:0016798,GO:0016798,GO:0016798,GO:0004553,0.6914,0.7592,0.7592,0.7592,0.6914,5,0.7321,0.2078,no
GH1_SAPOF,A0AAW1I778,Reference,Eukaryota,449,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. Beta-glycosidase that catalyzes the transfer of a modified glucose moiety to QA-triFRXX to produce QA-triF(Q)RXX via the elongation of the C-28 sugar chain with a D-quinovose.","Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. Beta-glycosidase that catalyzes the transfer of a modified glucose moiety to QA-triFRXX to produce QA-triF(Q)RXX via the elongation of the C-28 sugar chain with a D-quinovose.",,,,,,,GO:0008422; GO:0016757; GO:0016798,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.6606,0.6606,0.6606,0.6606,0.6606,5,0.6606,0.2078,no
GT732_SAPOF,A0AAW1J1B8,ESM2Text,Eukaryota,490,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A glycosyltransferase that mediates the conversion of QA-triFRX to QA-triFRXX via the elongation of the C-28 sugar chain with a D-xylose.",Glucosyltransferase that glucosylates the cell wall inhibitor hypostatin but not the cell wall inhibitor bacillibactin. Also acts on the non-reducing end of the glucosylated substrates.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0035251; GO:0008194,GO:0046527,GO:0016757,GO:0046527,GO:0016757,GO:0046527,0.7316,0.7608,0.7316,0.7608,0.7316,5,0.7433,0.2892,no
GT732_SAPOF,A0AAW1J1B8,Prot2Text,Eukaryota,490,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A glycosyltransferase that mediates the conversion of QA-triFRX to QA-triFRXX via the elongation of the C-28 sugar chain with a D-xylose.","Glucosyltransferase involved in the last step of benzoxazinoid glucoside biosynthesis. Catalyzes the glucosylation of hydroxamic acids utilizing UDP-glucose as glucose doner, reducing the toxicity of these natural insecticides.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0035251; GO:0008194,GO:0046527,GO:0035251,GO:0035251,GO:0035251,GO:0035251,0.7316,0.9042,0.9042,0.9042,0.9042,5,0.8697,0.2892,no
GT732_SAPOF,A0AAW1J1B8,ProtT3,Eukaryota,490,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A glycosyltransferase that mediates the conversion of QA-triFRX to QA-triFRXX via the elongation of the C-28 sugar chain with a D-xylose.",Belongs to the UDP-glycosyltransferase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0035251; GO:0008194,GO:0035251,GO:0035251,GO:0008194,GO:0016757,GO:0035251,0.9042,0.9042,0.9042,0.7608,0.9042,5,0.8755,0.2892,no
GT732_SAPOF,A0AAW1J1B8,ProtTale,Eukaryota,490,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A glycosyltransferase that mediates the conversion of QA-triFRX to QA-triFRXX via the elongation of the C-28 sugar chain with a D-xylose.",UDP-glycosyltransferase involved in the biosynthesis of cucurbitacin. Catalyzes the transfer of the 4-O-glucosyl moiety from UDP-glucose to the C-3 hydroxyl group of naringenin chalcone to yield naringenin 4-O- beta-D- glucoside.,Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0035251; GO:0008194,GO:0016757,GO:0016757,GO:0035251,GO:0016757,GO:0016757,0.7608,0.7608,0.9042,0.7608,0.7608,5,0.7895,0.2892,no
GT732_SAPOF,A0AAW1J1B8,Protein2Text,Eukaryota,490,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A glycosyltransferase that mediates the conversion of QA-triFRX to QA-triFRXX via the elongation of the C-28 sugar chain with a D-xylose.","This protein is involved in the molecular function of glucosyltransferase activity. It is a type of enzyme that catalyzes the transfer of a glucosyl group from UDP-glucose to a substrate, typically a steroid or flavonoid compound. This protein is specifically involved in the glucosylation of a particular substrate, which is not specified in the given text. However, it is likely involved in the biosynthesis of a glucosylated compound, such as a glycoside or a glucosylated flavonoid. 

In more detail, the molecular function of this protein can be broken down into the following steps:

1. Binding of UDP-glucose: The protein binds to UDP-glucose, a sugar nucleotide that serves as the glucosyl donor.
2. Binding of substrate: The protein binds to a specific substrate, such as a steroid or flavonoid compound.
3. Glucosyltransferase activity: The protein catalyzes the transfer of the glucosyl group from UDP-glucose to the substrate, resulting in the formation of a glucosylated compound.
4. Release of UDP: The protein releases UDP, a byproduct of the glucosyltransferase reaction.

Overall, the molecular function of this protein is to catalyze the glucosylation of a specific substrate, which is likely involved in the biosynthesis of a glucosylated compound.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0035251; GO:0008194,GO:0035251,GO:0035251,GO:0016757,GO:0035251,GO:0035251,0.9042,0.9042,0.7608,0.9042,0.9042,5,0.8755,0.2892,no
GT732_SAPOF,A0AAW1J1B8,Reference,Eukaryota,490,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A glycosyltransferase that mediates the conversion of QA-triFRX to QA-triFRXX via the elongation of the C-28 sugar chain with a D-xylose.","Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A glycosyltransferase that mediates the conversion of QA-triFRX to QA-triFRXX via the elongation of the C-28 sugar chain with a D-xylose.",,,,,,,GO:0035251; GO:0008194,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.7608,0.7608,0.7608,0.7608,0.7608,5,0.7608,0.2892,no
GT731_SAPOF,A0AAW1K8I9,ESM2Text,Eukaryota,492,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A glycosyltransferase that mediates the conversion of QA-mono to QA-di via the elongation of the C-3 sugar chain with a D-galactose.","Glucosyltransferase involved in montbretin A (MbA) biosynthesis. Catalyzes the 3-O-glucosylation of myricetin 3-O-glucoside to produce myricetin 3-O-sophoroside. In vitro, is able to glucosylate myricetin 3-O-(6-O-malonylglucoside) and myricetin 3-O-(6-O-glucosylation). In vitro, is able to glucosylate myricetin 3-O-(6-O-glucosylation) and myricetin 3-O-(3-O-glucosylation).",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0035251; GO:0008194,GO:0046527,GO:0016757,GO:0046527,GO:0016757,GO:0046527,0.7316,0.7608,0.7316,0.7608,0.7316,5,0.7433,0.3341,no
GT731_SAPOF,A0AAW1K8I9,Prot2Text,Eukaryota,492,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A glycosyltransferase that mediates the conversion of QA-mono to QA-di via the elongation of the C-3 sugar chain with a D-galactose.","UDP-glucose-dependent glucosyltransferase catalyzing the c-glucosylation of 2-hydroxyflavanones (2-hydroxynaringenin and 2-hydroxypinocembrin) and phloretin. No activity with flavanones, flavones or flavonols. Triggers the accumulation of 2-hydroxyflavanones in leaves.",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0035251; GO:0008194,GO:0046527,GO:0035251,GO:0035251,GO:0035251,GO:0035251,0.7316,0.9042,0.9042,0.9042,0.9042,5,0.8697,0.3341,no
GT731_SAPOF,A0AAW1K8I9,ProtT3,Eukaryota,492,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A glycosyltransferase that mediates the conversion of QA-mono to QA-di via the elongation of the C-3 sugar chain with a D-galactose.",Belongs to the UDP-glycosyltransferase family,Vague,Vague,Vague,Vague,No,not-Yes,GO:0035251; GO:0008194,GO:0035251,GO:0035251,GO:0008194,GO:0016757,GO:0035251,0.9042,0.9042,0.9042,0.7608,0.9042,5,0.8755,0.3341,no
GT731_SAPOF,A0AAW1K8I9,ProtTale,Eukaryota,492,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A glycosyltransferase that mediates the conversion of QA-mono to QA-di via the elongation of the C-3 sugar chain with a D-galactose.",Involved in the biosynthesis of rutin (quercetin-3-O-D-glucoside).,No,No,Vague,Vague,No,not-Yes,GO:0035251; GO:0008194,,,,,,,,,,,0,,0.3341,no
GT731_SAPOF,A0AAW1K8I9,Protein2Text,Eukaryota,492,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A glycosyltransferase that mediates the conversion of QA-mono to QA-di via the elongation of the C-3 sugar chain with a D-galactose.","The molecular function of this protein is not specified in the provided text. However, based on its classification as a cytochrome P450, it is likely that it is involved in a metabolic reaction, such as the hydroxylation or epoxidation of a substrate.",No,No,No,No,No,not-Yes,GO:0035251; GO:0008194,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.2969,0.2969,0.2969,0.2969,0.2969,5,0.2969,0.3341,no
GT731_SAPOF,A0AAW1K8I9,Reference,Eukaryota,492,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A glycosyltransferase that mediates the conversion of QA-mono to QA-di via the elongation of the C-3 sugar chain with a D-galactose.","Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A glycosyltransferase that mediates the conversion of QA-mono to QA-di via the elongation of the C-3 sugar chain with a D-galactose.",,,,,,,GO:0035251; GO:0008194,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.7608,0.7608,0.7608,0.7608,0.7608,5,0.7608,0.3341,no
BAHD1_SAPOF,A0AAW1LG41,ESM2Text,Eukaryota,459,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. An acyltransferase that catalyzes the transfer of an acyl moiety to QA-triF(Q)RXX to produce saponarioside B.","Involved in the biosynthesis of vindoline, a precursor of vinblastine and vincristine.",No,No,Vague,No,Maybe,not-Yes,GO:0016746,,,,,,,,,,,0,,0.2336,no
BAHD1_SAPOF,A0AAW1LG41,Prot2Text,Eukaryota,459,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. An acyltransferase that catalyzes the transfer of an acyl moiety to QA-triF(Q)RXX to produce saponarioside B.","Carboxyltransferase involved in the biosynthesis of the benzylisoquinoline alkaloid noscapine. Converts (13S,14R)-1,13-dihydroxy-N-methylcanadine to (13S,14R)-13-O-acetyl-1-hydroxy-N-methylcanadine.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016746,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016746,0.729,0.729,0.729,0.729,1.0,5,0.7832,0.2336,no
BAHD1_SAPOF,A0AAW1LG41,ProtT3,Eukaryota,459,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. An acyltransferase that catalyzes the transfer of an acyl moiety to QA-triF(Q)RXX to produce saponarioside B.",Acyltransferase involved in the biosynthesis of benzylisoquinoline alkaloids. Catalyzes the conversion of (S)-reticuline to (S)-scoulerine and (S)-scoulerine to (S)-scoulerine 6-O-glucoside. Can also use (S)-reticuline 6-O-glucoside and (S)-scoulerine 6-O-glucoside as substrates. Belongs to the plant acyltransferase family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016747,1.0,1.0,1.0,1.0,0.8416,5,0.9683,0.2336,no
BAHD1_SAPOF,A0AAW1LG41,ProtTale,Eukaryota,459,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. An acyltransferase that catalyzes the transfer of an acyl moiety to QA-triF(Q)RXX to produce saponarioside B.","Hydroxycinnamoyl transferase that catalyzes the transfer of an acyl from p-coumaryol-CoA to feruloyl-CoA, caffeoyl-CoA, and sinapoyl-CoA. Can use only p-coumaryol-CoA as acyl acceptor.",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016746,GO:0016746,1.0,1.0,0.8416,1.0,1.0,5,0.9683,0.2336,no
BAHD1_SAPOF,A0AAW1LG41,Protein2Text,Eukaryota,459,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. An acyltransferase that catalyzes the transfer of an acyl moiety to QA-triF(Q)RXX to produce saponarioside B.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its name and the fact that it is involved in the biosynthesis of a molecule, it can be inferred that it is likely involved in a metabolic process, possibly related to the synthesis of a specific compound.

However, based on the name of the protein, it can be inferred that it is involved in the biosynthesis of a molecule, possibly related to the synthesis of a specific compound.

A more detailed search of the protein database reveals that this protein is likely involved in the biosynthesis of a molecule, possibly related to the synthesis of a specific compound.

The specific molecular function of this protein is not explicitly stated in the provided text, but it can be inferred that it is likely involved in a metabolic process, possibly related to the synthesis of a specific compound.

Based on the name of the protein, it can be inferred that it is likely involved in the biosynthesis of a molecule, possibly related to the synthesis of a specific compound.

A more detailed search of the protein database reveals that this protein is likely involved in the biosynthesis of a molecule, possibly related to the synthesis of a specific compound.

The protein is likely involved in a metabolic process, possibly related to the synthesis of a specific compound.

The specific molecular function of this protein is not explicitly stated in the provided text, but it can be inferred that it is likely involved in a metabolic process, possibly related to the synthesis of a specific compound.

The protein is likely involved in the biosynthesis of a molecule, possibly related to the synthesis of a specific compound.

The specific molecular function of this protein is not explicitly stated in the provided text, but it can be inferred that it is likely involved in a metabolic process, possibly related to the synthesis of a specific compound.

The protein is likely involved in the biosynthesis of a molecule, possibly related to the synthesis of a specific compound.

The specific molecular function of this protein is not explicitly stated in the provided text, but it can be inferred that it is likely involved in a metabolic process, possibly related to the synthesis of a specific compound.

The protein is likely involved in the biosynthesis of a molecule, possibly related to the synthesis of a specific compound.

The specific molecular function of this protein is not explicitly stated in the provided text, but it can be inferred that it is likely involved in a metabolic process, possibly related to the synthesis of a specific compound.

The protein is likely involved in the biosynthesis of a molecule, possibly related to the synthesis of a specific",Vague,Vague,Vague,Vague,No,not-Yes,GO:0016746,,,,,,,,,,,0,,0.2336,no
BAHD1_SAPOF,A0AAW1LG41,Reference,Eukaryota,459,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. An acyltransferase that catalyzes the transfer of an acyl moiety to QA-triF(Q)RXX to produce saponarioside B.","Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. An acyltransferase that catalyzes the transfer of an acyl moiety to QA-triF(Q)RXX to produce saponarioside B.",,,,,,,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016746,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2336,no
GT741_SAPOF,A0AAW1M2U7,ESM2Text,Eukaryota,468,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A glycosyltransferase that, together with SDR1, mediates the conversion of QA-tri to QA-triF; UGT74CD1 may transfer 4-keto-6-deoxy-glucose to QA-tri, which is in turn reduced to D-fucose by SDR1, thus leading to QA-triF formation via the initiation of the C-28 sugar chain.",Possesses quercetin 3-O-glucosyltransferase and 4'-O-glucosyltransferase activities in vitro. Also active in vitro on benzoates and benzoate derivatives.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0080043; GO:0080044; GO:0008194,GO:0046527,GO:0016757,GO:0046527; GO:0080043,GO:0080043; GO:0016757,GO:0046527,0.6926,0.6979,0.8356,0.8975,0.6926,5,0.7632,0.2501,no
GT741_SAPOF,A0AAW1M2U7,Prot2Text,Eukaryota,468,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A glycosyltransferase that, together with SDR1, mediates the conversion of QA-tri to QA-triF; UGT74CD1 may transfer 4-keto-6-deoxy-glucose to QA-tri, which is in turn reduced to D-fucose by SDR1, thus leading to QA-triF formation via the initiation of the C-28 sugar chain.","UDP-glucosyltransferase that glucosylates the (+) enantiomer of abscisic acid ((+)-ABA). Can use DIMBOA and DIBOA as substrates, but not DIBOA.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0080043; GO:0080044; GO:0008194,GO:0046527,GO:0035251,GO:0035251,GO:0035251,GO:0035251,0.6926,0.8549,0.8549,0.8549,0.8549,5,0.8224,0.2501,no
GT741_SAPOF,A0AAW1M2U7,ProtT3,Eukaryota,468,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A glycosyltransferase that, together with SDR1, mediates the conversion of QA-tri to QA-triF; UGT74CD1 may transfer 4-keto-6-deoxy-glucose to QA-tri, which is in turn reduced to D-fucose by SDR1, thus leading to QA-triF formation via the initiation of the C-28 sugar chain.",Belongs to the UDP-glycosyltransferase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0080043; GO:0080044; GO:0008194,GO:0035251,GO:0035251,GO:0008194,GO:0016757,GO:0035251,0.8549,0.8549,0.8256,0.6979,0.8549,5,0.8176,0.2501,no
GT741_SAPOF,A0AAW1M2U7,ProtTale,Eukaryota,468,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A glycosyltransferase that, together with SDR1, mediates the conversion of QA-tri to QA-triF; UGT74CD1 may transfer 4-keto-6-deoxy-glucose to QA-tri, which is in turn reduced to D-fucose by SDR1, thus leading to QA-triF formation via the initiation of the C-28 sugar chain.","Involved in the biosynthesis of anthocyanins, the red pigments of plants.",No,No,Vague,Vague,No,not-Yes,GO:0080043; GO:0080044; GO:0008194,,,,,,,,,,,0,,0.2501,no
GT741_SAPOF,A0AAW1M2U7,Protein2Text,Eukaryota,468,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A glycosyltransferase that, together with SDR1, mediates the conversion of QA-tri to QA-triF; UGT74CD1 may transfer 4-keto-6-deoxy-glucose to QA-tri, which is in turn reduced to D-fucose by SDR1, thus leading to QA-triF formation via the initiation of the C-28 sugar chain.","This protein is a part of the UDP-glucosyltransferase family, which is involved in the transfer of a glucosyl group from UDP-glucose to a variety of acceptor molecules, including flavonoids, phenylpropanoids, and terpenoids. This protein specifically catalyzes the glucosylation of 2',4',4-trihydroxychalcone, a precursor of flavonoid glycosides, which are important plant metabolites.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0080043; GO:0080044; GO:0008194,GO:0035251,GO:0035251,GO:0016757,GO:0035251,GO:0035251,0.8549,0.8549,0.6979,0.8549,0.8549,5,0.8235,0.2501,no
GT741_SAPOF,A0AAW1M2U7,Reference,Eukaryota,468,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A glycosyltransferase that, together with SDR1, mediates the conversion of QA-tri to QA-triF; UGT74CD1 may transfer 4-keto-6-deoxy-glucose to QA-tri, which is in turn reduced to D-fucose by SDR1, thus leading to QA-triF formation via the initiation of the C-28 sugar chain.","Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A glycosyltransferase that, together with SDR1, mediates the conversion of QA-tri to QA-triF; UGT74CD1 may transfer 4-keto-6-deoxy-glucose to QA-tri, which is in turn reduced to D-fucose by SDR1, thus leading to QA-triF formation via the initiation of the C-28 sugar chain.",,,,,,,GO:0080043; GO:0080044; GO:0008194,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.6979,0.6979,0.6979,0.6979,0.6979,5,0.6979,0.2501,no
SDR1_SAPOF,A0AAW1NHX6,ESM2Text,Eukaryota,302,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A dehydrogenase/reductase that, together with UGT74CD1, mediates the conversion of QA-tri to QA-triF; UGT74CD1 may transfer 4-keto-6-deoxy- glucose to QA-tri, which is in turn reduced to D-fucose by SDR1, thus leading to QA-triF formation via the initiation of the C-28 sugar chain.","Involved in biosynthesis of cutin monomers. Cutin monomers are structural components of various cellular and developmental metabolites and are used to communicate developmental cues, provide metabolic information and are used to generate a supply of specific energy for cell action. Can use both NADH and NADPH as substrates, with a marked preference for NADPH.",No,No,No,No,No,not-Yes,GO:0016491; GO:0016616,GO:0016491,GO:0016491,,GO:0016491,,0.8966,0.8966,,0.8966,,3,0.8966,0.1578,no
SDR1_SAPOF,A0AAW1NHX6,Prot2Text,Eukaryota,302,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A dehydrogenase/reductase that, together with UGT74CD1, mediates the conversion of QA-tri to QA-triF; UGT74CD1 may transfer 4-keto-6-deoxy- glucose to QA-tri, which is in turn reduced to D-fucose by SDR1, thus leading to QA-triF formation via the initiation of the C-28 sugar chain.",Involved in biosynthesis of fatty acids in mitochondria.,No,No,No,No,No,not-Yes,GO:0016491; GO:0016616,,,,,,,,,,,0,,0.1578,no
SDR1_SAPOF,A0AAW1NHX6,ProtT3,Eukaryota,302,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A dehydrogenase/reductase that, together with UGT74CD1, mediates the conversion of QA-tri to QA-triF; UGT74CD1 may transfer 4-keto-6-deoxy- glucose to QA-tri, which is in turn reduced to D-fucose by SDR1, thus leading to QA-triF formation via the initiation of the C-28 sugar chain.",Putative short-chain dehydrogenase/reductase. Belongs to the short-chain dehydrogenases/reductases (SDR) family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016491; GO:0016616,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.8966,0.8966,0.8966,0.8966,0.8966,5,0.8966,0.1578,no
SDR1_SAPOF,A0AAW1NHX6,ProtTale,Eukaryota,302,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A dehydrogenase/reductase that, together with UGT74CD1, mediates the conversion of QA-tri to QA-triF; UGT74CD1 may transfer 4-keto-6-deoxy- glucose to QA-tri, which is in turn reduced to D-fucose by SDR1, thus leading to QA-triF formation via the initiation of the C-28 sugar chain.","Short-chain dehydrogenase/reductase involved in lipid metabolism. Catalyzes the reduction of a range of saturated and monounsaturated aldehydes and ketones. Catalyzes the reduction of 4-hydroxynonenal (4-HNE) into 4-hydroxyhexenal. In vitro, catalyzes the reduction of 2,4-dinitrophenylhydrazine (DNPH) to 2,4-dinitrophenylamine (DNP).",Maybe,Maybe,No,Maybe,No,not-Yes,GO:0016491; GO:0016616,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.8966,0.8966,0.8966,0.8966,0.8966,5,0.8966,0.1578,no
SDR1_SAPOF,A0AAW1NHX6,Protein2Text,Eukaryota,302,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A dehydrogenase/reductase that, together with UGT74CD1, mediates the conversion of QA-tri to QA-triF; UGT74CD1 may transfer 4-keto-6-deoxy- glucose to QA-tri, which is in turn reduced to D-fucose by SDR1, thus leading to QA-triF formation via the initiation of the C-28 sugar chain.","The molecular function of this protein is an oxidoreductase activity, specifically a NADP-dependent oxidoreductase activity.",Maybe,Maybe,Vague,Maybe,Maybe,not-Yes,GO:0016491; GO:0016616,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.8966,0.8966,0.8966,0.8966,0.8966,5,0.8966,0.1578,no
SDR1_SAPOF,A0AAW1NHX6,Reference,Eukaryota,302,"Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A dehydrogenase/reductase that, together with UGT74CD1, mediates the conversion of QA-tri to QA-triF; UGT74CD1 may transfer 4-keto-6-deoxy- glucose to QA-tri, which is in turn reduced to D-fucose by SDR1, thus leading to QA-triF formation via the initiation of the C-28 sugar chain.","Component of the oleanane-type triterpene saponins (e.g. saponarioside A and saponarioside B) biosynthetic pathway, leading to the production of natural products with detergent properties used as traditional sources of soap. A dehydrogenase/reductase that, together with UGT74CD1, mediates the conversion of QA-tri to QA-triF; UGT74CD1 may transfer 4-keto-6-deoxy- glucose to QA-tri, which is in turn reduced to D-fucose by SDR1, thus leading to QA-triF formation via the initiation of the C-28 sugar chain.",,,,,,,GO:0016491; GO:0016616,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.8966,0.8966,0.8966,0.8966,0.8966,5,0.8966,0.1578,no
PP2B_CANAR,A0AB36VXQ9,ESM2Text,Eukaryota,561,"Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals. Plays different roles in regulating extreme thermotolerance, cell wall and membrane integrity, antifungal drug resistance, and virulence. Required for virulence in both a Drosophila systemic infection model and a murine skin infection model. However, in a systemic murine infection model, appears to be dispensable for virulence. Also, the calcineurin pathway is dispensable for morphogenesis, biofilm formation, secreted aspartyl protease activity, and ploidy switching in Candida auris.","Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005516; GO:0046872; GO:0004722,GO:0004722,GO:0004722,GO:0004722; GO:0005509,GO:0004723,GO:0004723,0.5487,0.5487,0.7981,0.4963,0.4963,5,0.5776,0.4203,no
PP2B_CANAR,A0AB36VXQ9,Prot2Text,Eukaryota,561,"Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals. Plays different roles in regulating extreme thermotolerance, cell wall and membrane integrity, antifungal drug resistance, and virulence. Required for virulence in both a Drosophila systemic infection model and a murine skin infection model. However, in a systemic murine infection model, appears to be dispensable for virulence. Also, the calcineurin pathway is dispensable for morphogenesis, biofilm formation, secreted aspartyl protease activity, and ploidy switching in Candida auris.","Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005516; GO:0046872; GO:0004722,GO:0004722,GO:0004722,GO:0004723,GO:0004722,GO:0004723,0.5487,0.5487,0.4963,0.5487,0.4963,5,0.5277,0.4203,no
PP2B_CANAR,A0AB36VXQ9,ProtT3,Eukaryota,561,"Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals. Plays different roles in regulating extreme thermotolerance, cell wall and membrane integrity, antifungal drug resistance, and virulence. Required for virulence in both a Drosophila systemic infection model and a murine skin infection model. However, in a systemic murine infection model, appears to be dispensable for virulence. Also, the calcineurin pathway is dispensable for morphogenesis, biofilm formation, secreted aspartyl protease activity, and ploidy switching in Candida auris.","Calcium-dependent, calmodulin-stimulated protein phosphatase. Belongs to the PPP phosphatase family. PP-2B subfamily",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005516; GO:0046872; GO:0004722,GO:0004722; GO:0005509,GO:0004722; GO:0005509,GO:0004722; GO:0005516; GO:0005509,GO:0004722; GO:0005509,GO:0004722,0.7981,0.7981,0.9564,0.7981,0.5487,5,0.7799,0.4203,no
PP2B_CANAR,A0AB36VXQ9,ProtTale,Eukaryota,561,"Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals. Plays different roles in regulating extreme thermotolerance, cell wall and membrane integrity, antifungal drug resistance, and virulence. Required for virulence in both a Drosophila systemic infection model and a murine skin infection model. However, in a systemic murine infection model, appears to be dispensable for virulence. Also, the calcineurin pathway is dispensable for morphogenesis, biofilm formation, secreted aspartyl protease activity, and ploidy switching in Candida auris.",Calcium- and calmodulin-dependent protein phosphatase. May dephosphorylate or regulate components of the calcium release channel/ryanodine receptor (Ca(2+) release channel/RYR).,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005516; GO:0046872; GO:0004722,GO:0004722; GO:0005516,GO:0004722; GO:0005509,GO:0004722,GO:0004722; GO:0005509; GO:0005516,GO:0004722; GO:0005509,0.8569,0.7981,0.5487,0.9564,0.7981,5,0.7916,0.4203,no
PP2B_CANAR,A0AB36VXQ9,Protein2Text,Eukaryota,561,"Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals. Plays different roles in regulating extreme thermotolerance, cell wall and membrane integrity, antifungal drug resistance, and virulence. Required for virulence in both a Drosophila systemic infection model and a murine skin infection model. However, in a systemic murine infection model, appears to be dispensable for virulence. Also, the calcineurin pathway is dispensable for morphogenesis, biofilm formation, secreted aspartyl protease activity, and ploidy switching in Candida auris.","This protein is a type of phosphatase, which is an enzyme that removes phosphate groups from molecules. More specifically, it is a calcineurin-like phosphatase, which is a type of serine/threonine phosphatase.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005516; GO:0046872; GO:0004722,GO:0004722,GO:0004722,GO:0004722,GO:0004722,GO:0004722,0.5487,0.5487,0.5487,0.5487,0.5487,5,0.5487,0.4203,no
PP2B_CANAR,A0AB36VXQ9,Reference,Eukaryota,561,"Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals. Plays different roles in regulating extreme thermotolerance, cell wall and membrane integrity, antifungal drug resistance, and virulence. Required for virulence in both a Drosophila systemic infection model and a murine skin infection model. However, in a systemic murine infection model, appears to be dispensable for virulence. Also, the calcineurin pathway is dispensable for morphogenesis, biofilm formation, secreted aspartyl protease activity, and ploidy switching in Candida auris.","Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals. Plays different roles in regulating extreme thermotolerance, cell wall and membrane integrity, antifungal drug resistance, and virulence. Required for virulence in both a Drosophila systemic infection model and a murine skin infection model. However, in a systemic murine infection model, appears to be dispensable for virulence. Also, the calcineurin pathway is dispensable for morphogenesis, biofilm formation, secreted aspartyl protease activity, and ploidy switching in Candida auris.",,,,,,,GO:0005516; GO:0046872; GO:0004722,GO:0004722; GO:0005509; GO:0005516,GO:0004722; GO:0005509; GO:0005516,GO:0004722; GO:0005509; GO:0005516,GO:0004722; GO:0005509; GO:0005516,GO:0004722; GO:0005509; GO:0005516,0.9564,0.9564,0.9564,0.9564,0.9564,5,0.9564,0.4203,no
Y5008_MYCS2,A0R271,ESM2Text,Bacteria,578,"ABC transporter that contributes to drug efflux. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). Is able to transport isoniazid, but not ethambutol.","Mediates resistance to the antifungal drugs miconin, acriflavin and tetraphenylphosphate.",Maybe,Maybe,Vague,Maybe,Maybe,not-Yes,GO:0015421; GO:0005524; GO:0016887,,,,,,,,,,,0,,0.3684,no
Y5008_MYCS2,A0R271,Prot2Text,Bacteria,578,"ABC transporter that contributes to drug efflux. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). Is able to transport isoniazid, but not ethambutol.","Involved in the transport of four structurally unrelated drugs, including doxorubicin and mitoxantrone. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0015421; GO:0005524; GO:0016887,GO:0042626,GO:0016887,GO:0042626,GO:0042626,GO:0016887; GO:0005524,0.4645,0.5596,0.4645,0.4645,0.8355,5,0.5577,0.3684,no
Y5008_MYCS2,A0R271,ProtT3,Bacteria,578,"ABC transporter that contributes to drug efflux. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). Is able to transport isoniazid, but not ethambutol.",Cell membrane; Multi-pass membrane protein. Belongs to the ABC transporter superfamily,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0015421; GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0005524; GO:0016887,GO:0042626; GO:0005524,GO:0005524; GO:0016887,GO:0016887; GO:0005524,0.8355,0.8355,0.757,0.8355,0.8355,5,0.8198,0.3684,no
Y5008_MYCS2,A0R271,ProtTale,Bacteria,578,"ABC transporter that contributes to drug efflux. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). Is able to transport isoniazid, but not ethambutol.",Probably part of an ABC transporter complex involved in antibiotic efflux (Probable). Probably involved in multidrug resistance (Probable).,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0015421; GO:0005524; GO:0016887,,GO:0005524; GO:0016887,,,,,0.8355,,,,1,0.8355,0.3684,no
Y5008_MYCS2,A0R271,Protein2Text,Bacteria,578,"ABC transporter that contributes to drug efflux. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). Is able to transport isoniazid, but not ethambutol.","The molecular function of this protein is a transporter. More specifically, it is an ABC transporter, which is a type of transport protein that uses the energy of ATP hydrolysis to move molecules across cell membranes.",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0015421; GO:0005524; GO:0016887,GO:0042626,GO:0042626,GO:0022857,GO:0022857,GO:0005215,0.4645,0.4645,0.2899,0.2899,0.2427,5,0.3503,0.3684,no
Y5008_MYCS2,A0R271,Reference,Bacteria,578,"ABC transporter that contributes to drug efflux. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). Is able to transport isoniazid, but not ethambutol.","ABC transporter that contributes to drug efflux. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). Is able to transport isoniazid, but not ethambutol.",,,,,,,GO:0015421; GO:0005524; GO:0016887,GO:0016887; GO:0005524; GO:0042626,GO:0042626,GO:0016887; GO:0005524; GO:0042626,GO:0005524; GO:0016887,GO:0016887; GO:0005524; GO:0042626,0.9215,0.4645,0.9215,0.8355,0.9215,5,0.8129,0.3684,no
Y5009_MYCS2,A0R272,ESM2Text,Bacteria,630,"ABC transporter that contributes to drug efflux. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). Is able to transport isoniazid, but not ethambutol.","Mediates resistance to the antifungal drugs miconazole, tioconazole and ketoconazole.",Maybe,Maybe,Vague,Maybe,Maybe,not-Yes,GO:0140359; GO:0005524; GO:0016887,,,,,,,,,,,0,,0.4618,no
Y5009_MYCS2,A0R272,Prot2Text,Bacteria,630,"ABC transporter that contributes to drug efflux. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). Is able to transport isoniazid, but not ethambutol.",Mediates ATP-dependent translocation of the aminoglycoside antibiotic A-aminoacyl-homoserine lactone (AHL) to the cell membrane. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation.,Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0140359; GO:0005524; GO:0016887,GO:0042626,GO:0016887,GO:0042626,GO:0042626,GO:0016887; GO:0005524,0.5305,0.5717,0.5305,0.5305,0.8452,5,0.6017,0.4618,no
Y5009_MYCS2,A0R272,ProtT3,Bacteria,630,"ABC transporter that contributes to drug efflux. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). Is able to transport isoniazid, but not ethambutol.",Cell membrane; Multi-pass membrane protein. Belongs to the ABC transporter superfamily,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0140359; GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0005524; GO:0016887,GO:0042626; GO:0005524,GO:0005524; GO:0016887,GO:0016887; GO:0005524,0.8452,0.8452,0.8098,0.8452,0.8452,5,0.8381,0.4618,no
Y5009_MYCS2,A0R272,ProtTale,Bacteria,630,"ABC transporter that contributes to drug efflux. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). Is able to transport isoniazid, but not ethambutol.","Part of the ABC transporter complex CcmAB involved in the biogenesis of c-type cytochromes; once thought to export heme, this does not seem to be the case, but its exact role is uncertain. Responsible for energy coupling to the transport system.",Maybe,Maybe,No,No,Maybe,not-Yes,GO:0140359; GO:0005524; GO:0016887,GO:0005524,GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.5312,0.8452,0.8452,0.8452,0.8452,5,0.7824,0.4618,no
Y5009_MYCS2,A0R272,Protein2Text,Bacteria,630,"ABC transporter that contributes to drug efflux. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). Is able to transport isoniazid, but not ethambutol.","This protein is a part of the ABC transporter, which is involved in the transport of molecules across cell membranes. Specifically, it is responsible for the transport of molecules into the cell. The molecular function of this protein is to act as a permease, which is a component of an ABC transporter complex that facilitates the transport of molecules across cell membranes.",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0140359; GO:0005524; GO:0016887,GO:0042626,GO:0042626,GO:0022857,GO:0022857,GO:0005215,0.5305,0.5305,0.3126,0.3126,0.2721,5,0.3917,0.4618,no
Y5009_MYCS2,A0R272,Reference,Bacteria,630,"ABC transporter that contributes to drug efflux. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). Is able to transport isoniazid, but not ethambutol.","ABC transporter that contributes to drug efflux. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). Is able to transport isoniazid, but not ethambutol.",,,,,,,GO:0140359; GO:0005524; GO:0016887,GO:0016887; GO:0005524; GO:0042626,GO:0042626,GO:0016887; GO:0005524; GO:0042626,GO:0005524; GO:0016887,GO:0016887; GO:0005524; GO:0042626,0.9654,0.5305,0.9654,0.8452,0.9654,5,0.8544,0.4618,no
CAAA_ASPNC,A2QQV0,ESM2Text,Eukaryota,3605,"Hybrid PKS-NRPS synthetase; part of the gene cluster that produces the acyltetronic acid derivatives carlosic acid, agglomerin F and carlosic acid methyl ether. The PKS domains of caaA condenses two malonyl-CoAs into an acetyl starter unit, and form 1,3-diketohexanyl-ACP with the help of the trans-enoyl reductase caaB. Next, the C domain of caaA forms the ester bond between the acyl chain and L-malic acid (derived from the TCA cycle) and accepted by the A domain instead of an amino acid. Finally, the terminal reductase/Dieckmann cyclization (R/DKC) domain cyclizes the intermediate and releases the product as carlosic acid. Decarboxylation of carlosic acid followed by formation of the exocyclic double bond is likely to be catalyzed by the cytochrome P450 monooxygenase caaC. Thus, decarboxylation and oxidation would be coupled (performed by one enzyme) through concomitant abstraction of the hydrogen at C-4. Finally, sequential oxidations of the terminal C-10 methyl group to form carboxylic acid would be catalyzed by the 2-oxoglutarate-dependent dioxygenase caaD, which is required for the biosynthesis of agglomerin F.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the benzazepine alkaloid nanangelenin A which contains an unprecedented 3,4-dihydro-1-benzazepine-2,5-dione-N-prenyl-N-acetoxy-anthranilamide scaffold. The first step of nanangelenin biosynthesis is catalyzed by the indoleamine 2,3-dioxygenase nanC which produces N-formyl-kynurenine through the catabolism of tryptophan. The two-module NRPS nanA then utilizes anthranilate (Ant) and L-kynurenine (L-Kyn) to assemble the dipeptide product nanangelenin B. The first adenylation domain of nanA (A1) loads anthranilate onto the T1 domain, while A2 loads kynurenine, generated through spontaneous nonenzymatic deformylation of the nanC-supplied N-formyl-kynurenine. The peptide bond formation between the tethered amino acids is catalyzed by the first condensation domain",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0031177,,,,,,,,,,,0,,0.2857,no
CAAA_ASPNC,A2QQV0,Prot2Text,Eukaryota,3605,"Hybrid PKS-NRPS synthetase; part of the gene cluster that produces the acyltetronic acid derivatives carlosic acid, agglomerin F and carlosic acid methyl ether. The PKS domains of caaA condenses two malonyl-CoAs into an acetyl starter unit, and form 1,3-diketohexanyl-ACP with the help of the trans-enoyl reductase caaB. Next, the C domain of caaA forms the ester bond between the acyl chain and L-malic acid (derived from the TCA cycle) and accepted by the A domain instead of an amino acid. Finally, the terminal reductase/Dieckmann cyclization (R/DKC) domain cyclizes the intermediate and releases the product as carlosic acid. Decarboxylation of carlosic acid followed by formation of the exocyclic double bond is likely to be catalyzed by the cytochrome P450 monooxygenase caaC. Thus, decarboxylation and oxidation would be coupled (performed by one enzyme) through concomitant abstraction of the hydrogen at C-4. Finally, sequential oxidations of the terminal C-10 methyl group to form carboxylic acid would be catalyzed by the 2-oxoglutarate-dependent dioxygenase caaD, which is required for the biosynthesis of agglomerin F.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the benzazepine alkaloid nanangelenin A which contains an unprecedented 3,4-dihydro-1-benzazepine-2,5-dione-N-prenyl-N-acetoxy-anthranilamide scaffold. The first step of nanangelenin biosynthesis is catalyzed by the indoleamine 2,3-dioxygenase nanC which produces N-formyl-kynurenine through the catabolism of tryptophan. The two-module NRPS nanA then utilizes anthranilate (Ant) and L-kynurenine (L-Kyn) to assemble the dipeptide product nanangelenin B. The first adenylation domain of nanA (A1) loads anthranilate onto the T1 domain, while A2 loads kynurenine, generated through spontaneous nonenzymatic deformylation of the nanC-supplied N-formyl-kynurenine. The peptide bond formation between the tethered amino acids is catalyzed by the first condensation domain",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0031177,GO:0016747,,,GO:0016747,GO:0016746,0.5897,,,0.5897,0.5552,3,0.5782,0.2857,no
CAAA_ASPNC,A2QQV0,ProtT3,Eukaryota,3605,"Hybrid PKS-NRPS synthetase; part of the gene cluster that produces the acyltetronic acid derivatives carlosic acid, agglomerin F and carlosic acid methyl ether. The PKS domains of caaA condenses two malonyl-CoAs into an acetyl starter unit, and form 1,3-diketohexanyl-ACP with the help of the trans-enoyl reductase caaB. Next, the C domain of caaA forms the ester bond between the acyl chain and L-malic acid (derived from the TCA cycle) and accepted by the A domain instead of an amino acid. Finally, the terminal reductase/Dieckmann cyclization (R/DKC) domain cyclizes the intermediate and releases the product as carlosic acid. Decarboxylation of carlosic acid followed by formation of the exocyclic double bond is likely to be catalyzed by the cytochrome P450 monooxygenase caaC. Thus, decarboxylation and oxidation would be coupled (performed by one enzyme) through concomitant abstraction of the hydrogen at C-4. Finally, sequential oxidations of the terminal C-10 methyl group to form carboxylic acid would be catalyzed by the 2-oxoglutarate-dependent dioxygenase caaD, which is required for the biosynthesis of agglomerin F.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0031177,GO:0016746,GO:0016746,,GO:0016746,GO:0016747,0.5552,0.5552,,0.5552,0.5897,4,0.5638,0.2857,no
CAAA_ASPNC,A2QQV0,ProtTale,Eukaryota,3605,"Hybrid PKS-NRPS synthetase; part of the gene cluster that produces the acyltetronic acid derivatives carlosic acid, agglomerin F and carlosic acid methyl ether. The PKS domains of caaA condenses two malonyl-CoAs into an acetyl starter unit, and form 1,3-diketohexanyl-ACP with the help of the trans-enoyl reductase caaB. Next, the C domain of caaA forms the ester bond between the acyl chain and L-malic acid (derived from the TCA cycle) and accepted by the A domain instead of an amino acid. Finally, the terminal reductase/Dieckmann cyclization (R/DKC) domain cyclizes the intermediate and releases the product as carlosic acid. Decarboxylation of carlosic acid followed by formation of the exocyclic double bond is likely to be catalyzed by the cytochrome P450 monooxygenase caaC. Thus, decarboxylation and oxidation would be coupled (performed by one enzyme) through concomitant abstraction of the hydrogen at C-4. Finally, sequential oxidations of the terminal C-10 methyl group to form carboxylic acid would be catalyzed by the 2-oxoglutarate-dependent dioxygenase caaD, which is required for the biosynthesis of agglomerin F.","Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the",Maybe,Yes,Yes,Yes,Maybe,Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0031177,GO:0016491,GO:0016757,,,GO:0016746; GO:0016874,0.4041,0.4441,,,0.6958,3,0.5147,0.2857,no
CAAA_ASPNC,A2QQV0,Protein2Text,Eukaryota,3605,"Hybrid PKS-NRPS synthetase; part of the gene cluster that produces the acyltetronic acid derivatives carlosic acid, agglomerin F and carlosic acid methyl ether. The PKS domains of caaA condenses two malonyl-CoAs into an acetyl starter unit, and form 1,3-diketohexanyl-ACP with the help of the trans-enoyl reductase caaB. Next, the C domain of caaA forms the ester bond between the acyl chain and L-malic acid (derived from the TCA cycle) and accepted by the A domain instead of an amino acid. Finally, the terminal reductase/Dieckmann cyclization (R/DKC) domain cyclizes the intermediate and releases the product as carlosic acid. Decarboxylation of carlosic acid followed by formation of the exocyclic double bond is likely to be catalyzed by the cytochrome P450 monooxygenase caaC. Thus, decarboxylation and oxidation would be coupled (performed by one enzyme) through concomitant abstraction of the hydrogen at C-4. Finally, sequential oxidations of the terminal C-10 methyl group to form carboxylic acid would be catalyzed by the 2-oxoglutarate-dependent dioxygenase caaD, which is required for the biosynthesis of agglomerin F.","This protein is involved in the biosynthesis of the polyketide chain of surfactin, a cyclic lipopeptide antibiotic that is a potent antifungal agent and is widely used as a biosurfactant. This protein is a nonribosomal peptide synthetase that is involved in the biosynthesis of surfactin. The molecular function of this protein is to catalyze the polyketide chain extension of surfactin. It is responsible for the addition of the polyketide chain to the nonribosomal peptide synthetase (NRPS) domain of the surfactin synthetase. The polyketide chain is formed by the sequential addition of acetate units from malonyl-CoA to the chain, which is then extended by the NRPS domain. The resulting polyketide chain is then coupled to the cyclic peptide core of surfactin, resulting in the final product, surfactin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0031177,,,,,,,,,,,0,,0.2857,no
CAAA_ASPNC,A2QQV0,Reference,Eukaryota,3605,"Hybrid PKS-NRPS synthetase; part of the gene cluster that produces the acyltetronic acid derivatives carlosic acid, agglomerin F and carlosic acid methyl ether. The PKS domains of caaA condenses two malonyl-CoAs into an acetyl starter unit, and form 1,3-diketohexanyl-ACP with the help of the trans-enoyl reductase caaB. Next, the C domain of caaA forms the ester bond between the acyl chain and L-malic acid (derived from the TCA cycle) and accepted by the A domain instead of an amino acid. Finally, the terminal reductase/Dieckmann cyclization (R/DKC) domain cyclizes the intermediate and releases the product as carlosic acid. Decarboxylation of carlosic acid followed by formation of the exocyclic double bond is likely to be catalyzed by the cytochrome P450 monooxygenase caaC. Thus, decarboxylation and oxidation would be coupled (performed by one enzyme) through concomitant abstraction of the hydrogen at C-4. Finally, sequential oxidations of the terminal C-10 methyl group to form carboxylic acid would be catalyzed by the 2-oxoglutarate-dependent dioxygenase caaD, which is required for the biosynthesis of agglomerin F.","Hybrid PKS-NRPS synthetase; part of the gene cluster that produces the acyltetronic acid derivatives carlosic acid, agglomerin F and carlosic acid methyl ether. The PKS domains of caaA condenses two malonyl-CoAs into an acetyl starter unit, and form 1,3-diketohexanyl-ACP with the help of the trans-enoyl reductase caaB. Next, the C domain of caaA forms the ester bond between the acyl chain and L-malic acid (derived from the TCA cycle) and accepted by the A domain instead of an amino acid. Finally, the terminal reductase/Dieckmann cyclization (R/DKC) domain cyclizes the intermediate and releases the product as carlosic acid. Decarboxylation of carlosic acid followed by formation of the exocyclic double bond is likely to be catalyzed by the cytochrome P450 monooxygenase caaC. Thus, decarboxylation and oxidation would be coupled (performed by one enzyme) through concomitant abstraction of the hydrogen at C-4. Finally, sequential oxidations of the terminal C-10 methyl group to form carboxylic acid would be catalyzed by the 2-oxoglutarate-dependent dioxygenase caaD, which is required for the biosynthesis of agglomerin F.",,,,,,,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0031177,GO:0016746; GO:0016874,GO:0016874; GO:0016746,GO:0016746; GO:0016874,GO:0016874,GO:0016874,0.6958,0.6958,0.6958,0.5407,0.5407,5,0.6338,0.2857,no
BDGF_ASPNC,A2QVZ0,ESM2Text,Eukaryota,340,"Glycoside hydrolase family 43 beta-D-galactofuranosidase involved in the degradation of beta-galactofuranoside (Galf)-containing glycans such as galactomannan or O-glycans. Is not active on beta-1,5- or beta-1,6-linked beta-D-galactofuranose (Galf) residues.","Alpha-L-arabinofuranosidase involved in the degradation of arabinan, a structural polymer of the hemicellulose polymer of the secondary cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues of linear 1,5-alpha-L-arabinan and of oligo-oligosaccharides like L-arabinobiose (L-ABA), L-arabinan (L-ABA), L-arabinobiose (L-ABA) and L-arabinoxylan (L-AOX) to release L-arabinofuranose and L-ABA. It prefers L-ABA over L-ABA or L-ABA and is specific for L-ABA, the other major products in the medium are L-A products and L-A-binding.",No,No,No,No,No,not-Yes,GO:0004553,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.289,no
BDGF_ASPNC,A2QVZ0,Prot2Text,Eukaryota,340,"Glycoside hydrolase family 43 beta-D-galactofuranosidase involved in the degradation of beta-galactofuranoside (Galf)-containing glycans such as galactomannan or O-glycans. Is not active on beta-1,5- or beta-1,6-linked beta-D-galactofuranose (Galf) residues.",Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes only the cleavage of terminal alpha-(1->5)-L-arabinofuranosyl residues of the linear polysaccharides (from L-arabinofuranosyl (Araf) and L-arabinan to yield the arabinan backbone and L-arabinose as side products.,No,No,No,No,No,not-Yes,GO:0004553,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.289,no
BDGF_ASPNC,A2QVZ0,ProtT3,Eukaryota,340,"Glycoside hydrolase family 43 beta-D-galactofuranosidase involved in the degradation of beta-galactofuranoside (Galf)-containing glycans such as galactomannan or O-glycans. Is not active on beta-1,5- or beta-1,6-linked beta-D-galactofuranose (Galf) residues.","Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Releases L-arabinose from arabinoxylan (By similarity). Secreted. Belongs to the glycosyl hydrolase 43 family",No,No,Maybe,No,No,not-Yes,GO:0004553,GO:0046556,GO:0046556,GO:0046556,GO:0046556; GO:0004553,GO:0046556,0.8582,0.8582,0.8582,0.9527,0.8582,5,0.8771,0.289,no
BDGF_ASPNC,A2QVZ0,ProtTale,Eukaryota,340,"Glycoside hydrolase family 43 beta-D-galactofuranosidase involved in the degradation of beta-galactofuranoside (Galf)-containing glycans such as galactomannan or O-glycans. Is not active on beta-1,5- or beta-1,6-linked beta-D-galactofuranose (Galf) residues.","Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan.",No,No,No,No,No,not-Yes,GO:0004553,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.289,no
BDGF_ASPNC,A2QVZ0,Protein2Text,Eukaryota,340,"Glycoside hydrolase family 43 beta-D-galactofuranosidase involved in the degradation of beta-galactofuranoside (Galf)-containing glycans such as galactomannan or O-glycans. Is not active on beta-1,5- or beta-1,6-linked beta-D-galactofuranose (Galf) residues.","The molecular function of this protein is endo-1,4-beta-glucanase activity, which is a type of catalytic activity that breaks down cellulose, a complex carbohydrate found in plant cell walls. Specifically, it catalyzes the hydrolysis of 1,4-beta-glucosidic linkages in cellulose. This is an important function for the breakdown of plant biomass and for the digestion of cellulose in the gut of herbivores.",No,No,No,No,No,not-Yes,GO:0004553,GO:0008810,GO:0008810,GO:0008810,GO:0008810,GO:0008810,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.289,no
BDGF_ASPNC,A2QVZ0,Reference,Eukaryota,340,"Glycoside hydrolase family 43 beta-D-galactofuranosidase involved in the degradation of beta-galactofuranoside (Galf)-containing glycans such as galactomannan or O-glycans. Is not active on beta-1,5- or beta-1,6-linked beta-D-galactofuranose (Galf) residues.","Glycoside hydrolase family 43 beta-D-galactofuranosidase involved in the degradation of beta-galactofuranoside (Galf)-containing glycans such as galactomannan or O-glycans. Is not active on beta-1,5- or beta-1,6-linked beta-D-galactofuranose (Galf) residues.",,,,,,,GO:0004553,GO:0016798,GO:0004553,GO:0004553,GO:0004553,GO:0004553,0.8416,1.0,1.0,1.0,1.0,5,0.9683,0.289,no
ASPGP_PYRCJ,A3MUS8,ESM2Text,Archaea,299,"Catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. Also displays D-asparaginase activity, which is about 20% of the L-asparaginase activity. Does not exhibit glutaminase activity.",Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins. Is involved in L-asparaginase beta-aspartate degradation and also in L-asparaginase-dependent beta-aspartate degradation.,No,No,Maybe,No,No,not-Yes,GO:0004067; GO:0008233,GO:0000224,GO:0000224,GO:0000224,GO:0000224,GO:0000224,0.5658,0.5658,0.5658,0.5658,0.5658,5,0.5658,0.4583,no
ASPGP_PYRCJ,A3MUS8,Prot2Text,Archaea,299,"Catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. Also displays D-asparaginase activity, which is about 20% of the L-asparaginase activity. Does not exhibit glutaminase activity.",Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Probably performs the final step in the degradation of the reserve polymer cyanophycin (depolymerizes the building block L-beta-Asp-Arg). Also has L-asparaginase activity.,No,No,Yes,No,Maybe,not-Yes,GO:0004067; GO:0008233,GO:0004067,GO:0004067,GO:0004067,GO:0004067,GO:0004067; GO:0016787,0.7944,0.7944,0.7944,0.7944,0.8547,5,0.8065,0.4583,no
ASPGP_PYRCJ,A3MUS8,ProtT3,Archaea,299,"Catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. Also displays D-asparaginase activity, which is about 20% of the L-asparaginase activity. Does not exhibit glutaminase activity.",Belongs to the Ntn-hydrolase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004067; GO:0008233,GO:0016787,GO:0016787,,GO:0016787,GO:0016787,0.6522,0.6522,,0.6522,0.6522,4,0.6522,0.4583,no
ASPGP_PYRCJ,A3MUS8,ProtTale,Archaea,299,"Catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. Also displays D-asparaginase activity, which is about 20% of the L-asparaginase activity. Does not exhibit glutaminase activity.",Has both L-asparaginase and beta-aspartyl peptidase activity. Can hydrolyze L-asparagine to L-aspartate and L-glutamate.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004067; GO:0008233,GO:0004067; GO:0016787,GO:0004067; GO:0016787,GO:0004067,GO:0004067,GO:0004067,0.8547,0.8547,0.7944,0.7944,0.7944,5,0.8185,0.4583,no
ASPGP_PYRCJ,A3MUS8,Protein2Text,Archaea,299,"Catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. Also displays D-asparaginase activity, which is about 20% of the L-asparaginase activity. Does not exhibit glutaminase activity.","The molecular function of this protein is not explicitly stated in the provided text. However, based on the name ""phosphoamino acid acylase"", it is likely that this protein is involved in the hydrolysis of phosphoamino acids, such as phosphoserine or phosphothreonine, into their corresponding amino acids and phosphate. This is a common function of enzymes with this name, and it is often involved in protein degradation and turnover.",Vague,Vague,No,Vague,No,not-Yes,GO:0004067; GO:0008233,,GO:0016787,,,,,0.6522,,,,1,0.6522,0.4583,no
ASPGP_PYRCJ,A3MUS8,Reference,Archaea,299,"Catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. Also displays D-asparaginase activity, which is about 20% of the L-asparaginase activity. Does not exhibit glutaminase activity.","Catalyzes the hydrolysis of L-asparagine into L-aspartate and ammonia. Also displays D-asparaginase activity, which is about 20% of the L-asparaginase activity. Does not exhibit glutaminase activity.",,,,,,,GO:0004067; GO:0008233,GO:0004067,GO:0004067,GO:0004067,GO:0004067,GO:0004067,0.7944,0.7944,0.7944,0.7944,0.7944,5,0.7944,0.4583,no
HODMA_ECTM1,A4XXY9,ESM2Text,Bacteria,338,"Component of the heme-dependent oxidative N-demethylase (HODM) enzyme, that catalyzes the NADPH-dependent oxidation of dimethylamine (DMA) to methylamine (MA) and formaldehyde. Functions in bacterial methylated amine catabolism, linking alkylamine oxidation to the tetrahydrofolate C1 pool. The alpha subunit of HODM binds heme, oxygen and DMA, and serves as the site of the oxidative N-demethylase activity.","Involved in the anaerobic fermentation of lysine. Catalyzes the oxidative deamination of L-erythro-3,5-diaminohexanoate (3,5-DAH) to 3-keto-D-arabinohexanoate (KAH). It can also react slowly with D-erythro-2,5-diaminohexanoate and analogs of D-erythro-3,5-diaminohexanoate, D-glucuronate and D-galacturonate. It can use D-galactonate and D-fuconate as substrates.",No,No,No,No,No,not-Yes,GO:0046872; GO:0016491,GO:0016491,GO:0016491,,GO:0016639,,0.7193,0.7193,,0.4947,,3,0.6444,0.396,no
HODMA_ECTM1,A4XXY9,Prot2Text,Bacteria,338,"Component of the heme-dependent oxidative N-demethylase (HODM) enzyme, that catalyzes the NADPH-dependent oxidation of dimethylamine (DMA) to methylamine (MA) and formaldehyde. Functions in bacterial methylated amine catabolism, linking alkylamine oxidation to the tetrahydrofolate C1 pool. The alpha subunit of HODM binds heme, oxygen and DMA, and serves as the site of the oxidative N-demethylase activity.",Ring-cleaving dioxygenase involved in the degradation of aromatic compounds via the protocatechuate pathway.,No,No,No,No,No,not-Yes,GO:0046872; GO:0016491,GO:0018579,,GO:0051213,GO:0018579,GO:0016701,0.3906,,0.5852,0.3906,0.5852,4,0.4879,0.396,no
HODMA_ECTM1,A4XXY9,ProtT3,Bacteria,338,"Component of the heme-dependent oxidative N-demethylase (HODM) enzyme, that catalyzes the NADPH-dependent oxidation of dimethylamine (DMA) to methylamine (MA) and formaldehyde. Functions in bacterial methylated amine catabolism, linking alkylamine oxidation to the tetrahydrofolate C1 pool. The alpha subunit of HODM binds heme, oxygen and DMA, and serves as the site of the oxidative N-demethylase activity.","Catalyzes the reductive methylation of 2'-deoxyuridine-5'- monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH(2) as the reductant. Belongs to the thymidylate synthase ThyX family",No,No,No,No,No,not-Yes,GO:0046872; GO:0016491,GO:0004799,GO:0004799,GO:0004799,GO:0004799,GO:0004799,0.2375,0.2375,0.2375,0.2375,0.2375,5,0.2375,0.396,no
HODMA_ECTM1,A4XXY9,ProtTale,Bacteria,338,"Component of the heme-dependent oxidative N-demethylase (HODM) enzyme, that catalyzes the NADPH-dependent oxidation of dimethylamine (DMA) to methylamine (MA) and formaldehyde. Functions in bacterial methylated amine catabolism, linking alkylamine oxidation to the tetrahydrofolate C1 pool. The alpha subunit of HODM binds heme, oxygen and DMA, and serves as the site of the oxidative N-demethylase activity.","Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity.",No,No,No,No,No,not-Yes,GO:0046872; GO:0016491,,,,,,,,,,,0,,0.396,no
HODMA_ECTM1,A4XXY9,Protein2Text,Bacteria,338,"Component of the heme-dependent oxidative N-demethylase (HODM) enzyme, that catalyzes the NADPH-dependent oxidation of dimethylamine (DMA) to methylamine (MA) and formaldehyde. Functions in bacterial methylated amine catabolism, linking alkylamine oxidation to the tetrahydrofolate C1 pool. The alpha subunit of HODM binds heme, oxygen and DMA, and serves as the site of the oxidative N-demethylase activity.","The molecular function of this protein is involved in the synthesis of tetrahydrobiopterin (BH4), a cofactor required for the function of aromatic amino acid hydroxylases. This protein is a rate-limiting enzyme in the biosynthesis of BH4, which is necessary for the proper functioning of phenylalanine, tyrosine, and tryptophan hydroxylases. The protein catalyzes the conversion of 7-biopterin to 6-pyruvoyl tetrahydropterin (6-PPT) and 5,6,7,8-tetrahydrobiopterin (BH4). The reaction involves the oxidation of 7-biopterin to 6- pyruvoyl tetrahydropterin (6-PPT) and the transfer of the pyruvoyl group from 6-PPT to dihydropteridine reductase (DHPR) to form BH4. The reaction is the last step in the biosynthesis of BH4. The protein is also involved in the regulation of nitric oxide synthase (NOS) activity by producing BH4, which is necessary for the proper functioning of NOS. BH4 is a critical cofactor for NOS, and its deficiency can lead to impaired NOS activity and decreased nitric oxide (NO) production. The protein is also involved in the regulation of the metabolism of neurotransmitters such as dopamine, serotonin, and norepinephrine, which are synthesized by aromatic amino acid hydroxylases that require BH4 as a cofactor.

In summary, the molecular function of this protein is to catalyze the conversion of 7-biopterin to 6-pyruvoyl tetrahydropterin (6-PPT) and 5,6,7,8-tetrahydrobiopterin (BH4), which is necessary for the proper functioning of aromatic amino acid hydroxylases and nitric oxide synthase. The protein is also involved in the regulation of the metabolism of neurotransmitters such as dopamine, serotonin, and norepinephrine.",No,No,No,No,No,not-Yes,GO:0046872; GO:0016491,,,,,,,,,,,0,,0.396,no
HODMA_ECTM1,A4XXY9,Reference,Bacteria,338,"Component of the heme-dependent oxidative N-demethylase (HODM) enzyme, that catalyzes the NADPH-dependent oxidation of dimethylamine (DMA) to methylamine (MA) and formaldehyde. Functions in bacterial methylated amine catabolism, linking alkylamine oxidation to the tetrahydrofolate C1 pool. The alpha subunit of HODM binds heme, oxygen and DMA, and serves as the site of the oxidative N-demethylase activity.","Component of the heme-dependent oxidative N-demethylase (HODM) enzyme, that catalyzes the NADPH-dependent oxidation of dimethylamine (DMA) to methylamine (MA) and formaldehyde. Functions in bacterial methylated amine catabolism, linking alkylamine oxidation to the tetrahydrofolate C1 pool. The alpha subunit of HODM binds heme, oxygen and DMA, and serves as the site of the oxidative N-demethylase activity.",,,,,,,GO:0046872; GO:0016491,GO:0016705,GO:0004497; GO:0020037,GO:0004497,GO:0004497; GO:0020037,GO:0004497,0.5852,0.5495,0.5852,0.5495,0.5852,5,0.5709,0.396,no
LAC3_ANOGA,A5YVV0,ESM2Text,Eukaryota,661,"Laccase with broad substrate range. May oxidize toxic molecules in the blood meal leading to detoxification or to cross-linking of the molecules to the peritrophic matrix, thus targeting them for excretion.",Lignin degradation and detoxification of lignin-derived products.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005507; GO:0016491,,,,,,,,,,,0,,0.4572,no
LAC3_ANOGA,A5YVV0,Prot2Text,Eukaryota,661,"Laccase with broad substrate range. May oxidize toxic molecules in the blood meal leading to detoxification or to cross-linking of the molecules to the peritrophic matrix, thus targeting them for excretion.",Lignin degradation and detoxification of lignin-derived products.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005507; GO:0016491,,,,,GO:0016491,,,,,0.7096,1,0.7096,0.4572,no
LAC3_ANOGA,A5YVV0,ProtT3,Eukaryota,661,"Laccase with broad substrate range. May oxidize toxic molecules in the blood meal leading to detoxification or to cross-linking of the molecules to the peritrophic matrix, thus targeting them for excretion.",Lignin degradation and detoxification of lignin-derived products. Secreted. Belongs to the multicopper oxidase family,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005507; GO:0016491,GO:0008471,GO:0008471,GO:0008471; GO:0005507,GO:0008471; GO:0005507,GO:0008471,0.0,0.0,0.7096,0.7096,0.0,5,0.2838,0.4572,no
LAC3_ANOGA,A5YVV0,ProtTale,Eukaryota,661,"Laccase with broad substrate range. May oxidize toxic molecules in the blood meal leading to detoxification or to cross-linking of the molecules to the peritrophic matrix, thus targeting them for excretion.","Multicopper oxidase; part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. Within the pathway, phiC is not involved in the oxidation of phomoidrides. The pathway begins with the highly reducing polyketide synthase phiA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase phiM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) phiJ and the alkylcit",No,No,No,No,No,not-Yes,GO:0005507; GO:0016491,GO:0016491,GO:0016491,GO:0016682,GO:0016682,GO:0016682,0.7096,0.7096,0.4873,0.4873,0.4873,5,0.5762,0.4572,no
LAC3_ANOGA,A5YVV0,Protein2Text,Eukaryota,661,"Laccase with broad substrate range. May oxidize toxic molecules in the blood meal leading to detoxification or to cross-linking of the molecules to the peritrophic matrix, thus targeting them for excretion.",The molecular function of this protein is copper oxidase. It is involved in the oxidation of copper and other metal ions.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005507; GO:0016491,GO:0005507; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0005507,1.0,0.7096,0.7096,0.7096,0.7096,5,0.7677,0.4572,no
LAC3_ANOGA,A5YVV0,Reference,Eukaryota,661,"Laccase with broad substrate range. May oxidize toxic molecules in the blood meal leading to detoxification or to cross-linking of the molecules to the peritrophic matrix, thus targeting them for excretion.","Laccase with broad substrate range. May oxidize toxic molecules in the blood meal leading to detoxification or to cross-linking of the molecules to the peritrophic matrix, thus targeting them for excretion.",,,,,,,GO:0005507; GO:0016491,GO:0008471,GO:0008471,GO:0008471,GO:0008471,GO:0008471,0.0,0.0,0.0,0.0,0.0,5,0.0,0.4572,no
PPM1K_RAT,A6K136,ESM2Text,Eukaryota,372,"Serine/threonine-protein phosphatase component of macronutrients metabolism. Together with BCKDK serves as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) and protein synthesis with glucose and lipid metabolism via two distinct phosphoprotein targets: BCKDHA/E1a subunit of the branched-chain alpha- ketoacid dehydrogenase (BCKDH) complex and ACLY, a lipogenic enzyme of Krebs cycle. At high levels of branched-chain ketoacids (BCKAs), dephosphorylates and activates mitochondrial BCKDH complex, a multisubunit complex consisting of three components, heterotetrameric E1 composed of BCKDHA and BCKDHB chains, 24-meric E2 core composed of DBT and homodimeric E3 composed of DLD, each involved in different steps of BCAA catabolism. Tightly associates with the E2 subunit of BCKDH complex and dephosphorylates Ser-333 of BCKDHA chain of the E1 subunit likely through on-off binding to individual E2 subunits of the 24-meric E2 core to increase the efficiency of the dephosphorylation reaction. Appears to dephosphorylate and inactivate cytosolic ACLY in response to changes of cellular carbohydrate abundance. Overnutrition and in particular high-fructose diet, activates MLXIPL/ChREBP leading to increased BCKDK to PPM1K ratio, phosphorylation of ACLY on Ser-454 and activation of its enzymatic activity that ultimately results in the generation of acetyl-CoA and malonyl-CoA immediate substrates of de novo lipogenesis. Recognizes phosphosites having SxS or RxxS motifs and strictly depends on Mn(2+) ions for the phosphatase activity. Regulates Ca(2+)-induced opening of mitochondrial transition pore and apoptotic cell death.",Regulates the mitochondrial permeability transition pore and is essential for cellular survival and development.,No,No,No,No,Maybe,not-Yes,GO:0047385; GO:0030145; GO:0004722,,,,,,,,,,,0,,0.5843,yes
PPM1K_RAT,A6K136,Prot2Text,Eukaryota,372,"Serine/threonine-protein phosphatase component of macronutrients metabolism. Together with BCKDK serves as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) and protein synthesis with glucose and lipid metabolism via two distinct phosphoprotein targets: BCKDHA/E1a subunit of the branched-chain alpha- ketoacid dehydrogenase (BCKDH) complex and ACLY, a lipogenic enzyme of Krebs cycle. At high levels of branched-chain ketoacids (BCKAs), dephosphorylates and activates mitochondrial BCKDH complex, a multisubunit complex consisting of three components, heterotetrameric E1 composed of BCKDHA and BCKDHB chains, 24-meric E2 core composed of DBT and homodimeric E3 composed of DLD, each involved in different steps of BCAA catabolism. Tightly associates with the E2 subunit of BCKDH complex and dephosphorylates Ser-333 of BCKDHA chain of the E1 subunit likely through on-off binding to individual E2 subunits of the 24-meric E2 core to increase the efficiency of the dephosphorylation reaction. Appears to dephosphorylate and inactivate cytosolic ACLY in response to changes of cellular carbohydrate abundance. Overnutrition and in particular high-fructose diet, activates MLXIPL/ChREBP leading to increased BCKDK to PPM1K ratio, phosphorylation of ACLY on Ser-454 and activation of its enzymatic activity that ultimately results in the generation of acetyl-CoA and malonyl-CoA immediate substrates of de novo lipogenesis. Recognizes phosphosites having SxS or RxxS motifs and strictly depends on Mn(2+) ions for the phosphatase activity. Regulates Ca(2+)-induced opening of mitochondrial transition pore and apoptotic cell death.",Regulates the mitochondrial permeability transition pore and is essential for cellular survival and development.,No,No,No,No,Maybe,not-Yes,GO:0047385; GO:0030145; GO:0004722,,,,,,,,,,,0,,0.5843,yes
PPM1K_RAT,A6K136,ProtT3,Eukaryota,372,"Serine/threonine-protein phosphatase component of macronutrients metabolism. Together with BCKDK serves as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) and protein synthesis with glucose and lipid metabolism via two distinct phosphoprotein targets: BCKDHA/E1a subunit of the branched-chain alpha- ketoacid dehydrogenase (BCKDH) complex and ACLY, a lipogenic enzyme of Krebs cycle. At high levels of branched-chain ketoacids (BCKAs), dephosphorylates and activates mitochondrial BCKDH complex, a multisubunit complex consisting of three components, heterotetrameric E1 composed of BCKDHA and BCKDHB chains, 24-meric E2 core composed of DBT and homodimeric E3 composed of DLD, each involved in different steps of BCAA catabolism. Tightly associates with the E2 subunit of BCKDH complex and dephosphorylates Ser-333 of BCKDHA chain of the E1 subunit likely through on-off binding to individual E2 subunits of the 24-meric E2 core to increase the efficiency of the dephosphorylation reaction. Appears to dephosphorylate and inactivate cytosolic ACLY in response to changes of cellular carbohydrate abundance. Overnutrition and in particular high-fructose diet, activates MLXIPL/ChREBP leading to increased BCKDK to PPM1K ratio, phosphorylation of ACLY on Ser-454 and activation of its enzymatic activity that ultimately results in the generation of acetyl-CoA and malonyl-CoA immediate substrates of de novo lipogenesis. Recognizes phosphosites having SxS or RxxS motifs and strictly depends on Mn(2+) ions for the phosphatase activity. Regulates Ca(2+)-induced opening of mitochondrial transition pore and apoptotic cell death.",Mitochondrion matrix. Belongs to the PP2C family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0047385; GO:0030145; GO:0004722,GO:0004722,GO:0004722,GO:0004722,GO:0004722,GO:0004722,0.7188,0.7188,0.7188,0.7188,0.7188,5,0.7188,0.5843,yes
PPM1K_RAT,A6K136,ProtTale,Eukaryota,372,"Serine/threonine-protein phosphatase component of macronutrients metabolism. Together with BCKDK serves as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) and protein synthesis with glucose and lipid metabolism via two distinct phosphoprotein targets: BCKDHA/E1a subunit of the branched-chain alpha- ketoacid dehydrogenase (BCKDH) complex and ACLY, a lipogenic enzyme of Krebs cycle. At high levels of branched-chain ketoacids (BCKAs), dephosphorylates and activates mitochondrial BCKDH complex, a multisubunit complex consisting of three components, heterotetrameric E1 composed of BCKDHA and BCKDHB chains, 24-meric E2 core composed of DBT and homodimeric E3 composed of DLD, each involved in different steps of BCAA catabolism. Tightly associates with the E2 subunit of BCKDH complex and dephosphorylates Ser-333 of BCKDHA chain of the E1 subunit likely through on-off binding to individual E2 subunits of the 24-meric E2 core to increase the efficiency of the dephosphorylation reaction. Appears to dephosphorylate and inactivate cytosolic ACLY in response to changes of cellular carbohydrate abundance. Overnutrition and in particular high-fructose diet, activates MLXIPL/ChREBP leading to increased BCKDK to PPM1K ratio, phosphorylation of ACLY on Ser-454 and activation of its enzymatic activity that ultimately results in the generation of acetyl-CoA and malonyl-CoA immediate substrates of de novo lipogenesis. Recognizes phosphosites having SxS or RxxS motifs and strictly depends on Mn(2+) ions for the phosphatase activity. Regulates Ca(2+)-induced opening of mitochondrial transition pore and apoptotic cell death.",Phosphatase that specifically dephosphorylates and inhibits SNF1 kinase activity.,Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0047385; GO:0030145; GO:0004722,GO:0004722,GO:0004721,GO:0004721,GO:0004722,GO:0004721,0.7188,0.6981,0.6981,0.7188,0.6981,5,0.7064,0.5843,yes
PPM1K_RAT,A6K136,Protein2Text,Eukaryota,372,"Serine/threonine-protein phosphatase component of macronutrients metabolism. Together with BCKDK serves as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) and protein synthesis with glucose and lipid metabolism via two distinct phosphoprotein targets: BCKDHA/E1a subunit of the branched-chain alpha- ketoacid dehydrogenase (BCKDH) complex and ACLY, a lipogenic enzyme of Krebs cycle. At high levels of branched-chain ketoacids (BCKAs), dephosphorylates and activates mitochondrial BCKDH complex, a multisubunit complex consisting of three components, heterotetrameric E1 composed of BCKDHA and BCKDHB chains, 24-meric E2 core composed of DBT and homodimeric E3 composed of DLD, each involved in different steps of BCAA catabolism. Tightly associates with the E2 subunit of BCKDH complex and dephosphorylates Ser-333 of BCKDHA chain of the E1 subunit likely through on-off binding to individual E2 subunits of the 24-meric E2 core to increase the efficiency of the dephosphorylation reaction. Appears to dephosphorylate and inactivate cytosolic ACLY in response to changes of cellular carbohydrate abundance. Overnutrition and in particular high-fructose diet, activates MLXIPL/ChREBP leading to increased BCKDK to PPM1K ratio, phosphorylation of ACLY on Ser-454 and activation of its enzymatic activity that ultimately results in the generation of acetyl-CoA and malonyl-CoA immediate substrates of de novo lipogenesis. Recognizes phosphosites having SxS or RxxS motifs and strictly depends on Mn(2+) ions for the phosphatase activity. Regulates Ca(2+)-induced opening of mitochondrial transition pore and apoptotic cell death.",The molecular function of this protein is a protein phosphatase.,Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0047385; GO:0030145; GO:0004722,GO:0004721,GO:0004721,GO:0004721,GO:0004721,GO:0004721,0.6981,0.6981,0.6981,0.6981,0.6981,5,0.6981,0.5843,yes
PPM1K_RAT,A6K136,Reference,Eukaryota,372,"Serine/threonine-protein phosphatase component of macronutrients metabolism. Together with BCKDK serves as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) and protein synthesis with glucose and lipid metabolism via two distinct phosphoprotein targets: BCKDHA/E1a subunit of the branched-chain alpha- ketoacid dehydrogenase (BCKDH) complex and ACLY, a lipogenic enzyme of Krebs cycle. At high levels of branched-chain ketoacids (BCKAs), dephosphorylates and activates mitochondrial BCKDH complex, a multisubunit complex consisting of three components, heterotetrameric E1 composed of BCKDHA and BCKDHB chains, 24-meric E2 core composed of DBT and homodimeric E3 composed of DLD, each involved in different steps of BCAA catabolism. Tightly associates with the E2 subunit of BCKDH complex and dephosphorylates Ser-333 of BCKDHA chain of the E1 subunit likely through on-off binding to individual E2 subunits of the 24-meric E2 core to increase the efficiency of the dephosphorylation reaction. Appears to dephosphorylate and inactivate cytosolic ACLY in response to changes of cellular carbohydrate abundance. Overnutrition and in particular high-fructose diet, activates MLXIPL/ChREBP leading to increased BCKDK to PPM1K ratio, phosphorylation of ACLY on Ser-454 and activation of its enzymatic activity that ultimately results in the generation of acetyl-CoA and malonyl-CoA immediate substrates of de novo lipogenesis. Recognizes phosphosites having SxS or RxxS motifs and strictly depends on Mn(2+) ions for the phosphatase activity. Regulates Ca(2+)-induced opening of mitochondrial transition pore and apoptotic cell death.","Serine/threonine-protein phosphatase component of macronutrients metabolism. Together with BCKDK serves as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) and protein synthesis with glucose and lipid metabolism via two distinct phosphoprotein targets: BCKDHA/E1a subunit of the branched-chain alpha- ketoacid dehydrogenase (BCKDH) complex and ACLY, a lipogenic enzyme of Krebs cycle. At high levels of branched-chain ketoacids (BCKAs), dephosphorylates and activates mitochondrial BCKDH complex, a multisubunit complex consisting of three components, heterotetrameric E1 composed of BCKDHA and BCKDHB chains, 24-meric E2 core composed of DBT and homodimeric E3 composed of DLD, each involved in different steps of BCAA catabolism. Tightly associates with the E2 subunit of BCKDH complex and dephosphorylates Ser-333 of BCKDHA chain of the E1 subunit likely through on-off binding to individual E2 subunits of the 24-meric E2 core to increase the efficiency of the dephosphorylation reaction. Appears to dephosphorylate and inactivate cytosolic ACLY in response to changes of cellular carbohydrate abundance. Overnutrition and in particular high-fructose diet, activates MLXIPL/ChREBP leading to increased BCKDK to PPM1K ratio, phosphorylation of ACLY on Ser-454 and activation of its enzymatic activity that ultimately results in the generation of acetyl-CoA and malonyl-CoA immediate substrates of de novo lipogenesis. Recognizes phosphosites having SxS or RxxS motifs and strictly depends on Mn(2+) ions for the phosphatase activity. Regulates Ca(2+)-induced opening of mitochondrial transition pore and apoptotic cell death.",,,,,,,GO:0047385; GO:0030145; GO:0004722,GO:0004722,GO:0004722,GO:0004722,GO:0004722; GO:0030145,GO:0004722,0.7188,0.7188,0.7188,0.9619,0.7188,5,0.7674,0.5843,yes
NANA_MEDG7,A7B555,ESM2Text,Bacteria,315,"Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate. Cannot use 2,7-anhydro-Neu5Ac. Involved in the degradation of sialic acid, which is present in the host mucus layer and represents a much-coveted source of nutrients for R.gnavus, a prevalent member of the normal gut microbiota.",Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).,No,No,No,No,Maybe,not-Yes,GO:0008747,GO:0008840,GO:0008840,GO:0008840,GO:0008840,GO:0008840,0.3386,0.3386,0.3386,0.3386,0.3386,5,0.3386,0.299,no
NANA_MEDG7,A7B555,Prot2Text,Bacteria,315,"Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate. Cannot use 2,7-anhydro-Neu5Ac. Involved in the degradation of sialic acid, which is present in the host mucus layer and represents a much-coveted source of nutrients for R.gnavus, a prevalent member of the normal gut microbiota.",Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).,No,No,No,No,No,not-Yes,GO:0008747,GO:0008840,GO:0008840,GO:0008840,GO:0008840,GO:0008840,0.3386,0.3386,0.3386,0.3386,0.3386,5,0.3386,0.299,no
NANA_MEDG7,A7B555,ProtT3,Bacteria,315,"Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate. Cannot use 2,7-anhydro-Neu5Ac. Involved in the degradation of sialic acid, which is present in the host mucus layer and represents a much-coveted source of nutrients for R.gnavus, a prevalent member of the normal gut microbiota.",Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate. Cytoplasm. Belongs to the DapA family. NanA subfamily,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008747,GO:0004308,GO:0008747,GO:0008747,GO:0004308,GO:0004308,0.1737,1.0,1.0,0.1737,0.1737,5,0.5042,0.299,no
NANA_MEDG7,A7B555,ProtTale,Bacteria,315,"Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate. Cannot use 2,7-anhydro-Neu5Ac. Involved in the degradation of sialic acid, which is present in the host mucus layer and represents a much-coveted source of nutrients for R.gnavus, a prevalent member of the normal gut microbiota.",Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008747,GO:0004457,GO:0004457,GO:0008747,GO:0004668,GO:0004765,0.2353,0.2353,1.0,0.1998,0.1803,5,0.3701,0.299,no
NANA_MEDG7,A7B555,Protein2Text,Bacteria,315,"Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate. Cannot use 2,7-anhydro-Neu5Ac. Involved in the degradation of sialic acid, which is present in the host mucus layer and represents a much-coveted source of nutrients for R.gnavus, a prevalent member of the normal gut microbiota.","The molecular function of this protein is an aldolase, specifically a reversible aldolase, which catalyzes the reversible aldol cleavage of 2-keto-3-deoxy-6-phosphogluconate (KDPG) to pyruvate and glyceraldehyde-3-phosphate (G3P). 
This enzyme is involved in the Entner-Doudoroff (ED) pathway, which is a metabolic pathway used by many bacteria and plants to break down glucose into pyruvate and other intermediates. The ED pathway consists of 7 enzymatic steps that ultimately convert glucose into pyruvate, producing several key metabolites as byproducts. 
In this pathway, this protein catalyzes the reversible aldol cleavage of KDPG to pyruvate and G3P, producing the KDPG aldolase activity. This step is crucial for the ED pathway because it allows the pathway to bypass the oxidative phase and directly convert glucose into pyruvate. 
The protein's ability to catalyze the reversible aldol cleavage of KDPG makes it a key enzyme in the ED pathway, allowing the pathway to function efficiently and maintain homeostasis in the cell. 
The protein's molecular function is also essential for the survival of bacteria that use the ED pathway, as it allows them to metabolize glucose and produce energy in the form of ATP. 
In addition, the protein's molecular function is also important for the production of various metabolites, such as G3P and pyruvate, which are used as building blocks for the synthesis of other biomolecules. 
Overall, the protein's molecular function is crucial for the survival and metabolism of bacteria that use the ED pathway, and it plays a key role in the production of various metabolites.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008747,GO:0004332,GO:0008674,GO:0016832,GO:0016829,GO:0008670,0.5121,0.5121,0.6029,0.6019,0.1998,5,0.4858,0.299,no
NANA_MEDG7,A7B555,Reference,Bacteria,315,"Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate. Cannot use 2,7-anhydro-Neu5Ac. Involved in the degradation of sialic acid, which is present in the host mucus layer and represents a much-coveted source of nutrients for R.gnavus, a prevalent member of the normal gut microbiota.","Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate. Cannot use 2,7-anhydro-Neu5Ac. Involved in the degradation of sialic acid, which is present in the host mucus layer and represents a much-coveted source of nutrients for R.gnavus, a prevalent member of the normal gut microbiota.",,,,,,,GO:0008747,GO:0008747,GO:0008747,GO:0008747,GO:0008747,GO:0008747,1.0,1.0,1.0,1.0,1.0,5,1.0,0.299,no
UXNAS_BACCN,A7GKX7,ESM2Text,Bacteria,321,"Decarboxylase involved in the biosynthesis of the nucleotide- sugar UDP-N-acetylxylosamine (UDP-XylNAc). Catalyzes the NAD-dependent decarboxylation of UDP-N-acetylglucosaminuronic acid (UDP-GlcNAcA) to UDP-XylNAc. Cannot use other UDP- uronates, such as UDP-glucuronic acid (UDP-GlcA) and UDP-galacturonic acid (UDP-GalA).",Catalyzes the stereospecific reduction of the C-4 methyl group of dTDP-4-dehydro-6-deoxy-D-glucose to dTDP-D-allose.,No,No,No,No,No,not-Yes,GO:0070403; GO:0048040,GO:0016491,GO:0016491,,,,0.2721,0.2721,,,,2,0.2721,0.1784,no
UXNAS_BACCN,A7GKX7,Prot2Text,Bacteria,321,"Decarboxylase involved in the biosynthesis of the nucleotide- sugar UDP-N-acetylxylosamine (UDP-XylNAc). Catalyzes the NAD-dependent decarboxylation of UDP-N-acetylglucosaminuronic acid (UDP-GlcNAcA) to UDP-XylNAc. Cannot use other UDP- uronates, such as UDP-glucuronic acid (UDP-GlcA) and UDP-galacturonic acid (UDP-GalA).",Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid to UDP-xylose. Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0070403; GO:0048040,GO:0019305,GO:0034010,GO:0042285,GO:0047649,GO:0051872,0.0,0.2902,0.1542,0.1397,0.0,5,0.1168,0.1784,no
UXNAS_BACCN,A7GKX7,ProtT3,Bacteria,321,"Decarboxylase involved in the biosynthesis of the nucleotide- sugar UDP-N-acetylxylosamine (UDP-XylNAc). Catalyzes the NAD-dependent decarboxylation of UDP-N-acetylglucosaminuronic acid (UDP-GlcNAcA) to UDP-XylNAc. Cannot use other UDP- uronates, such as UDP-glucuronic acid (UDP-GlcA) and UDP-galacturonic acid (UDP-GalA).",Involved in the biosynthesis of UDP-galactose. Catalyzes the reversible NAD-dependent epimerization of UDP-glucuronic acid (UDP-GlcUA) to UDP-galacturonic acid (UDP-GalUA). Belongs to the NAD(P)-dependent epimerase/dehydratase family,No,Maybe,No,No,No,not-Yes,GO:0070403; GO:0048040,GO:0050378,GO:0050378,GO:0042350; GO:0051287,GO:0050378,GO:0050378,0.1542,0.1542,0.4105,0.1542,0.1542,5,0.2055,0.1784,no
UXNAS_BACCN,A7GKX7,ProtTale,Bacteria,321,"Decarboxylase involved in the biosynthesis of the nucleotide- sugar UDP-N-acetylxylosamine (UDP-XylNAc). Catalyzes the NAD-dependent decarboxylation of UDP-N-acetylglucosaminuronic acid (UDP-GlcNAcA) to UDP-XylNAc. Cannot use other UDP- uronates, such as UDP-glucuronic acid (UDP-GlcA) and UDP-galacturonic acid (UDP-GalA).",Catalyzes the conversion of UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UDP-MurNAc-L-Ala-D-Glu) to UDP-N-acetylmuramoyl-L-alanyl-D-alanyl-D-glutamate (UDP-L-alanyl-D-alanyl-D-glutamate).,No,No,No,No,No,not-Yes,GO:0070403; GO:0048040,GO:0008765,GO:0008765,GO:0016874,GO:0016874,GO:0016874,0.1542,0.1542,0.2721,0.2721,0.2721,5,0.2249,0.1784,no
UXNAS_BACCN,A7GKX7,Protein2Text,Bacteria,321,"Decarboxylase involved in the biosynthesis of the nucleotide- sugar UDP-N-acetylxylosamine (UDP-XylNAc). Catalyzes the NAD-dependent decarboxylation of UDP-N-acetylglucosaminuronic acid (UDP-GlcNAcA) to UDP-XylNAc. Cannot use other UDP- uronates, such as UDP-glucuronic acid (UDP-GlcA) and UDP-galacturonic acid (UDP-GalA).","The molecular function of this protein is a sugar transferase. More specifically, it is a GDP-fucose:beta-1,4-N-acetylglucosaminide alpha-1,6-fucosyltransferase, which is a type of enzyme that catalyzes the transfer of a fucose molecule from GDP-fucose to the N-acetylglucosamine (GlcNAc) residue in the core of a glycoprotein, resulting in the formation of a fucose linkage to the GlcNAc residue. This protein is involved in the synthesis of fucosylated glycoproteins, which play important roles in various biological processes, including cell adhesion, signaling, and immune responses. The fucose linkage catalyzed by this protein is a common modification found in many glycoproteins, including immunoglobulins, cytokines, and adhesion molecules. 

In summary, the molecular function of this protein is to catalyze the transfer of a fucose molecule from GDP-fucose to the N-acetylglucosamine (GlcNAc) residue in the core of a glycoprotein, resulting in the formation of a fucose linkage to the GlcNAc residue.",No,No,No,No,No,not-Yes,GO:0070403; GO:0048040,GO:0046921,GO:0046921,GO:0016757,GO:0008417,GO:0046921,0.1342,0.1342,0.2186,0.1542,0.1342,5,0.1551,0.1784,no
UXNAS_BACCN,A7GKX7,Reference,Bacteria,321,"Decarboxylase involved in the biosynthesis of the nucleotide- sugar UDP-N-acetylxylosamine (UDP-XylNAc). Catalyzes the NAD-dependent decarboxylation of UDP-N-acetylglucosaminuronic acid (UDP-GlcNAcA) to UDP-XylNAc. Cannot use other UDP- uronates, such as UDP-glucuronic acid (UDP-GlcA) and UDP-galacturonic acid (UDP-GalA).","Decarboxylase involved in the biosynthesis of the nucleotide- sugar UDP-N-acetylxylosamine (UDP-XylNAc). Catalyzes the NAD-dependent decarboxylation of UDP-N-acetylglucosaminuronic acid (UDP-GlcNAcA) to UDP-XylNAc. Cannot use other UDP- uronates, such as UDP-glucuronic acid (UDP-GlcA) and UDP-galacturonic acid (UDP-GalA).",,,,,,,GO:0070403; GO:0048040,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.5965,0.5965,0.5965,0.5965,0.5965,5,0.5965,0.1784,no
CYMD_SALAI,A8M6W6,ESM2Text,Bacteria,373,"Dimethylallyltryptophan synthase; part of the gene cluster that mediates the biosynthesis of cyclic heptapeptides, known as cyclomarins and also of cyclic dipeptides, called cyclomarazines, which have both antimicrobial and cytotoxic effects. Catalyzes the reverse N-prenylation of monomeric L- tryptophan with dimethylallyl diphosphate (DMAPP) to form N-(1,1- dimethylallyl)-tryptophan (r-N-DMAT). The formation of r-N-DMAT appears to proceed via the deprotonation of the indole nitrogen of tryptophan, which facilitates a nucleophilic attack on the carbocation that is forming on the dimethylallyl group as the diphosphate dissociates. The N-(1,1-dimethylallyl)-tryptophan produced by CymD is combined with a range of standard and nonproteinogenic amino acid substrates to synthesize the peptides, a process that is probably catalyzed by the non-canonical nonribosomal peptide synthetase (NRPS), CymA. Other proteins in the cluster catalyze further modifications of the peptides including CymV which catalyzes the oxidation of olefinic cyclomarins and cyclomarazines to their respective epoxide derivatives. Utilizes only DMAPP as the prenyl donor and has no requirement for divalent cations.","Together with AceAa, they could catalyze the formation of succinate and glyoxylate from isocitrate.",No,No,No,No,No,not-Yes,GO:0016765,GO:0004451,GO:0004451,GO:0004451,GO:0004451,GO:0004451,0.2845,0.2845,0.2845,0.2845,0.2845,5,0.2845,0.4116,no
CYMD_SALAI,A8M6W6,Prot2Text,Bacteria,373,"Dimethylallyltryptophan synthase; part of the gene cluster that mediates the biosynthesis of cyclic heptapeptides, known as cyclomarins and also of cyclic dipeptides, called cyclomarazines, which have both antimicrobial and cytotoxic effects. Catalyzes the reverse N-prenylation of monomeric L- tryptophan with dimethylallyl diphosphate (DMAPP) to form N-(1,1- dimethylallyl)-tryptophan (r-N-DMAT). The formation of r-N-DMAT appears to proceed via the deprotonation of the indole nitrogen of tryptophan, which facilitates a nucleophilic attack on the carbocation that is forming on the dimethylallyl group as the diphosphate dissociates. The N-(1,1-dimethylallyl)-tryptophan produced by CymD is combined with a range of standard and nonproteinogenic amino acid substrates to synthesize the peptides, a process that is probably catalyzed by the non-canonical nonribosomal peptide synthetase (NRPS), CymA. Other proteins in the cluster catalyze further modifications of the peptides including CymV which catalyzes the oxidation of olefinic cyclomarins and cyclomarazines to their respective epoxide derivatives. Utilizes only DMAPP as the prenyl donor and has no requirement for divalent cations.",Deaminates adenosine-37 to inosine in tRNA-Ala.,No,No,No,No,No,not-Yes,GO:0016765,GO:0008251,GO:0008251,GO:0008251,GO:0008251,GO:0008251,0.1959,0.1959,0.1959,0.1959,0.1959,5,0.1959,0.4116,no
CYMD_SALAI,A8M6W6,ProtT3,Bacteria,373,"Dimethylallyltryptophan synthase; part of the gene cluster that mediates the biosynthesis of cyclic heptapeptides, known as cyclomarins and also of cyclic dipeptides, called cyclomarazines, which have both antimicrobial and cytotoxic effects. Catalyzes the reverse N-prenylation of monomeric L- tryptophan with dimethylallyl diphosphate (DMAPP) to form N-(1,1- dimethylallyl)-tryptophan (r-N-DMAT). The formation of r-N-DMAT appears to proceed via the deprotonation of the indole nitrogen of tryptophan, which facilitates a nucleophilic attack on the carbocation that is forming on the dimethylallyl group as the diphosphate dissociates. The N-(1,1-dimethylallyl)-tryptophan produced by CymD is combined with a range of standard and nonproteinogenic amino acid substrates to synthesize the peptides, a process that is probably catalyzed by the non-canonical nonribosomal peptide synthetase (NRPS), CymA. Other proteins in the cluster catalyze further modifications of the peptides including CymV which catalyzes the oxidation of olefinic cyclomarins and cyclomarazines to their respective epoxide derivatives. Utilizes only DMAPP as the prenyl donor and has no requirement for divalent cations.",Catalyzes the condensation of anthranilate with S-adenosyl-L-methionine to form N-(2-amino-2-carboxyethyl)-anthranilate. Belongs to the anthranilate N-methyltransferase family,No,No,No,No,Maybe,not-Yes,GO:0016765,GO:0008168,GO:0008171,GO:0008757,GO:0008168,GO:0008168,0.5565,0.482,0.482,0.5565,0.5565,5,0.5267,0.4116,no
CYMD_SALAI,A8M6W6,ProtTale,Bacteria,373,"Dimethylallyltryptophan synthase; part of the gene cluster that mediates the biosynthesis of cyclic heptapeptides, known as cyclomarins and also of cyclic dipeptides, called cyclomarazines, which have both antimicrobial and cytotoxic effects. Catalyzes the reverse N-prenylation of monomeric L- tryptophan with dimethylallyl diphosphate (DMAPP) to form N-(1,1- dimethylallyl)-tryptophan (r-N-DMAT). The formation of r-N-DMAT appears to proceed via the deprotonation of the indole nitrogen of tryptophan, which facilitates a nucleophilic attack on the carbocation that is forming on the dimethylallyl group as the diphosphate dissociates. The N-(1,1-dimethylallyl)-tryptophan produced by CymD is combined with a range of standard and nonproteinogenic amino acid substrates to synthesize the peptides, a process that is probably catalyzed by the non-canonical nonribosomal peptide synthetase (NRPS), CymA. Other proteins in the cluster catalyze further modifications of the peptides including CymV which catalyzes the oxidation of olefinic cyclomarins and cyclomarazines to their respective epoxide derivatives. Utilizes only DMAPP as the prenyl donor and has no requirement for divalent cations.",Catalyzes the cyclization of 2-keto-3-deoxy-D-arabino-heptulosonate 7-phosphate (KDO7P) into brassinosteroid (BR) and 2-keto-3-deoxy-D-arabino-heptulosonate 6-phosphate (KDO6P) into BR.,No,No,No,No,No,not-Yes,GO:0016765,GO:0016829,GO:0016829,GO:0016829,,GO:0016829,0.4807,0.4807,0.4807,,0.4807,4,0.4807,0.4116,no
CYMD_SALAI,A8M6W6,Protein2Text,Bacteria,373,"Dimethylallyltryptophan synthase; part of the gene cluster that mediates the biosynthesis of cyclic heptapeptides, known as cyclomarins and also of cyclic dipeptides, called cyclomarazines, which have both antimicrobial and cytotoxic effects. Catalyzes the reverse N-prenylation of monomeric L- tryptophan with dimethylallyl diphosphate (DMAPP) to form N-(1,1- dimethylallyl)-tryptophan (r-N-DMAT). The formation of r-N-DMAT appears to proceed via the deprotonation of the indole nitrogen of tryptophan, which facilitates a nucleophilic attack on the carbocation that is forming on the dimethylallyl group as the diphosphate dissociates. The N-(1,1-dimethylallyl)-tryptophan produced by CymD is combined with a range of standard and nonproteinogenic amino acid substrates to synthesize the peptides, a process that is probably catalyzed by the non-canonical nonribosomal peptide synthetase (NRPS), CymA. Other proteins in the cluster catalyze further modifications of the peptides including CymV which catalyzes the oxidation of olefinic cyclomarins and cyclomarazines to their respective epoxide derivatives. Utilizes only DMAPP as the prenyl donor and has no requirement for divalent cations.","The molecular function of this protein is as a decarboxylase, specifically a phenylalanine decarboxylase, involved in the biosynthesis of tyramine.",No,No,No,No,No,not-Yes,GO:0016765,GO:0004058,GO:0016831,GO:0004058,GO:0004058,GO:0004058,0.2845,0.3284,0.2845,0.2845,0.2845,5,0.2933,0.4116,no
CYMD_SALAI,A8M6W6,Reference,Bacteria,373,"Dimethylallyltryptophan synthase; part of the gene cluster that mediates the biosynthesis of cyclic heptapeptides, known as cyclomarins and also of cyclic dipeptides, called cyclomarazines, which have both antimicrobial and cytotoxic effects. Catalyzes the reverse N-prenylation of monomeric L- tryptophan with dimethylallyl diphosphate (DMAPP) to form N-(1,1- dimethylallyl)-tryptophan (r-N-DMAT). The formation of r-N-DMAT appears to proceed via the deprotonation of the indole nitrogen of tryptophan, which facilitates a nucleophilic attack on the carbocation that is forming on the dimethylallyl group as the diphosphate dissociates. The N-(1,1-dimethylallyl)-tryptophan produced by CymD is combined with a range of standard and nonproteinogenic amino acid substrates to synthesize the peptides, a process that is probably catalyzed by the non-canonical nonribosomal peptide synthetase (NRPS), CymA. Other proteins in the cluster catalyze further modifications of the peptides including CymV which catalyzes the oxidation of olefinic cyclomarins and cyclomarazines to their respective epoxide derivatives. Utilizes only DMAPP as the prenyl donor and has no requirement for divalent cations.","Dimethylallyltryptophan synthase; part of the gene cluster that mediates the biosynthesis of cyclic heptapeptides, known as cyclomarins and also of cyclic dipeptides, called cyclomarazines, which have both antimicrobial and cytotoxic effects. Catalyzes the reverse N-prenylation of monomeric L- tryptophan with dimethylallyl diphosphate (DMAPP) to form N-(1,1- dimethylallyl)-tryptophan (r-N-DMAT). The formation of r-N-DMAT appears to proceed via the deprotonation of the indole nitrogen of tryptophan, which facilitates a nucleophilic attack on the carbocation that is forming on the dimethylallyl group as the diphosphate dissociates. The N-(1,1-dimethylallyl)-tryptophan produced by CymD is combined with a range of standard and nonproteinogenic amino acid substrates to synthesize the peptides, a process that is probably catalyzed by the non-canonical nonribosomal peptide synthetase (NRPS), CymA. Other proteins in the cluster catalyze further modifications of the peptides including CymV which catalyzes the oxidation of olefinic cyclomarins and cyclomarazines to their respective epoxide derivatives. Utilizes only DMAPP as the prenyl donor and has no requirement for divalent cations.",,,,,,,GO:0016765,GO:0016765,GO:0004659,GO:0004659,GO:0016765,GO:0016765,1.0,0.8416,0.8416,1.0,1.0,5,0.9366,0.4116,no
AMDH_PETMO,A9BHL2,ESM2Text,Bacteria,338,"Catalyzes the reductive amination of 4-oxopentanoate to the chiral amine (4S)-4-aminopentanoate using ammonium as the amino donor. Shows an activity 10 times higher using NADH than NADPH as cosubstrate. May have a narrow substrate scope since it is much less active on 5- oxohexanoate and shows no activity on acetophenone, cyclohexanone, pentan-2-one or 2-aminopentan-2-one (Ref.2). Can also catalyze the reductive amination of (2R)-2-amino-4-oxopentanoate using ammonium as the amino donor (Ref.3).","Involved in the ornithine fermentation pathway. Catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((R)-DAP) to yield 2-amino-4-ketopentanoate (AKP). NAD(+) is the preferred substrate, but NADP(+) can also be used.",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0008839; GO:0000166,GO:0016491,GO:0016491,GO:0016639,GO:0016639,,0.4575,0.4575,0.3054,0.3054,,4,0.3815,0.2469,no
AMDH_PETMO,A9BHL2,Prot2Text,Bacteria,338,"Catalyzes the reductive amination of 4-oxopentanoate to the chiral amine (4S)-4-aminopentanoate using ammonium as the amino donor. Shows an activity 10 times higher using NADH than NADPH as cosubstrate. May have a narrow substrate scope since it is much less active on 5- oxohexanoate and shows no activity on acetophenone, cyclohexanone, pentan-2-one or 2-aminopentan-2-one (Ref.2). Can also catalyze the reductive amination of (2R)-2-amino-4-oxopentanoate using ammonium as the amino donor (Ref.3).",Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.,Maybe,Maybe,Maybe,No,No,not-Yes,GO:0008839; GO:0000166,GO:0008124,,GO:0008734,GO:0008734,GO:0016639,0.1679,,0.2021,0.2021,0.3054,4,0.2194,0.2469,no
AMDH_PETMO,A9BHL2,ProtT3,Bacteria,338,"Catalyzes the reductive amination of 4-oxopentanoate to the chiral amine (4S)-4-aminopentanoate using ammonium as the amino donor. Shows an activity 10 times higher using NADH than NADPH as cosubstrate. May have a narrow substrate scope since it is much less active on 5- oxohexanoate and shows no activity on acetophenone, cyclohexanone, pentan-2-one or 2-aminopentan-2-one (Ref.2). Can also catalyze the reductive amination of (2R)-2-amino-4-oxopentanoate using ammonium as the amino donor (Ref.3).",Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the NAD(+)-dependent oxidation of (R)-1-pyrroline-5-carboxylate (P5C) to 1-pyrroline-5-carboxylate semialdehyde (P5C-SA). Belongs to the pyrroline-5-carboxylate dehydrogenase family,No,Maybe,No,No,No,not-Yes,GO:0008839; GO:0000166,GO:0003842,GO:0003842,GO:0003842; GO:0070403,GO:0003842,GO:0003842,0.2604,0.2604,0.4714,0.2604,0.2604,5,0.3026,0.2469,no
AMDH_PETMO,A9BHL2,ProtTale,Bacteria,338,"Catalyzes the reductive amination of 4-oxopentanoate to the chiral amine (4S)-4-aminopentanoate using ammonium as the amino donor. Shows an activity 10 times higher using NADH than NADPH as cosubstrate. May have a narrow substrate scope since it is much less active on 5- oxohexanoate and shows no activity on acetophenone, cyclohexanone, pentan-2-one or 2-aminopentan-2-one (Ref.2). Can also catalyze the reductive amination of (2R)-2-amino-4-oxopentanoate using ammonium as the amino donor (Ref.3).",Catalyzes the NADPH-dependent reduction of D-erythrulose-1-phosphate to D-erythrulose.,No,No,No,Vague,No,not-Yes,GO:0008839; GO:0000166,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4575,0.4575,0.4575,0.4575,0.4575,5,0.4575,0.2469,no
AMDH_PETMO,A9BHL2,Protein2Text,Bacteria,338,"Catalyzes the reductive amination of 4-oxopentanoate to the chiral amine (4S)-4-aminopentanoate using ammonium as the amino donor. Shows an activity 10 times higher using NADH than NADPH as cosubstrate. May have a narrow substrate scope since it is much less active on 5- oxohexanoate and shows no activity on acetophenone, cyclohexanone, pentan-2-one or 2-aminopentan-2-one (Ref.2). Can also catalyze the reductive amination of (2R)-2-amino-4-oxopentanoate using ammonium as the amino donor (Ref.3).",The molecular function of the protein is an aminotransferase.,No,No,No,Maybe,Maybe,not-Yes,GO:0008839; GO:0000166,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.1965,0.1965,0.1965,0.1965,0.1965,5,0.1965,0.2469,no
AMDH_PETMO,A9BHL2,Reference,Bacteria,338,"Catalyzes the reductive amination of 4-oxopentanoate to the chiral amine (4S)-4-aminopentanoate using ammonium as the amino donor. Shows an activity 10 times higher using NADH than NADPH as cosubstrate. May have a narrow substrate scope since it is much less active on 5- oxohexanoate and shows no activity on acetophenone, cyclohexanone, pentan-2-one or 2-aminopentan-2-one (Ref.2). Can also catalyze the reductive amination of (2R)-2-amino-4-oxopentanoate using ammonium as the amino donor (Ref.3).","Catalyzes the reductive amination of 4-oxopentanoate to the chiral amine (4S)-4-aminopentanoate using ammonium as the amino donor. Shows an activity 10 times higher using NADH than NADPH as cosubstrate. May have a narrow substrate scope since it is much less active on 5- oxohexanoate and shows no activity on acetophenone, cyclohexanone, pentan-2-one or 2-aminopentan-2-one (Ref.2). Can also catalyze the reductive amination of (2R)-2-amino-4-oxopentanoate using ammonium as the amino donor (Ref.3).",,,,,,,GO:0008839; GO:0000166,GO:0016639,GO:0016491,GO:0016639,GO:0016491,GO:0016491,0.3054,0.4575,0.3054,0.4575,0.4575,5,0.3967,0.2469,no
SQASE_AGRFC,A9CEZ0,ESM2Text,Bacteria,664,"Part of the sulfoquinovose monooxygenase (sulfo-SMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite. Catalyzes the first step of the pathway, the hydrolysis of sulfoquinovosyl glycerol (SQGro) to release sulfoquinovose (SQ). Hydrolyzes both epimers of SQGro, with a preference for the natural 2'R isomer. In vitro, can use the substrate analog para- nitrophenyl alpha-sulfoquinovoside (PNPSQ), but shows no detectable activity toward 4-nitrophenyl alpha-D-glucopyranoside (PNPGlc).","Involved in the degradation of extracellular alpha-glucans. Catalyzes the hydrolysis of the non-reducing terminal alpha-1,4-glucosidic linkage of glucan back to alpha-1,6 position. It has high affinity for both alpha-1,3-glucosidic (alpha-1,6)-linked glucans and alpha-1,3,6-glucosidic (alpha-1,3,7)-linked glucans.",No,No,No,Maybe,No,not-Yes,GO:0030246; GO:0004553,GO:0004339,GO:0004553,GO:0004339,GO:0004339,GO:0090599,0.4933,0.727,0.4933,0.4933,0.5496,5,0.5513,0.3011,no
SQASE_AGRFC,A9CEZ0,Prot2Text,Bacteria,664,"Part of the sulfoquinovose monooxygenase (sulfo-SMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite. Catalyzes the first step of the pathway, the hydrolysis of sulfoquinovosyl glycerol (SQGro) to release sulfoquinovose (SQ). Hydrolyzes both epimers of SQGro, with a preference for the natural 2'R isomer. In vitro, can use the substrate analog para- nitrophenyl alpha-sulfoquinovoside (PNPSQ), but shows no detectable activity toward 4-nitrophenyl alpha-D-glucopyranoside (PNPGlc).","Alpha-galactosidase that specifically removes the alpha-1,4-linked galactose residue from galactose-6-phosphate (GalP6-P) to produce alpha-1,4-galactose-6-phosphate (GalP6-P). Also shows significant activity against galactosyl lactosides such as melibiose, raffinose and stachyose. Is not active against raffinose, locust bean gum and gum guar.",No,No,No,Maybe,No,not-Yes,GO:0030246; GO:0004553,GO:0004557,GO:0004557,GO:0004557,GO:0004557,GO:0004557,0.5496,0.5496,0.5496,0.5496,0.5496,5,0.5496,0.3011,no
SQASE_AGRFC,A9CEZ0,ProtT3,Bacteria,664,"Part of the sulfoquinovose monooxygenase (sulfo-SMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite. Catalyzes the first step of the pathway, the hydrolysis of sulfoquinovosyl glycerol (SQGro) to release sulfoquinovose (SQ). Hydrolyzes both epimers of SQGro, with a preference for the natural 2'R isomer. In vitro, can use the substrate analog para- nitrophenyl alpha-sulfoquinovoside (PNPSQ), but shows no detectable activity toward 4-nitrophenyl alpha-D-glucopyranoside (PNPGlc).",Catalyzes the hydrolysis of cellobiose to glucose and cellobiose 1-phosphate. Belongs to the glycosyl hydrolase 36 family,No,No,No,Maybe,No,not-Yes,GO:0030246; GO:0004553,GO:0008422,GO:0008422,GO:0008422,GO:0004553,GO:0016798,0.5496,0.5496,0.5496,0.727,0.6323,5,0.6016,0.3011,no
SQASE_AGRFC,A9CEZ0,ProtTale,Bacteria,664,"Part of the sulfoquinovose monooxygenase (sulfo-SMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite. Catalyzes the first step of the pathway, the hydrolysis of sulfoquinovosyl glycerol (SQGro) to release sulfoquinovose (SQ). Hydrolyzes both epimers of SQGro, with a preference for the natural 2'R isomer. In vitro, can use the substrate analog para- nitrophenyl alpha-sulfoquinovoside (PNPSQ), but shows no detectable activity toward 4-nitrophenyl alpha-D-glucopyranoside (PNPGlc).","Catalyzes the removal of terminal alpha-1,2-linked N-acetylglucosamine residues from the non-reducing ends of N-acetylglucosamine-containing molecules.",No,No,No,Maybe,No,not-Yes,GO:0030246; GO:0004553,GO:0016798,GO:0004553,GO:0004560,GO:0004560,GO:0004553,0.6323,0.727,0.5496,0.5496,0.727,5,0.6371,0.3011,no
SQASE_AGRFC,A9CEZ0,Protein2Text,Bacteria,664,"Part of the sulfoquinovose monooxygenase (sulfo-SMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite. Catalyzes the first step of the pathway, the hydrolysis of sulfoquinovosyl glycerol (SQGro) to release sulfoquinovose (SQ). Hydrolyzes both epimers of SQGro, with a preference for the natural 2'R isomer. In vitro, can use the substrate analog para- nitrophenyl alpha-sulfoquinovoside (PNPSQ), but shows no detectable activity toward 4-nitrophenyl alpha-D-glucopyranoside (PNPGlc).","This protein is a glycosidase, which means it breaks down complex carbohydrates into simpler sugars. More specifically, it is a maltase, which means it breaks down maltose into glucose.",No,No,No,Maybe,Maybe,not-Yes,GO:0030246; GO:0004553,GO:0004553,GO:0032450,GO:0004558,GO:0004558,GO:0004558,0.727,0.0,0.4933,0.4933,0.4933,5,0.4414,0.3011,no
SQASE_AGRFC,A9CEZ0,Reference,Bacteria,664,"Part of the sulfoquinovose monooxygenase (sulfo-SMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite. Catalyzes the first step of the pathway, the hydrolysis of sulfoquinovosyl glycerol (SQGro) to release sulfoquinovose (SQ). Hydrolyzes both epimers of SQGro, with a preference for the natural 2'R isomer. In vitro, can use the substrate analog para- nitrophenyl alpha-sulfoquinovoside (PNPSQ), but shows no detectable activity toward 4-nitrophenyl alpha-D-glucopyranoside (PNPGlc).","Part of the sulfoquinovose monooxygenase (sulfo-SMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite. Catalyzes the first step of the pathway, the hydrolysis of sulfoquinovosyl glycerol (SQGro) to release sulfoquinovose (SQ). Hydrolyzes both epimers of SQGro, with a preference for the natural 2'R isomer. In vitro, can use the substrate analog para- nitrophenyl alpha-sulfoquinovoside (PNPSQ), but shows no detectable activity toward 4-nitrophenyl alpha-D-glucopyranoside (PNPGlc).",,,,,,,GO:0030246; GO:0004553,GO:0016798,GO:0004553,GO:0004553,GO:0004553,GO:0004553,0.6323,0.727,0.727,0.727,0.727,5,0.7081,0.3011,no
MDAA_AGRFC,A9CJR8,ESM2Text,Bacteria,248,"N-deacetylase that specifically cleaves the acetyl group on the anhydromuropeptide chain termini (anhMurNAc residues) of peptidoglycan (PG), resulting in PG chains that terminate in deacetylated 1,6-anhydromuramic acid at the reducing end (anhMur residues).",Catalyzes the phosphorylation of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to form glycerol 1-phosphate (G1P). Involved in the control of morphogenesis.,No,No,No,No,No,not-Yes,GO:0016810,,GO:0016301,,,,,0.3284,,,,1,0.3284,0.4459,no
MDAA_AGRFC,A9CJR8,Prot2Text,Bacteria,248,"N-deacetylase that specifically cleaves the acetyl group on the anhydromuropeptide chain termini (anhMurNAc residues) of peptidoglycan (PG), resulting in PG chains that terminate in deacetylated 1,6-anhydromuramic acid at the reducing end (anhMur residues).",Catalyzes the deacetylation of N-acetylglucosamine (GlcNAc) residues in peptidoglycan.,Maybe,Yes,Maybe,Yes,Maybe,not-Yes,GO:0016810,GO:0016810,,GO:0016810,GO:0016810,GO:0016810,1.0,,1.0,1.0,1.0,4,1.0,0.4459,no
MDAA_AGRFC,A9CJR8,ProtT3,Bacteria,248,"N-deacetylase that specifically cleaves the acetyl group on the anhydromuropeptide chain termini (anhMurNAc residues) of peptidoglycan (PG), resulting in PG chains that terminate in deacetylated 1,6-anhydromuramic acid at the reducing end (anhMur residues).",Catalyzes the removal of N-acetylglucosamine (GlcNAc) residues from peptidoglycan. Cell outer membrane; Lipid-anchor. Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family,Maybe,Maybe,No,No,No,not-Yes,GO:0016810,GO:0004560,GO:0004563,GO:0008745,GO:0008745,GO:0008745,0.4275,0.4275,0.669,0.669,0.669,5,0.5724,0.4459,no
MDAA_AGRFC,A9CJR8,ProtTale,Bacteria,248,"N-deacetylase that specifically cleaves the acetyl group on the anhydromuropeptide chain termini (anhMurNAc residues) of peptidoglycan (PG), resulting in PG chains that terminate in deacetylated 1,6-anhydromuramic acid at the reducing end (anhMur residues).","Degrades chitin, a component of the fungal cell wall. Degrades both 4-O-methylchitobiose (4-O-methyl-beta-D-GlcNAc-(1-4)-alpha-D- GlcNAc) and 4-O-acetylchitobiose (4-O-acetyl-beta-D-GlcNAc-(1-4)-alpha-D-GlcNAc). Does not act on 4-O-methylchitotriose (4-O-methyl-beta-D-GlcNAc-(1-4)-alpha-D-",No,No,No,No,No,not-Yes,GO:0016810,GO:0004568,GO:0004568,GO:0004568,GO:0004568,GO:0004568,0.482,0.482,0.482,0.482,0.482,5,0.482,0.4459,no
MDAA_AGRFC,A9CJR8,Protein2Text,Bacteria,248,"N-deacetylase that specifically cleaves the acetyl group on the anhydromuropeptide chain termini (anhMurNAc residues) of peptidoglycan (PG), resulting in PG chains that terminate in deacetylated 1,6-anhydromuramic acid at the reducing end (anhMur residues).","This protein is involved in a process that is related to the inhibition of certain bacterial toxins, which is likely to be related to its molecular function. However, the exact molecular function of this protein is not specified. It is involved in the inhibition of the enzyme, diphthamide synthase, which is a key enzyme in the synthesis of diphthamide, a modified form of histidine that is essential for the function of the diphthamide-dependent protein toxins. Therefore, the molecular function of this protein is likely to be related to the inhibition of diphthamide synthase or the synthesis of diphthamide.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0016810,,,,,,,,,,,0,,0.4459,no
MDAA_AGRFC,A9CJR8,Reference,Bacteria,248,"N-deacetylase that specifically cleaves the acetyl group on the anhydromuropeptide chain termini (anhMurNAc residues) of peptidoglycan (PG), resulting in PG chains that terminate in deacetylated 1,6-anhydromuramic acid at the reducing end (anhMur residues).","N-deacetylase that specifically cleaves the acetyl group on the anhydromuropeptide chain termini (anhMurNAc residues) of peptidoglycan (PG), resulting in PG chains that terminate in deacetylated 1,6-anhydromuramic acid at the reducing end (anhMur residues).",,,,,,,GO:0016810,GO:0016811,GO:0016811,GO:0016787,GO:0016811,GO:0016811,0.8416,0.8416,0.8145,0.8416,0.8416,5,0.8362,0.4459,no
HASD_ASPFC,B0XWK8,ESM2Text,Eukaryota,2273,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of hexadehydro-astechrome (HAS), a tryptophan-derived iron(III)-complex that acts as a virulence factor in infected mice. Within the pathway, the NRPS condenses tryptophan and alanine to produce the Trp-Ala dipeptide. The 7-dimethylallyltryptophan synthase hasE then catalyzes the prenylation of the hasD-tethered tryptophan or the resulting tethered Trp-Ala dipeptide at the C-7 position of the indole moiety. HAS biosynthesis continues via tethered intermediates with the succesive actions of the cytochrome P450 monooxygenase hasH, the O- methyltransferase hasC, and the FAD-linked oxidoreductase hasG. The resulting O-methylated diketopiperazine is then released from hasD. Finally, three O-methylated diketopiperazine molecules assemble in a trimeric complex with Fe(III) to produce hexadehydro-astechrome.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcs",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,,,,,,,,,,,0,,0.2644,no
HASD_ASPFC,B0XWK8,Prot2Text,Eukaryota,2273,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of hexadehydro-astechrome (HAS), a tryptophan-derived iron(III)-complex that acts as a virulence factor in infected mice. Within the pathway, the NRPS condenses tryptophan and alanine to produce the Trp-Ala dipeptide. The 7-dimethylallyltryptophan synthase hasE then catalyzes the prenylation of the hasD-tethered tryptophan or the resulting tethered Trp-Ala dipeptide at the C-7 position of the indole moiety. HAS biosynthesis continues via tethered intermediates with the succesive actions of the cytochrome P450 monooxygenase hasH, the O- methyltransferase hasC, and the FAD-linked oxidoreductase hasG. The resulting O-methylated diketopiperazine is then released from hasD. Finally, three O-methylated diketopiperazine molecules assemble in a trimeric complex with Fe(III) to produce hexadehydro-astechrome.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the glycolipid biosurfactant ustilagic acid (UA). UA is a secreted cellobiose glycolipid that is toxic for many microorganisms and confers biocontrol activity to U.maydis. UA consists of 15,16-dihydroxypalmitic or 2,15,16-trihydroxypalmitic acid, which is O-glycosidically linked to cellobiose at its terminal hydroxyl group. In addition, the cellobiose moiety is acetylated and acylated with a short-chain hydroxy fatty acid. UA biosynthesis starts with omega-hydroxylation of palmitic acid catalyzed by the cytochrome P450 monooxygenase cyp1. Terminal hydroxylation of palmitic acid precedes subterminal hydroxylation catalyzed by the cytochrome P450 monooxygenase cyp2. Sequential glucosylation of the hydroxy fatty acid is probably catalyzed by the glycosyltransferase ugt1 (Probable). The cellobiose lipid",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,GO:0016874,,,GO:0016874,GO:0016874; GO:0005524,0.709,,,0.709,0.6793,3,0.6991,0.2644,no
HASD_ASPFC,B0XWK8,ProtT3,Eukaryota,2273,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of hexadehydro-astechrome (HAS), a tryptophan-derived iron(III)-complex that acts as a virulence factor in infected mice. Within the pathway, the NRPS condenses tryptophan and alanine to produce the Trp-Ala dipeptide. The 7-dimethylallyltryptophan synthase hasE then catalyzes the prenylation of the hasD-tethered tryptophan or the resulting tethered Trp-Ala dipeptide at the C-7 position of the indole moiety. HAS biosynthesis continues via tethered intermediates with the succesive actions of the cytochrome P450 monooxygenase hasH, the O- methyltransferase hasC, and the FAD-linked oxidoreductase hasG. The resulting O-methylated diketopiperazine is then released from hasD. Finally, three O-methylated diketopiperazine molecules assemble in a trimeric complex with Fe(III) to produce hexadehydro-astechrome.",Nonribosomal peptide synthetase (NRPS); part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,GO:0016874; GO:0005524,GO:0016874,,GO:0016874; GO:0031177,GO:0016874; GO:0005524,0.6793,0.709,,1.0,0.6793,4,0.7669,0.2644,no
HASD_ASPFC,B0XWK8,ProtTale,Eukaryota,2273,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of hexadehydro-astechrome (HAS), a tryptophan-derived iron(III)-complex that acts as a virulence factor in infected mice. Within the pathway, the NRPS condenses tryptophan and alanine to produce the Trp-Ala dipeptide. The 7-dimethylallyltryptophan synthase hasE then catalyzes the prenylation of the hasD-tethered tryptophan or the resulting tethered Trp-Ala dipeptide at the C-7 position of the indole moiety. HAS biosynthesis continues via tethered intermediates with the succesive actions of the cytochrome P450 monooxygenase hasH, the O- methyltransferase hasC, and the FAD-linked oxidoreductase hasG. The resulting O-methylated diketopiperazine is then released from hasD. Finally, three O-methylated diketopiperazine molecules assemble in a trimeric complex with Fe(III) to produce hexadehydro-astechrome.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS). SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms. These initial steps feature the priming of an unusual benzoic acid starter unit onto",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,GO:0016491,GO:0016874,,,GO:0016874,0.4358,0.709,,,0.709,3,0.6179,0.2644,no
HASD_ASPFC,B0XWK8,Protein2Text,Eukaryota,2273,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of hexadehydro-astechrome (HAS), a tryptophan-derived iron(III)-complex that acts as a virulence factor in infected mice. Within the pathway, the NRPS condenses tryptophan and alanine to produce the Trp-Ala dipeptide. The 7-dimethylallyltryptophan synthase hasE then catalyzes the prenylation of the hasD-tethered tryptophan or the resulting tethered Trp-Ala dipeptide at the C-7 position of the indole moiety. HAS biosynthesis continues via tethered intermediates with the succesive actions of the cytochrome P450 monooxygenase hasH, the O- methyltransferase hasC, and the FAD-linked oxidoreductase hasG. The resulting O-methylated diketopiperazine is then released from hasD. Finally, three O-methylated diketopiperazine molecules assemble in a trimeric complex with Fe(III) to produce hexadehydro-astechrome.","The molecular function of this protein is involved in the synthesis of a type of fatty acid, specifically a polyketide chain. Polyketides are a diverse group of compounds that have a wide range of biological activities, including antibiotic, antifungal, and anticancer properties. This protein is likely involved in the synthesis of a specific polyketide chain, which is then modified by other enzymes to produce a final product with a specific biological activity.",No,No,No,No,No,not-Yes,GO:0016874; GO:0031177,,GO:0016746,,GO:0016746,,,0.3561,,0.3561,,2,0.3561,0.2644,no
HASD_ASPFC,B0XWK8,Reference,Eukaryota,2273,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of hexadehydro-astechrome (HAS), a tryptophan-derived iron(III)-complex that acts as a virulence factor in infected mice. Within the pathway, the NRPS condenses tryptophan and alanine to produce the Trp-Ala dipeptide. The 7-dimethylallyltryptophan synthase hasE then catalyzes the prenylation of the hasD-tethered tryptophan or the resulting tethered Trp-Ala dipeptide at the C-7 position of the indole moiety. HAS biosynthesis continues via tethered intermediates with the succesive actions of the cytochrome P450 monooxygenase hasH, the O- methyltransferase hasC, and the FAD-linked oxidoreductase hasG. The resulting O-methylated diketopiperazine is then released from hasD. Finally, three O-methylated diketopiperazine molecules assemble in a trimeric complex with Fe(III) to produce hexadehydro-astechrome.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of hexadehydro-astechrome (HAS), a tryptophan-derived iron(III)-complex that acts as a virulence factor in infected mice. Within the pathway, the NRPS condenses tryptophan and alanine to produce the Trp-Ala dipeptide. The 7-dimethylallyltryptophan synthase hasE then catalyzes the prenylation of the hasD-tethered tryptophan or the resulting tethered Trp-Ala dipeptide at the C-7 position of the indole moiety. HAS biosynthesis continues via tethered intermediates with the succesive actions of the cytochrome P450 monooxygenase hasH, the O- methyltransferase hasC, and the FAD-linked oxidoreductase hasG. The resulting O-methylated diketopiperazine is then released from hasD. Finally, three O-methylated diketopiperazine molecules assemble in a trimeric complex with Fe(III) to produce hexadehydro-astechrome.",,,,,,,GO:0016874; GO:0031177,GO:0016874,GO:0016874,GO:0016874,GO:0016874,GO:0016874,0.709,0.709,0.709,0.709,0.709,5,0.709,0.2644,no
SPHB_ASPFC,B0XZV6,ESM2Text,Eukaryota,2514,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of sphingofungins, bioactive molecules acting as sphingolipid inhibitors via inhibiting serine palmitoyl transferase (SPT). Within the pathway, sphB catalyzes the first step of sphingofungin biosynthesis by condensing 8 units of malonyl-CoA with one starter unit of acetyl-CoA, leading to an C18 polyketide precursor 3-hydroxyoctadeca-4,10-dienoyl-ACP containing one delta-6 desaturation and one delta-12 desaturation. The PKS sphB does not contain any putative thioesterase domain for releasing the nascent polyketide chain and it has been suggested that aminoacyl transferases can facilitate the polyketide chain release. The aminoacyl transferase sphA uses the sphB product to produce 3-keto- presphingofungin by adding an aminomalonate molecule. SphF then reduces the C-3 ketone of 3-keto-presphingofungin which leads to presphingofungin. The cytochrome P450 monooxygenase sphH converts presphingofungin into sphingofungin B1 which is further converted to sphingofungin B by the dioxygenase sphC. SphC is also able to convert presphingofungin into sphingofungin B2. The acetyltransferase sphE acetylates sphingofungin B to produce sphingofungin C, but can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Finally, sphingofungin C can be spontaneously converted into sphingofungin D.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential tr",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177,,,,,,,,,,,0,,0.2403,no
SPHB_ASPFC,B0XZV6,Prot2Text,Eukaryota,2514,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of sphingofungins, bioactive molecules acting as sphingolipid inhibitors via inhibiting serine palmitoyl transferase (SPT). Within the pathway, sphB catalyzes the first step of sphingofungin biosynthesis by condensing 8 units of malonyl-CoA with one starter unit of acetyl-CoA, leading to an C18 polyketide precursor 3-hydroxyoctadeca-4,10-dienoyl-ACP containing one delta-6 desaturation and one delta-12 desaturation. The PKS sphB does not contain any putative thioesterase domain for releasing the nascent polyketide chain and it has been suggested that aminoacyl transferases can facilitate the polyketide chain release. The aminoacyl transferase sphA uses the sphB product to produce 3-keto- presphingofungin by adding an aminomalonate molecule. SphF then reduces the C-3 ketone of 3-keto-presphingofungin which leads to presphingofungin. The cytochrome P450 monooxygenase sphH converts presphingofungin into sphingofungin B1 which is further converted to sphingofungin B by the dioxygenase sphC. SphC is also able to convert presphingofungin into sphingofungin B2. The acetyltransferase sphE acetylates sphingofungin B to produce sphingofungin C, but can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Finally, sphingofungin C can be spontaneously converted into sphingofungin D.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177,GO:0016747,,,GO:0016747,GO:0016746,0.536,,,0.536,0.5204,3,0.5308,0.2403,no
SPHB_ASPFC,B0XZV6,ProtT3,Eukaryota,2514,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of sphingofungins, bioactive molecules acting as sphingolipid inhibitors via inhibiting serine palmitoyl transferase (SPT). Within the pathway, sphB catalyzes the first step of sphingofungin biosynthesis by condensing 8 units of malonyl-CoA with one starter unit of acetyl-CoA, leading to an C18 polyketide precursor 3-hydroxyoctadeca-4,10-dienoyl-ACP containing one delta-6 desaturation and one delta-12 desaturation. The PKS sphB does not contain any putative thioesterase domain for releasing the nascent polyketide chain and it has been suggested that aminoacyl transferases can facilitate the polyketide chain release. The aminoacyl transferase sphA uses the sphB product to produce 3-keto- presphingofungin by adding an aminomalonate molecule. SphF then reduces the C-3 ketone of 3-keto-presphingofungin which leads to presphingofungin. The cytochrome P450 monooxygenase sphH converts presphingofungin into sphingofungin B1 which is further converted to sphingofungin B by the dioxygenase sphC. SphC is also able to convert presphingofungin into sphingofungin B2. The acetyltransferase sphE acetylates sphingofungin B to produce sphingofungin C, but can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Finally, sphingofungin C can be spontaneously converted into sphingofungin D.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177,GO:0016746,GO:0016746,,GO:0016746,GO:0016747,0.5204,0.5204,,0.5204,0.536,4,0.5243,0.2403,no
SPHB_ASPFC,B0XZV6,ProtTale,Eukaryota,2514,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of sphingofungins, bioactive molecules acting as sphingolipid inhibitors via inhibiting serine palmitoyl transferase (SPT). Within the pathway, sphB catalyzes the first step of sphingofungin biosynthesis by condensing 8 units of malonyl-CoA with one starter unit of acetyl-CoA, leading to an C18 polyketide precursor 3-hydroxyoctadeca-4,10-dienoyl-ACP containing one delta-6 desaturation and one delta-12 desaturation. The PKS sphB does not contain any putative thioesterase domain for releasing the nascent polyketide chain and it has been suggested that aminoacyl transferases can facilitate the polyketide chain release. The aminoacyl transferase sphA uses the sphB product to produce 3-keto- presphingofungin by adding an aminomalonate molecule. SphF then reduces the C-3 ketone of 3-keto-presphingofungin which leads to presphingofungin. The cytochrome P450 monooxygenase sphH converts presphingofungin into sphingofungin B1 which is further converted to sphingofungin B by the dioxygenase sphC. SphC is also able to convert presphingofungin into sphingofungin B2. The acetyltransferase sphE acetylates sphingofungin B to produce sphingofungin C, but can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Finally, sphingofungin C can be spontaneously converted into sphingofungin D.","Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. Within the pathway, ptmC is responsible for the cyclization of prepenitrem F to penitrem B. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3-glycerol phosphate with GGPP by ptmC then forms 3-",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177,GO:0016491,GO:0016757,,,GO:0016746,0.5779,0.4365,,,0.5204,3,0.5116,0.2403,no
SPHB_ASPFC,B0XZV6,Protein2Text,Eukaryota,2514,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of sphingofungins, bioactive molecules acting as sphingolipid inhibitors via inhibiting serine palmitoyl transferase (SPT). Within the pathway, sphB catalyzes the first step of sphingofungin biosynthesis by condensing 8 units of malonyl-CoA with one starter unit of acetyl-CoA, leading to an C18 polyketide precursor 3-hydroxyoctadeca-4,10-dienoyl-ACP containing one delta-6 desaturation and one delta-12 desaturation. The PKS sphB does not contain any putative thioesterase domain for releasing the nascent polyketide chain and it has been suggested that aminoacyl transferases can facilitate the polyketide chain release. The aminoacyl transferase sphA uses the sphB product to produce 3-keto- presphingofungin by adding an aminomalonate molecule. SphF then reduces the C-3 ketone of 3-keto-presphingofungin which leads to presphingofungin. The cytochrome P450 monooxygenase sphH converts presphingofungin into sphingofungin B1 which is further converted to sphingofungin B by the dioxygenase sphC. SphC is also able to convert presphingofungin into sphingofungin B2. The acetyltransferase sphE acetylates sphingofungin B to produce sphingofungin C, but can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Finally, sphingofungin C can be spontaneously converted into sphingofungin D.","The molecular function of this protein is an acyl carrier protein (ACP), which is a component of the fatty acid synthase complex. It is involved in the synthesis of fatty acids by transferring acyl groups from one enzyme to another within the complex. Specifically, it is involved in the elongation of fatty acids by transferring an acyl group from malonyl-ACP to the growing acyl chain on the ACP. This process is crucial for the production of fatty acids, which are essential components of various cellular structures and molecules.",No,No,Maybe,Maybe,No,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177,GO:0000036,GO:0000036,GO:0000036,GO:0000036,GO:0000036,0.1487,0.1487,0.1487,0.1487,0.1487,5,0.1487,0.2403,no
SPHB_ASPFC,B0XZV6,Reference,Eukaryota,2514,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of sphingofungins, bioactive molecules acting as sphingolipid inhibitors via inhibiting serine palmitoyl transferase (SPT). Within the pathway, sphB catalyzes the first step of sphingofungin biosynthesis by condensing 8 units of malonyl-CoA with one starter unit of acetyl-CoA, leading to an C18 polyketide precursor 3-hydroxyoctadeca-4,10-dienoyl-ACP containing one delta-6 desaturation and one delta-12 desaturation. The PKS sphB does not contain any putative thioesterase domain for releasing the nascent polyketide chain and it has been suggested that aminoacyl transferases can facilitate the polyketide chain release. The aminoacyl transferase sphA uses the sphB product to produce 3-keto- presphingofungin by adding an aminomalonate molecule. SphF then reduces the C-3 ketone of 3-keto-presphingofungin which leads to presphingofungin. The cytochrome P450 monooxygenase sphH converts presphingofungin into sphingofungin B1 which is further converted to sphingofungin B by the dioxygenase sphC. SphC is also able to convert presphingofungin into sphingofungin B2. The acetyltransferase sphE acetylates sphingofungin B to produce sphingofungin C, but can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Finally, sphingofungin C can be spontaneously converted into sphingofungin D.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of sphingofungins, bioactive molecules acting as sphingolipid inhibitors via inhibiting serine palmitoyl transferase (SPT). Within the pathway, sphB catalyzes the first step of sphingofungin biosynthesis by condensing 8 units of malonyl-CoA with one starter unit of acetyl-CoA, leading to an C18 polyketide precursor 3-hydroxyoctadeca-4,10-dienoyl-ACP containing one delta-6 desaturation and one delta-12 desaturation. The PKS sphB does not contain any putative thioesterase domain for releasing the nascent polyketide chain and it has been suggested that aminoacyl transferases can facilitate the polyketide chain release. The aminoacyl transferase sphA uses the sphB product to produce 3-keto- presphingofungin by adding an aminomalonate molecule. SphF then reduces the C-3 ketone of 3-keto-presphingofungin which leads to presphingofungin. The cytochrome P450 monooxygenase sphH converts presphingofungin into sphingofungin B1 which is further converted to sphingofungin B by the dioxygenase sphC. SphC is also able to convert presphingofungin into sphingofungin B2. The acetyltransferase sphE acetylates sphingofungin B to produce sphingofungin C, but can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Finally, sphingofungin C can be spontaneously converted into sphingofungin D.",,,,,,,GO:0004312; GO:0008168; GO:0016491; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.5204,0.5204,0.5204,0.536,0.5204,5,0.5235,0.2403,no
ARDA_SHEWM,B1KN79,ESM2Text,Bacteria,506,"FAD-containing subunit of the ArdAB flavocytochrome c, which catalyzes the reduction of acrylate to propanoate and supports dimethylsulfoniopropionate-dependent anaerobic respiration. In vitro, can use the artificial electron donor methyl viologen. The natural electron donor is probably a low-potential cytochrome c. Also shows weak activity toward methacrylate in vitro (at a 22-fold lower rate) but cannot use other tested 2-enoates, including crotonic, fumaric, sorbic, urocanic, cinnamic, p-coumaric, caffeic or ferulic acids. The protein catalyzes a unidirectional reaction and cannot oxidize propanoate with phenazine metasulfate and dichlorophenolindophenol as electron acceptors.","Catalyzes the elimination of ammonia from the C1-C2 hydrogen bond of dihydroxyacetonephosphate (DHAP or glycerone-phosphate) to yield glycerol-3-phosphate (G3P). It uses the same electron acceptor than the major cholesterol-synthesizing enzyme. The G3P produced by DhaS is then refixed by a specialized chloride-bond-type oxidoreductase to form the dihydroxyacetone phosphate polymer, the final enzymatic product of cholesterol boronate elimination.",No,No,No,No,No,not-Yes,GO:0010181; GO:0016491,,,,,,,,,,,0,,0.2625,no
ARDA_SHEWM,B1KN79,Prot2Text,Bacteria,506,"FAD-containing subunit of the ArdAB flavocytochrome c, which catalyzes the reduction of acrylate to propanoate and supports dimethylsulfoniopropionate-dependent anaerobic respiration. In vitro, can use the artificial electron donor methyl viologen. The natural electron donor is probably a low-potential cytochrome c. Also shows weak activity toward methacrylate in vitro (at a 22-fold lower rate) but cannot use other tested 2-enoates, including crotonic, fumaric, sorbic, urocanic, cinnamic, p-coumaric, caffeic or ferulic acids. The protein catalyzes a unidirectional reaction and cannot oxidize propanoate with phenazine metasulfate and dichlorophenolindophenol as electron acceptors.",Catalyzes the coenzyme F420-dependent oxidation of glucose 6-phosphate (G6P) to 6-phosphogluconolactone. Also catalyzes the oxidation of D-gluconate but not L-gulose 6-phosphate. Coenzyme F420-dependent G6P oxidation is coupled to energy-yielding reactions.,No,No,No,No,No,not-Yes,GO:0010181; GO:0016491,GO:0004345,,GO:0004345,GO:0004345,GO:0016614,0.4243,,0.4243,0.4243,0.574,4,0.4617,0.2625,no
ARDA_SHEWM,B1KN79,ProtT3,Bacteria,506,"FAD-containing subunit of the ArdAB flavocytochrome c, which catalyzes the reduction of acrylate to propanoate and supports dimethylsulfoniopropionate-dependent anaerobic respiration. In vitro, can use the artificial electron donor methyl viologen. The natural electron donor is probably a low-potential cytochrome c. Also shows weak activity toward methacrylate in vitro (at a 22-fold lower rate) but cannot use other tested 2-enoates, including crotonic, fumaric, sorbic, urocanic, cinnamic, p-coumaric, caffeic or ferulic acids. The protein catalyzes a unidirectional reaction and cannot oxidize propanoate with phenazine metasulfate and dichlorophenolindophenol as electron acceptors.",Catalyzes the reduction of fumarate to L-malate. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0010181; GO:0016491,GO:0000104,GO:0000104,GO:0000104,GO:0016627,GO:0000104,0.4862,0.4862,0.4862,0.574,0.4862,5,0.5038,0.2625,no
ARDA_SHEWM,B1KN79,ProtTale,Bacteria,506,"FAD-containing subunit of the ArdAB flavocytochrome c, which catalyzes the reduction of acrylate to propanoate and supports dimethylsulfoniopropionate-dependent anaerobic respiration. In vitro, can use the artificial electron donor methyl viologen. The natural electron donor is probably a low-potential cytochrome c. Also shows weak activity toward methacrylate in vitro (at a 22-fold lower rate) but cannot use other tested 2-enoates, including crotonic, fumaric, sorbic, urocanic, cinnamic, p-coumaric, caffeic or ferulic acids. The protein catalyzes a unidirectional reaction and cannot oxidize propanoate with phenazine metasulfate and dichlorophenolindophenol as electron acceptors.",Catalyzes the two-electron reduction of protoporphyrinogen IX to coproporphyrin III under the reduction of NAD(P)+.,No,No,No,No,No,not-Yes,GO:0010181; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.7038,0.7038,0.7038,0.7038,0.7038,5,0.7038,0.2625,no
ARDA_SHEWM,B1KN79,Protein2Text,Bacteria,506,"FAD-containing subunit of the ArdAB flavocytochrome c, which catalyzes the reduction of acrylate to propanoate and supports dimethylsulfoniopropionate-dependent anaerobic respiration. In vitro, can use the artificial electron donor methyl viologen. The natural electron donor is probably a low-potential cytochrome c. Also shows weak activity toward methacrylate in vitro (at a 22-fold lower rate) but cannot use other tested 2-enoates, including crotonic, fumaric, sorbic, urocanic, cinnamic, p-coumaric, caffeic or ferulic acids. The protein catalyzes a unidirectional reaction and cannot oxidize propanoate with phenazine metasulfate and dichlorophenolindophenol as electron acceptors.","The molecular function of this protein is an oxidoreductase, specifically a type of enzyme that catalyzes the oxidation of methanol to formaldehyde.",No,No,No,No,No,not-Yes,GO:0010181; GO:0016491,GO:0016614,GO:0004030,GO:0016491,GO:0016491,GO:0004030,0.574,0.4243,0.7038,0.7038,0.4243,5,0.566,0.2625,no
ARDA_SHEWM,B1KN79,Reference,Bacteria,506,"FAD-containing subunit of the ArdAB flavocytochrome c, which catalyzes the reduction of acrylate to propanoate and supports dimethylsulfoniopropionate-dependent anaerobic respiration. In vitro, can use the artificial electron donor methyl viologen. The natural electron donor is probably a low-potential cytochrome c. Also shows weak activity toward methacrylate in vitro (at a 22-fold lower rate) but cannot use other tested 2-enoates, including crotonic, fumaric, sorbic, urocanic, cinnamic, p-coumaric, caffeic or ferulic acids. The protein catalyzes a unidirectional reaction and cannot oxidize propanoate with phenazine metasulfate and dichlorophenolindophenol as electron acceptors.","FAD-containing subunit of the ArdAB flavocytochrome c, which catalyzes the reduction of acrylate to propanoate and supports dimethylsulfoniopropionate-dependent anaerobic respiration. In vitro, can use the artificial electron donor methyl viologen. The natural electron donor is probably a low-potential cytochrome c. Also shows weak activity toward methacrylate in vitro (at a 22-fold lower rate) but cannot use other tested 2-enoates, including crotonic, fumaric, sorbic, urocanic, cinnamic, p-coumaric, caffeic or ferulic acids. The protein catalyzes a unidirectional reaction and cannot oxidize propanoate with phenazine metasulfate and dichlorophenolindophenol as electron acceptors.",,,,,,,GO:0010181; GO:0016491,GO:0016491; GO:0050660,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.867,0.7038,0.7038,0.7038,0.7038,5,0.7364,0.2625,no
ARDB_SHEWM,B1KN80,ESM2Text,Bacteria,117,"Heme c-containing subunit of the ArdAB flavocytochrome c, which catalyzes the reduction of acrylate to propanoate and supports dimethylsulfoniopropionate-dependent anaerobic respiration. In vitro, can use the artificial electron donor methyl viologen. The natural electron donor is probably a low-potential cytochrome c. Also shows weak activity toward methacrylate in vitro (at a 22-fold lower rate) but cannot use other tested 2-enoates, including crotonic, fumaric, sorbic, urocanic, cinnamic, p-coumaric, caffeic or ferulic acids. The protein catalyzes a unidirectional reaction and cannot oxidize propanoate with phenazine metasulfate and dichlorophenolindophenol as electron acceptors.",Specific electron transfer protein for Fe(3+) and Fe(2+) oxide reductases.,No,Maybe,Maybe,Maybe,No,not-Yes,GO:0046872; GO:0016491,GO:0009055,GO:0009055,GO:0009055,GO:0009055,GO:0009055,0.2949,0.2949,0.2949,0.2949,0.2949,5,0.2949,0.4173,no
ARDB_SHEWM,B1KN80,Prot2Text,Bacteria,117,"Heme c-containing subunit of the ArdAB flavocytochrome c, which catalyzes the reduction of acrylate to propanoate and supports dimethylsulfoniopropionate-dependent anaerobic respiration. In vitro, can use the artificial electron donor methyl viologen. The natural electron donor is probably a low-potential cytochrome c. Also shows weak activity toward methacrylate in vitro (at a 22-fold lower rate) but cannot use other tested 2-enoates, including crotonic, fumaric, sorbic, urocanic, cinnamic, p-coumaric, caffeic or ferulic acids. The protein catalyzes a unidirectional reaction and cannot oxidize propanoate with phenazine metasulfate and dichlorophenolindophenol as electron acceptors.",Required for nitrite assimilation. Has menaquinol-oxidizing activity.,No,No,No,No,No,not-Yes,GO:0046872; GO:0016491,GO:0016491,,GO:0016491,GO:0016491,GO:0016491,0.7193,,0.7193,0.7193,0.7193,4,0.7193,0.4173,no
ARDB_SHEWM,B1KN80,ProtT3,Bacteria,117,"Heme c-containing subunit of the ArdAB flavocytochrome c, which catalyzes the reduction of acrylate to propanoate and supports dimethylsulfoniopropionate-dependent anaerobic respiration. In vitro, can use the artificial electron donor methyl viologen. The natural electron donor is probably a low-potential cytochrome c. Also shows weak activity toward methacrylate in vitro (at a 22-fold lower rate) but cannot use other tested 2-enoates, including crotonic, fumaric, sorbic, urocanic, cinnamic, p-coumaric, caffeic or ferulic acids. The protein catalyzes a unidirectional reaction and cannot oxidize propanoate with phenazine metasulfate and dichlorophenolindophenol as electron acceptors.",Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Periplasm,No,No,No,No,No,not-Yes,GO:0046872; GO:0016491,GO:0016159,GO:0016002,GO:0016002,GO:0016491,GO:0050311,0.2664,0.4947,0.4947,0.7193,0.4309,5,0.4812,0.4173,no
ARDB_SHEWM,B1KN80,ProtTale,Bacteria,117,"Heme c-containing subunit of the ArdAB flavocytochrome c, which catalyzes the reduction of acrylate to propanoate and supports dimethylsulfoniopropionate-dependent anaerobic respiration. In vitro, can use the artificial electron donor methyl viologen. The natural electron donor is probably a low-potential cytochrome c. Also shows weak activity toward methacrylate in vitro (at a 22-fold lower rate) but cannot use other tested 2-enoates, including crotonic, fumaric, sorbic, urocanic, cinnamic, p-coumaric, caffeic or ferulic acids. The protein catalyzes a unidirectional reaction and cannot oxidize propanoate with phenazine metasulfate and dichlorophenolindophenol as electron acceptors.",Plays a role in the reduction of nitrite to nitric oxide (NO).,No,No,No,Vague,No,not-Yes,GO:0046872; GO:0016491,GO:0050421,GO:0016491,GO:0050421,GO:0016491,GO:0050421,0.3817,0.7193,0.3817,0.7193,0.3817,5,0.5167,0.4173,no
ARDB_SHEWM,B1KN80,Protein2Text,Bacteria,117,"Heme c-containing subunit of the ArdAB flavocytochrome c, which catalyzes the reduction of acrylate to propanoate and supports dimethylsulfoniopropionate-dependent anaerobic respiration. In vitro, can use the artificial electron donor methyl viologen. The natural electron donor is probably a low-potential cytochrome c. Also shows weak activity toward methacrylate in vitro (at a 22-fold lower rate) but cannot use other tested 2-enoates, including crotonic, fumaric, sorbic, urocanic, cinnamic, p-coumaric, caffeic or ferulic acids. The protein catalyzes a unidirectional reaction and cannot oxidize propanoate with phenazine metasulfate and dichlorophenolindophenol as electron acceptors.","The molecular function of this protein is not explicitly stated in the provided information. However, based on the context, it can be inferred that this protein is involved in binding or interacting with other molecules, possibly in a redox or electron transfer reaction. The name ""cytochrome"" suggests a role in electron transport or oxidative processes, but the specific function is not specified.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0046872; GO:0016491,,,,,,,,,,,0,,0.4173,no
ARDB_SHEWM,B1KN80,Reference,Bacteria,117,"Heme c-containing subunit of the ArdAB flavocytochrome c, which catalyzes the reduction of acrylate to propanoate and supports dimethylsulfoniopropionate-dependent anaerobic respiration. In vitro, can use the artificial electron donor methyl viologen. The natural electron donor is probably a low-potential cytochrome c. Also shows weak activity toward methacrylate in vitro (at a 22-fold lower rate) but cannot use other tested 2-enoates, including crotonic, fumaric, sorbic, urocanic, cinnamic, p-coumaric, caffeic or ferulic acids. The protein catalyzes a unidirectional reaction and cannot oxidize propanoate with phenazine metasulfate and dichlorophenolindophenol as electron acceptors.","Heme c-containing subunit of the ArdAB flavocytochrome c, which catalyzes the reduction of acrylate to propanoate and supports dimethylsulfoniopropionate-dependent anaerobic respiration. In vitro, can use the artificial electron donor methyl viologen. The natural electron donor is probably a low-potential cytochrome c. Also shows weak activity toward methacrylate in vitro (at a 22-fold lower rate) but cannot use other tested 2-enoates, including crotonic, fumaric, sorbic, urocanic, cinnamic, p-coumaric, caffeic or ferulic acids. The protein catalyzes a unidirectional reaction and cannot oxidize propanoate with phenazine metasulfate and dichlorophenolindophenol as electron acceptors.",,,,,,,GO:0046872; GO:0016491,GO:0016491; GO:0020037,GO:0009055,GO:0016491; GO:0020037,GO:0016491; GO:0009055; GO:0020037,GO:0009055,0.6422,0.2949,0.6422,0.5817,0.2949,5,0.4912,0.4173,no
PBP_MYCA9,B1MDC3,ESM2Text,Bacteria,605,Transpeptidase that catalyzes cross-linking of the peptidoglycan cell wall. Required for normal cell elongation and division. Required for adequate localization of FtsZ. Involved in resistance to antibiotics including beta-lactams.,Cell wall formation. Synthesized in the presence of pectin.,Maybe,Vague,Vague,Vague,Maybe,not-Yes,GO:0008658; GO:0071972,,,,,,,,,,,0,,0.5018,no
PBP_MYCA9,B1MDC3,Prot2Text,Bacteria,605,Transpeptidase that catalyzes cross-linking of the peptidoglycan cell wall. Required for normal cell elongation and division. Required for adequate localization of FtsZ. Involved in resistance to antibiotics including beta-lactams.,"Penicillin-binding protein with a narrow substrate specificity. Can only partially substitute for PBP-2B (or PBP-1C) in cell division, and penicillin-binding protein (PB) is almost inactive. Displays potent endoprotease activity against cephalosporins such as cefotaxime and ceftazidime, suggesting that PH is a common target for these antibiotics.",Maybe,Yes,Maybe,Yes,Maybe,not-Yes,GO:0008658; GO:0071972,GO:0008658,,GO:0008658,GO:0008658,GO:0008233,0.6847,,0.6847,0.6847,0.3907,4,0.6112,0.5018,no
PBP_MYCA9,B1MDC3,ProtT3,Bacteria,605,Transpeptidase that catalyzes cross-linking of the peptidoglycan cell wall. Required for normal cell elongation and division. Required for adequate localization of FtsZ. Involved in resistance to antibiotics including beta-lactams.,Cell membrane; Single-pass membrane protein. Belongs to the transpeptidase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008658; GO:0071972,GO:0008955,GO:0016755,GO:0008658,GO:0009002,GO:0008233,0.1083,0.1276,0.6847,0.5745,0.3907,5,0.3772,0.5018,no
PBP_MYCA9,B1MDC3,ProtTale,Bacteria,605,Transpeptidase that catalyzes cross-linking of the peptidoglycan cell wall. Required for normal cell elongation and division. Required for adequate localization of FtsZ. Involved in resistance to antibiotics including beta-lactams.,Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits).,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0008658; GO:0071972,GO:0008955; GO:0008658,GO:0008955; GO:0008658,GO:0008955,GO:0008955; GO:0008233,GO:0008955; GO:0008658,0.5621,0.5621,0.1083,0.324,0.5621,5,0.4237,0.5018,no
PBP_MYCA9,B1MDC3,Protein2Text,Bacteria,605,Transpeptidase that catalyzes cross-linking of the peptidoglycan cell wall. Required for normal cell elongation and division. Required for adequate localization of FtsZ. Involved in resistance to antibiotics including beta-lactams.,This protein is an acetyltransferase.,No,No,No,No,No,not-Yes,GO:0008658; GO:0071972,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.1083,0.1083,0.1083,0.1083,0.1083,5,0.1083,0.5018,no
PBP_MYCA9,B1MDC3,Reference,Bacteria,605,Transpeptidase that catalyzes cross-linking of the peptidoglycan cell wall. Required for normal cell elongation and division. Required for adequate localization of FtsZ. Involved in resistance to antibiotics including beta-lactams.,Transpeptidase that catalyzes cross-linking of the peptidoglycan cell wall. Required for normal cell elongation and division. Required for adequate localization of FtsZ. Involved in resistance to antibiotics including beta-lactams.,,,,,,,GO:0008658; GO:0071972,GO:0016755,GO:0016755,GO:0016755,GO:0016755,GO:0016755,0.1276,0.1276,0.1276,0.1276,0.1276,5,0.1276,0.5018,no
NORA_STRON,B4ER92,ESM2Text,Bacteria,1897,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA. The first module, NorA, is used twice in an iterative fashion.",Iterative type I polyketide synthase that catalyzes the synthesis of the naphthoic acid moiety during the biosynthesis of the neocarzinostatin (NCS) chromophore.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0031177,,,,,,,,,,,0,,0.2495,no
NORA_STRON,B4ER92,Prot2Text,Bacteria,1897,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA. The first module, NorA, is used twice in an iterative fashion.","Part of the PpsABCDE complex involved in the biosynthesis of the lipid core common to phthiocerols and phenolphthiocerols by successive additions of malonyl-CoA or methylmalonyl-CoA extender units. PpsA can accept as substrate the activated forms of either icosanoyl (C20), docosanoyl (C22) or lignoceroyl (C24) groups from FadD26, or a (4-hydroxyphenyl)-C17 or (4-hydroxyphenyl)-C19 fatty acyl from FadD29. PpsA initiates the biosynthesis and extends its substrate using a malonyl-CoA extender unit. The PpsB and PpsC proteins add the second and third malonyl-CoA extender units. PpsD adds an (R)-methylmalonyl unit and PpsE adds a second (R)-methylmalonyl unit. The incorporation of the methylmalonyl units results in formation of two branched methyl groups in the elongated product.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0031177,GO:0016747,,GO:0016747,GO:0016747,GO:0016746,0.6667,,0.6667,0.6667,0.5734,4,0.6434,0.2495,no
NORA_STRON,B4ER92,ProtT3,Bacteria,1897,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA. The first module, NorA, is used twice in an iterative fashion.",Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004315; GO:0004312; GO:0031177,GO:0004315,GO:0004315,GO:0004312,GO:0004315,GO:0004315,0.7026,0.7026,0.7026,0.7026,0.7026,5,0.7026,0.2495,no
NORA_STRON,B4ER92,ProtTale,Bacteria,1897,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA. The first module, NorA, is used twice in an iterative fashion.",Involved in the biosynthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0031177,,,,,,,,,,,0,,0.2495,no
NORA_STRON,B4ER92,Protein2Text,Bacteria,1897,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA. The first module, NorA, is used twice in an iterative fashion.","This protein is a part of a fatty acid synthase system, which is responsible for the synthesis of fatty acids. In this system, the protein is likely involved in the condensation of acetyl-CoA with malonyl-CoA to form the fatty acid chain. This is a crucial step in the synthesis of fatty acids, which are important components of cellular membranes and energy storage molecules.",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0004315; GO:0004312; GO:0031177,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.7026,0.7026,0.7026,0.7026,0.7026,5,0.7026,0.2495,no
NORA_STRON,B4ER92,Reference,Bacteria,1897,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA. The first module, NorA, is used twice in an iterative fashion.","Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA. The first module, NorA, is used twice in an iterative fashion.",,,,,,,GO:0004315; GO:0004312; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.5734,0.5734,0.5734,0.6667,0.5734,5,0.5921,0.2495,no
NORA2_STRON,B4ER95,ESM2Text,Bacteria,3625,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.",Iterative type I polyketide synthase that catalyzes the biosynthesis of the naphthoic acid moiety during the biosynthesis of the neocarzinostatin (NCS) chromophore.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0031177,,,,,,,,,,,0,,0.3072,no
NORA2_STRON,B4ER95,Prot2Text,Bacteria,3625,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.",Iterative type I polyketide synthase that catalyzes the biosynthesis of the naphthoic acid moiety during the biosynthesis of the neocarzinostatin (NCS) chromophore.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0031177,GO:0004314,,GO:0004314,GO:0016746,GO:0016746,0.4054,,0.4054,0.5734,0.5734,4,0.4894,0.3072,no
NORA2_STRON,B4ER95,ProtT3,Bacteria,3625,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.",Involved in the biosynthesis of the nonribosomal peptide antibiotic bacillaene,Maybe,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0031177,GO:0016746,GO:0003988,GO:0016747,GO:0003988,GO:0004315,0.5734,0.4934,0.6667,0.4934,0.7026,5,0.5859,0.3072,no
NORA2_STRON,B4ER95,ProtTale,Bacteria,3625,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.",Involved in the biosynthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0031177,,,,,,,,,,,0,,0.3072,no
NORA2_STRON,B4ER95,Protein2Text,Bacteria,3625,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.","This protein is involved in the biosynthesis of cell wall components. More specifically, it is a component of the type VII secretion system and plays a role in peptidoglycan biosynthesis.",No,No,No,No,No,not-Yes,GO:0004315; GO:0004312; GO:0031177,,,,,,,,,,,0,,0.3072,no
NORA2_STRON,B4ER95,Reference,Bacteria,3625,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.","Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.",,,,,,,GO:0004315; GO:0004312; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.5734,0.5734,0.5734,0.6667,0.5734,5,0.5921,0.3072,no
NORB_STRON,B4ER96,ESM2Text,Bacteria,2174,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.",Involved in the biosynthesis of the pyridine ring of trigonelline (TG; N-methylnicotinate) used as a carbon source for bacterial growth. Catalyzes the synthesis of 6-methyl-5-naphthoate from nicotinate in the biosynthesis of the phospholipid (nicotinate-6-P) analog N-methylnicotinate (NMN).,Maybe,Maybe,No,No,No,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177; GO:0008270,,,,,,,,,,,0,,0.2291,no
NORB_STRON,B4ER96,Prot2Text,Bacteria,2174,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.","Polyketide synthase involved in the biosynthesis of methyl-branched fatty acids such as mycolipanoic, mycolipenic (phthienoic) and mycolipodienoic acids in the mycobacterial fatty acid elongation cycle.",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177; GO:0008270,GO:0004314,,GO:0004314,GO:0016746,GO:0016746,0.3221,,0.3221,0.4793,0.4793,4,0.4007,0.2291,no
NORB_STRON,B4ER96,ProtT3,Bacteria,2174,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.",Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177; GO:0008270,GO:0016746,GO:0003988,GO:0016747,GO:0003988,GO:0004315,0.4793,0.3916,0.526,0.3916,0.539,5,0.4655,0.2291,no
NORB_STRON,B4ER96,ProtTale,Bacteria,2174,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.",Involved in the biosynthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. The first step in bacillaene biosynthesis is the formation of the polyketide backbone by condensation of one acetyl-CoA starter unit with 7 malonyl-CoA units. Polyketides are derived from acetyl-CoA in bacillaene biosynthesis.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177; GO:0008270,GO:0016491,GO:0016757,,,GO:0016746,0.4944,0.3559,,,0.4793,3,0.4432,0.2291,no
NORB_STRON,B4ER96,Protein2Text,Bacteria,2174,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.","The molecular function of this protein is as a lipase, which is an enzyme that catalyzes the hydrolysis of lipids.",No,No,No,No,No,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177; GO:0008270,,,,,,,,,,,0,,0.2291,no
NORB_STRON,B4ER96,Reference,Bacteria,2174,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.","Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.",,,,,,,GO:0004315; GO:0004312; GO:0016491; GO:0031177; GO:0008270,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.4793,0.4793,0.4793,0.526,0.4793,5,0.4886,0.2291,no
NORC_STRON,B4ER97,ESM2Text,Bacteria,2266,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.","Component of the Pks1-Pks2 complex that is required for the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The Pks1-Pks2 complex catalyzes the condensation of tyrosine and acetyl-CoA to form the octaketide backbone of pyrichalasin H. The Pks1-Pks2 complex also functions as a reductase converting pyrichalasin H to pyridin-2-carboxylic acid.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0031177,,,,,,,,,,,0,,0.2672,no
NORC_STRON,B4ER97,Prot2Text,Bacteria,2266,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.",Probably involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It catalyzes the transfer of the malonyl group from malonyl-CoA to the acyl acceptor.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0031177,GO:0004314,,GO:0004314,GO:0016746,GO:0016746,0.4054,,0.4054,0.5734,0.5734,4,0.4894,0.2672,no
NORC_STRON,B4ER97,ProtT3,Bacteria,2266,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.",Catalyzes the condensation of malonyl-CoA with acetyl-CoA to form acetoacetyl-CoA. Belongs to the thiolase-like superfamily. Acetoacetyl-CoA synthase family,No,Maybe,Maybe,Maybe,No,not-Yes,GO:0004315; GO:0004312; GO:0031177,GO:0016746,GO:0003988,GO:0016747,GO:0003988,GO:0004315,0.5734,0.4934,0.6667,0.4934,0.7026,5,0.5859,0.2672,no
NORC_STRON,B4ER97,ProtTale,Bacteria,2266,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0031177,GO:0016491,GO:0016757,,,GO:0016746,0.2982,0.3882,,,0.5734,3,0.4199,0.2672,no
NORC_STRON,B4ER97,Protein2Text,Bacteria,2266,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.","This protein is involved in the breakdown of fatty acids. More specifically, it is a part of the fatty acid transport system, which plays a crucial role in the transport of fatty acids from the cytoplasm to the mitochondria for beta-oxidation.",No,No,No,No,No,not-Yes,GO:0004315; GO:0004312; GO:0031177,,,,,,,,,,,0,,0.2672,no
NORC_STRON,B4ER97,Reference,Bacteria,2266,"Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.","Component of a type I modular polyketide synthase (PKS) that generates the backbone of the antibiotic spectinabilin (also known as neoaureothin), a nitroaryl-substituted polyketide metabolite. This PKS system accepts the unusual starter unit 4- nitrobenzoyl-CoA and extends it by 6 molecules of (S)-methylmalonyl-CoA and a single molecule of malonyl-CoA.",,,,,,,GO:0004315; GO:0004312; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.5734,0.5734,0.5734,0.6667,0.5734,5,0.5921,0.2672,no
ICLRG_STREG,B4XYC8,ESM2Text,Bacteria,371,"DNA glycosylase involved in the repair of interstrand DNA cross-links (ICLs), which are highly toxic DNA lesions that covalently tether the opposing strands of DNA, thereby inhibiting essential cellular processes such as DNA replication and transcription. Acts by unhooking both sides of the ICLs, forming abasic (AP) sites on both strands. AlkZ specifically repairs DNA damage induced by azinomycin B (AZB), a natural product with potent antibiotic and antitumor activities that interacts covalently with duplex DNA and forms ICLs. AlkZ thus confers self- resistance to azinomycin B, which is produced by S.sahachiroi. It may also protect target sites by protein-DNA interaction. Binds sequence non-specifically to native DNA and structure-specifically to azinomycin B-modified sites, with higher affinity to azinomycin B-modified sites and lower affinity to native DNA duplex. In vitro, also acts on monoadducts and can catalyze the excision of N7-methylguanine (7mGua) from an oligonucleotide containing N7-methyldeoxyguanosine (d7mG). Is a monofunctional DNA glycosylase that does not have lyase activity.","Involved in chromosome condensation, segregation and cell cycle progression. May participate in facilitating chromosome segregation by condensation DNA from both sides of a centrally located replisome during cell division. Probably acts via its interaction with MukB and MukF.",No,No,No,No,No,not-Yes,GO:0003677; GO:0016787,,,,,,,,,,,0,,0.5924,yes
ICLRG_STREG,B4XYC8,Prot2Text,Bacteria,371,"DNA glycosylase involved in the repair of interstrand DNA cross-links (ICLs), which are highly toxic DNA lesions that covalently tether the opposing strands of DNA, thereby inhibiting essential cellular processes such as DNA replication and transcription. Acts by unhooking both sides of the ICLs, forming abasic (AP) sites on both strands. AlkZ specifically repairs DNA damage induced by azinomycin B (AZB), a natural product with potent antibiotic and antitumor activities that interacts covalently with duplex DNA and forms ICLs. AlkZ thus confers self- resistance to azinomycin B, which is produced by S.sahachiroi. It may also protect target sites by protein-DNA interaction. Binds sequence non-specifically to native DNA and structure-specifically to azinomycin B-modified sites, with higher affinity to azinomycin B-modified sites and lower affinity to native DNA duplex. In vitro, also acts on monoadducts and can catalyze the excision of N7-methylguanine (7mGua) from an oligonucleotide containing N7-methyldeoxyguanosine (d7mG). Is a monofunctional DNA glycosylase that does not have lyase activity.","Involved in transformation; part of the gene cluster that mediates the biosynthesis of the antibiotic 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA) and its derivatives. The direct non-reducing polyketide synthase dbaI product is 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA), produced by condensation of one acetyl-CoA starter unit with 4 malonyl-CoA units and one methylation step. The FAD-dependent monooxygenase dbaH is responsible for the synthesis of yellow pigments derived from the oxidation of DHMBA. The roles of dbaB, C, E and F have still to be determined (Probable).",No,No,No,No,No,not-Yes,GO:0003677; GO:0016787,,,,,,,,,,,0,,0.5924,yes
ICLRG_STREG,B4XYC8,ProtT3,Bacteria,371,"DNA glycosylase involved in the repair of interstrand DNA cross-links (ICLs), which are highly toxic DNA lesions that covalently tether the opposing strands of DNA, thereby inhibiting essential cellular processes such as DNA replication and transcription. Acts by unhooking both sides of the ICLs, forming abasic (AP) sites on both strands. AlkZ specifically repairs DNA damage induced by azinomycin B (AZB), a natural product with potent antibiotic and antitumor activities that interacts covalently with duplex DNA and forms ICLs. AlkZ thus confers self- resistance to azinomycin B, which is produced by S.sahachiroi. It may also protect target sites by protein-DNA interaction. Binds sequence non-specifically to native DNA and structure-specifically to azinomycin B-modified sites, with higher affinity to azinomycin B-modified sites and lower affinity to native DNA duplex. In vitro, also acts on monoadducts and can catalyze the excision of N7-methylguanine (7mGua) from an oligonucleotide containing N7-methyldeoxyguanosine (d7mG). Is a monofunctional DNA glycosylase that does not have lyase activity.","Involved in DNA repair. Recognizes and binds 7,8-dihydro-8-oxoguanine (8-oxoG) and 2,6-diamino-4-hydroxy-5-N- methylformamidopyrimidine (FAPy) DNA lesions. Belongs to the Tld family",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0003677; GO:0016787,GO:0003684,GO:0003677,GO:0003684,GO:0003684,GO:0003684,0.6214,0.7379,0.6214,0.6214,0.6214,5,0.6447,0.5924,yes
ICLRG_STREG,B4XYC8,ProtTale,Bacteria,371,"DNA glycosylase involved in the repair of interstrand DNA cross-links (ICLs), which are highly toxic DNA lesions that covalently tether the opposing strands of DNA, thereby inhibiting essential cellular processes such as DNA replication and transcription. Acts by unhooking both sides of the ICLs, forming abasic (AP) sites on both strands. AlkZ specifically repairs DNA damage induced by azinomycin B (AZB), a natural product with potent antibiotic and antitumor activities that interacts covalently with duplex DNA and forms ICLs. AlkZ thus confers self- resistance to azinomycin B, which is produced by S.sahachiroi. It may also protect target sites by protein-DNA interaction. Binds sequence non-specifically to native DNA and structure-specifically to azinomycin B-modified sites, with higher affinity to azinomycin B-modified sites and lower affinity to native DNA duplex. In vitro, also acts on monoadducts and can catalyze the excision of N7-methylguanine (7mGua) from an oligonucleotide containing N7-methyldeoxyguanosine (d7mG). Is a monofunctional DNA glycosylase that does not have lyase activity.","Involved in the biosynthesis of the osmoprotectant glycine betaine, which allows L.mesenteroides to survive in the presence of high levels of salt. Catalyzes the transfer of the guanosine moiety of guanosine 5'-phosphorylethanolamine (GPE) to adenosine 5'-phosphorylethanolamine (APREL) to yield betaine aldehyde and ADP-alpha-D-glucose. The enzyme also catalyzes the reverse reaction, i.e. the oxidation of APREL to adenosine 5'-phosphorylethanolamine (APRE)",No,No,No,No,No,not-Yes,GO:0003677; GO:0016787,,GO:0016491,,,,,0.4647,,,,1,0.4647,0.5924,yes
ICLRG_STREG,B4XYC8,Protein2Text,Bacteria,371,"DNA glycosylase involved in the repair of interstrand DNA cross-links (ICLs), which are highly toxic DNA lesions that covalently tether the opposing strands of DNA, thereby inhibiting essential cellular processes such as DNA replication and transcription. Acts by unhooking both sides of the ICLs, forming abasic (AP) sites on both strands. AlkZ specifically repairs DNA damage induced by azinomycin B (AZB), a natural product with potent antibiotic and antitumor activities that interacts covalently with duplex DNA and forms ICLs. AlkZ thus confers self- resistance to azinomycin B, which is produced by S.sahachiroi. It may also protect target sites by protein-DNA interaction. Binds sequence non-specifically to native DNA and structure-specifically to azinomycin B-modified sites, with higher affinity to azinomycin B-modified sites and lower affinity to native DNA duplex. In vitro, also acts on monoadducts and can catalyze the excision of N7-methylguanine (7mGua) from an oligonucleotide containing N7-methyldeoxyguanosine (d7mG). Is a monofunctional DNA glycosylase that does not have lyase activity.","The molecular function of this protein is part of a DNA repair pathway. It is involved in repairing damaged DNA. Specifically, it is part of the base excision repair (BER) pathway.",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0003677; GO:0016787,,,,,,,,,,,0,,0.5924,yes
ICLRG_STREG,B4XYC8,Reference,Bacteria,371,"DNA glycosylase involved in the repair of interstrand DNA cross-links (ICLs), which are highly toxic DNA lesions that covalently tether the opposing strands of DNA, thereby inhibiting essential cellular processes such as DNA replication and transcription. Acts by unhooking both sides of the ICLs, forming abasic (AP) sites on both strands. AlkZ specifically repairs DNA damage induced by azinomycin B (AZB), a natural product with potent antibiotic and antitumor activities that interacts covalently with duplex DNA and forms ICLs. AlkZ thus confers self- resistance to azinomycin B, which is produced by S.sahachiroi. It may also protect target sites by protein-DNA interaction. Binds sequence non-specifically to native DNA and structure-specifically to azinomycin B-modified sites, with higher affinity to azinomycin B-modified sites and lower affinity to native DNA duplex. In vitro, also acts on monoadducts and can catalyze the excision of N7-methylguanine (7mGua) from an oligonucleotide containing N7-methyldeoxyguanosine (d7mG). Is a monofunctional DNA glycosylase that does not have lyase activity.","DNA glycosylase involved in the repair of interstrand DNA cross-links (ICLs), which are highly toxic DNA lesions that covalently tether the opposing strands of DNA, thereby inhibiting essential cellular processes such as DNA replication and transcription. Acts by unhooking both sides of the ICLs, forming abasic (AP) sites on both strands. AlkZ specifically repairs DNA damage induced by azinomycin B (AZB), a natural product with potent antibiotic and antitumor activities that interacts covalently with duplex DNA and forms ICLs. AlkZ thus confers self- resistance to azinomycin B, which is produced by S.sahachiroi. It may also protect target sites by protein-DNA interaction. Binds sequence non-specifically to native DNA and structure-specifically to azinomycin B-modified sites, with higher affinity to azinomycin B-modified sites and lower affinity to native DNA duplex. In vitro, also acts on monoadducts and can catalyze the excision of N7-methylguanine (7mGua) from an oligonucleotide containing N7-methyldeoxyguanosine (d7mG). Is a monofunctional DNA glycosylase that does not have lyase activity.",,,,,,,GO:0003677; GO:0016787,GO:0019104,GO:0019104,GO:0019104,GO:0019104; GO:0003677,GO:0019104,0.3702,0.3702,0.3702,0.7498,0.3702,5,0.4461,0.5924,yes
AATA_PENCH,P15802,ESM2Text,Eukaryota,357,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic. The first step of the pathway is performed by the trimodular NRPS acvA that produces the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L- cysteinyl-D-valine (LLD-ACV or ACV) via condensation of the 3 residues L-2-aminoadipate, L-cysteine and L-valine. The precursor amino acids for penicillin biosynthesis are withdrawn from the vacuolar amino acid pool by the MFS-type transporter penV. Each of the constituent amino acids of the tripeptide acv are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. The tripeptide ACV is then cyclized to form isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin. This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively.","Isopenicillin-N;partic acid aminotransferase that catalyzes the hydrolytic amination of intracellular penicillin N and penicillin N-heterocyclic acid to yield the 10R,12S-containing penicillin precursor penitillin. Isopenicillin-N homoacetyltransferase that catalyzes the regioselective amination of intracellular phenolic acid to produce 10R,12S-pipienolacineNAc. The penicillin-N homoacetyltransferase is also able to produce the 10S,12S-pipitoneal acid-enantiomer. This amidation occurs via a beta-membrane beta-elimination.",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0050640,,,,,,,,,,,0,,0.1795,no
AATA_PENCH,P15802,Prot2Text,Eukaryota,357,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic. The first step of the pathway is performed by the trimodular NRPS acvA that produces the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L- cysteinyl-D-valine (LLD-ACV or ACV) via condensation of the 3 residues L-2-aminoadipate, L-cysteine and L-valine. The precursor amino acids for penicillin biosynthesis are withdrawn from the vacuolar amino acid pool by the MFS-type transporter penV. Each of the constituent amino acids of the tripeptide acv are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. The tripeptide ACV is then cyclized to form isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin. This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively.","Isopenicillin N-acyltransferase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic. The first step of penicillin biosynthesis is the production of the beta-methyl-proline precursor from penicillin precursor YWA1-P (Probable). Methylation of the bridge carbon of penicillin by the polyketide synthase PKS4 is then performed by the methyltransferase ORF19, whose target is not yet known. The geranylgeranyl pyrophosphate synthase ORF7 then converts GGDPQ into 5-O-geranylgeranylindole (5-O-GGI), the first precursor for the biosynthesis of penicillin. 5-O-GGI is then substrate of the cytochrome P450 monooxygenase ORF1, whose expression is repressed by the terpene cyclase ORF2 to increase the intracellular concentration of 5-O-geranylgeranylindole (5-O-GGI). The FAD-dependent monooxygenase ORF3 then catalyzes epoxidation of the two terminal alkenes of 5-O-GG",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0050640,GO:0018025,,GO:0047452,GO:0016746,GO:0016746,0.1956,,0.1737,0.6466,0.6466,4,0.4156,0.1795,no
AATA_PENCH,P15802,ProtT3,Eukaryota,357,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic. The first step of the pathway is performed by the trimodular NRPS acvA that produces the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L- cysteinyl-D-valine (LLD-ACV or ACV) via condensation of the 3 residues L-2-aminoadipate, L-cysteine and L-valine. The precursor amino acids for penicillin biosynthesis are withdrawn from the vacuolar amino acid pool by the MFS-type transporter penV. Each of the constituent amino acids of the tripeptide acv are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. The tripeptide ACV is then cyclized to form isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin. This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively.","Catalyzes the transfer of the acyl group from the acyl-CoA thioester to the aromatic amino acid residue of the substrate, leading to the release of the aromatic amino acid and the corresponding CoA thioester. Belongs to the aromatic-amino-acid-acyl-CoA thioesterase family",No,No,No,Maybe,No,not-Yes,GO:0050640,GO:0016790,GO:0016790,GO:0016790,GO:0016790,GO:0016790,0.2067,0.2067,0.2067,0.2067,0.2067,5,0.2067,0.1795,no
AATA_PENCH,P15802,ProtTale,Eukaryota,357,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic. The first step of the pathway is performed by the trimodular NRPS acvA that produces the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L- cysteinyl-D-valine (LLD-ACV or ACV) via condensation of the 3 residues L-2-aminoadipate, L-cysteine and L-valine. The precursor amino acids for penicillin biosynthesis are withdrawn from the vacuolar amino acid pool by the MFS-type transporter penV. Each of the constituent amino acids of the tripeptide acv are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. The tripeptide ACV is then cyclized to form isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin. This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively.",Catalyzes the decarboxylation of 2-oxoglutarate to succinate semialdehyde.,No,No,No,No,No,not-Yes,GO:0050640,GO:0004029,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.1493,0.2067,0.2067,0.2067,0.2067,5,0.1952,0.1795,no
AATA_PENCH,P15802,Protein2Text,Eukaryota,357,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic. The first step of the pathway is performed by the trimodular NRPS acvA that produces the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L- cysteinyl-D-valine (LLD-ACV or ACV) via condensation of the 3 residues L-2-aminoadipate, L-cysteine and L-valine. The precursor amino acids for penicillin biosynthesis are withdrawn from the vacuolar amino acid pool by the MFS-type transporter penV. Each of the constituent amino acids of the tripeptide acv are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. The tripeptide ACV is then cyclized to form isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin. This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively.","The molecular function of this protein is likely to be a hydrolase, specifically a type of hydrolase that catalyzes the hydrolysis of a specific substrate. This is based on its classification as a protein that is involved in a metabolic process, specifically in the breakdown of a certain molecule. However, without more specific information, it is difficult to determine the exact molecular function of this protein.",Vague,Vague,No,Vague,No,not-Yes,GO:0050640,,,,,,,,,,,0,,0.1795,no
AATA_PENCH,P15802,Reference,Eukaryota,357,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic. The first step of the pathway is performed by the trimodular NRPS acvA that produces the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L- cysteinyl-D-valine (LLD-ACV or ACV) via condensation of the 3 residues L-2-aminoadipate, L-cysteine and L-valine. The precursor amino acids for penicillin biosynthesis are withdrawn from the vacuolar amino acid pool by the MFS-type transporter penV. Each of the constituent amino acids of the tripeptide acv are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. The tripeptide ACV is then cyclized to form isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin. This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic. The first step of the pathway is performed by the trimodular NRPS acvA that produces the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L- cysteinyl-D-valine (LLD-ACV or ACV) via condensation of the 3 residues L-2-aminoadipate, L-cysteine and L-valine. The precursor amino acids for penicillin biosynthesis are withdrawn from the vacuolar amino acid pool by the MFS-type transporter penV. Each of the constituent amino acids of the tripeptide acv are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. The tripeptide ACV is then cyclized to form isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin. This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively.",,,,,,,GO:0050640,GO:0016874,GO:0016874,GO:0016874,GO:0016874,GO:0016874,0.3176,0.3176,0.3176,0.3176,0.3176,5,0.3176,0.1795,no
SHC1_SCHJY,B6K412,ESM2Text,Eukaryota,656,"Squalene cyclase that catalyzes the oxygen-independent cyclization of squalene into hopanoids, a class of cyclic triterpenoids including hop-22(29)-ene, hop-17(21)-ene, hop-21(22)-ene, and hopan-22- ol.",Catalyzes the cyclization of squalene into hopene.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0016829; GO:0051007,GO:0016872,GO:0016829,,GO:0045550,GO:0010333,0.4715,0.7754,,0.4096,0.4664,4,0.5307,0.2351,no
SHC1_SCHJY,B6K412,Prot2Text,Eukaryota,656,"Squalene cyclase that catalyzes the oxygen-independent cyclization of squalene into hopanoids, a class of cyclic triterpenoids including hop-22(29)-ene, hop-17(21)-ene, hop-21(22)-ene, and hopan-22- ol.",Catalyzes the cyclization of squalene into hopene.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0016829; GO:0051007,GO:0010333,,GO:0016853,GO:0016866,GO:0016853,0.4664,,0.5776,0.6171,0.5776,4,0.5597,0.2351,no
SHC1_SCHJY,B6K412,ProtT3,Eukaryota,656,"Squalene cyclase that catalyzes the oxygen-independent cyclization of squalene into hopanoids, a class of cyclic triterpenoids including hop-22(29)-ene, hop-17(21)-ene, hop-21(22)-ene, and hopan-22- ol.","Catalyzes the cyclization of (2E,6E,10E,14E,18E,22E,26E,30E,34E,38E,42E,46E,50E,54E,58E,62E,66E,70E,74E,78E,82E,86E,90E,94E,98E,102E,106E,110E,114E",Yes,Yes,Maybe,Maybe,No,not-Yes,GO:0016829; GO:0051007,GO:0010333,GO:0010333,GO:0010333,GO:0010333,GO:0010333,0.4664,0.4664,0.4664,0.4664,0.4664,5,0.4664,0.2351,no
SHC1_SCHJY,B6K412,ProtTale,Eukaryota,656,"Squalene cyclase that catalyzes the oxygen-independent cyclization of squalene into hopanoids, a class of cyclic triterpenoids including hop-22(29)-ene, hop-17(21)-ene, hop-21(22)-ene, and hopan-22- ol.",Catalyzes the cyclization of farnesyl diphosphate (FPP) to geranylgeranyl diphosphate (GGPP).,No,No,No,No,No,not-Yes,GO:0016829; GO:0051007,GO:0004337,GO:0004337,,GO:0016765,GO:0004311,0.2693,0.2693,,0.4096,0.2693,4,0.3044,0.2351,no
SHC1_SCHJY,B6K412,Protein2Text,Eukaryota,656,"Squalene cyclase that catalyzes the oxygen-independent cyclization of squalene into hopanoids, a class of cyclic triterpenoids including hop-22(29)-ene, hop-17(21)-ene, hop-21(22)-ene, and hopan-22- ol.","This protein is involved in the biosynthesis of sesterterpenoids, specifically in the production of sesterterpenoids with an isopropyl group at C-17. It is a part of the pathway that converts isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) into sesterterpenoids.",No,Maybe,No,Maybe,No,not-Yes,GO:0016829; GO:0051007,,GO:0016829,,GO:0010333,GO:0010333,,0.7754,,0.4664,0.4664,3,0.5694,0.2351,no
SHC1_SCHJY,B6K412,Reference,Eukaryota,656,"Squalene cyclase that catalyzes the oxygen-independent cyclization of squalene into hopanoids, a class of cyclic triterpenoids including hop-22(29)-ene, hop-17(21)-ene, hop-21(22)-ene, and hopan-22- ol.","Squalene cyclase that catalyzes the oxygen-independent cyclization of squalene into hopanoids, a class of cyclic triterpenoids including hop-22(29)-ene, hop-17(21)-ene, hop-21(22)-ene, and hopan-22- ol.",,,,,,,GO:0016829; GO:0051007,GO:0016872,GO:0051996,GO:0016829,GO:0016872,GO:0016829,0.4715,0.3019,0.7754,0.4715,0.7754,5,0.5591,0.2351,no
GNNA_ACIF2,B7JA34,ESM2Text,Bacteria,313,"Oxidoreductase involved in the synthesis of 2,3-diamino-2,3- dideoxy-D-glucopyranose (GlcN3N), which is a component of lipid A in some species. Catalyzes the NAD(+)-dependent oxidation of the glucosamine 3-position of UDP-N-acetyl-glucosamine (UDP-GlcNAc) to a ketone moiety, forming UDP-2-acetamido-3-dehydro-2- deoxy-alpha-D-glucopyranose (UDP-3-oxo-GlcNAc). Is specific for UDP-GlcNAc, no activity is observed with UDP-glucose (UDP-Glc), UDP-glucoronic acid (UDP-GlcA), UDP- galactose (UDP-Gal) and UDP-N-acetylgalactosamine (UDP-GalNAc). Cannot use FAD(+) and NADP(+).","Involved in the biosynthesis of the dTDP-D-desosamine, a highly reducing polyketide that forms the backbone of dTDP-6-keto-1,6-diene (DKD-1,6-TDP). Catalyzes the reduction of the C3-hydroxy group of C4-hydroxyacyl-CoA (C3HB-CoA) to yield DKD-1,6-DKD-1,6-D-allofolactone. It can use NAD or NADP but NAD is the preferred substrate.",No,No,No,No,No,not-Yes,GO:0000166; GO:0016491,,,,,,,,,,,0,,0.2088,no
GNNA_ACIF2,B7JA34,Prot2Text,Bacteria,313,"Oxidoreductase involved in the synthesis of 2,3-diamino-2,3- dideoxy-D-glucopyranose (GlcN3N), which is a component of lipid A in some species. Catalyzes the NAD(+)-dependent oxidation of the glucosamine 3-position of UDP-N-acetyl-glucosamine (UDP-GlcNAc) to a ketone moiety, forming UDP-2-acetamido-3-dehydro-2- deoxy-alpha-D-glucopyranose (UDP-3-oxo-GlcNAc). Is specific for UDP-GlcNAc, no activity is observed with UDP-glucose (UDP-Glc), UDP-glucoronic acid (UDP-GlcA), UDP- galactose (UDP-Gal) and UDP-N-acetylgalactosamine (UDP-GalNAc). Cannot use FAD(+) and NADP(+).",Involved in catabolism of D-apiose. Catalyzes oxidation of D-apiose to D-apionolactone.,No,No,Maybe,No,No,not-Yes,GO:0000166; GO:0016491,GO:0016614,,GO:0016614,GO:0016614,GO:0016614,0.5895,,0.5895,0.5895,0.5895,4,0.5895,0.2088,no
GNNA_ACIF2,B7JA34,ProtT3,Bacteria,313,"Oxidoreductase involved in the synthesis of 2,3-diamino-2,3- dideoxy-D-glucopyranose (GlcN3N), which is a component of lipid A in some species. Catalyzes the NAD(+)-dependent oxidation of the glucosamine 3-position of UDP-N-acetyl-glucosamine (UDP-GlcNAc) to a ketone moiety, forming UDP-2-acetamido-3-dehydro-2- deoxy-alpha-D-glucopyranose (UDP-3-oxo-GlcNAc). Is specific for UDP-GlcNAc, no activity is observed with UDP-glucose (UDP-Glc), UDP-glucoronic acid (UDP-GlcA), UDP- galactose (UDP-Gal) and UDP-N-acetylgalactosamine (UDP-GalNAc). Cannot use FAD(+) and NADP(+).",Involved in the oxidation of myo-inositol (MI) to 2-keto-myo- inositol (2KMI or 2-inosose). Belongs to the Gfo/Idh/MocA family,No,No,No,No,No,not-Yes,GO:0000166; GO:0016491,GO:0016614,GO:0050113,GO:0047832,GO:0016491,GO:0016614,0.5895,0.44,0.4359,0.7229,0.5895,5,0.5556,0.2088,no
GNNA_ACIF2,B7JA34,ProtTale,Bacteria,313,"Oxidoreductase involved in the synthesis of 2,3-diamino-2,3- dideoxy-D-glucopyranose (GlcN3N), which is a component of lipid A in some species. Catalyzes the NAD(+)-dependent oxidation of the glucosamine 3-position of UDP-N-acetyl-glucosamine (UDP-GlcNAc) to a ketone moiety, forming UDP-2-acetamido-3-dehydro-2- deoxy-alpha-D-glucopyranose (UDP-3-oxo-GlcNAc). Is specific for UDP-GlcNAc, no activity is observed with UDP-glucose (UDP-Glc), UDP-glucoronic acid (UDP-GlcA), UDP- galactose (UDP-Gal) and UDP-N-acetylgalactosamine (UDP-GalNAc). Cannot use FAD(+) and NADP(+).","Involved in the degradation of 3,6-anhydro-L-galactose (GalA). Catalyzes the NAD(P)H-dependent oxidation of 3,6-anhydro-L-galactose to 3,6-anhydro-D-galactonolactone.",No,No,Maybe,No,No,not-Yes,GO:0000166; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.7229,0.7229,0.7229,0.7229,0.7229,5,0.7229,0.2088,no
GNNA_ACIF2,B7JA34,Protein2Text,Bacteria,313,"Oxidoreductase involved in the synthesis of 2,3-diamino-2,3- dideoxy-D-glucopyranose (GlcN3N), which is a component of lipid A in some species. Catalyzes the NAD(+)-dependent oxidation of the glucosamine 3-position of UDP-N-acetyl-glucosamine (UDP-GlcNAc) to a ketone moiety, forming UDP-2-acetamido-3-dehydro-2- deoxy-alpha-D-glucopyranose (UDP-3-oxo-GlcNAc). Is specific for UDP-GlcNAc, no activity is observed with UDP-glucose (UDP-Glc), UDP-glucoronic acid (UDP-GlcA), UDP- galactose (UDP-Gal) and UDP-N-acetylgalactosamine (UDP-GalNAc). Cannot use FAD(+) and NADP(+).","The molecular function of this protein is as an enzyme, specifically a ketol-acid reductoisomerase, involved in the biosynthesis of branched-chain amino acids.
 
                This protein catalyzes the interconversion of dihydroxy-acetone phosphate (DHAP) and 2,3-diketo-3-phenylpropionate (DKPP). It also catalyzes the interconversion of 2,3-diketo-3-phenylpropionate (DKPP) and 2-hydroxy-3-oxo-3-phenylpropanoate (2-HOPP). 
 

                It is a key enzyme in the biosynthesis of branched-chain amino acids (BCAAs) (Leu, Ile and Val) via the branched-chain amino acid (BCAA) pathway. The BCAA pathway is a central metabolic pathway that provides the building blocks for proteins, fatty acids and other metabolites. 
 

                The protein has a preference for the L-isomer of the substrate.
 
                It also has a preference for the substrate with the phenyl group attached to the alpha carbon.
 
                It has a preference for the substrate with the hydroxyl group attached to the alpha carbon.
 
                It has a preference for the substrate with the hydroxyl group attached to the beta carbon.
 
                It has a preference for the substrate with the ketone group attached to the beta carbon.
 
                It has a preference for the substrate with the ketone group attached to the alpha carbon.
 
                It has a preference for the substrate with the hydroxyl group attached to the alpha carbon.
 
                It has a preference for the substrate with the hydroxyl group attached to the beta carbon.
 
                It has a preference for the substrate with the ketone group attached to the beta carbon.
 
                It has a preference for the substrate with the ketone group attached to the alpha carbon.
 
                It has a preference for the substrate with the hydroxyl group attached to the alpha carbon.
 
                It has a preference for the substrate with the hydroxyl group attached to the beta carbon.
 
                It has a preference for the substrate with the ketone group attached to the beta carbon.
 
                It has a preference for the substrate with the ketone group attached to the alpha carbon.
 
                It has a preference for the substrate with the hydroxyl group attached to the alpha carbon.
 
                It has a preference for the substrate",No,No,No,No,No,not-Yes,GO:0000166; GO:0016491,GO:0004455,GO:0004455,GO:0004455,GO:0004455,GO:0004455,0.4359,0.4359,0.4359,0.4359,0.4359,5,0.4359,0.2088,no
GNNA_ACIF2,B7JA34,Reference,Bacteria,313,"Oxidoreductase involved in the synthesis of 2,3-diamino-2,3- dideoxy-D-glucopyranose (GlcN3N), which is a component of lipid A in some species. Catalyzes the NAD(+)-dependent oxidation of the glucosamine 3-position of UDP-N-acetyl-glucosamine (UDP-GlcNAc) to a ketone moiety, forming UDP-2-acetamido-3-dehydro-2- deoxy-alpha-D-glucopyranose (UDP-3-oxo-GlcNAc). Is specific for UDP-GlcNAc, no activity is observed with UDP-glucose (UDP-Glc), UDP-glucoronic acid (UDP-GlcA), UDP- galactose (UDP-Gal) and UDP-N-acetylgalactosamine (UDP-GalNAc). Cannot use FAD(+) and NADP(+).","Oxidoreductase involved in the synthesis of 2,3-diamino-2,3- dideoxy-D-glucopyranose (GlcN3N), which is a component of lipid A in some species. Catalyzes the NAD(+)-dependent oxidation of the glucosamine 3-position of UDP-N-acetyl-glucosamine (UDP-GlcNAc) to a ketone moiety, forming UDP-2-acetamido-3-dehydro-2- deoxy-alpha-D-glucopyranose (UDP-3-oxo-GlcNAc). Is specific for UDP-GlcNAc, no activity is observed with UDP-glucose (UDP-Glc), UDP-glucoronic acid (UDP-GlcA), UDP- galactose (UDP-Gal) and UDP-N-acetylgalactosamine (UDP-GalNAc). Cannot use FAD(+) and NADP(+).",,,,,,,GO:0000166; GO:0016491,GO:0016616,GO:0016616,GO:0016616,GO:0016616,GO:0016616,0.4994,0.4994,0.4994,0.4994,0.4994,5,0.4994,0.2088,no
DHRSX_DANRE,B8A5W4,ESM2Text,Eukaryota,324,Oxidoreductase that plays a key role in early steps of protein N-linked glycosylation by mediating two non-consecutive steps in dolichol biosynthesis. Acts both as a NAD(+)- dependent dehydrogenase and as a NADPH-dependent reductase during the conversion of polyprenol into dolichol. First catalyzes the NAD(+)-dependent dehydrogenation of polyprenol into polyprenal; polyprenal is then reduced into dolichal by srd5a3. It then catalyzes the NADPH-dependent reduction of dolichal into dolichol.,Involved in the positive regulation of starvation-induced autophagy.,No,No,No,No,No,not-Yes,GO:0160197; GO:0160196,,,,,,,,,,,0,,0.264,no
DHRSX_DANRE,B8A5W4,Prot2Text,Eukaryota,324,Oxidoreductase that plays a key role in early steps of protein N-linked glycosylation by mediating two non-consecutive steps in dolichol biosynthesis. Acts both as a NAD(+)- dependent dehydrogenase and as a NADPH-dependent reductase during the conversion of polyprenol into dolichol. First catalyzes the NAD(+)-dependent dehydrogenation of polyprenol into polyprenal; polyprenal is then reduced into dolichal by srd5a3. It then catalyzes the NADPH-dependent reduction of dolichal into dolichol.,Probable oxidoreductase.,Vague,Vague,Vague,Vague,No,not-Yes,GO:0160197; GO:0160196,GO:0016491,,GO:0016491,GO:0016491,GO:0016491,0.6019,,0.6019,0.6019,0.6019,4,0.6019,0.264,no
DHRSX_DANRE,B8A5W4,ProtT3,Eukaryota,324,Oxidoreductase that plays a key role in early steps of protein N-linked glycosylation by mediating two non-consecutive steps in dolichol biosynthesis. Acts both as a NAD(+)- dependent dehydrogenase and as a NADPH-dependent reductase during the conversion of polyprenol into dolichol. First catalyzes the NAD(+)-dependent dehydrogenation of polyprenol into polyprenal; polyprenal is then reduced into dolichal by srd5a3. It then catalyzes the NADPH-dependent reduction of dolichal into dolichol.,Putative oxidoreductase. Secreted. Belongs to the short-chain dehydrogenases/reductases (SDR) family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0160197; GO:0160196,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.6019,0.6019,0.6019,0.6019,0.6019,5,0.6019,0.264,no
DHRSX_DANRE,B8A5W4,ProtTale,Eukaryota,324,Oxidoreductase that plays a key role in early steps of protein N-linked glycosylation by mediating two non-consecutive steps in dolichol biosynthesis. Acts both as a NAD(+)- dependent dehydrogenase and as a NADPH-dependent reductase during the conversion of polyprenol into dolichol. First catalyzes the NAD(+)-dependent dehydrogenation of polyprenol into polyprenal; polyprenal is then reduced into dolichal by srd5a3. It then catalyzes the NADPH-dependent reduction of dolichal into dolichol.,"Retinol-binding dehydrogenase that catalyzes the reversible NADPH-dependent oxidation of retinol to 11-oxo-retinol. May play a role in the metabolism of retinoids, such as all-trans-retinol and 11-oxo-retinol.",No,No,No,No,No,not-Yes,GO:0160197; GO:0160196,GO:0016491; GO:0000166,GO:0016491; GO:0004745,GO:0004745,GO:0004745,GO:0004745,0.4774,0.5167,0.261,0.261,0.261,5,0.3554,0.264,no
DHRSX_DANRE,B8A5W4,Protein2Text,Eukaryota,324,Oxidoreductase that plays a key role in early steps of protein N-linked glycosylation by mediating two non-consecutive steps in dolichol biosynthesis. Acts both as a NAD(+)- dependent dehydrogenase and as a NADPH-dependent reductase during the conversion of polyprenol into dolichol. First catalyzes the NAD(+)-dependent dehydrogenation of polyprenol into polyprenal; polyprenal is then reduced into dolichal by srd5a3. It then catalyzes the NADPH-dependent reduction of dolichal into dolichol.,"The molecular function of this protein is not explicitly stated in the provided text, but based on its name, it is likely to be involved in catalyzing a reaction, specifically the reduction of a substrate. In the context of the provided text, it is mentioned as being involved in the reduction of retinol, suggesting that it may have a role in the metabolism of retinoids. 

However, a more specific function of this protein is described in the text as being involved in the reduction of retinal to retinol. This suggests that the protein may play a role in the visual cycle, where retinol is converted to 11-cis retinal, which is then used in the synthesis of rhodopsin, the light-sensitive pigment in the retina.

Therefore, the molecular function of this protein is likely to be a retinol dehydrogenase, specifically involved in the reduction of retinal to retinol.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0160197; GO:0160196,GO:0004745,GO:0004745,GO:0004745,GO:0004745,GO:0004745,0.261,0.261,0.261,0.261,0.261,5,0.261,0.264,no
DHRSX_DANRE,B8A5W4,Reference,Eukaryota,324,Oxidoreductase that plays a key role in early steps of protein N-linked glycosylation by mediating two non-consecutive steps in dolichol biosynthesis. Acts both as a NAD(+)- dependent dehydrogenase and as a NADPH-dependent reductase during the conversion of polyprenol into dolichol. First catalyzes the NAD(+)-dependent dehydrogenation of polyprenol into polyprenal; polyprenal is then reduced into dolichal by srd5a3. It then catalyzes the NADPH-dependent reduction of dolichal into dolichol.,Oxidoreductase that plays a key role in early steps of protein N-linked glycosylation by mediating two non-consecutive steps in dolichol biosynthesis. Acts both as a NAD(+)- dependent dehydrogenase and as a NADPH-dependent reductase during the conversion of polyprenol into dolichol. First catalyzes the NAD(+)-dependent dehydrogenation of polyprenol into polyprenal; polyprenal is then reduced into dolichal by srd5a3. It then catalyzes the NADPH-dependent reduction of dolichal into dolichol.,,,,,,,GO:0160197; GO:0160196,GO:0016491,GO:0016616,GO:0016616; GO:0050051,GO:0016616,GO:0016491,0.6019,0.3987,0.3769,0.3987,0.6019,5,0.4756,0.264,no
ZN488_DANRE,B8A5Y1,ESM2Text,Eukaryota,502,"Transcriptional repressor. May have histone methyltransferase activity (Probable). Negatively regulates shh signaling activity in pMN progenitor cells which prevents their switch from motor neuron to oligodendrocyte precursor cell production. Independently of shh activity, also regulates oligodendrocyte formation.",Transcriptional regulator that specifically binds to the DNA sequence 5'-CCCTGC-3' found in the promoter of some cardiac mRNAs. Recruits ci to the nucleus and nucleates actin polymerization in muscle cells. Plays a role in oogenesis and early skeletal development.,Maybe,Maybe,Maybe,Maybe,Vague,not-Yes,GO:0003677; GO:0008168; GO:0008270,GO:0003700; GO:0003677,GO:0003700; GO:0003677,GO:0003700; GO:0003677,GO:0003700; GO:0003677,GO:0003700,0.5246,0.5246,0.5246,0.5246,0.1842,5,0.4565,0.7359,yes
ZN488_DANRE,B8A5Y1,Prot2Text,Eukaryota,502,"Transcriptional repressor. May have histone methyltransferase activity (Probable). Negatively regulates shh signaling activity in pMN progenitor cells which prevents their switch from motor neuron to oligodendrocyte precursor cell production. Independently of shh activity, also regulates oligodendrocyte formation.","Transcription factor involved in the regulation of MAG (Myelin-associated glycoprotein) expression, which is involved in myelin formation. Probably binds the consensus motif 5'-[AG]TGATTCAG-3' and other regulatory elements found in Myelin regulatory elements (MREs).",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0003677; GO:0008168; GO:0008270,GO:0003700,GO:0003700,GO:0003700,GO:0003700,GO:0003700,0.1842,0.1842,0.1842,0.1842,0.1842,5,0.1842,0.7359,yes
ZN488_DANRE,B8A5Y1,ProtT3,Eukaryota,502,"Transcriptional repressor. May have histone methyltransferase activity (Probable). Negatively regulates shh signaling activity in pMN progenitor cells which prevents their switch from motor neuron to oligodendrocyte precursor cell production. Independently of shh activity, also regulates oligodendrocyte formation.",Probable histone methyltransferase. Nucleus. Belongs to the class V-like SAM-binding methyltransferase superfamily,Maybe,Yes,Yes,Yes,Maybe,Yes,GO:0003677; GO:0008168; GO:0008270,GO:0018024,GO:0018024,GO:0042054,GO:0018024,GO:0018024,0.0,0.0,0.3639,0.0,0.0,5,0.0728,0.7359,yes
ZN488_DANRE,B8A5Y1,ProtTale,Eukaryota,502,"Transcriptional repressor. May have histone methyltransferase activity (Probable). Negatively regulates shh signaling activity in pMN progenitor cells which prevents their switch from motor neuron to oligodendrocyte precursor cell production. Independently of shh activity, also regulates oligodendrocyte formation.","Probable regulator of transcription. Has been implicated in a variety of biological processes, including cell proliferation, differentiation and apoptosis, and in the regulation of the glucocorticoid receptor (NR3C1). May inhibit the transcriptional activity of EP300 by competing for the same binding site on EP300.",Vague,Vague,Maybe,Maybe,No,not-Yes,GO:0003677; GO:0008168; GO:0008270,,,,,,,,,,,0,,0.7359,yes
ZN488_DANRE,B8A5Y1,Protein2Text,Eukaryota,502,"Transcriptional repressor. May have histone methyltransferase activity (Probable). Negatively regulates shh signaling activity in pMN progenitor cells which prevents their switch from motor neuron to oligodendrocyte precursor cell production. Independently of shh activity, also regulates oligodendrocyte formation.","The molecular function of the protein is not explicitly stated in the provided text. However, based on its name, it is likely involved in transcriptional regulation, possibly as a transcription factor or co-factor. Transcription factors are proteins that bind to specific DNA sequences near genes to control their transcription into RNA. They can activate or repress gene expression, depending on the context.",Maybe,Vague,Maybe,Vague,No,not-Yes,GO:0003677; GO:0008168; GO:0008270,,GO:0003700,GO:0003700,,,,0.1842,0.1842,,,2,0.1842,0.7359,yes
ZN488_DANRE,B8A5Y1,Reference,Eukaryota,502,"Transcriptional repressor. May have histone methyltransferase activity (Probable). Negatively regulates shh signaling activity in pMN progenitor cells which prevents their switch from motor neuron to oligodendrocyte precursor cell production. Independently of shh activity, also regulates oligodendrocyte formation.","Transcriptional repressor. May have histone methyltransferase activity (Probable). Negatively regulates shh signaling activity in pMN progenitor cells which prevents their switch from motor neuron to oligodendrocyte precursor cell production. Independently of shh activity, also regulates oligodendrocyte formation.",,,,,,,GO:0003677; GO:0008168; GO:0008270,,,,GO:0042054,GO:0042054,,,,0.3639,0.3639,2,0.3639,0.7359,yes
CAOYE_CHLAD,B8G5D6,ESM2Text,Bacteria,354,"Ene-reductase that catalyzes the stereoselective reduction of activated C-C double bonds. Shows very good activity with 4-ketoisophorone, 2-cyclohexen-1-one and 1-octen-3-one, and low activity with maleimide, 2-methyl-pentenal, 2-methyl-cyclohexen-1-one, 2-cyclopenten-1-one and trans-2-hexen-1-al. Shows the highest catalytic efficiency with ketoisophorone. Exhibits a restricted substrate spectrum with generally lower activities compared to other ene-reductases.","Catalyzes the reduction of the double bond of an array of alpha,beta-unsaturated aldehydes and ketones. It also reduces the nitro group of nitroester and nitroaromatic compounds. It could have a role in detoxification processes.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0010181; GO:0050661; GO:0003959,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016628,0.4044,0.4044,0.4044,0.4044,0.2729,5,0.3781,0.1281,no
CAOYE_CHLAD,B8G5D6,Prot2Text,Bacteria,354,"Ene-reductase that catalyzes the stereoselective reduction of activated C-C double bonds. Shows very good activity with 4-ketoisophorone, 2-cyclohexen-1-one and 1-octen-3-one, and low activity with maleimide, 2-methyl-pentenal, 2-methyl-cyclohexen-1-one, 2-cyclopenten-1-one and trans-2-hexen-1-al. Shows the highest catalytic efficiency with ketoisophorone. Exhibits a restricted substrate spectrum with generally lower activities compared to other ene-reductases.",Putative oxophytodienoate reductase that may be involved in the biosynthesis or metabolism of oxylipin signaling molecules.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0010181; GO:0050661; GO:0003959,GO:0016491,,GO:0016491,GO:0016631,GO:0016491,0.4044,,0.4044,0.2342,0.4044,4,0.3619,0.1281,no
CAOYE_CHLAD,B8G5D6,ProtT3,Bacteria,354,"Ene-reductase that catalyzes the stereoselective reduction of activated C-C double bonds. Shows very good activity with 4-ketoisophorone, 2-cyclohexen-1-one and 1-octen-3-one, and low activity with maleimide, 2-methyl-pentenal, 2-methyl-cyclohexen-1-one, 2-cyclopenten-1-one and trans-2-hexen-1-al. Shows the highest catalytic efficiency with ketoisophorone. Exhibits a restricted substrate spectrum with generally lower activities compared to other ene-reductases.","Catalyzes the reduction of the double bond of an array of alpha,beta-unsaturated aldehydes and ketones. It also reduces the nitro group of nitroester and nitroaromatic compounds. It could have a role in detoxification processes. Belongs to the NADH:flavin oxidoreductase/NADH oxidase family. NamA subfamily",Yes,Yes,Yes,Yes,Yes,Yes,GO:0010181; GO:0050661; GO:0003959,GO:0016651,GO:0016491,GO:0016491; GO:0050660,GO:0016491; GO:0071949,GO:0016491,0.4693,0.4044,0.6778,0.6396,0.4044,5,0.5191,0.1281,no
CAOYE_CHLAD,B8G5D6,ProtTale,Bacteria,354,"Ene-reductase that catalyzes the stereoselective reduction of activated C-C double bonds. Shows very good activity with 4-ketoisophorone, 2-cyclohexen-1-one and 1-octen-3-one, and low activity with maleimide, 2-methyl-pentenal, 2-methyl-cyclohexen-1-one, 2-cyclopenten-1-one and trans-2-hexen-1-al. Shows the highest catalytic efficiency with ketoisophorone. Exhibits a restricted substrate spectrum with generally lower activities compared to other ene-reductases.","Catalyzes the reduction of the double bond of an array of alpha,beta-unsaturated aldehydes and ketones. It also reduces the nitro group of nitroester and nitroaromatic compounds. It could have a role in detoxification processes.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0010181; GO:0050661; GO:0003959,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4044,0.4044,0.4044,0.4044,0.4044,5,0.4044,0.1281,no
CAOYE_CHLAD,B8G5D6,Protein2Text,Bacteria,354,"Ene-reductase that catalyzes the stereoselective reduction of activated C-C double bonds. Shows very good activity with 4-ketoisophorone, 2-cyclohexen-1-one and 1-octen-3-one, and low activity with maleimide, 2-methyl-pentenal, 2-methyl-cyclohexen-1-one, 2-cyclopenten-1-one and trans-2-hexen-1-al. Shows the highest catalytic efficiency with ketoisophorone. Exhibits a restricted substrate spectrum with generally lower activities compared to other ene-reductases.","This protein is an oxidoreductase, specifically a dehydrogenase. It is involved in the reduction of a compound, likely a substrate, using NADH as a cofactor.",Maybe,Vague,Vague,Vague,Maybe,not-Yes,GO:0010181; GO:0050661; GO:0003959,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4044,0.4044,0.4044,0.4044,0.4044,5,0.4044,0.1281,no
CAOYE_CHLAD,B8G5D6,Reference,Bacteria,354,"Ene-reductase that catalyzes the stereoselective reduction of activated C-C double bonds. Shows very good activity with 4-ketoisophorone, 2-cyclohexen-1-one and 1-octen-3-one, and low activity with maleimide, 2-methyl-pentenal, 2-methyl-cyclohexen-1-one, 2-cyclopenten-1-one and trans-2-hexen-1-al. Shows the highest catalytic efficiency with ketoisophorone. Exhibits a restricted substrate spectrum with generally lower activities compared to other ene-reductases.","Ene-reductase that catalyzes the stereoselective reduction of activated C-C double bonds. Shows very good activity with 4-ketoisophorone, 2-cyclohexen-1-one and 1-octen-3-one, and low activity with maleimide, 2-methyl-pentenal, 2-methyl-cyclohexen-1-one, 2-cyclopenten-1-one and trans-2-hexen-1-al. Shows the highest catalytic efficiency with ketoisophorone. Exhibits a restricted substrate spectrum with generally lower activities compared to other ene-reductases.",,,,,,,GO:0010181; GO:0050661; GO:0003959,GO:0016628,GO:0016491,GO:0016631,GO:0016628,GO:0016491,0.2729,0.4044,0.2342,0.2729,0.4044,5,0.3178,0.1281,no
RAMA_METBA,B8Y445,ESM2Text,Archaea,540,"Reductase required for the activation of corrinoid-dependent methylamine methyltransferase reactions during methanogenesis. Mediates the ATP-dependent reduction of corrinoid proteins from the inactive cobalt(II) state to the active cobalt(I) state. Acts on the corrinoid proteins involved in methanogenesis from monomethylamine (MMA), dimethylamine (DMA) and trimethylamine (TMA), namely MtmC, MtbC and MttC, respectively.",Catalyzes the reversible phosphorylation of pyruvate to acetyl-CoA and CO(2). It can also use butyryl-CoA and dihydroxyacetone phosphate as phosphoryl donors. May be involved in the control of metabolic pathways that utilize pyruvate as a carbon source.,No,No,No,No,No,not-Yes,GO:0051539; GO:0046872; GO:0016491,,,,,,,,,,,0,,0.3739,no
RAMA_METBA,B8Y445,Prot2Text,Archaea,540,"Reductase required for the activation of corrinoid-dependent methylamine methyltransferase reactions during methanogenesis. Mediates the ATP-dependent reduction of corrinoid proteins from the inactive cobalt(II) state to the active cobalt(I) state. Acts on the corrinoid proteins involved in methanogenesis from monomethylamine (MMA), dimethylamine (DMA) and trimethylamine (TMA), namely MtmC, MtbC and MttC, respectively.","Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.",No,No,No,No,No,not-Yes,GO:0051539; GO:0046872; GO:0016491,GO:0004594,GO:0004594,GO:0004594,GO:0004594,GO:0004594; GO:0005524,0.1972,0.1972,0.1972,0.1972,0.2816,5,0.2141,0.3739,no
RAMA_METBA,B8Y445,ProtT3,Archaea,540,"Reductase required for the activation of corrinoid-dependent methylamine methyltransferase reactions during methanogenesis. Mediates the ATP-dependent reduction of corrinoid proteins from the inactive cobalt(II) state to the active cobalt(I) state. Acts on the corrinoid proteins involved in methanogenesis from monomethylamine (MMA), dimethylamine (DMA) and trimethylamine (TMA), namely MtmC, MtbC and MttC, respectively.",Catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to 2-keto-3-deoxy-6-phosphogluconate (KDPG). Belongs to the FGGY kinase family,No,No,No,No,No,not-Yes,GO:0051539; GO:0046872; GO:0016491,GO:0016301; GO:0005524,GO:0019200; GO:0005524,GO:0008673; GO:0005524,GO:0016301; GO:0005524,GO:0008673,0.3188,0.298,0.271,0.3188,0.181,5,0.2775,0.3739,no
RAMA_METBA,B8Y445,ProtTale,Archaea,540,"Reductase required for the activation of corrinoid-dependent methylamine methyltransferase reactions during methanogenesis. Mediates the ATP-dependent reduction of corrinoid proteins from the inactive cobalt(II) state to the active cobalt(I) state. Acts on the corrinoid proteins involved in methanogenesis from monomethylamine (MMA), dimethylamine (DMA) and trimethylamine (TMA), namely MtmC, MtbC and MttC, respectively.",Catalyzes the reversible interconversion of 2-isopropylmalate and 3- isopropylmalate.,No,No,No,No,No,not-Yes,GO:0051539; GO:0046872; GO:0016491,GO:0016829,GO:0003861,GO:0003861,GO:0003861,GO:0003861,0.374,0.222,0.222,0.222,0.222,5,0.2524,0.3739,no
RAMA_METBA,B8Y445,Protein2Text,Archaea,540,"Reductase required for the activation of corrinoid-dependent methylamine methyltransferase reactions during methanogenesis. Mediates the ATP-dependent reduction of corrinoid proteins from the inactive cobalt(II) state to the active cobalt(I) state. Acts on the corrinoid proteins involved in methanogenesis from monomethylamine (MMA), dimethylamine (DMA) and trimethylamine (TMA), namely MtmC, MtbC and MttC, respectively.",The molecular function of this protein is an ATP-coupled cysteine desulfurase.,No,No,No,No,No,not-Yes,GO:0051539; GO:0046872; GO:0016491,GO:0031071,GO:0031071,GO:0031071,GO:0031071,GO:0031071,0.222,0.222,0.222,0.222,0.222,5,0.222,0.3739,no
RAMA_METBA,B8Y445,Reference,Archaea,540,"Reductase required for the activation of corrinoid-dependent methylamine methyltransferase reactions during methanogenesis. Mediates the ATP-dependent reduction of corrinoid proteins from the inactive cobalt(II) state to the active cobalt(I) state. Acts on the corrinoid proteins involved in methanogenesis from monomethylamine (MMA), dimethylamine (DMA) and trimethylamine (TMA), namely MtmC, MtbC and MttC, respectively.","Reductase required for the activation of corrinoid-dependent methylamine methyltransferase reactions during methanogenesis. Mediates the ATP-dependent reduction of corrinoid proteins from the inactive cobalt(II) state to the active cobalt(I) state. Acts on the corrinoid proteins involved in methanogenesis from monomethylamine (MMA), dimethylamine (DMA) and trimethylamine (TMA), namely MtmC, MtbC and MttC, respectively.",,,,,,,GO:0051539; GO:0046872; GO:0016491,GO:0016491; GO:0005524,GO:0016491; GO:0005524,GO:0016491; GO:0005524,GO:0016491; GO:0005524,GO:0016491; GO:0005524,0.5559,0.5559,0.5559,0.5559,0.5559,5,0.5559,0.3739,no
GUOP_HALLT,B9LS20,ESM2Text,Archaea,241,"Phosphorylase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the phosphorolytic cleavage of guanosine to guanine and ribose-1-phosphate (R1P). Exhibits the highest activity toward guanosine, but also shows lower activity against inosine and adenosine.","Catalyzes the reversible phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0047975; GO:0004731,GO:0004731,GO:0004731,GO:0004731,GO:0004731,GO:0004731,0.9564,0.9564,0.9564,0.9564,0.9564,5,0.9564,0.5401,yes
GUOP_HALLT,B9LS20,Prot2Text,Archaea,241,"Phosphorylase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the phosphorolytic cleavage of guanosine to guanine and ribose-1-phosphate (R1P). Exhibits the highest activity toward guanosine, but also shows lower activity against inosine and adenosine.","Catalyzes the reversible phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0047975; GO:0004731,GO:0004731,GO:0004731,GO:0004731,GO:0004731,GO:0004731,0.9564,0.9564,0.9564,0.9564,0.9564,5,0.9564,0.5401,yes
GUOP_HALLT,B9LS20,ProtT3,Archaea,241,"Phosphorylase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the phosphorolytic cleavage of guanosine to guanine and ribose-1-phosphate (R1P). Exhibits the highest activity toward guanosine, but also shows lower activity against inosine and adenosine.","Catalyzes the reversible phosphorolytic breakdown of the N- glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1- phosphate. Belongs to the PNP/UDP phosphorylase family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0047975; GO:0004731,GO:0004731,GO:0004731,GO:0004731,GO:0004731,GO:0004731,0.9564,0.9564,0.9564,0.9564,0.9564,5,0.9564,0.5401,yes
GUOP_HALLT,B9LS20,ProtTale,Archaea,241,"Phosphorylase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the phosphorolytic cleavage of guanosine to guanine and ribose-1-phosphate (R1P). Exhibits the highest activity toward guanosine, but also shows lower activity against inosine and adenosine.","Catalyzes the reversible phosphorolytic breakdown of the N- glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0047975; GO:0004731,GO:0004731,GO:0004731,GO:0004731,GO:0004731,GO:0004731,0.9564,0.9564,0.9564,0.9564,0.9564,5,0.9564,0.5401,yes
GUOP_HALLT,B9LS20,Protein2Text,Archaea,241,"Phosphorylase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the phosphorolytic cleavage of guanosine to guanine and ribose-1-phosphate (R1P). Exhibits the highest activity toward guanosine, but also shows lower activity against inosine and adenosine.","The molecular function of this protein is an enzyme that catalyzes the transfer of an amino group from a nucleoside to a cytidine or uridine, resulting in the formation of a new nucleoside. Specifically, it catalyzes the reversible transfer of an amino group from 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) to cytidine or uridine, resulting in the formation of IMP or UMP, respectively. This reaction is part of the purine and pyrimidine salvage pathways, which allow cells to synthesize nucleotides from pre-formed nucleosides and bases rather than from scratch. The protein is also involved in the regulation of purine and pyrimidine metabolism, and has been implicated in various cellular processes, including cell growth, differentiation, and survival.",No,No,No,No,No,not-Yes,GO:0047975; GO:0004731,,,,,,,,,,,0,,0.5401,yes
GUOP_HALLT,B9LS20,Reference,Archaea,241,"Phosphorylase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the phosphorolytic cleavage of guanosine to guanine and ribose-1-phosphate (R1P). Exhibits the highest activity toward guanosine, but also shows lower activity against inosine and adenosine.","Phosphorylase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the phosphorolytic cleavage of guanosine to guanine and ribose-1-phosphate (R1P). Exhibits the highest activity toward guanosine, but also shows lower activity against inosine and adenosine.",,,,,,,GO:0047975; GO:0004731,GO:0004731,GO:0004731,GO:0004731,GO:0004731,GO:0004731,0.9564,0.9564,0.9564,0.9564,0.9564,5,0.9564,0.5401,yes
CNDG_CHOCO,B9ZUK6,ESM2Text,Bacteria,541,"Oxidative decarboxylase involved in the biosynthesis of the antibiotics chondrochloren A and chondrochloren B. Catalyzes the decarboxylation of biologically inactive pre- chondrochloren A and pre-chondrochloren B to yield mature chondrochloren A and chondrochloren B, respectively. Cannot decarboxylate free L-tyrosine, 3-chloro-tyrosine or a number of chlorinated and non-chlorinated analog substrates containing variable N-acyl chains.","Catalyzes the reduction of the double bond of an array of alpha,beta-unsaturated aldehydes and ketones.",No,No,No,No,No,not-Yes,GO:0004458; GO:0008720; GO:0071949; GO:0016829,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016628,0.4307,0.4307,0.4307,0.4307,0.2951,5,0.4036,0.4515,no
CNDG_CHOCO,B9ZUK6,Prot2Text,Bacteria,541,"Oxidative decarboxylase involved in the biosynthesis of the antibiotics chondrochloren A and chondrochloren B. Catalyzes the decarboxylation of biologically inactive pre- chondrochloren A and pre-chondrochloren B to yield mature chondrochloren A and chondrochloren B, respectively. Cannot decarboxylate free L-tyrosine, 3-chloro-tyrosine or a number of chlorinated and non-chlorinated analog substrates containing variable N-acyl chains.","Catalyzes the dehydrogenation of D-lactate to pyruvate. Is likely involved in the utilization of D-lactate as a sole source of carbon for growth. Active with a variety of electron acceptors including cytochrome c, 2,5-dichlorophenolindophenol (DCIP), 2-methyl-1,4-benzoquinone (MPBQ), pyridine-4-carboxylate, methyl-alpha-D-lactate, FAD, FMN and quinones.",No,No,No,No,No,not-Yes,GO:0004458; GO:0008720; GO:0071949; GO:0016829,GO:0004458,GO:0008720,GO:0008720,GO:0004458,GO:0008720,0.5926,0.5861,0.5861,0.5926,0.5861,5,0.5887,0.4515,no
CNDG_CHOCO,B9ZUK6,ProtT3,Bacteria,541,"Oxidative decarboxylase involved in the biosynthesis of the antibiotics chondrochloren A and chondrochloren B. Catalyzes the decarboxylation of biologically inactive pre- chondrochloren A and pre-chondrochloren B to yield mature chondrochloren A and chondrochloren B, respectively. Cannot decarboxylate free L-tyrosine, 3-chloro-tyrosine or a number of chlorinated and non-chlorinated analog substrates containing variable N-acyl chains.",Cell membrane; Single-pass membrane protein. Belongs to the FAD-dependent oxidoreductase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004458; GO:0008720; GO:0071949; GO:0016829,GO:0016491; GO:0071949,GO:0016491; GO:0071949,GO:0016491; GO:0050660,GO:0016491; GO:0071949,GO:0016491,0.6726,0.6726,0.6442,0.6726,0.4307,5,0.6185,0.4515,no
CNDG_CHOCO,B9ZUK6,ProtTale,Bacteria,541,"Oxidative decarboxylase involved in the biosynthesis of the antibiotics chondrochloren A and chondrochloren B. Catalyzes the decarboxylation of biologically inactive pre- chondrochloren A and pre-chondrochloren B to yield mature chondrochloren A and chondrochloren B, respectively. Cannot decarboxylate free L-tyrosine, 3-chloro-tyrosine or a number of chlorinated and non-chlorinated analog substrates containing variable N-acyl chains.","Catalyzes the NAD(+)-dependent oxidation of L-gulonate 6-phosphate to L-2,3-diketo-L-gulonate 6-phosphate.",No,No,No,No,No,not-Yes,GO:0004458; GO:0008720; GO:0071949; GO:0016829,GO:0016616,GO:0016616,GO:0016491,GO:0016616,GO:0016491,0.4255,0.4255,0.4307,0.4255,0.4307,5,0.4276,0.4515,no
CNDG_CHOCO,B9ZUK6,Protein2Text,Bacteria,541,"Oxidative decarboxylase involved in the biosynthesis of the antibiotics chondrochloren A and chondrochloren B. Catalyzes the decarboxylation of biologically inactive pre- chondrochloren A and pre-chondrochloren B to yield mature chondrochloren A and chondrochloren B, respectively. Cannot decarboxylate free L-tyrosine, 3-chloro-tyrosine or a number of chlorinated and non-chlorinated analog substrates containing variable N-acyl chains.","This protein is involved in the oxidation of aldehydes. It is likely a part of a metabolic pathway that converts aldehydes into carboxylic acids or other compounds. The specific molecular function of this protein is to catalyze the oxidation of a particular aldehyde, resulting in the formation of a carboxylic acid. This is a common type of reaction in metabolism, and it is often used to convert toxic or reactive compounds into less harmful ones.",No,Maybe,Maybe,Maybe,No,not-Yes,GO:0004458; GO:0008720; GO:0071949; GO:0016829,GO:0016491,GO:0016491,GO:0016491,GO:0016903,GO:0016903,0.4307,0.4307,0.4307,0.3507,0.3507,5,0.3987,0.4515,no
CNDG_CHOCO,B9ZUK6,Reference,Bacteria,541,"Oxidative decarboxylase involved in the biosynthesis of the antibiotics chondrochloren A and chondrochloren B. Catalyzes the decarboxylation of biologically inactive pre- chondrochloren A and pre-chondrochloren B to yield mature chondrochloren A and chondrochloren B, respectively. Cannot decarboxylate free L-tyrosine, 3-chloro-tyrosine or a number of chlorinated and non-chlorinated analog substrates containing variable N-acyl chains.","Oxidative decarboxylase involved in the biosynthesis of the antibiotics chondrochloren A and chondrochloren B. Catalyzes the decarboxylation of biologically inactive pre- chondrochloren A and pre-chondrochloren B to yield mature chondrochloren A and chondrochloren B, respectively. Cannot decarboxylate free L-tyrosine, 3-chloro-tyrosine or a number of chlorinated and non-chlorinated analog substrates containing variable N-acyl chains.",,,,,,,GO:0004458; GO:0008720; GO:0071949; GO:0016829,GO:0016491; GO:0016831,GO:0016831; GO:0016491,GO:0016491; GO:0016831,GO:0016491; GO:0016831,GO:0016831; GO:0016491,0.4905,0.4905,0.4905,0.4905,0.4905,5,0.4905,0.4515,no
PA2A_LACAO,C0HMB2,ESM2Text,Eukaryota,122,"PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. In vivo, is non- lethal to mice when intravenously injected up to a concentration of 30 ug, however does show significant edematogenic activity at the injection site.",PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005509; GO:0005543,GO:0004623,GO:0004623,GO:0004623,GO:0004623,GO:0004623,0.0856,0.0856,0.0856,0.0856,0.0856,5,0.0856,0.2256,no
PA2A_LACAO,C0HMB2,Prot2Text,Eukaryota,122,"PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. In vivo, is non- lethal to mice when intravenously injected up to a concentration of 30 ug, however does show significant edematogenic activity at the injection site.",PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005509; GO:0005543,GO:0004623,GO:0004623,GO:0004623,GO:0004623,GO:0004623,0.0856,0.0856,0.0856,0.0856,0.0856,5,0.0856,0.2256,no
PA2A_LACAO,C0HMB2,ProtT3,Eukaryota,122,"PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. In vivo, is non- lethal to mice when intravenously injected up to a concentration of 30 ug, however does show significant edematogenic activity at the injection site.",PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Secreted. Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005509; GO:0005543,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623,0.5875,0.5875,0.5875,0.5875,0.0856,5,0.4871,0.2256,no
PA2A_LACAO,C0HMB2,ProtTale,Eukaryota,122,"PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. In vivo, is non- lethal to mice when intravenously injected up to a concentration of 30 ug, however does show significant edematogenic activity at the injection site.",Snake venom phospholipase A2 (PLA2) that inhibits platelet aggregation. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005509; GO:0005543,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623; GO:0005509,0.5875,0.5875,0.5875,0.5875,0.5875,5,0.5875,0.2256,no
PA2A_LACAO,C0HMB2,Protein2Text,Eukaryota,122,"PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. In vivo, is non- lethal to mice when intravenously injected up to a concentration of 30 ug, however does show significant edematogenic activity at the injection site.",The molecular function of this protein is phospholipase activity.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005509; GO:0005543,GO:0004623,GO:0016788,GO:0016788,GO:0016788,,0.0856,0.153,0.153,0.153,,4,0.1361,0.2256,no
PA2A_LACAO,C0HMB2,Reference,Eukaryota,122,"PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. In vivo, is non- lethal to mice when intravenously injected up to a concentration of 30 ug, however does show significant edematogenic activity at the injection site.","PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. In vivo, is non- lethal to mice when intravenously injected up to a concentration of 30 ug, however does show significant edematogenic activity at the injection site.",,,,,,,GO:0005509; GO:0005543,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623; GO:0005509,0.5875,0.5875,0.5875,0.5875,0.5875,5,0.5875,0.2256,no
DHP3_ECOLX,C0HMD9,ESM2Text,Bacteria,263,"Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives. Confers resistance to sulfonamide antibiotics, including sulfamethoxazole (SMX), sulfadiazine and sulfisoxazole.","Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004156; GO:0046872,GO:0004156,GO:0004156,GO:0004156,GO:0004156,GO:0004156,0.7015,0.7015,0.7015,0.7015,0.7015,5,0.7015,0.3937,no
DHP3_ECOLX,C0HMD9,Prot2Text,Bacteria,263,"Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives. Confers resistance to sulfonamide antibiotics, including sulfamethoxazole (SMX), sulfadiazine and sulfisoxazole.","Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004156; GO:0046872,GO:0004156,GO:0004156,GO:0004156,GO:0004156,GO:0004156,0.7015,0.7015,0.7015,0.7015,0.7015,5,0.7015,0.3937,no
DHP3_ECOLX,C0HMD9,ProtT3,Bacteria,263,"Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives. Confers resistance to sulfonamide antibiotics, including sulfamethoxazole (SMX), sulfadiazine and sulfisoxazole.","Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives. Belongs to the DHPS family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004156; GO:0046872,GO:0004156,GO:0004156,GO:0004156,GO:0004156,GO:0004156,0.7015,0.7015,0.7015,0.7015,0.7015,5,0.7015,0.3937,no
DHP3_ECOLX,C0HMD9,ProtTale,Bacteria,263,"Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives. Confers resistance to sulfonamide antibiotics, including sulfamethoxazole (SMX), sulfadiazine and sulfisoxazole.","Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004156; GO:0046872,GO:0004150,GO:0004150,GO:0004156,GO:0004156,GO:0004156,0.1865,0.1865,0.7015,0.7015,0.7015,5,0.4955,0.3937,no
DHP3_ECOLX,C0HMD9,Protein2Text,Bacteria,263,"Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives. Confers resistance to sulfonamide antibiotics, including sulfamethoxazole (SMX), sulfadiazine and sulfisoxazole.","The molecular function of this protein is not specified in the provided information. However, it is known to be a part of the purine salvage pathway, which is responsible for the synthesis of purine nucleotides from ribonucleosides. The specific molecular function of this protein may involve catalyzing a reaction in this pathway, such as converting inosine to hypoxanthine. Further research would be needed to determine the exact molecular function of this protein.",No,No,No,No,No,not-Yes,GO:0004156; GO:0046872,,,,,,,,,,,0,,0.3937,no
DHP3_ECOLX,C0HMD9,Reference,Bacteria,263,"Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives. Confers resistance to sulfonamide antibiotics, including sulfamethoxazole (SMX), sulfadiazine and sulfisoxazole.","Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives. Confers resistance to sulfonamide antibiotics, including sulfamethoxazole (SMX), sulfadiazine and sulfisoxazole.",,,,,,,GO:0004156; GO:0046872,GO:0004156,GO:0004156,GO:0004156,GO:0004156,GO:0004156,0.7015,0.7015,0.7015,0.7015,0.7015,5,0.7015,0.3937,no
OXDA_MAIZE,C0PBF8,ESM2Text,Eukaryota,386,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Enables the organism to utilize D-amino acids as a source of nutrients.,"Magnesium-dependent oxidoreductase that mediates the oxidative rearrangement of L-serine, leading to the formation of amines. Can use various amines including N-methylpropionitrile, N-ethylbutane-1-carboxylate, N-ethylacetone, N-ethylglutamate, N-ethylpentanoate and N-ethylpentanoyl but not N-ethylbutane-3-carboxylate, propionitrile, acetate and propylene oxide. Able to reduce the standard GST substrate N-ethylpropionitrile but not the standard GST substrate N-ethylbutane-3-carboxylate.",No,No,No,No,No,not-Yes,GO:0003884; GO:0008445,,,,,,,,,,,0,,0.2685,no
OXDA_MAIZE,C0PBF8,Prot2Text,Eukaryota,386,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Enables the organism to utilize D-amino acids as a source of nutrients.,Probable oxidoreductase that negatively regulates the retrieval of cargo from late endosomes to the Golgi.,No,No,Vague,Vague,No,not-Yes,GO:0003884; GO:0008445,GO:0016491,,GO:0016491,,GO:0016491,0.5223,,0.5223,,0.5223,3,0.5223,0.2685,no
OXDA_MAIZE,C0PBF8,ProtT3,Eukaryota,386,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Enables the organism to utilize D-amino acids as a source of nutrients.,Mitochondrion. Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family,No,Vague,Vague,Vague,Vague,not-Yes,GO:0003884; GO:0008445,GO:0016616,GO:0016616,GO:0016616,GO:0016616,GO:0016616,0.3381,0.3381,0.3381,0.3381,0.3381,5,0.3381,0.2685,no
OXDA_MAIZE,C0PBF8,ProtTale,Eukaryota,386,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Enables the organism to utilize D-amino acids as a source of nutrients.,"Monooxygenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",No,No,No,No,No,not-Yes,GO:0003884; GO:0008445,GO:0016491; GO:0071949,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.4069,0.414,0.414,0.414,0.414,5,0.4126,0.2685,no
OXDA_MAIZE,C0PBF8,Protein2Text,Eukaryota,386,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Enables the organism to utilize D-amino acids as a source of nutrients.,This protein has a molecular function as a monooxygenase.,No,No,No,No,No,not-Yes,GO:0003884; GO:0008445,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.414,0.414,0.414,0.414,0.414,5,0.414,0.2685,no
OXDA_MAIZE,C0PBF8,Reference,Eukaryota,386,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Enables the organism to utilize D-amino acids as a source of nutrients.,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Enables the organism to utilize D-amino acids as a source of nutrients.,,,,,,,GO:0003884; GO:0008445,GO:0003884,GO:0003884,GO:0003884,GO:0003884,GO:0003884,0.9589,0.9589,0.9589,0.9589,0.9589,5,0.9589,0.2685,no
PEX6_KOMPG,C4QXI8,ESM2Text,Eukaryota,1166,"Component of the PEX1-PEX6 AAA ATPase complex involved in peroxisome biosynthesis. The complex acts as a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.",Involved in peroxisome biosynthesis.,Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0005524; GO:0016887; GO:0140318,,,,,,,,,,,0,,0.5122,no
PEX6_KOMPG,C4QXI8,Prot2Text,Eukaryota,1166,"Component of the PEX1-PEX6 AAA ATPase complex involved in peroxisome biosynthesis. The complex acts as a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.",Involved in peroxisome biosynthesis.,Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0005524; GO:0016887; GO:0140318,GO:0016887,GO:0016887,GO:0016887,GO:0016887,GO:0016887; GO:0005524,0.5527,0.5527,0.5527,0.5527,0.83,5,0.6082,0.5122,no
PEX6_KOMPG,C4QXI8,ProtT3,Eukaryota,1166,"Component of the PEX1-PEX6 AAA ATPase complex involved in peroxisome biosynthesis. The complex acts as a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.","Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor (By similarity). The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 8 nm (By similarity). Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the",No,Maybe,No,No,No,not-Yes,GO:0005524; GO:0016887; GO:0140318,,,,,,,,,,,0,,0.5122,no
PEX6_KOMPG,C4QXI8,ProtTale,Eukaryota,1166,"Component of the PEX1-PEX6 AAA ATPase complex involved in peroxisome biosynthesis. The complex acts as a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.","Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0140318,GO:0005524,GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.537,0.83,0.83,0.83,0.83,5,0.7714,0.5122,no
PEX6_KOMPG,C4QXI8,Protein2Text,Eukaryota,1166,"Component of the PEX1-PEX6 AAA ATPase complex involved in peroxisome biosynthesis. The complex acts as a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.","The molecular function of this protein is not explicitly stated in the provided information. However, based on its name, it can be inferred that it is involved in the synthesis of molecules, likely nucleotides or nucleic acids, as it is classified as a DNA-binding protein. More specifically, it is involved in the synthesis of nucleotides, which are the building blocks of DNA and RNA.",Vague,No,No,Vague,No,not-Yes,GO:0005524; GO:0016887; GO:0140318,,,,,,,,,,,0,,0.5122,no
PEX6_KOMPG,C4QXI8,Reference,Eukaryota,1166,"Component of the PEX1-PEX6 AAA ATPase complex involved in peroxisome biosynthesis. The complex acts as a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.","Component of the PEX1-PEX6 AAA ATPase complex involved in peroxisome biosynthesis. The complex acts as a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.",,,,,,,GO:0005524; GO:0016887; GO:0140318,GO:0016887; GO:0005524,GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.83,0.5527,0.83,0.83,0.83,5,0.7745,0.5122,no
OXDD_KOMPG,C4R6B0,ESM2Text,Eukaryota,375,Selectively catalyzes the oxidative deamination of acidic amino acids. Protects the organism from the toxicity of D-amino acids. Enables the organism to utilize D- amino acids as a source of nutrients. Enables the organism to utilize D-aspartate as a nitrogen source.,"Selectively catalyzes the oxidative deamination of D-aspartate and its N-methylated derivative, N-methyl D-aspartate.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0008445; GO:0071949,GO:0003884,GO:0003884,GO:0033182,GO:0033781,GO:0008453,0.6047,0.6047,0.0,0.1825,0.1258,5,0.3035,0.2004,no
OXDD_KOMPG,C4R6B0,Prot2Text,Eukaryota,375,Selectively catalyzes the oxidative deamination of acidic amino acids. Protects the organism from the toxicity of D-amino acids. Enables the organism to utilize D- amino acids as a source of nutrients. Enables the organism to utilize D-aspartate as a nitrogen source.,Oxidizes L-pipecolate and L-proline. Does not act on D-pipecolate and on D-piproline.,No,No,No,No,No,not-Yes,GO:0008445; GO:0071949,GO:0016491,,GO:0016491,GO:0016491,GO:0016491,0.3665,,0.3665,0.3665,0.3665,4,0.3665,0.2004,no
OXDD_KOMPG,C4R6B0,ProtT3,Eukaryota,375,Selectively catalyzes the oxidative deamination of acidic amino acids. Protects the organism from the toxicity of D-amino acids. Enables the organism to utilize D- amino acids as a source of nutrients. Enables the organism to utilize D-aspartate as a nitrogen source.,Belongs to the DapA family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008445; GO:0071949,GO:0008840,GO:0008840,GO:0008840,GO:0008840,GO:0008840,0.1258,0.1258,0.1258,0.1258,0.1258,5,0.1258,0.2004,no
OXDD_KOMPG,C4R6B0,ProtTale,Eukaryota,375,Selectively catalyzes the oxidative deamination of acidic amino acids. Protects the organism from the toxicity of D-amino acids. Enables the organism to utilize D- amino acids as a source of nutrients. Enables the organism to utilize D-aspartate as a nitrogen source.,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Enables the organism to utilize D-amino acids as a source of nutrients.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008445; GO:0071949,GO:0003884,GO:0003862,GO:0003884,GO:0003884,GO:0003884,0.6047,0.1971,0.6047,0.6047,0.6047,5,0.5232,0.2004,no
OXDD_KOMPG,C4R6B0,Protein2Text,Eukaryota,375,Selectively catalyzes the oxidative deamination of acidic amino acids. Protects the organism from the toxicity of D-amino acids. Enables the organism to utilize D- amino acids as a source of nutrients. Enables the organism to utilize D-aspartate as a nitrogen source.,"The molecular function of this protein is an aminotransferase, specifically a pyridoxal phosphate-dependent aminotransferase. It catalyzes the reversible transfer of an amino group from an amino acid to a 2-keto acid. In this case, it is involved in the degradation of glutamate.",No,No,No,No,No,not-Yes,GO:0008445; GO:0071949,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.1504,0.1504,0.1504,0.1504,0.1504,5,0.1504,0.2004,no
OXDD_KOMPG,C4R6B0,Reference,Eukaryota,375,Selectively catalyzes the oxidative deamination of acidic amino acids. Protects the organism from the toxicity of D-amino acids. Enables the organism to utilize D- amino acids as a source of nutrients. Enables the organism to utilize D-aspartate as a nitrogen source.,Selectively catalyzes the oxidative deamination of acidic amino acids. Protects the organism from the toxicity of D-amino acids. Enables the organism to utilize D- amino acids as a source of nutrients. Enables the organism to utilize D-aspartate as a nitrogen source.,,,,,,,GO:0008445; GO:0071949,GO:0003884,GO:0003884,GO:0003884,GO:0003884,GO:0003884,0.6047,0.6047,0.6047,0.6047,0.6047,5,0.6047,0.2004,no
PEX1_KOMPG,C4R6C2,ESM2Text,Eukaryota,1121,"Component of the PEX1-PEX6 AAA ATPase complex involved in peroxisome biosynthesis. The complex acts as a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.",Involved in peroxisome biosynthesis. May play a direct or indirect role in delivering membrane material to developing peroxisomes. It may also be involved in intracellular membrane movement.,Maybe,Vague,Vague,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887; GO:0140318,,,,,,,,,,,0,,0.5327,no
PEX1_KOMPG,C4R6C2,Prot2Text,Eukaryota,1121,"Component of the PEX1-PEX6 AAA ATPase complex involved in peroxisome biosynthesis. The complex acts as a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.","Involved in peroxisome biosynthesis. Required for stability of the PTS1 receptor. Anchored by PEX26 to peroxisome membranes, possibly to form heteromeric AAA ATPase complexes required for the import of proteins into peroxisomes.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0016887; GO:0140318,GO:0016887,GO:0016887,GO:0016887,GO:0016887,GO:0016887; GO:0005524,0.5527,0.5527,0.5527,0.5527,0.83,5,0.6082,0.5327,no
PEX1_KOMPG,C4R6C2,ProtT3,Eukaryota,1121,"Component of the PEX1-PEX6 AAA ATPase complex involved in peroxisome biosynthesis. The complex acts as a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.","Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor (By similarity). The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 10 nm (By similarity). Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with",No,Maybe,No,No,No,not-Yes,GO:0005524; GO:0016887; GO:0140318,,,,,,,,,,,0,,0.5327,no
PEX1_KOMPG,C4R6C2,ProtTale,Eukaryota,1121,"Component of the PEX1-PEX6 AAA ATPase complex involved in peroxisome biosynthesis. The complex acts as a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.","Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0140318,GO:0005524,GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.537,0.83,0.83,0.83,0.83,5,0.7714,0.5327,no
PEX1_KOMPG,C4R6C2,Protein2Text,Eukaryota,1121,"Component of the PEX1-PEX6 AAA ATPase complex involved in peroxisome biosynthesis. The complex acts as a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.","The molecular function of the protein is not explicitly stated in the provided text, but based on the context, it can be inferred that it is involved in the replication of DNA, specifically in the replication of a particular type of DNA molecule. The text mentions that the protein is found in a specific type of DNA, and that it is involved in the replication of that DNA. Therefore, it is likely that the molecular function of this protein is involved in DNA replication.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016887; GO:0140318,,,,,,,,,,,0,,0.5327,no
PEX1_KOMPG,C4R6C2,Reference,Eukaryota,1121,"Component of the PEX1-PEX6 AAA ATPase complex involved in peroxisome biosynthesis. The complex acts as a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.","Component of the PEX1-PEX6 AAA ATPase complex involved in peroxisome biosynthesis. The complex acts as a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.",,,,,,,GO:0005524; GO:0016887; GO:0140318,GO:0016887; GO:0005524,GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.83,0.5527,0.83,0.83,0.83,5,0.7745,0.5327,no
MCDA_HALNC,D0KZ82,ESM2Text,Bacteria,216,"McdA and McdB together mediate carboxysome positioning on the nucleoid and prevent their aggregation in the cell. McdA is an ATPase that forms dynamic gradients on the nucleoid in response to adapter protein McdB, which associates with carboxysomes. The interplay between McdA gradients on the nucleoid and McdB-bound carboxysomes result in the equal spacing of Cbs along the cell length.","Component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016787; GO:0046872,,,GO:0022877,GO:0008982,GO:0008982,,,0.1186,0.1568,0.1568,3,0.1441,0.3369,no
MCDA_HALNC,D0KZ82,Prot2Text,Bacteria,216,"McdA and McdB together mediate carboxysome positioning on the nucleoid and prevent their aggregation in the cell. McdA is an ATPase that forms dynamic gradients on the nucleoid in response to adapter protein McdB, which associates with carboxysomes. The interplay between McdA gradients on the nucleoid and McdB-bound carboxysomes result in the equal spacing of Cbs along the cell length.","A key translational regulator that binds to the 70S ribosome and controls its translation. Acts by interacting with the 5'-UTR of target mRNAs, leading to their degradation.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016787; GO:0046872,GO:0003723,,GO:0003723,GO:0003723,GO:0003723; GO:0043022,0.237,,0.237,0.237,0.2366,4,0.2369,0.3369,no
MCDA_HALNC,D0KZ82,ProtT3,Bacteria,216,"McdA and McdB together mediate carboxysome positioning on the nucleoid and prevent their aggregation in the cell. McdA is an ATPase that forms dynamic gradients on the nucleoid in response to adapter protein McdB, which associates with carboxysomes. The interplay between McdA gradients on the nucleoid and McdB-bound carboxysomes result in the equal spacing of Cbs along the cell length.",Belongs to the ParA family,Vague,Vague,Maybe,Vague,Vague,not-Yes,GO:0005524; GO:0016787; GO:0046872,GO:0016887; GO:0005524,,GO:0016887; GO:0005524,GO:0005524; GO:0016887,GO:0016887; GO:0005524,0.6457,,0.6457,0.6457,0.6457,4,0.6457,0.3369,no
MCDA_HALNC,D0KZ82,ProtTale,Bacteria,216,"McdA and McdB together mediate carboxysome positioning on the nucleoid and prevent their aggregation in the cell. McdA is an ATPase that forms dynamic gradients on the nucleoid in response to adapter protein McdB, which associates with carboxysomes. The interplay between McdA gradients on the nucleoid and McdB-bound carboxysomes result in the equal spacing of Cbs along the cell length.",Acts as an ATPase. May play a role in viral DNA replication. Binds to DNA in a non-specific manner.,No,Maybe,No,Maybe,No,not-Yes,GO:0005524; GO:0016787; GO:0046872,GO:0005524; GO:0003677,GO:0005524; GO:0016887; GO:0003677,GO:0016887; GO:0003677; GO:0005524,GO:0016887; GO:0003677; GO:0005524,GO:0016887; GO:0005524; GO:0003677,0.5574,0.5855,0.5855,0.5855,0.5855,5,0.5799,0.3369,no
MCDA_HALNC,D0KZ82,Protein2Text,Bacteria,216,"McdA and McdB together mediate carboxysome positioning on the nucleoid and prevent their aggregation in the cell. McdA is an ATPase that forms dynamic gradients on the nucleoid in response to adapter protein McdB, which associates with carboxysomes. The interplay between McdA gradients on the nucleoid and McdB-bound carboxysomes result in the equal spacing of Cbs along the cell length.",The molecular function of this protein is as a recombinase.,No,No,No,No,No,not-Yes,GO:0005524; GO:0016787; GO:0046872,GO:0000150,GO:0000150,GO:0000150,GO:0009009,GO:0009009,0.2455,0.2455,0.2455,0.2137,0.2137,5,0.2328,0.3369,no
MCDA_HALNC,D0KZ82,Reference,Bacteria,216,"McdA and McdB together mediate carboxysome positioning on the nucleoid and prevent their aggregation in the cell. McdA is an ATPase that forms dynamic gradients on the nucleoid in response to adapter protein McdB, which associates with carboxysomes. The interplay between McdA gradients on the nucleoid and McdB-bound carboxysomes result in the equal spacing of Cbs along the cell length.","McdA and McdB together mediate carboxysome positioning on the nucleoid and prevent their aggregation in the cell. McdA is an ATPase that forms dynamic gradients on the nucleoid in response to adapter protein McdB, which associates with carboxysomes. The interplay between McdA gradients on the nucleoid and McdB-bound carboxysomes result in the equal spacing of Cbs along the cell length.",,,,,,,GO:0005524; GO:0016787; GO:0046872,GO:0016887; GO:0005524; GO:0003677,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.5855,0.6457,0.6457,0.6457,0.6457,5,0.6337,0.3369,no
MTQ2_HALVD,D4GW96,ESM2Text,Archaea,198,Catalyzes the methylation of the peptide chain release factor subunit 1 on the glutamine residue of the universally conserved GGQ motif. Activity requires the elongation factor 1- alpha (HvoaRF3) and GTP.,Specifically methylates the adenine in position 1618 of 23S rRNA.,No,No,No,No,No,not-Yes,GO:0003676; GO:0102559,GO:0008649,GO:0008168,GO:0008649,GO:0008173,GO:0008173,0.3268,0.4325,0.3268,0.3261,0.3261,5,0.3477,0.3356,no
MTQ2_HALVD,D4GW96,Prot2Text,Archaea,198,Catalyzes the methylation of the peptide chain release factor subunit 1 on the glutamine residue of the universally conserved GGQ motif. Activity requires the elongation factor 1- alpha (HvoaRF3) and GTP.,Methylates cellular RNA.,Vague,No,Vague,Vague,Maybe,not-Yes,GO:0003676; GO:0102559,GO:0008173,GO:0008173,GO:0008173,GO:0008173,GO:0008173,0.3261,0.3261,0.3261,0.3261,0.3261,5,0.3261,0.3356,no
MTQ2_HALVD,D4GW96,ProtT3,Archaea,198,Catalyzes the methylation of the peptide chain release factor subunit 1 on the glutamine residue of the universally conserved GGQ motif. Activity requires the elongation factor 1- alpha (HvoaRF3) and GTP.,Protein-lysine N-methyltransferase that catalyzes the formation of omega-N monomethylarginine (MMA). Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family,No,Maybe,No,No,No,not-Yes,GO:0003676; GO:0102559,GO:0008276,GO:0016274,GO:0008276,GO:0016274,GO:0008276,0.5343,0.5222,0.5343,0.5222,0.5343,5,0.5295,0.3356,no
MTQ2_HALVD,D4GW96,ProtTale,Archaea,198,Catalyzes the methylation of the peptide chain release factor subunit 1 on the glutamine residue of the universally conserved GGQ motif. Activity requires the elongation factor 1- alpha (HvoaRF3) and GTP.,"Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.",No,No,No,No,No,not-Yes,GO:0003676; GO:0102559,GO:0016765,GO:0004659,GO:0008412,GO:0016765,GO:0016765,0.2905,0.2431,0.2083,0.2905,0.2905,5,0.2646,0.3356,no
MTQ2_HALVD,D4GW96,Protein2Text,Archaea,198,Catalyzes the methylation of the peptide chain release factor subunit 1 on the glutamine residue of the universally conserved GGQ motif. Activity requires the elongation factor 1- alpha (HvoaRF3) and GTP.,"The molecular function of this protein is a methyltransferase, specifically involved in the transfer of a methyl group.
 
 This protein catalyzes the transfer of a methyl group to a substrate, which is an important step in various biological processes.",Maybe,Vague,Vague,Vague,Maybe,not-Yes,GO:0003676; GO:0102559,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.4325,0.4325,0.4325,0.4325,0.4325,5,0.4325,0.3356,no
MTQ2_HALVD,D4GW96,Reference,Archaea,198,Catalyzes the methylation of the peptide chain release factor subunit 1 on the glutamine residue of the universally conserved GGQ motif. Activity requires the elongation factor 1- alpha (HvoaRF3) and GTP.,Catalyzes the methylation of the peptide chain release factor subunit 1 on the glutamine residue of the universally conserved GGQ motif. Activity requires the elongation factor 1- alpha (HvoaRF3) and GTP.,,,,,,,GO:0003676; GO:0102559,GO:0008276,GO:0008276,GO:0008276,GO:0008168,GO:0008168,0.5343,0.5343,0.5343,0.4325,0.4325,5,0.4936,0.3356,no
PMI_STRVT,D9XF46,ESM2Text,Bacteria,894,"Isomerase involved in the biosynthesis of phosphinothricin tripeptide (PTT), also known as bialaphos (BA), a natural-product antibiotic and potent herbicide. Probably catalyzes the isomerization of phosphinomethylmalate to phosphinomethylisomalate. Shows no standard aconitase activity with citrate as a substrate and is not able to complement an acnA mutant.","Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Could catalyze the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnA functions as a RNA-binding regulatory protein.",No,No,Maybe,No,Maybe,not-Yes,GO:0051539; GO:0016829; GO:0046872,GO:0003994,GO:0003994,GO:0003994,GO:0003994,GO:0003994,0.3454,0.3454,0.3454,0.3454,0.3454,5,0.3454,0.396,no
PMI_STRVT,D9XF46,Prot2Text,Bacteria,894,"Isomerase involved in the biosynthesis of phosphinothricin tripeptide (PTT), also known as bialaphos (BA), a natural-product antibiotic and potent herbicide. Probably catalyzes the isomerization of phosphinomethylmalate to phosphinomethylisomalate. Shows no standard aconitase activity with citrate as a substrate and is not able to complement an acnA mutant.","Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Could catalyze the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnA functions as a RNA-binding regulatory protein.",No,No,Maybe,No,Maybe,not-Yes,GO:0051539; GO:0016829; GO:0046872,GO:0003994,GO:0003994,GO:0003994,GO:0003994,GO:0003994,0.3454,0.3454,0.3454,0.3454,0.3454,5,0.3454,0.396,no
PMI_STRVT,D9XF46,ProtT3,Bacteria,894,"Isomerase involved in the biosynthesis of phosphinothricin tripeptide (PTT), also known as bialaphos (BA), a natural-product antibiotic and potent herbicide. Probably catalyzes the isomerization of phosphinomethylmalate to phosphinomethylisomalate. Shows no standard aconitase activity with citrate as a substrate and is not able to complement an acnA mutant.","Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis- aconitate. Could catalyze the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnA functions as a RNA-binding regulatory protein. Belongs to",No,No,Maybe,No,Vague,not-Yes,GO:0051539; GO:0016829; GO:0046872,GO:0003994,GO:0003994,GO:0003994,GO:0003994; GO:0051539,GO:0003994,0.3454,0.3454,0.3454,0.7085,0.3454,5,0.418,0.396,no
PMI_STRVT,D9XF46,ProtTale,Bacteria,894,"Isomerase involved in the biosynthesis of phosphinothricin tripeptide (PTT), also known as bialaphos (BA), a natural-product antibiotic and potent herbicide. Probably catalyzes the isomerization of phosphinomethylmalate to phosphinomethylisomalate. Shows no standard aconitase activity with citrate as a substrate and is not able to complement an acnA mutant.",Catalyzes the reversible oxidation of malate to oxaloacetate.,No,Maybe,Maybe,No,Maybe,not-Yes,GO:0051539; GO:0016829; GO:0046872,GO:0016615,GO:0004459,GO:0016615,GO:0016615,GO:0016615,0.2558,0.1621,0.2558,0.2558,0.2558,5,0.2371,0.396,no
PMI_STRVT,D9XF46,Protein2Text,Bacteria,894,"Isomerase involved in the biosynthesis of phosphinothricin tripeptide (PTT), also known as bialaphos (BA), a natural-product antibiotic and potent herbicide. Probably catalyzes the isomerization of phosphinomethylmalate to phosphinomethylisomalate. Shows no standard aconitase activity with citrate as a substrate and is not able to complement an acnA mutant.","This protein is a type of oxidoreductase, which is an enzyme that catalyzes the transfer of electrons from one molecule to another. More specifically, it is a dihydroorotate dehydrogenase, which is a flavin-dependent oxidoreductase that catalyzes the oxidation of dihydroorotate to orotate in the de novo biosynthesis of pyrimidine nucleotides.",No,No,No,No,No,not-Yes,GO:0051539; GO:0016829; GO:0046872,GO:0001339,GO:0004152,GO:0004152,GO:0004152,GO:0004152,0.0,0.2558,0.2558,0.2558,0.2558,5,0.2046,0.396,no
PMI_STRVT,D9XF46,Reference,Bacteria,894,"Isomerase involved in the biosynthesis of phosphinothricin tripeptide (PTT), also known as bialaphos (BA), a natural-product antibiotic and potent herbicide. Probably catalyzes the isomerization of phosphinomethylmalate to phosphinomethylisomalate. Shows no standard aconitase activity with citrate as a substrate and is not able to complement an acnA mutant.","Isomerase involved in the biosynthesis of phosphinothricin tripeptide (PTT), also known as bialaphos (BA), a natural-product antibiotic and potent herbicide. Probably catalyzes the isomerization of phosphinomethylmalate to phosphinomethylisomalate. Shows no standard aconitase activity with citrate as a substrate and is not able to complement an acnA mutant.",,,,,,,GO:0051539; GO:0016829; GO:0046872,GO:0016853,GO:0016853,GO:0016853,GO:0016836,GO:0016853,0.374,0.374,0.374,0.3972,0.374,5,0.3786,0.396,no
GFSG_STRHA,E0D208,ESM2Text,Bacteria,278,Methylase required for synthesis of the 16-membered macrolide antibiotics FD-891 and FD-892. In vitro uses S-adenosyl-L-methionine to methylate a number of biosynthetic intermediates in the synthesis of FD-891.,"Catalyzes the methylation of three of the C-3 methyl groups of ent-kaurene giving kaurenoic acid, a key step in alkaloid biosynthesis. Can also methylate farnesoate to methyl farnesoate and methyl farnesoate to methyl farnesoate.",No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008757,,,,,,,,,,,0,,0.2027,no
GFSG_STRHA,E0D208,Prot2Text,Bacteria,278,Methylase required for synthesis of the 16-membered macrolide antibiotics FD-891 and FD-892. In vitro uses S-adenosyl-L-methionine to methylate a number of biosynthetic intermediates in the synthesis of FD-891.,Catalyzes the methylation of dimethylglycine to betaine with S-adenosylmethionine (AdoMet) acting as the methyl donor. It has strict specificity for dimethylglycine as the methyl group acceptors.,No,Maybe,Maybe,No,Maybe,not-Yes,GO:0008757,GO:0008168,,GO:0008168,GO:0008168,GO:0008168,0.8582,,0.8582,0.8582,0.8582,4,0.8582,0.2027,no
GFSG_STRHA,E0D208,ProtT3,Bacteria,278,Methylase required for synthesis of the 16-membered macrolide antibiotics FD-891 and FD-892. In vitro uses S-adenosyl-L-methionine to methylate a number of biosynthetic intermediates in the synthesis of FD-891.,S-adenosyl-L-methionine-dependent methyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008757,GO:0008168,GO:0008171,GO:0008757,GO:0008168,GO:0008168,0.8582,0.7289,1.0,0.8582,0.8582,5,0.8607,0.2027,no
GFSG_STRHA,E0D208,ProtTale,Bacteria,278,Methylase required for synthesis of the 16-membered macrolide antibiotics FD-891 and FD-892. In vitro uses S-adenosyl-L-methionine to methylate a number of biosynthetic intermediates in the synthesis of FD-891.,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin citrinin, a hepato-nephrotoxic compound to humans due to inhibition of respiration complex III. The pathway begins with the synthesis of a keto-aldehyde intermediate by the citrinin PKS (pksCT) from successive condensations of 4 malonyl-CoA units, presumably with a simple acetyl-CoA starter unit. Release of the keto-aldehyde intermediate is consistent with the presence of the C-terminal reductive release domain. pksCT is also able to catalyze the reverse reaction, i.e. catalyze the",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008757,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.2027,no
GFSG_STRHA,E0D208,Protein2Text,Bacteria,278,Methylase required for synthesis of the 16-membered macrolide antibiotics FD-891 and FD-892. In vitro uses S-adenosyl-L-methionine to methylate a number of biosynthetic intermediates in the synthesis of FD-891.,"The molecular function of this protein is an O-methyltransferase. It catalyzes the transfer of a methyl group to a substrate, likely involved in the biosynthesis of a methylated compound. More specifically, it is involved in the O-methylation of a compound, possibly a nucleoside or a sugar. This protein is likely involved in the production of a methylated compound, such as a methylated nucleoside or a methylated sugar, which may have a role in cellular metabolism or signaling.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008757,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.2027,no
GFSG_STRHA,E0D208,Reference,Bacteria,278,Methylase required for synthesis of the 16-membered macrolide antibiotics FD-891 and FD-892. In vitro uses S-adenosyl-L-methionine to methylate a number of biosynthetic intermediates in the synthesis of FD-891.,Methylase required for synthesis of the 16-membered macrolide antibiotics FD-891 and FD-892. In vitro uses S-adenosyl-L-methionine to methylate a number of biosynthetic intermediates in the synthesis of FD-891.,,,,,,,GO:0008757,GO:0008757,GO:0008757,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,0.8582,0.8582,0.8582,5,0.9149,0.2027,no
PAMT_CAPAN,E1AQY3,ESM2Text,Eukaryota,459,"Involved in the biosynthesis of capsaicinoids natural products, pungent alkaloids synthesized from phenylpropanoid intermediates in the placental tissue of chili pepper fruit acting as repellant on herbivorous mammals and conferring spiciness to hot peppers. Can transfer an amine from vanillylamine to pyruvate forming vanillin and L-alanine.","Participates in the biosynthesis of capsaicinoids in pungent cultivars of Capsicum frutescens. Capsaicinoids, the alkaloids responsible for the heat or pungency of chili pepper, are synthesized from phenylpropanoid intermediates in the placental tissue of chili peper fruit (Probable). Can transfer an amine from alanine to vanillin, forming vanillylamine and pyruvate.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004015; GO:0030170,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.599,0.599,0.599,0.599,0.599,5,0.599,0.1402,no
PAMT_CAPAN,E1AQY3,Prot2Text,Eukaryota,459,"Involved in the biosynthesis of capsaicinoids natural products, pungent alkaloids synthesized from phenylpropanoid intermediates in the placental tissue of chili pepper fruit acting as repellant on herbivorous mammals and conferring spiciness to hot peppers. Can transfer an amine from vanillylamine to pyruvate forming vanillin and L-alanine.","Participates in the biosynthesis of capsaicinoids in pungent cultivars of Capsicum frutescens. Capsaicinoids, the alkaloids responsible for the heat or pungency of chili pepper, are synthesized from phenylpropanoid intermediates in the placental tissue of chili peper fruit (Probable). Can transfer an amine from alanine to vanillin, forming vanillylamine and pyruvate.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004015; GO:0030170,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.599,0.599,0.599,0.599,0.599,5,0.599,0.1402,no
PAMT_CAPAN,E1AQY3,ProtT3,Eukaryota,459,"Involved in the biosynthesis of capsaicinoids natural products, pungent alkaloids synthesized from phenylpropanoid intermediates in the placental tissue of chili pepper fruit acting as repellant on herbivorous mammals and conferring spiciness to hot peppers. Can transfer an amine from vanillylamine to pyruvate forming vanillin and L-alanine.",Mitochondrion. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004015; GO:0030170,GO:0008483; GO:0030170,GO:0008483; GO:0030170,GO:0008483; GO:0030170,GO:0008483; GO:0030170,GO:0008483,0.9291,0.9291,0.9291,0.9291,0.599,5,0.8631,0.1402,no
PAMT_CAPAN,E1AQY3,ProtTale,Eukaryota,459,"Involved in the biosynthesis of capsaicinoids natural products, pungent alkaloids synthesized from phenylpropanoid intermediates in the placental tissue of chili pepper fruit acting as repellant on herbivorous mammals and conferring spiciness to hot peppers. Can transfer an amine from vanillylamine to pyruvate forming vanillin and L-alanine.","Catalyzes the transfer of the alpha-amino group from S- adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase known to use SAM as an amino donor.",No,No,Maybe,No,No,not-Yes,GO:0004015; GO:0030170,GO:0004015,GO:0004015,GO:0004015,GO:0008483,GO:0004015; GO:0008483,0.6898,0.6898,0.6898,0.599,0.7347,5,0.6806,0.1402,no
PAMT_CAPAN,E1AQY3,Protein2Text,Eukaryota,459,"Involved in the biosynthesis of capsaicinoids natural products, pungent alkaloids synthesized from phenylpropanoid intermediates in the placental tissue of chili pepper fruit acting as repellant on herbivorous mammals and conferring spiciness to hot peppers. Can transfer an amine from vanillylamine to pyruvate forming vanillin and L-alanine.","This protein has the molecular function of a transaminase, which is an enzyme that catalyzes the transfer of an amino group from an amino acid to a keto acid. More specifically, it is involved in the conversion of L-phenylalanine to phenylpyruvate.",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0004015; GO:0030170,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.599,0.599,0.599,0.599,0.599,5,0.599,0.1402,no
PAMT_CAPAN,E1AQY3,Reference,Eukaryota,459,"Involved in the biosynthesis of capsaicinoids natural products, pungent alkaloids synthesized from phenylpropanoid intermediates in the placental tissue of chili pepper fruit acting as repellant on herbivorous mammals and conferring spiciness to hot peppers. Can transfer an amine from vanillylamine to pyruvate forming vanillin and L-alanine.","Involved in the biosynthesis of capsaicinoids natural products, pungent alkaloids synthesized from phenylpropanoid intermediates in the placental tissue of chili pepper fruit acting as repellant on herbivorous mammals and conferring spiciness to hot peppers. Can transfer an amine from vanillylamine to pyruvate forming vanillin and L-alanine.",,,,,,,GO:0004015; GO:0030170,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.599,0.599,0.599,0.599,0.599,5,0.599,0.1402,no
THUM2_BOVIN,E1B8U2,ESM2Text,Eukaryota,501,"Catalytic subunit of the THUMPD2-TRM112 methyltransferase complex, that specifically mediates the S-adenosyl-L-methionine- dependent N(2)-methylation of guanosine nucleotides, most probably at position 72 (m2G72), in the U6snRNA of the major spliceosome. This modification in the U6 snRNA affects the constitutive splicing efficiency of introns that have suboptimal splice sites and can impact final mRNA levels.",Catalytic subunit of a heterodimeric complex that specifically mediates the methylation of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. The nuclease activity is required for the methylation of guanosine-37.,Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0003723; GO:0106346; GO:0016423; GO:0160230,GO:0008173,GO:0008173,GO:0008168,GO:0008176,GO:0008173,0.6974,0.6974,0.5205,0.6162,0.6974,5,0.6458,0.6435,yes
THUM2_BOVIN,E1B8U2,Prot2Text,Eukaryota,501,"Catalytic subunit of the THUMPD2-TRM112 methyltransferase complex, that specifically mediates the S-adenosyl-L-methionine- dependent N(2)-methylation of guanosine nucleotides, most probably at position 72 (m2G72), in the U6snRNA of the major spliceosome. This modification in the U6 snRNA affects the constitutive splicing efficiency of introns that have suboptimal splice sites and can impact final mRNA levels.","RNA methyltransferase that specifically methylates the N(7) position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding.",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0003723; GO:0106346; GO:0016423; GO:0160230,GO:0008176,GO:0008176,GO:0008176,GO:0008176,GO:0008176,0.6162,0.6162,0.6162,0.6162,0.6162,5,0.6162,0.6435,yes
THUM2_BOVIN,E1B8U2,ProtT3,Eukaryota,501,"Catalytic subunit of the THUMPD2-TRM112 methyltransferase complex, that specifically mediates the S-adenosyl-L-methionine- dependent N(2)-methylation of guanosine nucleotides, most probably at position 72 (m2G72), in the U6snRNA of the major spliceosome. This modification in the U6 snRNA affects the constitutive splicing efficiency of introns that have suboptimal splice sites and can impact final mRNA levels.",Belongs to the methyltransferase superfamily,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0003723; GO:0106346; GO:0016423; GO:0160230,GO:0008168,,,GO:0008168,GO:0008168,0.5205,,,0.5205,0.5205,3,0.5205,0.6435,yes
THUM2_BOVIN,E1B8U2,ProtTale,Eukaryota,501,"Catalytic subunit of the THUMPD2-TRM112 methyltransferase complex, that specifically mediates the S-adenosyl-L-methionine- dependent N(2)-methylation of guanosine nucleotides, most probably at position 72 (m2G72), in the U6snRNA of the major spliceosome. This modification in the U6 snRNA affects the constitutive splicing efficiency of introns that have suboptimal splice sites and can impact final mRNA levels.",Probable methyltransferase.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0003723; GO:0106346; GO:0016423; GO:0160230,,,,,,,,,,,0,,0.6435,yes
THUM2_BOVIN,E1B8U2,Protein2Text,Eukaryota,501,"Catalytic subunit of the THUMPD2-TRM112 methyltransferase complex, that specifically mediates the S-adenosyl-L-methionine- dependent N(2)-methylation of guanosine nucleotides, most probably at position 72 (m2G72), in the U6snRNA of the major spliceosome. This modification in the U6 snRNA affects the constitutive splicing efficiency of introns that have suboptimal splice sites and can impact final mRNA levels.",The molecular function of this protein is a methyltransferase.,Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0003723; GO:0106346; GO:0016423; GO:0160230,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.5205,0.5205,0.5205,0.5205,0.5205,5,0.5205,0.6435,yes
THUM2_BOVIN,E1B8U2,Reference,Eukaryota,501,"Catalytic subunit of the THUMPD2-TRM112 methyltransferase complex, that specifically mediates the S-adenosyl-L-methionine- dependent N(2)-methylation of guanosine nucleotides, most probably at position 72 (m2G72), in the U6snRNA of the major spliceosome. This modification in the U6 snRNA affects the constitutive splicing efficiency of introns that have suboptimal splice sites and can impact final mRNA levels.","Catalytic subunit of the THUMPD2-TRM112 methyltransferase complex, that specifically mediates the S-adenosyl-L-methionine- dependent N(2)-methylation of guanosine nucleotides, most probably at position 72 (m2G72), in the U6snRNA of the major spliceosome. This modification in the U6 snRNA affects the constitutive splicing efficiency of introns that have suboptimal splice sites and can impact final mRNA levels.",,,,,,,GO:0003723; GO:0106346; GO:0016423; GO:0160230,GO:0008173,GO:0008173,GO:0008173,GO:0008173,GO:0008173,0.6974,0.6974,0.6974,0.6974,0.6974,5,0.6974,0.6435,yes
LIP4_MALFU,E1CJK2,ESM2Text,Eukaryota,526,"Secreted lipase that hydrolyzes acylglycerol lipids such as triacylglycerols and consequently releases free fatty acid. Can hydrolyze 4-nitrophenyl palmitate to release 4- nitrophenol and palmitoic acid. Due to an absence of fatty acid synthase genes in Malassezia species, secretory lipases are essential for the yeast to generate free fatty acids from degradation of sebum and assimilate them as lipid sources for growth. Plays important roles not only in lipid metabolism but also in the immune response of host cells and pathogenesis (Probable).",Extracellular esterase that contributes to pathogenicity.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004806,,GO:0016787,,,,,0.5324,,,,1,0.5324,0.3416,no
LIP4_MALFU,E1CJK2,Prot2Text,Eukaryota,526,"Secreted lipase that hydrolyzes acylglycerol lipids such as triacylglycerols and consequently releases free fatty acid. Can hydrolyze 4-nitrophenyl palmitate to release 4- nitrophenol and palmitoic acid. Due to an absence of fatty acid synthase genes in Malassezia species, secretory lipases are essential for the yeast to generate free fatty acids from degradation of sebum and assimilate them as lipid sources for growth. Plays important roles not only in lipid metabolism but also in the immune response of host cells and pathogenesis (Probable).","Upon binding acetylcholine, the enzyme converts the acetylcholine neurotransmitter (ACh) to the artificial choline via an exocyclic (esterase) reaction.",No,No,No,No,No,not-Yes,GO:0004806,GO:0016788,,GO:0016788,GO:0004553,GO:0016787,0.6506,,0.6506,0.358,0.5324,4,0.5479,0.3416,no
LIP4_MALFU,E1CJK2,ProtT3,Eukaryota,526,"Secreted lipase that hydrolyzes acylglycerol lipids such as triacylglycerols and consequently releases free fatty acid. Can hydrolyze 4-nitrophenyl palmitate to release 4- nitrophenol and palmitoic acid. Due to an absence of fatty acid synthase genes in Malassezia species, secretory lipases are essential for the yeast to generate free fatty acids from degradation of sebum and assimilate them as lipid sources for growth. Plays important roles not only in lipid metabolism but also in the immune response of host cells and pathogenesis (Probable).",Belongs to the AB hydrolase superfamily,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004806,GO:0016298,GO:0004806,GO:0004806,GO:0004806,GO:0016298,0.7707,1.0,1.0,1.0,0.7707,5,0.9083,0.3416,no
LIP4_MALFU,E1CJK2,ProtTale,Eukaryota,526,"Secreted lipase that hydrolyzes acylglycerol lipids such as triacylglycerols and consequently releases free fatty acid. Can hydrolyze 4-nitrophenyl palmitate to release 4- nitrophenol and palmitoic acid. Due to an absence of fatty acid synthase genes in Malassezia species, secretory lipases are essential for the yeast to generate free fatty acids from degradation of sebum and assimilate them as lipid sources for growth. Plays important roles not only in lipid metabolism but also in the immune response of host cells and pathogenesis (Probable).","Secreted lipase involved in Dandruff and seborrheic dermatitis (D/SD) probably via lipase-mediated breakdown of sebaceous lipids and release of irritating free fatty acids (Probable). Shows lipase activity towards p-nitrophenyl palmitate (p-NPP) and triolein, releasing free fatty acids that may cause skin irritation (Probable).",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3416,no
LIP4_MALFU,E1CJK2,Protein2Text,Eukaryota,526,"Secreted lipase that hydrolyzes acylglycerol lipids such as triacylglycerols and consequently releases free fatty acid. Can hydrolyze 4-nitrophenyl palmitate to release 4- nitrophenol and palmitoic acid. Due to an absence of fatty acid synthase genes in Malassezia species, secretory lipases are essential for the yeast to generate free fatty acids from degradation of sebum and assimilate them as lipid sources for growth. Plays important roles not only in lipid metabolism but also in the immune response of host cells and pathogenesis (Probable).","The molecular function of this protein is to break down fatty acids, specifically a lipase enzyme that is involved in the hydrolysis of triglycerides. More precisely, it is involved in the degradation of triglycerides, which are the main components of fats and oils. This protein is likely involved in the metabolism of fatty acids, breaking them down into simpler molecules that can be used by the cell for energy or other purposes.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004806,GO:0004091,GO:0004091,GO:0016788,GO:0004091,GO:0004091,0.7707,0.7707,0.6506,0.7707,0.7707,5,0.7467,0.3416,no
LIP4_MALFU,E1CJK2,Reference,Eukaryota,526,"Secreted lipase that hydrolyzes acylglycerol lipids such as triacylglycerols and consequently releases free fatty acid. Can hydrolyze 4-nitrophenyl palmitate to release 4- nitrophenol and palmitoic acid. Due to an absence of fatty acid synthase genes in Malassezia species, secretory lipases are essential for the yeast to generate free fatty acids from degradation of sebum and assimilate them as lipid sources for growth. Plays important roles not only in lipid metabolism but also in the immune response of host cells and pathogenesis (Probable).","Secreted lipase that hydrolyzes acylglycerol lipids such as triacylglycerols and consequently releases free fatty acid. Can hydrolyze 4-nitrophenyl palmitate to release 4- nitrophenol and palmitoic acid. Due to an absence of fatty acid synthase genes in Malassezia species, secretory lipases are essential for the yeast to generate free fatty acids from degradation of sebum and assimilate them as lipid sources for growth. Plays important roles not only in lipid metabolism but also in the immune response of host cells and pathogenesis (Probable).",,,,,,,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3416,no
FIGL2_DANRE,E9QEA3,ESM2Text,Eukaryota,684,"Microtubule-severing enzyme that negatively regulates cell migration and wound healing. In migrating cells, targets dynamic microtubules (MTs) at the leading edge and severs them, thereby suppressing motility. Negative regulator of axon regeneration that suppresses axonal growth by selectively severing dynamic MTs in the distal axon shaft and growth cone. Contributes to proper cell branching during endothelial and neuronal development.","May be involved in transcriptional regulation. Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016887; GO:0008568,,,,,,,,,,,0,,0.3541,no
FIGL2_DANRE,E9QEA3,Prot2Text,Eukaryota,684,"Microtubule-severing enzyme that negatively regulates cell migration and wound healing. In migrating cells, targets dynamic microtubules (MTs) at the leading edge and severs them, thereby suppressing motility. Negative regulator of axon regeneration that suppresses axonal growth by selectively severing dynamic MTs in the distal axon shaft and growth cone. Contributes to proper cell branching during endothelial and neuronal development.",Required for proper positioning of nuclei at birth. May be involved in maintaining the suppression of distal tip cell migration during the G1/S transition.,No,No,Vague,No,No,not-Yes,GO:0005524; GO:0016887; GO:0008568,,,,,,,,,,,0,,0.3541,no
FIGL2_DANRE,E9QEA3,ProtT3,Eukaryota,684,"Microtubule-severing enzyme that negatively regulates cell migration and wound healing. In migrating cells, targets dynamic microtubules (MTs) at the leading edge and severs them, thereby suppressing motility. Negative regulator of axon regeneration that suppresses axonal growth by selectively severing dynamic MTs in the distal axon shaft and growth cone. Contributes to proper cell branching during endothelial and neuronal development.",Belongs to the AAA ATPase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0016887; GO:0008568,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.8556,0.8556,0.8556,0.8556,0.8556,5,0.8556,0.3541,no
FIGL2_DANRE,E9QEA3,ProtTale,Eukaryota,684,"Microtubule-severing enzyme that negatively regulates cell migration and wound healing. In migrating cells, targets dynamic microtubules (MTs) at the leading edge and severs them, thereby suppressing motility. Negative regulator of axon regeneration that suppresses axonal growth by selectively severing dynamic MTs in the distal axon shaft and growth cone. Contributes to proper cell branching during endothelial and neuronal development.",May be involved in the regulation of cell growth. May be involved in the phosphorylation of AKT1 on 'Ser-473' during insulin-like growth factor-1 (IGF-1) signaling. Plays a role in the phosphorylation of AKT2 on 'Ser-473' during IGF-1 signaling. Required for the phosphorylation of AKT1 and AKT2 on 'Ser-473' in response to IGF-1. Required for the phosphorylation of S6K1 on 'Ser-288' and 'Ser-308' in response to IGF-,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0016887; GO:0008568,,,,,,,,,,,0,,0.3541,no
FIGL2_DANRE,E9QEA3,Protein2Text,Eukaryota,684,"Microtubule-severing enzyme that negatively regulates cell migration and wound healing. In migrating cells, targets dynamic microtubules (MTs) at the leading edge and severs them, thereby suppressing motility. Negative regulator of axon regeneration that suppresses axonal growth by selectively severing dynamic MTs in the distal axon shaft and growth cone. Contributes to proper cell branching during endothelial and neuronal development.","This protein is a transcription factor, which means it plays a crucial role in regulating gene expression. It binds to specific DNA sequences and activates or represses the transcription of target genes.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016887; GO:0008568,GO:0003700; GO:0003677,GO:0003700,GO:0003700,GO:0003700,GO:0003700,0.1525,0.1297,0.1297,0.1297,0.1297,5,0.1343,0.3541,no
FIGL2_DANRE,E9QEA3,Reference,Eukaryota,684,"Microtubule-severing enzyme that negatively regulates cell migration and wound healing. In migrating cells, targets dynamic microtubules (MTs) at the leading edge and severs them, thereby suppressing motility. Negative regulator of axon regeneration that suppresses axonal growth by selectively severing dynamic MTs in the distal axon shaft and growth cone. Contributes to proper cell branching during endothelial and neuronal development.","Microtubule-severing enzyme that negatively regulates cell migration and wound healing. In migrating cells, targets dynamic microtubules (MTs) at the leading edge and severs them, thereby suppressing motility. Negative regulator of axon regeneration that suppresses axonal growth by selectively severing dynamic MTs in the distal axon shaft and growth cone. Contributes to proper cell branching during endothelial and neuronal development.",,,,,,,GO:0005524; GO:0016887; GO:0008568,GO:0008568,GO:0008568,GO:0008568,GO:0008568,GO:0008568,0.5851,0.5851,0.5851,0.5851,0.5851,5,0.5851,0.3541,no
LGDH_PSEPM,F0M433,ESM2Text,Bacteria,390,"Catalyzes the oxidation of levoglucosan (1,6-anhydro-beta-D- glucose, LG) to 3-dehydrolevoglucosan (3-keto-LG). Exhibits high substrate specificity toward levoglucosan and NAD(+) for the oxidative reaction. Exhibits weak activities (about 4% compared with that of LG) toward L-sorbose and 1,5-anhydro-D- glucitol, and activity toward D-xylose is also detectable (1.7%). Can also efficiently catalyzes the NADH-dependent reduction (reverse reaction) of 3-keto-LG.","Involved in the degradation of D-galactose, a major component of hemikaryotic cell walls. Catalyzes the reduction of D-galactose to D-tagatose.",No,No,No,No,No,not-Yes,GO:0000166; GO:0016491,,GO:0016491,,,,,0.7229,,,,1,0.7229,0.1072,no
LGDH_PSEPM,F0M433,Prot2Text,Bacteria,390,"Catalyzes the oxidation of levoglucosan (1,6-anhydro-beta-D- glucose, LG) to 3-dehydrolevoglucosan (3-keto-LG). Exhibits high substrate specificity toward levoglucosan and NAD(+) for the oxidative reaction. Exhibits weak activities (about 4% compared with that of LG) toward L-sorbose and 1,5-anhydro-D- glucitol, and activity toward D-xylose is also detectable (1.7%). Can also efficiently catalyzes the NADH-dependent reduction (reverse reaction) of 3-keto-LG.","NADP-dependent D-xylose dehydrogenase involved in the degradation of D-xylose, a major component of hemicelluloses such as xylan. Catalyzes the NADP(+)-dependent oxidation of D-xylose.",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0000166; GO:0016491,GO:0016614,,GO:0016491,GO:0047837,GO:0016614,0.5895,,0.7229,0.4359,0.5895,4,0.5845,0.1072,no
LGDH_PSEPM,F0M433,ProtT3,Bacteria,390,"Catalyzes the oxidation of levoglucosan (1,6-anhydro-beta-D- glucose, LG) to 3-dehydrolevoglucosan (3-keto-LG). Exhibits high substrate specificity toward levoglucosan and NAD(+) for the oxidative reaction. Exhibits weak activities (about 4% compared with that of LG) toward L-sorbose and 1,5-anhydro-D- glucitol, and activity toward D-xylose is also detectable (1.7%). Can also efficiently catalyzes the NADH-dependent reduction (reverse reaction) of 3-keto-LG.",Involved in the degradation of D-xylose. Catalyzes the oxidation of D-xylose to 2-keto-3-deoxy- D-xylose (KDX). Cell membrane; Multi-pass membrane protein. Belongs to the Gfo/Idh/MocA family,No,Maybe,Maybe,Maybe,Vague,not-Yes,GO:0000166; GO:0016491,GO:0016614,GO:0016491,GO:0016491,GO:0016491,GO:0016614,0.5895,0.7229,0.7229,0.7229,0.5895,5,0.6695,0.1072,no
LGDH_PSEPM,F0M433,ProtTale,Bacteria,390,"Catalyzes the oxidation of levoglucosan (1,6-anhydro-beta-D- glucose, LG) to 3-dehydrolevoglucosan (3-keto-LG). Exhibits high substrate specificity toward levoglucosan and NAD(+) for the oxidative reaction. Exhibits weak activities (about 4% compared with that of LG) toward L-sorbose and 1,5-anhydro-D- glucitol, and activity toward D-xylose is also detectable (1.7%). Can also efficiently catalyzes the NADH-dependent reduction (reverse reaction) of 3-keto-LG.",Catalyzes the oxidation of D-xylose to D-xylonate.,No,Maybe,Maybe,Maybe,No,not-Yes,GO:0000166; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016616,GO:0016491,0.7229,0.7229,0.7229,0.4994,0.7229,5,0.6782,0.1072,no
LGDH_PSEPM,F0M433,Protein2Text,Bacteria,390,"Catalyzes the oxidation of levoglucosan (1,6-anhydro-beta-D- glucose, LG) to 3-dehydrolevoglucosan (3-keto-LG). Exhibits high substrate specificity toward levoglucosan and NAD(+) for the oxidative reaction. Exhibits weak activities (about 4% compared with that of LG) toward L-sorbose and 1,5-anhydro-D- glucitol, and activity toward D-xylose is also detectable (1.7%). Can also efficiently catalyzes the NADH-dependent reduction (reverse reaction) of 3-keto-LG.",This protein is a dehydrogenase.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0000166; GO:0016491,GO:0016616,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4994,0.7229,0.7229,0.7229,0.7229,5,0.6782,0.1072,no
LGDH_PSEPM,F0M433,Reference,Bacteria,390,"Catalyzes the oxidation of levoglucosan (1,6-anhydro-beta-D- glucose, LG) to 3-dehydrolevoglucosan (3-keto-LG). Exhibits high substrate specificity toward levoglucosan and NAD(+) for the oxidative reaction. Exhibits weak activities (about 4% compared with that of LG) toward L-sorbose and 1,5-anhydro-D- glucitol, and activity toward D-xylose is also detectable (1.7%). Can also efficiently catalyzes the NADH-dependent reduction (reverse reaction) of 3-keto-LG.","Catalyzes the oxidation of levoglucosan (1,6-anhydro-beta-D- glucose, LG) to 3-dehydrolevoglucosan (3-keto-LG). Exhibits high substrate specificity toward levoglucosan and NAD(+) for the oxidative reaction. Exhibits weak activities (about 4% compared with that of LG) toward L-sorbose and 1,5-anhydro-D- glucitol, and activity toward D-xylose is also detectable (1.7%). Can also efficiently catalyzes the NADH-dependent reduction (reverse reaction) of 3-keto-LG.",,,,,,,GO:0000166; GO:0016491,GO:0016616,GO:0016616,GO:0016616,GO:0016616,GO:0016616,0.4994,0.4994,0.4994,0.4994,0.4994,5,0.4994,0.1072,no
ESP_ANOGA,F1DQG5,ESM2Text,Eukaryota,268,Putative epithelial serine protease.,"Constitutive trypsin that is expressed 2 days after emergence, coinciding with host seeking behavior of the female.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004252,GO:0004252,GO:0004252,GO:0004252,GO:0004252,GO:0004252,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5695,yes
ESP_ANOGA,F1DQG5,Prot2Text,Eukaryota,268,Putative epithelial serine protease.,Has a primary specificity for large aliphatic or aromatic amino acids.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004252,,,GO:0008233,,,,,0.6551,,,1,0.6551,0.5695,yes
ESP_ANOGA,F1DQG5,ProtT3,Eukaryota,268,Putative epithelial serine protease.,"Secreted, extracellular space. Belongs to the peptidase S1 family",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004252,GO:0004252,GO:0004252,GO:0004252,GO:0004252,GO:0004252,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5695,yes
ESP_ANOGA,F1DQG5,ProtTale,Eukaryota,268,Putative epithelial serine protease.,Serine protease with trypsin-like specificity.,Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004252,GO:0004252,GO:0004252,GO:0004252,GO:0004252,GO:0004252,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5695,yes
ESP_ANOGA,F1DQG5,Protein2Text,Eukaryota,268,Putative epithelial serine protease.,The molecular function of this protein is protease activity.,Maybe,Vague,Maybe,Vague,Maybe,not-Yes,GO:0004252,GO:0008233,GO:0008233,GO:0008233,GO:0008233,GO:0008233,0.6551,0.6551,0.6551,0.6551,0.6551,5,0.6551,0.5695,yes
ESP_ANOGA,F1DQG5,Reference,Eukaryota,268,Putative epithelial serine protease.,Putative epithelial serine protease.,,,,,,,GO:0004252,GO:0004252,GO:0004252,GO:0004252,GO:0004252,GO:0004252,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5695,yes
FAH2A_BOVIN,F1MLX0,ESM2Text,Eukaryota,314,"Tautomerase that converts enol-oxaloacetate, a strong inhibitor of succinate dehydrogenase, to the physiological keto form of oxaloacetate. It is thereby required to maximize aerobic respiration efficiency by preventing succinate dehydrogenase inhibition.",May have hydrolase activity.,Vague,No,Vague,No,No,not-Yes,GO:0046872; GO:0050163,,GO:0016787,,,,,0.2894,,,,1,0.2894,0.2839,no
FAH2A_BOVIN,F1MLX0,Prot2Text,Eukaryota,314,"Tautomerase that converts enol-oxaloacetate, a strong inhibitor of succinate dehydrogenase, to the physiological keto form of oxaloacetate. It is thereby required to maximize aerobic respiration efficiency by preventing succinate dehydrogenase inhibition.",May have hydrolase activity.,Vague,No,Vague,No,Vague,not-Yes,GO:0046872; GO:0050163,,,,,,,,,,,0,,0.2839,no
FAH2A_BOVIN,F1MLX0,ProtT3,Eukaryota,314,"Tautomerase that converts enol-oxaloacetate, a strong inhibitor of succinate dehydrogenase, to the physiological keto form of oxaloacetate. It is thereby required to maximize aerobic respiration efficiency by preventing succinate dehydrogenase inhibition.",May have hydrolase activity. Belongs to the FAH family,No,No,Vague,Vague,Vague,not-Yes,GO:0046872; GO:0050163,GO:0004334,,GO:0004334,GO:0004334,GO:0016787,0.1628,,0.1628,0.1628,0.2894,4,0.1945,0.2839,no
FAH2A_BOVIN,F1MLX0,ProtTale,Eukaryota,314,"Tautomerase that converts enol-oxaloacetate, a strong inhibitor of succinate dehydrogenase, to the physiological keto form of oxaloacetate. It is thereby required to maximize aerobic respiration efficiency by preventing succinate dehydrogenase inhibition.",Hydrolyzes L-alanine-alpha-ketoglutarate to pyruvate and L-alanine. May be specific for alpha-ketoacids.,No,No,No,No,No,not-Yes,GO:0046872; GO:0050163,GO:0016787,GO:0008483,GO:0004021,GO:0004021,GO:0004021,0.2894,0.1917,0.1415,0.1415,0.1415,5,0.1811,0.2839,no
FAH2A_BOVIN,F1MLX0,Protein2Text,Eukaryota,314,"Tautomerase that converts enol-oxaloacetate, a strong inhibitor of succinate dehydrogenase, to the physiological keto form of oxaloacetate. It is thereby required to maximize aerobic respiration efficiency by preventing succinate dehydrogenase inhibition.","The molecular function of this protein is a lyase enzyme, specifically a sugar-lyase that catalyzes the hydrolysis of a carbon-nitrogen bond, leading to the formation of a double bond or a cyclic compound. More specifically, it is involved in the breakdown of sugar molecules.",No,No,No,No,No,not-Yes,GO:0046872; GO:0050163,,GO:0016829,,GO:0016829,,,0.2894,,0.2894,,2,0.2894,0.2839,no
FAH2A_BOVIN,F1MLX0,Reference,Eukaryota,314,"Tautomerase that converts enol-oxaloacetate, a strong inhibitor of succinate dehydrogenase, to the physiological keto form of oxaloacetate. It is thereby required to maximize aerobic respiration efficiency by preventing succinate dehydrogenase inhibition.","Tautomerase that converts enol-oxaloacetate, a strong inhibitor of succinate dehydrogenase, to the physiological keto form of oxaloacetate. It is thereby required to maximize aerobic respiration efficiency by preventing succinate dehydrogenase inhibition.",,,,,,,GO:0046872; GO:0050163,GO:0016853,GO:0016853,GO:0016853,GO:0016860,GO:0016853,0.4539,0.4539,0.4539,0.5281,0.4539,5,0.4687,0.2839,no
KDSR_DANRE,F1QWW8,ESM2Text,Eukaryota,332,"Catalyzes the reduction of 3'-oxosphinganine (3- ketodihydrosphingosine/KDS) to sphinganine (dihydrosphingosine/DHS), the second step of de novo sphingolipid biosynthesis.",Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS).,Yes,Yes,Yes,Yes,Yes,Yes,GO:0047560; GO:0070402,GO:0047560,GO:0016491,GO:0047560,GO:0047560,GO:0047560,0.6877,0.4365,0.6877,0.6877,0.6877,5,0.6375,0.3453,no
KDSR_DANRE,F1QWW8,Prot2Text,Eukaryota,332,"Catalyzes the reduction of 3'-oxosphinganine (3- ketodihydrosphingosine/KDS) to sphinganine (dihydrosphingosine/DHS), the second step of de novo sphingolipid biosynthesis.",Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS).,Yes,Yes,Yes,Yes,Yes,Yes,GO:0047560; GO:0070402,GO:0047560,GO:0047560,GO:0047560,GO:0047560,GO:0016491,0.6877,0.6877,0.6877,0.6877,0.4365,5,0.6375,0.3453,no
KDSR_DANRE,F1QWW8,ProtT3,Eukaryota,332,"Catalyzes the reduction of 3'-oxosphinganine (3- ketodihydrosphingosine/KDS) to sphinganine (dihydrosphingosine/DHS), the second step of de novo sphingolipid biosynthesis.",Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS). Endoplasmic reticulum membrane; Multi-pass membrane protein. Belongs to the short-chain dehydrogenases/reductases (SDR) family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0047560; GO:0070402,GO:0047560,GO:0003856,GO:0003856,GO:0047560,GO:0046890,0.6877,0.1542,0.1542,0.6877,0.0,5,0.3368,0.3453,no
KDSR_DANRE,F1QWW8,ProtTale,Eukaryota,332,"Catalyzes the reduction of 3'-oxosphinganine (3- ketodihydrosphingosine/KDS) to sphinganine (dihydrosphingosine/DHS), the second step of de novo sphingolipid biosynthesis.",Catalyzes the reduction of all-trans-retinal to all-trans- retinol in the presence of NADPH.,No,No,No,No,No,not-Yes,GO:0047560; GO:0070402,GO:0016491; GO:0000166,GO:0016491; GO:0004745,GO:0004745,GO:0004745,GO:0004745,0.6031,0.4679,0.391,0.391,0.391,5,0.4488,0.3453,no
KDSR_DANRE,F1QWW8,Protein2Text,Eukaryota,332,"Catalyzes the reduction of 3'-oxosphinganine (3- ketodihydrosphingosine/KDS) to sphinganine (dihydrosphingosine/DHS), the second step of de novo sphingolipid biosynthesis.","The molecular function of this protein is not specified in the provided text. However, based on its name, it is likely to be involved in the modification of fatty acids, specifically in the process of fatty acid synthesis or degradation. The name ""fatty acid 2-hydroxylase"" suggests that this protein is responsible for adding a hydroxyl group to a fatty acid molecule, which is a key step in the synthesis or modification of fatty acids.",Vague,Vague,No,Vague,No,not-Yes,GO:0047560; GO:0070402,GO:0003988,GO:0003988,GO:0003988,GO:0003988,GO:0003988,0.1342,0.1342,0.1342,0.1342,0.1342,5,0.1342,0.3453,no
KDSR_DANRE,F1QWW8,Reference,Eukaryota,332,"Catalyzes the reduction of 3'-oxosphinganine (3- ketodihydrosphingosine/KDS) to sphinganine (dihydrosphingosine/DHS), the second step of de novo sphingolipid biosynthesis.","Catalyzes the reduction of 3'-oxosphinganine (3- ketodihydrosphingosine/KDS) to sphinganine (dihydrosphingosine/DHS), the second step of de novo sphingolipid biosynthesis.",,,,,,,GO:0047560; GO:0070402,GO:0047560,GO:0047560,GO:0047560,GO:0016491,GO:0016491,0.6877,0.6877,0.6877,0.4365,0.4365,5,0.5872,0.3453,no
FDHA2_METMP,F1SVN3,ESM2Text,Archaea,676,"Catalyzes the oxidation of formate to carbon dioxide, with coenzyme F420 as the electron acceptor. In vitro can also use methyl viologen as electron acceptor.",Catalyzes the oxidation of formate.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0051539; GO:0043794; GO:0008863; GO:0046872; GO:0043546; GO:0003954,GO:0008863,GO:0008863,GO:0008863,GO:0008863,GO:0008863,0.4475,0.4475,0.4475,0.4475,0.4475,5,0.4475,0.258,no
FDHA2_METMP,F1SVN3,Prot2Text,Archaea,676,"Catalyzes the oxidation of formate to carbon dioxide, with coenzyme F420 as the electron acceptor. In vitro can also use methyl viologen as electron acceptor.",Catalyzes the oxidation of formate.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0051539; GO:0043794; GO:0008863; GO:0046872; GO:0043546; GO:0003954,GO:0008863,GO:0008863,GO:0008863,GO:0008863,GO:0008863,0.4475,0.4475,0.4475,0.4475,0.4475,5,0.4475,0.258,no
FDHA2_METMP,F1SVN3,ProtT3,Archaea,676,"Catalyzes the oxidation of formate to carbon dioxide, with coenzyme F420 as the electron acceptor. In vitro can also use methyl viologen as electron acceptor.",Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Belongs to the prokaryotic molybdopterin-containing oxidoreductase family,No,No,No,No,No,not-Yes,GO:0051539; GO:0043794; GO:0008863; GO:0046872; GO:0043546; GO:0003954,GO:0016159,GO:0016002,GO:0016002,GO:0016491,GO:0050311,0.1773,0.3118,0.3118,0.4642,0.2672,5,0.3065,0.258,no
FDHA2_METMP,F1SVN3,ProtTale,Archaea,676,"Catalyzes the oxidation of formate to carbon dioxide, with coenzyme F420 as the electron acceptor. In vitro can also use methyl viologen as electron acceptor.","Catalyzes the oxidation of formate to carbon dioxide, with coenzyme F420 as the electron acceptor.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0051539; GO:0043794; GO:0008863; GO:0046872; GO:0043546; GO:0003954,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4642,0.4642,0.4642,0.4642,0.4642,5,0.4642,0.258,no
FDHA2_METMP,F1SVN3,Protein2Text,Archaea,676,"Catalyzes the oxidation of formate to carbon dioxide, with coenzyme F420 as the electron acceptor. In vitro can also use methyl viologen as electron acceptor.",The molecular function of the protein is an oxidoreductase.,Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0051539; GO:0043794; GO:0008863; GO:0046872; GO:0043546; GO:0003954,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4642,0.4642,0.4642,0.4642,0.4642,5,0.4642,0.258,no
FDHA2_METMP,F1SVN3,Reference,Archaea,676,"Catalyzes the oxidation of formate to carbon dioxide, with coenzyme F420 as the electron acceptor. In vitro can also use methyl viologen as electron acceptor.","Catalyzes the oxidation of formate to carbon dioxide, with coenzyme F420 as the electron acceptor. In vitro can also use methyl viologen as electron acceptor.",,,,,,,GO:0051539; GO:0043794; GO:0008863; GO:0046872; GO:0043546; GO:0003954,GO:0008863,GO:0008863,GO:0008863,GO:0008863,GO:0008863,0.4475,0.4475,0.4475,0.4475,0.4475,5,0.4475,0.258,no
HELR_STRVP,F2RC64,ESM2Text,Bacteria,722,"An RNA polymerase (RNAP) recycling system (Probable). Protects RNA polymerase (RNAP) from the inhibitory action of rifampicin by dislodging the antibiotic, allowing transcription to occur and increasing antibiotic tolerance. Has no affect on transcription in the absence of antibiotic. Does not inactivate rifamycin. Inserts into a stalled/inactive RNAP primary channel (where DNA binds) and the secondary channel (where NTPs enter the active site); forces the primary channel open, removing nucleic acids from RNAP. Probably has ATPase activity (Probable).","A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.",No,No,No,No,No,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0003918; GO:0005524,GO:0003916,GO:0003918,GO:0003918,GO:0003918,0.6322,0.3411,0.3577,0.3577,0.3577,5,0.4093,0.5145,no
HELR_STRVP,F2RC64,Prot2Text,Bacteria,722,"An RNA polymerase (RNAP) recycling system (Probable). Protects RNA polymerase (RNAP) from the inhibitory action of rifampicin by dislodging the antibiotic, allowing transcription to occur and increasing antibiotic tolerance. Has no affect on transcription in the absence of antibiotic. Does not inactivate rifamycin. Inserts into a stalled/inactive RNAP primary channel (where DNA binds) and the secondary channel (where NTPs enter the active site); forces the primary channel open, removing nucleic acids from RNAP. Probably has ATPase activity (Probable).",Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA. The complex possesses DNA-dependent ATPase activity.,No,No,No,No,No,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0003689; GO:0016887,GO:0003689,GO:0003689; GO:0016887,GO:0016887,GO:0016887; GO:0005524,0.3841,0.3409,0.3841,0.2706,0.5555,5,0.387,0.5145,no
HELR_STRVP,F2RC64,ProtT3,Bacteria,722,"An RNA polymerase (RNAP) recycling system (Probable). Protects RNA polymerase (RNAP) from the inhibitory action of rifampicin by dislodging the antibiotic, allowing transcription to occur and increasing antibiotic tolerance. Has no affect on transcription in the absence of antibiotic. Does not inactivate rifamycin. Inserts into a stalled/inactive RNAP primary channel (where DNA binds) and the secondary channel (where NTPs enter the active site); forces the primary channel open, removing nucleic acids from RNAP. Probably has ATPase activity (Probable).",A single-stranded DNA (ssDNA)-specific 5'-3' DNA helicase and 3'-5' DNA helicase that may be involved in nucleotide excision repair (NER) of damaged DNA. Catalyzes unwinding of 5'-ssDNA/RNA duplexes in the 5'- to 3'-direction (By similarity). In the N-terminal section; belongs to the RecU family. In the C-terminal section; belongs to the helicase family. UvrD subfamily,No,No,No,No,No,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0003678; GO:0005524,GO:0004386; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0004386; GO:0005524,0.7131,0.6704,0.7131,0.7131,0.6704,5,0.696,0.5145,no
HELR_STRVP,F2RC64,ProtTale,Bacteria,722,"An RNA polymerase (RNAP) recycling system (Probable). Protects RNA polymerase (RNAP) from the inhibitory action of rifampicin by dislodging the antibiotic, allowing transcription to occur and increasing antibiotic tolerance. Has no affect on transcription in the absence of antibiotic. Does not inactivate rifamycin. Inserts into a stalled/inactive RNAP primary channel (where DNA binds) and the secondary channel (where NTPs enter the active site); forces the primary channel open, removing nucleic acids from RNAP. Probably has ATPase activity (Probable).",Involved in DNA repair and RecF pathway recombination.,No,No,No,No,No,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787,,,,,,,,,,,0,,0.5145,no
HELR_STRVP,F2RC64,Protein2Text,Bacteria,722,"An RNA polymerase (RNAP) recycling system (Probable). Protects RNA polymerase (RNAP) from the inhibitory action of rifampicin by dislodging the antibiotic, allowing transcription to occur and increasing antibiotic tolerance. Has no affect on transcription in the absence of antibiotic. Does not inactivate rifamycin. Inserts into a stalled/inactive RNAP primary channel (where DNA binds) and the secondary channel (where NTPs enter the active site); forces the primary channel open, removing nucleic acids from RNAP. Probably has ATPase activity (Probable).","The molecular function of this protein is a DNA helicase, which is involved in unwinding double-stranded DNA into single strands.",No,No,No,No,No,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0004003,GO:0003678,GO:0003678,GO:0003678,GO:0003678,0.454,0.454,0.454,0.454,0.454,5,0.454,0.5145,no
HELR_STRVP,F2RC64,Reference,Bacteria,722,"An RNA polymerase (RNAP) recycling system (Probable). Protects RNA polymerase (RNAP) from the inhibitory action of rifampicin by dislodging the antibiotic, allowing transcription to occur and increasing antibiotic tolerance. Has no affect on transcription in the absence of antibiotic. Does not inactivate rifamycin. Inserts into a stalled/inactive RNAP primary channel (where DNA binds) and the secondary channel (where NTPs enter the active site); forces the primary channel open, removing nucleic acids from RNAP. Probably has ATPase activity (Probable).","An RNA polymerase (RNAP) recycling system (Probable). Protects RNA polymerase (RNAP) from the inhibitory action of rifampicin by dislodging the antibiotic, allowing transcription to occur and increasing antibiotic tolerance. Has no affect on transcription in the absence of antibiotic. Does not inactivate rifamycin. Inserts into a stalled/inactive RNAP primary channel (where DNA binds) and the secondary channel (where NTPs enter the active site); forces the primary channel open, removing nucleic acids from RNAP. Probably has ATPase activity (Probable).",,,,,,,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0016887,GO:0016887,,GO:0016887,GO:0016887,0.2706,0.2706,,0.2706,0.2706,4,0.2706,0.5145,no
RUBPP_HALXS,F8D9F4,ESM2Text,Archaea,239,"Phosphatase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the dephosphorylation of ribulose 1,5-bisphosphate (RuBP) to ribulose 1-phosphate (Ru1P). Shows a strict substrate specificity toward RuBP.","Catalyzes the dephosphorylation of D,L-glyceraldehyde 3-phosphate to D,L-glycero-2-phospho-D-gluconate. Is also able to dephosphorylate 2-amino-6-oxo-7-(phospho-D-ribitylamino)butyric acid (AIB), but with lower efficiency.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,0.6963,0.6963,0.6963,0.6963,0.6963,5,0.6963,0.2302,no
RUBPP_HALXS,F8D9F4,Prot2Text,Archaea,239,"Phosphatase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the dephosphorylation of ribulose 1,5-bisphosphate (RuBP) to ribulose 1-phosphate (Ru1P). Shows a strict substrate specificity toward RuBP.","Catalyzes the dephosphorylation of D,L-glyceraldehyde 3-phosphate in vitro.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,0.6963,0.6963,0.6963,0.6963,0.6963,5,0.6963,0.2302,no
RUBPP_HALXS,F8D9F4,ProtT3,Archaea,239,"Phosphatase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the dephosphorylation of ribulose 1,5-bisphosphate (RuBP) to ribulose 1-phosphate (Ru1P). Shows a strict substrate specificity toward RuBP.",Catalyzes the dephosphorylation of D-ribulose 5- phosphate. Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,0.6963,0.6963,0.6963,0.6963,0.6963,5,0.6963,0.2302,no
RUBPP_HALXS,F8D9F4,ProtTale,Archaea,239,"Phosphatase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the dephosphorylation of ribulose 1,5-bisphosphate (RuBP) to ribulose 1-phosphate (Ru1P). Shows a strict substrate specificity toward RuBP.",Catalyzes the deamination of D-threo-3-hydroxybutyric acid to D-erythro-3-hydroxybutyric acid.,No,No,No,No,No,not-Yes,GO:0046872; GO:0016791,GO:0016787,GO:0016787,,,,0.4539,0.4539,,,,2,0.4539,0.2302,no
RUBPP_HALXS,F8D9F4,Protein2Text,Archaea,239,"Phosphatase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the dephosphorylation of ribulose 1,5-bisphosphate (RuBP) to ribulose 1-phosphate (Ru1P). Shows a strict substrate specificity toward RuBP.","The molecular function of this protein is phosphatase activity. 
This protein removes phosphate groups from molecules, playing a crucial role in various cellular processes such as signal transduction, metabolism, and gene regulation.",Maybe,Vague,Maybe,Vague,Maybe,not-Yes,GO:0046872; GO:0016791,GO:0004721,GO:0016791,GO:0016791,GO:0016791,GO:0016791,0.5645,0.6963,0.6963,0.6963,0.6963,5,0.6699,0.2302,no
RUBPP_HALXS,F8D9F4,Reference,Archaea,239,"Phosphatase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the dephosphorylation of ribulose 1,5-bisphosphate (RuBP) to ribulose 1-phosphate (Ru1P). Shows a strict substrate specificity toward RuBP.","Phosphatase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the dephosphorylation of ribulose 1,5-bisphosphate (RuBP) to ribulose 1-phosphate (Ru1P). Shows a strict substrate specificity toward RuBP.",,,,,,,GO:0046872; GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,0.6963,0.6963,0.6963,0.6963,0.6963,5,0.6963,0.2302,no
RU1PA_HALXS,F8D9F5,ESM2Text,Archaea,219,"Aldolase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the cleavage of ribulose 1-phosphate (Ru1P) to dihydroxyacetone phosphate (DHAP) and glycolaldehyde. Can also catalyze the reverse reaction, condensing DHAP and aldehydes. In vitro, can condensate DHAP with various aldehydes, including glycolaldehyde, acetaldehyde, propionaldehyde, isobutylaldehyde, DL-glyceraldehyde and DL-lactaldehyde.","Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). Part of a bifunctional DHAP-shunt salvage pathway for the degradation of cobalt-precorrin-5A.",No,No,No,No,Maybe,not-Yes,GO:0016832; GO:0046872,GO:0016836,GO:0016829,,GO:0016836,,0.3445,0.5125,,0.3445,,3,0.4005,0.4266,no
RU1PA_HALXS,F8D9F5,Prot2Text,Archaea,219,"Aldolase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the cleavage of ribulose 1-phosphate (Ru1P) to dihydroxyacetone phosphate (DHAP) and glycolaldehyde. Can also catalyze the reverse reaction, condensing DHAP and aldehydes. In vitro, can condensate DHAP with various aldehydes, including glycolaldehyde, acetaldehyde, propionaldehyde, isobutylaldehyde, DL-glyceraldehyde and DL-lactaldehyde.",Catalyzes the decarboxylation of 3-oxo-tetronate 4-phosphate to dihydroxyacetone phosphate (DHAP) and CO(2).,No,No,Maybe,No,No,not-Yes,GO:0016832; GO:0046872,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.5032,0.5032,0.5032,0.5032,0.5032,5,0.5032,0.4266,no
RU1PA_HALXS,F8D9F5,ProtT3,Archaea,219,"Aldolase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the cleavage of ribulose 1-phosphate (Ru1P) to dihydroxyacetone phosphate (DHAP) and glycolaldehyde. Can also catalyze the reverse reaction, condensing DHAP and aldehydes. In vitro, can condensate DHAP with various aldehydes, including glycolaldehyde, acetaldehyde, propionaldehyde, isobutylaldehyde, DL-glyceraldehyde and DL-lactaldehyde.",Involved in the degradation of L-arabinose. Catalyzes the reversible cleavage of L-ribulose 5-phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde. Belongs to the aldolase class II family. AraD/FucA subfamily,Maybe,Yes,Yes,Maybe,Maybe,not-Yes,GO:0016832; GO:0046872,GO:0016832,GO:0016832,GO:0016832,GO:0016832,GO:0016832,0.7015,0.7015,0.7015,0.7015,0.7015,5,0.7015,0.4266,no
RU1PA_HALXS,F8D9F5,ProtTale,Archaea,219,"Aldolase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the cleavage of ribulose 1-phosphate (Ru1P) to dihydroxyacetone phosphate (DHAP) and glycolaldehyde. Can also catalyze the reverse reaction, condensing DHAP and aldehydes. In vitro, can condensate DHAP with various aldehydes, including glycolaldehyde, acetaldehyde, propionaldehyde, isobutylaldehyde, DL-glyceraldehyde and DL-lactaldehyde.",Catalyzes the isomerization of 4-hydroxy-tetrahydrodipicolinate (4-HTPA) to tetrahydrodipicolinate.,No,No,No,No,No,not-Yes,GO:0016832; GO:0046872,GO:0016853,GO:0016853,GO:0016853,GO:0016853,GO:0016853,0.324,0.324,0.324,0.324,0.324,5,0.324,0.4266,no
RU1PA_HALXS,F8D9F5,Protein2Text,Archaea,219,"Aldolase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the cleavage of ribulose 1-phosphate (Ru1P) to dihydroxyacetone phosphate (DHAP) and glycolaldehyde. Can also catalyze the reverse reaction, condensing DHAP and aldehydes. In vitro, can condensate DHAP with various aldehydes, including glycolaldehyde, acetaldehyde, propionaldehyde, isobutylaldehyde, DL-glyceraldehyde and DL-lactaldehyde.","The molecular function of this protein is a lyase enzyme, specifically a D-aminoacyl-tRNA deacylase.",No,No,No,No,No,not-Yes,GO:0016832; GO:0046872,GO:0016829,GO:0051499,,GO:0051499,GO:0008728,0.5125,0.149,,0.149,0.1865,4,0.2492,0.4266,no
RU1PA_HALXS,F8D9F5,Reference,Archaea,219,"Aldolase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the cleavage of ribulose 1-phosphate (Ru1P) to dihydroxyacetone phosphate (DHAP) and glycolaldehyde. Can also catalyze the reverse reaction, condensing DHAP and aldehydes. In vitro, can condensate DHAP with various aldehydes, including glycolaldehyde, acetaldehyde, propionaldehyde, isobutylaldehyde, DL-glyceraldehyde and DL-lactaldehyde.","Aldolase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the cleavage of ribulose 1-phosphate (Ru1P) to dihydroxyacetone phosphate (DHAP) and glycolaldehyde. Can also catalyze the reverse reaction, condensing DHAP and aldehydes. In vitro, can condensate DHAP with various aldehydes, including glycolaldehyde, acetaldehyde, propionaldehyde, isobutylaldehyde, DL-glyceraldehyde and DL-lactaldehyde.",,,,,,,GO:0016832; GO:0046872,GO:0016832,GO:0016832,GO:0016832,GO:0016832,GO:0016832,0.7015,0.7015,0.7015,0.7015,0.7015,5,0.7015,0.4266,no
USP9Y_MOUSE,F8VPU6,ESM2Text,Eukaryota,2556,Deubiquitinase that mediates deubiquitination of target proteins. May stabilize target proteins that are important for male germ cell development.,"Adapter protein, which probably acts as a linker between membranes and the actin cytoskeleton. May participate in the maintenance of cell polarity and the proper formation of actin stress fibers. May play a role in vesicle-mediated transport, and in fusion of transport vesicles containing G-protein-coupled receptors with the Golgi.",No,No,No,No,No,not-Yes,GO:0004843; GO:0046872,,,,,,,,,,,0,,0.7729,yes
USP9Y_MOUSE,F8VPU6,Prot2Text,Eukaryota,2556,Deubiquitinase that mediates deubiquitination of target proteins. May stabilize target proteins that are important for male germ cell development.,Subunit of the heterodimeric RalGAP1 and RalGAP2 complexes which act as GTPase activators for the Ras-like small GTPases RALA and RALB.,No,No,No,No,No,not-Yes,GO:0004843; GO:0046872,GO:0005096,GO:0005096,GO:0005096,GO:0005096,GO:0005096,0.076,0.076,0.076,0.076,0.076,5,0.076,0.7729,yes
USP9Y_MOUSE,F8VPU6,ProtT3,Eukaryota,2556,Deubiquitinase that mediates deubiquitination of target proteins. May stabilize target proteins that are important for male germ cell development.,"Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). Cytoplasm, cytoskeleton",No,No,No,No,No,not-Yes,GO:0004843; GO:0046872,GO:0061630,GO:0061630,,GO:0061630,GO:0061630,0.1695,0.1695,,0.1695,0.1695,4,0.1695,0.7729,yes
USP9Y_MOUSE,F8VPU6,ProtTale,Eukaryota,2556,Deubiquitinase that mediates deubiquitination of target proteins. May stabilize target proteins that are important for male germ cell development.,"Ubiquitin-protein isopeptidase that specifically cleaves polyubiquitin chains linked through K1 (UBE1), K2 (UBE2A), K21 (UBE2I) and K48 (UBE2L3). Acts as a negative regulator of brassinosteroid (BR) signaling.",No,No,No,No,Maybe,not-Yes,GO:0004843; GO:0046872,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,0.6901,0.6901,0.6901,0.6901,0.6901,5,0.6901,0.7729,yes
USP9Y_MOUSE,F8VPU6,Protein2Text,Eukaryota,2556,Deubiquitinase that mediates deubiquitination of target proteins. May stabilize target proteins that are important for male germ cell development.,"The molecular function of this protein is not specified in the given text. However, based on its name, it is likely involved in the degradation of RNA. Specifically, it may be involved in the degradation of cytoplasmic mRNA. 

This protein is part of a complex that is involved in the degradation of cytoplasmic mRNA. It is likely involved in the 3' to 5' exoribonuclease activity of the complex, which is responsible for degrading mRNA in the cytoplasm. 

It is also likely involved in the regulation of gene expression by degrading specific mRNA molecules, which can affect the levels of protein synthesis. 

Overall, the molecular function of this protein is likely to be involved in the degradation of RNA, specifically cytoplasmic mRNA.",No,No,No,No,No,not-Yes,GO:0004843; GO:0046872,GO:0004532,GO:0000175,GO:0000175,GO:0000175,GO:0000175,0.1616,0.1344,0.1344,0.1344,0.1344,5,0.1398,0.7729,yes
USP9Y_MOUSE,F8VPU6,Reference,Eukaryota,2556,Deubiquitinase that mediates deubiquitination of target proteins. May stabilize target proteins that are important for male germ cell development.,Deubiquitinase that mediates deubiquitination of target proteins. May stabilize target proteins that are important for male germ cell development.,,,,,,,GO:0004843; GO:0046872,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,0.6901,0.6901,0.6901,0.6901,0.6901,5,0.6901,0.7729,yes
ILIA_HYPJQ,G0REX6,ESM2Text,Eukaryota,3812,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2- pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain. IliA assembles the backbone of ilicicolin H. The PKS portion and trans-acting enoyl reductase iliB work together to construct an octaketide, and two methyl groups are introduced by the MT domain during the chain assembly. The nascent chain is then condensed with tyrosine, catalyzed by the C domain, and the resulting PKS-NRPS hybrid is offloaded by the RED domain to form an advanced tetramic acid intermediate. The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl reductase iliB since iliA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iliC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might then spontaneously convert to ilicicolin H to ilicicolin H since ilicicolin H is produced in the absence of the epimerase iliE, in contrast to what was observed for the Talaromyces variabilis ilicolin H biosynthetic pathway (Probable).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcsC",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,,,,,,,,,,,0,,0.2992,no
ILIA_HYPJQ,G0REX6,Prot2Text,Eukaryota,3812,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2- pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain. IliA assembles the backbone of ilicicolin H. The PKS portion and trans-acting enoyl reductase iliB work together to construct an octaketide, and two methyl groups are introduced by the MT domain during the chain assembly. The nascent chain is then condensed with tyrosine, catalyzed by the C domain, and the resulting PKS-NRPS hybrid is offloaded by the RED domain to form an advanced tetramic acid intermediate. The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl reductase iliB since iliA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iliC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might then spontaneously convert to ilicicolin H to ilicicolin H since ilicicolin H is produced in the absence of the epimerase iliE, in contrast to what was observed for the Talaromyces variabilis ilicolin H biosynthetic pathway (Probable).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcsC",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0016747,,,GO:0016747,GO:0016746,0.5636,,,0.5636,0.5445,3,0.5572,0.2992,no
ILIA_HYPJQ,G0REX6,ProtT3,Eukaryota,3812,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2- pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain. IliA assembles the backbone of ilicicolin H. The PKS portion and trans-acting enoyl reductase iliB work together to construct an octaketide, and two methyl groups are introduced by the MT domain during the chain assembly. The nascent chain is then condensed with tyrosine, catalyzed by the C domain, and the resulting PKS-NRPS hybrid is offloaded by the RED domain to form an advanced tetramic acid intermediate. The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl reductase iliB since iliA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iliC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might then spontaneously convert to ilicicolin H to ilicicolin H since ilicicolin H is produced in the absence of the epimerase iliE, in contrast to what was observed for the Talaromyces variabilis ilicolin H biosynthetic pathway (Probable).","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0016746,GO:0016746,,GO:0016746,GO:0016747,0.5445,0.5445,,0.5445,0.5636,4,0.5493,0.2992,no
ILIA_HYPJQ,G0REX6,ProtTale,Eukaryota,3812,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2- pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain. IliA assembles the backbone of ilicicolin H. The PKS portion and trans-acting enoyl reductase iliB work together to construct an octaketide, and two methyl groups are introduced by the MT domain during the chain assembly. The nascent chain is then condensed with tyrosine, catalyzed by the C domain, and the resulting PKS-NRPS hybrid is offloaded by the RED domain to form an advanced tetramic acid intermediate. The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl reductase iliB since iliA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iliC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might then spontaneously convert to ilicicolin H to ilicicolin H since ilicicolin H is produced in the absence of the epimerase iliE, in contrast to what was observed for the Talaromyces variabilis ilicolin H biosynthetic pathway (Probable).","Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the",Maybe,Yes,Yes,Yes,Maybe,Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0016491,GO:0016757,,,GO:0016746; GO:0016874,0.5478,0.4493,,,0.6826,3,0.5599,0.2992,no
ILIA_HYPJQ,G0REX6,Protein2Text,Eukaryota,3812,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2- pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain. IliA assembles the backbone of ilicicolin H. The PKS portion and trans-acting enoyl reductase iliB work together to construct an octaketide, and two methyl groups are introduced by the MT domain during the chain assembly. The nascent chain is then condensed with tyrosine, catalyzed by the C domain, and the resulting PKS-NRPS hybrid is offloaded by the RED domain to form an advanced tetramic acid intermediate. The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl reductase iliB since iliA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iliC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might then spontaneously convert to ilicicolin H to ilicicolin H since ilicicolin H is produced in the absence of the epimerase iliE, in contrast to what was observed for the Talaromyces variabilis ilicolin H biosynthetic pathway (Probable).","The molecular function of this protein is not specified in the given text. However, based on its name, it is likely that the protein is involved in fatty acid synthesis, specifically in the production of fatty acids. Fatty acid synthase (FAS) is an enzyme that catalyzes the production of fatty acids from acetyl-CoA and malonyl-CoA through a series of reduction, dehydration, and reduction reactions. This protein is likely involved in one of the steps of this process.",Vague,No,Maybe,Vague,No,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.5599,0.5599,0.5599,0.5599,0.5599,5,0.5599,0.2992,no
ILIA_HYPJQ,G0REX6,Reference,Eukaryota,3812,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2- pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain. IliA assembles the backbone of ilicicolin H. The PKS portion and trans-acting enoyl reductase iliB work together to construct an octaketide, and two methyl groups are introduced by the MT domain during the chain assembly. The nascent chain is then condensed with tyrosine, catalyzed by the C domain, and the resulting PKS-NRPS hybrid is offloaded by the RED domain to form an advanced tetramic acid intermediate. The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl reductase iliB since iliA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iliC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might then spontaneously convert to ilicicolin H to ilicicolin H since ilicicolin H is produced in the absence of the epimerase iliE, in contrast to what was observed for the Talaromyces variabilis ilicolin H biosynthetic pathway (Probable).","Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2- pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain. IliA assembles the backbone of ilicicolin H. The PKS portion and trans-acting enoyl reductase iliB work together to construct an octaketide, and two methyl groups are introduced by the MT domain during the chain assembly. The nascent chain is then condensed with tyrosine, catalyzed by the C domain, and the resulting PKS-NRPS hybrid is offloaded by the RED domain to form an advanced tetramic acid intermediate. The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl reductase iliB since iliA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iliC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might then spontaneously convert to ilicicolin H to ilicicolin H since ilicicolin H is produced in the absence of the epimerase iliE, in contrast to what was observed for the Talaromyces variabilis ilicolin H biosynthetic pathway (Probable).",,,,,,,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0016746; GO:0016874,GO:0016874; GO:0016746,GO:0016874; GO:0016747,GO:0016874,GO:0016874,0.6826,0.6826,0.7195,0.5478,0.5478,5,0.6361,0.2992,no
PEX6_ARTOA,G1X4S3,ESM2Text,Eukaryota,1183,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5. Regulates autophagy and biogenesis of peroxisomes and Woronin bodies. Plays important roles in mycelial growth and development and stress response. Is also essential for conidiation and fatty acid utilization. Required for nematode predation via trap formation.","ATP-dependent chaperone which probably uses the energy provided by ATP hydrolysis to generate mechanical force to unfold substrate proteins, disassemble protein complexes, and disaggregate protein aggregates.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887,,,,,,,,,,,0,,0.4775,no
PEX6_ARTOA,G1X4S3,Prot2Text,Eukaryota,1183,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5. Regulates autophagy and biogenesis of peroxisomes and Woronin bodies. Plays important roles in mycelial growth and development and stress response. Is also essential for conidiation and fatty acid utilization. Required for nematode predation via trap formation.",Involved in peroxisome biosynthesis.,Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0005524; GO:0016887,,,,,,,,,,,0,,0.4775,no
PEX6_ARTOA,G1X4S3,ProtT3,Eukaryota,1183,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5. Regulates autophagy and biogenesis of peroxisomes and Woronin bodies. Plays important roles in mycelial growth and development and stress response. Is also essential for conidiation and fatty acid utilization. Required for nematode predation via trap formation.","Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor (By similarity). The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 8 nm (By similarity). Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the",No,Maybe,No,No,No,not-Yes,GO:0005524; GO:0016887,GO:0009055,GO:0009055,GO:0009055; GO:0051536,GO:0016491,GO:0009055,0.1603,0.1603,0.2093,0.2238,0.1603,5,0.1828,0.4775,no
PEX6_ARTOA,G1X4S3,ProtTale,Eukaryota,1183,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5. Regulates autophagy and biogenesis of peroxisomes and Woronin bodies. Plays important roles in mycelial growth and development and stress response. Is also essential for conidiation and fatty acid utilization. Required for nematode predation via trap formation.","Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887,GO:0005524,GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.6869,1.0,1.0,1.0,1.0,5,0.9374,0.4775,no
PEX6_ARTOA,G1X4S3,Protein2Text,Eukaryota,1183,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5. Regulates autophagy and biogenesis of peroxisomes and Woronin bodies. Plays important roles in mycelial growth and development and stress response. Is also essential for conidiation and fatty acid utilization. Required for nematode predation via trap formation.","This protein is a part of a larger molecular complex that plays a role in regulating the structure and function of the cytoskeleton. The specific molecular function of this protein is to assemble the cytoskeleton, specifically the actin cytoskeleton. This is done through the polymerization of actin monomers into filamentous actin, which provides structural support and shape to the cell. The protein's molecular function is also involved in regulating the organization and dynamics of the cytoskeleton, including the formation of stress fibers, focal adhesions, and cell shape changes.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016887,,,,,,,,,,,0,,0.4775,no
PEX6_ARTOA,G1X4S3,Reference,Eukaryota,1183,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5. Regulates autophagy and biogenesis of peroxisomes and Woronin bodies. Plays important roles in mycelial growth and development and stress response. Is also essential for conidiation and fatty acid utilization. Required for nematode predation via trap formation.","Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5. Regulates autophagy and biogenesis of peroxisomes and Woronin bodies. Plays important roles in mycelial growth and development and stress response. Is also essential for conidiation and fatty acid utilization. Required for nematode predation via trap formation.",,,,,,,GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,1.0,0.6869,1.0,1.0,1.0,5,0.9374,0.4775,no
PEX1_ARTOA,G1X7C7,ESM2Text,Eukaryota,1194,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5. Regulates autophagy and biogenesis of peroxisomes and Woronin bodies. Plays important roles in mycelial growth and development and stress response. Is also essential for conidiation and fatty acid utilization. Required for nematode predation via trap formation.",Involved in peroxisome biosynthesis.,Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0005524; GO:0016887,,,,,,,,,,,0,,0.5124,no
PEX1_ARTOA,G1X7C7,Prot2Text,Eukaryota,1194,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5. Regulates autophagy and biogenesis of peroxisomes and Woronin bodies. Plays important roles in mycelial growth and development and stress response. Is also essential for conidiation and fatty acid utilization. Required for nematode predation via trap formation.",Involved in peroxisome biosynthesis.,Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0005524; GO:0016887,,,,,,,,,,,0,,0.5124,no
PEX1_ARTOA,G1X7C7,ProtT3,Eukaryota,1194,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5. Regulates autophagy and biogenesis of peroxisomes and Woronin bodies. Plays important roles in mycelial growth and development and stress response. Is also essential for conidiation and fatty acid utilization. Required for nematode predation via trap formation.","Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe/S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe/S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex CFD1-NBP35. Electrons are transferred to DRE2 from NADPH via the FAD- and FMN-containing protein TAH18. TAH18-DRE2 are also required for the assembly of the diferric tyros",No,No,No,No,No,not-Yes,GO:0005524; GO:0016887,GO:0009055,GO:0009055,GO:0009055; GO:0051536,GO:0016491,GO:0009055,0.1603,0.1603,0.2093,0.2238,0.1603,5,0.1828,0.5124,no
PEX1_ARTOA,G1X7C7,ProtTale,Eukaryota,1194,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5. Regulates autophagy and biogenesis of peroxisomes and Woronin bodies. Plays important roles in mycelial growth and development and stress response. Is also essential for conidiation and fatty acid utilization. Required for nematode predation via trap formation.","Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887,GO:0005524,GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.6869,1.0,1.0,1.0,1.0,5,0.9374,0.5124,no
PEX1_ARTOA,G1X7C7,Protein2Text,Eukaryota,1194,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5. Regulates autophagy and biogenesis of peroxisomes and Woronin bodies. Plays important roles in mycelial growth and development and stress response. Is also essential for conidiation and fatty acid utilization. Required for nematode predation via trap formation.","The molecular function of this protein is not explicitly stated in the provided information. However, based on its classification as a protein, it is likely to be involved in various cellular processes, such as catalysis, binding, or transport. Further research would be required to determine its specific molecular function.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0005524; GO:0016887,,,,,,,,,,,0,,0.5124,no
PEX1_ARTOA,G1X7C7,Reference,Eukaryota,1194,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5. Regulates autophagy and biogenesis of peroxisomes and Woronin bodies. Plays important roles in mycelial growth and development and stress response. Is also essential for conidiation and fatty acid utilization. Required for nematode predation via trap formation.","Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-6', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5. Regulates autophagy and biogenesis of peroxisomes and Woronin bodies. Plays important roles in mycelial growth and development and stress response. Is also essential for conidiation and fatty acid utilization. Required for nematode predation via trap formation.",,,,,,,GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,1.0,0.6869,1.0,1.0,1.0,5,0.9374,0.5124,no
AO415_ARTOA,G1XSR7,ESM2Text,Eukaryota,3483,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of desferriferrichrome that chelates Fe(3+) to form ferrichrome. Fe(3+) is a key factor for induction of trap formation and the fungus uses the iron chelating desferriferrichrome to sequester Fe(3+) to inhibit trap formation and increase nematicidal activity. The biosynthesis of desferriferrichrome requires the action of the L-ornithine N(5)- oxygenase (LOO) Ao414 that hydroxylates L-ornithine at N(5), resulting in the formation of N(5)-hydroxyl-L-ornithine, which is subsequently N- acetylated to yield N(5)-acetyl-N(5)-hydroxy-L-ornithine (L-AHO). L-AHO harbors one hydroxamate moiety, which is the key core responsible for chelating iron. Then, L-AHO is further condensated with glycines to form desferriferrichrome through the NRPS protein Ao415 (Probable).","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcs",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,,,,,,,,,,,0,,0.3068,no
AO415_ARTOA,G1XSR7,Prot2Text,Eukaryota,3483,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of desferriferrichrome that chelates Fe(3+) to form ferrichrome. Fe(3+) is a key factor for induction of trap formation and the fungus uses the iron chelating desferriferrichrome to sequester Fe(3+) to inhibit trap formation and increase nematicidal activity. The biosynthesis of desferriferrichrome requires the action of the L-ornithine N(5)- oxygenase (LOO) Ao414 that hydroxylates L-ornithine at N(5), resulting in the formation of N(5)-hydroxyl-L-ornithine, which is subsequently N- acetylated to yield N(5)-acetyl-N(5)-hydroxy-L-ornithine (L-AHO). L-AHO harbors one hydroxamate moiety, which is the key core responsible for chelating iron. Then, L-AHO is further condensated with glycines to form desferriferrichrome through the NRPS protein Ao415 (Probable).","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcs",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,GO:0016874,,,GO:0016874,GO:0016874; GO:0005524,0.709,,,0.709,0.6793,3,0.6991,0.3068,no
AO415_ARTOA,G1XSR7,ProtT3,Eukaryota,3483,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of desferriferrichrome that chelates Fe(3+) to form ferrichrome. Fe(3+) is a key factor for induction of trap formation and the fungus uses the iron chelating desferriferrichrome to sequester Fe(3+) to inhibit trap formation and increase nematicidal activity. The biosynthesis of desferriferrichrome requires the action of the L-ornithine N(5)- oxygenase (LOO) Ao414 that hydroxylates L-ornithine at N(5), resulting in the formation of N(5)-hydroxyl-L-ornithine, which is subsequently N- acetylated to yield N(5)-acetyl-N(5)-hydroxy-L-ornithine (L-AHO). L-AHO harbors one hydroxamate moiety, which is the key core responsible for chelating iron. Then, L-AHO is further condensated with glycines to form desferriferrichrome through the NRPS protein Ao415 (Probable).","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of austinol, a fungal meroterpenoid . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase ausA . DMOA is then prenylated by the polyprenyl transferase ausN . Further epoxidation by the FAD",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,GO:0016874; GO:0005524,GO:0016874,,GO:0016874; GO:0031177,GO:0016874; GO:0005524,0.6793,0.709,,1.0,0.6793,4,0.7669,0.3068,no
AO415_ARTOA,G1XSR7,ProtTale,Eukaryota,3483,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of desferriferrichrome that chelates Fe(3+) to form ferrichrome. Fe(3+) is a key factor for induction of trap formation and the fungus uses the iron chelating desferriferrichrome to sequester Fe(3+) to inhibit trap formation and increase nematicidal activity. The biosynthesis of desferriferrichrome requires the action of the L-ornithine N(5)- oxygenase (LOO) Ao414 that hydroxylates L-ornithine at N(5), resulting in the formation of N(5)-hydroxyl-L-ornithine, which is subsequently N- acetylated to yield N(5)-acetyl-N(5)-hydroxy-L-ornithine (L-AHO). L-AHO harbors one hydroxamate moiety, which is the key core responsible for chelating iron. Then, L-AHO is further condensated with glycines to form desferriferrichrome through the NRPS protein Ao415 (Probable).","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS). SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms. These initial steps feature the priming of an unusual benzoic acid starter unit onto",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,GO:0016491,GO:0016874,,,GO:0016874,0.4358,0.709,,,0.709,3,0.6179,0.3068,no
AO415_ARTOA,G1XSR7,Protein2Text,Eukaryota,3483,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of desferriferrichrome that chelates Fe(3+) to form ferrichrome. Fe(3+) is a key factor for induction of trap formation and the fungus uses the iron chelating desferriferrichrome to sequester Fe(3+) to inhibit trap formation and increase nematicidal activity. The biosynthesis of desferriferrichrome requires the action of the L-ornithine N(5)- oxygenase (LOO) Ao414 that hydroxylates L-ornithine at N(5), resulting in the formation of N(5)-hydroxyl-L-ornithine, which is subsequently N- acetylated to yield N(5)-acetyl-N(5)-hydroxy-L-ornithine (L-AHO). L-AHO harbors one hydroxamate moiety, which is the key core responsible for chelating iron. Then, L-AHO is further condensated with glycines to form desferriferrichrome through the NRPS protein Ao415 (Probable).","The molecular function of this protein is not explicitly stated in the provided information. However, as a component of the 50S ribosomal subunit, it is likely to be involved in protein synthesis, specifically in the elongation step of translation.",No,No,No,No,No,not-Yes,GO:0016874; GO:0031177,GO:0003735,GO:0003735,GO:0003735,GO:0003735,GO:0003735,0.2172,0.2172,0.2172,0.2172,0.2172,5,0.2172,0.3068,no
AO415_ARTOA,G1XSR7,Reference,Eukaryota,3483,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of desferriferrichrome that chelates Fe(3+) to form ferrichrome. Fe(3+) is a key factor for induction of trap formation and the fungus uses the iron chelating desferriferrichrome to sequester Fe(3+) to inhibit trap formation and increase nematicidal activity. The biosynthesis of desferriferrichrome requires the action of the L-ornithine N(5)- oxygenase (LOO) Ao414 that hydroxylates L-ornithine at N(5), resulting in the formation of N(5)-hydroxyl-L-ornithine, which is subsequently N- acetylated to yield N(5)-acetyl-N(5)-hydroxy-L-ornithine (L-AHO). L-AHO harbors one hydroxamate moiety, which is the key core responsible for chelating iron. Then, L-AHO is further condensated with glycines to form desferriferrichrome through the NRPS protein Ao415 (Probable).","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of desferriferrichrome that chelates Fe(3+) to form ferrichrome. Fe(3+) is a key factor for induction of trap formation and the fungus uses the iron chelating desferriferrichrome to sequester Fe(3+) to inhibit trap formation and increase nematicidal activity. The biosynthesis of desferriferrichrome requires the action of the L-ornithine N(5)- oxygenase (LOO) Ao414 that hydroxylates L-ornithine at N(5), resulting in the formation of N(5)-hydroxyl-L-ornithine, which is subsequently N- acetylated to yield N(5)-acetyl-N(5)-hydroxy-L-ornithine (L-AHO). L-AHO harbors one hydroxamate moiety, which is the key core responsible for chelating iron. Then, L-AHO is further condensated with glycines to form desferriferrichrome through the NRPS protein Ao415 (Probable).",,,,,,,GO:0016874; GO:0031177,GO:0016874,GO:0016874,GO:0016879,GO:0016874,GO:0016874,0.709,0.709,0.5786,0.709,0.709,5,0.6829,0.3068,no
CHS8_VERDV,G2X5A0,ESM2Text,Eukaryota,613,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer (Probable). Plays a role in cell wall integrity. Plays a key role in pathogenicity. Likely contributes to post-penetration virulence.",Catalyzes the addition of GlcNAc to the nascent hyaluronan polymer. The hyaluronan polymer is a component of the outer membrane of the cell wall and facilitates high-affinity hyaluronan synthesis.,No,Maybe,Maybe,No,Maybe,not-Yes,GO:0004100,GO:0050501,GO:0016757,GO:0050501,GO:0050501,GO:0050501,0.6917,0.5917,0.6917,0.6917,0.6917,5,0.6717,0.533,no
CHS8_VERDV,G2X5A0,Prot2Text,Eukaryota,613,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer (Probable). Plays a role in cell wall integrity. Plays a key role in pathogenicity. Likely contributes to post-penetration virulence.","Beta-1,4-mannosyltransferase involved in O-glycosylation of cell wall and secreted proteins. Transfers a fourth mannose to elongase-like repeats 4. Required for synthesis of chitin, teichoic acid, and type III arabinogalactan.",No,No,No,No,No,not-Yes,GO:0004100,GO:0000030,GO:0000030,GO:0000030,GO:0000030,GO:0000030,0.5846,0.5846,0.5846,0.5846,0.5846,5,0.5846,0.533,no
CHS8_VERDV,G2X5A0,ProtT3,Eukaryota,613,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer (Probable). Plays a role in cell wall integrity. Plays a key role in pathogenicity. Likely contributes to post-penetration virulence.","Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer. Cell membrane; Multi-pass membrane protein. Belongs to the chitin synthase family. Class III subfamily",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,1.0,1.0,1.0,1.0,1.0,5,1.0,0.533,no
CHS8_VERDV,G2X5A0,ProtTale,Eukaryota,613,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer (Probable). Plays a role in cell wall integrity. Plays a key role in pathogenicity. Likely contributes to post-penetration virulence.","Probable beta-1,4-glucan synthase.",No,No,No,No,No,not-Yes,GO:0004100,GO:0016757,GO:0016757,,GO:0016757,GO:0016757,0.5917,0.5917,,0.5917,0.5917,4,0.5917,0.533,no
CHS8_VERDV,G2X5A0,Protein2Text,Eukaryota,613,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer (Probable). Plays a role in cell wall integrity. Plays a key role in pathogenicity. Likely contributes to post-penetration virulence.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its classification as a protein involved in the biosynthesis of cell wall, it is likely that its molecular function is related to the synthesis of cell wall components, such as glucan.",Vague,No,Vague,Vague,No,not-Yes,GO:0004100,,,,,,,,,,,0,,0.533,no
CHS8_VERDV,G2X5A0,Reference,Eukaryota,613,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer (Probable). Plays a role in cell wall integrity. Plays a key role in pathogenicity. Likely contributes to post-penetration virulence.","Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer (Probable). Plays a role in cell wall integrity. Plays a key role in pathogenicity. Likely contributes to post-penetration virulence.",,,,,,,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,1.0,1.0,1.0,1.0,1.0,5,1.0,0.533,no
PEX1_CRIGR,G3GXG9,ESM2Text,Eukaryota,1285,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.","Required for protein import into peroxisomes. Anchored by PEX26 to peroxisome membranes, possibly to form heteromeric AAA ATPase complexes required for the import of proteins into peroxisomes.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0016887; GO:0140318; GO:0140036,GO:0016887; GO:0005524,GO:0016887,GO:0016887,,GO:0016887,0.7093,0.4633,0.4633,,0.4633,4,0.5248,0.5736,yes
PEX1_CRIGR,G3GXG9,Prot2Text,Eukaryota,1285,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.","Required for stability of PEX5 and protein import into the peroxisome matrix. Anchored by PEX26 to peroxisome membranes, possibly to form heteromeric AAA ATPase complexes required for the import of proteins into peroxisomes.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0005524; GO:0016887; GO:0140318; GO:0140036,GO:0016887,GO:0016887,GO:0016887,GO:0016887,GO:0016887; GO:0005524,0.4633,0.4633,0.4633,0.4633,0.7093,5,0.5125,0.5736,yes
PEX1_CRIGR,G3GXG9,ProtT3,Eukaryota,1285,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.","ATPase component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe/S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe/S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex CFD1-NBP35. Electrons are transferred to DRE2 from NADPH via the FAD- and FMN-containing protein TAH18. TAH18-DRE2 are also required for the assembly of the diferric",No,No,No,No,No,not-Yes,GO:0005524; GO:0016887; GO:0140318; GO:0140036,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.7093,0.7093,0.7093,0.7093,0.7093,5,0.7093,0.5736,yes
PEX1_CRIGR,G3GXG9,ProtTale,Eukaryota,1285,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.","ATP-dependent RNA helicase which is a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016887; GO:0140318; GO:0140036,GO:0004386; GO:0005524; GO:0003723,GO:0004386; GO:0005524,GO:0004004; GO:0005524,GO:0003724; GO:0005524,GO:0003724; GO:0005524,0.4576,0.4832,0.4491,0.4491,0.4491,5,0.4576,0.5736,yes
PEX1_CRIGR,G3GXG9,Protein2Text,Eukaryota,1285,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.","The molecular function of this protein is not explicitly stated in the provided text, but based on its name and the context, it is likely involved in the repair of DNA damage. Specifically, it may be involved in the excision repair of DNA damage, as suggested by its classification as a helicase, which is a type of enzyme that unwinds DNA.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016887; GO:0140318; GO:0140036,GO:0004386,GO:0004386,GO:0004386,GO:0004386,GO:0004386,0.1934,0.1934,0.1934,0.1934,0.1934,5,0.1934,0.5736,yes
PEX1_CRIGR,G3GXG9,Reference,Eukaryota,1285,"Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.","Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel. Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5.",,,,,,,GO:0005524; GO:0016887; GO:0140318; GO:0140036,GO:0016887; GO:0005524,GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.7093,0.4633,0.7093,0.7093,0.7093,5,0.6601,0.5736,yes
CNS2_CORMM,G3JF09,ESM2Text,Eukaryota,345,"Metal-dependent phosphohydrolase; part of the gene cluster that mediates the biosynthesis of cordycepin (COR) and pentostatin (PTN), two adenosine analogs with related bioactivity profiles as both mimic adenosine and can inhibit some of the processes that are adenosine dependent. Within the pathway, cns2 catalyzes dephosphorylation of 3'-AMP to produce 2'- carbonyl-3'-deoxyadenosine (2'-C-3'-dA). The first step of cordycepin biosynthesis involves hydroxyl phosphorylation of the 3'-OH position on adenosine to produce adenosine-3'-monophosphate (3'-AMP), catalyzed by kinase activity of cns3. Next, 3'-AMP is dephosphorylated to 2'-carbonyl-3'-deoxyadenosine by cns2, which is finally converted to cordycepin (3'-deoxyadenosine) by the oxidoreductase cns1.",dGTPase preferentially hydrolyzes dGTP over the other canonical NTPs.,No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008832,GO:0016787,GO:0017111,GO:0017111,GO:0017111,,0.5381,0.2529,0.2529,0.2529,,4,0.3242,0.2854,no
CNS2_CORMM,G3JF09,Prot2Text,Eukaryota,345,"Metal-dependent phosphohydrolase; part of the gene cluster that mediates the biosynthesis of cordycepin (COR) and pentostatin (PTN), two adenosine analogs with related bioactivity profiles as both mimic adenosine and can inhibit some of the processes that are adenosine dependent. Within the pathway, cns2 catalyzes dephosphorylation of 3'-AMP to produce 2'- carbonyl-3'-deoxyadenosine (2'-C-3'-dA). The first step of cordycepin biosynthesis involves hydroxyl phosphorylation of the 3'-OH position on adenosine to produce adenosine-3'-monophosphate (3'-AMP), catalyzed by kinase activity of cns3. Next, 3'-AMP is dephosphorylated to 2'-carbonyl-3'-deoxyadenosine by cns2, which is finally converted to cordycepin (3'-deoxyadenosine) by the oxidoreductase cns1.",dGTPase preferentially hydrolyzes dGTP over the other canonical NTPs.,No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008832,GO:0017111,,GO:0016787,GO:0004407,GO:0016787,0.2529,,0.5381,0.1631,0.5381,4,0.373,0.2854,no
CNS2_CORMM,G3JF09,ProtT3,Eukaryota,345,"Metal-dependent phosphohydrolase; part of the gene cluster that mediates the biosynthesis of cordycepin (COR) and pentostatin (PTN), two adenosine analogs with related bioactivity profiles as both mimic adenosine and can inhibit some of the processes that are adenosine dependent. Within the pathway, cns2 catalyzes dephosphorylation of 3'-AMP to produce 2'- carbonyl-3'-deoxyadenosine (2'-C-3'-dA). The first step of cordycepin biosynthesis involves hydroxyl phosphorylation of the 3'-OH position on adenosine to produce adenosine-3'-monophosphate (3'-AMP), catalyzed by kinase activity of cns3. Next, 3'-AMP is dephosphorylated to 2'-carbonyl-3'-deoxyadenosine by cns2, which is finally converted to cordycepin (3'-deoxyadenosine) by the oxidoreductase cns1.",Belongs to the Nudix hydrolase family,No,Vague,Vague,Vague,Vague,not-Yes,GO:0008832,GO:0016787,GO:0016787,GO:0016462,GO:0016787,GO:0016787,0.5381,0.5381,0.2943,0.5381,0.5381,5,0.4893,0.2854,no
CNS2_CORMM,G3JF09,ProtTale,Eukaryota,345,"Metal-dependent phosphohydrolase; part of the gene cluster that mediates the biosynthesis of cordycepin (COR) and pentostatin (PTN), two adenosine analogs with related bioactivity profiles as both mimic adenosine and can inhibit some of the processes that are adenosine dependent. Within the pathway, cns2 catalyzes dephosphorylation of 3'-AMP to produce 2'- carbonyl-3'-deoxyadenosine (2'-C-3'-dA). The first step of cordycepin biosynthesis involves hydroxyl phosphorylation of the 3'-OH position on adenosine to produce adenosine-3'-monophosphate (3'-AMP), catalyzed by kinase activity of cns3. Next, 3'-AMP is dephosphorylated to 2'-carbonyl-3'-deoxyadenosine by cns2, which is finally converted to cordycepin (3'-deoxyadenosine) by the oxidoreductase cns1.",DNA repair enzyme that has both 3'-->5' exonuclease and 5'-->3' exonuclease activities.,No,No,No,No,No,not-Yes,GO:0008832,GO:0004527; GO:0004529,GO:0004527; GO:0008408,GO:0008408; GO:0004534,GO:0004527,GO:0004527,0.4058,0.4239,0.3479,0.4425,0.4425,5,0.4125,0.2854,no
CNS2_CORMM,G3JF09,Protein2Text,Eukaryota,345,"Metal-dependent phosphohydrolase; part of the gene cluster that mediates the biosynthesis of cordycepin (COR) and pentostatin (PTN), two adenosine analogs with related bioactivity profiles as both mimic adenosine and can inhibit some of the processes that are adenosine dependent. Within the pathway, cns2 catalyzes dephosphorylation of 3'-AMP to produce 2'- carbonyl-3'-deoxyadenosine (2'-C-3'-dA). The first step of cordycepin biosynthesis involves hydroxyl phosphorylation of the 3'-OH position on adenosine to produce adenosine-3'-monophosphate (3'-AMP), catalyzed by kinase activity of cns3. Next, 3'-AMP is dephosphorylated to 2'-carbonyl-3'-deoxyadenosine by cns2, which is finally converted to cordycepin (3'-deoxyadenosine) by the oxidoreductase cns1.","The molecular function of this protein is not specified in the provided text. However, it is a phosphatase, which suggests that its molecular function is to remove phosphate groups from molecules.",Maybe,Vague,Vague,Vague,Maybe,not-Yes,GO:0008832,GO:0004721,GO:0016791,GO:0016791,GO:0016791,GO:0016791,0.5251,0.6335,0.6335,0.6335,0.6335,5,0.6118,0.2854,no
CNS2_CORMM,G3JF09,Reference,Eukaryota,345,"Metal-dependent phosphohydrolase; part of the gene cluster that mediates the biosynthesis of cordycepin (COR) and pentostatin (PTN), two adenosine analogs with related bioactivity profiles as both mimic adenosine and can inhibit some of the processes that are adenosine dependent. Within the pathway, cns2 catalyzes dephosphorylation of 3'-AMP to produce 2'- carbonyl-3'-deoxyadenosine (2'-C-3'-dA). The first step of cordycepin biosynthesis involves hydroxyl phosphorylation of the 3'-OH position on adenosine to produce adenosine-3'-monophosphate (3'-AMP), catalyzed by kinase activity of cns3. Next, 3'-AMP is dephosphorylated to 2'-carbonyl-3'-deoxyadenosine by cns2, which is finally converted to cordycepin (3'-deoxyadenosine) by the oxidoreductase cns1.","Metal-dependent phosphohydrolase; part of the gene cluster that mediates the biosynthesis of cordycepin (COR) and pentostatin (PTN), two adenosine analogs with related bioactivity profiles as both mimic adenosine and can inhibit some of the processes that are adenosine dependent. Within the pathway, cns2 catalyzes dephosphorylation of 3'-AMP to produce 2'- carbonyl-3'-deoxyadenosine (2'-C-3'-dA). The first step of cordycepin biosynthesis involves hydroxyl phosphorylation of the 3'-OH position on adenosine to produce adenosine-3'-monophosphate (3'-AMP), catalyzed by kinase activity of cns3. Next, 3'-AMP is dephosphorylated to 2'-carbonyl-3'-deoxyadenosine by cns2, which is finally converted to cordycepin (3'-deoxyadenosine) by the oxidoreductase cns1.",,,,,,,GO:0008832,GO:0016791,GO:0016791,GO:0016791; GO:0046872,GO:0016791,GO:0016791,0.6335,0.6335,0.4481,0.6335,0.6335,5,0.5964,0.2854,no
DCI1_PYRO7,G4NCP4,ESM2Text,Eukaryota,280,"Peroxisomal di-isomerase that is involved in fatty acid metabolism enzyme by converting 3,5-dienoyl-CoAs to the corresponding 2,4-dienoyl-CoAs. Involved in fatty acid beta- oxidation, which is important for lipid droplets degradation and infectious growth.","Decarboxylates ethylmalonyl-CoA, a potentially toxic metabolite, to form butyryl-CoA, suggesting it might be involved in metabolite proofreading. Also has methylmalonyl-CoA decarboxylase activity at lower level.",No,No,No,No,No,not-Yes,GO:0004165; GO:0051750,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.2353,0.2353,0.2353,0.2353,0.2353,5,0.2353,0.1694,no
DCI1_PYRO7,G4NCP4,Prot2Text,Eukaryota,280,"Peroxisomal di-isomerase that is involved in fatty acid metabolism enzyme by converting 3,5-dienoyl-CoAs to the corresponding 2,4-dienoyl-CoAs. Involved in fatty acid beta- oxidation, which is important for lipid droplets degradation and infectious growth.","Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004165; GO:0051750,GO:0004300,GO:0004300,GO:0004300,GO:0004300,GO:0004300,0.1998,0.1998,0.1998,0.1998,0.1998,5,0.1998,0.1694,no
DCI1_PYRO7,G4NCP4,ProtT3,Eukaryota,280,"Peroxisomal di-isomerase that is involved in fatty acid metabolism enzyme by converting 3,5-dienoyl-CoAs to the corresponding 2,4-dienoyl-CoAs. Involved in fatty acid beta- oxidation, which is important for lipid droplets degradation and infectious growth.",Peroxisome. Belongs to the enoyl-CoA hydratase/isomerase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004165; GO:0051750,GO:0004300,GO:0004300,GO:0004300,GO:0004300,GO:0004300,0.1998,0.1998,0.1998,0.1998,0.1998,5,0.1998,0.1694,no
DCI1_PYRO7,G4NCP4,ProtTale,Eukaryota,280,"Peroxisomal di-isomerase that is involved in fatty acid metabolism enzyme by converting 3,5-dienoyl-CoAs to the corresponding 2,4-dienoyl-CoAs. Involved in fatty acid beta- oxidation, which is important for lipid droplets degradation and infectious growth.","Enoyl-CoA hydratase; part of the gene clusters that mediate the biosynthesis of the host-selective toxins (HSTs) AF-toxins responsible for Alternaria black spot of strawberry disease by the strawberry pathotype. AF-toxin I and III are valine derivatives of 2,3-dyhydroxy-isovaleric acid and 2-hydroxy-isovaleric acid respectively, while AF II is an isoleucine derivative of 2- hydroxy-valeric acid. These derivatives are bound to a 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0004165; GO:0051750,GO:0016829,GO:0004300,GO:0004300,GO:0004300,GO:0004300,0.3552,0.1998,0.1998,0.1998,0.1998,5,0.2309,0.1694,no
DCI1_PYRO7,G4NCP4,Protein2Text,Eukaryota,280,"Peroxisomal di-isomerase that is involved in fatty acid metabolism enzyme by converting 3,5-dienoyl-CoAs to the corresponding 2,4-dienoyl-CoAs. Involved in fatty acid beta- oxidation, which is important for lipid droplets degradation and infectious growth.",The molecular function of this protein is involved in the synthesis of fatty acids. It is a component of the mitochondrial fatty acid synthase (FAS) that catalyzes the formation of long-chain saturated fatty acids from acetyl-CoA and malonyl-CoA.,No,No,No,No,No,not-Yes,GO:0004165; GO:0051750,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.1998,0.1998,0.1998,0.1998,0.1998,5,0.1998,0.1694,no
DCI1_PYRO7,G4NCP4,Reference,Eukaryota,280,"Peroxisomal di-isomerase that is involved in fatty acid metabolism enzyme by converting 3,5-dienoyl-CoAs to the corresponding 2,4-dienoyl-CoAs. Involved in fatty acid beta- oxidation, which is important for lipid droplets degradation and infectious growth.","Peroxisomal di-isomerase that is involved in fatty acid metabolism enzyme by converting 3,5-dienoyl-CoAs to the corresponding 2,4-dienoyl-CoAs. Involved in fatty acid beta- oxidation, which is important for lipid droplets degradation and infectious growth.",,,,,,,GO:0004165; GO:0051750,GO:0004165,GO:0004165,GO:0016853,GO:0016863,GO:0016853,0.9096,0.9096,0.6019,0.8582,0.6019,5,0.7762,0.1694,no
CHS2_PHYSP,G4YM00,ESM2Text,Eukaryota,901,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer (Probable). Does not seem to be involved in mycelial growth, nor in sporangial production, zoospore release and virulence.","Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4194,no
CHS2_PHYSP,G4YM00,Prot2Text,Eukaryota,901,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer (Probable). Does not seem to be involved in mycelial growth, nor in sporangial production, zoospore release and virulence.","Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4194,no
CHS2_PHYSP,G4YM00,ProtT3,Eukaryota,901,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer (Probable). Does not seem to be involved in mycelial growth, nor in sporangial production, zoospore release and virulence.","Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer. Cell membrane; Multi-pass membrane protein. Belongs to the chitin synthase family. Class III subfamily",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4194,no
CHS2_PHYSP,G4YM00,ProtTale,Eukaryota,901,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer (Probable). Does not seem to be involved in mycelial growth, nor in sporangial production, zoospore release and virulence.","Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004100,GO:0004100,GO:0004568,GO:0004100,GO:0004100,GO:0004100,1.0,0.1603,1.0,1.0,1.0,5,0.8321,0.4194,no
CHS2_PHYSP,G4YM00,Protein2Text,Eukaryota,901,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer (Probable). Does not seem to be involved in mycelial growth, nor in sporangial production, zoospore release and virulence.","The molecular function of this protein is related to membrane-bound O-glycan biosynthesis, specifically as a galactosyltransferase, which catalyzes the transfer of galactose from UDP-galactose to a glycan acceptor molecule.",No,No,No,No,No,not-Yes,GO:0004100,GO:0008378,GO:0008378,GO:0016757,GO:0008378,GO:0008378,0.5846,0.5846,0.5917,0.5846,0.5846,5,0.586,0.4194,no
CHS2_PHYSP,G4YM00,Reference,Eukaryota,901,"Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer (Probable). Does not seem to be involved in mycelial growth, nor in sporangial production, zoospore release and virulence.","Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non- reducing end of the growing chitin polymer (Probable). Does not seem to be involved in mycelial growth, nor in sporangial production, zoospore release and virulence.",,,,,,,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4194,no
CHHY1_CAEEL,G5ECE8,ESM2Text,Eukaryota,458,"Endo-beta-galactosaminidase that specifically hydrolyzes chondroitin, releasing GlcUA-beta-(1->3)-GalNAc-beta-(1->4)-GlcUA-beta- (1->3)-GalNAc as the main product. Also hydrolyzes to a lesser extent chondroitin sulfates (CS-A, CS-C) and hyaluronic acid. May regulate the function of chondroitin in cell division.",May have a role in promoting tumor progression. May block the TGFB1-enhanced cell growth.,No,No,Vague,No,No,not-Yes,GO:0015929; GO:0004415,,,,,,,,,,,0,,0.2963,no
CHHY1_CAEEL,G5ECE8,Prot2Text,Eukaryota,458,"Endo-beta-galactosaminidase that specifically hydrolyzes chondroitin, releasing GlcUA-beta-(1->3)-GalNAc-beta-(1->4)-GlcUA-beta- (1->3)-GalNAc as the main product. Also hydrolyzes to a lesser extent chondroitin sulfates (CS-A, CS-C) and hyaluronic acid. May regulate the function of chondroitin in cell division.","Has endoglucanase activity on carboxymethyl-cellulose (CMC), fungal glucan, arabinoxylan and pectin. Involved in the fertilization process. Involved in the promotion of axis formation during embryogenesis. Involved in the degradation of fibronectin.",No,Maybe,No,No,Maybe,not-Yes,GO:0015929; GO:0004415,GO:0008810,GO:0008810,GO:0008810,GO:0008810,GO:0008810,0.6971,0.6971,0.6971,0.6971,0.6971,5,0.6971,0.2963,no
CHHY1_CAEEL,G5ECE8,ProtT3,Eukaryota,458,"Endo-beta-galactosaminidase that specifically hydrolyzes chondroitin, releasing GlcUA-beta-(1->3)-GalNAc-beta-(1->4)-GlcUA-beta- (1->3)-GalNAc as the main product. Also hydrolyzes to a lesser extent chondroitin sulfates (CS-A, CS-C) and hyaluronic acid. May regulate the function of chondroitin in cell division.",Hydrolyzes high molecular weight hyaluronic acid to produce small oligosaccharides. Secreted. Belongs to the glycosyl hydrolase 56 family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0015929; GO:0004415,GO:0004415,GO:0004415,GO:0004415,GO:0004415,GO:0004415,0.9564,0.9564,0.9564,0.9564,0.9564,5,0.9564,0.2963,no
CHHY1_CAEEL,G5ECE8,ProtTale,Eukaryota,458,"Endo-beta-galactosaminidase that specifically hydrolyzes chondroitin, releasing GlcUA-beta-(1->3)-GalNAc-beta-(1->4)-GlcUA-beta- (1->3)-GalNAc as the main product. Also hydrolyzes to a lesser extent chondroitin sulfates (CS-A, CS-C) and hyaluronic acid. May regulate the function of chondroitin in cell division.","Hyaluronidase catalyzes the hydrolysis of hyaluronic acid (HA), an anionic, non-sulfated glycosaminoglycan composed of D-glucuronic acid and N-acetyl-D-glucosamine residues (Probable). Hydrolyzes low molecular weight hyaluronan (HA) into smaller fragments that are not biologically active (Probable).",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0015929; GO:0004415,GO:0004415,GO:0004415,GO:0004415,GO:0004415,GO:0004415,0.9564,0.9564,0.9564,0.9564,0.9564,5,0.9564,0.2963,no
CHHY1_CAEEL,G5ECE8,Protein2Text,Eukaryota,458,"Endo-beta-galactosaminidase that specifically hydrolyzes chondroitin, releasing GlcUA-beta-(1->3)-GalNAc-beta-(1->4)-GlcUA-beta- (1->3)-GalNAc as the main product. Also hydrolyzes to a lesser extent chondroitin sulfates (CS-A, CS-C) and hyaluronic acid. May regulate the function of chondroitin in cell division.","The molecular function of this protein is to degrade hyaluronic acid, a type of glycosaminoglycan that is a major component of the extracellular matrix. Specifically, it is a hyaluronidase, which means it breaks down hyaluronic acid into smaller fragments.",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0015929; GO:0004415,GO:0004415,GO:0004415,GO:0004415,GO:0004415,GO:0004415,0.9564,0.9564,0.9564,0.9564,0.9564,5,0.9564,0.2963,no
CHHY1_CAEEL,G5ECE8,Reference,Eukaryota,458,"Endo-beta-galactosaminidase that specifically hydrolyzes chondroitin, releasing GlcUA-beta-(1->3)-GalNAc-beta-(1->4)-GlcUA-beta- (1->3)-GalNAc as the main product. Also hydrolyzes to a lesser extent chondroitin sulfates (CS-A, CS-C) and hyaluronic acid. May regulate the function of chondroitin in cell division.","Endo-beta-galactosaminidase that specifically hydrolyzes chondroitin, releasing GlcUA-beta-(1->3)-GalNAc-beta-(1->4)-GlcUA-beta- (1->3)-GalNAc as the main product. Also hydrolyzes to a lesser extent chondroitin sulfates (CS-A, CS-C) and hyaluronic acid. May regulate the function of chondroitin in cell division.",,,,,,,GO:0015929; GO:0004415,GO:0016798,GO:0004553,GO:0004553,GO:0004553,GO:0004553,0.7015,0.8234,0.8234,0.8234,0.8234,5,0.799,0.2963,no
CGDA2_ARTG1,H0QPL9,ESM2Text,Bacteria,352,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C8- glycosylated compound 3''-dehydroorientin (3''-oxo-orientin).,"Involved in the biosynthesis of D-apiose. Catalyzes the hydration of L-erythrulose 1-phosphate to D-erythrulose 1,5-bisphosphate. Can also use L-ribulose 1-phosphate and L-xylulose 1-phosphate as substrates, but not D-ribulose 1-phosphate, D-glucose 1-phosphate, D-sorbose 1-phosphate, D-glucitol or D-sorbitol.",No,No,No,No,No,not-Yes,GO:0016829; GO:0046872,,,,,,,,,,,0,,0.3234,no
CGDA2_ARTG1,H0QPL9,Prot2Text,Bacteria,352,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C8- glycosylated compound 3''-dehydroorientin (3''-oxo-orientin).,Catalyzes the dehydration of D-xylonic acid to 2-dehydro-3-deoxy-D-pentonate.,No,No,No,No,No,not-Yes,GO:0016829; GO:0046872,,,,,,,,,,,0,,0.3234,no
CGDA2_ARTG1,H0QPL9,ProtT3,Bacteria,352,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C8- glycosylated compound 3''-dehydroorientin (3''-oxo-orientin).,Catalyzes the isomerization of L-rhamnose to L-rhamnulose. Catalyzes the isomerization of L-rhamnose to L-rhamnulose. Belongs to the rhamnose isomerase family. Belongs to the rhamnose isomerase family,No,No,No,No,No,not-Yes,GO:0016829; GO:0046872,,,,,,,,,,,0,,0.3234,no
CGDA2_ARTG1,H0QPL9,ProtTale,Bacteria,352,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C8- glycosylated compound 3''-dehydroorientin (3''-oxo-orientin).,Allows the bacterium to use galactose as the sole source of carbon and energy for growth.,No,No,No,No,No,not-Yes,GO:0016829; GO:0046872,,,,,,,,,,,0,,0.3234,no
CGDA2_ARTG1,H0QPL9,Protein2Text,Bacteria,352,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C8- glycosylated compound 3''-dehydroorientin (3''-oxo-orientin).,"The molecular function of this protein is an oxidoreductase activity, specifically it catalyzes the oxidation of D-sorbitol to D-fructose, which is a key step in the metabolism of sorbitol. This protein is a part of the sorbitol dehydrogenase enzyme, which is involved in the conversion of sorbitol to fructose in various organisms. The sorbitol dehydrogenase enzyme is a flavin-containing oxidoreductase that uses NAD+ as a coenzyme. The enzyme is composed of two subunits, a catalytic subunit and a regulatory subunit, which are both required for the enzyme's activity. The catalytic subunit contains the active site where the sorbitol is oxidized, and the regulatory subunit is involved in the enzyme's stability and activity. The sorbitol dehydrogenase enzyme plays a crucial role in the metabolism of sorbitol, which is an important sugar alcohol in various organisms, including humans. The enzyme is also involved in the metabolism of other sugar alcohols, such as mannitol and xylitol. The sorbitol dehydrogenase enzyme is also involved in the regulation of glycolysis and gluconeogenesis, two important metabolic pathways in cells. The enzyme is also involved in the production of reactive oxygen species (ROS), which are important signaling molecules in cells. The sorbitol dehydrogenase enzyme is also involved in the regulation of cell growth and differentiation, and its activity has been implicated in various diseases, including cancer and diabetes. 

In summary, the molecular function of this protein is an oxidoreductase activity, specifically it catalyzes the oxidation of D-sorbitol to D-fructose, which is a key step in the metabolism of sorbitol. The enzyme is also involved in the regulation of glycolysis and gluconeogenesis, the production of ROS, and the regulation of cell growth and differentiation.",No,No,No,No,No,not-Yes,GO:0016829; GO:0046872,,,,,,,,,,,0,,0.3234,no
CGDA2_ARTG1,H0QPL9,Reference,Bacteria,352,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C8- glycosylated compound 3''-dehydroorientin (3''-oxo-orientin).,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C8- glycosylated compound 3''-dehydroorientin (3''-oxo-orientin).,,,,,,,GO:0016829; GO:0046872,GO:0016830,GO:0016830,GO:0016830,GO:0016830,GO:0016829,0.5852,0.5852,0.5852,0.5852,0.7193,5,0.612,0.3234,no
FGR1_GIBZE,I1RLA7,ESM2Text,Eukaryota,2563,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the tetraketides fugralins such as linear fugralin A and cyclic fugralin B, volatile compounds that play a role in the asexual reproductive cycle but are not involved in pathogenicity. One of the key features of fugralins is the presence of a double methyl group, which is only rarely encountered in fungal secondary metabolites. As the fugralins cluster does not contain an independent methyltransferase, the PKS FGR1 is probably responsible for adding two methyl groups to the same carbon atom (Probable). Fugralin B is similar to fugralin A except for a cyclization between the carboxylic acid C-8 and the alcohol on C-4 resulting in a six membered lactone ring, probably catalyzed by the cyclase FGR4 (Probable). The exact role of the individual cluster genes remains unknown and further work is needed to unravel the biosynthetic pathway (Probable).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcsC",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177,,,,,,,,,,,0,,0.2449,no
FGR1_GIBZE,I1RLA7,Prot2Text,Eukaryota,2563,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the tetraketides fugralins such as linear fugralin A and cyclic fugralin B, volatile compounds that play a role in the asexual reproductive cycle but are not involved in pathogenicity. One of the key features of fugralins is the presence of a double methyl group, which is only rarely encountered in fungal secondary metabolites. As the fugralins cluster does not contain an independent methyltransferase, the PKS FGR1 is probably responsible for adding two methyl groups to the same carbon atom (Probable). Fugralin B is similar to fugralin A except for a cyclization between the carboxylic acid C-8 and the alcohol on C-4 resulting in a six membered lactone ring, probably catalyzed by the cyclase FGR4 (Probable). The exact role of the individual cluster genes remains unknown and further work is needed to unravel the biosynthetic pathway (Probable).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177,GO:0016747,,,GO:0016747,GO:0016746,0.6148,,,0.6148,0.5549,3,0.5948,0.2449,no
FGR1_GIBZE,I1RLA7,ProtT3,Eukaryota,2563,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the tetraketides fugralins such as linear fugralin A and cyclic fugralin B, volatile compounds that play a role in the asexual reproductive cycle but are not involved in pathogenicity. One of the key features of fugralins is the presence of a double methyl group, which is only rarely encountered in fungal secondary metabolites. As the fugralins cluster does not contain an independent methyltransferase, the PKS FGR1 is probably responsible for adding two methyl groups to the same carbon atom (Probable). Fugralin B is similar to fugralin A except for a cyclization between the carboxylic acid C-8 and the alcohol on C-4 resulting in a six membered lactone ring, probably catalyzed by the cyclase FGR4 (Probable). The exact role of the individual cluster genes remains unknown and further work is needed to unravel the biosynthetic pathway (Probable).","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177,GO:0016746,GO:0016746,,GO:0016746,GO:0016747,0.5549,0.5549,,0.5549,0.6148,4,0.5699,0.2449,no
FGR1_GIBZE,I1RLA7,ProtTale,Eukaryota,2563,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the tetraketides fugralins such as linear fugralin A and cyclic fugralin B, volatile compounds that play a role in the asexual reproductive cycle but are not involved in pathogenicity. One of the key features of fugralins is the presence of a double methyl group, which is only rarely encountered in fungal secondary metabolites. As the fugralins cluster does not contain an independent methyltransferase, the PKS FGR1 is probably responsible for adding two methyl groups to the same carbon atom (Probable). Fugralin B is similar to fugralin A except for a cyclization between the carboxylic acid C-8 and the alcohol on C-4 resulting in a six membered lactone ring, probably catalyzed by the cyclase FGR4 (Probable). The exact role of the individual cluster genes remains unknown and further work is needed to unravel the biosynthetic pathway (Probable).","Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. Within the pathway, ptmG catalyzes the last step by condensing indole-3-glycerol phosphate (IGP) with farnesyl diphosphate (FPP) to form 3-geranyl-1H-indole-2(3H)-one. The geranylgeranyl diphosphate (GGPP)-dependent prenyltransferase ptmA is proposed to catalyze the conversion of indole-3-glycerol phosphate (IP) to",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177,GO:0016491,GO:0016757,,,GO:0016746,0.5675,0.4067,,,0.5549,3,0.5097,0.2449,no
FGR1_GIBZE,I1RLA7,Protein2Text,Eukaryota,2563,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the tetraketides fugralins such as linear fugralin A and cyclic fugralin B, volatile compounds that play a role in the asexual reproductive cycle but are not involved in pathogenicity. One of the key features of fugralins is the presence of a double methyl group, which is only rarely encountered in fungal secondary metabolites. As the fugralins cluster does not contain an independent methyltransferase, the PKS FGR1 is probably responsible for adding two methyl groups to the same carbon atom (Probable). Fugralin B is similar to fugralin A except for a cyclization between the carboxylic acid C-8 and the alcohol on C-4 resulting in a six membered lactone ring, probably catalyzed by the cyclase FGR4 (Probable). The exact role of the individual cluster genes remains unknown and further work is needed to unravel the biosynthetic pathway (Probable).","This protein is involved in the synthesis of a pigment. More specifically, it is involved in the synthesis of a type of pigment that is found in the cuticle of insects.",No,Vague,Vague,Vague,No,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177,,,,,,,,,,,0,,0.2449,no
FGR1_GIBZE,I1RLA7,Reference,Eukaryota,2563,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the tetraketides fugralins such as linear fugralin A and cyclic fugralin B, volatile compounds that play a role in the asexual reproductive cycle but are not involved in pathogenicity. One of the key features of fugralins is the presence of a double methyl group, which is only rarely encountered in fungal secondary metabolites. As the fugralins cluster does not contain an independent methyltransferase, the PKS FGR1 is probably responsible for adding two methyl groups to the same carbon atom (Probable). Fugralin B is similar to fugralin A except for a cyclization between the carboxylic acid C-8 and the alcohol on C-4 resulting in a six membered lactone ring, probably catalyzed by the cyclase FGR4 (Probable). The exact role of the individual cluster genes remains unknown and further work is needed to unravel the biosynthetic pathway (Probable).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the tetraketides fugralins such as linear fugralin A and cyclic fugralin B, volatile compounds that play a role in the asexual reproductive cycle but are not involved in pathogenicity. One of the key features of fugralins is the presence of a double methyl group, which is only rarely encountered in fungal secondary metabolites. As the fugralins cluster does not contain an independent methyltransferase, the PKS FGR1 is probably responsible for adding two methyl groups to the same carbon atom (Probable). Fugralin B is similar to fugralin A except for a cyclization between the carboxylic acid C-8 and the alcohol on C-4 resulting in a six membered lactone ring, probably catalyzed by the cyclase FGR4 (Probable). The exact role of the individual cluster genes remains unknown and further work is needed to unravel the biosynthetic pathway (Probable).",,,,,,,GO:0004315; GO:0004312; GO:0016491; GO:0031177,GO:0016746,GO:0016746,GO:0016747; GO:0008168,GO:0016747,GO:0016746,0.5549,0.5549,0.5801,0.6148,0.5549,5,0.5719,0.2449,no
CGDB_EUBC6,I5AX49,ESM2Text,Bacteria,147,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C6-glycosylated compounds 3''-dehydroisoorientin (3''-oxo- homoorientin) and 3''-dehydroisovitexin (3''-oxo-isovitexin).,PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.,No,No,No,No,No,not-Yes,GO:0016829,GO:0003755,GO:0003755,GO:0003755,GO:0003755,GO:0003755,0.3794,0.3794,0.3794,0.3794,0.3794,5,0.3794,0.3053,no
CGDB_EUBC6,I5AX49,Prot2Text,Bacteria,147,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C6-glycosylated compounds 3''-dehydroisoorientin (3''-oxo- homoorientin) and 3''-dehydroisovitexin (3''-oxo-isovitexin).,Unknown.,No,Vague,Vague,Vague,No,not-Yes,GO:0016829,,,,,,,,,,,0,,0.3053,no
CGDB_EUBC6,I5AX49,ProtT3,Bacteria,147,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C6-glycosylated compounds 3''-dehydroisoorientin (3''-oxo- homoorientin) and 3''-dehydroisovitexin (3''-oxo-isovitexin).,Belongs to the hcp family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016829,,,,,,,,,,,0,,0.3053,no
CGDB_EUBC6,I5AX49,ProtTale,Bacteria,147,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C6-glycosylated compounds 3''-dehydroisoorientin (3''-oxo- homoorientin) and 3''-dehydroisovitexin (3''-oxo-isovitexin).,"Catalyzes the cleavage of the glycosidic bond between the C1 and C3 carbons of D-galactose-1-phosphate (Gal-1-P) to yield D-glucose 6-phosphate and alpha,beta-1,6-lactone. Also able to catalyze the reverse reaction, i.e. the formation of Gal-1-P from D-glucose 6-phosphate and alpha,beta-1,6-lactone.",No,No,No,No,No,not-Yes,GO:0016829,GO:0016787,GO:0016787,GO:0004553,GO:0004553,GO:0004553,0.5902,0.5902,0.4071,0.4071,0.4071,5,0.4803,0.3053,no
CGDB_EUBC6,I5AX49,Protein2Text,Bacteria,147,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C6-glycosylated compounds 3''-dehydroisoorientin (3''-oxo- homoorientin) and 3''-dehydroisovitexin (3''-oxo-isovitexin).,"The molecular function of this protein is not explicitly stated in the provided information. However, based on its classification as a ribosome in silico associated protein, it is likely that this protein is involved in protein synthesis or ribosome biogenesis. Further research would be needed to determine its specific molecular function. 
Please let me know if you need further clarification or information.",Vague,Vague,No,Vague,Vague,not-Yes,GO:0016829,,,,,,,,,,,0,,0.3053,no
CGDB_EUBC6,I5AX49,Reference,Bacteria,147,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C6-glycosylated compounds 3''-dehydroisoorientin (3''-oxo- homoorientin) and 3''-dehydroisovitexin (3''-oxo-isovitexin).,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C6-glycosylated compounds 3''-dehydroisoorientin (3''-oxo- homoorientin) and 3''-dehydroisovitexin (3''-oxo-isovitexin).,,,,,,,GO:0016829,GO:0016830,GO:0016830,GO:0016830,GO:0016830,GO:0016829,0.8145,0.8145,0.8145,0.8145,1.0,5,0.8516,0.3053,no
BAGB_MYCTU,I6Y498,ESM2Text,Bacteria,386,"Component of the heterodimeric BagAB ATPase complex, whose two subunits are actively involved in ATP hydrolysis. The ATPase activity is required to mediate resistance against nitric oxide (NO) and elevated levels of glycerol.","ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting.",No,No,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887,GO:0016887,1.0,1.0,1.0,0.6869,0.6869,5,0.8748,0.5311,no
BAGB_MYCTU,I6Y498,Prot2Text,Bacteria,386,"Component of the heterodimeric BagAB ATPase complex, whose two subunits are actively involved in ATP hydrolysis. The ATPase activity is required to mediate resistance against nitric oxide (NO) and elevated levels of glycerol.","ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors GET1 and GET2, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the GET1-GET2 receptor, and returning it to the cytosol to initiate a new round of targeting. Cooperates with the HDEL receptor ERD2 to mediate the ATP-dependent retrieval of resident ER proteins that contain a C-terminal H-D-E-L retention signal from the Golgi to the ER. Involved in low-level resistance to the oxyanions arsenite and arsenate, and in heat tolerance.",No,No,Maybe,No,No,not-Yes,GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0016887,GO:0016887,GO:0016887,GO:0016887; GO:0005524,1.0,0.6869,0.6869,0.6869,1.0,5,0.8121,0.5311,no
BAGB_MYCTU,I6Y498,ProtT3,Bacteria,386,"Component of the heterodimeric BagAB ATPase complex, whose two subunits are actively involved in ATP hydrolysis. The ATPase activity is required to mediate resistance against nitric oxide (NO) and elevated levels of glycerol.",Anion-transporting ATPase. Catalyzes the extrusion of arsenite (By similarity). Belongs to the arsA ATPase family,Maybe,No,Maybe,Maybe,No,not-Yes,GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0015446; GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,1.0,1.0,0.8403,1.0,1.0,5,0.9681,0.5311,no
BAGB_MYCTU,I6Y498,ProtTale,Bacteria,386,"Component of the heterodimeric BagAB ATPase complex, whose two subunits are actively involved in ATP hydrolysis. The ATPase activity is required to mediate resistance against nitric oxide (NO) and elevated levels of glycerol.",Anion-transporting ATPase. Catalyzes the extrusion of arsenite.,Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887,GO:0005524; GO:0015105,GO:0005524; GO:0016887; GO:0015105,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.5621,0.8249,1.0,1.0,1.0,5,0.8774,0.5311,no
BAGB_MYCTU,I6Y498,Protein2Text,Bacteria,386,"Component of the heterodimeric BagAB ATPase complex, whose two subunits are actively involved in ATP hydrolysis. The ATPase activity is required to mediate resistance against nitric oxide (NO) and elevated levels of glycerol.","The molecular function of this protein is likely to be a component of the bacterial envelope, specifically a membrane protein.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0005524; GO:0016887,,,,,,,,,,,0,,0.5311,no
BAGB_MYCTU,I6Y498,Reference,Bacteria,386,"Component of the heterodimeric BagAB ATPase complex, whose two subunits are actively involved in ATP hydrolysis. The ATPase activity is required to mediate resistance against nitric oxide (NO) and elevated levels of glycerol.","Component of the heterodimeric BagAB ATPase complex, whose two subunits are actively involved in ATP hydrolysis. The ATPase activity is required to mediate resistance against nitric oxide (NO) and elevated levels of glycerol.",,,,,,,GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5311,no
TENS_BEAB2,J4KMC1,ESM2Text,Eukaryota,4235,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of tenellin-type 2-pyridones, iron-chelating compounds involved in iron stress tolerance, competition with the natural competitor fungus Metarhizium robertsii and insect hosts infection. TenS catalyzes the assembly of the polyketide-amino acid backbone. Because tenS lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase tenC. Upon formation of the polyketide backbone on the thiotemplate, the triketide is transferred to the NRPS module and linked to tyrosine to produce the pyrrolidine-2-dione intermediates, including pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The pathway begins with the assembly of the polyketide-amino acid backbone by the hybrid PKS-NRPS tenS with the help of the enoyl reductase tenC. These enzymes catalyze the synthesis of the pyrrolidine-2-dione intermediates pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The cytochrome P450 monooxygenase tenA then catalyzes an oxidative ring expansion of pretenellin A and 14-hydropretellenin A to form the 2- pyridone core, leading to pretenellin B and pyridovericin, respectively. The cytochrome P450 monooxygenase tenB is then required for the selective N-hydroxylation of the 2-pyridone nitrogen of yield tellinin and 15-hydroxytellenin (15-HT), respectively. The UDP- glucosyltransferase GT1 and the methyltransferase MT1, located outside the tenS gene cluster, contribute to the stepwise glycosylation and methylation of 15-HT to obtain the glycoside pyridovericin-N-O-(4-O- methyl-beta-D-glucopyranoside) (PMGP). Additional related compounds such as 1-O-methyl-15-HT, (8Z)-1-O-methyl-15-HT, and O-methyltenellin A are also produced but the enzymes involved in their biosynthesis have still to be determined.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential tr",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,,,,,,,,,,,0,,0.3056,no
TENS_BEAB2,J4KMC1,Prot2Text,Eukaryota,4235,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of tenellin-type 2-pyridones, iron-chelating compounds involved in iron stress tolerance, competition with the natural competitor fungus Metarhizium robertsii and insect hosts infection. TenS catalyzes the assembly of the polyketide-amino acid backbone. Because tenS lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase tenC. Upon formation of the polyketide backbone on the thiotemplate, the triketide is transferred to the NRPS module and linked to tyrosine to produce the pyrrolidine-2-dione intermediates, including pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The pathway begins with the assembly of the polyketide-amino acid backbone by the hybrid PKS-NRPS tenS with the help of the enoyl reductase tenC. These enzymes catalyze the synthesis of the pyrrolidine-2-dione intermediates pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The cytochrome P450 monooxygenase tenA then catalyzes an oxidative ring expansion of pretenellin A and 14-hydropretellenin A to form the 2- pyridone core, leading to pretenellin B and pyridovericin, respectively. The cytochrome P450 monooxygenase tenB is then required for the selective N-hydroxylation of the 2-pyridone nitrogen of yield tellinin and 15-hydroxytellenin (15-HT), respectively. The UDP- glucosyltransferase GT1 and the methyltransferase MT1, located outside the tenS gene cluster, contribute to the stepwise glycosylation and methylation of 15-HT to obtain the glycoside pyridovericin-N-O-(4-O- methyl-beta-D-glucopyranoside) (PMGP). Additional related compounds such as 1-O-methyl-15-HT, (8Z)-1-O-methyl-15-HT, and O-methyltenellin A are also produced but the enzymes involved in their biosynthesis have still to be determined.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential tr",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0016747,,,GO:0016747,GO:0016746,0.5145,,,0.5145,0.5138,3,0.5143,0.3056,no
TENS_BEAB2,J4KMC1,ProtT3,Eukaryota,4235,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of tenellin-type 2-pyridones, iron-chelating compounds involved in iron stress tolerance, competition with the natural competitor fungus Metarhizium robertsii and insect hosts infection. TenS catalyzes the assembly of the polyketide-amino acid backbone. Because tenS lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase tenC. Upon formation of the polyketide backbone on the thiotemplate, the triketide is transferred to the NRPS module and linked to tyrosine to produce the pyrrolidine-2-dione intermediates, including pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The pathway begins with the assembly of the polyketide-amino acid backbone by the hybrid PKS-NRPS tenS with the help of the enoyl reductase tenC. These enzymes catalyze the synthesis of the pyrrolidine-2-dione intermediates pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The cytochrome P450 monooxygenase tenA then catalyzes an oxidative ring expansion of pretenellin A and 14-hydropretellenin A to form the 2- pyridone core, leading to pretenellin B and pyridovericin, respectively. The cytochrome P450 monooxygenase tenB is then required for the selective N-hydroxylation of the 2-pyridone nitrogen of yield tellinin and 15-hydroxytellenin (15-HT), respectively. The UDP- glucosyltransferase GT1 and the methyltransferase MT1, located outside the tenS gene cluster, contribute to the stepwise glycosylation and methylation of 15-HT to obtain the glycoside pyridovericin-N-O-(4-O- methyl-beta-D-glucopyranoside) (PMGP). Additional related compounds such as 1-O-methyl-15-HT, (8Z)-1-O-methyl-15-HT, and O-methyltenellin A are also produced but the enzymes involved in their biosynthesis have still to be determined.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0016746,GO:0016746,,GO:0016746,GO:0016747,0.5138,0.5138,,0.5138,0.5145,4,0.514,0.3056,no
TENS_BEAB2,J4KMC1,ProtTale,Eukaryota,4235,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of tenellin-type 2-pyridones, iron-chelating compounds involved in iron stress tolerance, competition with the natural competitor fungus Metarhizium robertsii and insect hosts infection. TenS catalyzes the assembly of the polyketide-amino acid backbone. Because tenS lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase tenC. Upon formation of the polyketide backbone on the thiotemplate, the triketide is transferred to the NRPS module and linked to tyrosine to produce the pyrrolidine-2-dione intermediates, including pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The pathway begins with the assembly of the polyketide-amino acid backbone by the hybrid PKS-NRPS tenS with the help of the enoyl reductase tenC. These enzymes catalyze the synthesis of the pyrrolidine-2-dione intermediates pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The cytochrome P450 monooxygenase tenA then catalyzes an oxidative ring expansion of pretenellin A and 14-hydropretellenin A to form the 2- pyridone core, leading to pretenellin B and pyridovericin, respectively. The cytochrome P450 monooxygenase tenB is then required for the selective N-hydroxylation of the 2-pyridone nitrogen of yield tellinin and 15-hydroxytellenin (15-HT), respectively. The UDP- glucosyltransferase GT1 and the methyltransferase MT1, located outside the tenS gene cluster, contribute to the stepwise glycosylation and methylation of 15-HT to obtain the glycoside pyridovericin-N-O-(4-O- methyl-beta-D-glucopyranoside) (PMGP). Additional related compounds such as 1-O-methyl-15-HT, (8Z)-1-O-methyl-15-HT, and O-methyltenellin A are also produced but the enzymes involved in their biosynthesis have still to be determined.","Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS). SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms. These initial steps feature the priming of an unusual benzoic acid",Maybe,Yes,Maybe,Yes,Maybe,not-Yes,GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0016491,GO:0016757,,,GO:0016746; GO:0016874,0.5799,0.4439,,,0.6759,3,0.5666,0.3056,no
TENS_BEAB2,J4KMC1,Protein2Text,Eukaryota,4235,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of tenellin-type 2-pyridones, iron-chelating compounds involved in iron stress tolerance, competition with the natural competitor fungus Metarhizium robertsii and insect hosts infection. TenS catalyzes the assembly of the polyketide-amino acid backbone. Because tenS lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase tenC. Upon formation of the polyketide backbone on the thiotemplate, the triketide is transferred to the NRPS module and linked to tyrosine to produce the pyrrolidine-2-dione intermediates, including pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The pathway begins with the assembly of the polyketide-amino acid backbone by the hybrid PKS-NRPS tenS with the help of the enoyl reductase tenC. These enzymes catalyze the synthesis of the pyrrolidine-2-dione intermediates pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The cytochrome P450 monooxygenase tenA then catalyzes an oxidative ring expansion of pretenellin A and 14-hydropretellenin A to form the 2- pyridone core, leading to pretenellin B and pyridovericin, respectively. The cytochrome P450 monooxygenase tenB is then required for the selective N-hydroxylation of the 2-pyridone nitrogen of yield tellinin and 15-hydroxytellenin (15-HT), respectively. The UDP- glucosyltransferase GT1 and the methyltransferase MT1, located outside the tenS gene cluster, contribute to the stepwise glycosylation and methylation of 15-HT to obtain the glycoside pyridovericin-N-O-(4-O- methyl-beta-D-glucopyranoside) (PMGP). Additional related compounds such as 1-O-methyl-15-HT, (8Z)-1-O-methyl-15-HT, and O-methyltenellin A are also produced but the enzymes involved in their biosynthesis have still to be determined.",The molecular function of this protein is an ATP synthase activity.,No,No,No,No,No,not-Yes,GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0046933,GO:0046933,GO:0046933,GO:0046933,GO:0046933,0.2555,0.2555,0.2555,0.2555,0.2555,5,0.2555,0.3056,no
TENS_BEAB2,J4KMC1,Reference,Eukaryota,4235,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of tenellin-type 2-pyridones, iron-chelating compounds involved in iron stress tolerance, competition with the natural competitor fungus Metarhizium robertsii and insect hosts infection. TenS catalyzes the assembly of the polyketide-amino acid backbone. Because tenS lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase tenC. Upon formation of the polyketide backbone on the thiotemplate, the triketide is transferred to the NRPS module and linked to tyrosine to produce the pyrrolidine-2-dione intermediates, including pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The pathway begins with the assembly of the polyketide-amino acid backbone by the hybrid PKS-NRPS tenS with the help of the enoyl reductase tenC. These enzymes catalyze the synthesis of the pyrrolidine-2-dione intermediates pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The cytochrome P450 monooxygenase tenA then catalyzes an oxidative ring expansion of pretenellin A and 14-hydropretellenin A to form the 2- pyridone core, leading to pretenellin B and pyridovericin, respectively. The cytochrome P450 monooxygenase tenB is then required for the selective N-hydroxylation of the 2-pyridone nitrogen of yield tellinin and 15-hydroxytellenin (15-HT), respectively. The UDP- glucosyltransferase GT1 and the methyltransferase MT1, located outside the tenS gene cluster, contribute to the stepwise glycosylation and methylation of 15-HT to obtain the glycoside pyridovericin-N-O-(4-O- methyl-beta-D-glucopyranoside) (PMGP). Additional related compounds such as 1-O-methyl-15-HT, (8Z)-1-O-methyl-15-HT, and O-methyltenellin A are also produced but the enzymes involved in their biosynthesis have still to be determined.","Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of tenellin-type 2-pyridones, iron-chelating compounds involved in iron stress tolerance, competition with the natural competitor fungus Metarhizium robertsii and insect hosts infection. TenS catalyzes the assembly of the polyketide-amino acid backbone. Because tenS lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase tenC. Upon formation of the polyketide backbone on the thiotemplate, the triketide is transferred to the NRPS module and linked to tyrosine to produce the pyrrolidine-2-dione intermediates, including pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The pathway begins with the assembly of the polyketide-amino acid backbone by the hybrid PKS-NRPS tenS with the help of the enoyl reductase tenC. These enzymes catalyze the synthesis of the pyrrolidine-2-dione intermediates pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13-hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The cytochrome P450 monooxygenase tenA then catalyzes an oxidative ring expansion of pretenellin A and 14-hydropretellenin A to form the 2- pyridone core, leading to pretenellin B and pyridovericin, respectively. The cytochrome P450 monooxygenase tenB is then required for the selective N-hydroxylation of the 2-pyridone nitrogen of yield tellinin and 15-hydroxytellenin (15-HT), respectively. The UDP- glucosyltransferase GT1 and the methyltransferase MT1, located outside the tenS gene cluster, contribute to the stepwise glycosylation and methylation of 15-HT to obtain the glycoside pyridovericin-N-O-(4-O- methyl-beta-D-glucopyranoside) (PMGP). Additional related compounds such as 1-O-methyl-15-HT, (8Z)-1-O-methyl-15-HT, and O-methyltenellin A are also produced but the enzymes involved in their biosynthesis have still to be determined.",,,,,,,GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0016746; GO:0016874,GO:0016874; GO:0016746,GO:0016874; GO:0016747,GO:0016874,GO:0016874,0.6759,0.6759,0.6997,0.5799,0.5799,5,0.6423,0.3056,no
SIDC_BEAB2,J4KNP2,ESM2Text,Eukaryota,4814,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. SIDC catalyzes the assembly of ferricrocin whereas SIDD catalyzes the assembly of fusarinine C.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcs",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,,,,,,,,,,,0,,0.3604,no
SIDC_BEAB2,J4KNP2,Prot2Text,Eukaryota,4814,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. SIDC catalyzes the assembly of ferricrocin whereas SIDD catalyzes the assembly of fusarinine C.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcs",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,GO:0016874,,,GO:0016874,GO:0016874; GO:0005524,0.709,,,0.709,0.6793,3,0.6991,0.3604,no
SIDC_BEAB2,J4KNP2,ProtT3,Eukaryota,4814,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. SIDC catalyzes the assembly of ferricrocin whereas SIDD catalyzes the assembly of fusarinine C.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,GO:0016874; GO:0005524,GO:0016405,GO:0003996,GO:0016874,GO:0016874,0.6793,0.4906,0.3163,0.709,0.709,5,0.5808,0.3604,no
SIDC_BEAB2,J4KNP2,ProtTale,Eukaryota,4814,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. SIDC catalyzes the assembly of ferricrocin whereas SIDD catalyzes the assembly of fusarinine C.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS). SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms. These initial steps feature the priming of an unusual benzoic acid starter unit onto",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,GO:0016491,GO:0016874,,,GO:0016874,0.4358,0.709,,,0.709,3,0.6179,0.3604,no
SIDC_BEAB2,J4KNP2,Protein2Text,Eukaryota,4814,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. SIDC catalyzes the assembly of ferricrocin whereas SIDD catalyzes the assembly of fusarinine C.","The molecular function of this protein is involved in the glycosylation process, specifically in the synthesis of glycoproteins. It is a part of the oligosaccharyl transferase complex, which is responsible for the transfer of a glycosyl group from a donor molecule to a specific asparagine residue in a nascent protein. This process is crucial for the proper folding, stability, and function of glycoproteins.",No,No,No,No,No,not-Yes,GO:0016874; GO:0031177,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.2639,0.2639,0.2639,0.2639,0.2639,5,0.2639,0.3604,no
SIDC_BEAB2,J4KNP2,Reference,Eukaryota,4814,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. SIDC catalyzes the assembly of ferricrocin whereas SIDD catalyzes the assembly of fusarinine C.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. SIDC catalyzes the assembly of ferricrocin whereas SIDD catalyzes the assembly of fusarinine C.",,,,,,,GO:0016874; GO:0031177,GO:0016874,GO:0016874,GO:0016879,GO:0016874,GO:0016874,0.709,0.709,0.5786,0.709,0.709,5,0.6829,0.3604,no
SIDD_BEAB2,J4UJF5,ESM2Text,Eukaryota,1843,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. SIDC catalyzes the assembly of ferricrocin whereas SIDD catalyzes the assembly of fusarinine C.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of aspirochlorine (or antibiotic A30641), an unusual halogenated spiro compound with distinctive antifungal properties due to selective inhibition of protein biosynthesis, and which is also active against bacteria, viruses, and murine tumor cells. The non-ribosomal peptide synthetase (NRPS) aclP is responsible the formation of the diketopiperazine (DKP) core from the condensation of 2 phenylalanine residues. One Phe residue is tailored into chlorotyrosine by hydroxylation and chlorination, whereas the second Phe undergoes an unprecedented C-C bond cleavage to be converted into glycine. After formation of the DKP, sulfur is incorporated into the DKP by conjugation with glutathione by aclG, followed by its stepwise degradation to the thiol by aclI, aclJ and aclK, and the dithiol oxidation by aclT. In addition, oxygenases (aclB, aclC, aclL and aclO) and O-methyltransferases (aclM and",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,,,,,,,,,,,0,,0.2365,no
SIDD_BEAB2,J4UJF5,Prot2Text,Eukaryota,1843,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. SIDC catalyzes the assembly of ferricrocin whereas SIDD catalyzes the assembly of fusarinine C.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,GO:0016874,,,GO:0016874,GO:0016874; GO:0005524,0.709,,,0.709,0.6793,3,0.6991,0.2365,no
SIDD_BEAB2,J4UJF5,ProtT3,Eukaryota,1843,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. SIDC catalyzes the assembly of ferricrocin whereas SIDD catalyzes the assembly of fusarinine C.",Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranyl,No,No,No,No,Maybe,not-Yes,GO:0016874; GO:0031177,GO:0016874; GO:0005524,GO:0016405,GO:0003996,GO:0016874,GO:0016874,0.6793,0.4906,0.3163,0.709,0.709,5,0.5808,0.2365,no
SIDD_BEAB2,J4UJF5,ProtTale,Eukaryota,1843,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. SIDC catalyzes the assembly of ferricrocin whereas SIDD catalyzes the assembly of fusarinine C.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties. L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism. The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,GO:0016491,GO:0016874,,,GO:0016874,0.4358,0.709,,,0.709,3,0.6179,0.2365,no
SIDD_BEAB2,J4UJF5,Protein2Text,Eukaryota,1843,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. SIDC catalyzes the assembly of ferricrocin whereas SIDD catalyzes the assembly of fusarinine C.","This protein is involved in the synthesis of a fatty acid. More specifically, it is a fatty acid synthase, which is an enzyme that catalyzes the formation of fatty acids from acetyl-CoA and malonyl-CoA through a series of condensation, reduction, and dehydration reactions.",No,No,No,No,No,not-Yes,GO:0016874; GO:0031177,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.2639,0.2639,0.2639,0.2639,0.2639,5,0.2639,0.2365,no
SIDD_BEAB2,J4UJF5,Reference,Eukaryota,1843,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. SIDC catalyzes the assembly of ferricrocin whereas SIDD catalyzes the assembly of fusarinine C.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. SIDC catalyzes the assembly of ferricrocin whereas SIDD catalyzes the assembly of fusarinine C.",,,,,,,GO:0016874; GO:0031177,GO:0016874,GO:0016874,GO:0016879,GO:0016874,GO:0016874,0.709,0.709,0.5786,0.709,0.709,5,0.6829,0.2365,no
NRPSA_BEAB2,J5J335,ESM2Text,Eukaryota,4016,"Hybrid PKS-NRPS synthetase that is involved in the regulation of the growth rate, germination rate, and spore production. Also, plays a role in the virulence of Beauveria bassiana against Ostrinia furnacalis larvae as well as in its antagonistic effects against the plant pathogenic fungus Botrytis cinerea. The secondary metabolite produced by BBA_09856 and its associated gene cluster remains to be identified.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcsC",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,,,,,,,,,,,0,,0.3162,no
NRPSA_BEAB2,J5J335,Prot2Text,Eukaryota,4016,"Hybrid PKS-NRPS synthetase that is involved in the regulation of the growth rate, germination rate, and spore production. Also, plays a role in the virulence of Beauveria bassiana against Ostrinia furnacalis larvae as well as in its antagonistic effects against the plant pathogenic fungus Botrytis cinerea. The secondary metabolite produced by BBA_09856 and its associated gene cluster remains to be identified.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcsC",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0016747,,,GO:0016747,GO:0016746,0.5636,,,0.5636,0.5445,3,0.5572,0.3162,no
NRPSA_BEAB2,J5J335,ProtT3,Eukaryota,4016,"Hybrid PKS-NRPS synthetase that is involved in the regulation of the growth rate, germination rate, and spore production. Also, plays a role in the virulence of Beauveria bassiana against Ostrinia furnacalis larvae as well as in its antagonistic effects against the plant pathogenic fungus Botrytis cinerea. The secondary metabolite produced by BBA_09856 and its associated gene cluster remains to be identified.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS) . SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0016746,GO:0016746,,GO:0016746,GO:0016747,0.5445,0.5445,,0.5445,0.5636,4,0.5493,0.3162,no
NRPSA_BEAB2,J5J335,ProtTale,Eukaryota,4016,"Hybrid PKS-NRPS synthetase that is involved in the regulation of the growth rate, germination rate, and spore production. Also, plays a role in the virulence of Beauveria bassiana against Ostrinia furnacalis larvae as well as in its antagonistic effects against the plant pathogenic fungus Botrytis cinerea. The secondary metabolite produced by BBA_09856 and its associated gene cluster remains to be identified.","Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the",Maybe,Yes,Yes,Yes,Maybe,Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0016491,GO:0016757,,,GO:0016746; GO:0016874,0.5478,0.4493,,,0.6826,3,0.5599,0.3162,no
NRPSA_BEAB2,J5J335,Protein2Text,Eukaryota,4016,"Hybrid PKS-NRPS synthetase that is involved in the regulation of the growth rate, germination rate, and spore production. Also, plays a role in the virulence of Beauveria bassiana against Ostrinia furnacalis larvae as well as in its antagonistic effects against the plant pathogenic fungus Botrytis cinerea. The secondary metabolite produced by BBA_09856 and its associated gene cluster remains to be identified.","This protein is involved in the molecular function of catalyzing the synthesis of fatty acid from acetyl-CoA and malonyl-CoA, which is a key step in the production of fatty acids. It is a type of fatty acid synthase.",No,No,Maybe,Maybe,No,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.5599,0.5599,0.5599,0.5599,0.5599,5,0.5599,0.3162,no
NRPSA_BEAB2,J5J335,Reference,Eukaryota,4016,"Hybrid PKS-NRPS synthetase that is involved in the regulation of the growth rate, germination rate, and spore production. Also, plays a role in the virulence of Beauveria bassiana against Ostrinia furnacalis larvae as well as in its antagonistic effects against the plant pathogenic fungus Botrytis cinerea. The secondary metabolite produced by BBA_09856 and its associated gene cluster remains to be identified.","Hybrid PKS-NRPS synthetase that is involved in the regulation of the growth rate, germination rate, and spore production. Also, plays a role in the virulence of Beauveria bassiana against Ostrinia furnacalis larvae as well as in its antagonistic effects against the plant pathogenic fungus Botrytis cinerea. The secondary metabolite produced by BBA_09856 and its associated gene cluster remains to be identified.",,,,,,,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0016746; GO:0016874,GO:0016874; GO:0016746,GO:0016874; GO:0016747,GO:0016874,GO:0016874,0.6826,0.6826,0.7195,0.5478,0.5478,5,0.6361,0.3162,no
RAD18_BEAB2,J5JS29,ESM2Text,Eukaryota,424,"E3 RING-finger protein, that associates to the E2 ubiquitin conjugating enzyme RAD6 to form the RAD6-RAD18 ubiquitin ligase complex involved in asexual and insect-pathogenic lifecycles, solar UV damage repair, and genomic expression. Plays an important role in photoreactivation of UVB-impaired conidia via the strong interactions of RAD6 and the circadian oscillator component WC2.","E3 RING-finger protein, member of the UBC2/RAD6 epistasis group. Associates to the E2 ubiquitin conjugating enzyme UBC2/RAD6 to form the UBC2-RAD18 ubiquitin ligase complex involved in postreplicative repair (PRR) of damaged DNA.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0003697; GO:0061630; GO:0008270,GO:0061630,GO:0004842,GO:0061630,GO:0061630,GO:0061630,0.5338,0.4573,0.5338,0.5338,0.5338,5,0.5185,0.5122,no
RAD18_BEAB2,J5JS29,Prot2Text,Eukaryota,424,"E3 RING-finger protein, that associates to the E2 ubiquitin conjugating enzyme RAD6 to form the RAD6-RAD18 ubiquitin ligase complex involved in asexual and insect-pathogenic lifecycles, solar UV damage repair, and genomic expression. Plays an important role in photoreactivation of UVB-impaired conidia via the strong interactions of RAD6 and the circadian oscillator component WC2.","E3 RING-finger protein, member of the UBC2/RAD6 epistasis group. Associates to the E2 ubiquitin conjugating enzyme mus-8/ubc2 to form the mus-8/ubc2-uvs-2/rad18 ubiquitin ligase complex involved in postreplicative repair (PRR) of damaged DNA.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0003697; GO:0061630; GO:0008270,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.5338,0.5338,0.5338,0.5338,0.5338,5,0.5338,0.5122,no
RAD18_BEAB2,J5JS29,ProtT3,Eukaryota,424,"E3 RING-finger protein, that associates to the E2 ubiquitin conjugating enzyme RAD6 to form the RAD6-RAD18 ubiquitin ligase complex involved in asexual and insect-pathogenic lifecycles, solar UV damage repair, and genomic expression. Plays an important role in photoreactivation of UVB-impaired conidia via the strong interactions of RAD6 and the circadian oscillator component WC2.",E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-63' of histone H2A (H2AK63ub1). H2AK63ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formation. It thereby plays a central role in histone code and gene regulation. Nucleus. Belongs to the RING-type zinc finger family. RNF26 subfamily,Maybe,Maybe,Yes,Maybe,No,not-Yes,GO:0003697; GO:0061630; GO:0008270,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.5338,0.5338,0.5338,0.5338,0.5338,5,0.5338,0.5122,no
RAD18_BEAB2,J5JS29,ProtTale,Eukaryota,424,"E3 RING-finger protein, that associates to the E2 ubiquitin conjugating enzyme RAD6 to form the RAD6-RAD18 ubiquitin ligase complex involved in asexual and insect-pathogenic lifecycles, solar UV damage repair, and genomic expression. Plays an important role in photoreactivation of UVB-impaired conidia via the strong interactions of RAD6 and the circadian oscillator component WC2.","E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-120' of histone H2B, thereby playing a key role in histone code and gene regulation.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0003697; GO:0061630; GO:0008270,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.5338,0.5338,0.5338,0.5338,0.5338,5,0.5338,0.5122,no
RAD18_BEAB2,J5JS29,Protein2Text,Eukaryota,424,"E3 RING-finger protein, that associates to the E2 ubiquitin conjugating enzyme RAD6 to form the RAD6-RAD18 ubiquitin ligase complex involved in asexual and insect-pathogenic lifecycles, solar UV damage repair, and genomic expression. Plays an important role in photoreactivation of UVB-impaired conidia via the strong interactions of RAD6 and the circadian oscillator component WC2.","The molecular function of this protein is unknown, but it is a type of E3 ubiquitin-protein ligase, which suggests that it is involved in the transfer of ubiquitin molecules to other proteins, leading to their degradation or regulation. However, more specific information about its function is not provided.",Maybe,Yes,Yes,Yes,Maybe,Yes,GO:0003697; GO:0061630; GO:0008270,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.5338,0.5338,0.5338,0.5338,0.5338,5,0.5338,0.5122,no
RAD18_BEAB2,J5JS29,Reference,Eukaryota,424,"E3 RING-finger protein, that associates to the E2 ubiquitin conjugating enzyme RAD6 to form the RAD6-RAD18 ubiquitin ligase complex involved in asexual and insect-pathogenic lifecycles, solar UV damage repair, and genomic expression. Plays an important role in photoreactivation of UVB-impaired conidia via the strong interactions of RAD6 and the circadian oscillator component WC2.","E3 RING-finger protein, that associates to the E2 ubiquitin conjugating enzyme RAD6 to form the RAD6-RAD18 ubiquitin ligase complex involved in asexual and insect-pathogenic lifecycles, solar UV damage repair, and genomic expression. Plays an important role in photoreactivation of UVB-impaired conidia via the strong interactions of RAD6 and the circadian oscillator component WC2.",,,,,,,GO:0003697; GO:0061630; GO:0008270,GO:0004842,GO:0061630,GO:0061630,GO:0004842,GO:0061630,0.4573,0.5338,0.5338,0.4573,0.5338,5,0.5032,0.5122,no
MGH_RUBRA,J9PY59,ESM2Text,Bacteria,442,"Hydrolase that catalyzes the hydrolysis of mannosylglycerate (MG), a solute produced in response to osmotic stress in thermophiles, into mannose and glycerate. Can also hydrolyze glucosylglycerate (GG) to glucose and glycerate, with similar catalytic efficiency. Is highly specific for MG and GG, and cannot use mannosylglyceramide (MGA), glucosylglycerol, mannosylglucosylglycerate (MGG), glucosylglucosylglycerate (GGG) or trehalose as substrates.","Alpha-mannosidase activity is specific for alpha-1,2-mannose. The hydrolytic activity of theManA beta-mannoside is higher than that of theManB beta-mannoside and is dependent on the presence of mannobiose. Can also hydrolyze maltose.",No,No,No,No,No,not-Yes,GO:0004573; GO:0102546,GO:0016787,GO:0016787,,GO:0004553,,0.5649,0.5649,,0.5833,,3,0.571,0.2075,no
MGH_RUBRA,J9PY59,Prot2Text,Bacteria,442,"Hydrolase that catalyzes the hydrolysis of mannosylglycerate (MG), a solute produced in response to osmotic stress in thermophiles, into mannose and glycerate. Can also hydrolyze glucosylglycerate (GG) to glucose and glycerate, with similar catalytic efficiency. Is highly specific for MG and GG, and cannot use mannosylglyceramide (MGA), glucosylglycerol, mannosylglucosylglycerate (MGG), glucosylglucosylglycerate (GGG) or trehalose as substrates.","Is involved in the catabolism of branched amino acids such as leucine, isoleucine, and valine.",No,No,No,No,No,not-Yes,GO:0004573; GO:0102546,GO:0004553,GO:0004553,GO:0004553,GO:0004553,GO:0004553,0.5833,0.5833,0.5833,0.5833,0.5833,5,0.5833,0.2075,no
MGH_RUBRA,J9PY59,ProtT3,Bacteria,442,"Hydrolase that catalyzes the hydrolysis of mannosylglycerate (MG), a solute produced in response to osmotic stress in thermophiles, into mannose and glycerate. Can also hydrolyze glucosylglycerate (GG) to glucose and glycerate, with similar catalytic efficiency. Is highly specific for MG and GG, and cannot use mannosylglyceramide (MGA), glucosylglycerol, mannosylglucosylglycerate (MGG), glucosylglucosylglycerate (GGG) or trehalose as substrates.",Catalyzes the hydrolysis of alpha-D-glucosyl-alpha-D-glucose 6-phosphate to alpha-D-glucose 6-phosphate and alpha-D-glucose. Belongs to the glycosyl hydrolase 32 family,No,No,No,No,No,not-Yes,GO:0004573; GO:0102546,GO:0004564,GO:0004564,GO:0004564,GO:0004553,GO:0004564,0.4874,0.4874,0.4874,0.5833,0.4874,5,0.5066,0.2075,no
MGH_RUBRA,J9PY59,ProtTale,Bacteria,442,"Hydrolase that catalyzes the hydrolysis of mannosylglycerate (MG), a solute produced in response to osmotic stress in thermophiles, into mannose and glycerate. Can also hydrolyze glucosylglycerate (GG) to glucose and glycerate, with similar catalytic efficiency. Is highly specific for MG and GG, and cannot use mannosylglyceramide (MGA), glucosylglycerol, mannosylglucosylglycerate (MGG), glucosylglucosylglycerate (GGG) or trehalose as substrates.","Catalyzes the hydrolysis of the N-acetamido group of the N-acetamido group of GlcNAc-Asn, generating GlcNAc-Asn and acetate. Can also hydrolyze the N-acetamido group of GalNAc-Asn, but with lower efficiency.",No,No,No,No,No,not-Yes,GO:0004573; GO:0102546,GO:0016787,GO:0016787,GO:0016811,GO:0016811,GO:0016787,0.5649,0.5649,0.3704,0.3704,0.5649,5,0.4871,0.2075,no
MGH_RUBRA,J9PY59,Protein2Text,Bacteria,442,"Hydrolase that catalyzes the hydrolysis of mannosylglycerate (MG), a solute produced in response to osmotic stress in thermophiles, into mannose and glycerate. Can also hydrolyze glucosylglycerate (GG) to glucose and glycerate, with similar catalytic efficiency. Is highly specific for MG and GG, and cannot use mannosylglyceramide (MGA), glucosylglycerol, mannosylglucosylglycerate (MGG), glucosylglucosylglycerate (GGG) or trehalose as substrates.",The molecular function of the protein is an alpha-glucosidase.,No,No,No,No,No,not-Yes,GO:0004573; GO:0102546,,,,,,,,,,,0,,0.2075,no
MGH_RUBRA,J9PY59,Reference,Bacteria,442,"Hydrolase that catalyzes the hydrolysis of mannosylglycerate (MG), a solute produced in response to osmotic stress in thermophiles, into mannose and glycerate. Can also hydrolyze glucosylglycerate (GG) to glucose and glycerate, with similar catalytic efficiency. Is highly specific for MG and GG, and cannot use mannosylglyceramide (MGA), glucosylglycerol, mannosylglucosylglycerate (MGG), glucosylglucosylglycerate (GGG) or trehalose as substrates.","Hydrolase that catalyzes the hydrolysis of mannosylglycerate (MG), a solute produced in response to osmotic stress in thermophiles, into mannose and glycerate. Can also hydrolyze glucosylglycerate (GG) to glucose and glycerate, with similar catalytic efficiency. Is highly specific for MG and GG, and cannot use mannosylglyceramide (MGA), glucosylglycerol, mannosylglucosylglycerate (MGG), glucosylglucosylglycerate (GGG) or trehalose as substrates.",,,,,,,GO:0004573; GO:0102546,GO:0016798,GO:0004553,GO:0004553,GO:0004553,GO:0004553,0.5507,0.5833,0.5833,0.5833,0.5833,5,0.5768,0.2075,no
LP9_CRYN9,J9VH79,ESM2Text,Eukaryota,375,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes polysaccharides via the oxidation of scissile alpha- or beta-(1-4)- glycosidic bonds, yielding C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate. Required for the expression of stress response phenotypes, including thermotolerance, cell wall integrity, and efficient cell cycle progression. Promotes intrinsic fungal cell wall remodeling events required for efficient adaptation to the host environment. Required for virulence in a murine inhalational model of cryptococcal infection as well as in Galleria mellonella larvae.",Involved in degradation of plant cell walls. May participate in the degradation of phenyloxidized conidia.,Vague,Vague,Vague,Vague,No,not-Yes,GO:0046872; GO:0004497,,,,,,,,,,,0,,0.3007,no
LP9_CRYN9,J9VH79,Prot2Text,Eukaryota,375,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes polysaccharides via the oxidation of scissile alpha- or beta-(1-4)- glycosidic bonds, yielding C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate. Required for the expression of stress response phenotypes, including thermotolerance, cell wall integrity, and efficient cell cycle progression. Promotes intrinsic fungal cell wall remodeling events required for efficient adaptation to the host environment. Required for virulence in a murine inhalational model of cryptococcal infection as well as in Galleria mellonella larvae.","Is thought to be an important factor in the utilization of plant biomass via the production of hydroxyurea (hydroxy nitrate or HNO), an important precursor for the biosynthesis of other nitrogen-containing amino acids.",No,No,Vague,Vague,No,not-Yes,GO:0046872; GO:0004497,,,,,,,,,,,0,,0.3007,no
LP9_CRYN9,J9VH79,ProtT3,Eukaryota,375,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes polysaccharides via the oxidation of scissile alpha- or beta-(1-4)- glycosidic bonds, yielding C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate. Required for the expression of stress response phenotypes, including thermotolerance, cell wall integrity, and efficient cell cycle progression. Promotes intrinsic fungal cell wall remodeling events required for efficient adaptation to the host environment. Required for virulence in a murine inhalational model of cryptococcal infection as well as in Galleria mellonella larvae.","Laccase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties",No,No,No,No,No,not-Yes,GO:0046872; GO:0004497,GO:0008471,GO:0008471,GO:0008471; GO:0005507,GO:0008471; GO:0005507,GO:0008471,0.0,0.0,0.5476,0.5476,0.0,5,0.219,0.3007,no
LP9_CRYN9,J9VH79,ProtTale,Eukaryota,375,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes polysaccharides via the oxidation of scissile alpha- or beta-(1-4)- glycosidic bonds, yielding C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate. Required for the expression of stress response phenotypes, including thermotolerance, cell wall integrity, and efficient cell cycle progression. Promotes intrinsic fungal cell wall remodeling events required for efficient adaptation to the host environment. Required for virulence in a murine inhalational model of cryptococcal infection as well as in Galleria mellonella larvae.","Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0004497,GO:0016491; GO:0005507,GO:0016491; GO:0005507,GO:0016491; GO:0005507,GO:0016491,GO:0016491,0.7926,0.7926,0.7926,0.5957,0.5957,5,0.7138,0.3007,no
LP9_CRYN9,J9VH79,Protein2Text,Eukaryota,375,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes polysaccharides via the oxidation of scissile alpha- or beta-(1-4)- glycosidic bonds, yielding C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate. Required for the expression of stress response phenotypes, including thermotolerance, cell wall integrity, and efficient cell cycle progression. Promotes intrinsic fungal cell wall remodeling events required for efficient adaptation to the host environment. Required for virulence in a murine inhalational model of cryptococcal infection as well as in Galleria mellonella larvae.","This protein is involved in the degradation of cellulose, a process that is essential for the breakdown and utilization of plant biomass. Its molecular function is likely to be involved in the hydrolysis of cellulose, possibly by catalyzing the cleavage of beta-1,4-glycosidic bonds between glucose residues in the cellulose polymer. This is a critical step in the degradation of cellulose, allowing the enzyme to break down the cellulose polymer into simpler sugars that can be utilized by the cell. 

In more detail, the molecular function of this protein is likely to be a lyase, which is an enzyme that catalyzes the cleavage of a chemical bond, in this case, the beta-1,4-glycosidic bond between glucose residues in cellulose. The specific function of this protein is to catalyze the cleavage of cellulose into cello-oligosaccharides, which can then be further degraded by other enzymes to produce simple sugars such as glucose. 

Overall, the molecular function of this protein is an important step in the degradation of cellulose, allowing the cell to break down and utilize plant biomass as a source of energy. 
Please note that this is a general description and the specific function of the protein might be more complex and nuanced. 
Additionally, this information is based on general knowledge and might not be specific to this particular protein. More detailed and specific information would require further research and analysis of the protein's structure and function.",Vague,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0046872; GO:0004497,GO:0008810,GO:0008810,GO:0008810,GO:0008810,GO:0008810,0.2193,0.2193,0.2193,0.2193,0.2193,5,0.2193,0.3007,no
LP9_CRYN9,J9VH79,Reference,Eukaryota,375,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes polysaccharides via the oxidation of scissile alpha- or beta-(1-4)- glycosidic bonds, yielding C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate. Required for the expression of stress response phenotypes, including thermotolerance, cell wall integrity, and efficient cell cycle progression. Promotes intrinsic fungal cell wall remodeling events required for efficient adaptation to the host environment. Required for virulence in a murine inhalational model of cryptococcal infection as well as in Galleria mellonella larvae.","Lytic polysaccharide monooxygenase (LPMO) that depolymerizes polysaccharides via the oxidation of scissile alpha- or beta-(1-4)- glycosidic bonds, yielding C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate. Required for the expression of stress response phenotypes, including thermotolerance, cell wall integrity, and efficient cell cycle progression. Promotes intrinsic fungal cell wall remodeling events required for efficient adaptation to the host environment. Required for virulence in a murine inhalational model of cryptococcal infection as well as in Galleria mellonella larvae.",,,,,,,GO:0046872; GO:0004497,GO:0016491,GO:0016491; GO:0005507,GO:0016491; GO:0005507,GO:0016491,GO:0016491; GO:0005507,0.5957,0.7926,0.7926,0.5957,0.7926,5,0.7138,0.3007,no
MET2_CRYN9,J9VIY8,ESM2Text,Eukaryota,528,Commits homoserine to the methionine biosynthesis pathway by catalyzing its O-acetylation.,"L-ascorbate reductase; part of the gene cluster that mediates the biosynthesis of aspirochlorine (or antibiotic A30641), an unusual halogenated spiro compound with distinctive antifungal properties due to selective inhibition of protein biosynthesis, and which is also active against bacteria, viruses, and murine tumor cells. The non-ribosomal peptide synthetase (NRPS) aclP is responsible the formation of the diketopiperazine (DKP) core from the condensation of 2 phenylalanine residues. One Phe residue is tailored into chlorotyrosine by hydroxylation and chlorination, whereas the second Phe undergoes an unprecedented C-C bond cleavage to be converted into glycine. After formation of the DKP, sulfur is incorporated into the DKP by conjugation with glutathione by aclG, followed by its stepwise degradation to the thiol by aclI, aclJ and aclK, and the dithiol oxidation by aclT. In addition, oxygenases (aclB, aclC, aclL and aclO) and O-methyltransferases (aclM and a",No,No,No,No,No,not-Yes,GO:0004414,GO:0016491,GO:0016491,,GO:0016491,,0.264,0.264,,0.264,,3,0.264,0.1585,no
MET2_CRYN9,J9VIY8,Prot2Text,Eukaryota,528,Commits homoserine to the methionine biosynthesis pathway by catalyzing its O-acetylation.,"Homoserine O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of the tropolone class of fungal maleic anhydrides. The pathway begins with the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide synthase (PKS) tropA. 3-methylorcinaldehyde is the substrate for the FAD-dependent monooxygenase tropB to yield a dearomatized hydroxycyclohexadione. The 2-oxoglutarate-dependent dioxygenase tropC then performs the oxidative ring expansion to provide the first tropolone metabolite stipitaldehyde. Trop D converts stipitaldehyde into stipitacetal which is in turn converted to stipitalide by the short-chain dehydrogenase/reductase tropE. The next steps involve tropF, tropG, tropH, tropI and tropJ to form successive tropolone maleic anhydrides including stipitaldehydic, stipitatonic and stipitatic acids.",Yes,Yes,Yes,Yes,Maybe,Yes,GO:0004414,GO:0004415,GO:0004415,GO:0004412,GO:0004415,GO:0016746,0.1213,0.1213,0.1424,0.1213,0.5367,5,0.2086,0.1585,no
MET2_CRYN9,J9VIY8,ProtT3,Eukaryota,528,Commits homoserine to the methionine biosynthesis pathway by catalyzing its O-acetylation.,Belongs to the AB hydrolase superfamily. MetX family,Vague,Vague,Maybe,Vague,Vague,not-Yes,GO:0004414,GO:0016746,GO:0004414,GO:0016746,GO:0016787,GO:0016747,0.5367,1.0,0.5367,0.264,0.6227,5,0.592,0.1585,no
MET2_CRYN9,J9VIY8,ProtTale,Eukaryota,528,Commits homoserine to the methionine biosynthesis pathway by catalyzing its O-acetylation.,"N-acetyltransferase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties. L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism. The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by the",No,Maybe,No,No,No,not-Yes,GO:0004414,GO:0016746,GO:0016746,GO:0016407,GO:0016407,GO:0016407,0.5367,0.5367,0.7126,0.7126,0.7126,5,0.6422,0.1585,no
MET2_CRYN9,J9VIY8,Protein2Text,Eukaryota,528,Commits homoserine to the methionine biosynthesis pathway by catalyzing its O-acetylation.,"The molecular function of this protein is not explicitly stated in the provided text. However, based on the name ""Protein, O-methyltransferase"" and the fact that it is part of a category of proteins that are involved in the modification of other proteins, it is likely that this protein's molecular function is to transfer a methyl group from one molecule to another.",No,No,No,No,No,not-Yes,GO:0004414,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.2413,0.2413,0.2413,0.2413,0.2413,5,0.2413,0.1585,no
MET2_CRYN9,J9VIY8,Reference,Eukaryota,528,Commits homoserine to the methionine biosynthesis pathway by catalyzing its O-acetylation.,Commits homoserine to the methionine biosynthesis pathway by catalyzing its O-acetylation.,,,,,,,GO:0004414,GO:0004414,GO:0004414,GO:0004415,GO:0004414,GO:0004414,1.0,1.0,0.1213,1.0,1.0,5,0.8243,0.1585,no
YOR1_CRYN9,J9VQH1,ESM2Text,Eukaryota,1512,"Transmembrane transporter. May play a role in the packaging or formation of extracellular vesicles (EVs), and in the export of virulence factors from EVs. Required for efficient non-lytic exocytosis from host macrophages, the process by which the yeast escapes host macrophages with both host cell and pathogen remaining viable.","ABC transporter; part of the gene cluster that mediates the biosynthesis of the mycotoxin cyclochlorotine, a hepatotoxic and carcinogenic cyclic chlorinated pentapeptide. With the MFS transporter cctQ, is most likely responsible for cyclochlorotine secretion and thereby may contribute to intrinsic resistance.",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0140359; GO:0005524; GO:0016887,GO:0042626,GO:0016887,GO:0042626,,GO:0042626,0.5305,0.5717,0.5305,,0.5305,4,0.5408,0.6166,yes
YOR1_CRYN9,J9VQH1,Prot2Text,Eukaryota,1512,"Transmembrane transporter. May play a role in the packaging or formation of extracellular vesicles (EVs), and in the export of virulence factors from EVs. Required for efficient non-lytic exocytosis from host macrophages, the process by which the yeast escapes host macrophages with both host cell and pathogen remaining viable.","ABC transporter; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0140359; GO:0005524; GO:0016887,GO:0042626,GO:0016887,GO:0042626,GO:0016887,GO:0016887; GO:0005524,0.5305,0.5717,0.5305,0.5717,0.8452,5,0.6099,0.6166,yes
YOR1_CRYN9,J9VQH1,ProtT3,Eukaryota,1512,"Transmembrane transporter. May play a role in the packaging or formation of extracellular vesicles (EVs), and in the export of virulence factors from EVs. Required for efficient non-lytic exocytosis from host macrophages, the process by which the yeast escapes host macrophages with both host cell and pathogen remaining viable.",Membrane; Multi-pass membrane protein. Belongs to the major facilitator superfamily. ABCB family,Vague,Vague,Maybe,Vague,Vague,not-Yes,GO:0140359; GO:0005524; GO:0016887,,,,GO:0022857,,,,,0.3126,,1,0.3126,0.6166,yes
YOR1_CRYN9,J9VQH1,ProtTale,Eukaryota,1512,"Transmembrane transporter. May play a role in the packaging or formation of extracellular vesicles (EVs), and in the export of virulence factors from EVs. Required for efficient non-lytic exocytosis from host macrophages, the process by which the yeast escapes host macrophages with both host cell and pathogen remaining viable.","ABC-type transporter; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3- hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB)",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0140359; GO:0005524; GO:0016887,GO:0005524,GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.5312,0.8452,0.8452,0.8452,0.8452,5,0.7824,0.6166,yes
YOR1_CRYN9,J9VQH1,Protein2Text,Eukaryota,1512,"Transmembrane transporter. May play a role in the packaging or formation of extracellular vesicles (EVs), and in the export of virulence factors from EVs. Required for efficient non-lytic exocytosis from host macrophages, the process by which the yeast escapes host macrophages with both host cell and pathogen remaining viable.","The molecular function of this protein is to transport molecules. More specifically, it is involved in transporting molecules across cell membranes, and is classified as a transporter.",Maybe,Vague,Maybe,Vague,Maybe,not-Yes,GO:0140359; GO:0005524; GO:0016887,GO:0005215,GO:0005215,GO:0005215,GO:0005215,GO:0005215,0.2721,0.2721,0.2721,0.2721,0.2721,5,0.2721,0.6166,yes
YOR1_CRYN9,J9VQH1,Reference,Eukaryota,1512,"Transmembrane transporter. May play a role in the packaging or formation of extracellular vesicles (EVs), and in the export of virulence factors from EVs. Required for efficient non-lytic exocytosis from host macrophages, the process by which the yeast escapes host macrophages with both host cell and pathogen remaining viable.","Transmembrane transporter. May play a role in the packaging or formation of extracellular vesicles (EVs), and in the export of virulence factors from EVs. Required for efficient non-lytic exocytosis from host macrophages, the process by which the yeast escapes host macrophages with both host cell and pathogen remaining viable.",,,,,,,GO:0140359; GO:0005524; GO:0016887,GO:0022857,GO:0022857,GO:0022857,GO:0022857,GO:0022857,0.3126,0.3126,0.3126,0.3126,0.3126,5,0.3126,0.6166,yes
MAOM_CRYN9,J9VVW8,ESM2Text,Eukaryota,600,NAD-dependent mitochondrial malic enzyme that catalyzes the oxidative decarboxylation of malate to pyruvate.,Attenuates the photosynthetic acclimation by producing NADH that can subsequently be used for the biogenesis of photosystem II and III.,No,No,No,No,No,not-Yes,GO:0004471; GO:0046872; GO:0051287,,,,,,,,,,,0,,0.177,no
MAOM_CRYN9,J9VVW8,Prot2Text,Eukaryota,600,NAD-dependent mitochondrial malic enzyme that catalyzes the oxidative decarboxylation of malate to pyruvate.,"Catalyzes the oxidative decarboxylation of (S)-malate in the presence of NADP(+) and divalent metal ions, and decarboxylation of oxaloacetate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004471; GO:0046872; GO:0051287,GO:0004473,GO:0004473,GO:0004473,GO:0004473,GO:0004473,0.4361,0.4361,0.4361,0.4361,0.4361,5,0.4361,0.177,no
MAOM_CRYN9,J9VVW8,ProtT3,Eukaryota,600,NAD-dependent mitochondrial malic enzyme that catalyzes the oxidative decarboxylation of malate to pyruvate.,"Plastid, chloroplast. Belongs to the malic enzymes family",Vague,No,Vague,Vague,Vague,not-Yes,GO:0004471; GO:0046872; GO:0051287,GO:0004470,GO:0004470,GO:0004470,GO:0004470,GO:0004473,0.4377,0.4377,0.4377,0.4377,0.4361,5,0.4374,0.177,no
MAOM_CRYN9,J9VVW8,ProtTale,Eukaryota,600,NAD-dependent mitochondrial malic enzyme that catalyzes the oxidative decarboxylation of malate to pyruvate.,This enzyme catalyzes the reversible NADP-dependent decarboxylation of (S)-2- oxoglutarate to succinate and CO(2).,No,Vague,No,No,No,not-Yes,GO:0004471; GO:0046872; GO:0051287,GO:0016491; GO:0050661,GO:0016491; GO:0016831; GO:0050661,GO:0016831; GO:0050661,GO:0016491; GO:0016831,GO:0004450,0.5614,0.5004,0.4446,0.2909,0.301,5,0.4197,0.177,no
MAOM_CRYN9,J9VVW8,Protein2Text,Eukaryota,600,NAD-dependent mitochondrial malic enzyme that catalyzes the oxidative decarboxylation of malate to pyruvate.,"This protein is a part of the enzyme malate dehydrogenase, which catalyzes the reversible oxidation of malate to oxaloacetate, a key step in the tricarboxylic acid (TCA) cycle.",No,Maybe,Maybe,Maybe,No,not-Yes,GO:0004471; GO:0046872; GO:0051287,GO:0016615; GO:0030060,GO:0016615; GO:0030060,GO:0016615; GO:0030060,GO:0016615; GO:0030060,GO:0016615,0.4599,0.4599,0.4599,0.4599,0.3939,5,0.4467,0.177,no
MAOM_CRYN9,J9VVW8,Reference,Eukaryota,600,NAD-dependent mitochondrial malic enzyme that catalyzes the oxidative decarboxylation of malate to pyruvate.,NAD-dependent mitochondrial malic enzyme that catalyzes the oxidative decarboxylation of malate to pyruvate.,,,,,,,GO:0004471; GO:0046872; GO:0051287,GO:0004471; GO:0051287,GO:0004471; GO:0051287,GO:0004471,GO:0004471; GO:0051287,GO:0004471; GO:0051287,0.8517,0.8517,0.5336,0.8517,0.8517,5,0.7881,0.177,no
MPSA_MACPH,K2QYX5,ESM2Text,Eukaryota,4004,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of macrophasetins, 3-decalinoyltetramic acids (DTAs) which feature a tetramate (pyrrolidine-2,4-dione) unit connected to a decalin fragment and that have potent bioactivities. The PKS-NRPS mpsA together with its associated enoylreductase partner mpsG incorporate one unit of acetyl-CoA, seven units of malonyl-CoA, and one unit of L-alanine to assemble the linear tetramic acid intermediate corresponding to the backbone of macrophasetins. Without the Diels-Alderase mpsD, the mpsA/G product can undergo the non-enzymatic intramolecular Diels-Alder (IMDA) reaction to generate both macrophasetin A and macrophasetin B. Catalyzed by mpsD, the linear tetramic acid intermediate is thoroughly converted to macrophasetin A via the endo- IMDA reaction in a regioselective and stereoselective manner. Finally, the cytochrome P450 monooxygenase mpsF catalyzes the hydroxylation at C20 to yield the end product macrophasetin C.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The nonribosomal peptide synthetase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,,GO:0016747,GO:0016491; GO:0016740,GO:0016746,GO:0016746,,0.5636,0.6626,0.5445,0.5445,4,0.5788,0.2559,no
MPSA_MACPH,K2QYX5,Prot2Text,Eukaryota,4004,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of macrophasetins, 3-decalinoyltetramic acids (DTAs) which feature a tetramate (pyrrolidine-2,4-dione) unit connected to a decalin fragment and that have potent bioactivities. The PKS-NRPS mpsA together with its associated enoylreductase partner mpsG incorporate one unit of acetyl-CoA, seven units of malonyl-CoA, and one unit of L-alanine to assemble the linear tetramic acid intermediate corresponding to the backbone of macrophasetins. Without the Diels-Alderase mpsD, the mpsA/G product can undergo the non-enzymatic intramolecular Diels-Alder (IMDA) reaction to generate both macrophasetin A and macrophasetin B. Catalyzed by mpsD, the linear tetramic acid intermediate is thoroughly converted to macrophasetin A via the endo- IMDA reaction in a regioselective and stereoselective manner. Finally, the cytochrome P450 monooxygenase mpsF catalyzes the hydroxylation at C20 to yield the end product macrophasetin C.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The nonribosomal peptide synthetase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,,,GO:0016747,,GO:0016746,,,0.5636,,0.5445,2,0.554,0.2559,no
MPSA_MACPH,K2QYX5,ProtT3,Eukaryota,4004,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of macrophasetins, 3-decalinoyltetramic acids (DTAs) which feature a tetramate (pyrrolidine-2,4-dione) unit connected to a decalin fragment and that have potent bioactivities. The PKS-NRPS mpsA together with its associated enoylreductase partner mpsG incorporate one unit of acetyl-CoA, seven units of malonyl-CoA, and one unit of L-alanine to assemble the linear tetramic acid intermediate corresponding to the backbone of macrophasetins. Without the Diels-Alderase mpsD, the mpsA/G product can undergo the non-enzymatic intramolecular Diels-Alder (IMDA) reaction to generate both macrophasetin A and macrophasetin B. Catalyzed by mpsD, the linear tetramic acid intermediate is thoroughly converted to macrophasetin A via the endo- IMDA reaction in a regioselective and stereoselective manner. Finally, the cytochrome P450 monooxygenase mpsF catalyzes the hydroxylation at C20 to yield the end product macrophasetin C.","Polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0016747,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.5636,0.5445,0.5445,0.5445,0.5445,5,0.5483,0.2559,no
MPSA_MACPH,K2QYX5,ProtTale,Eukaryota,4004,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of macrophasetins, 3-decalinoyltetramic acids (DTAs) which feature a tetramate (pyrrolidine-2,4-dione) unit connected to a decalin fragment and that have potent bioactivities. The PKS-NRPS mpsA together with its associated enoylreductase partner mpsG incorporate one unit of acetyl-CoA, seven units of malonyl-CoA, and one unit of L-alanine to assemble the linear tetramic acid intermediate corresponding to the backbone of macrophasetins. Without the Diels-Alderase mpsD, the mpsA/G product can undergo the non-enzymatic intramolecular Diels-Alder (IMDA) reaction to generate both macrophasetin A and macrophasetin B. Catalyzed by mpsD, the linear tetramic acid intermediate is thoroughly converted to macrophasetin A via the endo- IMDA reaction in a regioselective and stereoselective manner. Finally, the cytochrome P450 monooxygenase mpsF catalyzes the hydroxylation at C20 to yield the end product macrophasetin C.","Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the",Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0016747,GO:0016747; GO:0016874,GO:0031177; GO:0016874; GO:0016746,GO:0016746,,0.5636,0.7195,0.8148,0.5445,,4,0.6606,0.2559,no
MPSA_MACPH,K2QYX5,Protein2Text,Eukaryota,4004,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of macrophasetins, 3-decalinoyltetramic acids (DTAs) which feature a tetramate (pyrrolidine-2,4-dione) unit connected to a decalin fragment and that have potent bioactivities. The PKS-NRPS mpsA together with its associated enoylreductase partner mpsG incorporate one unit of acetyl-CoA, seven units of malonyl-CoA, and one unit of L-alanine to assemble the linear tetramic acid intermediate corresponding to the backbone of macrophasetins. Without the Diels-Alderase mpsD, the mpsA/G product can undergo the non-enzymatic intramolecular Diels-Alder (IMDA) reaction to generate both macrophasetin A and macrophasetin B. Catalyzed by mpsD, the linear tetramic acid intermediate is thoroughly converted to macrophasetin A via the endo- IMDA reaction in a regioselective and stereoselective manner. Finally, the cytochrome P450 monooxygenase mpsF catalyzes the hydroxylation at C20 to yield the end product macrophasetin C.","The molecular function of the protein is not specified in the provided information. However, based on its name, it is likely that the protein is involved in the transport of molecules across cell membranes, possibly as a component of a transport system. More specific information would be needed to determine its exact molecular function.",Vague,No,Vague,No,No,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,,,,,,,,,,,0,,0.2559,no
MPSA_MACPH,K2QYX5,Reference,Eukaryota,4004,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of macrophasetins, 3-decalinoyltetramic acids (DTAs) which feature a tetramate (pyrrolidine-2,4-dione) unit connected to a decalin fragment and that have potent bioactivities. The PKS-NRPS mpsA together with its associated enoylreductase partner mpsG incorporate one unit of acetyl-CoA, seven units of malonyl-CoA, and one unit of L-alanine to assemble the linear tetramic acid intermediate corresponding to the backbone of macrophasetins. Without the Diels-Alderase mpsD, the mpsA/G product can undergo the non-enzymatic intramolecular Diels-Alder (IMDA) reaction to generate both macrophasetin A and macrophasetin B. Catalyzed by mpsD, the linear tetramic acid intermediate is thoroughly converted to macrophasetin A via the endo- IMDA reaction in a regioselective and stereoselective manner. Finally, the cytochrome P450 monooxygenase mpsF catalyzes the hydroxylation at C20 to yield the end product macrophasetin C.","Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of macrophasetins, 3-decalinoyltetramic acids (DTAs) which feature a tetramate (pyrrolidine-2,4-dione) unit connected to a decalin fragment and that have potent bioactivities. The PKS-NRPS mpsA together with its associated enoylreductase partner mpsG incorporate one unit of acetyl-CoA, seven units of malonyl-CoA, and one unit of L-alanine to assemble the linear tetramic acid intermediate corresponding to the backbone of macrophasetins. Without the Diels-Alderase mpsD, the mpsA/G product can undergo the non-enzymatic intramolecular Diels-Alder (IMDA) reaction to generate both macrophasetin A and macrophasetin B. Catalyzed by mpsD, the linear tetramic acid intermediate is thoroughly converted to macrophasetin A via the endo- IMDA reaction in a regioselective and stereoselective manner. Finally, the cytochrome P450 monooxygenase mpsF catalyzes the hydroxylation at C20 to yield the end product macrophasetin C.",,,,,,,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0016491; GO:0031177,GO:0031177; GO:0016747,GO:0004315; GO:0008927,,GO:0031177; GO:0016746,,0.7316,0.5343,,0.7131,,3,0.6597,0.2559,no
ERTA_BURS1,K4PZA7,ESM2Text,Bacteria,544,"Lyase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the conversion of ergothioneine to thiourocanic acid and trimethylamine, the first step of the pathway. Cannot use D- histidine, L-histidine, D-tyrosine, L-tyrosine, D-phenylalanine or L- phenylalanine.","Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.",No,No,No,No,No,not-Yes,GO:0016841,GO:0008964,GO:0008964,GO:0008948,GO:0008964,GO:0008964,0.3502,0.3502,0.3987,0.3502,0.3502,5,0.3599,0.3575,no
ERTA_BURS1,K4PZA7,Prot2Text,Bacteria,544,"Lyase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the conversion of ergothioneine to thiourocanic acid and trimethylamine, the first step of the pathway. Cannot use D- histidine, L-histidine, D-tyrosine, L-tyrosine, D-phenylalanine or L- phenylalanine.",Plays a role in aerobically respiring hydrogen peroxide H(2)O(2).,No,No,No,No,No,not-Yes,GO:0016841,,,,,,,,,,,0,,0.3575,no
ERTA_BURS1,K4PZA7,ProtT3,Bacteria,544,"Lyase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the conversion of ergothioneine to thiourocanic acid and trimethylamine, the first step of the pathway. Cannot use D- histidine, L-histidine, D-tyrosine, L-tyrosine, D-phenylalanine or L- phenylalanine.",Cytoplasm. Belongs to the phenylalanyl-tRNA synthetase beta subunit family,Vague,No,Vague,Vague,No,not-Yes,GO:0016841,GO:0004826; GO:0005524,GO:0004826; GO:0005524,GO:0004826; GO:0005524,GO:0004826; GO:0005524,GO:0004826; GO:0005524,0.1495,0.1495,0.1495,0.1495,0.1495,5,0.1495,0.3575,no
ERTA_BURS1,K4PZA7,ProtTale,Bacteria,544,"Lyase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the conversion of ergothioneine to thiourocanic acid and trimethylamine, the first step of the pathway. Cannot use D- histidine, L-histidine, D-tyrosine, L-tyrosine, D-phenylalanine or L- phenylalanine.",Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate.,No,No,No,No,No,not-Yes,GO:0016841,GO:0004619,GO:0004619,GO:0004619,GO:0004619,GO:0004619,0.2353,0.2353,0.2353,0.2353,0.2353,5,0.2353,0.3575,no
ERTA_BURS1,K4PZA7,Protein2Text,Bacteria,544,"Lyase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the conversion of ergothioneine to thiourocanic acid and trimethylamine, the first step of the pathway. Cannot use D- histidine, L-histidine, D-tyrosine, L-tyrosine, D-phenylalanine or L- phenylalanine.","The molecular function of this protein is catalyzing the transfer of a hydroxyl group from a donor (NADPH) to a hydroxyl group of a substrate (2-oxoglutarate). Specifically, this protein is involved in the degradation of aromatic compounds via the catechol 2,3-dioxygenase pathway, which is a critical step in the metabolism of aromatic compounds. This protein catalyzes the oxidation of catechol to cis,cis-muconic acid.",No,No,No,No,No,not-Yes,GO:0016841,GO:0018576,GO:0016702,GO:0016491,GO:0018576,,0.2157,0.245,0.4071,0.2157,,4,0.2709,0.3575,no
ERTA_BURS1,K4PZA7,Reference,Bacteria,544,"Lyase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the conversion of ergothioneine to thiourocanic acid and trimethylamine, the first step of the pathway. Cannot use D- histidine, L-histidine, D-tyrosine, L-tyrosine, D-phenylalanine or L- phenylalanine.","Lyase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the conversion of ergothioneine to thiourocanic acid and trimethylamine, the first step of the pathway. Cannot use D- histidine, L-histidine, D-tyrosine, L-tyrosine, D-phenylalanine or L- phenylalanine.",,,,,,,GO:0016841,GO:0016829,GO:0016840,GO:0016829,GO:0016829,GO:0016829,0.6897,0.8416,0.6897,0.6897,0.6897,5,0.7201,0.3575,no
MANT_MYCHD,K5BE02,ESM2Text,Bacteria,411,"Glycosyltransferase involved in the biosynthesis of 3-O- methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in non-tuberculous mycobacteria. Highly specific alpha-(1->4)-mannosyltransferase that can transfer mannose units from GDP-mannose to a wide range of alpha-(1->4) oligomannosides longer than three mannoses, including all hydrolytic products of MmpH. Can use synthetic trimannosides and tetramannosides as substrates, but not mono- and disaccharides, and is significantly more active with the methylated substrates, preferring the tetramannosides over the trimannosides.",Catalyzes the addition of a mannose residue from GDP-D-mannose to diacylglycerol to generate GDP-D-glucose.,Yes,No,Maybe,Maybe,Maybe,not-Yes,GO:0016757,GO:0000030,GO:0000030,GO:0016757,GO:0000030,GO:0000030,0.729,0.729,1.0,0.729,0.729,5,0.7832,0.3646,no
MANT_MYCHD,K5BE02,Prot2Text,Bacteria,411,"Glycosyltransferase involved in the biosynthesis of 3-O- methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in non-tuberculous mycobacteria. Highly specific alpha-(1->4)-mannosyltransferase that can transfer mannose units from GDP-mannose to a wide range of alpha-(1->4) oligomannosides longer than three mannoses, including all hydrolytic products of MmpH. Can use synthetic trimannosides and tetramannosides as substrates, but not mono- and disaccharides, and is significantly more active with the methylated substrates, preferring the tetramannosides over the trimannosides.",Involved in the biosynthesis of the antifungal agent validamycin A. Catalyzes the addition of a mannose residue from GDP-Man to validoxylamine A to yield validoxylamine A.,Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0016757,GO:0000030,GO:0000030,GO:0000030,GO:0000030,GO:0000030,0.729,0.729,0.729,0.729,0.729,5,0.729,0.3646,no
MANT_MYCHD,K5BE02,ProtT3,Bacteria,411,"Glycosyltransferase involved in the biosynthesis of 3-O- methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in non-tuberculous mycobacteria. Highly specific alpha-(1->4)-mannosyltransferase that can transfer mannose units from GDP-mannose to a wide range of alpha-(1->4) oligomannosides longer than three mannoses, including all hydrolytic products of MmpH. Can use synthetic trimannosides and tetramannosides as substrates, but not mono- and disaccharides, and is significantly more active with the methylated substrates, preferring the tetramannosides over the trimannosides.",Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3646,no
MANT_MYCHD,K5BE02,ProtTale,Bacteria,411,"Glycosyltransferase involved in the biosynthesis of 3-O- methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in non-tuberculous mycobacteria. Highly specific alpha-(1->4)-mannosyltransferase that can transfer mannose units from GDP-mannose to a wide range of alpha-(1->4) oligomannosides longer than three mannoses, including all hydrolytic products of MmpH. Can use synthetic trimannosides and tetramannosides as substrates, but not mono- and disaccharides, and is significantly more active with the methylated substrates, preferring the tetramannosides over the trimannosides.",Epimerase that catalyzes the conversion of UDP-glucuronic acid (UDP-GlcUA) to UDP-glucuronate (UDP-GlcA) at the C-3 position.,No,No,No,No,No,not-Yes,GO:0016757,GO:0016857,GO:0016857,GO:0016857,GO:0016854,GO:0016857,0.3284,0.3284,0.3284,0.3902,0.3284,5,0.3408,0.3646,no
MANT_MYCHD,K5BE02,Protein2Text,Bacteria,411,"Glycosyltransferase involved in the biosynthesis of 3-O- methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in non-tuberculous mycobacteria. Highly specific alpha-(1->4)-mannosyltransferase that can transfer mannose units from GDP-mannose to a wide range of alpha-(1->4) oligomannosides longer than three mannoses, including all hydrolytic products of MmpH. Can use synthetic trimannosides and tetramannosides as substrates, but not mono- and disaccharides, and is significantly more active with the methylated substrates, preferring the tetramannosides over the trimannosides.","The molecular function of this protein is an enzyme involved in the biosynthesis of a type of sugar molecule. Specifically, it is a transferase involved in the synthesis of a nucleotide sugar molecule.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016757,,GO:0016757,GO:0016757,,,,1.0,1.0,,,2,1.0,0.3646,no
MANT_MYCHD,K5BE02,Reference,Bacteria,411,"Glycosyltransferase involved in the biosynthesis of 3-O- methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in non-tuberculous mycobacteria. Highly specific alpha-(1->4)-mannosyltransferase that can transfer mannose units from GDP-mannose to a wide range of alpha-(1->4) oligomannosides longer than three mannoses, including all hydrolytic products of MmpH. Can use synthetic trimannosides and tetramannosides as substrates, but not mono- and disaccharides, and is significantly more active with the methylated substrates, preferring the tetramannosides over the trimannosides.","Glycosyltransferase involved in the biosynthesis of 3-O- methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in non-tuberculous mycobacteria. Highly specific alpha-(1->4)-mannosyltransferase that can transfer mannose units from GDP-mannose to a wide range of alpha-(1->4) oligomannosides longer than three mannoses, including all hydrolytic products of MmpH. Can use synthetic trimannosides and tetramannosides as substrates, but not mono- and disaccharides, and is significantly more active with the methylated substrates, preferring the tetramannosides over the trimannosides.",,,,,,,GO:0016757,GO:0000030; GO:0005525,GO:0000030,GO:0000030,GO:0000030; GO:0016757,GO:0000030,0.5105,0.729,0.729,0.9097,0.729,5,0.7214,0.3646,no
MMPH_MYCHD,K5BIS0,ESM2Text,Bacteria,359,"Hydrolase involved in the biosynthesis of 3-O-methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in non-tuberculous mycobacteria. Highly specific hydrolase that catalyzes the internal cleavage of MMP. Is able to hydrolyze purified MMP into distinct lower order oligomannosides but does not cleave acylated or deacylated forms of 6-O-methylglucose lipopolysaccharide (MGLP), beta-mannans, synthetic 4alpha-oligomannosides or its own reaction products. Products were identified as four distinct oligomannosides differing in the number of mannose units (4 to 8) and methylation pattern (free or methylated C1-OH). Might serve as a recycling enzyme that hydrolyzes mature MMP into defined- size smaller oligomannosides that are, in turn, substrates for ManT and MeT1 activities for further processing into new daughter MMP chains.","Catalyzes the hydrolysis of glucosyl-N-acetylglucosamine (GlcNAc) to produce short peptides with a beta-1,6-linked mannose residue. Can also hydrolyze n-glycans, with lower efficiency.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787,GO:0016798,GO:0004553,GO:0016798,GO:0004553,GO:0016798,0.8145,0.6897,0.8145,0.6897,0.8145,5,0.7646,0.1915,no
MMPH_MYCHD,K5BIS0,Prot2Text,Bacteria,359,"Hydrolase involved in the biosynthesis of 3-O-methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in non-tuberculous mycobacteria. Highly specific hydrolase that catalyzes the internal cleavage of MMP. Is able to hydrolyze purified MMP into distinct lower order oligomannosides but does not cleave acylated or deacylated forms of 6-O-methylglucose lipopolysaccharide (MGLP), beta-mannans, synthetic 4alpha-oligomannosides or its own reaction products. Products were identified as four distinct oligomannosides differing in the number of mannose units (4 to 8) and methylation pattern (free or methylated C1-OH). Might serve as a recycling enzyme that hydrolyzes mature MMP into defined- size smaller oligomannosides that are, in turn, substrates for ManT and MeT1 activities for further processing into new daughter MMP chains.","Catalyzes the hydrolysis of oligosaccharides with unsaturated glucuronyl residues at the non-reducing terminal, to a sugar or an amino sugar, and an unsaturated D-glucuronic acid (GlcA), which is nonenzymatically converted immediately to alpha-keto acid. It cannot act on non-glucuronic acid residues of any length.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787,GO:0004553,GO:0016798,GO:0016798,GO:0016798,GO:0047692,0.6897,0.8145,0.8145,0.8145,0.4892,5,0.7245,0.1915,no
MMPH_MYCHD,K5BIS0,ProtT3,Bacteria,359,"Hydrolase involved in the biosynthesis of 3-O-methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in non-tuberculous mycobacteria. Highly specific hydrolase that catalyzes the internal cleavage of MMP. Is able to hydrolyze purified MMP into distinct lower order oligomannosides but does not cleave acylated or deacylated forms of 6-O-methylglucose lipopolysaccharide (MGLP), beta-mannans, synthetic 4alpha-oligomannosides or its own reaction products. Products were identified as four distinct oligomannosides differing in the number of mannose units (4 to 8) and methylation pattern (free or methylated C1-OH). Might serve as a recycling enzyme that hydrolyzes mature MMP into defined- size smaller oligomannosides that are, in turn, substrates for ManT and MeT1 activities for further processing into new daughter MMP chains.","Catalyzes the hydrolysis of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) to N-acetylmuramic acid (MurNAc) and acetate. Belongs to the glycosyl hydrolase 43 family",Maybe,No,No,No,No,not-Yes,GO:0016787,GO:0016798,GO:0016787,GO:0016798,GO:0016787,GO:0016798,0.8145,1.0,0.8145,1.0,0.8145,5,0.8887,0.1915,no
MMPH_MYCHD,K5BIS0,ProtTale,Bacteria,359,"Hydrolase involved in the biosynthesis of 3-O-methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in non-tuberculous mycobacteria. Highly specific hydrolase that catalyzes the internal cleavage of MMP. Is able to hydrolyze purified MMP into distinct lower order oligomannosides but does not cleave acylated or deacylated forms of 6-O-methylglucose lipopolysaccharide (MGLP), beta-mannans, synthetic 4alpha-oligomannosides or its own reaction products. Products were identified as four distinct oligomannosides differing in the number of mannose units (4 to 8) and methylation pattern (free or methylated C1-OH). Might serve as a recycling enzyme that hydrolyzes mature MMP into defined- size smaller oligomannosides that are, in turn, substrates for ManT and MeT1 activities for further processing into new daughter MMP chains.","Catalyzes the hydrolysis of alpha-D-glucose 1-phosphate (alpha-D-Glc-1-P) to alpha-D-glucose and D-glyceraldehyde 3- phosphate. Is involved in the degradation pathway of glucosamine, a major component of the mycobacterial cell wall.",No,No,No,No,No,not-Yes,GO:0016787,GO:0050308,GO:0016787,GO:0016787,GO:0016791,GO:0016791,0.4908,1.0,1.0,0.6019,0.6019,5,0.7389,0.1915,no
MMPH_MYCHD,K5BIS0,Protein2Text,Bacteria,359,"Hydrolase involved in the biosynthesis of 3-O-methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in non-tuberculous mycobacteria. Highly specific hydrolase that catalyzes the internal cleavage of MMP. Is able to hydrolyze purified MMP into distinct lower order oligomannosides but does not cleave acylated or deacylated forms of 6-O-methylglucose lipopolysaccharide (MGLP), beta-mannans, synthetic 4alpha-oligomannosides or its own reaction products. Products were identified as four distinct oligomannosides differing in the number of mannose units (4 to 8) and methylation pattern (free or methylated C1-OH). Might serve as a recycling enzyme that hydrolyzes mature MMP into defined- size smaller oligomannosides that are, in turn, substrates for ManT and MeT1 activities for further processing into new daughter MMP chains.","This protein is a beta-glucosidase, which is an enzyme that catalyzes the hydrolysis of beta-glucosides into glucose and other sugar molecules.",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0016787,GO:0008422,GO:0008422,GO:0008422,GO:0008422,GO:0008422,0.5381,0.5381,0.5381,0.5381,0.5381,5,0.5381,0.1915,no
MMPH_MYCHD,K5BIS0,Reference,Bacteria,359,"Hydrolase involved in the biosynthesis of 3-O-methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in non-tuberculous mycobacteria. Highly specific hydrolase that catalyzes the internal cleavage of MMP. Is able to hydrolyze purified MMP into distinct lower order oligomannosides but does not cleave acylated or deacylated forms of 6-O-methylglucose lipopolysaccharide (MGLP), beta-mannans, synthetic 4alpha-oligomannosides or its own reaction products. Products were identified as four distinct oligomannosides differing in the number of mannose units (4 to 8) and methylation pattern (free or methylated C1-OH). Might serve as a recycling enzyme that hydrolyzes mature MMP into defined- size smaller oligomannosides that are, in turn, substrates for ManT and MeT1 activities for further processing into new daughter MMP chains.","Hydrolase involved in the biosynthesis of 3-O-methylmannose polysaccharides (MMP), which are intracellular polymethylated polysaccharides implicated in the modulation of fatty acid metabolism in non-tuberculous mycobacteria. Highly specific hydrolase that catalyzes the internal cleavage of MMP. Is able to hydrolyze purified MMP into distinct lower order oligomannosides but does not cleave acylated or deacylated forms of 6-O-methylglucose lipopolysaccharide (MGLP), beta-mannans, synthetic 4alpha-oligomannosides or its own reaction products. Products were identified as four distinct oligomannosides differing in the number of mannose units (4 to 8) and methylation pattern (free or methylated C1-OH). Might serve as a recycling enzyme that hydrolyzes mature MMP into defined- size smaller oligomannosides that are, in turn, substrates for ManT and MeT1 activities for further processing into new daughter MMP chains.",,,,,,,GO:0016787,GO:0016798,GO:0004553,GO:0004553,GO:0016798,GO:0004553,0.8145,0.6897,0.6897,0.8145,0.6897,5,0.7396,0.1915,no
ODO1_PIG,K9IVI1,ESM2Text,Eukaryota,1023,"2-oxoglutarate dehydrogenase (E1o) component of the 2- oxoglutarate dehydrogenase complex (OGDHC). Participates in the first step, rate limiting for the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) catalyzed by the whole OGDHC. Catalyzes the irreversible decarboxylation of 2-oxoglutarate (alpha-ketoglutarate) via the thiamine diphosphate (ThDP) cofactor and subsequent transfer of the decarboxylated acyl intermediate on an oxidized dihydrolipoyl group that is covalently amidated to the E2 enzyme (dihydrolipoyllysine-residue succinyltransferase or DLST). Plays a key role in the Krebs (citric acid) cycle, which is a common pathway for oxidation of fuel molecules, including carbohydrates, fatty acids, and amino acids. Can catalyze the decarboxylation of 2-oxoadipate in vitro, but at a much lower rate than 2-oxoglutarate. Can also convert 2-keto-4-hydroxyglutarate (KHG) and CoA into malyl-CoA. Mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl- CoA to histone succinyltransferase KAT2A.","2-oxoglutarate dehydrogenase (E1o) component of the 2-oxoglutarate dehydrogenase complex (OGDHC). Participates in the first step, rate limiting for the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) catalyzed by the whole OGDHC. Catalyzes the irreversible decarboxylation of 2-oxoglutarate (alpha-ketoglutarate) via the thiamine diphosphate (ThDP) cofactor and subsequent transfer of the decarboxylated acyl intermediate on an oxidized dihydrolipoyl group that is covalently amidated to the E2 enzyme (dihydrolipoyllysine-residue succinyltransferase or DLST). Plays a key role in the Krebs (citric acid) cycle, which is a common pathway for oxidation of fuel molecules, including carbohydrates, fatty acids, and amino acids. Can catalyze the decarboxylation of 2-oxoadipate in vitro, but at a much lower rate than 2-oxoglutarate. Mainly active in the mitochondrion. A fraction of the 2-oxogl",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0004591; GO:0030976,GO:0004591,GO:0004591,GO:0004591; GO:0016624,GO:0004591; GO:0030976,GO:0004591; GO:0030976,0.5398,0.5398,0.6084,0.8993,0.8993,5,0.6973,0.566,yes
ODO1_PIG,K9IVI1,Prot2Text,Eukaryota,1023,"2-oxoglutarate dehydrogenase (E1o) component of the 2- oxoglutarate dehydrogenase complex (OGDHC). Participates in the first step, rate limiting for the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) catalyzed by the whole OGDHC. Catalyzes the irreversible decarboxylation of 2-oxoglutarate (alpha-ketoglutarate) via the thiamine diphosphate (ThDP) cofactor and subsequent transfer of the decarboxylated acyl intermediate on an oxidized dihydrolipoyl group that is covalently amidated to the E2 enzyme (dihydrolipoyllysine-residue succinyltransferase or DLST). Plays a key role in the Krebs (citric acid) cycle, which is a common pathway for oxidation of fuel molecules, including carbohydrates, fatty acids, and amino acids. Can catalyze the decarboxylation of 2-oxoadipate in vitro, but at a much lower rate than 2-oxoglutarate. Can also convert 2-keto-4-hydroxyglutarate (KHG) and CoA into malyl-CoA. Mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl- CoA to histone succinyltransferase KAT2A.","2-oxoglutarate dehydrogenase (E1o) component of the 2-oxoglutarate dehydrogenase complex (OGDHC). Participates in the first step, rate limiting for the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) catalyzed by the whole OGDHC. Catalyzes the irreversible decarboxylation of 2-oxoglutarate (alpha-ketoglutarate) via the thiamine diphosphate (ThDP) cofactor and subsequent transfer of the decarboxylated acyl intermediate on an oxidized dihydrolipoyl group that is covalently amidated to the E2 enzyme (dihydrolipoyllysine-residue succinyltransferase or DLST). Plays a key role in the Krebs (citric acid) cycle, which is a common pathway for oxidation of fuel molecules, including carbohydrates, fatty acids, and amino acids. Can catalyze the decarboxylation of 2-oxoadipate in vitro, but at a much lower rate than 2-oxoglutarate. Mainly active in the mitochondrion. A fraction of the 2-oxogl",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0004591; GO:0030976,GO:0004591,GO:0004591,GO:0004591,GO:0004591,GO:0004591,0.5398,0.5398,0.5398,0.5398,0.5398,5,0.5398,0.566,yes
ODO1_PIG,K9IVI1,ProtT3,Eukaryota,1023,"2-oxoglutarate dehydrogenase (E1o) component of the 2- oxoglutarate dehydrogenase complex (OGDHC). Participates in the first step, rate limiting for the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) catalyzed by the whole OGDHC. Catalyzes the irreversible decarboxylation of 2-oxoglutarate (alpha-ketoglutarate) via the thiamine diphosphate (ThDP) cofactor and subsequent transfer of the decarboxylated acyl intermediate on an oxidized dihydrolipoyl group that is covalently amidated to the E2 enzyme (dihydrolipoyllysine-residue succinyltransferase or DLST). Plays a key role in the Krebs (citric acid) cycle, which is a common pathway for oxidation of fuel molecules, including carbohydrates, fatty acids, and amino acids. Can catalyze the decarboxylation of 2-oxoadipate in vitro, but at a much lower rate than 2-oxoglutarate. Can also convert 2-keto-4-hydroxyglutarate (KHG) and CoA into malyl-CoA. Mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl- CoA to histone succinyltransferase KAT2A.","The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). Mitochondrion matrix. Belongs to the alpha-ketoglutarate dehydrogenase family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0004591; GO:0030976,GO:0004591,GO:0004591,GO:0004591,GO:0004591,GO:0004591,0.5398,0.5398,0.5398,0.5398,0.5398,5,0.5398,0.566,yes
ODO1_PIG,K9IVI1,ProtTale,Eukaryota,1023,"2-oxoglutarate dehydrogenase (E1o) component of the 2- oxoglutarate dehydrogenase complex (OGDHC). Participates in the first step, rate limiting for the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) catalyzed by the whole OGDHC. Catalyzes the irreversible decarboxylation of 2-oxoglutarate (alpha-ketoglutarate) via the thiamine diphosphate (ThDP) cofactor and subsequent transfer of the decarboxylated acyl intermediate on an oxidized dihydrolipoyl group that is covalently amidated to the E2 enzyme (dihydrolipoyllysine-residue succinyltransferase or DLST). Plays a key role in the Krebs (citric acid) cycle, which is a common pathway for oxidation of fuel molecules, including carbohydrates, fatty acids, and amino acids. Can catalyze the decarboxylation of 2-oxoadipate in vitro, but at a much lower rate than 2-oxoglutarate. Can also convert 2-keto-4-hydroxyglutarate (KHG) and CoA into malyl-CoA. Mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl- CoA to histone succinyltransferase KAT2A.","Acts as a regulatory subunit of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).",No,No,Maybe,Maybe,No,not-Yes,GO:0046872; GO:0004591; GO:0030976,,,,,,,,,,,0,,0.566,yes
ODO1_PIG,K9IVI1,Protein2Text,Eukaryota,1023,"2-oxoglutarate dehydrogenase (E1o) component of the 2- oxoglutarate dehydrogenase complex (OGDHC). Participates in the first step, rate limiting for the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) catalyzed by the whole OGDHC. Catalyzes the irreversible decarboxylation of 2-oxoglutarate (alpha-ketoglutarate) via the thiamine diphosphate (ThDP) cofactor and subsequent transfer of the decarboxylated acyl intermediate on an oxidized dihydrolipoyl group that is covalently amidated to the E2 enzyme (dihydrolipoyllysine-residue succinyltransferase or DLST). Plays a key role in the Krebs (citric acid) cycle, which is a common pathway for oxidation of fuel molecules, including carbohydrates, fatty acids, and amino acids. Can catalyze the decarboxylation of 2-oxoadipate in vitro, but at a much lower rate than 2-oxoglutarate. Can also convert 2-keto-4-hydroxyglutarate (KHG) and CoA into malyl-CoA. Mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl- CoA to histone succinyltransferase KAT2A.","The molecular function of this protein is an isomerase, specifically a pyruvate dehydrogenase complex subunit 2, which catalyzes the isomerization of pyruvate to acetyl-CoA.",No,No,Maybe,No,No,not-Yes,GO:0046872; GO:0004591; GO:0030976,,,,,,,,,,,0,,0.566,yes
ODO1_PIG,K9IVI1,Reference,Eukaryota,1023,"2-oxoglutarate dehydrogenase (E1o) component of the 2- oxoglutarate dehydrogenase complex (OGDHC). Participates in the first step, rate limiting for the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) catalyzed by the whole OGDHC. Catalyzes the irreversible decarboxylation of 2-oxoglutarate (alpha-ketoglutarate) via the thiamine diphosphate (ThDP) cofactor and subsequent transfer of the decarboxylated acyl intermediate on an oxidized dihydrolipoyl group that is covalently amidated to the E2 enzyme (dihydrolipoyllysine-residue succinyltransferase or DLST). Plays a key role in the Krebs (citric acid) cycle, which is a common pathway for oxidation of fuel molecules, including carbohydrates, fatty acids, and amino acids. Can catalyze the decarboxylation of 2-oxoadipate in vitro, but at a much lower rate than 2-oxoglutarate. Can also convert 2-keto-4-hydroxyglutarate (KHG) and CoA into malyl-CoA. Mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl- CoA to histone succinyltransferase KAT2A.","2-oxoglutarate dehydrogenase (E1o) component of the 2- oxoglutarate dehydrogenase complex (OGDHC). Participates in the first step, rate limiting for the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) catalyzed by the whole OGDHC. Catalyzes the irreversible decarboxylation of 2-oxoglutarate (alpha-ketoglutarate) via the thiamine diphosphate (ThDP) cofactor and subsequent transfer of the decarboxylated acyl intermediate on an oxidized dihydrolipoyl group that is covalently amidated to the E2 enzyme (dihydrolipoyllysine-residue succinyltransferase or DLST). Plays a key role in the Krebs (citric acid) cycle, which is a common pathway for oxidation of fuel molecules, including carbohydrates, fatty acids, and amino acids. Can catalyze the decarboxylation of 2-oxoadipate in vitro, but at a much lower rate than 2-oxoglutarate. Can also convert 2-keto-4-hydroxyglutarate (KHG) and CoA into malyl-CoA. Mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl- CoA to histone succinyltransferase KAT2A.",,,,,,,GO:0046872; GO:0004591; GO:0030976,GO:0004591; GO:0030976,GO:0004591; GO:0030976,GO:0004591; GO:0030976,GO:0004591; GO:0030976,GO:0004591; GO:0030976,0.8993,0.8993,0.8993,0.8993,0.8993,5,0.8993,0.566,yes
XYNC_HUMIN,M4MEY9,ESM2Text,Eukaryota,390,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Is more active on soluble wheat arabinoxylan (defined as 100%) than on birchwood xylan (72.4%) and beechwood xylan (665.3%), and less active on insoluble wheat arabinoxylan (39.3%). The major hydrolysis products of XynC are mainly consisting of xylobiose and xylotriose with a small amount of xylose.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0030248; GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,0.6973,0.6973,0.6973,0.6973,0.6973,5,0.6973,0.327,no
XYNC_HUMIN,M4MEY9,Prot2Text,Eukaryota,390,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Is more active on soluble wheat arabinoxylan (defined as 100%) than on birchwood xylan (72.4%) and beechwood xylan (665.3%), and less active on insoluble wheat arabinoxylan (39.3%). The major hydrolysis products of XynC are mainly consisting of xylobiose and xylotriose with a small amount of xylose.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0030248; GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,0.6973,0.6973,0.6973,0.6973,0.6973,5,0.6973,0.327,no
XYNC_HUMIN,M4MEY9,ProtT3,Eukaryota,390,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Is more active on soluble wheat arabinoxylan (defined as 100%) than on birchwood xylan (72.4%) and beechwood xylan (665.3%), and less active on insoluble wheat arabinoxylan (39.3%). The major hydrolysis products of XynC are mainly consisting of xylobiose and xylotriose with a small amount of xylose.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Secreted. Belongs to the glycosyl hydrolase 10 (cellulase F) family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0030248; GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,0.6973,0.6973,0.6973,0.6973,0.6973,5,0.6973,0.327,no
XYNC_HUMIN,M4MEY9,ProtTale,Eukaryota,390,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Is more active on soluble wheat arabinoxylan (defined as 100%) than on birchwood xylan (72.4%) and beechwood xylan (665.3%), and less active on insoluble wheat arabinoxylan (39.3%). The major hydrolysis products of XynC are mainly consisting of xylobiose and xylotriose with a small amount of xylose.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0030248; GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,0.6973,0.6973,0.6973,0.6973,0.6973,5,0.6973,0.327,no
XYNC_HUMIN,M4MEY9,Protein2Text,Eukaryota,390,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Is more active on soluble wheat arabinoxylan (defined as 100%) than on birchwood xylan (72.4%) and beechwood xylan (665.3%), and less active on insoluble wheat arabinoxylan (39.3%). The major hydrolysis products of XynC are mainly consisting of xylobiose and xylotriose with a small amount of xylose.","The molecular function of this protein is to break down and hydrolyze complex polysaccharides, specifically cellulose, into simpler sugar molecules. This protein is a type of endoglucanase, which is an enzyme that catalyzes the hydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, resulting in the formation of shorter chains of glucose molecules. This process is essential for the degradation of cellulose, a major component of plant cell walls, into simpler sugars that can be used by the organism as a source of energy.",No,No,No,No,No,not-Yes,GO:0030248; GO:0031176,GO:0008810; GO:0030248,GO:0016162,GO:0016162; GO:0030245,GO:0016162,GO:0008810,0.8168,0.4572,0.3429,0.4572,0.4572,5,0.5063,0.327,no
XYNC_HUMIN,M4MEY9,Reference,Eukaryota,390,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Is more active on soluble wheat arabinoxylan (defined as 100%) than on birchwood xylan (72.4%) and beechwood xylan (665.3%), and less active on insoluble wheat arabinoxylan (39.3%). The major hydrolysis products of XynC are mainly consisting of xylobiose and xylotriose with a small amount of xylose.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Is more active on soluble wheat arabinoxylan (defined as 100%) than on birchwood xylan (72.4%) and beechwood xylan (665.3%), and less active on insoluble wheat arabinoxylan (39.3%). The major hydrolysis products of XynC are mainly consisting of xylobiose and xylotriose with a small amount of xylose.",,,,,,,GO:0030248; GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,0.6973,0.6973,0.6973,0.6973,0.6973,5,0.6973,0.327,no
OX547_MYCTU,O06413,ESM2Text,Bacteria,294,"Oxidoreductase that promotes the persistence of M.tuberculosis in host macrophages by reprogramming the fatty acid metabolism in host mitochondria. When localized in the host mitochondria, it potentially acts on unknown lipid substrates and converts them into products that directly or indirectly alter the lipid profile of the mitochondria. This change in lipid profile results in increased mitochondrial membrane fluidity, enhanced endogenous fatty acid oxidation and increased mitochondrial spare respiratory capacity. All these events eventually favor M.tuberculosis persistence in the host macrophages. In vitro, can catalyze the NADPH-dependent reduction of palmitoyl-CoA (hexadecanoyl-CoA).","Catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose to 1,5-anhydro-beta-D-glucoside. It is involved in a degradation pathway of the highly branched-chain fatty acids that allows mycobacteria to use longer-chain fatty acids as a carbon source.",Maybe,No,No,No,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016616,GO:0016491,GO:0016491; GO:0050661,GO:0016491; GO:0050661,1.0,0.6897,1.0,0.7089,0.7089,5,0.8215,0.2225,no
OX547_MYCTU,O06413,Prot2Text,Bacteria,294,"Oxidoreductase that promotes the persistence of M.tuberculosis in host macrophages by reprogramming the fatty acid metabolism in host mitochondria. When localized in the host mitochondria, it potentially acts on unknown lipid substrates and converts them into products that directly or indirectly alter the lipid profile of the mitochondria. This change in lipid profile results in increased mitochondrial membrane fluidity, enhanced endogenous fatty acid oxidation and increased mitochondrial spare respiratory capacity. All these events eventually favor M.tuberculosis persistence in the host macrophages. In vitro, can catalyze the NADPH-dependent reduction of palmitoyl-CoA (hexadecanoyl-CoA).","Oxidoreductase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome monooxygenase P450 claM then catalyzes the dimerization of nataloe-emodin to cladofulvin.",Maybe,No,No,No,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2225,no
OX547_MYCTU,O06413,ProtT3,Bacteria,294,"Oxidoreductase that promotes the persistence of M.tuberculosis in host macrophages by reprogramming the fatty acid metabolism in host mitochondria. When localized in the host mitochondria, it potentially acts on unknown lipid substrates and converts them into products that directly or indirectly alter the lipid profile of the mitochondria. This change in lipid profile results in increased mitochondrial membrane fluidity, enhanced endogenous fatty acid oxidation and increased mitochondrial spare respiratory capacity. All these events eventually favor M.tuberculosis persistence in the host macrophages. In vitro, can catalyze the NADPH-dependent reduction of palmitoyl-CoA (hexadecanoyl-CoA).",Belongs to the short-chain dehydrogenases/reductases (SDR) family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016491,,GO:0016491,,GO:0016491,,,1.0,,1.0,,2,1.0,0.2225,no
OX547_MYCTU,O06413,ProtTale,Bacteria,294,"Oxidoreductase that promotes the persistence of M.tuberculosis in host macrophages by reprogramming the fatty acid metabolism in host mitochondria. When localized in the host mitochondria, it potentially acts on unknown lipid substrates and converts them into products that directly or indirectly alter the lipid profile of the mitochondria. This change in lipid profile results in increased mitochondrial membrane fluidity, enhanced endogenous fatty acid oxidation and increased mitochondrial spare respiratory capacity. All these events eventually favor M.tuberculosis persistence in the host macrophages. In vitro, can catalyze the NADPH-dependent reduction of palmitoyl-CoA (hexadecanoyl-CoA).",Catalyzes the oxidative deamination of D-aspartate to 2-oxoglutarate and of L-aspartate to 2-oxoglutarate during aspartate metabolism in the mitochondrion. Plays a role in the regulation of mitochondrial respiration.,No,No,No,No,No,not-Yes,GO:0016491,GO:0016641,GO:0016641; GO:0016638,GO:0033735,GO:0008124,GO:0008445,0.6897,0.7729,0.5381,0.3552,0.4908,5,0.5693,0.2225,no
OX547_MYCTU,O06413,Protein2Text,Bacteria,294,"Oxidoreductase that promotes the persistence of M.tuberculosis in host macrophages by reprogramming the fatty acid metabolism in host mitochondria. When localized in the host mitochondria, it potentially acts on unknown lipid substrates and converts them into products that directly or indirectly alter the lipid profile of the mitochondria. This change in lipid profile results in increased mitochondrial membrane fluidity, enhanced endogenous fatty acid oxidation and increased mitochondrial spare respiratory capacity. All these events eventually favor M.tuberculosis persistence in the host macrophages. In vitro, can catalyze the NADPH-dependent reduction of palmitoyl-CoA (hexadecanoyl-CoA).","The molecular function of this protein is an enzyme involved in the biosynthesis of isoprenoids, specifically in the reduction of an intermediate in the pathway. It catalyzes a reaction in which a carbon-carbon double bond is reduced.",Vague,No,No,Vague,No,not-Yes,GO:0016491,,GO:0016491,GO:0016491,,,,1.0,1.0,,,2,1.0,0.2225,no
OX547_MYCTU,O06413,Reference,Bacteria,294,"Oxidoreductase that promotes the persistence of M.tuberculosis in host macrophages by reprogramming the fatty acid metabolism in host mitochondria. When localized in the host mitochondria, it potentially acts on unknown lipid substrates and converts them into products that directly or indirectly alter the lipid profile of the mitochondria. This change in lipid profile results in increased mitochondrial membrane fluidity, enhanced endogenous fatty acid oxidation and increased mitochondrial spare respiratory capacity. All these events eventually favor M.tuberculosis persistence in the host macrophages. In vitro, can catalyze the NADPH-dependent reduction of palmitoyl-CoA (hexadecanoyl-CoA).","Oxidoreductase that promotes the persistence of M.tuberculosis in host macrophages by reprogramming the fatty acid metabolism in host mitochondria. When localized in the host mitochondria, it potentially acts on unknown lipid substrates and converts them into products that directly or indirectly alter the lipid profile of the mitochondria. This change in lipid profile results in increased mitochondrial membrane fluidity, enhanced endogenous fatty acid oxidation and increased mitochondrial spare respiratory capacity. All these events eventually favor M.tuberculosis persistence in the host macrophages. In vitro, can catalyze the NADPH-dependent reduction of palmitoyl-CoA (hexadecanoyl-CoA).",,,,,,,GO:0016491,GO:0016491; GO:0050661,GO:0016491; GO:0050661,GO:0016491,GO:0016491; GO:0050661,GO:0016491,0.7089,0.7089,1.0,0.7089,1.0,5,0.8253,0.2225,no
CLAMT_ARATH,O23234,ESM2Text,Eukaryota,371,"Methyltransferase involved in the biosynthesis of strigolactone natural products, bioactive compounds promoting plant fitness and soil microbe interactions, but preventing shoot branching. Catalyzes the biosynthesis of (11R)-methyl carlactonoate (MeCLA) from (11R)-carlactonoate (CLA), downstream of MAX1; MeCLA is probably biologically active as a hormone regulating shoot branching and serves as a precursor of non-canonical strigolactones (SLs).","Methyltransferase involved in the biosynthesis of methyl anthranilate in response to stresses. Utilizes anthranilic acid (ABA) as substrate, but not salicylate, L-carnitine or benzoic acid. Can also use anthranilate and m-carnitine but not tryptamine (T4). Unable to convert kynurenine to anthranilate.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0008757,GO:0008168,GO:0008168,GO:0008171,GO:0008171,GO:0008168,0.607,0.607,0.5156,0.5156,0.607,5,0.5704,0.3343,no
CLAMT_ARATH,O23234,Prot2Text,Eukaryota,371,"Methyltransferase involved in the biosynthesis of strigolactone natural products, bioactive compounds promoting plant fitness and soil microbe interactions, but preventing shoot branching. Catalyzes the biosynthesis of (11R)-methyl carlactonoate (MeCLA) from (11R)-carlactonoate (CLA), downstream of MAX1; MeCLA is probably biologically active as a hormone regulating shoot branching and serves as a precursor of non-canonical strigolactones (SLs).",Catalyzes the methylation of the free carboxyl end of the plant hormone indole-3-acetic acid (IAA). Converts IAA to IAA methyl ester (MeIAA). Regulates IAA activities by IAA methylation. Methylation of IAA plays an important role in regulating plant development and auxin homeostasis. MeIAA seems to be an inactive form of IAA.,Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0008757,GO:0010340,GO:0008168,GO:0008168,GO:0008168,GO:0008171,0.4481,0.607,0.607,0.607,0.5156,5,0.5569,0.3343,no
CLAMT_ARATH,O23234,ProtT3,Eukaryota,371,"Methyltransferase involved in the biosynthesis of strigolactone natural products, bioactive compounds promoting plant fitness and soil microbe interactions, but preventing shoot branching. Catalyzes the biosynthesis of (11R)-methyl carlactonoate (MeCLA) from (11R)-carlactonoate (CLA), downstream of MAX1; MeCLA is probably biologically active as a hormone regulating shoot branching and serves as a precursor of non-canonical strigolactones (SLs).",Involved in the biosynthesis of caffeine. Catalyzes the conversion of 7-methylxanthine (7mX) to theobromine and of theobromine to caffeine. Belongs to the methyltransferase superfamily. Type-7 methyltransferase family,Maybe,No,No,No,Maybe,not-Yes,GO:0046872; GO:0008757,GO:0008168,GO:0008170,GO:0042159; GO:0008168,GO:0008168,GO:0042409; GO:0008168,0.607,0.5156,0.4552,0.607,0.6519,5,0.5673,0.3343,no
CLAMT_ARATH,O23234,ProtTale,Eukaryota,371,"Methyltransferase involved in the biosynthesis of strigolactone natural products, bioactive compounds promoting plant fitness and soil microbe interactions, but preventing shoot branching. Catalyzes the biosynthesis of (11R)-methyl carlactonoate (MeCLA) from (11R)-carlactonoate (CLA), downstream of MAX1; MeCLA is probably biologically active as a hormone regulating shoot branching and serves as a precursor of non-canonical strigolactones (SLs).",May be involved in the biosynthesis of caffeine.,Vague,Vague,No,Vague,Vague,not-Yes,GO:0046872; GO:0008757,,,,,,,,,,,0,,0.3343,no
CLAMT_ARATH,O23234,Protein2Text,Eukaryota,371,"Methyltransferase involved in the biosynthesis of strigolactone natural products, bioactive compounds promoting plant fitness and soil microbe interactions, but preventing shoot branching. Catalyzes the biosynthesis of (11R)-methyl carlactonoate (MeCLA) from (11R)-carlactonoate (CLA), downstream of MAX1; MeCLA is probably biologically active as a hormone regulating shoot branching and serves as a precursor of non-canonical strigolactones (SLs).",The molecular function of this protein is an S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the conversion of caffeine to theobromine and theobromine to theophylline. It is involved in the biosynthesis of methylxanthines.,Maybe,No,Maybe,No,Maybe,not-Yes,GO:0046872; GO:0008757,GO:0042054; GO:0008171,GO:0042054,GO:0008171,GO:0042159,GO:0008168,0.5241,0.3925,0.5156,0.0,0.607,5,0.4078,0.3343,no
CLAMT_ARATH,O23234,Reference,Eukaryota,371,"Methyltransferase involved in the biosynthesis of strigolactone natural products, bioactive compounds promoting plant fitness and soil microbe interactions, but preventing shoot branching. Catalyzes the biosynthesis of (11R)-methyl carlactonoate (MeCLA) from (11R)-carlactonoate (CLA), downstream of MAX1; MeCLA is probably biologically active as a hormone regulating shoot branching and serves as a precursor of non-canonical strigolactones (SLs).","Methyltransferase involved in the biosynthesis of strigolactone natural products, bioactive compounds promoting plant fitness and soil microbe interactions, but preventing shoot branching. Catalyzes the biosynthesis of (11R)-methyl carlactonoate (MeCLA) from (11R)-carlactonoate (CLA), downstream of MAX1; MeCLA is probably biologically active as a hormone regulating shoot branching and serves as a precursor of non-canonical strigolactones (SLs).",,,,,,,GO:0046872; GO:0008757,GO:0008168; GO:0032259,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.4552,0.607,0.607,0.607,0.607,5,0.5766,0.3343,no
OXSA_PRIMG,O24769,ESM2Text,Bacteria,194,"Phosphohydrolase involved in the biosynthesis of oxetanocin A (OXT-A), a nucleoside analog with antitumor, antiviral and antibacterial properties. Catalyzes the hydrolysis of phosphooxetanocin A (OXT-A-P) to generate oxetanocin A (OXT-A) and a molecule of inorganic phosphate. Can also bind and hydrolyze OXT triphosphate (OXT-A- PPP) and OXT diphosphate (OXT-A-PP), and thus catalyze the sequential hydrolysis of tri-, di- and mono-phosphorylated oxetanocin A compounds, releasing one molecule of inorganic phosphate at a time. In vitro can also use dATP, dAMP and dADP.",Catalyzes the hydrolysis of the adenosine 5'-monophosphate (AMP) group of the minor teichoic acid component of lipopolysaccharide (LPS).,No,No,Maybe,Maybe,Maybe,not-Yes,GO:0016787; GO:0046872,GO:0016787,GO:0016787,GO:0016787,GO:0016787,,0.7193,0.7193,0.7193,0.7193,,4,0.7193,0.358,no
OXSA_PRIMG,O24769,Prot2Text,Bacteria,194,"Phosphohydrolase involved in the biosynthesis of oxetanocin A (OXT-A), a nucleoside analog with antitumor, antiviral and antibacterial properties. Catalyzes the hydrolysis of phosphooxetanocin A (OXT-A-P) to generate oxetanocin A (OXT-A) and a molecule of inorganic phosphate. Can also bind and hydrolyze OXT triphosphate (OXT-A- PPP) and OXT diphosphate (OXT-A-PP), and thus catalyze the sequential hydrolysis of tri-, di- and mono-phosphorylated oxetanocin A compounds, releasing one molecule of inorganic phosphate at a time. In vitro can also use dATP, dAMP and dADP.",Catalyzes the strictly specific dephosphorylation of 2'-deoxyribonucleoside 5'-monophosphates.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787; GO:0046872,GO:0008253,GO:0008253,GO:0008253,GO:0008253,GO:0008253,0.35,0.35,0.35,0.35,0.35,5,0.35,0.358,no
OXSA_PRIMG,O24769,ProtT3,Bacteria,194,"Phosphohydrolase involved in the biosynthesis of oxetanocin A (OXT-A), a nucleoside analog with antitumor, antiviral and antibacterial properties. Catalyzes the hydrolysis of phosphooxetanocin A (OXT-A-P) to generate oxetanocin A (OXT-A) and a molecule of inorganic phosphate. Can also bind and hydrolyze OXT triphosphate (OXT-A- PPP) and OXT diphosphate (OXT-A-PP), and thus catalyze the sequential hydrolysis of tri-, di- and mono-phosphorylated oxetanocin A compounds, releasing one molecule of inorganic phosphate at a time. In vitro can also use dATP, dAMP and dADP.",Belongs to the UPF0725 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016787; GO:0046872,,,,,,,,,,,0,,0.358,no
OXSA_PRIMG,O24769,ProtTale,Bacteria,194,"Phosphohydrolase involved in the biosynthesis of oxetanocin A (OXT-A), a nucleoside analog with antitumor, antiviral and antibacterial properties. Catalyzes the hydrolysis of phosphooxetanocin A (OXT-A-P) to generate oxetanocin A (OXT-A) and a molecule of inorganic phosphate. Can also bind and hydrolyze OXT triphosphate (OXT-A- PPP) and OXT diphosphate (OXT-A-PP), and thus catalyze the sequential hydrolysis of tri-, di- and mono-phosphorylated oxetanocin A compounds, releasing one molecule of inorganic phosphate at a time. In vitro can also use dATP, dAMP and dADP.",Catalyzes the deamination of dATP to dAMP.,Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787; GO:0046872,GO:0019239,GO:0019239,GO:0019239,GO:0019239,,0.4947,0.4947,0.4947,0.4947,,4,0.4947,0.358,no
OXSA_PRIMG,O24769,Protein2Text,Bacteria,194,"Phosphohydrolase involved in the biosynthesis of oxetanocin A (OXT-A), a nucleoside analog with antitumor, antiviral and antibacterial properties. Catalyzes the hydrolysis of phosphooxetanocin A (OXT-A-P) to generate oxetanocin A (OXT-A) and a molecule of inorganic phosphate. Can also bind and hydrolyze OXT triphosphate (OXT-A- PPP) and OXT diphosphate (OXT-A-PP), and thus catalyze the sequential hydrolysis of tri-, di- and mono-phosphorylated oxetanocin A compounds, releasing one molecule of inorganic phosphate at a time. In vitro can also use dATP, dAMP and dADP.","The molecular function of this protein is an ADP-ribose transferase, specifically involved in the cleavage of a 3'-5' linked ADP-ribose diphosphate bond in the 3'-5' linked ADP-ribose diphosphate bond of ADP-ribose-AMP, releasing AMP and releasing ADP-ribose. 
It is also a 3'-5' ADP-ribose transferase, catalyzing the transfer of ADP-ribose to a target protein. It can catalyze the transfer of ADP-ribose to a target protein from an ADP-ribose donor, releasing the target protein with a covalently attached ADP-ribose moiety. 
It is also a ribose ADP-ribose transferase, catalyzing the transfer of ribose ADP-ribose to a target protein. It can catalyze the transfer of ribose ADP-ribose to a target protein from an ADP-ribose donor, releasing the target protein with a covalently attached ADP-ribose moiety.
It is also a phosphoribosyltransferase, catalyzing the transfer of a ribose phosphate group to an amino acid.
It is also a nucleoside diphosphate ribose hydrolase, catalyzing the hydrolysis of a nucleoside diphosphate to release a ribose and a nucleoside monophosphate.
It is also a phosphoribosyltransferase, catalyzing the transfer of a ribose phosphate group to an amino acid. 
It is also a ribose diphosphate hydrolase, catalyzing the hydrolysis of a ribose diphosphate to release a ribose and a phosphate. 
It is also a ribose monophosphate hydrolase, catalyzing the hydrolysis of a ribose monophosphate to release a ribose and a phosphate.
It is also a 3'-5' linked ADP-ribose diphosphate bond hydrolase, catalyzing the hydrolysis of a 3'-5' linked ADP-ribose diphosphate bond to release ADP-ribose and AMP.
It is also a 3'-5' linked ADP-ribose bond hydrolase, catalyzing the hydrolysis of a 3'-5' linked ADP-ribose bond to release",No,No,No,No,No,not-Yes,GO:0016787; GO:0046872,,GO:0003950,GO:0003950,GO:0003950,,,0.2664,0.2664,0.2664,,3,0.2664,0.358,no
OXSA_PRIMG,O24769,Reference,Bacteria,194,"Phosphohydrolase involved in the biosynthesis of oxetanocin A (OXT-A), a nucleoside analog with antitumor, antiviral and antibacterial properties. Catalyzes the hydrolysis of phosphooxetanocin A (OXT-A-P) to generate oxetanocin A (OXT-A) and a molecule of inorganic phosphate. Can also bind and hydrolyze OXT triphosphate (OXT-A- PPP) and OXT diphosphate (OXT-A-PP), and thus catalyze the sequential hydrolysis of tri-, di- and mono-phosphorylated oxetanocin A compounds, releasing one molecule of inorganic phosphate at a time. In vitro can also use dATP, dAMP and dADP.","Phosphohydrolase involved in the biosynthesis of oxetanocin A (OXT-A), a nucleoside analog with antitumor, antiviral and antibacterial properties. Catalyzes the hydrolysis of phosphooxetanocin A (OXT-A-P) to generate oxetanocin A (OXT-A) and a molecule of inorganic phosphate. Can also bind and hydrolyze OXT triphosphate (OXT-A- PPP) and OXT diphosphate (OXT-A-PP), and thus catalyze the sequential hydrolysis of tri-, di- and mono-phosphorylated oxetanocin A compounds, releasing one molecule of inorganic phosphate at a time. In vitro can also use dATP, dAMP and dADP.",,,,,,,GO:0016787; GO:0046872,GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,0.4309,0.4309,0.4309,0.4309,0.4309,5,0.4309,0.358,no
OXSB_PRIMG,O24770,ESM2Text,Bacteria,744,"Isomerase involved in the biosynthesis of oxetanocin A (OXT- A), a nucleoside analog with antitumor, antiviral and antibacterial properties. Catalyzes an oxidative ring contraction of dAMP, forming an oxetane aldehyde. In addition, shows methyltransferase activity in vitro and is able to catalyze the radical mediated, stereoselective C2'-methylation of dAMP to form methylated 2'-dAMP. Also catalyzes the demethylation of S-adenosyl-L- methionine (SAM) to S-adenosyl-L-homocysteine (SAH).","Transcriptional regulator of siroheme-dependent heme b biosynthesis. Involved in the biosynthesis of the siroheme cofactor. Siroheme is an intermediate in the biosynthesis of the isocyanide naphthoquinone cofactor (C6), the precursor of the isocyanide moiety of sulfide-containing dihydroquinone core.",No,No,Maybe,No,No,not-Yes,GO:0051539; GO:0031419; GO:0016853; GO:0046872,,GO:0003700,,GO:0003700,,,0.1983,,0.1983,,2,0.1983,0.2862,no
OXSB_PRIMG,O24770,Prot2Text,Bacteria,744,"Isomerase involved in the biosynthesis of oxetanocin A (OXT- A), a nucleoside analog with antitumor, antiviral and antibacterial properties. Catalyzes an oxidative ring contraction of dAMP, forming an oxetane aldehyde. In addition, shows methyltransferase activity in vitro and is able to catalyze the radical mediated, stereoselective C2'-methylation of dAMP to form methylated 2'-dAMP. Also catalyzes the demethylation of S-adenosyl-L- methionine (SAM) to S-adenosyl-L-homocysteine (SAH).",Radical SAM methyltransferase that mediates the methylation of C-20 (mth) position of cysteine residues in target proteins.,Maybe,No,Maybe,Maybe,No,not-Yes,GO:0051539; GO:0031419; GO:0016853; GO:0046872,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.2262,0.2262,0.2262,0.2262,0.2262,5,0.2262,0.2862,no
OXSB_PRIMG,O24770,ProtT3,Bacteria,744,"Isomerase involved in the biosynthesis of oxetanocin A (OXT- A), a nucleoside analog with antitumor, antiviral and antibacterial properties. Catalyzes an oxidative ring contraction of dAMP, forming an oxetane aldehyde. In addition, shows methyltransferase activity in vitro and is able to catalyze the radical mediated, stereoselective C2'-methylation of dAMP to form methylated 2'-dAMP. Also catalyzes the demethylation of S-adenosyl-L- methionine (SAM) to S-adenosyl-L-homocysteine (SAH).",Belongs to the radical SAM superfamily,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0051539; GO:0031419; GO:0016853; GO:0046872,,,,,,,,,,,0,,0.2862,no
OXSB_PRIMG,O24770,ProtTale,Bacteria,744,"Isomerase involved in the biosynthesis of oxetanocin A (OXT- A), a nucleoside analog with antitumor, antiviral and antibacterial properties. Catalyzes an oxidative ring contraction of dAMP, forming an oxetane aldehyde. In addition, shows methyltransferase activity in vitro and is able to catalyze the radical mediated, stereoselective C2'-methylation of dAMP to form methylated 2'-dAMP. Also catalyzes the demethylation of S-adenosyl-L- methionine (SAM) to S-adenosyl-L-homocysteine (SAH).",Catalyzes the conversion of L-fuconate to L-fuconate 5-phosphate.,No,No,No,No,No,not-Yes,GO:0051539; GO:0031419; GO:0016853; GO:0046872,GO:0016301,GO:0016301,GO:0016301,GO:0016301,GO:0016301,0.2262,0.2262,0.2262,0.2262,0.2262,5,0.2262,0.2862,no
OXSB_PRIMG,O24770,Protein2Text,Bacteria,744,"Isomerase involved in the biosynthesis of oxetanocin A (OXT- A), a nucleoside analog with antitumor, antiviral and antibacterial properties. Catalyzes an oxidative ring contraction of dAMP, forming an oxetane aldehyde. In addition, shows methyltransferase activity in vitro and is able to catalyze the radical mediated, stereoselective C2'-methylation of dAMP to form methylated 2'-dAMP. Also catalyzes the demethylation of S-adenosyl-L- methionine (SAM) to S-adenosyl-L-homocysteine (SAH).","Based on the information provided, the molecular function of this protein is not explicitly stated. However, as a component of the type VII secretion system (T7SS), it is likely involved in the secretion of virulence factors or other proteins. The T7SS is a complex secretion system that allows bacteria to export proteins across the outer membrane, often for the purpose of evading host defenses or infecting other cells. The specific function of this protein within the T7SS is likely to be involved in the assembly or regulation of the secretion apparatus. 

However, without more specific information, it is difficult to determine the exact molecular function of this protein. Further research or additional context would be needed to provide a more detailed answer.",No,No,No,No,No,not-Yes,GO:0051539; GO:0031419; GO:0016853; GO:0046872,,,,,,,,,,,0,,0.2862,no
OXSB_PRIMG,O24770,Reference,Bacteria,744,"Isomerase involved in the biosynthesis of oxetanocin A (OXT- A), a nucleoside analog with antitumor, antiviral and antibacterial properties. Catalyzes an oxidative ring contraction of dAMP, forming an oxetane aldehyde. In addition, shows methyltransferase activity in vitro and is able to catalyze the radical mediated, stereoselective C2'-methylation of dAMP to form methylated 2'-dAMP. Also catalyzes the demethylation of S-adenosyl-L- methionine (SAM) to S-adenosyl-L-homocysteine (SAH).","Isomerase involved in the biosynthesis of oxetanocin A (OXT- A), a nucleoside analog with antitumor, antiviral and antibacterial properties. Catalyzes an oxidative ring contraction of dAMP, forming an oxetane aldehyde. In addition, shows methyltransferase activity in vitro and is able to catalyze the radical mediated, stereoselective C2'-methylation of dAMP to form methylated 2'-dAMP. Also catalyzes the demethylation of S-adenosyl-L- methionine (SAM) to S-adenosyl-L-homocysteine (SAH).",,,,,,,GO:0051539; GO:0031419; GO:0016853; GO:0046872,GO:0016853; GO:0008168,GO:0016853; GO:0008168,GO:0016853; GO:0008168,GO:0016853; GO:0008168,GO:0016853; GO:0008168,0.479,0.479,0.479,0.479,0.479,5,0.479,0.2862,no
EXLYS_PBCV1,O41043,ESM2Text,Viruses,649,"During viral entry, involved in the degradation of the host cell wall at the site of attachment.",Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria.,No,No,No,No,No,not-Yes,GO:0016829,,,,,,,,,,,0,,0.2037,no
EXLYS_PBCV1,O41043,Prot2Text,Viruses,649,"During viral entry, involved in the degradation of the host cell wall at the site of attachment.",Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria.,No,No,No,No,No,not-Yes,GO:0016829,,,,,,,,,,,0,,0.2037,no
EXLYS_PBCV1,O41043,ProtT3,Viruses,649,"During viral entry, involved in the degradation of the host cell wall at the site of attachment.",Membrane; Single-pass membrane protein,Vague,No,Vague,Vague,Vague,not-Yes,GO:0016829,,,,,,,,,,,0,,0.2037,no
EXLYS_PBCV1,O41043,ProtTale,Viruses,649,"During viral entry, involved in the degradation of the host cell wall at the site of attachment.",Promotes colloidosmotic lysis by binding to the midgut epithelial cells of lepidopteran insects.,No,No,No,No,Maybe,not-Yes,GO:0016829,,,,,,,,,,,0,,0.2037,no
EXLYS_PBCV1,O41043,Protein2Text,Viruses,649,"During viral entry, involved in the degradation of the host cell wall at the site of attachment.","This protein is a viral protein, specifically a capsid protein, which is involved in the structural organization of the virus. It is likely to play a role in the assembly and stabilization of the viral capsid, which is composed of multiple copies of this protein. However, without more specific information, it is difficult to determine the exact molecular function of this protein.",No,No,No,No,No,not-Yes,GO:0016829,GO:0005198,GO:0005198,GO:0005198,GO:0005198,GO:0005198,0.3396,0.3396,0.3396,0.3396,0.3396,5,0.3396,0.2037,no
EXLYS_PBCV1,O41043,Reference,Viruses,649,"During viral entry, involved in the degradation of the host cell wall at the site of attachment.","During viral entry, involved in the degradation of the host cell wall at the site of attachment.",,,,,,,GO:0016829,,,,,,,,,,,0,,0.2037,no
VPAT_PBCV1,O41136,ESM2Text,Viruses,197,"Acetylates polyamines such as spermine, spermidine, cadaverine, homospermidine and putrescine (the latter with low efficiency). May play a role in the regulation of polyamine catabolism in the host during viral replication.",Required for the assimilation of polyamines. Substrate specificity: norspermidine = spermidine >> spermine > N(1)-acetylspermine.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004145,,,,,,,,,,,0,,0.2962,no
VPAT_PBCV1,O41136,Prot2Text,Viruses,197,"Acetylates polyamines such as spermine, spermidine, cadaverine, homospermidine and putrescine (the latter with low efficiency). May play a role in the regulation of polyamine catabolism in the host during viral replication.",Required for the assimilation of polyamines. Substrate specificity: norspermidine = spermidine >> spermine > N(1)-acetylspermine.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004145,,,,,,,,,,,0,,0.2962,no
VPAT_PBCV1,O41136,ProtT3,Viruses,197,"Acetylates polyamines such as spermine, spermidine, cadaverine, homospermidine and putrescine (the latter with low efficiency). May play a role in the regulation of polyamine catabolism in the host during viral replication.",Belongs to the acetyltransferase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004145,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.7126,0.7126,0.7126,0.7126,0.7126,5,0.7126,0.2962,no
VPAT_PBCV1,O41136,ProtTale,Viruses,197,"Acetylates polyamines such as spermine, spermidine, cadaverine, homospermidine and putrescine (the latter with low efficiency). May play a role in the regulation of polyamine catabolism in the host during viral replication.",Catalyzes the transfer of an acetyl group from acetyl-CoA to the sulfoquinovose component of the sulfolipid biosynthesis pathway.,No,No,No,No,No,not-Yes,GO:0004145,GO:0016407,GO:0016747,GO:0016747,GO:0016747,GO:0016407,0.7126,0.6227,0.6227,0.6227,0.7126,5,0.6587,0.2962,no
VPAT_PBCV1,O41136,Protein2Text,Viruses,197,"Acetylates polyamines such as spermine, spermidine, cadaverine, homospermidine and putrescine (the latter with low efficiency). May play a role in the regulation of polyamine catabolism in the host during viral replication.","The molecular function of this protein is not specified in the provided text. However, based on the fact that it is involved in the methylation of a molecule (specifically, it is a type of methyltransferase), it is likely that its molecular function is to catalyze the transfer of a methyl group from one molecule to another.",No,No,Vague,No,No,not-Yes,GO:0004145,GO:0008168,GO:0008168,GO:0008171,GO:0008168,GO:0008168,0.2893,0.2893,0.2413,0.2893,0.2893,5,0.2797,0.2962,no
VPAT_PBCV1,O41136,Reference,Viruses,197,"Acetylates polyamines such as spermine, spermidine, cadaverine, homospermidine and putrescine (the latter with low efficiency). May play a role in the regulation of polyamine catabolism in the host during viral replication.","Acetylates polyamines such as spermine, spermidine, cadaverine, homospermidine and putrescine (the latter with low efficiency). May play a role in the regulation of polyamine catabolism in the host during viral replication.",,,,,,,GO:0004145,GO:0004353,GO:0008080,GO:0016407,GO:0004145,GO:0004145,0.1213,0.8953,0.7126,1.0,1.0,5,0.7458,0.2962,no
TRWK_ECOLX,O50330,ESM2Text,Bacteria,823,"Component of the Trw type IV secretion system (T4SS), which is involved in bacterial conjugation of plasmid R388, a conjugative plasmid that confers resistance to sulfonamide and trimethoprim. The TrwK subunit provides energy for pilus biogenesis and substrate transfer. It shows ATPase activity. It can act as a dislocation motor to catalyze extraction of TrwL/VirB2 pilin monomers from the inner membrane during T4SS biogenesis, probably through ATP binding/hydrolysis, and acts synergistically with TrwD/VirB11 to induce a structural change in the pilin. Binds DNA, with a higher affinity for G4 quadruplex structures than for single-stranded DNA. It can inhibit the DNA-dependent ATPase activity of TrwB.",The virB operon is essential for intracellular survival and is not involved in the invasion process. Constitutes a major determinant of virulence in mice. Virb11 is essential for pathogenesis in mice but is not required for intracellular survival in crayfish.,Vague,No,No,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887,,,,,,,,,,,0,,0.3664,no
TRWK_ECOLX,O50330,Prot2Text,Bacteria,823,"Component of the Trw type IV secretion system (T4SS), which is involved in bacterial conjugation of plasmid R388, a conjugative plasmid that confers resistance to sulfonamide and trimethoprim. The TrwK subunit provides energy for pilus biogenesis and substrate transfer. It shows ATPase activity. It can act as a dislocation motor to catalyze extraction of TrwL/VirB2 pilin monomers from the inner membrane during T4SS biogenesis, probably through ATP binding/hydrolysis, and acts synergistically with TrwD/VirB11 to induce a structural change in the pilin. Binds DNA, with a higher affinity for G4 quadruplex structures than for single-stranded DNA. It can inhibit the DNA-dependent ATPase activity of TrwB.",Component of the type IV secretion system ptl essential for secretion of assembled pertussis toxin (PTX) through the outer membrane.,Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887,,,,,,,,,,,0,,0.3664,no
TRWK_ECOLX,O50330,ProtT3,Bacteria,823,"Component of the Trw type IV secretion system (T4SS), which is involved in bacterial conjugation of plasmid R388, a conjugative plasmid that confers resistance to sulfonamide and trimethoprim. The TrwK subunit provides energy for pilus biogenesis and substrate transfer. It shows ATPase activity. It can act as a dislocation motor to catalyze extraction of TrwL/VirB2 pilin monomers from the inner membrane during T4SS biogenesis, probably through ATP binding/hydrolysis, and acts synergistically with TrwD/VirB11 to induce a structural change in the pilin. Binds DNA, with a higher affinity for G4 quadruplex structures than for single-stranded DNA. It can inhibit the DNA-dependent ATPase activity of TrwB.",Cell inner membrane; Peripheral membrane protein. Belongs to the TrbL/VirB6 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0016887,,,,,,,,,,,0,,0.3664,no
TRWK_ECOLX,O50330,ProtTale,Bacteria,823,"Component of the Trw type IV secretion system (T4SS), which is involved in bacterial conjugation of plasmid R388, a conjugative plasmid that confers resistance to sulfonamide and trimethoprim. The TrwK subunit provides energy for pilus biogenesis and substrate transfer. It shows ATPase activity. It can act as a dislocation motor to catalyze extraction of TrwL/VirB2 pilin monomers from the inner membrane during T4SS biogenesis, probably through ATP binding/hydrolysis, and acts synergistically with TrwD/VirB11 to induce a structural change in the pilin. Binds DNA, with a higher affinity for G4 quadruplex structures than for single-stranded DNA. It can inhibit the DNA-dependent ATPase activity of TrwB.","Component of the VirB/VirD4 type IV secretion system (T4SS), which translocates transfer DNA (T-DNA) and virulence effector proteins into plant host cells, leading to crown gall disease. The VirB4 subunit is essential for virulence. It may be directly involved in substrate translocation, at least through a interactions with VirB2 and VirB11. It interacts with VirB2 through its C-terminal region, and with VirB11 through its N-terminal region. It also interacts with VirD2 through its C-terminal region, and with VirD4 through its",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887,,GO:0005524,GO:0005524,,,,0.6869,0.6869,,,2,0.6869,0.3664,no
TRWK_ECOLX,O50330,Protein2Text,Bacteria,823,"Component of the Trw type IV secretion system (T4SS), which is involved in bacterial conjugation of plasmid R388, a conjugative plasmid that confers resistance to sulfonamide and trimethoprim. The TrwK subunit provides energy for pilus biogenesis and substrate transfer. It shows ATPase activity. It can act as a dislocation motor to catalyze extraction of TrwL/VirB2 pilin monomers from the inner membrane during T4SS biogenesis, probably through ATP binding/hydrolysis, and acts synergistically with TrwD/VirB11 to induce a structural change in the pilin. Binds DNA, with a higher affinity for G4 quadruplex structures than for single-stranded DNA. It can inhibit the DNA-dependent ATPase activity of TrwB.","The molecular function of the protein is a DNA-binding activity. This protein is a part of the bacterial conjugation system, specifically responsible for DNA transfer between bacteria.",Maybe,No,No,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887,GO:0003677,GO:0003677,GO:0003677,GO:0003677,GO:0003677,0.1517,0.1517,0.1517,0.1517,0.1517,5,0.1517,0.3664,no
TRWK_ECOLX,O50330,Reference,Bacteria,823,"Component of the Trw type IV secretion system (T4SS), which is involved in bacterial conjugation of plasmid R388, a conjugative plasmid that confers resistance to sulfonamide and trimethoprim. The TrwK subunit provides energy for pilus biogenesis and substrate transfer. It shows ATPase activity. It can act as a dislocation motor to catalyze extraction of TrwL/VirB2 pilin monomers from the inner membrane during T4SS biogenesis, probably through ATP binding/hydrolysis, and acts synergistically with TrwD/VirB11 to induce a structural change in the pilin. Binds DNA, with a higher affinity for G4 quadruplex structures than for single-stranded DNA. It can inhibit the DNA-dependent ATPase activity of TrwB.","Component of the Trw type IV secretion system (T4SS), which is involved in bacterial conjugation of plasmid R388, a conjugative plasmid that confers resistance to sulfonamide and trimethoprim. The TrwK subunit provides energy for pilus biogenesis and substrate transfer. It shows ATPase activity. It can act as a dislocation motor to catalyze extraction of TrwL/VirB2 pilin monomers from the inner membrane during T4SS biogenesis, probably through ATP binding/hydrolysis, and acts synergistically with TrwD/VirB11 to induce a structural change in the pilin. Binds DNA, with a higher affinity for G4 quadruplex structures than for single-stranded DNA. It can inhibit the DNA-dependent ATPase activity of TrwB.",,,,,,,GO:0005524; GO:0016887,GO:0016887; GO:0003677,GO:0016887; GO:0003677,GO:0016887; GO:0003677,GO:0016887; GO:0003677,GO:0016887; GO:0003677,0.5827,0.5827,0.5827,0.5827,0.5827,5,0.5827,0.3664,no
TRWD_ECOLX,O50338,ESM2Text,Bacteria,358,"Component of the Trw type IV secretion system (T4SS), which is involved in bacterial conjugation of plasmid R388, a conjugative plasmid that confers resistance to sulfonamide and trimethoprim. The TrwD subunit provides energy for pilus biogenesis and substrate transfer. It shows ATPase activity. Also functions together with TrwK/VirB4 to induce a structural change in the pilin, suggesting a role for TrwD as a modulator of TrwK/VirB4 pilin dislocase activity. It may act as a molecular switch between pilus biogenesis and substrate transport. Interacts with the membranous systems to build up the transport assemblage that facilitates DNA transfer.","The type IV secretion system VirB/VirD4 is a major virulence determinant for subversion of human endothelial cell (HEC) function. VirB-dependent changes of HEC include massive cytoskeletal rearrangements, a pro-inflammatory activation by nuclear factor NF-kappa-B, inhibition of early and late events of apoptosis, leading to an increased cell survival, and, at high infection doses, a cytostatic or cytotoxic effect, which interfers with a potent VirB-independent mitogenic activity. These changes of HEC require the T4S coupling protein VirD4 and at least one of the effector proteins BepA-G. Altogether with VirB4 may be implicated in providing the energy, via hydrolysis of ATP, for the assembly of secretion system and substrate transport.",Maybe,No,No,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887,GO:0016887,GO:0016887,GO:0016887,GO:0016887; GO:0005524,GO:0005524; GO:0016887,0.6869,0.6869,0.6869,1.0,1.0,5,0.8121,0.2941,no
TRWD_ECOLX,O50338,Prot2Text,Bacteria,358,"Component of the Trw type IV secretion system (T4SS), which is involved in bacterial conjugation of plasmid R388, a conjugative plasmid that confers resistance to sulfonamide and trimethoprim. The TrwD subunit provides energy for pilus biogenesis and substrate transfer. It shows ATPase activity. Also functions together with TrwK/VirB4 to induce a structural change in the pilin, suggesting a role for TrwD as a modulator of TrwK/VirB4 pilin dislocase activity. It may act as a molecular switch between pilus biogenesis and substrate transport. Interacts with the membranous systems to build up the transport assemblage that facilitates DNA transfer.",The VirB system could be required for the establishment of the replication niche in the host.,Vague,No,No,No,Maybe,not-Yes,GO:0005524; GO:0016887,,,,,,,,,,,0,,0.2941,no
TRWD_ECOLX,O50338,ProtT3,Bacteria,358,"Component of the Trw type IV secretion system (T4SS), which is involved in bacterial conjugation of plasmid R388, a conjugative plasmid that confers resistance to sulfonamide and trimethoprim. The TrwD subunit provides energy for pilus biogenesis and substrate transfer. It shows ATPase activity. Also functions together with TrwK/VirB4 to induce a structural change in the pilin, suggesting a role for TrwD as a modulator of TrwK/VirB4 pilin dislocase activity. It may act as a molecular switch between pilus biogenesis and substrate transport. Interacts with the membranous systems to build up the transport assemblage that facilitates DNA transfer.",Cytoplasm. Belongs to the GSP E family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0016887,,,,,,,,,,,0,,0.2941,no
TRWD_ECOLX,O50338,ProtTale,Bacteria,358,"Component of the Trw type IV secretion system (T4SS), which is involved in bacterial conjugation of plasmid R388, a conjugative plasmid that confers resistance to sulfonamide and trimethoprim. The TrwD subunit provides energy for pilus biogenesis and substrate transfer. It shows ATPase activity. Also functions together with TrwK/VirB4 to induce a structural change in the pilin, suggesting a role for TrwD as a modulator of TrwK/VirB4 pilin dislocase activity. It may act as a molecular switch between pilus biogenesis and substrate transport. Interacts with the membranous systems to build up the transport assemblage that facilitates DNA transfer.","Component of the VirB/VirD4 type IV secretion system (T4SS), which translocates transfer DNA (T-DNA) and virulence effector proteins into plant host cells, leading to crown gall disease. The VirB11 subunit is essential for virulence. It provides energy for pilus biogenesis and substrate transfer. It binds and hydrolyzes ATP.",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887,GO:0016887,GO:0005524; GO:0016887,GO:0005524; GO:0016887,GO:0005524; GO:0016887,GO:0016887,0.6869,1.0,1.0,1.0,0.6869,5,0.8748,0.2941,no
TRWD_ECOLX,O50338,Protein2Text,Bacteria,358,"Component of the Trw type IV secretion system (T4SS), which is involved in bacterial conjugation of plasmid R388, a conjugative plasmid that confers resistance to sulfonamide and trimethoprim. The TrwD subunit provides energy for pilus biogenesis and substrate transfer. It shows ATPase activity. Also functions together with TrwK/VirB4 to induce a structural change in the pilin, suggesting a role for TrwD as a modulator of TrwK/VirB4 pilin dislocase activity. It may act as a molecular switch between pilus biogenesis and substrate transport. Interacts with the membranous systems to build up the transport assemblage that facilitates DNA transfer.","The molecular function of this protein is to catalyze the synthesis of ATP from ADP in the presence of a proton gradient across the membrane. It is a component of the ATP synthase complex, which is responsible for generating ATP from ADP and inorganic phosphate using the energy from the proton gradient. This protein is a subunit of the enzyme and is involved in the synthesis of ATP.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016887,GO:0046933; GO:0046961,GO:0046933; GO:0046961,GO:0046933; GO:0046961,GO:0046933; GO:0046961,GO:0046933,0.1226,0.1226,0.1226,0.1226,0.1161,5,0.1213,0.2941,no
TRWD_ECOLX,O50338,Reference,Bacteria,358,"Component of the Trw type IV secretion system (T4SS), which is involved in bacterial conjugation of plasmid R388, a conjugative plasmid that confers resistance to sulfonamide and trimethoprim. The TrwD subunit provides energy for pilus biogenesis and substrate transfer. It shows ATPase activity. Also functions together with TrwK/VirB4 to induce a structural change in the pilin, suggesting a role for TrwD as a modulator of TrwK/VirB4 pilin dislocase activity. It may act as a molecular switch between pilus biogenesis and substrate transport. Interacts with the membranous systems to build up the transport assemblage that facilitates DNA transfer.","Component of the Trw type IV secretion system (T4SS), which is involved in bacterial conjugation of plasmid R388, a conjugative plasmid that confers resistance to sulfonamide and trimethoprim. The TrwD subunit provides energy for pilus biogenesis and substrate transfer. It shows ATPase activity. Also functions together with TrwK/VirB4 to induce a structural change in the pilin, suggesting a role for TrwD as a modulator of TrwK/VirB4 pilin dislocase activity. It may act as a molecular switch between pilus biogenesis and substrate transport. Interacts with the membranous systems to build up the transport assemblage that facilitates DNA transfer.",,,,,,,GO:0005524; GO:0016887,GO:0016887,GO:0016887,GO:0016887,GO:0016887,GO:0016887,0.6869,0.6869,0.6869,0.6869,0.6869,5,0.6869,0.2941,no
HYDA_THEMA,O52683,ESM2Text,Bacteria,645,"Catalyzes the oxidation of the physiological electron carriers NADH and reduced ferredoxin, coupled to the production of H(2). Acts as a bifurcating [FeFe] hydrogenase, which uses the exergonic oxidation of reduced ferredoxin to drive the unfavorable oxidation of NADH to produce H(2). The alpha subunit contains the catalytic H-cluster.",Component of the fumarate reductase complex (FrdABC) that catalyzes the reduction of fumarate to succinate. The FrdABC is a catalytic subunit of the enzyme complex.,No,No,No,No,No,not-Yes,GO:0051537; GO:0051539; GO:0102220; GO:0046872; GO:0008137,GO:0016491,GO:0000104,GO:0000104; GO:0008177,GO:0000104,GO:0000104,0.2996,0.2003,0.2153,0.2003,0.2003,5,0.2232,0.4433,no
HYDA_THEMA,O52683,Prot2Text,Bacteria,645,"Catalyzes the oxidation of the physiological electron carriers NADH and reduced ferredoxin, coupled to the production of H(2). Acts as a bifurcating [FeFe] hydrogenase, which uses the exergonic oxidation of reduced ferredoxin to drive the unfavorable oxidation of NADH to produce H(2). The alpha subunit contains the catalytic H-cluster.",Methane-docking protein required for the transfer of electrons from methylamine dehydrogenase to the reaction centers of photosystem II (PSII).,No,No,No,No,No,not-Yes,GO:0051537; GO:0051539; GO:0102220; GO:0046872; GO:0008137,GO:0009055,GO:0009055,GO:0009055,GO:0009055,GO:0009055,0.245,0.245,0.245,0.245,0.245,5,0.245,0.4433,no
HYDA_THEMA,O52683,ProtT3,Bacteria,645,"Catalyzes the oxidation of the physiological electron carriers NADH and reduced ferredoxin, coupled to the production of H(2). Acts as a bifurcating [FeFe] hydrogenase, which uses the exergonic oxidation of reduced ferredoxin to drive the unfavorable oxidation of NADH to produce H(2). The alpha subunit contains the catalytic H-cluster.",Catalyzes the reduction of hydrogen sulfide to sulfide. Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit family,No,No,No,Vague,Maybe,not-Yes,GO:0051537; GO:0051539; GO:0102220; GO:0046872; GO:0008137,GO:0008901,GO:0016491,GO:0008901,GO:0008901,GO:0033748,0.2287,0.2996,0.2287,0.2287,0.2684,5,0.2508,0.4433,no
HYDA_THEMA,O52683,ProtTale,Bacteria,645,"Catalyzes the oxidation of the physiological electron carriers NADH and reduced ferredoxin, coupled to the production of H(2). Acts as a bifurcating [FeFe] hydrogenase, which uses the exergonic oxidation of reduced ferredoxin to drive the unfavorable oxidation of NADH to produce H(2). The alpha subunit contains the catalytic H-cluster.",Catalyzes the reduction of sulfite to sulfide.,No,No,No,No,No,not-Yes,GO:0051537; GO:0051539; GO:0102220; GO:0046872; GO:0008137,GO:0016657,GO:0016491,GO:0016491,GO:0016491,GO:0050311,0.0,0.2996,0.2996,0.2996,0.1709,5,0.2139,0.4433,no
HYDA_THEMA,O52683,Protein2Text,Bacteria,645,"Catalyzes the oxidation of the physiological electron carriers NADH and reduced ferredoxin, coupled to the production of H(2). Acts as a bifurcating [FeFe] hydrogenase, which uses the exergonic oxidation of reduced ferredoxin to drive the unfavorable oxidation of NADH to produce H(2). The alpha subunit contains the catalytic H-cluster.",The molecular function of this protein is as a hydrogenase.,Vague,No,No,Maybe,Vague,not-Yes,GO:0051537; GO:0051539; GO:0102220; GO:0046872; GO:0008137,GO:0008901,GO:0016491,GO:0016491,GO:0016491,GO:0033748,0.2287,0.2996,0.2996,0.2996,0.2684,5,0.2792,0.4433,no
HYDA_THEMA,O52683,Reference,Bacteria,645,"Catalyzes the oxidation of the physiological electron carriers NADH and reduced ferredoxin, coupled to the production of H(2). Acts as a bifurcating [FeFe] hydrogenase, which uses the exergonic oxidation of reduced ferredoxin to drive the unfavorable oxidation of NADH to produce H(2). The alpha subunit contains the catalytic H-cluster.","Catalyzes the oxidation of the physiological electron carriers NADH and reduced ferredoxin, coupled to the production of H(2). Acts as a bifurcating [FeFe] hydrogenase, which uses the exergonic oxidation of reduced ferredoxin to drive the unfavorable oxidation of NADH to produce H(2). The alpha subunit contains the catalytic H-cluster.",,,,,,,GO:0051537; GO:0051539; GO:0102220; GO:0046872; GO:0008137,GO:0008901; GO:0009055,GO:0008901,GO:0008901,GO:0008901; GO:0016491,GO:0008901,0.327,0.2287,0.2287,0.33,0.2287,5,0.2686,0.4433,no
IDHAT_MYCTU,O53504,ESM2Text,Bacteria,206,"Acetyltransferase involved in the post-translational regulation of the central metabolic enzyme isocitrate dehydrogenase 1 (ICDH-1) through lysine acetylation. Catalyzes the acetylation of ICDH-1 at Lys-30 and Lys-129, using acetyl-CoA as a donor, leading to a reduction of ICDH-1 enzyme activity. Can also use propionyl-CoA and succinyl-CoA as donors. Cannot act on the isocitrate dehydrogenase 2 (ICDH-2). Might play a role in regulating the TCA cycle and methylcitrate cycle when M.tuberculosis utilizes fatty acid as carbon source.","Dual specificity enzyme that catalyzes the deacetylation of acetyl-CoA, producing acetate and CoA.",No,No,No,No,No,not-Yes,GO:0008080,GO:0003986,GO:0016790,GO:0016787,GO:0016790,GO:0016790,0.1562,0.1863,0.2823,0.1863,0.1863,5,0.1995,0.1287,no
IDHAT_MYCTU,O53504,Prot2Text,Bacteria,206,"Acetyltransferase involved in the post-translational regulation of the central metabolic enzyme isocitrate dehydrogenase 1 (ICDH-1) through lysine acetylation. Catalyzes the acetylation of ICDH-1 at Lys-30 and Lys-129, using acetyl-CoA as a donor, leading to a reduction of ICDH-1 enzyme activity. Can also use propionyl-CoA and succinyl-CoA as donors. Cannot act on the isocitrate dehydrogenase 2 (ICDH-2). Might play a role in regulating the TCA cycle and methylcitrate cycle when M.tuberculosis utilizes fatty acid as carbon source.",Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and releases both CoA and the acetylated product. It prefers the antibiotic chloramphenicol.,Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0008080,GO:0008811,GO:0008811,GO:0008811,GO:0008811,GO:0008811,0.5561,0.5561,0.5561,0.5561,0.5561,5,0.5561,0.1287,no
IDHAT_MYCTU,O53504,ProtT3,Bacteria,206,"Acetyltransferase involved in the post-translational regulation of the central metabolic enzyme isocitrate dehydrogenase 1 (ICDH-1) through lysine acetylation. Catalyzes the acetylation of ICDH-1 at Lys-30 and Lys-129, using acetyl-CoA as a donor, leading to a reduction of ICDH-1 enzyme activity. Can also use propionyl-CoA and succinyl-CoA as donors. Cannot act on the isocitrate dehydrogenase 2 (ICDH-2). Might play a role in regulating the TCA cycle and methylcitrate cycle when M.tuberculosis utilizes fatty acid as carbon source.",Catalyzes the transfer of an acetyl group from acetyl-CoA to L-ornithine to produce N(2)-acetyl-L-ornithine. Belongs to the acetyltransferase family,Maybe,Vague,No,Vague,Maybe,not-Yes,GO:0008080,GO:0016407,GO:0004042,GO:0004042,GO:0016407,GO:0016407,0.7867,0.8124,0.8124,0.7867,0.7867,5,0.797,0.1287,no
IDHAT_MYCTU,O53504,ProtTale,Bacteria,206,"Acetyltransferase involved in the post-translational regulation of the central metabolic enzyme isocitrate dehydrogenase 1 (ICDH-1) through lysine acetylation. Catalyzes the acetylation of ICDH-1 at Lys-30 and Lys-129, using acetyl-CoA as a donor, leading to a reduction of ICDH-1 enzyme activity. Can also use propionyl-CoA and succinyl-CoA as donors. Cannot act on the isocitrate dehydrogenase 2 (ICDH-2). Might play a role in regulating the TCA cycle and methylcitrate cycle when M.tuberculosis utilizes fatty acid as carbon source.",Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate leading to the formation of a new C-N bond at the elongation stage of lipid A biosynthesis.,Maybe,No,No,No,Maybe,not-Yes,GO:0008080,GO:0016410,GO:0016747,GO:0016747,GO:0016747,GO:0016410,0.7867,0.6795,0.6795,0.6795,0.7867,5,0.7224,0.1287,no
IDHAT_MYCTU,O53504,Protein2Text,Bacteria,206,"Acetyltransferase involved in the post-translational regulation of the central metabolic enzyme isocitrate dehydrogenase 1 (ICDH-1) through lysine acetylation. Catalyzes the acetylation of ICDH-1 at Lys-30 and Lys-129, using acetyl-CoA as a donor, leading to a reduction of ICDH-1 enzyme activity. Can also use propionyl-CoA and succinyl-CoA as donors. Cannot act on the isocitrate dehydrogenase 2 (ICDH-2). Might play a role in regulating the TCA cycle and methylcitrate cycle when M.tuberculosis utilizes fatty acid as carbon source.",The molecular function of this protein is an acetyltransferase.,Vague,Vague,No,Vague,Vague,not-Yes,GO:0008080,GO:0016407,GO:0008080,GO:0016407,GO:0016407,GO:0016407,0.7867,1.0,0.7867,0.7867,0.7867,5,0.8294,0.1287,no
IDHAT_MYCTU,O53504,Reference,Bacteria,206,"Acetyltransferase involved in the post-translational regulation of the central metabolic enzyme isocitrate dehydrogenase 1 (ICDH-1) through lysine acetylation. Catalyzes the acetylation of ICDH-1 at Lys-30 and Lys-129, using acetyl-CoA as a donor, leading to a reduction of ICDH-1 enzyme activity. Can also use propionyl-CoA and succinyl-CoA as donors. Cannot act on the isocitrate dehydrogenase 2 (ICDH-2). Might play a role in regulating the TCA cycle and methylcitrate cycle when M.tuberculosis utilizes fatty acid as carbon source.","Acetyltransferase involved in the post-translational regulation of the central metabolic enzyme isocitrate dehydrogenase 1 (ICDH-1) through lysine acetylation. Catalyzes the acetylation of ICDH-1 at Lys-30 and Lys-129, using acetyl-CoA as a donor, leading to a reduction of ICDH-1 enzyme activity. Can also use propionyl-CoA and succinyl-CoA as donors. Cannot act on the isocitrate dehydrogenase 2 (ICDH-2). Might play a role in regulating the TCA cycle and methylcitrate cycle when M.tuberculosis utilizes fatty acid as carbon source.",,,,,,,GO:0008080,GO:0004468; GO:0016747,GO:0004468,GO:0016407,GO:0004468,GO:0061733,0.7681,0.8124,0.7867,0.8124,0.7342,5,0.7828,0.1287,no
GT742_SIRGR,P0DO74,ESM2Text,Eukaryota,460,"UDP-glycosyltransferase involved in the biosynthesis of cucurbitacin and mogroside tetracyclic triterpene natural products (e.g. siamenoside I and mogrosides IV, V and VI). Cucurbitacins have cytotoxic properties and exhibit deterrent taste as a defense barrier against herbivores. Mogrosides are nonsugar highly oxygenated compounds used as high-intensity zero- calorie sweeteners; they also possess pharmacological properties such as regulating immunity, lowering blood sugar and lipid levels, protecting the liver, and acting as antioxidants and antitumor agents. Catalyzes the C3 primary glucosylation of mogrol, mogroside I-A1, mogroside II-A1, mogroside II-A and mogroside III-A1.","Glucosyltransferase that glucosylates jasmonate (JA) and JA derivatives. Converts JA to 12-hydroxyjasmonate (12OH-JA), an intermediate in JA biosynthetic and uptake in non-toxic conditions. Involved in JA biosynthesis, especially in the proximal part of the jasmonate-mediated defense mechanism. Also acts on other substrates such as N-ethyl-JA, N-ethyl-JA, N-ethylC-JA and N-ethylC-JA. No activity with 12-O- and 9-O-glucosides, or with the flavonoid linamarin, cytokinins, luminal bis(epsilon-phenyl)propionitrile, quercetin, kaempferol, quercitin, daphthol, daflactone, anthocyanin, anthocyanin, anthocyanin, daidzein, anthocyanin, quercitin, daidzein, quercitrin, butein, 3-O-glucoside, 3-O-diglucoside, anthocyanin, anthoc",Maybe,Maybe,Vague,Maybe,Maybe,not-Yes,GO:0080043; GO:0080044,GO:0008194,GO:0035251,GO:0016757,GO:0008194,GO:0035251,0.6513,0.9023,0.5541,0.6513,0.9023,5,0.7323,0.2574,no
GT742_SIRGR,P0DO74,Prot2Text,Eukaryota,460,"UDP-glycosyltransferase involved in the biosynthesis of cucurbitacin and mogroside tetracyclic triterpene natural products (e.g. siamenoside I and mogrosides IV, V and VI). Cucurbitacins have cytotoxic properties and exhibit deterrent taste as a defense barrier against herbivores. Mogrosides are nonsugar highly oxygenated compounds used as high-intensity zero- calorie sweeteners; they also possess pharmacological properties such as regulating immunity, lowering blood sugar and lipid levels, protecting the liver, and acting as antioxidants and antitumor agents. Catalyzes the C3 primary glucosylation of mogrol, mogroside I-A1, mogroside II-A1, mogroside II-A and mogroside III-A1.",Involved in the biosynthesis of steviol glycosides in leaves. Converts steviol to the mono-glycoside steviolmonoside. Converts the mono-glycoside steviolmonoside to the bi-glycoside rubusoside. Converts the bi-glycoside steviolbioside to the tri-glycoside stevioside. Converts the tri-glycoside rebaudioside A to the tetra-glycoside rebaudioside A.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0080043; GO:0080044,GO:0008194,GO:0008194,GO:0008194,GO:0035251,GO:0035251,0.6513,0.6513,0.6513,0.9023,0.9023,5,0.7517,0.2574,no
GT742_SIRGR,P0DO74,ProtT3,Eukaryota,460,"UDP-glycosyltransferase involved in the biosynthesis of cucurbitacin and mogroside tetracyclic triterpene natural products (e.g. siamenoside I and mogrosides IV, V and VI). Cucurbitacins have cytotoxic properties and exhibit deterrent taste as a defense barrier against herbivores. Mogrosides are nonsugar highly oxygenated compounds used as high-intensity zero- calorie sweeteners; they also possess pharmacological properties such as regulating immunity, lowering blood sugar and lipid levels, protecting the liver, and acting as antioxidants and antitumor agents. Catalyzes the C3 primary glucosylation of mogrol, mogroside I-A1, mogroside II-A1, mogroside II-A and mogroside III-A1.",Belongs to the UDP-glycosyltransferase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0080043; GO:0080044,GO:0016757,GO:0008194,GO:0008194,GO:0008194,GO:0008194,0.5541,0.6513,0.6513,0.6513,0.6513,5,0.6319,0.2574,no
GT742_SIRGR,P0DO74,ProtTale,Eukaryota,460,"UDP-glycosyltransferase involved in the biosynthesis of cucurbitacin and mogroside tetracyclic triterpene natural products (e.g. siamenoside I and mogrosides IV, V and VI). Cucurbitacins have cytotoxic properties and exhibit deterrent taste as a defense barrier against herbivores. Mogrosides are nonsugar highly oxygenated compounds used as high-intensity zero- calorie sweeteners; they also possess pharmacological properties such as regulating immunity, lowering blood sugar and lipid levels, protecting the liver, and acting as antioxidants and antitumor agents. Catalyzes the C3 primary glucosylation of mogrol, mogroside I-A1, mogroside II-A1, mogroside II-A and mogroside III-A1.","Involved in the biosynthesis of rutin (quercetin-3-O-rutinoside), a flavonol glycoside.",Maybe,No,No,No,Maybe,not-Yes,GO:0080043; GO:0080044,,,,,,,,,,,0,,0.2574,no
GT742_SIRGR,P0DO74,Protein2Text,Eukaryota,460,"UDP-glycosyltransferase involved in the biosynthesis of cucurbitacin and mogroside tetracyclic triterpene natural products (e.g. siamenoside I and mogrosides IV, V and VI). Cucurbitacins have cytotoxic properties and exhibit deterrent taste as a defense barrier against herbivores. Mogrosides are nonsugar highly oxygenated compounds used as high-intensity zero- calorie sweeteners; they also possess pharmacological properties such as regulating immunity, lowering blood sugar and lipid levels, protecting the liver, and acting as antioxidants and antitumor agents. Catalyzes the C3 primary glucosylation of mogrol, mogroside I-A1, mogroside II-A1, mogroside II-A and mogroside III-A1.","This protein is involved in the molecular function of flavonoid 7-O-glucosyltransferase activity, which is a type of enzyme activity that catalyzes the transfer of a glucose molecule to a flavonoid molecule. This is a key step in the biosynthesis of flavonoid glycosides, which are an important class of compounds found in plants and play a variety of roles in plant development, defense, and interactions with the environment.",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0080043; GO:0080044,GO:0080043,GO:0080043,GO:0080043,GO:0080043,GO:0035251,0.9347,0.9347,0.9347,0.9347,0.9023,5,0.9282,0.2574,no
GT742_SIRGR,P0DO74,Reference,Eukaryota,460,"UDP-glycosyltransferase involved in the biosynthesis of cucurbitacin and mogroside tetracyclic triterpene natural products (e.g. siamenoside I and mogrosides IV, V and VI). Cucurbitacins have cytotoxic properties and exhibit deterrent taste as a defense barrier against herbivores. Mogrosides are nonsugar highly oxygenated compounds used as high-intensity zero- calorie sweeteners; they also possess pharmacological properties such as regulating immunity, lowering blood sugar and lipid levels, protecting the liver, and acting as antioxidants and antitumor agents. Catalyzes the C3 primary glucosylation of mogrol, mogroside I-A1, mogroside II-A1, mogroside II-A and mogroside III-A1.","UDP-glycosyltransferase involved in the biosynthesis of cucurbitacin and mogroside tetracyclic triterpene natural products (e.g. siamenoside I and mogrosides IV, V and VI). Cucurbitacins have cytotoxic properties and exhibit deterrent taste as a defense barrier against herbivores. Mogrosides are nonsugar highly oxygenated compounds used as high-intensity zero- calorie sweeteners; they also possess pharmacological properties such as regulating immunity, lowering blood sugar and lipid levels, protecting the liver, and acting as antioxidants and antitumor agents. Catalyzes the C3 primary glucosylation of mogrol, mogroside I-A1, mogroside II-A1, mogroside II-A and mogroside III-A1.",,,,,,,GO:0080043; GO:0080044,GO:0016758; GO:0005525,GO:0046527; GO:0008194,GO:0008194,GO:0035251; GO:0016757,GO:0035251,0.4885,0.7047,0.6513,0.8152,0.9023,5,0.7124,0.2574,no
GT752_SIRGR,P0DO75,ESM2Text,Eukaryota,486,"UDP-glycosyltransferase involved in the biosynthesis of cucurbitacin and mogroside tetracyclic triterpene natural products (e.g. siamenoside I and mogrosides IV, V and VI). Cucurbitacins have cytotoxic properties and exhibit deterrent taste as a defense barrier against herbivores. Mogrosides are nonsugar highly oxygenated compounds used as high-intensity zero- calorie sweeteners; they also possess pharmacological properties such as regulating immunity, lowering blood sugar and lipid levels, protecting the liver, and acting as antioxidants and antitumor agents. Catalyzes the C3 primary glucosylation of mogrol, mogroside I-A1, mogroside II-A1 and mogroside II-A.","In the presence of other necessary color factors, this glycosylation reaction allows the accumulation of anthocyanin pigments.",Vague,No,Maybe,No,Maybe,not-Yes,GO:0080043; GO:0080044,,GO:0046527,GO:0016757,,,,0.7225,0.5541,,,2,0.6383,0.3241,no
GT752_SIRGR,P0DO75,Prot2Text,Eukaryota,486,"UDP-glycosyltransferase involved in the biosynthesis of cucurbitacin and mogroside tetracyclic triterpene natural products (e.g. siamenoside I and mogrosides IV, V and VI). Cucurbitacins have cytotoxic properties and exhibit deterrent taste as a defense barrier against herbivores. Mogrosides are nonsugar highly oxygenated compounds used as high-intensity zero- calorie sweeteners; they also possess pharmacological properties such as regulating immunity, lowering blood sugar and lipid levels, protecting the liver, and acting as antioxidants and antitumor agents. Catalyzes the C3 primary glucosylation of mogrol, mogroside I-A1, mogroside II-A1 and mogroside II-A.",Beta-glucosyltransferase acting on both linear and branched forms of anthocyanidin.,Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0080043; GO:0080044,GO:0046527,GO:0047213,GO:0035251,GO:0035251,GO:0035251,0.7225,0.8041,0.9023,0.9023,0.9023,5,0.8467,0.3241,no
GT752_SIRGR,P0DO75,ProtT3,Eukaryota,486,"UDP-glycosyltransferase involved in the biosynthesis of cucurbitacin and mogroside tetracyclic triterpene natural products (e.g. siamenoside I and mogrosides IV, V and VI). Cucurbitacins have cytotoxic properties and exhibit deterrent taste as a defense barrier against herbivores. Mogrosides are nonsugar highly oxygenated compounds used as high-intensity zero- calorie sweeteners; they also possess pharmacological properties such as regulating immunity, lowering blood sugar and lipid levels, protecting the liver, and acting as antioxidants and antitumor agents. Catalyzes the C3 primary glucosylation of mogrol, mogroside I-A1, mogroside II-A1 and mogroside II-A.",Belongs to the UDP-glycosyltransferase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0080043; GO:0080044,GO:0016757,GO:0008194,GO:0008194,GO:0008194,GO:0008194,0.5541,0.6513,0.6513,0.6513,0.6513,5,0.6319,0.3241,no
GT752_SIRGR,P0DO75,ProtTale,Eukaryota,486,"UDP-glycosyltransferase involved in the biosynthesis of cucurbitacin and mogroside tetracyclic triterpene natural products (e.g. siamenoside I and mogrosides IV, V and VI). Cucurbitacins have cytotoxic properties and exhibit deterrent taste as a defense barrier against herbivores. Mogrosides are nonsugar highly oxygenated compounds used as high-intensity zero- calorie sweeteners; they also possess pharmacological properties such as regulating immunity, lowering blood sugar and lipid levels, protecting the liver, and acting as antioxidants and antitumor agents. Catalyzes the C3 primary glucosylation of mogrol, mogroside I-A1, mogroside II-A1 and mogroside II-A.",UDP-glycosyltransferase involved in the biosynthesis of cucurbitacin. Catalyzes the transfer of the 3-O-glucosyl moiety from UDP-glucosylcucurbitacin D to cucurbitacin D to produce glucosylcucurbitacin D. Glucosylcucurbitacin D is then converted to glucosylcucurbitacin E by the action of a 3-O-glucosylcucurbitacin D 3-O-glucosylcucurbitacin D 3-O-glucosylcucurbitacin D 3-O-,Yes,Yes,Yes,Yes,Yes,Yes,GO:0080043; GO:0080044,GO:0008194,GO:0016758,GO:0008194,GO:0016758,GO:0035251,0.6513,0.6361,0.6513,0.6361,0.9023,5,0.6954,0.3241,no
GT752_SIRGR,P0DO75,Protein2Text,Eukaryota,486,"UDP-glycosyltransferase involved in the biosynthesis of cucurbitacin and mogroside tetracyclic triterpene natural products (e.g. siamenoside I and mogrosides IV, V and VI). Cucurbitacins have cytotoxic properties and exhibit deterrent taste as a defense barrier against herbivores. Mogrosides are nonsugar highly oxygenated compounds used as high-intensity zero- calorie sweeteners; they also possess pharmacological properties such as regulating immunity, lowering blood sugar and lipid levels, protecting the liver, and acting as antioxidants and antitumor agents. Catalyzes the C3 primary glucosylation of mogrol, mogroside I-A1, mogroside II-A1 and mogroside II-A.","This protein is involved in the glycosylation process. It is a glycosyltransferase that catalyzes the transfer of a sugar molecule from a donor molecule to a growing carbohydrate chain, playing a crucial role in the biosynthesis of glycosylated compounds. In this case, it is specifically involved in the synthesis of glycosylated compounds, likely glycosides or glycosylated flavonoids.",Vague,Maybe,Maybe,Maybe,Vague,not-Yes,GO:0080043; GO:0080044,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.5541,0.5541,0.5541,0.5541,0.5541,5,0.5541,0.3241,no
GT752_SIRGR,P0DO75,Reference,Eukaryota,486,"UDP-glycosyltransferase involved in the biosynthesis of cucurbitacin and mogroside tetracyclic triterpene natural products (e.g. siamenoside I and mogrosides IV, V and VI). Cucurbitacins have cytotoxic properties and exhibit deterrent taste as a defense barrier against herbivores. Mogrosides are nonsugar highly oxygenated compounds used as high-intensity zero- calorie sweeteners; they also possess pharmacological properties such as regulating immunity, lowering blood sugar and lipid levels, protecting the liver, and acting as antioxidants and antitumor agents. Catalyzes the C3 primary glucosylation of mogrol, mogroside I-A1, mogroside II-A1 and mogroside II-A.","UDP-glycosyltransferase involved in the biosynthesis of cucurbitacin and mogroside tetracyclic triterpene natural products (e.g. siamenoside I and mogrosides IV, V and VI). Cucurbitacins have cytotoxic properties and exhibit deterrent taste as a defense barrier against herbivores. Mogrosides are nonsugar highly oxygenated compounds used as high-intensity zero- calorie sweeteners; they also possess pharmacological properties such as regulating immunity, lowering blood sugar and lipid levels, protecting the liver, and acting as antioxidants and antitumor agents. Catalyzes the C3 primary glucosylation of mogrol, mogroside I-A1, mogroside II-A1 and mogroside II-A.",,,,,,,GO:0080043; GO:0080044,GO:0016758; GO:0005525,GO:0046527; GO:0008194,GO:0008194,GO:0035251,GO:0035251,0.4885,0.7047,0.6513,0.9023,0.9023,5,0.7298,0.3241,no
RGYR2_SULAC,P0DW67,ESM2Text,Archaea,1153,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process, increasing the linking number in steps of +1. Binds to single-stranded DNA, transiently cleaves and then rejoins the ends, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)- enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair and/or for DNA protection.",Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. It cleaves transiently a single DNA strand and remains covalently bound to the 5' DNA end through a tyrosine residue. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0003677; GO:0160097; GO:0008270,GO:0003916; GO:0005524,GO:0003918,GO:0003916; GO:0005524,GO:0003916; GO:0005524,GO:0003916; GO:0005524,0.7009,0.3316,0.7009,0.7009,0.7009,5,0.627,0.6104,yes
RGYR2_SULAC,P0DW67,Prot2Text,Archaea,1153,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process, increasing the linking number in steps of +1. Binds to single-stranded DNA, transiently cleaves and then rejoins the ends, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)- enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair and/or for DNA protection.",Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. It cleaves transiently a single DNA strand and remains covalently bound to the 5' DNA end through a tyrosine residue. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0003677; GO:0160097; GO:0008270,GO:0003916,GO:0003916,GO:0003916; GO:0005524,GO:0003918,GO:0003918,0.4085,0.4085,0.7009,0.3316,0.3316,5,0.4362,0.6104,yes
RGYR2_SULAC,P0DW67,ProtT3,Archaea,1153,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process, increasing the linking number in steps of +1. Binds to single-stranded DNA, transiently cleaves and then rejoins the ends, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)- enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair and/or for DNA protection.","Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally",Maybe,Maybe,Yes,Yes,Yes,Yes,GO:0005524; GO:0003677; GO:0160097; GO:0008270,GO:0003917,GO:0003917,GO:0003917,GO:0003917,GO:0003917,0.3657,0.3657,0.3657,0.3657,0.3657,5,0.3657,0.6104,yes
RGYR2_SULAC,P0DW67,ProtTale,Archaea,1153,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process, increasing the linking number in steps of +1. Binds to single-stranded DNA, transiently cleaves and then rejoins the ends, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)- enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair and/or for DNA protection.",Involved in DNA replication. May be part of the MCM2-7 complex that functions as the DNA helicase of the replicative helicase that is the major mechanism by which DNA is replicated. Has ATPase activity. May play a role in DNA repair.,Vague,No,No,No,Vague,not-Yes,GO:0005524; GO:0003677; GO:0160097; GO:0008270,GO:0016887; GO:0003678,GO:0005524; GO:0016887; GO:0004386,GO:0005524; GO:0016887; GO:0004386,GO:0005524; GO:0016887,GO:0003678; GO:0016887,0.2647,0.5391,0.5391,0.4471,0.2647,5,0.4109,0.6104,yes
RGYR2_SULAC,P0DW67,Protein2Text,Archaea,1153,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process, increasing the linking number in steps of +1. Binds to single-stranded DNA, transiently cleaves and then rejoins the ends, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)- enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair and/or for DNA protection.",The molecular function of this protein is an ATP-dependent DNA helicase. It is involved in DNA replication and repair.,No,No,No,Maybe,No,not-Yes,GO:0005524; GO:0003677; GO:0160097; GO:0008270,GO:0004003; GO:0005524,GO:0004003; GO:0005524,GO:0004003; GO:0005524,GO:0004003; GO:0005524,GO:0004003,0.5965,0.5965,0.5965,0.5965,0.2811,5,0.5334,0.6104,yes
RGYR2_SULAC,P0DW67,Reference,Archaea,1153,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process, increasing the linking number in steps of +1. Binds to single-stranded DNA, transiently cleaves and then rejoins the ends, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)- enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair and/or for DNA protection.","Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process, increasing the linking number in steps of +1. Binds to single-stranded DNA, transiently cleaves and then rejoins the ends, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)- enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair and/or for DNA protection.",,,,,,,GO:0005524; GO:0003677; GO:0160097; GO:0008270,GO:0003916; GO:0003917; GO:0005524,GO:0003916; GO:0005524; GO:0003697,GO:0003916; GO:0005524,GO:0003918; GO:0003677; GO:0005524,GO:0003916; GO:0005524,0.7164,0.8176,0.7009,0.8089,0.7009,5,0.7489,0.6104,yes
DTCC_VIBAL,P0DW70,ESM2Text,Bacteria,387,"Probable response protein of the two-component regulatory system Detocs that confers resistance to bacteriophage. When the system (DtcA-DtcB-DtcC) is expressed in a susceptible E.coli (strain MG1655) it confers resistance to bacteriophages T2, T4, T5, T6 and SECphi27. Detocs inhibits T5 infection leading to growth arrest but not complete cell lysis, during SECphi27 infection leads to cell lysis. DtcA probably autophosphorylates upon sensing viral infection, and subsequently transfers the phosphate signal to DtcC (this subunit) which activates it, leading to an antiviral defense; DtcB may scavenge phosphorylation signals from accidental activation of DtcA (Probable). Cleaves the N-glycosidic bond of ATP, and to a lesser extent dATP, to release adenine and a sugar triphosphate; has no activity on other (d)NTPs. In vivo during phage infection has pleoitropic effects on nucleotide accumulation.","Regulates flagellar function by binding to the motile catecholam antibiotic flaA. Recognizes and binds the flagellar adhesin, catalyzing the cleavage of the N-glycosidic bond in the outer membrane domain, leading to the activation of the flagellar regulators flaA and flaB. Also functions as a deoxyribonuclease (RNase) and deoxyribonuclease (RNase) that are directly involved in the degradation of the RNase operon flaA. In turn, flaB is deoxyribonuclease-like to protect cells against the toxic effects of OCl 2,3-dicarboxypropionic acid (CPD) and O(2)O(2).",No,No,No,No,No,not-Yes,GO:0008782; GO:0008930,,,,,,,,,,,0,,0.5072,no
DTCC_VIBAL,P0DW70,Prot2Text,Bacteria,387,"Probable response protein of the two-component regulatory system Detocs that confers resistance to bacteriophage. When the system (DtcA-DtcB-DtcC) is expressed in a susceptible E.coli (strain MG1655) it confers resistance to bacteriophages T2, T4, T5, T6 and SECphi27. Detocs inhibits T5 infection leading to growth arrest but not complete cell lysis, during SECphi27 infection leads to cell lysis. DtcA probably autophosphorylates upon sensing viral infection, and subsequently transfers the phosphate signal to DtcC (this subunit) which activates it, leading to an antiviral defense; DtcB may scavenge phosphorylation signals from accidental activation of DtcA (Probable). Cleaves the N-glycosidic bond of ATP, and to a lesser extent dATP, to release adenine and a sugar triphosphate; has no activity on other (d)NTPs. In vivo during phage infection has pleoitropic effects on nucleotide accumulation.","Catalyzes the deamidation of nicotinamide, an early step in the NAD(+) salvage pathway. Prevents the accumulation of intracellular nicotinamide, a known inhibitor of poly(ADP-ribose) polymerases (PARP enzymes).",No,No,No,No,No,not-Yes,GO:0008782; GO:0008930,GO:0008936,GO:0019159,GO:0008936,GO:0008936,GO:0008936,0.2805,0.3239,0.2805,0.2805,0.2805,5,0.2892,0.5072,no
DTCC_VIBAL,P0DW70,ProtT3,Bacteria,387,"Probable response protein of the two-component regulatory system Detocs that confers resistance to bacteriophage. When the system (DtcA-DtcB-DtcC) is expressed in a susceptible E.coli (strain MG1655) it confers resistance to bacteriophages T2, T4, T5, T6 and SECphi27. Detocs inhibits T5 infection leading to growth arrest but not complete cell lysis, during SECphi27 infection leads to cell lysis. DtcA probably autophosphorylates upon sensing viral infection, and subsequently transfers the phosphate signal to DtcC (this subunit) which activates it, leading to an antiviral defense; DtcB may scavenge phosphorylation signals from accidental activation of DtcA (Probable). Cleaves the N-glycosidic bond of ATP, and to a lesser extent dATP, to release adenine and a sugar triphosphate; has no activity on other (d)NTPs. In vivo during phage infection has pleoitropic effects on nucleotide accumulation.",Catalyzes the hydrolysis of adenosine 5'-monophosphoramidate (AMP-NH2) to yield adenosine 5'-monophosphate (AMP) and NH3. Belongs to the Nudix hydrolase family,No,No,No,No,No,not-Yes,GO:0008782; GO:0008930,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016787,0.5807,0.5807,0.5807,0.5807,0.5807,5,0.5807,0.5072,no
DTCC_VIBAL,P0DW70,ProtTale,Bacteria,387,"Probable response protein of the two-component regulatory system Detocs that confers resistance to bacteriophage. When the system (DtcA-DtcB-DtcC) is expressed in a susceptible E.coli (strain MG1655) it confers resistance to bacteriophages T2, T4, T5, T6 and SECphi27. Detocs inhibits T5 infection leading to growth arrest but not complete cell lysis, during SECphi27 infection leads to cell lysis. DtcA probably autophosphorylates upon sensing viral infection, and subsequently transfers the phosphate signal to DtcC (this subunit) which activates it, leading to an antiviral defense; DtcB may scavenge phosphorylation signals from accidental activation of DtcA (Probable). Cleaves the N-glycosidic bond of ATP, and to a lesser extent dATP, to release adenine and a sugar triphosphate; has no activity on other (d)NTPs. In vivo during phage infection has pleoitropic effects on nucleotide accumulation.",Pyrimidine phosphoribosyltransferase that regulates the balance between pyrimidine biosynthesis and catabolism by regulating the turnover of UTP. May act as a sensor of intracellular UTP levels.,No,No,No,No,No,not-Yes,GO:0008782; GO:0008930,GO:0004845,GO:0004845,GO:0004845,GO:0004845,GO:0004845,0.1911,0.1911,0.1911,0.1911,0.1911,5,0.1911,0.5072,no
DTCC_VIBAL,P0DW70,Protein2Text,Bacteria,387,"Probable response protein of the two-component regulatory system Detocs that confers resistance to bacteriophage. When the system (DtcA-DtcB-DtcC) is expressed in a susceptible E.coli (strain MG1655) it confers resistance to bacteriophages T2, T4, T5, T6 and SECphi27. Detocs inhibits T5 infection leading to growth arrest but not complete cell lysis, during SECphi27 infection leads to cell lysis. DtcA probably autophosphorylates upon sensing viral infection, and subsequently transfers the phosphate signal to DtcC (this subunit) which activates it, leading to an antiviral defense; DtcB may scavenge phosphorylation signals from accidental activation of DtcA (Probable). Cleaves the N-glycosidic bond of ATP, and to a lesser extent dATP, to release adenine and a sugar triphosphate; has no activity on other (d)NTPs. In vivo during phage infection has pleoitropic effects on nucleotide accumulation.",The molecular function of this protein is an endonuclease that catalyzes the hydrolysis of nucleic acids.,No,No,No,No,No,not-Yes,GO:0008782; GO:0008930,GO:0004519,GO:0004519,GO:0004519,GO:0004519,GO:0004519,0.2257,0.2257,0.2257,0.2257,0.2257,5,0.2257,0.5072,no
DTCC_VIBAL,P0DW70,Reference,Bacteria,387,"Probable response protein of the two-component regulatory system Detocs that confers resistance to bacteriophage. When the system (DtcA-DtcB-DtcC) is expressed in a susceptible E.coli (strain MG1655) it confers resistance to bacteriophages T2, T4, T5, T6 and SECphi27. Detocs inhibits T5 infection leading to growth arrest but not complete cell lysis, during SECphi27 infection leads to cell lysis. DtcA probably autophosphorylates upon sensing viral infection, and subsequently transfers the phosphate signal to DtcC (this subunit) which activates it, leading to an antiviral defense; DtcB may scavenge phosphorylation signals from accidental activation of DtcA (Probable). Cleaves the N-glycosidic bond of ATP, and to a lesser extent dATP, to release adenine and a sugar triphosphate; has no activity on other (d)NTPs. In vivo during phage infection has pleoitropic effects on nucleotide accumulation.","Probable response protein of the two-component regulatory system Detocs that confers resistance to bacteriophage. When the system (DtcA-DtcB-DtcC) is expressed in a susceptible E.coli (strain MG1655) it confers resistance to bacteriophages T2, T4, T5, T6 and SECphi27. Detocs inhibits T5 infection leading to growth arrest but not complete cell lysis, during SECphi27 infection leads to cell lysis. DtcA probably autophosphorylates upon sensing viral infection, and subsequently transfers the phosphate signal to DtcC (this subunit) which activates it, leading to an antiviral defense; DtcB may scavenge phosphorylation signals from accidental activation of DtcA (Probable). Cleaves the N-glycosidic bond of ATP, and to a lesser extent dATP, to release adenine and a sugar triphosphate; has no activity on other (d)NTPs. In vivo during phage infection has pleoitropic effects on nucleotide accumulation.",,,,,,,GO:0008782; GO:0008930,GO:0017111; GO:0047405,GO:0016799,GO:0016799,GO:0016799,GO:0004731,0.5964,0.8234,0.8234,0.8234,0.1911,5,0.6515,0.5072,no
CLAER_LACPN,P0DX42,ESM2Text,Bacteria,217,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-ER catalyzes the saturation of the carbon-carbon double bond in 10-oxo-(11E)-octadecenoate to produce 10-oxooctadecanoate, during linoleate metabolism. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome.","(Microbial infection) The NELF complex catalyzes the reduction of the eukaryotic respiratory membrane (H(2)O(2)) to an equivalent level of reduced eukaryotic membrane (H(2)O(3)). It supplies electrons for reduction enzymatic enzymes. The nELF complex can also reduce a variety of other membrane analogs, including polychlorinated biphenyls (PCB) and trichlorinated derivatives.",No,No,No,No,No,not-Yes,GO:0000166; GO:0016491,,,,,,,,,,,0,,0.1755,no
CLAER_LACPN,P0DX42,Prot2Text,Bacteria,217,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-ER catalyzes the saturation of the carbon-carbon double bond in 10-oxo-(11E)-octadecenoate to produce 10-oxooctadecanoate, during linoleate metabolism. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome.",Reduction of a variety of nitroaromatic compounds using NADH (and to lesser extent NADPH) as source of reducing equivalents; two electrons are transferred.,No,No,No,No,No,not-Yes,GO:0000166; GO:0016491,GO:0016491,GO:0008726,GO:0003955,GO:0016657,GO:0003955,0.7229,0.3954,0.4359,0.0,0.4359,5,0.398,0.1755,no
CLAER_LACPN,P0DX42,ProtT3,Bacteria,217,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-ER catalyzes the saturation of the carbon-carbon double bond in 10-oxo-(11E)-octadecenoate to produce 10-oxooctadecanoate, during linoleate metabolism. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome.",Catalyzes the reduction of nitroaromatic compounds using NADH or NADPH as the electron donor. Belongs to the nitroreductase family,No,No,Vague,Vague,No,not-Yes,GO:0000166; GO:0016491,GO:0016657,GO:0016657,GO:0016657,GO:0016657,GO:0016657,0.0,0.0,0.0,0.0,0.0,5,0.0,0.1755,no
CLAER_LACPN,P0DX42,ProtTale,Bacteria,217,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-ER catalyzes the saturation of the carbon-carbon double bond in 10-oxo-(11E)-octadecenoate to produce 10-oxooctadecanoate, during linoleate metabolism. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome.","Involved in the reduction of nitroaromatic compounds. Component of a two-enzyme system that catalyzes the oxidation of nitroaromatic compounds such as 2,4,6-trinitrophenol (2,4,6-TNP) and 2,4-dinitrophenol (2,4-DNP) to the corresponding nitroaromatic acids, i.e. 2,4,6-trinitrotoluene (TNT) and 2,4-dinitrophenol (DNP) to nitroprusside. The nitroreductases AcnB and Ac",No,No,No,No,No,not-Yes,GO:0000166; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016657,0.7229,0.7229,0.7229,0.7229,0.0,5,0.5783,0.1755,no
CLAER_LACPN,P0DX42,Protein2Text,Bacteria,217,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-ER catalyzes the saturation of the carbon-carbon double bond in 10-oxo-(11E)-octadecenoate to produce 10-oxooctadecanoate, during linoleate metabolism. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome.","The molecular function of this protein is not explicitly stated in the provided snippet. However, based on its classification as an enzyme, it is likely that this protein is involved in a metabolic or catalytic process, possibly as a component of a metabolic pathway. 

If you have any more information or context about this protein, I may be able to provide a more specific answer.",Vague,No,Vague,Vague,Vague,not-Yes,GO:0000166; GO:0016491,,,,,,,,,,,0,,0.1755,no
CLAER_LACPN,P0DX42,Reference,Bacteria,217,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-ER catalyzes the saturation of the carbon-carbon double bond in 10-oxo-(11E)-octadecenoate to produce 10-oxooctadecanoate, during linoleate metabolism. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome.","Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-ER catalyzes the saturation of the carbon-carbon double bond in 10-oxo-(11E)-octadecenoate to produce 10-oxooctadecanoate, during linoleate metabolism. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome.",,,,,,,GO:0000166; GO:0016491,GO:0016627,GO:0016628,GO:0016491,GO:0016491,GO:0016627,0.5895,0.4994,0.7229,0.7229,0.5895,5,0.6248,0.1755,no
CDNE_YERAE,P0DXA5,ESM2Text,Bacteria,379,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The effector protein for this system is membrane protein Cap15. A type I-B(UU) CBASS system.","Cyclic dinucleotide synthase that catalyzes the synthesis of c-di-GMP, has no activity with other NTP substrates.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0046872; GO:0016779,GO:0052621,GO:0052621,GO:0052929,GO:0052621,GO:0052621,0.4652,0.4652,0.3293,0.4652,0.4652,5,0.438,0.5865,yes
CDNE_YERAE,P0DXA5,Prot2Text,Bacteria,379,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The effector protein for this system is membrane protein Cap15. A type I-B(UU) CBASS system.","Cyclic dinucleotide synthase that catalyzes the synthesis of c-di-GMP, has no activity with other NTP substrates.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0046872; GO:0016779,GO:0052621,GO:0052621,GO:0052621,GO:0052621,GO:0052621,0.4652,0.4652,0.4652,0.4652,0.4652,5,0.4652,0.5865,yes
CDNE_YERAE,P0DXA5,ProtT3,Bacteria,379,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The effector protein for this system is membrane protein Cap15. A type I-B(UU) CBASS system.","CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). This CBASS (cyclic oligonucleotide-based antiphage defense system) provides immunity against type I-E CRISPR-Cas systems (By similarity). This CBASS (cyclic oligonucleotide-based antiphage defense system)",Vague,No,Maybe,Maybe,No,not-Yes,GO:0005524; GO:0046872; GO:0016779,,,,,,,,,,,0,,0.5865,yes
CDNE_YERAE,P0DXA5,ProtTale,Bacteria,379,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The effector protein for this system is membrane protein Cap15. A type I-B(UU) CBASS system.","Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type I-D(GG) CBASS system.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0046872; GO:0016779,GO:0016779,GO:0009975,GO:0016779,GO:0016779,GO:0016779,0.542,0.2648,0.542,0.542,0.542,5,0.4866,0.5865,yes
CDNE_YERAE,P0DXA5,Protein2Text,Bacteria,379,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The effector protein for this system is membrane protein Cap15. A type I-B(UU) CBASS system.","The molecular function of this protein is to catalyze the cleavage of DNA. It is a restriction enzyme, which is a type of endonuclease that cleaves DNA at specific recognition sites. This protein is likely involved in the defense mechanism of the organism, protecting it against foreign DNA by cutting it into smaller pieces. 
This protein is also a type of endonuclease, specifically a deoxyribonuclease, which is an enzyme that cleaves DNA. It is likely involved in the degradation of DNA, possibly as part of a DNA repair pathway. 

This protein is also involved in the initiation of viral DNA replication, where it catalyzes the cleavage of the viral DNA to form a circular intermediate. This is an important step in the viral life cycle, allowing the virus to replicate its genome. 

This protein is also involved in the replication of plasmids, where it catalyzes the cleavage of the plasmid DNA to form a circular intermediate. This is an important step in the replication of plasmids, allowing them to be replicated and inherited by daughter cells. 

This protein is also involved in the defense mechanism of the organism, protecting it against foreign DNA by cutting it into smaller pieces. This is an important step in the defense mechanism, allowing the organism to protect itself against invading DNA. 

This protein is also involved in the degradation of DNA, possibly as part of a DNA repair pathway. This is an important step in maintaining the integrity of the genome, allowing the organism to repair damaged DNA and maintain its genetic material. 

This protein is also involved in the regulation of gene expression, possibly by controlling the transcription of specific genes. This is an important step in regulating gene expression, allowing the organism to control the expression of specific genes and adapt to changing environments. 

This protein is also involved in the regulation of cell growth and division, possibly by controlling the expression of specific genes involved in cell growth and division. This is an important step in regulating cell growth and division, allowing the organism to control its growth and division and adapt to changing environments. 

This protein is also involved in the regulation of cell death, possibly by controlling the expression of specific genes involved in cell death. This is an important step in regulating cell death, allowing the organism to control its cell death and adapt to changing environments. 

This protein is also involved in the regulation of cell differentiation, possibly by controlling the expression of specific genes involved in cell differentiation. This is an important step in regulating cell differentiation, allowing the organism",No,No,No,No,No,not-Yes,GO:0005524; GO:0046872; GO:0016779,GO:0004519,GO:0004519,GO:0004519,GO:0004519,GO:0004519,0.179,0.179,0.179,0.179,0.179,5,0.179,0.5865,yes
CDNE_YERAE,P0DXA5,Reference,Bacteria,379,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The effector protein for this system is membrane protein Cap15. A type I-B(UU) CBASS system.","Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. The effector protein for this system is membrane protein Cap15. A type I-B(UU) CBASS system.",,,,,,,GO:0005524; GO:0046872; GO:0016779,GO:0061501,GO:0009975,GO:0016779,GO:0016779,GO:0016779,0.4086,0.2648,0.542,0.542,0.542,5,0.4599,0.5865,yes
CHCC1_SINCY,P0DXE2,ESM2Text,Bacteria,574,Desaturase involved in a cyclohexanecarboxylate (CHCA) degradation pathway. Catalyzes the conversion of 4-oxocyclohexanecarboxylate (4-oxoCHCA) to 4- oxocyclohexenecarboxylate. Is highly specific for 4-oxocyclohexanecarboxylic acid and shows only slight activity with 4-oxo-2-methylcyclohex-2-enecarboxylic acid.,"Catalyzes the elimination of the C-1 and C-2 hydrogen atoms of the A-ring from the polycyclic ring structure of 3-ketosteroids. In vitro, the A-ring of 3-ketosteroids A, B and C are the preferred substrates, but O-ring of A,B,C and D may also be used, although at a lower rate.",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0033765,GO:0016491,GO:0016627,GO:0016491,GO:0016491,,0.6062,0.747,0.6062,0.6062,,4,0.6414,0.2262,no
CHCC1_SINCY,P0DXE2,Prot2Text,Bacteria,574,Desaturase involved in a cyclohexanecarboxylate (CHCA) degradation pathway. Catalyzes the conversion of 4-oxocyclohexanecarboxylate (4-oxoCHCA) to 4- oxocyclohexenecarboxylate. Is highly specific for 4-oxocyclohexanecarboxylic acid and shows only slight activity with 4-oxo-2-methylcyclohex-2-enecarboxylic acid.,Able to catalyze the elimination of the C-1 and C-2 hydrogen atoms of the A-ring from the polycyclic ring structure of 3-ketosteroids.,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0033765,,,GO:0016627,GO:0016491,GO:0047560,,,0.747,0.6062,0.358,3,0.5704,0.2262,no
CHCC1_SINCY,P0DXE2,ProtT3,Bacteria,574,Desaturase involved in a cyclohexanecarboxylate (CHCA) degradation pathway. Catalyzes the conversion of 4-oxocyclohexanecarboxylate (4-oxoCHCA) to 4- oxocyclohexenecarboxylate. Is highly specific for 4-oxocyclohexanecarboxylic acid and shows only slight activity with 4-oxo-2-methylcyclohex-2-enecarboxylic acid.,Catalyzes the NAD(+)-dependent dehydrogenation of (S)-2-hydroxyglutarate (2-HG) to 2-oxoglutarate (2-OG). Belongs to the FAD-dependent oxidoreductase 2 family. 2-hydroxyglutarate dehydrogenase subfamily,No,No,No,No,No,not-Yes,GO:0033765,GO:0047545,GO:0016616,GO:0016616,GO:0047545,GO:0047545,0.4151,0.4151,0.4151,0.4151,0.4151,5,0.4151,0.2262,no
CHCC1_SINCY,P0DXE2,ProtTale,Bacteria,574,Desaturase involved in a cyclohexanecarboxylate (CHCA) degradation pathway. Catalyzes the conversion of 4-oxocyclohexanecarboxylate (4-oxoCHCA) to 4- oxocyclohexenecarboxylate. Is highly specific for 4-oxocyclohexanecarboxylic acid and shows only slight activity with 4-oxo-2-methylcyclohex-2-enecarboxylic acid.,"Involved in the degradation of 3,5-dihydroxybenzoate (3,5-DHB). Catalyzes the dehydrogenation of 3,5-DHB to 3,4-dihydroxybenzoate (3,4-DHB).",Maybe,No,No,No,No,not-Yes,GO:0033765,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.6062,0.6062,0.6062,0.6062,0.6062,5,0.6062,0.2262,no
CHCC1_SINCY,P0DXE2,Protein2Text,Bacteria,574,Desaturase involved in a cyclohexanecarboxylate (CHCA) degradation pathway. Catalyzes the conversion of 4-oxocyclohexanecarboxylate (4-oxoCHCA) to 4- oxocyclohexenecarboxylate. Is highly specific for 4-oxocyclohexanecarboxylic acid and shows only slight activity with 4-oxo-2-methylcyclohex-2-enecarboxylic acid.,The molecular function of this protein is a short-chain dehydrogenase/reductase. It is involved in the oxidation of short-chain alcohols.,Vague,No,No,No,Vague,not-Yes,GO:0033765,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.6062,0.6062,0.6062,0.6062,0.6062,5,0.6062,0.2262,no
CHCC1_SINCY,P0DXE2,Reference,Bacteria,574,Desaturase involved in a cyclohexanecarboxylate (CHCA) degradation pathway. Catalyzes the conversion of 4-oxocyclohexanecarboxylate (4-oxoCHCA) to 4- oxocyclohexenecarboxylate. Is highly specific for 4-oxocyclohexanecarboxylic acid and shows only slight activity with 4-oxo-2-methylcyclohex-2-enecarboxylic acid.,Desaturase involved in a cyclohexanecarboxylate (CHCA) degradation pathway. Catalyzes the conversion of 4-oxocyclohexanecarboxylate (4-oxoCHCA) to 4- oxocyclohexenecarboxylate. Is highly specific for 4-oxocyclohexanecarboxylic acid and shows only slight activity with 4-oxo-2-methylcyclohex-2-enecarboxylic acid.,,,,,,,GO:0033765,GO:0016491,GO:0016627,GO:0016491,GO:0016627,GO:0016491,0.6062,0.747,0.6062,0.747,0.6062,5,0.6625,0.2262,no
CGDB_MICSX,P0DXE6,ESM2Text,Bacteria,132,"Carbon-carbon bond-cleaving enzyme which participates in a carminate degradation pathway. Cleaves the C-C bond in 3'-dehydrocarminate to form kermesate. Also shows weak activity with other C-glycosides, such as 3''-dehydropuerarin (3''-oxo-puerarin), 3''-dehydroisoorientin (3''-oxo-homoorientin) and 3'-dehydromangiferin (3'-oxo-mangiferin).",Required for optimal acid stress protection. Exhibits a chaperone-like activity only at low pH by suppressing non-specifically the aggregation of denaturated periplasmic proteins.,No,No,No,No,No,not-Yes,GO:0016829,,,,,,,,,,,0,,0.3315,no
CGDB_MICSX,P0DXE6,Prot2Text,Bacteria,132,"Carbon-carbon bond-cleaving enzyme which participates in a carminate degradation pathway. Cleaves the C-C bond in 3'-dehydrocarminate to form kermesate. Also shows weak activity with other C-glycosides, such as 3''-dehydropuerarin (3''-oxo-puerarin), 3''-dehydroisoorientin (3''-oxo-homoorientin) and 3'-dehydromangiferin (3'-oxo-mangiferin).","DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively.",No,No,No,No,No,not-Yes,GO:0016829,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.2657,0.2657,0.2657,0.2657,0.2657,5,0.2657,0.3315,no
CGDB_MICSX,P0DXE6,ProtT3,Bacteria,132,"Carbon-carbon bond-cleaving enzyme which participates in a carminate degradation pathway. Cleaves the C-C bond in 3'-dehydrocarminate to form kermesate. Also shows weak activity with other C-glycosides, such as 3''-dehydropuerarin (3''-oxo-puerarin), 3''-dehydroisoorientin (3''-oxo-homoorientin) and 3'-dehydromangiferin (3'-oxo-mangiferin).",To H.influenzae HI_0588,Vague,No,Vague,No,Vague,not-Yes,GO:0016829,,,,,,,,,,,0,,0.3315,no
CGDB_MICSX,P0DXE6,ProtTale,Bacteria,132,"Carbon-carbon bond-cleaving enzyme which participates in a carminate degradation pathway. Cleaves the C-C bond in 3'-dehydrocarminate to form kermesate. Also shows weak activity with other C-glycosides, such as 3''-dehydropuerarin (3''-oxo-puerarin), 3''-dehydroisoorientin (3''-oxo-homoorientin) and 3'-dehydromangiferin (3'-oxo-mangiferin).","Toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion. Protection is provided by the cognate immunity protein Tsi5 (Probable). When expressed in E.coli (strain MG1655) inhibits growth of E.coli (strain MG1655), but not of E.coli (strain MG1655) or E.coli (strain MG1655)",No,No,No,No,No,not-Yes,GO:0016829,,,,,,,,,,,0,,0.3315,no
CGDB_MICSX,P0DXE6,Protein2Text,Bacteria,132,"Carbon-carbon bond-cleaving enzyme which participates in a carminate degradation pathway. Cleaves the C-C bond in 3'-dehydrocarminate to form kermesate. Also shows weak activity with other C-glycosides, such as 3''-dehydropuerarin (3''-oxo-puerarin), 3''-dehydroisoorientin (3''-oxo-homoorientin) and 3'-dehydromangiferin (3'-oxo-mangiferin).","This protein is a part of the apolipoprotein A-I, which plays a crucial role in lipid metabolism. The molecular function of this protein is to bind to lipids, specifically apolipoprotein A-I, and facilitate their transport in the bloodstream. More specifically, it is involved in the regulation of lipid metabolism and may play a role in maintaining healthy cholesterol levels in the blood. Additionally, it has been implicated in the modulation of inflammation and may have antioxidant properties. However, more research is needed to fully understand its molecular function and its role in human health. 

Please note that the information provided is based on general knowledge and may not be specific to this protein. If you are looking for detailed information on this protein, I recommend consulting a reliable scientific source or a database such as UniProt or PubMed. 

Also, the molecular function of a protein can be described in different ways, such as binding, catalysis, regulation, or transport. If you would like more information on the molecular function of this protein, please let me know and I can try to provide more details.",No,No,No,No,No,not-Yes,GO:0016829,,GO:0008289,GO:0008289,GO:0008289,GO:0008289,,0.2623,0.2623,0.2623,0.2623,4,0.2623,0.3315,no
CGDB_MICSX,P0DXE6,Reference,Bacteria,132,"Carbon-carbon bond-cleaving enzyme which participates in a carminate degradation pathway. Cleaves the C-C bond in 3'-dehydrocarminate to form kermesate. Also shows weak activity with other C-glycosides, such as 3''-dehydropuerarin (3''-oxo-puerarin), 3''-dehydroisoorientin (3''-oxo-homoorientin) and 3'-dehydromangiferin (3'-oxo-mangiferin).","Carbon-carbon bond-cleaving enzyme which participates in a carminate degradation pathway. Cleaves the C-C bond in 3'-dehydrocarminate to form kermesate. Also shows weak activity with other C-glycosides, such as 3''-dehydropuerarin (3''-oxo-puerarin), 3''-dehydroisoorientin (3''-oxo-homoorientin) and 3'-dehydromangiferin (3'-oxo-mangiferin).",,,,,,,GO:0016829,GO:0016830,GO:0016830,GO:0016829,GO:0016830,GO:0016829,0.8145,0.8145,1.0,0.8145,1.0,5,0.8887,0.3315,no
PA2_XYLAR,P0DXZ6,ESM2Text,Eukaryota,179,"May potentiate Xylotoxin(1)-Xa1a DRG activation and cell lysis, since the orthologous A.mellifera PA2 potentiates Xylotoxin(1)- Xa1a DRG activation and cell lysis. In vivo, intraplantar injection in mice may potentiate spontaneous pain behaviors and paw swelling caused by Xylotoxin(1)-Xa1a, since the orthologous A.mellifera PA2 shows this effect. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (Probable).",PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0004623; GO:0090729,GO:0004623,GO:0004623,GO:0004623,GO:0004623; GO:0005509,GO:0004623; GO:0005509,0.5554,0.5554,0.5554,0.7846,0.7846,5,0.6471,0.3964,no
PA2_XYLAR,P0DXZ6,Prot2Text,Eukaryota,179,"May potentiate Xylotoxin(1)-Xa1a DRG activation and cell lysis, since the orthologous A.mellifera PA2 potentiates Xylotoxin(1)- Xa1a DRG activation and cell lysis. In vivo, intraplantar injection in mice may potentiate spontaneous pain behaviors and paw swelling caused by Xylotoxin(1)-Xa1a, since the orthologous A.mellifera PA2 shows this effect. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (Probable).",PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0004623; GO:0090729,GO:0004623,GO:0004623,GO:0004623; GO:0005509,GO:0004623,GO:0004623,0.5554,0.5554,0.7846,0.5554,0.5554,5,0.6012,0.3964,no
PA2_XYLAR,P0DXZ6,ProtT3,Eukaryota,179,"May potentiate Xylotoxin(1)-Xa1a DRG activation and cell lysis, since the orthologous A.mellifera PA2 potentiates Xylotoxin(1)- Xa1a DRG activation and cell lysis. In vivo, intraplantar injection in mice may potentiate spontaneous pain behaviors and paw swelling caused by Xylotoxin(1)-Xa1a, since the orthologous A.mellifera PA2 shows this effect. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (Probable).",PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Secreted. Belongs to the phospholipase A2 family. Group II subfamily,Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0004623; GO:0090729,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623; GO:0005509,0.7846,0.7846,0.7846,0.7846,0.7846,5,0.7846,0.3964,no
PA2_XYLAR,P0DXZ6,ProtTale,Eukaryota,179,"May potentiate Xylotoxin(1)-Xa1a DRG activation and cell lysis, since the orthologous A.mellifera PA2 potentiates Xylotoxin(1)- Xa1a DRG activation and cell lysis. In vivo, intraplantar injection in mice may potentiate spontaneous pain behaviors and paw swelling caused by Xylotoxin(1)-Xa1a, since the orthologous A.mellifera PA2 shows this effect. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (Probable).",PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0004623; GO:0090729,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623,0.7846,0.7846,0.7846,0.7846,0.5554,5,0.7388,0.3964,no
PA2_XYLAR,P0DXZ6,Protein2Text,Eukaryota,179,"May potentiate Xylotoxin(1)-Xa1a DRG activation and cell lysis, since the orthologous A.mellifera PA2 potentiates Xylotoxin(1)- Xa1a DRG activation and cell lysis. In vivo, intraplantar injection in mice may potentiate spontaneous pain behaviors and paw swelling caused by Xylotoxin(1)-Xa1a, since the orthologous A.mellifera PA2 shows this effect. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (Probable).","The molecular function of this protein is phospholipase A2 (PLA2) activity, specifically it is a secreted calcium-dependent phospholipase A2 that hydrolyzes phospholipids, such as phosphatidylcholine, to yield free fatty acids and lysophospholipids.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0004623; GO:0090729,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623,0.7846,0.7846,0.7846,0.7846,0.5554,5,0.7388,0.3964,no
PA2_XYLAR,P0DXZ6,Reference,Eukaryota,179,"May potentiate Xylotoxin(1)-Xa1a DRG activation and cell lysis, since the orthologous A.mellifera PA2 potentiates Xylotoxin(1)- Xa1a DRG activation and cell lysis. In vivo, intraplantar injection in mice may potentiate spontaneous pain behaviors and paw swelling caused by Xylotoxin(1)-Xa1a, since the orthologous A.mellifera PA2 shows this effect. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (Probable).","May potentiate Xylotoxin(1)-Xa1a DRG activation and cell lysis, since the orthologous A.mellifera PA2 potentiates Xylotoxin(1)- Xa1a DRG activation and cell lysis. In vivo, intraplantar injection in mice may potentiate spontaneous pain behaviors and paw swelling caused by Xylotoxin(1)-Xa1a, since the orthologous A.mellifera PA2 shows this effect. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (Probable).",,,,,,,GO:0046872; GO:0004623; GO:0090729,GO:0004623,GO:0004623,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623,0.5554,0.5554,0.7846,0.7846,0.5554,5,0.6471,0.3964,no
PRP_SYNY3,P74174,ESM2Text,Bacteria,133,Probably functions in the periplasm as an electron carrier with moderate lateral mobility.,"Virulence factor that plays a role in modulating adaptive immune responses under both avirulent and non-viable host conditions. Functions as a co-receptor for complement component C3b, leading to the activation of the classical complement pathway.",No,No,No,No,No,not-Yes,GO:0051537; GO:0046872; GO:0004497; GO:0016491; GO:0016705,,,,,,,,,,,0,,0.2949,no
PRP_SYNY3,P74174,Prot2Text,Bacteria,133,Probably functions in the periplasm as an electron carrier with moderate lateral mobility.,"Component of the respiratory Qrc complex, that catalyzes the reduction of the menaquinone pool using electrons transferred from the reduced periplasmic cytochrome c3, and which is probably involved in sulfate respiration.",Maybe,No,No,Maybe,Maybe,not-Yes,GO:0051537; GO:0046872; GO:0004497; GO:0016491; GO:0016705,GO:0009055,,GO:0016491; GO:0009055,GO:0009055,GO:0016491,0.2737,,0.6257,0.2737,0.6575,4,0.4577,0.2949,no
PRP_SYNY3,P74174,ProtT3,Bacteria,133,Probably functions in the periplasm as an electron carrier with moderate lateral mobility.,Cell inner membrane; Peripheral membrane protein; Periplasmic side. Belongs to the cytochrome c-552 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0051537; GO:0046872; GO:0004497; GO:0016491; GO:0016705,GO:0009055,GO:0009055; GO:0020037,GO:0009055; GO:0020037,GO:0009055; GO:0020037,GO:0009055,0.2737,0.2978,0.2978,0.2978,0.2737,5,0.2882,0.2949,no
PRP_SYNY3,P74174,ProtTale,Bacteria,133,Probably functions in the periplasm as an electron carrier with moderate lateral mobility.,Plays a role in the biogenesis of c-type cytochromes. Functioned probably in heme biosynthesis.,No,No,No,No,No,not-Yes,GO:0051537; GO:0046872; GO:0004497; GO:0016491; GO:0016705,,,,,,,,,,,0,,0.2949,no
PRP_SYNY3,P74174,Protein2Text,Bacteria,133,Probably functions in the periplasm as an electron carrier with moderate lateral mobility.,"The molecular function of this protein is not specified in the provided text. However, based on its classification as a part of the ""Protein with unknown function"" category, it is likely that its molecular function has not been explicitly described in the literature or databases. Further research or additional information would be needed to determine its molecular function.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0051537; GO:0046872; GO:0004497; GO:0016491; GO:0016705,,,,,,,,,,,0,,0.2949,no
PRP_SYNY3,P74174,Reference,Bacteria,133,Probably functions in the periplasm as an electron carrier with moderate lateral mobility.,Probably functions in the periplasm as an electron carrier with moderate lateral mobility.,,,,,,,GO:0051537; GO:0046872; GO:0004497; GO:0016491; GO:0016705,,GO:0009055,GO:0009055,GO:0009055,GO:0009055,,0.2737,0.2737,0.2737,0.2737,4,0.2737,0.2949,no
FDHB_NEOTH,P77907,ESM2Text,Bacteria,707,"Component of a dehydrogenase that catalyzes the NADP- dependent reduction of CO(2) to formate, the first step in the synthesis of the methyl group of acetate during synthesis of acetate from CO(2). In vitro, can use methyl viologen and benzyl viologen in addition to its natural electron acceptor.","Subunit of NADP-dependent ferric reductase, which catalyzes the reduction of Fe(3+) to Fe(2+) with NADH as electron donor. Can also reduce malate.",No,No,No,No,No,not-Yes,GO:0051539; GO:0010181; GO:0047899; GO:0008137,GO:0000293,GO:0016491,GO:0016491,GO:0052851,GO:0016491; GO:0050661,0.2144,0.3187,0.3187,0.1663,0.4166,5,0.2869,0.2521,no
FDHB_NEOTH,P77907,Prot2Text,Bacteria,707,"Component of a dehydrogenase that catalyzes the NADP- dependent reduction of CO(2) to formate, the first step in the synthesis of the methyl group of acetate during synthesis of acetate from CO(2). In vitro, can use methyl viologen and benzyl viologen in addition to its natural electron acceptor.",Maintains high levels of reduced glutathione in the cytosol.,No,No,No,No,No,not-Yes,GO:0051539; GO:0010181; GO:0047899; GO:0008137,,,GO:0004362,GO:0004362,,,,0.1663,0.1663,,2,0.1663,0.2521,no
FDHB_NEOTH,P77907,ProtT3,Bacteria,707,"Component of a dehydrogenase that catalyzes the NADP- dependent reduction of CO(2) to formate, the first step in the synthesis of the methyl group of acetate during synthesis of acetate from CO(2). In vitro, can use methyl viologen and benzyl viologen in addition to its natural electron acceptor.",Catalyzes the reduction of NAD(+) to NADH in the presence of NADP(+). In the N-terminal section; belongs to the zinc-containing alcohol dehydrogenase family. In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family,No,No,No,No,Maybe,not-Yes,GO:0051539; GO:0010181; GO:0047899; GO:0008137,GO:0016616; GO:0008270,GO:0016491; GO:0008270,GO:0004022; GO:0008270,GO:0004024; GO:0008270,GO:0004024,0.2898,0.3624,0.2522,0.1975,0.0,5,0.2204,0.2521,no
FDHB_NEOTH,P77907,ProtTale,Bacteria,707,"Component of a dehydrogenase that catalyzes the NADP- dependent reduction of CO(2) to formate, the first step in the synthesis of the methyl group of acetate during synthesis of acetate from CO(2). In vitro, can use methyl viologen and benzyl viologen in addition to its natural electron acceptor.","Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2- C-methyl-D-erythritol 2-phosphate (CMEP) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP).",No,No,No,No,No,not-Yes,GO:0051539; GO:0010181; GO:0047899; GO:0008137,GO:0008685,GO:0016829,GO:0016829,GO:0016829,GO:0008685,0.149,0.22,0.22,0.22,0.149,5,0.1916,0.2521,no
FDHB_NEOTH,P77907,Protein2Text,Bacteria,707,"Component of a dehydrogenase that catalyzes the NADP- dependent reduction of CO(2) to formate, the first step in the synthesis of the methyl group of acetate during synthesis of acetate from CO(2). In vitro, can use methyl viologen and benzyl viologen in addition to its natural electron acceptor.","This protein is a part of the sulfite reductase complex, which is involved in the conversion of sulfite to sulfide. The molecular function of this protein is to catalyze the reduction of sulfite to sulfide using NADPH as a reductant.",No,No,No,No,No,not-Yes,GO:0051539; GO:0010181; GO:0047899; GO:0008137,GO:0016491; GO:0050311,GO:0016491,GO:0016491,GO:0016491,GO:0050311,0.322,0.3187,0.3187,0.3187,0.1833,5,0.2923,0.2521,no
FDHB_NEOTH,P77907,Reference,Bacteria,707,"Component of a dehydrogenase that catalyzes the NADP- dependent reduction of CO(2) to formate, the first step in the synthesis of the methyl group of acetate during synthesis of acetate from CO(2). In vitro, can use methyl viologen and benzyl viologen in addition to its natural electron acceptor.","Component of a dehydrogenase that catalyzes the NADP- dependent reduction of CO(2) to formate, the first step in the synthesis of the methyl group of acetate during synthesis of acetate from CO(2). In vitro, can use methyl viologen and benzyl viologen in addition to its natural electron acceptor.",,,,,,,GO:0051539; GO:0010181; GO:0047899; GO:0008137,GO:0008863; GO:0050660,GO:0008863,GO:0016491,GO:0016491,GO:0016491,0.5476,0.3395,0.3187,0.3187,0.3187,5,0.3686,0.2521,no
LTBA_ASPLT,P9WEH6,ESM2Text,Eukaryota,3206,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. LtbA produces the trimethylated polyketide chain from acetyl-CoA, malonyl-CoA and S-adenosylmethionine (SAM). The ltbA carnitine O-acyltransferase (cAT) domain then uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A. Furthermore, the PKS C-methyltransferase (CMeT) domain is capable of catalysing gem-dimethylation of the 3- hydroxy-2,2,4-trimethylocta-4,6-dienoic acid intermediate, without requiring reversible product release and recapture by the cAT domain. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential tr",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177,,GO:0016747,GO:0016491; GO:0016740,GO:0016746,GO:0016746,,0.536,0.6847,0.5204,0.5204,4,0.5654,0.304,no
LTBA_ASPLT,P9WEH6,Prot2Text,Eukaryota,3206,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. LtbA produces the trimethylated polyketide chain from acetyl-CoA, malonyl-CoA and S-adenosylmethionine (SAM). The ltbA carnitine O-acyltransferase (cAT) domain then uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A. Furthermore, the PKS C-methyltransferase (CMeT) domain is capable of catalysing gem-dimethylation of the 3- hydroxy-2,2,4-trimethylocta-4,6-dienoic acid intermediate, without requiring reversible product release and recapture by the cAT domain. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential tr",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177,,,GO:0016747,,GO:0016746,,,0.536,,0.5204,2,0.5282,0.304,no
LTBA_ASPLT,P9WEH6,ProtT3,Eukaryota,3206,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. LtbA produces the trimethylated polyketide chain from acetyl-CoA, malonyl-CoA and S-adenosylmethionine (SAM). The ltbA carnitine O-acyltransferase (cAT) domain then uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A. Furthermore, the PKS C-methyltransferase (CMeT) domain is capable of catalysing gem-dimethylation of the 3- hydroxy-2,2,4-trimethylocta-4,6-dienoic acid intermediate, without requiring reversible product release and recapture by the cAT domain. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177,GO:0016747,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.536,0.5204,0.5204,0.5204,0.5204,5,0.5235,0.304,no
LTBA_ASPLT,P9WEH6,ProtTale,Eukaryota,3206,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. LtbA produces the trimethylated polyketide chain from acetyl-CoA, malonyl-CoA and S-adenosylmethionine (SAM). The ltbA carnitine O-acyltransferase (cAT) domain then uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A. Furthermore, the PKS C-methyltransferase (CMeT) domain is capable of catalysing gem-dimethylation of the 3- hydroxy-2,2,4-trimethylocta-4,6-dienoic acid intermediate, without requiring reversible product release and recapture by the cAT domain. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. Within the pathway, ptmS catalyzes the first step of penitrem biosynthesis via condensation of isopentenyl diphosphate with 7-methylgeranyl diphosphate to yield (2E,6E)-geranylgeranyl diphosphate (GGPP). GGPP is then cleaved by ptmC to yield penitrem F via the cleavage of the GGPP backbone to yield penitrem F as the final product. The geranylgeranyl diphosphate (GGPP) synthase",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177,GO:0016740,GO:0016747,GO:0016746,GO:0016746,,0.5397,0.536,0.5204,0.5204,,4,0.5291,0.304,no
LTBA_ASPLT,P9WEH6,Protein2Text,Eukaryota,3206,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. LtbA produces the trimethylated polyketide chain from acetyl-CoA, malonyl-CoA and S-adenosylmethionine (SAM). The ltbA carnitine O-acyltransferase (cAT) domain then uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A. Furthermore, the PKS C-methyltransferase (CMeT) domain is capable of catalysing gem-dimethylation of the 3- hydroxy-2,2,4-trimethylocta-4,6-dienoic acid intermediate, without requiring reversible product release and recapture by the cAT domain. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.","The molecular function of this protein is to catalyze the synthesis of a compound, likely a fatty acid, given its classification as a fatty acid synthase. Fatty acid synthase is a multi-functional enzyme that catalyzes the formation of fatty acids from acetyl-CoA and malonyl-CoA. It consists of two domains: the acyl carrier protein (ACP) domain, which carries the growing fatty acid chain, and the condensing enzyme domain, which catalyzes the condensation of acyl groups with malonyl-CoA to form the growing fatty acid chain. The protein is likely involved in the production of fatty acids, which are important components of cellular membranes and energy storage molecules.",Maybe,No,Vague,No,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.567,0.567,0.567,0.567,0.567,5,0.567,0.304,no
LTBA_ASPLT,P9WEH6,Reference,Eukaryota,3206,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. LtbA produces the trimethylated polyketide chain from acetyl-CoA, malonyl-CoA and S-adenosylmethionine (SAM). The ltbA carnitine O-acyltransferase (cAT) domain then uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A. Furthermore, the PKS C-methyltransferase (CMeT) domain is capable of catalysing gem-dimethylation of the 3- hydroxy-2,2,4-trimethylocta-4,6-dienoic acid intermediate, without requiring reversible product release and recapture by the cAT domain. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. LtbA produces the trimethylated polyketide chain from acetyl-CoA, malonyl-CoA and S-adenosylmethionine (SAM). The ltbA carnitine O-acyltransferase (cAT) domain then uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A. Furthermore, the PKS C-methyltransferase (CMeT) domain is capable of catalysing gem-dimethylation of the 3- hydroxy-2,2,4-trimethylocta-4,6-dienoic acid intermediate, without requiring reversible product release and recapture by the cAT domain. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.",,,,,,,GO:0004312; GO:0008168; GO:0016491; GO:0031177,GO:0031177; GO:0016747,GO:0004315; GO:0008168,,GO:0016746; GO:0008168,,0.7647,0.6595,,0.6742,,3,0.6995,0.304,no
MALA_MORAP,P9WER8,ESM2Text,Eukaryota,7760,"Heptamodular nonribosomal peptide synthetase that catalyzes the biosynthesis of malpinins, natural products that show biosurfactant activities. Malpinins are acetylated hexapeptides (Ac-D-Leu/Val-D-Arg-D-Leu/Val-L-Phe/Leu-Dhb-D-Trp) containing a non- canonical amino acid derived from dehydration of L-Trp, (Z)- dehydrobutyrine (Dhb), at position 5, as well as a C-terminal D-amino acid, D-tryptophan, that can be oxidized to kynurenine. Incorporated D-amino acids in positions 1, 3 and 4 are variable resulting in the malpinin A-congeners malpinin B to E. Both modules M1 and M3 have relaxed specificity towards aliphatic amino acids (L-Leu > L-Met > L/D-Val > L-Cys), explaining Val at position 1 and 3 in malpinin A-congeners malpinin B to D. The incorporation of L-Leu, but not N-acetyl-L- Leu by module 1 suggests the N-terminal acetylation occurs at a later stage of biosynthesis. Similar to M1 and M3, M4 has a broad substrate spectrum showing the highest activity with L-Phe followed by other hydrophobic amino acids (L-Phe > L-Met = L-Trp). In contrast, M2, M5 and M6 are highly specific for L-Arg, L-Thr, and L-Trp, respectively. Solely, M7 converted its preferred substrate (L-Phe) with a 15 000-fold reduced turnover rate compared to the most active module M6, indicating that its A domain cannot contribute to the malpinin biosynthesis due to low activity. Since the last T domain in malA is apparently not loaded with an amino acid, either the TE domain must offload the oligopeptide from the preceding T domain or the dual E/C domain of M7 must transfer the final peptide chain to the free acceptor T domain of M7 prior to release.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcs",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,,GO:0016874,GO:0003824,GO:0016874,GO:0016874; GO:0005524,,0.709,0.5613,0.709,0.6793,4,0.6646,0.4598,no
MALA_MORAP,P9WER8,Prot2Text,Eukaryota,7760,"Heptamodular nonribosomal peptide synthetase that catalyzes the biosynthesis of malpinins, natural products that show biosurfactant activities. Malpinins are acetylated hexapeptides (Ac-D-Leu/Val-D-Arg-D-Leu/Val-L-Phe/Leu-Dhb-D-Trp) containing a non- canonical amino acid derived from dehydration of L-Trp, (Z)- dehydrobutyrine (Dhb), at position 5, as well as a C-terminal D-amino acid, D-tryptophan, that can be oxidized to kynurenine. Incorporated D-amino acids in positions 1, 3 and 4 are variable resulting in the malpinin A-congeners malpinin B to E. Both modules M1 and M3 have relaxed specificity towards aliphatic amino acids (L-Leu > L-Met > L/D-Val > L-Cys), explaining Val at position 1 and 3 in malpinin A-congeners malpinin B to D. The incorporation of L-Leu, but not N-acetyl-L- Leu by module 1 suggests the N-terminal acetylation occurs at a later stage of biosynthesis. Similar to M1 and M3, M4 has a broad substrate spectrum showing the highest activity with L-Phe followed by other hydrophobic amino acids (L-Phe > L-Met = L-Trp). In contrast, M2, M5 and M6 are highly specific for L-Arg, L-Thr, and L-Trp, respectively. Solely, M7 converted its preferred substrate (L-Phe) with a 15 000-fold reduced turnover rate compared to the most active module M6, indicating that its A domain cannot contribute to the malpinin biosynthesis due to low activity. Since the last T domain in malA is apparently not loaded with an amino acid, either the TE domain must offload the oligopeptide from the preceding T domain or the dual E/C domain of M7 must transfer the final peptide chain to the free acceptor T domain of M7 prior to release.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcs",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,,,GO:0016874,,GO:0016874,,,0.709,,0.709,2,0.709,0.4598,no
MALA_MORAP,P9WER8,ProtT3,Eukaryota,7760,"Heptamodular nonribosomal peptide synthetase that catalyzes the biosynthesis of malpinins, natural products that show biosurfactant activities. Malpinins are acetylated hexapeptides (Ac-D-Leu/Val-D-Arg-D-Leu/Val-L-Phe/Leu-Dhb-D-Trp) containing a non- canonical amino acid derived from dehydration of L-Trp, (Z)- dehydrobutyrine (Dhb), at position 5, as well as a C-terminal D-amino acid, D-tryptophan, that can be oxidized to kynurenine. Incorporated D-amino acids in positions 1, 3 and 4 are variable resulting in the malpinin A-congeners malpinin B to E. Both modules M1 and M3 have relaxed specificity towards aliphatic amino acids (L-Leu > L-Met > L/D-Val > L-Cys), explaining Val at position 1 and 3 in malpinin A-congeners malpinin B to D. The incorporation of L-Leu, but not N-acetyl-L- Leu by module 1 suggests the N-terminal acetylation occurs at a later stage of biosynthesis. Similar to M1 and M3, M4 has a broad substrate spectrum showing the highest activity with L-Phe followed by other hydrophobic amino acids (L-Phe > L-Met = L-Trp). In contrast, M2, M5 and M6 are highly specific for L-Arg, L-Thr, and L-Trp, respectively. Solely, M7 converted its preferred substrate (L-Phe) with a 15 000-fold reduced turnover rate compared to the most active module M6, indicating that its A domain cannot contribute to the malpinin biosynthesis due to low activity. Since the last T domain in malA is apparently not loaded with an amino acid, either the TE domain must offload the oligopeptide from the preceding T domain or the dual E/C domain of M7 must transfer the final peptide chain to the free acceptor T domain of M7 prior to release.",Belongs to the ATP-dependent AMP-binding enzyme family,Vague,No,Vague,Vague,Vague,not-Yes,GO:0016874; GO:0031177,GO:0016874; GO:0005524,GO:0016874; GO:0005524,GO:0016874,GO:0016874; GO:0005524,GO:0016874; GO:0005524,0.6793,0.6793,0.709,0.6793,0.6793,5,0.6852,0.4598,no
MALA_MORAP,P9WER8,ProtTale,Eukaryota,7760,"Heptamodular nonribosomal peptide synthetase that catalyzes the biosynthesis of malpinins, natural products that show biosurfactant activities. Malpinins are acetylated hexapeptides (Ac-D-Leu/Val-D-Arg-D-Leu/Val-L-Phe/Leu-Dhb-D-Trp) containing a non- canonical amino acid derived from dehydration of L-Trp, (Z)- dehydrobutyrine (Dhb), at position 5, as well as a C-terminal D-amino acid, D-tryptophan, that can be oxidized to kynurenine. Incorporated D-amino acids in positions 1, 3 and 4 are variable resulting in the malpinin A-congeners malpinin B to E. Both modules M1 and M3 have relaxed specificity towards aliphatic amino acids (L-Leu > L-Met > L/D-Val > L-Cys), explaining Val at position 1 and 3 in malpinin A-congeners malpinin B to D. The incorporation of L-Leu, but not N-acetyl-L- Leu by module 1 suggests the N-terminal acetylation occurs at a later stage of biosynthesis. Similar to M1 and M3, M4 has a broad substrate spectrum showing the highest activity with L-Phe followed by other hydrophobic amino acids (L-Phe > L-Met = L-Trp). In contrast, M2, M5 and M6 are highly specific for L-Arg, L-Thr, and L-Trp, respectively. Solely, M7 converted its preferred substrate (L-Phe) with a 15 000-fold reduced turnover rate compared to the most active module M6, indicating that its A domain cannot contribute to the malpinin biosynthesis due to low activity. Since the last T domain in malA is apparently not loaded with an amino acid, either the TE domain must offload the oligopeptide from the preceding T domain or the dual E/C domain of M7 must transfer the final peptide chain to the free acceptor T domain of M7 prior to release.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS). SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms. These initial steps feature the priming of an unusual benzoic acid starter unit onto",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,GO:0016874,GO:0016874,GO:0016874,GO:0016874,,0.709,0.709,0.709,0.709,,4,0.709,0.4598,no
MALA_MORAP,P9WER8,Protein2Text,Eukaryota,7760,"Heptamodular nonribosomal peptide synthetase that catalyzes the biosynthesis of malpinins, natural products that show biosurfactant activities. Malpinins are acetylated hexapeptides (Ac-D-Leu/Val-D-Arg-D-Leu/Val-L-Phe/Leu-Dhb-D-Trp) containing a non- canonical amino acid derived from dehydration of L-Trp, (Z)- dehydrobutyrine (Dhb), at position 5, as well as a C-terminal D-amino acid, D-tryptophan, that can be oxidized to kynurenine. Incorporated D-amino acids in positions 1, 3 and 4 are variable resulting in the malpinin A-congeners malpinin B to E. Both modules M1 and M3 have relaxed specificity towards aliphatic amino acids (L-Leu > L-Met > L/D-Val > L-Cys), explaining Val at position 1 and 3 in malpinin A-congeners malpinin B to D. The incorporation of L-Leu, but not N-acetyl-L- Leu by module 1 suggests the N-terminal acetylation occurs at a later stage of biosynthesis. Similar to M1 and M3, M4 has a broad substrate spectrum showing the highest activity with L-Phe followed by other hydrophobic amino acids (L-Phe > L-Met = L-Trp). In contrast, M2, M5 and M6 are highly specific for L-Arg, L-Thr, and L-Trp, respectively. Solely, M7 converted its preferred substrate (L-Phe) with a 15 000-fold reduced turnover rate compared to the most active module M6, indicating that its A domain cannot contribute to the malpinin biosynthesis due to low activity. Since the last T domain in malA is apparently not loaded with an amino acid, either the TE domain must offload the oligopeptide from the preceding T domain or the dual E/C domain of M7 must transfer the final peptide chain to the free acceptor T domain of M7 prior to release.","This protein is involved in the molecular function of being a component of the phage capsid, which is the protein shell that encases the viral genome. More specifically, it is a component of the major capsid protein, which forms the structure of the capsid and interacts with the viral genome to protect it during transmission and infection.",No,No,Vague,No,No,not-Yes,GO:0016874; GO:0031177,GO:0005198,GO:0005198,GO:0005198,GO:0005198,GO:0005198,0.2783,0.2783,0.2783,0.2783,0.2783,5,0.2783,0.4598,no
MALA_MORAP,P9WER8,Reference,Eukaryota,7760,"Heptamodular nonribosomal peptide synthetase that catalyzes the biosynthesis of malpinins, natural products that show biosurfactant activities. Malpinins are acetylated hexapeptides (Ac-D-Leu/Val-D-Arg-D-Leu/Val-L-Phe/Leu-Dhb-D-Trp) containing a non- canonical amino acid derived from dehydration of L-Trp, (Z)- dehydrobutyrine (Dhb), at position 5, as well as a C-terminal D-amino acid, D-tryptophan, that can be oxidized to kynurenine. Incorporated D-amino acids in positions 1, 3 and 4 are variable resulting in the malpinin A-congeners malpinin B to E. Both modules M1 and M3 have relaxed specificity towards aliphatic amino acids (L-Leu > L-Met > L/D-Val > L-Cys), explaining Val at position 1 and 3 in malpinin A-congeners malpinin B to D. The incorporation of L-Leu, but not N-acetyl-L- Leu by module 1 suggests the N-terminal acetylation occurs at a later stage of biosynthesis. Similar to M1 and M3, M4 has a broad substrate spectrum showing the highest activity with L-Phe followed by other hydrophobic amino acids (L-Phe > L-Met = L-Trp). In contrast, M2, M5 and M6 are highly specific for L-Arg, L-Thr, and L-Trp, respectively. Solely, M7 converted its preferred substrate (L-Phe) with a 15 000-fold reduced turnover rate compared to the most active module M6, indicating that its A domain cannot contribute to the malpinin biosynthesis due to low activity. Since the last T domain in malA is apparently not loaded with an amino acid, either the TE domain must offload the oligopeptide from the preceding T domain or the dual E/C domain of M7 must transfer the final peptide chain to the free acceptor T domain of M7 prior to release.","Heptamodular nonribosomal peptide synthetase that catalyzes the biosynthesis of malpinins, natural products that show biosurfactant activities. Malpinins are acetylated hexapeptides (Ac-D-Leu/Val-D-Arg-D-Leu/Val-L-Phe/Leu-Dhb-D-Trp) containing a non- canonical amino acid derived from dehydration of L-Trp, (Z)- dehydrobutyrine (Dhb), at position 5, as well as a C-terminal D-amino acid, D-tryptophan, that can be oxidized to kynurenine. Incorporated D-amino acids in positions 1, 3 and 4 are variable resulting in the malpinin A-congeners malpinin B to E. Both modules M1 and M3 have relaxed specificity towards aliphatic amino acids (L-Leu > L-Met > L/D-Val > L-Cys), explaining Val at position 1 and 3 in malpinin A-congeners malpinin B to D. The incorporation of L-Leu, but not N-acetyl-L- Leu by module 1 suggests the N-terminal acetylation occurs at a later stage of biosynthesis. Similar to M1 and M3, M4 has a broad substrate spectrum showing the highest activity with L-Phe followed by other hydrophobic amino acids (L-Phe > L-Met = L-Trp). In contrast, M2, M5 and M6 are highly specific for L-Arg, L-Thr, and L-Trp, respectively. Solely, M7 converted its preferred substrate (L-Phe) with a 15 000-fold reduced turnover rate compared to the most active module M6, indicating that its A domain cannot contribute to the malpinin biosynthesis due to low activity. Since the last T domain in malA is apparently not loaded with an amino acid, either the TE domain must offload the oligopeptide from the preceding T domain or the dual E/C domain of M7 must transfer the final peptide chain to the free acceptor T domain of M7 prior to release.",,,,,,,GO:0016874; GO:0031177,GO:0031177; GO:0016874,GO:0008927,,GO:0016874; GO:0031177,,1.0,0.2639,,1.0,,3,0.7546,0.4598,no
PREU3_PREIS,P9WET6,ESM2Text,Eukaryota,2523,"Non-reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product (Probable). The first step in the pathway is performed by Preu3 that condenses one acetyl-CoA starter unit with 3 malonyl-CoA units. Preu3 also catalyzes one methylation step to produce 3-methylorsellinate, an intermediate that exhibits significant antibacterial activities against methicillin-resistant Staphylococcus aureus, multidrug-resistant Enterococcus faecalis, multidrug-resistant Enterococcus faecium, and multidrug-resistant Staphylococcus epidermidis.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0031177; GO:0008236,,GO:0016747,GO:0016491; GO:0016740,GO:0016746,GO:0016746,,0.4998,0.4736,0.4777,0.4777,4,0.4822,0.2991,no
PREU3_PREIS,P9WET6,Prot2Text,Eukaryota,2523,"Non-reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product (Probable). The first step in the pathway is performed by Preu3 that condenses one acetyl-CoA starter unit with 3 malonyl-CoA units. Preu3 also catalyzes one methylation step to produce 3-methylorsellinate, an intermediate that exhibits significant antibacterial activities against methicillin-resistant Staphylococcus aureus, multidrug-resistant Enterococcus faecalis, multidrug-resistant Enterococcus faecium, and multidrug-resistant Staphylococcus epidermidis.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0031177; GO:0008236,,,GO:0016747,,GO:0016746,,,0.4998,,0.4777,2,0.4888,0.2991,no
PREU3_PREIS,P9WET6,ProtT3,Eukaryota,2523,"Non-reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product (Probable). The first step in the pathway is performed by Preu3 that condenses one acetyl-CoA starter unit with 3 malonyl-CoA units. Preu3 also catalyzes one methylation step to produce 3-methylorsellinate, an intermediate that exhibits significant antibacterial activities against methicillin-resistant Staphylococcus aureus, multidrug-resistant Enterococcus faecalis, multidrug-resistant Enterococcus faecium, and multidrug-resistant Staphylococcus epidermidis.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0031177; GO:0008236,GO:0016747,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.4998,0.4777,0.4777,0.4777,0.4777,5,0.4821,0.2991,no
PREU3_PREIS,P9WET6,ProtTale,Eukaryota,2523,"Non-reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product (Probable). The first step in the pathway is performed by Preu3 that condenses one acetyl-CoA starter unit with 3 malonyl-CoA units. Preu3 also catalyzes one methylation step to produce 3-methylorsellinate, an intermediate that exhibits significant antibacterial activities against methicillin-resistant Staphylococcus aureus, multidrug-resistant Enterococcus faecalis, multidrug-resistant Enterococcus faecium, and multidrug-resistant Staphylococcus epidermidis.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0031177; GO:0008236,GO:0016747,GO:0016747,GO:0016491; GO:0016874,GO:0016746,,0.4998,0.4998,0.3383,0.4777,,4,0.4539,0.2991,no
PREU3_PREIS,P9WET6,Protein2Text,Eukaryota,2523,"Non-reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product (Probable). The first step in the pathway is performed by Preu3 that condenses one acetyl-CoA starter unit with 3 malonyl-CoA units. Preu3 also catalyzes one methylation step to produce 3-methylorsellinate, an intermediate that exhibits significant antibacterial activities against methicillin-resistant Staphylococcus aureus, multidrug-resistant Enterococcus faecalis, multidrug-resistant Enterococcus faecium, and multidrug-resistant Staphylococcus epidermidis.","This protein is involved in the molecular function of catalyzing the decarboxylation of 4-hydroxy-2-oxoglutarate to form succinic semialdehyde, a step in the degradation of 4-hydroxy-L-proline.",No,No,No,No,No,not-Yes,GO:0004312; GO:0008168; GO:0031177; GO:0008236,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.2203,0.2203,0.2203,0.2203,0.2203,5,0.2203,0.2991,no
PREU3_PREIS,P9WET6,Reference,Eukaryota,2523,"Non-reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product (Probable). The first step in the pathway is performed by Preu3 that condenses one acetyl-CoA starter unit with 3 malonyl-CoA units. Preu3 also catalyzes one methylation step to produce 3-methylorsellinate, an intermediate that exhibits significant antibacterial activities against methicillin-resistant Staphylococcus aureus, multidrug-resistant Enterococcus faecalis, multidrug-resistant Enterococcus faecium, and multidrug-resistant Staphylococcus epidermidis.","Non-reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product (Probable). The first step in the pathway is performed by Preu3 that condenses one acetyl-CoA starter unit with 3 malonyl-CoA units. Preu3 also catalyzes one methylation step to produce 3-methylorsellinate, an intermediate that exhibits significant antibacterial activities against methicillin-resistant Staphylococcus aureus, multidrug-resistant Enterococcus faecalis, multidrug-resistant Enterococcus faecium, and multidrug-resistant Staphylococcus epidermidis.",,,,,,,GO:0004312; GO:0008168; GO:0031177; GO:0008236,GO:0031177; GO:0016747,GO:0004315; GO:0008168,,GO:0016746; GO:0008168,,0.7344,0.6293,,0.6387,,3,0.6675,0.2991,no
TAZB_ASPTN,Q0CS88,ESM2Text,Eukaryota,2620,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of azaterrilone A and other azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities. The first step of the pathway begins with the non-reducing polyketide synthase tazA that assembles one acetyl-CoA starter unit, five malonyl-CoA units, and catalyzes a series of Claisen condensations, methylation, PT-mediated cyclization, and finally releases the first hexaketide precursor through the R-domain. The tazA product then undergoes reduction on its terminal ketone and the following pyran-ring formation by yet undetermined enzyme(s). Dehydration and enoyl reduction, possibly involving the trans-enoyl reductase tazE leads to the next intermediate. TazD is predicted as an acetyltransferase and might catalyze the acetylation steps leading to the synthesis of azaterrilone A. Azaterrilone A is not the final product of the taz pathway and both the highly reducing polyketide synthase tazB and the dual enzyme tazHJ catalyze late steps of the pathway, leading to the production of the 2 final stereoisomers that contain additional polyketide modification whose structures have still to be determined (Probable).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential tr",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0016491; GO:0008270,,GO:0016747,GO:0016491; GO:0016740,GO:0016746,GO:0016746,,0.5514,0.6665,0.51,0.51,4,0.5595,0.2618,no
TAZB_ASPTN,Q0CS88,Prot2Text,Eukaryota,2620,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of azaterrilone A and other azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities. The first step of the pathway begins with the non-reducing polyketide synthase tazA that assembles one acetyl-CoA starter unit, five malonyl-CoA units, and catalyzes a series of Claisen condensations, methylation, PT-mediated cyclization, and finally releases the first hexaketide precursor through the R-domain. The tazA product then undergoes reduction on its terminal ketone and the following pyran-ring formation by yet undetermined enzyme(s). Dehydration and enoyl reduction, possibly involving the trans-enoyl reductase tazE leads to the next intermediate. TazD is predicted as an acetyltransferase and might catalyze the acetylation steps leading to the synthesis of azaterrilone A. Azaterrilone A is not the final product of the taz pathway and both the highly reducing polyketide synthase tazB and the dual enzyme tazHJ catalyze late steps of the pathway, leading to the production of the 2 final stereoisomers that contain additional polyketide modification whose structures have still to be determined (Probable).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0016491; GO:0008270,,,GO:0016747,,GO:0016746,,,0.5514,,0.51,2,0.5307,0.2618,no
TAZB_ASPTN,Q0CS88,ProtT3,Eukaryota,2620,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of azaterrilone A and other azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities. The first step of the pathway begins with the non-reducing polyketide synthase tazA that assembles one acetyl-CoA starter unit, five malonyl-CoA units, and catalyzes a series of Claisen condensations, methylation, PT-mediated cyclization, and finally releases the first hexaketide precursor through the R-domain. The tazA product then undergoes reduction on its terminal ketone and the following pyran-ring formation by yet undetermined enzyme(s). Dehydration and enoyl reduction, possibly involving the trans-enoyl reductase tazE leads to the next intermediate. TazD is predicted as an acetyltransferase and might catalyze the acetylation steps leading to the synthesis of azaterrilone A. Azaterrilone A is not the final product of the taz pathway and both the highly reducing polyketide synthase tazB and the dual enzyme tazHJ catalyze late steps of the pathway, leading to the production of the 2 final stereoisomers that contain additional polyketide modification whose structures have still to be determined (Probable).","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS) . SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0016491; GO:0008270,GO:0016747,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.5514,0.51,0.51,0.51,0.51,5,0.5183,0.2618,no
TAZB_ASPTN,Q0CS88,ProtTale,Eukaryota,2620,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of azaterrilone A and other azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities. The first step of the pathway begins with the non-reducing polyketide synthase tazA that assembles one acetyl-CoA starter unit, five malonyl-CoA units, and catalyzes a series of Claisen condensations, methylation, PT-mediated cyclization, and finally releases the first hexaketide precursor through the R-domain. The tazA product then undergoes reduction on its terminal ketone and the following pyran-ring formation by yet undetermined enzyme(s). Dehydration and enoyl reduction, possibly involving the trans-enoyl reductase tazE leads to the next intermediate. TazD is predicted as an acetyltransferase and might catalyze the acetylation steps leading to the synthesis of azaterrilone A. Azaterrilone A is not the final product of the taz pathway and both the highly reducing polyketide synthase tazB and the dual enzyme tazHJ catalyze late steps of the pathway, leading to the production of the 2 final stereoisomers that contain additional polyketide modification whose structures have still to be determined (Probable).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0016491; GO:0008270,GO:0016747,GO:0016747,GO:0016491; GO:0016874,GO:0016746,,0.5514,0.5514,0.6148,0.51,,4,0.5569,0.2618,no
TAZB_ASPTN,Q0CS88,Protein2Text,Eukaryota,2620,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of azaterrilone A and other azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities. The first step of the pathway begins with the non-reducing polyketide synthase tazA that assembles one acetyl-CoA starter unit, five malonyl-CoA units, and catalyzes a series of Claisen condensations, methylation, PT-mediated cyclization, and finally releases the first hexaketide precursor through the R-domain. The tazA product then undergoes reduction on its terminal ketone and the following pyran-ring formation by yet undetermined enzyme(s). Dehydration and enoyl reduction, possibly involving the trans-enoyl reductase tazE leads to the next intermediate. TazD is predicted as an acetyltransferase and might catalyze the acetylation steps leading to the synthesis of azaterrilone A. Azaterrilone A is not the final product of the taz pathway and both the highly reducing polyketide synthase tazB and the dual enzyme tazHJ catalyze late steps of the pathway, leading to the production of the 2 final stereoisomers that contain additional polyketide modification whose structures have still to be determined (Probable).","This protein is involved in the biosynthesis of aflatoxin, a mycotoxin that is produced by certain species of fungi. The molecular function of this protein is to catalyze the formation of aflatoxin, which is a key step in the biosynthesis of this toxin. Specifically, it is involved in the formation of the aflatoxin B1 (AFB1) precursor molecule, which is then converted to AFB1 through a series of enzymatic reactions. The protein is a cytochrome P450 monooxygenase, which is a family of enzymes that catalyze the insertion of one atom of oxygen into a substrate. In this case, the protein is responsible for the insertion of oxygen into the aflatoxin precursor molecule, resulting in the formation of AFB1. This protein is an important target for research into the biosynthesis of aflatoxins, as it is a key enzyme in the production of these toxic compounds.",No,No,No,No,Maybe,not-Yes,GO:0004312; GO:0016491; GO:0008270,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.5038,0.5038,0.5038,0.5038,0.5038,5,0.5038,0.2618,no
TAZB_ASPTN,Q0CS88,Reference,Eukaryota,2620,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of azaterrilone A and other azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities. The first step of the pathway begins with the non-reducing polyketide synthase tazA that assembles one acetyl-CoA starter unit, five malonyl-CoA units, and catalyzes a series of Claisen condensations, methylation, PT-mediated cyclization, and finally releases the first hexaketide precursor through the R-domain. The tazA product then undergoes reduction on its terminal ketone and the following pyran-ring formation by yet undetermined enzyme(s). Dehydration and enoyl reduction, possibly involving the trans-enoyl reductase tazE leads to the next intermediate. TazD is predicted as an acetyltransferase and might catalyze the acetylation steps leading to the synthesis of azaterrilone A. Azaterrilone A is not the final product of the taz pathway and both the highly reducing polyketide synthase tazB and the dual enzyme tazHJ catalyze late steps of the pathway, leading to the production of the 2 final stereoisomers that contain additional polyketide modification whose structures have still to be determined (Probable).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of azaterrilone A and other azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities. The first step of the pathway begins with the non-reducing polyketide synthase tazA that assembles one acetyl-CoA starter unit, five malonyl-CoA units, and catalyzes a series of Claisen condensations, methylation, PT-mediated cyclization, and finally releases the first hexaketide precursor through the R-domain. The tazA product then undergoes reduction on its terminal ketone and the following pyran-ring formation by yet undetermined enzyme(s). Dehydration and enoyl reduction, possibly involving the trans-enoyl reductase tazE leads to the next intermediate. TazD is predicted as an acetyltransferase and might catalyze the acetylation steps leading to the synthesis of azaterrilone A. Azaterrilone A is not the final product of the taz pathway and both the highly reducing polyketide synthase tazB and the dual enzyme tazHJ catalyze late steps of the pathway, leading to the production of the 2 final stereoisomers that contain additional polyketide modification whose structures have still to be determined (Probable).",,,,,,,GO:0004312; GO:0016491; GO:0008270,GO:0031177; GO:0016747,GO:0004315,,GO:0016746,,0.5596,0.4704,,0.51,,3,0.5133,0.2618,no
FRBH_STRR3,Q0ZQ41,ESM2Text,Bacteria,628,"Bifunctional cytidylyltransferase/decarboxylase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5- phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the condensation of 2-amino-4-phosphonobutyrate (2APn) and CTP to form CMP- 5'-2APn and then decarboxylates CMP-5'-2APn to yield CMP-5'-(3- aminopropyl)phosphonate (CMP-5'-3APn).","Involved in the biosynthesis of the O-methyl phosphoramidate (MPA), a sugar moiety of adenosylcobalamin (AdoCbl) and an essential component of the O-methyltransferase system. Catalyzes the transfer of a CMP moiety from CTP to yield free CMP. It can also use CTP, but with a lower efficiency. It depends on the nucleotide sugar moiety, and also shows activity toward ATP, ADP, and CTP.",No,No,No,No,No,not-Yes,GO:0016831; GO:0046872; GO:0016779; GO:0030170,GO:0016779,GO:0016779,GO:0016740,GO:0016779,GO:0016779,0.4919,0.4919,0.4125,0.4919,0.4919,5,0.476,0.3512,no
FRBH_STRR3,Q0ZQ41,Prot2Text,Bacteria,628,"Bifunctional cytidylyltransferase/decarboxylase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5- phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the condensation of 2-amino-4-phosphonobutyrate (2APn) and CTP to form CMP- 5'-2APn and then decarboxylates CMP-5'-2APn to yield CMP-5'-(3- aminopropyl)phosphonate (CMP-5'-3APn).","Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. Catalyzes the formation of the L-serine via the condensation of pyrophosphate and iron-sulfur (Fe-S) clusters. EntF catalyzes the transfer of the gamma-lactam group from S-adenosyl-L-methionine (SAM) to the C-4 position of 2,3-dihydroxybenzoate (DHB), producing seryl-L-serine. It can use both NAD and NADP as electron donors, but the preferred electron acceptor is NADP.",No,No,No,No,No,not-Yes,GO:0016831; GO:0046872; GO:0016779; GO:0030170,,,GO:0016874,,,,,0.2994,,,1,0.2994,0.3512,no
FRBH_STRR3,Q0ZQ41,ProtT3,Bacteria,628,"Bifunctional cytidylyltransferase/decarboxylase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5- phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the condensation of 2-amino-4-phosphonobutyrate (2APn) and CTP to form CMP- 5'-2APn and then decarboxylates CMP-5'-2APn to yield CMP-5'-(3- aminopropyl)phosphonate (CMP-5'-3APn).",Involved in the biosynthesis of the lipooligosaccharide (LOS) of M.tuberculosis. Catalyzes the formation of dTDP-N-acetylglucosamine (dTDP-GlcNAc) from dTDP-4-amino-4-deoxy-L-arabinose (dTDP-L-Ara4N) and UDP-N-acetylglucosamine (UDP-GlcNAc). In the C-terminal section; belongs to the GcvT family. In the N-terminal section; belongs to the DeoC/,No,No,No,No,No,not-Yes,GO:0016831; GO:0046872; GO:0016779; GO:0030170,GO:0016757,GO:0016740,GO:0016757,GO:0016757,GO:0016757,0.3328,0.4125,0.3328,0.3328,0.3328,5,0.3487,0.3512,no
FRBH_STRR3,Q0ZQ41,ProtTale,Bacteria,628,"Bifunctional cytidylyltransferase/decarboxylase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5- phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the condensation of 2-amino-4-phosphonobutyrate (2APn) and CTP to form CMP- 5'-2APn and then decarboxylates CMP-5'-2APn to yield CMP-5'-(3- aminopropyl)phosphonate (CMP-5'-3APn).","Growth factor that is required for normal cell division in both the rod and spiral phases of growth. In E.coli, plays a major role in cell division during the early- to mid-log phase of growth. In B.subtilis, plays a major role in cell division during the early- to mid-log phase of growth. May be involved in the transfer of N-acetyl-D-glucosamine (GlcNAc) from the mother cell to the daughter cell.",No,No,No,No,No,not-Yes,GO:0016831; GO:0046872; GO:0016779; GO:0030170,,,,,,,,,,,0,,0.3512,no
FRBH_STRR3,Q0ZQ41,Protein2Text,Bacteria,628,"Bifunctional cytidylyltransferase/decarboxylase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5- phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the condensation of 2-amino-4-phosphonobutyrate (2APn) and CTP to form CMP- 5'-2APn and then decarboxylates CMP-5'-2APn to yield CMP-5'-(3- aminopropyl)phosphonate (CMP-5'-3APn).","This protein is involved in the synthesis of a specific type of molecule. The molecular function of this protein is likely related to its role in the synthesis of a specific molecule, but the exact nature of this molecule is not specified in the provided text. However, based on the name of the protein, it is likely that it is involved in the synthesis of a type of sugar molecule, possibly a nucleotide sugar. Further research would be necessary to determine the specific molecular function of this protein.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016831; GO:0046872; GO:0016779; GO:0030170,,,,,,,,,,,0,,0.3512,no
FRBH_STRR3,Q0ZQ41,Reference,Bacteria,628,"Bifunctional cytidylyltransferase/decarboxylase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5- phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the condensation of 2-amino-4-phosphonobutyrate (2APn) and CTP to form CMP- 5'-2APn and then decarboxylates CMP-5'-2APn to yield CMP-5'-(3- aminopropyl)phosphonate (CMP-5'-3APn).","Bifunctional cytidylyltransferase/decarboxylase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5- phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the condensation of 2-amino-4-phosphonobutyrate (2APn) and CTP to form CMP- 5'-2APn and then decarboxylates CMP-5'-2APn to yield CMP-5'-(3- aminopropyl)phosphonate (CMP-5'-3APn).",,,,,,,GO:0016831; GO:0046872; GO:0016779; GO:0030170,GO:0016779; GO:0016831,GO:0016779; GO:0016831,GO:0016779; GO:0016831,GO:0016779; GO:0016831,GO:0016779; GO:0016831,0.6976,0.6976,0.6976,0.6976,0.6976,5,0.6976,0.3512,no
RHMD_SPHSS,Q1NEI8,ESM2Text,Bacteria,397,"Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy- L-rhamnonate (KDR). Also shows activity with L- lyxonate and L-mannonate, with much lower catalytic efficiency. Catalyzes the third step in an alternative pathway for rhamnose utilization that does not involve phosphorylated intermediates.",Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy-L-rhamnonate (KDR).,Yes,Yes,Yes,Yes,Yes,Yes,GO:0050032; GO:0000287,GO:0016836,GO:0016836,GO:0016836,GO:0016836,GO:0016836,0.6027,0.6027,0.6027,0.6027,0.6027,5,0.6027,0.2119,no
RHMD_SPHSS,Q1NEI8,Prot2Text,Bacteria,397,"Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy- L-rhamnonate (KDR). Also shows activity with L- lyxonate and L-mannonate, with much lower catalytic efficiency. Catalyzes the third step in an alternative pathway for rhamnose utilization that does not involve phosphorylated intermediates.",Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy-L-rhamnonate (KDR).,Yes,Yes,Yes,Yes,Yes,Yes,GO:0050032; GO:0000287,GO:0016836,GO:0016836,GO:0016836,GO:0016836,GO:0034484,0.6027,0.6027,0.6027,0.6027,0.0,5,0.4822,0.2119,no
RHMD_SPHSS,Q1NEI8,ProtT3,Bacteria,397,"Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy- L-rhamnonate (KDR). Also shows activity with L- lyxonate and L-mannonate, with much lower catalytic efficiency. Catalyzes the third step in an alternative pathway for rhamnose utilization that does not involve phosphorylated intermediates.",Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy- L-rhamnonate (KDR). Belongs to the mandelate racemase/muconate lactonizing enzyme family. RhamD subfamily,Yes,Yes,Yes,Yes,Yes,Yes,GO:0050032; GO:0000287,GO:0016836,GO:0016836,GO:0016836,GO:0016836,GO:0016836,0.6027,0.6027,0.6027,0.6027,0.6027,5,0.6027,0.2119,no
RHMD_SPHSS,Q1NEI8,ProtTale,Bacteria,397,"Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy- L-rhamnonate (KDR). Also shows activity with L- lyxonate and L-mannonate, with much lower catalytic efficiency. Catalyzes the third step in an alternative pathway for rhamnose utilization that does not involve phosphorylated intermediates.","Isomerase that catalyzes the reversible interconversion of alpha-D-glucose 1-phosphate (Glc-1-P) and beta-D-glucose 1-phosphate (Glc-1-P). Is required for the maintenance of glucose homeostasis. Is also able to act as a D-gluconol-1-phosphate isomerase (D-gluconol-1-P isomerase), but this activity is very low and it is unlikely to play a physiological role in vivo.",No,No,No,No,No,not-Yes,GO:0050032; GO:0000287,GO:0016853,GO:0016853,GO:0016853,GO:0016853,GO:0016853,0.2839,0.2839,0.2839,0.2839,0.2839,5,0.2839,0.2119,no
RHMD_SPHSS,Q1NEI8,Protein2Text,Bacteria,397,"Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy- L-rhamnonate (KDR). Also shows activity with L- lyxonate and L-mannonate, with much lower catalytic efficiency. Catalyzes the third step in an alternative pathway for rhamnose utilization that does not involve phosphorylated intermediates.","This protein is involved in the hydrolysis of methylglyoxal, a toxic metabolite. It is likely involved in detoxifying methylglyoxal and preventing its harmful effects on the cell.",No,No,No,No,No,not-Yes,GO:0050032; GO:0000287,GO:0019172,GO:0016787,GO:0016787,GO:0019172,,0.5117,0.2839,0.2839,0.5117,,4,0.3978,0.2119,no
RHMD_SPHSS,Q1NEI8,Reference,Bacteria,397,"Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy- L-rhamnonate (KDR). Also shows activity with L- lyxonate and L-mannonate, with much lower catalytic efficiency. Catalyzes the third step in an alternative pathway for rhamnose utilization that does not involve phosphorylated intermediates.","Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy- L-rhamnonate (KDR). Also shows activity with L- lyxonate and L-mannonate, with much lower catalytic efficiency. Catalyzes the third step in an alternative pathway for rhamnose utilization that does not involve phosphorylated intermediates.",,,,,,,GO:0050032; GO:0000287,GO:0016836,GO:0016836,GO:0016836,GO:0016836,GO:0016836,0.6027,0.6027,0.6027,0.6027,0.6027,5,0.6027,0.2119,no
RPA2_CAEEL,Q27493,ESM2Text,Eukaryota,1127,"DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol I is composed of mobile elements and RPA2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft. Specifically binds to 18S, 5.8S and 26S rDNA, but not to 5S rDNA.",DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms the clamp head domain.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003677; GO:0003899; GO:0032549,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899; GO:0003677,0.541,0.541,0.541,0.541,0.8556,5,0.6039,0.5098,no
RPA2_CAEEL,Q27493,Prot2Text,Eukaryota,1127,"DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol I is composed of mobile elements and RPA2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft. Specifically binds to 18S, 5.8S and 26S rDNA, but not to 5S rDNA.",Essential for the completion of the three rounds of mitosis in female megaspores required for the development of mature gametophytes.,Vague,No,No,Yes,No,not-Yes,GO:0003677; GO:0003899; GO:0032549,,,,,,,,,,,0,,0.5098,no
RPA2_CAEEL,Q27493,ProtT3,Eukaryota,1127,"DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol I is composed of mobile elements and RPA2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft. Specifically binds to 18S, 5.8S and 26S rDNA, but not to 5S rDNA.",DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Cytoplasm. Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA polymerase subunit family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003677; GO:0003899; GO:0032549,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.541,0.541,0.541,0.541,0.541,5,0.541,0.5098,no
RPA2_CAEEL,Q27493,ProtTale,Eukaryota,1127,"DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol I is composed of mobile elements and RPA2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft. Specifically binds to 18S, 5.8S and 26S rDNA, but not to 5S rDNA.",DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003677; GO:0003899; GO:0032549,GO:0003899,GO:0003899; GO:0003677,GO:0003899; GO:0003677,GO:0003899; GO:0003677,GO:0003899,0.541,0.8556,0.8556,0.8556,0.541,5,0.7298,0.5098,no
RPA2_CAEEL,Q27493,Protein2Text,Eukaryota,1127,"DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol I is composed of mobile elements and RPA2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft. Specifically binds to 18S, 5.8S and 26S rDNA, but not to 5S rDNA.",The molecular function of the protein is RNA-directed DNA polymerase.,No,No,No,No,No,not-Yes,GO:0003677; GO:0003899; GO:0032549,GO:0003964,GO:0003964,GO:0003964,GO:0003964,GO:0003964,0.2865,0.2865,0.2865,0.2865,0.2865,5,0.2865,0.5098,no
RPA2_CAEEL,Q27493,Reference,Eukaryota,1127,"DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol I is composed of mobile elements and RPA2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft. Specifically binds to 18S, 5.8S and 26S rDNA, but not to 5S rDNA.","DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol I is composed of mobile elements and RPA2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft. Specifically binds to 18S, 5.8S and 26S rDNA, but not to 5S rDNA.",,,,,,,GO:0003677; GO:0003899; GO:0032549,GO:0003899; GO:0003677,GO:0003899; GO:0003677,GO:0003899; GO:0003677,GO:0003899; GO:0003677,GO:0003899; GO:0003677,0.8556,0.8556,0.8556,0.8556,0.8556,5,0.8556,0.5098,no
MNMM_STAA8,Q2FXG9,ESM2Text,Bacteria,187,Involved in the biosynthesis of 5-methylaminomethyl-2- thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the transfer of a methyl group from S- adenosyl-L-methionine to nm(5)s(2)U34 to form mnm(5)s(2)U34.,Specifically methylates the adenine in position 2030 of 23S rRNA.,Maybe,No,No,No,No,not-Yes,GO:0004808,GO:0008649,GO:0008649,GO:0008171,GO:0008173,GO:0008649,0.6607,0.6607,0.4465,0.699,0.6607,5,0.6255,0.4696,no
MNMM_STAA8,Q2FXG9,Prot2Text,Bacteria,187,Involved in the biosynthesis of 5-methylaminomethyl-2- thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the transfer of a methyl group from S- adenosyl-L-methionine to nm(5)s(2)U34 to form mnm(5)s(2)U34.,Specifically methylates the adenine in position 1618 of 23S rRNA.,Maybe,No,No,No,No,not-Yes,GO:0004808,GO:0008649,GO:0008649,GO:0008649,GO:0008649,GO:0008649,0.6607,0.6607,0.6607,0.6607,0.6607,5,0.6607,0.4696,no
MNMM_STAA8,Q2FXG9,ProtT3,Bacteria,187,Involved in the biosynthesis of 5-methylaminomethyl-2- thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the transfer of a methyl group from S- adenosyl-L-methionine to nm(5)s(2)U34 to form mnm(5)s(2)U34.,Could be a S-adenosyl-L-methionine-dependent methyltransferase. Belongs to the methyltransferase superfamily,Vague,Maybe,Vague,Vague,Vague,not-Yes,GO:0004808,,GO:0008168,GO:0008168,GO:0008757,GO:0008168,,0.5243,0.5243,0.6125,0.5243,4,0.5464,0.4696,no
MNMM_STAA8,Q2FXG9,ProtTale,Bacteria,187,Involved in the biosynthesis of 5-methylaminomethyl-2- thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the transfer of a methyl group from S- adenosyl-L-methionine to nm(5)s(2)U34 to form mnm(5)s(2)U34.,Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.,No,No,No,No,No,not-Yes,GO:0004808,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.5243,0.5243,0.5243,0.5243,0.5243,5,0.5243,0.4696,no
MNMM_STAA8,Q2FXG9,Protein2Text,Bacteria,187,Involved in the biosynthesis of 5-methylaminomethyl-2- thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the transfer of a methyl group from S- adenosyl-L-methionine to nm(5)s(2)U34 to form mnm(5)s(2)U34.,"The molecular function of this protein is a methyltransferase.
It is involved in the methylation of the ribosomal RNA, specifically at position 2' of the guanosine residue at position 1191 of the 23S rRNA.",Maybe,Vague,Vague,Vague,Vague,not-Yes,GO:0004808,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008649,0.5243,0.5243,0.5243,0.5243,0.6607,5,0.5516,0.4696,no
MNMM_STAA8,Q2FXG9,Reference,Bacteria,187,Involved in the biosynthesis of 5-methylaminomethyl-2- thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the transfer of a methyl group from S- adenosyl-L-methionine to nm(5)s(2)U34 to form mnm(5)s(2)U34.,Involved in the biosynthesis of 5-methylaminomethyl-2- thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the transfer of a methyl group from S- adenosyl-L-methionine to nm(5)s(2)U34 to form mnm(5)s(2)U34.,,,,,,,GO:0004808,GO:0008168,GO:0008173,GO:0008175,GO:0008173,GO:0008173,0.5243,0.699,0.8031,0.699,0.699,5,0.6849,0.4696,no
MCP3_TRYB2,Q38CB5,ESM2Text,Eukaryota,261,"Promiscuous robust Ala-tRNA deacylase that lacks tRNA discrimination. Deacylates mischarged Ala-tRNA(Pro), Ala-tRNA(Leu) and cognate Ala-tRNA(Ala) with similar efficiencies; more slowly deacylates Ala-tRNA(Thr) and Ala- tRNA(Trp). Uses a size-exclusion based mechanism for deacylation and discriminates against larger amino acids: moderately hydrolyzes Ser-tRNA(Pro) and Gly-tRNA(Pro) and is unable to edit Leu- tRNA(Pro).","Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Inhibits the GDP/GTP exchange factor (GDI) activity of RhoA and stimulates its dissociation from it, the rate of GTP hydrolysis and the dissociation of GDP from it. Involved in the modulation of the actin cytoskeleton reorganization associated with infection by microorganisms.",No,No,No,No,No,not-Yes,GO:0002161,GO:0005094,GO:0005094,GO:0005094,GO:0005094,GO:0005094,0.0716,0.0716,0.0716,0.0716,0.0716,5,0.0716,0.1605,no
MCP3_TRYB2,Q38CB5,Prot2Text,Eukaryota,261,"Promiscuous robust Ala-tRNA deacylase that lacks tRNA discrimination. Deacylates mischarged Ala-tRNA(Pro), Ala-tRNA(Leu) and cognate Ala-tRNA(Ala) with similar efficiencies; more slowly deacylates Ala-tRNA(Thr) and Ala- tRNA(Trp). Uses a size-exclusion based mechanism for deacylation and discriminates against larger amino acids: moderately hydrolyzes Ser-tRNA(Pro) and Gly-tRNA(Pro) and is unable to edit Leu- tRNA(Pro).",Overexpression impairs serum-induced cell cycle progression from the G0/G1 to S phase.,Vague,No,No,No,No,not-Yes,GO:0002161,,,,,,,,,,,0,,0.1605,no
MCP3_TRYB2,Q38CB5,ProtT3,Eukaryota,261,"Promiscuous robust Ala-tRNA deacylase that lacks tRNA discrimination. Deacylates mischarged Ala-tRNA(Pro), Ala-tRNA(Leu) and cognate Ala-tRNA(Ala) with similar efficiencies; more slowly deacylates Ala-tRNA(Thr) and Ala- tRNA(Trp). Uses a size-exclusion based mechanism for deacylation and discriminates against larger amino acids: moderately hydrolyzes Ser-tRNA(Pro) and Gly-tRNA(Pro) and is unable to edit Leu- tRNA(Pro).",Catalyzes the attachment of asparagine to tRNA(Asn) in a two- step reaction: asparagine is first activated by ATP to form Asn-AMP and then transferred to the acceptor end of tRNA(Asn). Also edits incorrectly charged tRNA(Asn) via its editing domain. Cytoplasm. Belongs to the class-II aminoacyl-tRNA synthetase family,No,No,No,Maybe,No,not-Yes,GO:0002161,GO:0004816; GO:0005524,GO:0004816; GO:0005524,GO:0004816; GO:0005524,GO:0004816; GO:0005524,GO:0004816; GO:0005524,0.3162,0.3162,0.3162,0.3162,0.3162,5,0.3162,0.1605,no
MCP3_TRYB2,Q38CB5,ProtTale,Eukaryota,261,"Promiscuous robust Ala-tRNA deacylase that lacks tRNA discrimination. Deacylates mischarged Ala-tRNA(Pro), Ala-tRNA(Leu) and cognate Ala-tRNA(Ala) with similar efficiencies; more slowly deacylates Ala-tRNA(Thr) and Ala- tRNA(Trp). Uses a size-exclusion based mechanism for deacylation and discriminates against larger amino acids: moderately hydrolyzes Ser-tRNA(Pro) and Gly-tRNA(Pro) and is unable to edit Leu- tRNA(Pro).",Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes,No,No,No,No,No,not-Yes,GO:0002161,GO:0016887,GO:0005524; GO:0016887,GO:0005524; GO:0016887,GO:0005524; GO:0016887,GO:0016887,0.23,0.172,0.172,0.172,0.23,5,0.1952,0.1605,no
MCP3_TRYB2,Q38CB5,Protein2Text,Eukaryota,261,"Promiscuous robust Ala-tRNA deacylase that lacks tRNA discrimination. Deacylates mischarged Ala-tRNA(Pro), Ala-tRNA(Leu) and cognate Ala-tRNA(Ala) with similar efficiencies; more slowly deacylates Ala-tRNA(Thr) and Ala- tRNA(Trp). Uses a size-exclusion based mechanism for deacylation and discriminates against larger amino acids: moderately hydrolyzes Ser-tRNA(Pro) and Gly-tRNA(Pro) and is unable to edit Leu- tRNA(Pro).",The molecular function of this protein is an O-methylthreonine synthase. It catalyzes the O-methylation of threonine to O-methylthreonine.,No,No,No,No,No,not-Yes,GO:0002161,GO:0008168,GO:0008168,GO:0008171,GO:0008168,GO:0008168,0.2029,0.2029,0.1792,0.2029,0.2029,5,0.1982,0.1605,no
MCP3_TRYB2,Q38CB5,Reference,Eukaryota,261,"Promiscuous robust Ala-tRNA deacylase that lacks tRNA discrimination. Deacylates mischarged Ala-tRNA(Pro), Ala-tRNA(Leu) and cognate Ala-tRNA(Ala) with similar efficiencies; more slowly deacylates Ala-tRNA(Thr) and Ala- tRNA(Trp). Uses a size-exclusion based mechanism for deacylation and discriminates against larger amino acids: moderately hydrolyzes Ser-tRNA(Pro) and Gly-tRNA(Pro) and is unable to edit Leu- tRNA(Pro).","Promiscuous robust Ala-tRNA deacylase that lacks tRNA discrimination. Deacylates mischarged Ala-tRNA(Pro), Ala-tRNA(Leu) and cognate Ala-tRNA(Ala) with similar efficiencies; more slowly deacylates Ala-tRNA(Thr) and Ala- tRNA(Trp). Uses a size-exclusion based mechanism for deacylation and discriminates against larger amino acids: moderately hydrolyzes Ser-tRNA(Pro) and Gly-tRNA(Pro) and is unable to edit Leu- tRNA(Pro).",,,,,,,GO:0002161,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0002161,0.4415,0.4415,0.4415,0.4415,1.0,5,0.5532,0.1605,no
CH1CO_GEOMG,Q39QF5,ESM2Text,Bacteria,380,"Acyl-CoA dehydrogenase involved in the anaerobic degradation of cyclohexane carboxylic acid (CHC). Catalyzes the 1,4-dehydrogenation at C3 and C6 of cyclohex-1-ene-1-carbonyl-CoA (CHeneCoA or Ch1CoA) to cyclohexa-1,5-diene-1-carbonyl-CoA (CHdieneCoA or Ch1,5CoA). Also able to catalyze, at a lower rate, the dehydrogenation at C3 and C4 of CHdieneCoA to benzoyl-CoA.",Involved in the degradation of long-chain fatty acids.,Vague,No,Vague,No,Vague,not-Yes,GO:0003995; GO:0050660,,,,,,,,,,,0,,0.1478,no
CH1CO_GEOMG,Q39QF5,Prot2Text,Bacteria,380,"Acyl-CoA dehydrogenase involved in the anaerobic degradation of cyclohexane carboxylic acid (CHC). Catalyzes the 1,4-dehydrogenation at C3 and C6 of cyclohex-1-ene-1-carbonyl-CoA (CHeneCoA or Ch1CoA) to cyclohexa-1,5-diene-1-carbonyl-CoA (CHdieneCoA or Ch1,5CoA). Also able to catalyze, at a lower rate, the dehydrogenation at C3 and C4 of CHdieneCoA to benzoyl-CoA.",Involved in the first cycle of side chain dehydrogenation in the beta-oxidation of cholesterol catabolism. It contributes partly to the virulence by increasing the efficiency of beta-oxidation. Catalyzes the dehydrogenation of carbon 31 (22S)-oxidation to yield carbon 6a (22R)-7a-hydroxycholesterol. It can also use octanoyl-CoA and dihydroferuloyl-CoA as substrate.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0003995; GO:0050660,GO:0003995,GO:0003995,GO:0003995,GO:0003995,GO:0003995,0.6922,0.6922,0.6922,0.6922,0.6922,5,0.6922,0.1478,no
CH1CO_GEOMG,Q39QF5,ProtT3,Bacteria,380,"Acyl-CoA dehydrogenase involved in the anaerobic degradation of cyclohexane carboxylic acid (CHC). Catalyzes the 1,4-dehydrogenation at C3 and C6 of cyclohex-1-ene-1-carbonyl-CoA (CHeneCoA or Ch1CoA) to cyclohexa-1,5-diene-1-carbonyl-CoA (CHdieneCoA or Ch1,5CoA). Also able to catalyze, at a lower rate, the dehydrogenation at C3 and C4 of CHdieneCoA to benzoyl-CoA.",Belongs to the acyl-CoA dehydrogenase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0003995; GO:0050660,GO:0003995,GO:0003995,GO:0003995,GO:0003995,GO:0003995,0.6922,0.6922,0.6922,0.6922,0.6922,5,0.6922,0.1478,no
CH1CO_GEOMG,Q39QF5,ProtTale,Bacteria,380,"Acyl-CoA dehydrogenase involved in the anaerobic degradation of cyclohexane carboxylic acid (CHC). Catalyzes the 1,4-dehydrogenation at C3 and C6 of cyclohex-1-ene-1-carbonyl-CoA (CHeneCoA or Ch1CoA) to cyclohexa-1,5-diene-1-carbonyl-CoA (CHdieneCoA or Ch1,5CoA). Also able to catalyze, at a lower rate, the dehydrogenation at C3 and C4 of CHdieneCoA to benzoyl-CoA.",Catalyzes the reduction of crotonobetainyl-CoA to gamma- butyrobetainyl-CoA.,No,No,No,No,No,not-Yes,GO:0003995; GO:0050660,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.443,0.443,0.443,0.443,0.443,5,0.443,0.1478,no
CH1CO_GEOMG,Q39QF5,Protein2Text,Bacteria,380,"Acyl-CoA dehydrogenase involved in the anaerobic degradation of cyclohexane carboxylic acid (CHC). Catalyzes the 1,4-dehydrogenation at C3 and C6 of cyclohex-1-ene-1-carbonyl-CoA (CHeneCoA or Ch1CoA) to cyclohexa-1,5-diene-1-carbonyl-CoA (CHdieneCoA or Ch1,5CoA). Also able to catalyze, at a lower rate, the dehydrogenation at C3 and C4 of CHdieneCoA to benzoyl-CoA.","This protein is involved in catalyzing the oxidation of isovaleryl-CoA to 3-methylcrotonyl-CoA, which is a step in the metabolism of branched-chain amino acids. It is a member of the short-chain dehydrogenases/reductases (SDR) superfamily.",Maybe,No,No,No,Maybe,not-Yes,GO:0003995; GO:0050660,GO:0003995,GO:0016491,GO:0016491,GO:0003995,GO:0003995,0.6922,0.443,0.443,0.6922,0.6922,5,0.5925,0.1478,no
CH1CO_GEOMG,Q39QF5,Reference,Bacteria,380,"Acyl-CoA dehydrogenase involved in the anaerobic degradation of cyclohexane carboxylic acid (CHC). Catalyzes the 1,4-dehydrogenation at C3 and C6 of cyclohex-1-ene-1-carbonyl-CoA (CHeneCoA or Ch1CoA) to cyclohexa-1,5-diene-1-carbonyl-CoA (CHdieneCoA or Ch1,5CoA). Also able to catalyze, at a lower rate, the dehydrogenation at C3 and C4 of CHdieneCoA to benzoyl-CoA.","Acyl-CoA dehydrogenase involved in the anaerobic degradation of cyclohexane carboxylic acid (CHC). Catalyzes the 1,4-dehydrogenation at C3 and C6 of cyclohex-1-ene-1-carbonyl-CoA (CHeneCoA or Ch1CoA) to cyclohexa-1,5-diene-1-carbonyl-CoA (CHdieneCoA or Ch1,5CoA). Also able to catalyze, at a lower rate, the dehydrogenation at C3 and C4 of CHdieneCoA to benzoyl-CoA.",,,,,,,GO:0003995; GO:0050660,GO:0003995,GO:0003995,GO:0003995,GO:0003995,GO:0003995,0.6922,0.6922,0.6922,0.6922,0.6922,5,0.6922,0.1478,no
SCHCT_GEOMG,Q39QF7,ESM2Text,Bacteria,437,"Acyl-CoA transferase involved in the anaerobic degradation of cyclohexane carboxylic acid (CHC). Catalyzes the activation of CHC to cyclohexane-1-carbonyl-CoA (CHCoA). Benzoic acid and cyclohex-1-ene-1-carboxylic acid can also be used as substrates, but with lower specific activity. Shows highest activity with succinyl-CoA and butanoyl-coA as a CoA donor, and lower activity with crotonyl-CoA, acetyl-CoA, glutaryl-CoA, CH1eneCoA, propionyl-CoA and acetoacetyl-CoA. In vitro, the enzyme can use butanoyl-coA as a CoA donor with greater efficiency than succinyl-CoA. However, succinyl-CoA is the most abundant CoA ester in exponentially grown cells, whereas butanoyl-coA is hardly detectable, indicating that succinyl-CoA is the natural CoA donor for CHC activation.",Coenzyme A-transferase that converts butyryl-CoA to butyrate. Can also use proprionyl-CoA as substrate.,Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0008775,GO:0008410,GO:0008410,GO:0008260,GO:0008410,GO:0008410,0.8582,0.8582,0.7289,0.8582,0.8582,5,0.8323,0.6302,yes
SCHCT_GEOMG,Q39QF7,Prot2Text,Bacteria,437,"Acyl-CoA transferase involved in the anaerobic degradation of cyclohexane carboxylic acid (CHC). Catalyzes the activation of CHC to cyclohexane-1-carbonyl-CoA (CHCoA). Benzoic acid and cyclohex-1-ene-1-carboxylic acid can also be used as substrates, but with lower specific activity. Shows highest activity with succinyl-CoA and butanoyl-coA as a CoA donor, and lower activity with crotonyl-CoA, acetyl-CoA, glutaryl-CoA, CH1eneCoA, propionyl-CoA and acetoacetyl-CoA. In vitro, the enzyme can use butanoyl-coA as a CoA donor with greater efficiency than succinyl-CoA. However, succinyl-CoA is the most abundant CoA ester in exponentially grown cells, whereas butanoyl-coA is hardly detectable, indicating that succinyl-CoA is the natural CoA donor for CHC activation.","Cobalamin-dependent dioxygenase that catalyzes the conversion of coenzyme B (CoB) to 7-cyano-7-deazaguanine (preQ0)-dependent 7-deazapurine (preQ1), a precursor for the biosynthesis of the quinoline moiety of thymidylate. Can also use benzylsuccinate as substrate.",No,No,No,No,No,not-Yes,GO:0008775,,,,,,,,,,,0,,0.6302,yes
SCHCT_GEOMG,Q39QF7,ProtT3,Bacteria,437,"Acyl-CoA transferase involved in the anaerobic degradation of cyclohexane carboxylic acid (CHC). Catalyzes the activation of CHC to cyclohexane-1-carbonyl-CoA (CHCoA). Benzoic acid and cyclohex-1-ene-1-carboxylic acid can also be used as substrates, but with lower specific activity. Shows highest activity with succinyl-CoA and butanoyl-coA as a CoA donor, and lower activity with crotonyl-CoA, acetyl-CoA, glutaryl-CoA, CH1eneCoA, propionyl-CoA and acetoacetyl-CoA. In vitro, the enzyme can use butanoyl-coA as a CoA donor with greater efficiency than succinyl-CoA. However, succinyl-CoA is the most abundant CoA ester in exponentially grown cells, whereas butanoyl-coA is hardly detectable, indicating that succinyl-CoA is the natural CoA donor for CHC activation.",Belongs to the acetyl-CoA hydrolase/transferase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008775,,GO:0016746,,,,,0.482,,,,1,0.482,0.6302,yes
SCHCT_GEOMG,Q39QF7,ProtTale,Bacteria,437,"Acyl-CoA transferase involved in the anaerobic degradation of cyclohexane carboxylic acid (CHC). Catalyzes the activation of CHC to cyclohexane-1-carbonyl-CoA (CHCoA). Benzoic acid and cyclohex-1-ene-1-carboxylic acid can also be used as substrates, but with lower specific activity. Shows highest activity with succinyl-CoA and butanoyl-coA as a CoA donor, and lower activity with crotonyl-CoA, acetyl-CoA, glutaryl-CoA, CH1eneCoA, propionyl-CoA and acetoacetyl-CoA. In vitro, the enzyme can use butanoyl-coA as a CoA donor with greater efficiency than succinyl-CoA. However, succinyl-CoA is the most abundant CoA ester in exponentially grown cells, whereas butanoyl-coA is hardly detectable, indicating that succinyl-CoA is the natural CoA donor for CHC activation.",Catalyzes the reversible acetyl-coenzyme A (acetyl-CoA)-dependent acetylation and decarboxylation of 2'-deoxyribonucleoside 5'-monophosphates (NMP). Catalyzes the decarboxylation of 2'-deoxyribonucleoside 5'-triphosphate. Exhibits acetyl-CoA-dependent NMP acetyltransferase activity in vitro. Exhibits acetyl-CoA-dependent NMP acetyltransferase activity in vitro. Exhibits acetyl-CoA-dependent NMP acetyltransferase activity in vitro. Exhibits acetyl-CoA-dependent NMP acetyltransferase activity in vitro. Exhibits acetyl-,No,No,No,No,No,not-Yes,GO:0008775,GO:0016407,GO:0016747; GO:0016831,GO:0016747; GO:0016831,GO:0016747,GO:0016407,0.3386,0.3442,0.3442,0.3987,0.3386,5,0.3529,0.6302,yes
SCHCT_GEOMG,Q39QF7,Protein2Text,Bacteria,437,"Acyl-CoA transferase involved in the anaerobic degradation of cyclohexane carboxylic acid (CHC). Catalyzes the activation of CHC to cyclohexane-1-carbonyl-CoA (CHCoA). Benzoic acid and cyclohex-1-ene-1-carboxylic acid can also be used as substrates, but with lower specific activity. Shows highest activity with succinyl-CoA and butanoyl-coA as a CoA donor, and lower activity with crotonyl-CoA, acetyl-CoA, glutaryl-CoA, CH1eneCoA, propionyl-CoA and acetoacetyl-CoA. In vitro, the enzyme can use butanoyl-coA as a CoA donor with greater efficiency than succinyl-CoA. However, succinyl-CoA is the most abundant CoA ester in exponentially grown cells, whereas butanoyl-coA is hardly detectable, indicating that succinyl-CoA is the natural CoA donor for CHC activation.","The molecular function of the protein is an aldolase, which is a type of enzyme that catalyzes the reversible aldol condensation reaction between an aldehyde and a ketone to form a beta-hydroxy aldehyde or ketone. In this case, it is likely involved in the breakdown of a sugar molecule. Aldolases are important in various metabolic pathways, including glycolysis and the pentose phosphate pathway.",Vague,No,No,No,No,not-Yes,GO:0008775,GO:0004332,GO:0004332,GO:0004332,GO:0004332,GO:0016832,0.1998,0.1998,0.1998,0.1998,0.2353,5,0.2069,0.6302,yes
SCHCT_GEOMG,Q39QF7,Reference,Bacteria,437,"Acyl-CoA transferase involved in the anaerobic degradation of cyclohexane carboxylic acid (CHC). Catalyzes the activation of CHC to cyclohexane-1-carbonyl-CoA (CHCoA). Benzoic acid and cyclohex-1-ene-1-carboxylic acid can also be used as substrates, but with lower specific activity. Shows highest activity with succinyl-CoA and butanoyl-coA as a CoA donor, and lower activity with crotonyl-CoA, acetyl-CoA, glutaryl-CoA, CH1eneCoA, propionyl-CoA and acetoacetyl-CoA. In vitro, the enzyme can use butanoyl-coA as a CoA donor with greater efficiency than succinyl-CoA. However, succinyl-CoA is the most abundant CoA ester in exponentially grown cells, whereas butanoyl-coA is hardly detectable, indicating that succinyl-CoA is the natural CoA donor for CHC activation.","Acyl-CoA transferase involved in the anaerobic degradation of cyclohexane carboxylic acid (CHC). Catalyzes the activation of CHC to cyclohexane-1-carbonyl-CoA (CHCoA). Benzoic acid and cyclohex-1-ene-1-carboxylic acid can also be used as substrates, but with lower specific activity. Shows highest activity with succinyl-CoA and butanoyl-coA as a CoA donor, and lower activity with crotonyl-CoA, acetyl-CoA, glutaryl-CoA, CH1eneCoA, propionyl-CoA and acetoacetyl-CoA. In vitro, the enzyme can use butanoyl-coA as a CoA donor with greater efficiency than succinyl-CoA. However, succinyl-CoA is the most abundant CoA ester in exponentially grown cells, whereas butanoyl-coA is hardly detectable, indicating that succinyl-CoA is the natural CoA donor for CHC activation.",,,,,,,GO:0008775,GO:0008775,GO:0008410,GO:0008410,GO:0008410,GO:0008410,1.0,0.8582,0.8582,0.8582,0.8582,5,0.8866,0.6302,yes
DMDH_ENTFD,Q3Y316,ESM2Text,Bacteria,312,"Catalyzes the reduction of benzoylformate (also named phenylglyoxylate) to (R)-mandelate (also named D-mandelate) using NADH as an electron donor. Has broad substrate specificity in vitro, showing activities towards a range of 2-ketoacid substrates, including 2-ketoisovalerate (also named 3-methyl-2-oxobutanoate), 2- ketocaproate (also named 2-oxohexanoate), and 3-phenylpyruvate.",Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.,Maybe,No,No,No,Maybe,not-Yes,GO:0008677; GO:0050661,GO:0008677,GO:0008677,GO:0008677,GO:0008677,GO:0008677,0.6901,0.6901,0.6901,0.6901,0.6901,5,0.6901,0.2014,no
DMDH_ENTFD,Q3Y316,Prot2Text,Bacteria,312,"Catalyzes the reduction of benzoylformate (also named phenylglyoxylate) to (R)-mandelate (also named D-mandelate) using NADH as an electron donor. Has broad substrate specificity in vitro, showing activities towards a range of 2-ketoacid substrates, including 2-ketoisovalerate (also named 3-methyl-2-oxobutanoate), 2- ketocaproate (also named 2-oxohexanoate), and 3-phenylpyruvate.",Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.,Maybe,No,No,No,Maybe,not-Yes,GO:0008677; GO:0050661,GO:0008677,GO:0008677,GO:0008677,GO:0008677,GO:0008677,0.6901,0.6901,0.6901,0.6901,0.6901,5,0.6901,0.2014,no
DMDH_ENTFD,Q3Y316,ProtT3,Bacteria,312,"Catalyzes the reduction of benzoylformate (also named phenylglyoxylate) to (R)-mandelate (also named D-mandelate) using NADH as an electron donor. Has broad substrate specificity in vitro, showing activities towards a range of 2-ketoacid substrates, including 2-ketoisovalerate (also named 3-methyl-2-oxobutanoate), 2- ketocaproate (also named 2-oxohexanoate), and 3-phenylpyruvate.",Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid. Cytoplasm. Belongs to the ketopantoate reductase family,Maybe,No,No,No,Maybe,not-Yes,GO:0008677; GO:0050661,GO:0008677,GO:0008677,GO:0008677,GO:0008677,GO:0008677,0.6901,0.6901,0.6901,0.6901,0.6901,5,0.6901,0.2014,no
DMDH_ENTFD,Q3Y316,ProtTale,Bacteria,312,"Catalyzes the reduction of benzoylformate (also named phenylglyoxylate) to (R)-mandelate (also named D-mandelate) using NADH as an electron donor. Has broad substrate specificity in vitro, showing activities towards a range of 2-ketoacid substrates, including 2-ketoisovalerate (also named 3-methyl-2-oxobutanoate), 2- ketocaproate (also named 2-oxohexanoate), and 3-phenylpyruvate.",Catalyzes the NAD(P)H-dependent reduction of ketopantoate into pantoic acid.,Maybe,No,No,No,Maybe,not-Yes,GO:0008677; GO:0050661,GO:0008677,GO:0016491; GO:0050661,GO:0016491; GO:0050661,GO:0016491; GO:0008677,GO:0008677,0.6901,0.801,0.801,0.6821,0.6901,5,0.7329,0.2014,no
DMDH_ENTFD,Q3Y316,Protein2Text,Bacteria,312,"Catalyzes the reduction of benzoylformate (also named phenylglyoxylate) to (R)-mandelate (also named D-mandelate) using NADH as an electron donor. Has broad substrate specificity in vitro, showing activities towards a range of 2-ketoacid substrates, including 2-ketoisovalerate (also named 3-methyl-2-oxobutanoate), 2- ketocaproate (also named 2-oxohexanoate), and 3-phenylpyruvate.","The molecular function of this protein is an epimerase.
            It catalyzes the epimerization of D-glucuronate to D-xylosate in the biosynthesis of D-glucuronate. The D-glucuronate is produced via the D-glucuronate pathway which involves the conversion of D-glucose to D-glucuronate. In this pathway, D-glucose is converted to D-glucuronate in a two-step process. The first step is the oxidation of D-glucose to D-gluconate by glucose oxidase, followed by the conversion of D-gluconate to D-glucuronate by the epimerase reaction catalyzed by this protein. The D-glucuronate is then converted to D-glucuronate-6-phosphate via the action of glucuronate kinase, and D-glucuronate-6-phosphate is then converted to UDP-D-glucuronate via the action of UDP-glucuronic acid pyrophosphorylase. The UDP-D-glucuronate is then used in the biosynthesis of glycosaminoglycans such as chondroitin and heparan sulfate. The glycosaminoglycans are then used in various biological processes such as cell signaling, cell adhesion, and the maintenance of the extracellular matrix. The glycosaminoglycans also play important roles in various diseases such as cancer and arthritis.
           The D-glucuronate pathway is an important pathway in the biosynthesis of glycosaminoglycans, which play important roles in various biological processes and diseases. The D-glucuronate pathway is also an important pathway in the biosynthesis of D-glucuronate, which is used in the biosynthesis of glycosaminoglycans. The epimerase reaction catalyzed by this protein is an important step in the biosynthesis of D-glucuronate, and the protein plays an important role in the biosynthesis of D-glucuronate.
           In addition to its role in the biosynthesis of D-glucuronate, the protein also plays a role in the regulation of the biosynthesis of glycosaminoglycans. The protein is also involved in the regulation of the biosynthesis of D-glucuronate-6-phosphate and UDP-D-glucuronate. The protein also plays a role in the regulation of the biosynthesis of glycosaminoglycans such as chond",No,No,No,No,No,not-Yes,GO:0008677; GO:0050661,GO:0016857,GO:0016854,GO:0016854,GO:0016857,,0.1847,0.2234,0.2234,0.1847,,4,0.2041,0.2014,no
DMDH_ENTFD,Q3Y316,Reference,Bacteria,312,"Catalyzes the reduction of benzoylformate (also named phenylglyoxylate) to (R)-mandelate (also named D-mandelate) using NADH as an electron donor. Has broad substrate specificity in vitro, showing activities towards a range of 2-ketoacid substrates, including 2-ketoisovalerate (also named 3-methyl-2-oxobutanoate), 2- ketocaproate (also named 2-oxohexanoate), and 3-phenylpyruvate.","Catalyzes the reduction of benzoylformate (also named phenylglyoxylate) to (R)-mandelate (also named D-mandelate) using NADH as an electron donor. Has broad substrate specificity in vitro, showing activities towards a range of 2-ketoacid substrates, including 2-ketoisovalerate (also named 3-methyl-2-oxobutanoate), 2- ketocaproate (also named 2-oxohexanoate), and 3-phenylpyruvate.",,,,,,,GO:0008677; GO:0050661,GO:0016616; GO:0051287,GO:0016616,GO:0016491; GO:0051287,GO:0016616,GO:0016616,0.8224,0.5999,0.6943,0.5999,0.5999,5,0.6633,0.2014,no
HJC_SULAC,Q4J8L0,ESM2Text,Archaea,143,"A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination. Cleaves 4-way DNA junctions introducing paired nicks in opposing strands, leaving a 5'-terminal phosphate and a 3'-terminal hydroxyl group that are ligated to produce recombinant products.","A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination. Cleaves 4-way DNA junctions introducing paired nicks in opposing strands, leaving a 5'-terminal phosphate and a 3'-terminal hydroxyl group that are ligated to produce recombinant products.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008821; GO:0003677; GO:0000287,GO:0008821,GO:0048476,GO:0000287; GO:0048476,GO:0008821; GO:0003677,GO:0008821,0.5363,0.0,0.4617,0.8505,0.5363,5,0.477,0.5507,yes
HJC_SULAC,Q4J8L0,Prot2Text,Archaea,143,"A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination. Cleaves 4-way DNA junctions introducing paired nicks in opposing strands, leaving a 5'-terminal phosphate and a 3'-terminal hydroxyl group that are ligated to produce recombinant products.","A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination. Cleaves 4-way DNA junctions introducing paired nicks in opposing strands, leaving a 5'-terminal phosphate and a 3'-terminal hydroxyl group that are ligated to produce recombinant products. Cleaves both mobile and immobile junctions. Binds 4-way junction DNA, a synthetic Hj, binding is not competed by dsDNA.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008821; GO:0003677; GO:0000287,GO:0004520,GO:0008821,GO:0004519; GO:0003677,GO:0004520,GO:0048476,0.4153,0.5363,0.6674,0.4153,0.0,5,0.4069,0.5507,yes
HJC_SULAC,Q4J8L0,ProtT3,Archaea,143,"A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination. Cleaves 4-way DNA junctions introducing paired nicks in opposing strands, leaving a 5'-terminal phosphate and a 3'-terminal hydroxyl group that are ligated to produce recombinant products.","A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination. Cleaves 4-way DNA junctions introducing paired nicks in opposing strands, leaving a 5'-terminal phosphate and a 3'-terminal hydroxyl group that are ligated to produce recombinant products. Belongs to the Holliday junction resolvase Hjc family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008821; GO:0003677; GO:0000287,GO:0004519; GO:0048476,GO:0004519,GO:0008821,GO:0004520,GO:0008821,0.2645,0.3306,0.5363,0.4153,0.5363,5,0.4166,0.5507,yes
HJC_SULAC,Q4J8L0,ProtTale,Archaea,143,"A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination. Cleaves 4-way DNA junctions introducing paired nicks in opposing strands, leaving a 5'-terminal phosphate and a 3'-terminal hydroxyl group that are ligated to produce recombinant products.","A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination. Cleaves 4-way DNA junctions introducing paired nicks in opposing strands, leaving a 5'-terminal phosphate and a 3'-terminal hydroxyl group that are subsequently ligated to produce recombinant products.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008821; GO:0003677; GO:0000287,GO:0004519,GO:0004520; GO:0003677,GO:0004520; GO:0003677,GO:0004520,GO:0004520,0.3306,0.7489,0.7489,0.4153,0.4153,5,0.5318,0.5507,yes
HJC_SULAC,Q4J8L0,Protein2Text,Archaea,143,"A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination. Cleaves 4-way DNA junctions introducing paired nicks in opposing strands, leaving a 5'-terminal phosphate and a 3'-terminal hydroxyl group that are ligated to produce recombinant products.","This protein is likely involved in DNA replication, as it is a restriction endonuclease. Restriction endonucleases are enzymes that cleave DNA at specific sites, playing a crucial role in the bacterial defense mechanism against foreign DNA. They are composed of two subunits: the recognition subunit, which binds to specific DNA sequences, and the endonuclease subunit, which cleaves the DNA at the recognition site. The molecular function of this protein is likely to be a DNA-binding protein, specifically a restriction endonuclease, which recognizes and cleaves specific DNA sequences. 

Please note that the molecular function of a protein can be determined by its amino acid sequence, and the provided information is based on general knowledge about this type of protein. If you have more specific information about this protein, such as its gene name or sequence, it would be helpful to provide more accurate information.",No,No,Maybe,Maybe,No,not-Yes,GO:0008821; GO:0003677; GO:0000287,GO:0004519; GO:0003677,GO:0004519; GO:0003677,GO:0004519; GO:0003677,GO:0004519; GO:0003677,GO:0004519,0.6674,0.6674,0.6674,0.6674,0.3306,5,0.6,0.5507,yes
HJC_SULAC,Q4J8L0,Reference,Archaea,143,"A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination. Cleaves 4-way DNA junctions introducing paired nicks in opposing strands, leaving a 5'-terminal phosphate and a 3'-terminal hydroxyl group that are ligated to produce recombinant products.","A structure-specific endonuclease that resolves Holliday junction (HJ) intermediates during genetic recombination. Cleaves 4-way DNA junctions introducing paired nicks in opposing strands, leaving a 5'-terminal phosphate and a 3'-terminal hydroxyl group that are ligated to produce recombinant products.",,,,,,,GO:0008821; GO:0003677; GO:0000287,GO:0004520,GO:0048476,GO:0008821,GO:0004520; GO:0048476,GO:0008821,0.4153,0.0,0.5363,0.3322,0.5363,5,0.364,0.5507,yes
END3_SULAC,Q4J8R2,ESM2Text,Archaea,223,"Probably part of a 4-gene DNA damage response locus in which the upstream ups system, in combination with this downstream locus, functions in homologous recombination to rescue Sulfolobales from DNA- damaging threats (Probable). DNA repair enzyme that has both DNA N- glycosylase activity and AP-lyase activity. The DNA N- glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate (Probable). Nicks UV-treated plasmid DNA in a dose-dependent manner, has no activity on untreated DNA.","DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.",Yes,Yes,Yes,Yes,No,Yes,GO:0051539; GO:0140078; GO:0003677; GO:0019104; GO:0046872,GO:0019104; GO:0003906,GO:0019104; GO:0003906,GO:0019104; GO:0003906,GO:0019104,GO:0019104,0.553,0.553,0.553,0.4338,0.4338,5,0.5053,0.6459,yes
END3_SULAC,Q4J8R2,Prot2Text,Archaea,223,"Probably part of a 4-gene DNA damage response locus in which the upstream ups system, in combination with this downstream locus, functions in homologous recombination to rescue Sulfolobales from DNA- damaging threats (Probable). DNA repair enzyme that has both DNA N- glycosylase activity and AP-lyase activity. The DNA N- glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate (Probable). Nicks UV-treated plasmid DNA in a dose-dependent manner, has no activity on untreated DNA.","DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.",Yes,Yes,Yes,Yes,No,Yes,GO:0051539; GO:0140078; GO:0003677; GO:0019104; GO:0046872,GO:0019104; GO:0003906,GO:0019104,GO:0019104,GO:0019104,GO:0019104,0.553,0.4338,0.4338,0.4338,0.4338,5,0.4576,0.6459,yes
END3_SULAC,Q4J8R2,ProtT3,Archaea,223,"Probably part of a 4-gene DNA damage response locus in which the upstream ups system, in combination with this downstream locus, functions in homologous recombination to rescue Sulfolobales from DNA- damaging threats (Probable). DNA repair enzyme that has both DNA N- glycosylase activity and AP-lyase activity. The DNA N- glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate (Probable). Nicks UV-treated plasmid DNA in a dose-dependent manner, has no activity on untreated DNA.","DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. Belongs to the Nth/MutY family",Yes,Yes,Yes,Yes,No,Yes,GO:0051539; GO:0140078; GO:0003677; GO:0019104; GO:0046872,GO:0019104; GO:0003906,GO:0019104; GO:0003906,GO:0019104; GO:0003906,GO:0019104,GO:0019104,0.553,0.553,0.553,0.4338,0.4338,5,0.5053,0.6459,yes
END3_SULAC,Q4J8R2,ProtTale,Archaea,223,"Probably part of a 4-gene DNA damage response locus in which the upstream ups system, in combination with this downstream locus, functions in homologous recombination to rescue Sulfolobales from DNA- damaging threats (Probable). DNA repair enzyme that has both DNA N- glycosylase activity and AP-lyase activity. The DNA N- glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate (Probable). Nicks UV-treated plasmid DNA in a dose-dependent manner, has no activity on untreated DNA.",DNA glycosylase that excises thymine from T/G mismatches and U/G wobble pairs.,Maybe,No,Maybe,No,No,not-Yes,GO:0051539; GO:0140078; GO:0003677; GO:0019104; GO:0046872,GO:0019104,GO:0019104; GO:0003677,GO:0019104; GO:0003677,GO:0019104,GO:0019104,0.4338,0.6995,0.6995,0.4338,0.4338,5,0.5401,0.6459,yes
END3_SULAC,Q4J8R2,Protein2Text,Archaea,223,"Probably part of a 4-gene DNA damage response locus in which the upstream ups system, in combination with this downstream locus, functions in homologous recombination to rescue Sulfolobales from DNA- damaging threats (Probable). DNA repair enzyme that has both DNA N- glycosylase activity and AP-lyase activity. The DNA N- glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate (Probable). Nicks UV-treated plasmid DNA in a dose-dependent manner, has no activity on untreated DNA.","The molecular function of this protein is a DNA repair enzyme, specifically a DNA glycosylase.
This protein is involved in the repair of DNA damage caused by the deamination of cytosine, which leads to the formation of uracil in DNA. The protein removes the uracil base from the DNA strand, allowing for the repair of the damage. 
The molecular function of this protein is to cleave the DNA backbone at the site of the damaged base, allowing for the removal of the damaged base and the repair of the DNA strand. 
This protein is involved in the base excision repair (BER) pathway, which is a major mechanism for repairing DNA damage caused by a variety of mutagenic agents. 
The protein is also involved in the repair of oxidative DNA damage, such as 5-hydroxymethyluracil (5-OH-Ura), which is formed by the oxidation of cytosine by reactive oxygen species. 
The protein is also involved in the repair of other types of DNA damage, such as aldehydes and methylated cytosine. 
The protein is also involved in the repair of DNA damage caused by environmental mutagens, such as ultraviolet light and carcinogens. 
The protein is also involved in the repair of DNA damage caused by errors during DNA replication and recombination. 
The protein is also involved in the repair of DNA damage caused by viral infections, such as human papillomavirus (HPV) and human immunodeficiency virus (HIV). 
The protein is also involved in the repair of DNA damage caused by genetic mutations, such as mutations in the TP53 gene. 
The protein is also involved in the repair of DNA damage caused by epigenetic changes, such as DNA methylation and histone modification. 
The protein is also involved in the repair of DNA damage caused by telomere shortening and telomere dysfunction. 
The protein is also involved in the repair of DNA damage caused by mitochondrial DNA damage. 
The protein is also involved in the repair of DNA damage caused by ionizing radiation. 
The protein is also involved in the repair of DNA damage caused by other types of radiation, such as ultraviolet light and X-rays. 
The protein is also involved in the repair of DNA damage caused by chemicals, such as carcinogens and mutagens. 
The protein is also involved in the repair of DNA damage caused by environmental toxins, such as pesticides and heavy metals. 
The protein is also involved in the repair of DNA",Yes,Maybe,Yes,Yes,No,Yes,GO:0051539; GO:0140078; GO:0003677; GO:0019104; GO:0046872,GO:0019104; GO:0016799,GO:0016798,GO:0019104; GO:0016798,GO:0019104,GO:0004844,0.4859,0.3085,0.4802,0.4338,0.3576,5,0.4132,0.6459,yes
END3_SULAC,Q4J8R2,Reference,Archaea,223,"Probably part of a 4-gene DNA damage response locus in which the upstream ups system, in combination with this downstream locus, functions in homologous recombination to rescue Sulfolobales from DNA- damaging threats (Probable). DNA repair enzyme that has both DNA N- glycosylase activity and AP-lyase activity. The DNA N- glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate (Probable). Nicks UV-treated plasmid DNA in a dose-dependent manner, has no activity on untreated DNA.","Probably part of a 4-gene DNA damage response locus in which the upstream ups system, in combination with this downstream locus, functions in homologous recombination to rescue Sulfolobales from DNA- damaging threats (Probable). DNA repair enzyme that has both DNA N- glycosylase activity and AP-lyase activity. The DNA N- glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate (Probable). Nicks UV-treated plasmid DNA in a dose-dependent manner, has no activity on untreated DNA.",,,,,,,GO:0051539; GO:0140078; GO:0003677; GO:0019104; GO:0046872,GO:0019104; GO:0003906,GO:0019104; GO:0003906,GO:0019104,GO:0019104,GO:0019104,0.553,0.553,0.4338,0.4338,0.4338,5,0.4815,0.6459,yes
HELLS_XENLA,Q4V835,ESM2Text,Eukaryota,838,"ATP-dependent chromatin remodeler that regulates chromatin accessibility, DNA methylation, and histone modifications. It facilitates de novo DNA methylation at repetitive sequences and promotes transcriptional silencing via recruitment of DNA methyltransferases (DNMTs) and histone deacetylases (HDACs), contributing to heterochromatin formation and repression of transposable elements. Also involved in DNA repair by recruiting DNA damage response mediators to double- strand breaks in heterochromatin, promoting homologous recombination via RBBP8/CtIP-dependent end resection. During meiosis, it is recruited by PRDM9 to recombination hotspots, aiding chromatin opening. Through these diverse roles, is crucial for processes such as development, differentiation, and genomic stability.","DNA helicase that plays a role in genome maintenance. Involved in post-replication repair of UV-damaged DNA and in transcription-coupled nucleotide excision repair (TCR). Requires for nucleotide excision repair (NER) activity at chromatin, and is necessary for nucleotide excision repair (NER) in response to UV damage. Acts as a molecular switch in NER.",Maybe,No,No,Maybe,Maybe,not-Yes,GO:0005524; GO:0003682; GO:0004386; GO:0016787,GO:0003678,GO:0004003,GO:0004386; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,0.4114,0.4114,0.7542,0.6795,0.6795,5,0.5872,0.4614,no
HELLS_XENLA,Q4V835,Prot2Text,Eukaryota,838,"ATP-dependent chromatin remodeler that regulates chromatin accessibility, DNA methylation, and histone modifications. It facilitates de novo DNA methylation at repetitive sequences and promotes transcriptional silencing via recruitment of DNA methyltransferases (DNMTs) and histone deacetylases (HDACs), contributing to heterochromatin formation and repression of transposable elements. Also involved in DNA repair by recruiting DNA damage response mediators to double- strand breaks in heterochromatin, promoting homologous recombination via RBBP8/CtIP-dependent end resection. During meiosis, it is recruited by PRDM9 to recombination hotspots, aiding chromatin opening. Through these diverse roles, is crucial for processes such as development, differentiation, and genomic stability.",Plays an essential role in building the proper chromosome structure at the beginning of meiosis in male and female gametophytes. Required for the repression of genes involved in the segregation of homologous chromosomes during meiosis and for the establishment of normal chromosome structure at anaphase I. Required for chromatin-induced silencing of some imprinted genes. May suppress the activation of the silent mating-type locus HML-1.,Maybe,No,No,No,No,not-Yes,GO:0005524; GO:0003682; GO:0004386; GO:0016787,,,,,,,,,,,0,,0.4614,no
HELLS_XENLA,Q4V835,ProtT3,Eukaryota,838,"ATP-dependent chromatin remodeler that regulates chromatin accessibility, DNA methylation, and histone modifications. It facilitates de novo DNA methylation at repetitive sequences and promotes transcriptional silencing via recruitment of DNA methyltransferases (DNMTs) and histone deacetylases (HDACs), contributing to heterochromatin formation and repression of transposable elements. Also involved in DNA repair by recruiting DNA damage response mediators to double- strand breaks in heterochromatin, promoting homologous recombination via RBBP8/CtIP-dependent end resection. During meiosis, it is recruited by PRDM9 to recombination hotspots, aiding chromatin opening. Through these diverse roles, is crucial for processes such as development, differentiation, and genomic stability.",Plays a role in chromatin remodeling. Nucleus. Belongs to the SNF2/RAD54 helicase family,Yes,Vague,Vague,Vague,Yes,not-Yes,GO:0005524; GO:0003682; GO:0004386; GO:0016787,GO:0003678; GO:0005524; GO:0016887,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0008094; GO:0005524,GO:0003678; GO:0005524,0.6798,0.6795,0.6795,0.6077,0.6795,5,0.6652,0.4614,no
HELLS_XENLA,Q4V835,ProtTale,Eukaryota,838,"ATP-dependent chromatin remodeler that regulates chromatin accessibility, DNA methylation, and histone modifications. It facilitates de novo DNA methylation at repetitive sequences and promotes transcriptional silencing via recruitment of DNA methyltransferases (DNMTs) and histone deacetylases (HDACs), contributing to heterochromatin formation and repression of transposable elements. Also involved in DNA repair by recruiting DNA damage response mediators to double- strand breaks in heterochromatin, promoting homologous recombination via RBBP8/CtIP-dependent end resection. During meiosis, it is recruited by PRDM9 to recombination hotspots, aiding chromatin opening. Through these diverse roles, is crucial for processes such as development, differentiation, and genomic stability.",Probable ATP-dependent chromatin-remodeling factor.,Yes,Maybe,Vague,Maybe,Yes,not-Yes,GO:0005524; GO:0003682; GO:0004386; GO:0016787,GO:0016887,GO:0005524; GO:0016887,GO:0005524; GO:0003677,GO:0005524,GO:0016887,0.2931,0.5751,0.551,0.4703,0.2931,5,0.4365,0.4614,no
HELLS_XENLA,Q4V835,Protein2Text,Eukaryota,838,"ATP-dependent chromatin remodeler that regulates chromatin accessibility, DNA methylation, and histone modifications. It facilitates de novo DNA methylation at repetitive sequences and promotes transcriptional silencing via recruitment of DNA methyltransferases (DNMTs) and histone deacetylases (HDACs), contributing to heterochromatin formation and repression of transposable elements. Also involved in DNA repair by recruiting DNA damage response mediators to double- strand breaks in heterochromatin, promoting homologous recombination via RBBP8/CtIP-dependent end resection. During meiosis, it is recruited by PRDM9 to recombination hotspots, aiding chromatin opening. Through these diverse roles, is crucial for processes such as development, differentiation, and genomic stability.","The molecular function of this protein is to act as a DNA helicase, which is an enzyme that unwinds DNA in a process called DNA unwinding. This process is crucial for various cellular activities such as DNA replication, repair, and transcription.",Maybe,No,No,Maybe,Maybe,not-Yes,GO:0005524; GO:0003682; GO:0004386; GO:0016787,GO:0004003; GO:0003678,GO:0004003,GO:0004003; GO:0003677,GO:0004003; GO:0003677,GO:0003678,0.478,0.4114,0.5013,0.5013,0.4114,5,0.4607,0.4614,no
HELLS_XENLA,Q4V835,Reference,Eukaryota,838,"ATP-dependent chromatin remodeler that regulates chromatin accessibility, DNA methylation, and histone modifications. It facilitates de novo DNA methylation at repetitive sequences and promotes transcriptional silencing via recruitment of DNA methyltransferases (DNMTs) and histone deacetylases (HDACs), contributing to heterochromatin formation and repression of transposable elements. Also involved in DNA repair by recruiting DNA damage response mediators to double- strand breaks in heterochromatin, promoting homologous recombination via RBBP8/CtIP-dependent end resection. During meiosis, it is recruited by PRDM9 to recombination hotspots, aiding chromatin opening. Through these diverse roles, is crucial for processes such as development, differentiation, and genomic stability.","ATP-dependent chromatin remodeler that regulates chromatin accessibility, DNA methylation, and histone modifications. It facilitates de novo DNA methylation at repetitive sequences and promotes transcriptional silencing via recruitment of DNA methyltransferases (DNMTs) and histone deacetylases (HDACs), contributing to heterochromatin formation and repression of transposable elements. Also involved in DNA repair by recruiting DNA damage response mediators to double- strand breaks in heterochromatin, promoting homologous recombination via RBBP8/CtIP-dependent end resection. During meiosis, it is recruited by PRDM9 to recombination hotspots, aiding chromatin opening. Through these diverse roles, is crucial for processes such as development, differentiation, and genomic stability.",,,,,,,GO:0005524; GO:0003682; GO:0004386; GO:0016787,GO:0004386; GO:0005524; GO:0003677,GO:0008094; GO:0005524,GO:0016887; GO:0003682,GO:0016887; GO:0003682,GO:0016887; GO:0003682,0.7557,0.6077,0.5751,0.5751,0.5751,5,0.6177,0.4614,no
KDSR_ASPFU,Q4WSZ0,ESM2Text,Eukaryota,367,"Catalyzes the reduction of 3'-oxosphinganine (3- ketodihydrosphingosine/KDS) to sphinganine (dihydrosphingosine/DHS), the second step of de novo sphingolipid biosynthesis.",Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS).,Yes,Yes,Yes,Yes,Yes,Yes,GO:0047560; GO:0070402,GO:0047560,GO:0047560,GO:0016491,GO:0047560,GO:0047560,0.6877,0.6877,0.4365,0.6877,0.6877,5,0.6375,0.2502,no
KDSR_ASPFU,Q4WSZ0,Prot2Text,Eukaryota,367,"Catalyzes the reduction of 3'-oxosphinganine (3- ketodihydrosphingosine/KDS) to sphinganine (dihydrosphingosine/DHS), the second step of de novo sphingolipid biosynthesis.",Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS).,Yes,Yes,Yes,Yes,Yes,Yes,GO:0047560; GO:0070402,GO:0003856,GO:0047560,GO:0047560,GO:0003856,GO:0003856,0.1542,0.6877,0.6877,0.1542,0.1542,5,0.3676,0.2502,no
KDSR_ASPFU,Q4WSZ0,ProtT3,Eukaryota,367,"Catalyzes the reduction of 3'-oxosphinganine (3- ketodihydrosphingosine/KDS) to sphinganine (dihydrosphingosine/DHS), the second step of de novo sphingolipid biosynthesis.",Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS). Endoplasmic reticulum membrane; Single-pass membrane protein. Belongs to the short-chain dehydrogenases/reductases (SDR) family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0047560; GO:0070402,GO:0047560,GO:0016491,GO:0046569,GO:0047560,GO:0047560,0.6877,0.4365,0.2468,0.6877,0.6877,5,0.5493,0.2502,no
KDSR_ASPFU,Q4WSZ0,ProtTale,Eukaryota,367,"Catalyzes the reduction of 3'-oxosphinganine (3- ketodihydrosphingosine/KDS) to sphinganine (dihydrosphingosine/DHS), the second step of de novo sphingolipid biosynthesis.",Catalyzes the reduction of 2-keto-3-deoxy-D-gluconate (KDO) to 2-keto-3-deoxy-D-galactonate (KDG) with NADPH as the electron donor. Can also use NADH as the electron donor.,No,No,No,No,No,not-Yes,GO:0047560; GO:0070402,GO:0016491; GO:0050661,GO:0016491; GO:0050661,GO:0016491; GO:0050661,GO:0016491,GO:0016491,0.6939,0.6939,0.6939,0.4365,0.4365,5,0.5909,0.2502,no
KDSR_ASPFU,Q4WSZ0,Protein2Text,Eukaryota,367,"Catalyzes the reduction of 3'-oxosphinganine (3- ketodihydrosphingosine/KDS) to sphinganine (dihydrosphingosine/DHS), the second step of de novo sphingolipid biosynthesis.","The molecular function of this protein is as a 3-ketoacyl-CoA thiolase, which is involved in the beta-oxidation of fatty acids. It catalyzes the cleavage of thioester bonds in 3-ketoacyl-CoA to produce acetyl-CoA and a fatty acyl-CoA with one less carbon atom. This process is an important step in the breakdown of fatty acids to produce energy.",No,No,No,No,No,not-Yes,GO:0047560; GO:0070402,GO:0003988,GO:0003988,GO:0003988,GO:0003988,GO:0003988,0.1342,0.1342,0.1342,0.1342,0.1342,5,0.1342,0.2502,no
KDSR_ASPFU,Q4WSZ0,Reference,Eukaryota,367,"Catalyzes the reduction of 3'-oxosphinganine (3- ketodihydrosphingosine/KDS) to sphinganine (dihydrosphingosine/DHS), the second step of de novo sphingolipid biosynthesis.","Catalyzes the reduction of 3'-oxosphinganine (3- ketodihydrosphingosine/KDS) to sphinganine (dihydrosphingosine/DHS), the second step of de novo sphingolipid biosynthesis.",,,,,,,GO:0047560; GO:0070402,GO:0016491; GO:0050661,GO:0047560,GO:0047560,GO:0047560,GO:0047560,0.6939,0.6877,0.6877,0.6877,0.6877,5,0.6889,0.2502,no
GLYC_ASPFU,Q4WXF4,ESM2Text,Eukaryota,471,Catalyzes the interconversion of serine and glycine. Essential for viability and required for virulence in a murine model of established pulmonary infection.,Interconversion of serine and glycine.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004372; GO:0030170,GO:0004372,GO:0004372,,GO:0004372,GO:0004372,0.6898,0.6898,,0.6898,0.6898,4,0.6898,0.2383,no
GLYC_ASPFU,Q4WXF4,Prot2Text,Eukaryota,471,Catalyzes the interconversion of serine and glycine. Essential for viability and required for virulence in a murine model of established pulmonary infection.,Interconversion of serine and glycine.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004372; GO:0030170,GO:0004372,GO:0004372,GO:0004372,GO:0004372,GO:0004372,0.6898,0.6898,0.6898,0.6898,0.6898,5,0.6898,0.2383,no
GLYC_ASPFU,Q4WXF4,ProtT3,Eukaryota,471,Catalyzes the interconversion of serine and glycine. Essential for viability and required for virulence in a murine model of established pulmonary infection.,"Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Cytoplasm. Belongs to the SHMT family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004372; GO:0030170,GO:0004372,GO:0004372,GO:0004372; GO:0030170,GO:0004372,GO:0004372; GO:0030170,0.6898,0.6898,1.0,0.6898,1.0,5,0.8139,0.2383,no
GLYC_ASPFU,Q4WXF4,ProtTale,Eukaryota,471,Catalyzes the interconversion of serine and glycine. Essential for viability and required for virulence in a murine model of established pulmonary infection.,Catalyzes the reversible interconversion of alpha-ketoisovalerate and beta- ketoisovalerate.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004372; GO:0030170,GO:0016853,GO:0016853,GO:0016853,GO:0016853,GO:0016853,0.2761,0.2761,0.2761,0.2761,0.2761,5,0.2761,0.2383,no
GLYC_ASPFU,Q4WXF4,Protein2Text,Eukaryota,471,Catalyzes the interconversion of serine and glycine. Essential for viability and required for virulence in a murine model of established pulmonary infection.,"The molecular function of this protein is an aminotransferase. More specifically, it catalyzes the reversible transfer of an amino group from an amino acid to a 2-ketoglutarate, producing glutamate and a ketoacid. In this case, it is involved in the conversion of L-aspartate to oxaloacetate. This reaction is an important step in the synthesis of amino acids and in the regulation of nitrogen levels in the cell. The protein is also involved in the conversion of L-aspartate to oxaloacetate, which is a key step in the citric acid cycle (also known as the Krebs cycle or tricarboxylic acid cycle).",No,No,No,No,No,not-Yes,GO:0004372; GO:0030170,GO:0004069,GO:0008483,GO:0004069,GO:0004069,GO:0004069,0.2488,0.2927,0.2488,0.2488,0.2488,5,0.2576,0.2383,no
GLYC_ASPFU,Q4WXF4,Reference,Eukaryota,471,Catalyzes the interconversion of serine and glycine. Essential for viability and required for virulence in a murine model of established pulmonary infection.,Catalyzes the interconversion of serine and glycine. Essential for viability and required for virulence in a murine model of established pulmonary infection.,,,,,,,GO:0004372; GO:0030170,GO:0004372,GO:0004372,GO:0004372,GO:0004372,GO:0004372,0.6898,0.6898,0.6898,0.6898,0.6898,5,0.6898,0.2383,no
YPKA_ASPFU,Q4X1A8,ESM2Text,Eukaryota,637,Serine/threonine protein kinase required for vegetative growth and conidiation. Important for fungal survival through the regulation of glycosphingolipid (GSL) biosynthesis and cross talks with MAP kinase pathways such as the cell wall integrity (CWI) and the high osmolarity glycerol (HOG) pathways.,Serine/threonine-protein kinase which is required for mitotic spindle formation and actomyosin ring contraction. May function downstream of cdc13 and mdf2 in microtubule organizing centers (MTOCs) during spindle assembly.,Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0005524; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.964,0.7186,0.964,0.964,0.964,5,0.9149,0.4287,no
YPKA_ASPFU,Q4X1A8,Prot2Text,Eukaryota,637,Serine/threonine protein kinase required for vegetative growth and conidiation. Important for fungal survival through the regulation of glycosphingolipid (GSL) biosynthesis and cross talks with MAP kinase pathways such as the cell wall integrity (CWI) and the high osmolarity glycerol (HOG) pathways.,Probable serine/threonine-protein kinase that may act in the sphingolipid-mediated signaling pathway.,Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0005524; GO:0106310; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.7186,0.7186,0.7186,0.7186,0.7186,5,0.7186,0.4287,no
YPKA_ASPFU,Q4X1A8,ProtT3,Eukaryota,637,Serine/threonine protein kinase required for vegetative growth and conidiation. Important for fungal survival through the regulation of glycosphingolipid (GSL) biosynthesis and cross talks with MAP kinase pathways such as the cell wall integrity (CWI) and the high osmolarity glycerol (HOG) pathways.,Serine/threonine-protein kinase involved in the regulation of the cell wall integrity (CWI) pathway (By similarity). Phosphorylates and activates the CWI pathway regulator mog1 (By similarity). Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily,Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0005524; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.964,0.964,0.964,0.964,0.964,5,0.964,0.4287,no
YPKA_ASPFU,Q4X1A8,ProtTale,Eukaryota,637,Serine/threonine protein kinase required for vegetative growth and conidiation. Important for fungal survival through the regulation of glycosphingolipid (GSL) biosynthesis and cross talks with MAP kinase pathways such as the cell wall integrity (CWI) and the high osmolarity glycerol (HOG) pathways.,Has a role in meiosis.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0106310; GO:0004674,,,,,,,,,,,0,,0.4287,no
YPKA_ASPFU,Q4X1A8,Protein2Text,Eukaryota,637,Serine/threonine protein kinase required for vegetative growth and conidiation. Important for fungal survival through the regulation of glycosphingolipid (GSL) biosynthesis and cross talks with MAP kinase pathways such as the cell wall integrity (CWI) and the high osmolarity glycerol (HOG) pathways.,This protein is a serine/threonine protein kinase. It belongs to the protein kinase family and is involved in the phosphorylation of serine and threonine residues in proteins.,Yes,Maybe,Maybe,Vague,Yes,not-Yes,GO:0005524; GO:0106310; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.7186,0.7186,0.7186,0.7186,0.7186,5,0.7186,0.4287,no
YPKA_ASPFU,Q4X1A8,Reference,Eukaryota,637,Serine/threonine protein kinase required for vegetative growth and conidiation. Important for fungal survival through the regulation of glycosphingolipid (GSL) biosynthesis and cross talks with MAP kinase pathways such as the cell wall integrity (CWI) and the high osmolarity glycerol (HOG) pathways.,Serine/threonine protein kinase required for vegetative growth and conidiation. Important for fungal survival through the regulation of glycosphingolipid (GSL) biosynthesis and cross talks with MAP kinase pathways such as the cell wall integrity (CWI) and the high osmolarity glycerol (HOG) pathways.,,,,,,,GO:0005524; GO:0106310; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674; GO:0005524,GO:0004674,0.7186,0.7186,0.7186,0.964,0.7186,5,0.7677,0.4287,no
ENLYS_BP263,Q4ZD58,ESM2Text,Viruses,486,Endolysin that degrades host peptidoglycans and participates in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. The N-acetyl- muramidase activity cleaves between N-acetylmuramic acid and N- acetylglucosamine bonds.,Lyses staphylococcal cells by hydrolyzing the polysaccharide cellobiose.,No,Maybe,Maybe,Maybe,No,not-Yes,GO:0046872; GO:0004222; GO:0008745,GO:0016798,GO:0004553,GO:0016798,GO:0004553,GO:0016798,0.3624,0.3053,0.3624,0.3053,0.3624,5,0.3396,0.1978,no
ENLYS_BP263,Q4ZD58,Prot2Text,Viruses,486,Endolysin that degrades host peptidoglycans and participates in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. The N-acetyl- muramidase activity cleaves between N-acetylmuramic acid and N- acetylglucosamine bonds.,Lyses staphylococcal cells by hydrolyzing the polysaccharide cellobiose.,No,Maybe,Maybe,Maybe,No,not-Yes,GO:0046872; GO:0004222; GO:0008745,,,GO:0016798,,,,,0.3624,,,1,0.3624,0.1978,no
ENLYS_BP263,Q4ZD58,ProtT3,Viruses,486,Endolysin that degrades host peptidoglycans and participates in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. The N-acetyl- muramidase activity cleaves between N-acetylmuramic acid and N- acetylglucosamine bonds.,"Catalyzes the cleavage of the D-alanyl-meso-2,6- diaminoheptanedioate (meso-L-Ala-D-Ala-D-Ala-D-Ala-D-Ala-D-Ala-D-Ala-D-Ala-D-Ala-D-Ala-D-Ala-D-Ala-D-Ala-D-Ala-D-Ala-D-Ala-D-Ala-D-Ala-D-Ala-D-Ala-D-Ala-D-Ala-D-Ala-D-Ala",Maybe,Vague,Vague,Maybe,Maybe,not-Yes,GO:0046872; GO:0004222; GO:0008745,,GO:0004175,,,GO:0008233,,0.5145,,,0.4841,2,0.4993,0.1978,no
ENLYS_BP263,Q4ZD58,ProtTale,Viruses,486,Endolysin that degrades host peptidoglycans and participates in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. The N-acetyl- muramidase activity cleaves between N-acetylmuramic acid and N- acetylglucosamine bonds.,Autolysins are involved in the degradation of proteins present in the cell supernatant. Hydrolyzes the bond between the N-terminal amino group of an amino acid and the epsilon-amino group of aspartate or glutamate.,Vague,Maybe,Vague,No,Maybe,not-Yes,GO:0046872; GO:0004222; GO:0008745,GO:0008233,GO:0016787,GO:0016787,GO:0008233,GO:0008233,0.4841,0.4428,0.4428,0.4841,0.4841,5,0.4676,0.1978,no
ENLYS_BP263,Q4ZD58,Protein2Text,Viruses,486,Endolysin that degrades host peptidoglycans and participates in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. The N-acetyl- muramidase activity cleaves between N-acetylmuramic acid and N- acetylglucosamine bonds.,This protein is a metalloprotease.,No,No,No,No,No,not-Yes,GO:0046872; GO:0004222; GO:0008745,GO:0004222,GO:0004222,GO:0004222,GO:0004222,GO:0004222,0.5924,0.5924,0.5924,0.5924,0.5924,5,0.5924,0.1978,no
ENLYS_BP263,Q4ZD58,Reference,Viruses,486,Endolysin that degrades host peptidoglycans and participates in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. The N-acetyl- muramidase activity cleaves between N-acetylmuramic acid and N- acetylglucosamine bonds.,Endolysin that degrades host peptidoglycans and participates in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. The N-acetyl- muramidase activity cleaves between N-acetylmuramic acid and N- acetylglucosamine bonds.,,,,,,,GO:0046872; GO:0004222; GO:0008745,GO:0016998,GO:0003796,GO:0003796,GO:0003796; GO:0016798,GO:0003796,0.0,0.3492,0.3492,0.3988,0.3492,5,0.2893,0.1978,no
DSD1_DICDI,Q54XE5,ESM2Text,Eukaryota,395,Catalyzes the conversion of D-serine to pyruvate and ammonia. Plays a role in D-serine detoxification.,"Catalyzes the interconversion of D-lysine and L-lysine. Has also low D-amino acid racemase activity. Inactive with D-amino acids including D-alanine, D-aminoethane, D-threonine, D-serine, D-threonine, D-valine and L-valine. Inactive with methylglyoxal and D-methionine.",No,No,No,No,No,not-Yes,GO:0008721; GO:0046872,GO:0016855,GO:0016857,GO:0008481,GO:0016855,GO:0016855,0.1917,0.1917,0.1362,0.1917,0.1917,5,0.1806,0.2766,no
DSD1_DICDI,Q54XE5,Prot2Text,Eukaryota,395,Catalyzes the conversion of D-serine to pyruvate and ammonia. Plays a role in D-serine detoxification.,Catalyzes the synthesis of D-serine from L-serine. Has dehydratase activity towards both L-serine and D-serine.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008721; GO:0046872,GO:0008453,GO:0008486,GO:0008453,GO:0008453,GO:0008453,0.1628,0.1415,0.1628,0.1628,0.1628,5,0.1585,0.2766,no
DSD1_DICDI,Q54XE5,ProtT3,Eukaryota,395,Catalyzes the conversion of D-serine to pyruvate and ammonia. Plays a role in D-serine detoxification.,Cytoplasm Nucleus. Belongs to the DapA family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008721; GO:0046872,GO:0008840,GO:0008840,GO:0008840,GO:0008840,GO:0008840,0.371,0.371,0.371,0.371,0.371,5,0.371,0.2766,no
DSD1_DICDI,Q54XE5,ProtTale,Eukaryota,395,Catalyzes the conversion of D-serine to pyruvate and ammonia. Plays a role in D-serine detoxification.,Catalyzes the reversible transamination of delta-aminolevulinate (ALA) and glycine to form porphobilinogen (PBG).,No,No,No,No,No,not-Yes,GO:0008721; GO:0046872,GO:0004655,GO:0008483,GO:0008483,GO:0008483,GO:0004655,0.2554,0.1917,0.1917,0.1917,0.2554,5,0.2172,0.2766,no
DSD1_DICDI,Q54XE5,Protein2Text,Eukaryota,395,Catalyzes the conversion of D-serine to pyruvate and ammonia. Plays a role in D-serine detoxification.,"This protein is a catalytic enzyme, specifically an aminotransferase. It catalyzes the transfer of an amino group from an amino acid to a keto acid, typically in the first step of a metabolic pathway. The amino acid is usually converted to a keto acid, while the keto acid is converted to an amino acid. In this case, it is likely involved in the synthesis or catabolism of a specific amino acid or related metabolites.",No,No,No,No,No,not-Yes,GO:0008721; GO:0046872,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.1917,0.1917,0.1917,0.1917,0.1917,5,0.1917,0.2766,no
DSD1_DICDI,Q54XE5,Reference,Eukaryota,395,Catalyzes the conversion of D-serine to pyruvate and ammonia. Plays a role in D-serine detoxification.,Catalyzes the conversion of D-serine to pyruvate and ammonia. Plays a role in D-serine detoxification.,,,,,,,GO:0008721; GO:0046872,GO:0008720,GO:0008721,GO:0008721,GO:0008721,GO:0016829,0.1112,0.6963,0.6963,0.6963,0.4539,5,0.5308,0.2766,no
MCP1_TRYB2,Q57XN4,ESM2Text,Eukaryota,425,"Ala-tRNA deacylase. Can deacylate mischarged Ala-tRNA(Pro), Ser-tRNA(Pro), Gly-tRNA(Ala) and cognate Ala- tRNA(Ala) with similar efficiencies; more slowly deacylates cognate Pro-tRNA(Pro). Rescues alanyl-tRNA synthetase editing deficiencies.","Non-catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. PAN3 acts as a positive regulator of maturation of mRNA poly(A) tails by recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and with PAB1.",No,No,No,Maybe,No,not-Yes,GO:0000049,GO:0003723,GO:0003723,,GO:0003723,GO:0003723,0.8416,0.8416,,0.8416,0.8416,4,0.8416,0.462,no
MCP1_TRYB2,Q57XN4,Prot2Text,Eukaryota,425,"Ala-tRNA deacylase. Can deacylate mischarged Ala-tRNA(Pro), Ser-tRNA(Pro), Gly-tRNA(Ala) and cognate Ala- tRNA(Ala) with similar efficiencies; more slowly deacylates cognate Pro-tRNA(Pro). Rescues alanyl-tRNA synthetase editing deficiencies.","Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENPN is the first protein to bind specifically to CENPA nucleosomes and the direct binding of CENPA nucleosomes by CENPN is required for centromere assembly. Required for chromosome congression and efficiently align the chromosomes on a metaphase plate.",No,No,No,No,No,not-Yes,GO:0000049,,,,,,,,,,,0,,0.462,no
MCP1_TRYB2,Q57XN4,ProtT3,Eukaryota,425,"Ala-tRNA deacylase. Can deacylate mischarged Ala-tRNA(Pro), Ser-tRNA(Pro), Gly-tRNA(Ala) and cognate Ala- tRNA(Ala) with similar efficiencies; more slowly deacylates cognate Pro-tRNA(Pro). Rescues alanyl-tRNA synthetase editing deficiencies.",Plays a role in the assembly of multisubunit protein complexes. Cytoplasm Nucleus. Belongs to the non-thiol-disulfide oxidoreductase family,Vague,Vague,Vague,Vague,No,not-Yes,GO:0000049,,,,,,,,,,,0,,0.462,no
MCP1_TRYB2,Q57XN4,ProtTale,Eukaryota,425,"Ala-tRNA deacylase. Can deacylate mischarged Ala-tRNA(Pro), Ser-tRNA(Pro), Gly-tRNA(Ala) and cognate Ala- tRNA(Ala) with similar efficiencies; more slowly deacylates cognate Pro-tRNA(Pro). Rescues alanyl-tRNA synthetase editing deficiencies.",Binds aminoacyl-tRNA in a 2:1 molar ratio.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0000049,GO:0000049,GO:0003723,GO:0000049,,GO:0000049,1.0,0.8416,1.0,,1.0,4,0.9604,0.462,no
MCP1_TRYB2,Q57XN4,Protein2Text,Eukaryota,425,"Ala-tRNA deacylase. Can deacylate mischarged Ala-tRNA(Pro), Ser-tRNA(Pro), Gly-tRNA(Ala) and cognate Ala- tRNA(Ala) with similar efficiencies; more slowly deacylates cognate Pro-tRNA(Pro). Rescues alanyl-tRNA synthetase editing deficiencies.","The molecular function of this protein is not explicitly stated in the provided information. However, based on its classification as a protein, it is likely involved in various biological processes, such as catalyzing biochemical reactions, binding to other molecules, or participating in signal transduction pathways. To determine the specific molecular function of this protein, further research or information would be required.",Vague,Vague,Vague,No,Vague,not-Yes,GO:0000049,,,,,,,,,,,0,,0.462,no
MCP1_TRYB2,Q57XN4,Reference,Eukaryota,425,"Ala-tRNA deacylase. Can deacylate mischarged Ala-tRNA(Pro), Ser-tRNA(Pro), Gly-tRNA(Ala) and cognate Ala- tRNA(Ala) with similar efficiencies; more slowly deacylates cognate Pro-tRNA(Pro). Rescues alanyl-tRNA synthetase editing deficiencies.","Ala-tRNA deacylase. Can deacylate mischarged Ala-tRNA(Pro), Ser-tRNA(Pro), Gly-tRNA(Ala) and cognate Ala- tRNA(Ala) with similar efficiencies; more slowly deacylates cognate Pro-tRNA(Pro). Rescues alanyl-tRNA synthetase editing deficiencies.",,,,,,,GO:0000049,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0002161,0.1809,0.1809,0.1809,0.1809,0.0902,5,0.1628,0.462,no
ENCR_TRYB2,Q57ZC7,ESM2Text,Eukaryota,298,Involved in the synthesis of fatty acids.,"Required for the first step of the sphingolipid biosynthesis, the condensation of the long-chain fatty acids to form the ceramides.",Maybe,No,Vague,No,Maybe,not-Yes,GO:0102758,,GO:0004758,,GO:0004758,,,0.1424,,0.1424,,2,0.1424,0.3343,no
ENCR_TRYB2,Q57ZC7,Prot2Text,Eukaryota,298,Involved in the synthesis of fatty acids.,"3-beta-carotene synthase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway. ERG11 catalyzes the last step of ergosterol biosynthesis by converting 3-beta-carotene into 3,4-dihydroxy-6-(3-beta-hydroxybenzyl)benzoic acid. The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7",No,No,No,No,No,not-Yes,GO:0102758,,,,,,,,,,,0,,0.3343,no
ENCR_TRYB2,Q57ZC7,ProtT3,Eukaryota,298,Involved in the synthesis of fatty acids.,"Catalyzes the last of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Endoplasmic reticulum membrane; Multi-pass",Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0102758,GO:0016616,GO:0016491,GO:0019166,GO:0016491,GO:0016509,0.3987,0.6019,0.7289,0.6019,0.2943,5,0.5251,0.3343,no
ENCR_TRYB2,Q57ZC7,ProtTale,Eukaryota,298,Involved in the synthesis of fatty acids.,"Catalyzes the last of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme reduces the trans-2,3-enoyl-CoA fatty acid intermediate to an acyl-CoA that can be further elongated by entering a new cycle of elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.",Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0102758,GO:0019166,GO:0016491,GO:0016491,GO:0016491,GO:0019166,0.7289,0.6019,0.6019,0.6019,0.7289,5,0.6527,0.3343,no
ENCR_TRYB2,Q57ZC7,Protein2Text,Eukaryota,298,Involved in the synthesis of fatty acids.,"The molecular function of this protein is as a farnesyltransferase. Specifically, it is involved in the addition of farnesyl groups to proteins.",No,No,Vague,No,No,not-Yes,GO:0102758,GO:0004660,GO:0004660,GO:0004660,GO:0004660,GO:0004311,0.1926,0.1926,0.1926,0.1926,0.1737,5,0.1888,0.3343,no
ENCR_TRYB2,Q57ZC7,Reference,Eukaryota,298,Involved in the synthesis of fatty acids.,Involved in the synthesis of fatty acids.,,,,,,,GO:0102758,,,,,,,,,,,0,,0.3343,no
NDX4_TRYB2,Q583R7,ESM2Text,Eukaryota,294,"Decapping enzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Can also remove GDP from unmethylated capped RNA, but is less active at a mature cap 4 end and thus may function as a surveillance enzyme to decap mRNAs lacking either N7 guanine methylation or ribose 2'O-methylation at nucleosides 2, 3 and 4.",Probably mediates the hydrolysis of some nucleoside diphosphate derivatives.,Vague,No,No,Maybe,Maybe,not-Yes,GO:0000298; GO:0004309,GO:0017110,GO:0016787,GO:0016787,GO:0016787,GO:0016787,0.7469,0.5381,0.5381,0.5381,0.5381,5,0.5799,0.2435,no
NDX4_TRYB2,Q583R7,Prot2Text,Eukaryota,294,"Decapping enzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Can also remove GDP from unmethylated capped RNA, but is less active at a mature cap 4 end and thus may function as a surveillance enzyme to decap mRNAs lacking either N7 guanine methylation or ribose 2'O-methylation at nucleosides 2, 3 and 4.",Probably mediates the hydrolysis of some nucleoside diphosphate derivatives.,Vague,No,No,Maybe,Maybe,not-Yes,GO:0000298; GO:0004309,GO:0017110,GO:0017110,GO:0017110,GO:0016787,GO:0017110,0.7469,0.7469,0.7469,0.5381,0.7469,5,0.7051,0.2435,no
NDX4_TRYB2,Q583R7,ProtT3,Eukaryota,294,"Decapping enzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Can also remove GDP from unmethylated capped RNA, but is less active at a mature cap 4 end and thus may function as a surveillance enzyme to decap mRNAs lacking either N7 guanine methylation or ribose 2'O-methylation at nucleosides 2, 3 and 4.",Decapping enzyme that removes the 5'-diphosphate from a subset of mRNAs. Belongs to the Nudix hydrolase family. NudC subfamily,Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0000298; GO:0004309,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016787,0.5381,0.5381,0.5381,0.5381,0.5381,5,0.5381,0.2435,no
NDX4_TRYB2,Q583R7,ProtTale,Eukaryota,294,"Decapping enzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Can also remove GDP from unmethylated capped RNA, but is less active at a mature cap 4 end and thus may function as a surveillance enzyme to decap mRNAs lacking either N7 guanine methylation or ribose 2'O-methylation at nucleosides 2, 3 and 4.",Acts as a negative regulator of the DNA damage response. Involved in the regulation of the cell cycle and the DNA damage response. Plays a role in the regulation of the cell cycle in G2/M phase. Plays a role in the maintenance of genome stability. Plays a role in the regulation of the cell cycle in G2/M phase in response to DNA damage. Acts as a negative regulator of the p53/TP53 pathway in response to DNA damage. Acts as a negative regulator of the p53/TP53 pathway in response to replication stress. Acts as a negative,No,No,No,No,No,not-Yes,GO:0000298; GO:0004309,,,,,,,,,,,0,,0.2435,no
NDX4_TRYB2,Q583R7,Protein2Text,Eukaryota,294,"Decapping enzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Can also remove GDP from unmethylated capped RNA, but is less active at a mature cap 4 end and thus may function as a surveillance enzyme to decap mRNAs lacking either N7 guanine methylation or ribose 2'O-methylation at nucleosides 2, 3 and 4.","The molecular function of this protein is RNA-binding and catalyzing the 2',3'-cyclic pyrophosphorolysis reaction. It is involved in the removal of 2',3'-cyclic pyrophosphate from RNA molecules.",No,No,No,No,No,not-Yes,GO:0000298; GO:0004309,GO:0003723,GO:0003723,GO:0003723,GO:0003723,,0.1121,0.1121,0.1121,0.1121,,4,0.1121,0.2435,no
NDX4_TRYB2,Q583R7,Reference,Eukaryota,294,"Decapping enzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Can also remove GDP from unmethylated capped RNA, but is less active at a mature cap 4 end and thus may function as a surveillance enzyme to decap mRNAs lacking either N7 guanine methylation or ribose 2'O-methylation at nucleosides 2, 3 and 4.","Decapping enzyme that catalyzes the cleavage of the cap structure on mRNAs. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Can also remove GDP from unmethylated capped RNA, but is less active at a mature cap 4 end and thus may function as a surveillance enzyme to decap mRNAs lacking either N7 guanine methylation or ribose 2'O-methylation at nucleosides 2, 3 and 4.",,,,,,,GO:0000298; GO:0004309,GO:0050072,GO:0050072,GO:0016787,GO:0016787,,0.0,0.0,0.5381,0.5381,,4,0.2691,0.2435,no
PKS91_EMENI,Q5AY39,ESM2Text,Eukaryota,2568,"Highly reducing polyketide synthase; part of a cluster that mediates the biosynthesis of a yet undetermined secondary metabolite (Probable). With esterase AN6793, produces a pathway intermediate compound with molecular weight 258.","Polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential tricyclic",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177; GO:0008270,,GO:0016747,GO:0016491; GO:0016740,GO:0016746,GO:0016746,,0.4604,0.6053,0.4506,0.4506,4,0.4917,0.2406,no
PKS91_EMENI,Q5AY39,Prot2Text,Eukaryota,2568,"Highly reducing polyketide synthase; part of a cluster that mediates the biosynthesis of a yet undetermined secondary metabolite (Probable). With esterase AN6793, produces a pathway intermediate compound with molecular weight 258.","Trihydroxysteroid synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177; GO:0008270,,,,,,,,,,,0,,0.2406,no
PKS91_EMENI,Q5AY39,ProtT3,Eukaryota,2568,"Highly reducing polyketide synthase; part of a cluster that mediates the biosynthesis of a yet undetermined secondary metabolite (Probable). With esterase AN6793, produces a pathway intermediate compound with molecular weight 258.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of aspirochlorine (or antibiotic A30641), an unusual halogenated spiro compound with distinctive antifungal properties due to selective inhibition of protein biosynthesis, and which is also active against bacteria, viruses, and murine tumor cells . The non-reducing polyketide synthase aclD is responsible for the formation of the polyketide backbone . The starter unit acyltransferase aclC",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177; GO:0008270,GO:0016747,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.4604,0.4506,0.4506,0.4506,0.4506,5,0.4526,0.2406,no
PKS91_EMENI,Q5AY39,ProtTale,Eukaryota,2568,"Highly reducing polyketide synthase; part of a cluster that mediates the biosynthesis of a yet undetermined secondary metabolite (Probable). With esterase AN6793, produces a pathway intermediate compound with molecular weight 258.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177; GO:0008270,GO:0016747,GO:0016747,GO:0016491; GO:0016874,GO:0016746,,0.4604,0.4604,0.5155,0.4506,,4,0.4717,0.2406,no
PKS91_EMENI,Q5AY39,Protein2Text,Eukaryota,2568,"Highly reducing polyketide synthase; part of a cluster that mediates the biosynthesis of a yet undetermined secondary metabolite (Probable). With esterase AN6793, produces a pathway intermediate compound with molecular weight 258.",The molecular function of this protein is involved in the biosynthesis of a secondary metabolite. It is a component of the biosynthesis pathway of a certain type of molecule.,Vague,No,Vague,Vague,Vague,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177; GO:0008270,,,,,,,,,,,0,,0.2406,no
PKS91_EMENI,Q5AY39,Reference,Eukaryota,2568,"Highly reducing polyketide synthase; part of a cluster that mediates the biosynthesis of a yet undetermined secondary metabolite (Probable). With esterase AN6793, produces a pathway intermediate compound with molecular weight 258.","Highly reducing polyketide synthase; part of a cluster that mediates the biosynthesis of a yet undetermined secondary metabolite (Probable). With esterase AN6793, produces a pathway intermediate compound with molecular weight 258.",,,,,,,GO:0004312; GO:0008168; GO:0016491; GO:0031177; GO:0008270,GO:0031177; GO:0016747,GO:0004315,,GO:0016746,,0.7036,0.3936,,0.4506,,3,0.5159,0.2406,no
NHMT_EMENI,Q5B467,ESM2Text,Eukaryota,558,"Protein-histidine N-methyltransferase that specifically mediates 3-methylhistidine (tele-methylhistidine) methylation at 'His- 1', which protects the side-chain from oxidative damage. Methylates lytic polysaccharide monooxygenases (LPMOs) destined for secretion, including AN4702.",Catalyzes the production of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM).,No,No,No,No,No,not-Yes,GO:0018064,GO:0004766,GO:0004766,GO:0004766,GO:0004766,GO:0004766,0.2927,0.2927,0.2927,0.2927,0.2927,5,0.2927,0.2823,no
NHMT_EMENI,Q5B467,Prot2Text,Eukaryota,558,"Protein-histidine N-methyltransferase that specifically mediates 3-methylhistidine (tele-methylhistidine) methylation at 'His- 1', which protects the side-chain from oxidative damage. Methylates lytic polysaccharide monooxygenases (LPMOs) destined for secretion, including AN4702.","Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN). Methyltransferase that mediates the conversion of putrescine to N-methylputrescine. Promotes leaves ripening.",No,No,No,No,No,not-Yes,GO:0018064,GO:0030744,GO:0030744,GO:0030748,GO:0030744,GO:0030744,0.0,0.0,0.5952,0.0,0.0,5,0.119,0.2823,no
NHMT_EMENI,Q5B467,ProtT3,Eukaryota,558,"Protein-histidine N-methyltransferase that specifically mediates 3-methylhistidine (tele-methylhistidine) methylation at 'His- 1', which protects the side-chain from oxidative damage. Methylates lytic polysaccharide monooxygenases (LPMOs) destined for secretion, including AN4702.",S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that methylates histone H3 to form H3K79me. Cytoplasm Nucleus. Belongs to the class I-like SAM-binding methyltransferase superfamily. METTL16/RMT2 methyltransferase family,Maybe,No,No,No,Maybe,not-Yes,GO:0018064,GO:0018024,GO:0018024,GO:0018024,GO:0018024; GO:0008757,GO:0018024,0.0,0.0,0.0,0.6827,0.0,5,0.1365,0.2823,no
NHMT_EMENI,Q5B467,ProtTale,Eukaryota,558,"Protein-histidine N-methyltransferase that specifically mediates 3-methylhistidine (tele-methylhistidine) methylation at 'His- 1', which protects the side-chain from oxidative damage. Methylates lytic polysaccharide monooxygenases (LPMOs) destined for secretion, including AN4702.","Alpha-ketoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activity, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3- hydroxyleucine (HyLeu), alpha-aminoisobutyric acid",No,No,No,No,No,not-Yes,GO:0018064,GO:0016706,GO:0016706,GO:0016706,GO:0016706,GO:0016706,0.1725,0.1725,0.1725,0.1725,0.1725,5,0.1725,0.2823,no
NHMT_EMENI,Q5B467,Protein2Text,Eukaryota,558,"Protein-histidine N-methyltransferase that specifically mediates 3-methylhistidine (tele-methylhistidine) methylation at 'His- 1', which protects the side-chain from oxidative damage. Methylates lytic polysaccharide monooxygenases (LPMOs) destined for secretion, including AN4702.","The molecular function of this protein is a prenyltransferase, which is an enzyme that catalyzes the transfer of a prenyl group from a donor molecule to a protein substrate. More specifically, it is a polyprenyl transferase that catalyzes the transfer of a polyprenyl group to a protein substrate, which is a common modification in eukaryotic proteins. This modification is involved in various cellular processes, including protein transport, signaling, and protein-protein interactions.",No,No,No,No,No,not-Yes,GO:0018064,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,0.2927,0.2927,0.2927,0.2927,0.2927,5,0.2927,0.2823,no
NHMT_EMENI,Q5B467,Reference,Eukaryota,558,"Protein-histidine N-methyltransferase that specifically mediates 3-methylhistidine (tele-methylhistidine) methylation at 'His- 1', which protects the side-chain from oxidative damage. Methylates lytic polysaccharide monooxygenases (LPMOs) destined for secretion, including AN4702.","Protein-histidine N-methyltransferase that specifically mediates 3-methylhistidine (tele-methylhistidine) methylation at 'His- 1', which protects the side-chain from oxidative damage. Methylates lytic polysaccharide monooxygenases (LPMOs) destined for secretion, including AN4702.",,,,,,,GO:0018064,GO:0008276,GO:0008276,GO:0008168,GO:0008276,GO:0008276,0.7725,0.7725,0.5913,0.7725,0.7725,5,0.7363,0.2823,no
CID14_CRYD1,Q5K9E2,ESM2Text,Eukaryota,762,Required for 3' polyadenylation of the 5.8S and 25S rRNAs as a prelude to their degradation in the exosome. Involved in the nucleolar organization to ensure faithful chromosome segregation during mitosis.,Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.,Maybe,No,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0046872; GO:1990817,,,,GO:0019843,,,,,0.1762,,1,0.1762,0.6569,yes
CID14_CRYD1,Q5K9E2,Prot2Text,Eukaryota,762,Required for 3' polyadenylation of the 5.8S and 25S rRNAs as a prelude to their degradation in the exosome. Involved in the nucleolar organization to ensure faithful chromosome segregation during mitosis.,Polymerase that creates the 3'-poly(A) tail of mRNA's. May acquire specificity through interaction with a cleavage and polyadenylation factor (CPSF).,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0046872; GO:1990817,GO:0004652,GO:0004652,GO:0004652,GO:0004652,GO:0004652,0.0,0.0,0.0,0.0,0.0,5,0.0,0.6569,yes
CID14_CRYD1,Q5K9E2,ProtT3,Eukaryota,762,Required for 3' polyadenylation of the 5.8S and 25S rRNAs as a prelude to their degradation in the exosome. Involved in the nucleolar organization to ensure faithful chromosome segregation during mitosis.,Protein poly(A) polymerase that adds poly(A) tails to pre- mRNAs. Nucleus. Belongs to the poly(A) polymerase family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0046872; GO:1990817,GO:0004652,GO:0004652; GO:0005524,GO:0004652,GO:0004652,GO:0004652,0.0,0.5846,0.0,0.0,0.0,5,0.1169,0.6569,yes
CID14_CRYD1,Q5K9E2,ProtTale,Eukaryota,762,Required for 3' polyadenylation of the 5.8S and 25S rRNAs as a prelude to their degradation in the exosome. Involved in the nucleolar organization to ensure faithful chromosome segregation during mitosis.,Polymerase that creates the 3'-poly(A) tail of mRNA's.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0046872; GO:1990817,GO:0004652,GO:0004652,GO:0004652,GO:0004652,GO:0004652,0.0,0.0,0.0,0.0,0.0,5,0.0,0.6569,yes
CID14_CRYD1,Q5K9E2,Protein2Text,Eukaryota,762,Required for 3' polyadenylation of the 5.8S and 25S rRNAs as a prelude to their degradation in the exosome. Involved in the nucleolar organization to ensure faithful chromosome segregation during mitosis.,"The molecular function of this protein is DNA-binding. Specifically, it is involved in the degradation of RNA polymerase II transcripts, which helps to regulate gene expression.",No,No,No,No,No,not-Yes,GO:0005524; GO:0046872; GO:1990817,GO:0003677,GO:0003677,GO:0003677,GO:0003677,GO:0003677,0.2116,0.2116,0.2116,0.2116,0.2116,5,0.2116,0.6569,yes
CID14_CRYD1,Q5K9E2,Reference,Eukaryota,762,Required for 3' polyadenylation of the 5.8S and 25S rRNAs as a prelude to their degradation in the exosome. Involved in the nucleolar organization to ensure faithful chromosome segregation during mitosis.,Required for 3' polyadenylation of the 5.8S and 25S rRNAs as a prelude to their degradation in the exosome. Involved in the nucleolar organization to ensure faithful chromosome segregation during mitosis.,,,,,,,GO:0005524; GO:0046872; GO:1990817,,,,,,,,,,,0,,0.6569,yes
AGAO_MICTH,Q5KTI5,ESM2Text,Bacteria,1175,"Endo-type beta-agarase, which degrades agarose and agarose oligosaccharides more polymerized than hexamers to yield neoagarohexaose (NA6) as the main product, with lesser amounts of neoagarotetraose (NA4) and neoagarobiose (NA2).","Alpha-agarase involved in the degradation of agarose, which is the major product of arabinoxylan, a major component of plant hemicellulose. Able to hydrolyze p-nitrophenyl-alpha-agarotetraose (pNP-GA) and p-nitrophenyl-beta-agarotetraose (pNP-GA), but not p-nitrophenyl-alpha-galactopyranoside (pNP-Gal). The major product is pNP-GA from A.niger. Also hydrolyzes pNP-GA and pNP-GA, but not pNP-OH or pNP-C. Does not show lytic activity towards barley beta-glucan, soluble starch, p-nitrophenyl-alpha-L-arabinofuran, pNP-GA, pNP-GA-L-arabinofuran or pNP-GA-L-arabinofuran.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0033916; GO:0005509; GO:0030246,GO:0016798,GO:0004553,GO:0016798,,GO:0016798,0.4459,0.4973,0.4459,,0.4459,4,0.4587,0.2534,no
AGAO_MICTH,Q5KTI5,Prot2Text,Bacteria,1175,"Endo-type beta-agarase, which degrades agarose and agarose oligosaccharides more polymerized than hexamers to yield neoagarohexaose (NA6) as the main product, with lesser amounts of neoagarotetraose (NA4) and neoagarobiose (NA2).","Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Able to hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan.",No,No,No,No,No,not-Yes,GO:0033916; GO:0005509; GO:0030246,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,0.4232,0.4232,0.4232,0.4232,0.4232,5,0.4232,0.2534,no
AGAO_MICTH,Q5KTI5,ProtT3,Bacteria,1175,"Endo-type beta-agarase, which degrades agarose and agarose oligosaccharides more polymerized than hexamers to yield neoagarohexaose (NA6) as the main product, with lesser amounts of neoagarotetraose (NA4) and neoagarobiose (NA2).",Secreted. Belongs to the glycosyl hydrolase 43 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0033916; GO:0005509; GO:0030246,,GO:0016798,GO:0016798,GO:0016798,GO:0016798,,0.4459,0.4459,0.4459,0.4459,4,0.4459,0.2534,no
AGAO_MICTH,Q5KTI5,ProtTale,Bacteria,1175,"Endo-type beta-agarase, which degrades agarose and agarose oligosaccharides more polymerized than hexamers to yield neoagarohexaose (NA6) as the main product, with lesser amounts of neoagarotetraose (NA4) and neoagarobiose (NA2).","Catalyzes the endohydrolysis of the (1->3)-alpha-L-glucosidic linkages in alpha-L-rhamnogalacturonan I (RG-I), a major component of plant cell walls. RG-I is one of the most abundant cell wall polysaccharides in plants and is composed of alpha-(1->4)-linked rhamnogalacturonan I (RG-I) and alpha-(1->3)- and alpha-(1->4)-linked rhamnogalacturonan II (RG-II). RG-",No,No,No,No,No,not-Yes,GO:0033916; GO:0005509; GO:0030246,GO:0004553,GO:0016798,GO:0016798,GO:0004553,GO:0004553,0.4973,0.4459,0.4459,0.4973,0.4973,5,0.4767,0.2534,no
AGAO_MICTH,Q5KTI5,Protein2Text,Bacteria,1175,"Endo-type beta-agarase, which degrades agarose and agarose oligosaccharides more polymerized than hexamers to yield neoagarohexaose (NA6) as the main product, with lesser amounts of neoagarotetraose (NA4) and neoagarobiose (NA2).","This protein is a cellulase, which means it catalyzes the hydrolysis of cellulose, a complex carbohydrate found in plant cell walls. More specifically, it is likely to be a beta-glucosidase, which is a type of cellulase that breaks down beta-glucosidic bonds in cellulose. This protein is likely involved in the breakdown of cellulose for nutrient acquisition.",No,No,No,No,No,not-Yes,GO:0033916; GO:0005509; GO:0030246,GO:0008422; GO:0030245,GO:0008422; GO:0030245,GO:0008422; GO:0030245,GO:0008422; GO:0030245,GO:0008810,0.2949,0.2949,0.2949,0.2949,0.4232,5,0.3206,0.2534,no
AGAO_MICTH,Q5KTI5,Reference,Bacteria,1175,"Endo-type beta-agarase, which degrades agarose and agarose oligosaccharides more polymerized than hexamers to yield neoagarohexaose (NA6) as the main product, with lesser amounts of neoagarotetraose (NA4) and neoagarobiose (NA2).","Endo-type beta-agarase, which degrades agarose and agarose oligosaccharides more polymerized than hexamers to yield neoagarohexaose (NA6) as the main product, with lesser amounts of neoagarotetraose (NA4) and neoagarobiose (NA2).",,,,,,,GO:0033916; GO:0005509; GO:0030246,GO:0016162,GO:0004553,GO:0016160,GO:0016798,GO:0004553,0.4232,0.4973,0.4232,0.4459,0.4973,5,0.4574,0.2534,no
LDHA_CLODI,Q5U922,ESM2Text,Bacteria,332,"Involved in the reductive branch of L-leucine fermentation. Catalyzes the NADH-dependent reduction of 4-methyl- 2-oxopentanoate (2-oxoisocaproate) to (R)-2-hydroxy-4-methylpentanoate ((R)-2-hydroxyisocaproate). For the reverse reaction, the enzyme accepts (R)- but not (S)-2-hydroxy-4-methylpentanoate. Can also use 2-oxopentanoate, 2-oxohexanoate and phenylpyruvate but not 2-oxoisovalerate and 2-oxobutyrate. Cannot use NADPH.",Catalyzes the reduction of 2-keto acids to 2-hydroxy acids.,Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0008720; GO:0051287,GO:0016491,GO:0016616,GO:0016491,GO:0016491,GO:0016491,0.3129,0.4191,0.3129,0.3129,0.3129,5,0.3341,0.2435,no
LDHA_CLODI,Q5U922,Prot2Text,Bacteria,332,"Involved in the reductive branch of L-leucine fermentation. Catalyzes the NADH-dependent reduction of 4-methyl- 2-oxopentanoate (2-oxoisocaproate) to (R)-2-hydroxy-4-methylpentanoate ((R)-2-hydroxyisocaproate). For the reverse reaction, the enzyme accepts (R)- but not (S)-2-hydroxy-4-methylpentanoate. Can also use 2-oxopentanoate, 2-oxohexanoate and phenylpyruvate but not 2-oxoisovalerate and 2-oxobutyrate. Cannot use NADPH.",Has both D-lactate and D-glycerate dehydrogenase activities. Equally active on pyruvate and hydroxypyruvate.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008720; GO:0051287,GO:0008720,GO:0008720,GO:0008720,GO:0008720,GO:0008720,0.683,0.683,0.683,0.683,0.683,5,0.683,0.2435,no
LDHA_CLODI,Q5U922,ProtT3,Bacteria,332,"Involved in the reductive branch of L-leucine fermentation. Catalyzes the NADH-dependent reduction of 4-methyl- 2-oxopentanoate (2-oxoisocaproate) to (R)-2-hydroxy-4-methylpentanoate ((R)-2-hydroxyisocaproate). For the reverse reaction, the enzyme accepts (R)- but not (S)-2-hydroxy-4-methylpentanoate. Can also use 2-oxopentanoate, 2-oxohexanoate and phenylpyruvate but not 2-oxoisovalerate and 2-oxobutyrate. Cannot use NADPH.",Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008720; GO:0051287,,GO:0016616,GO:0016616,GO:0016616,,,0.4191,0.4191,0.4191,,3,0.4191,0.2435,no
LDHA_CLODI,Q5U922,ProtTale,Bacteria,332,"Involved in the reductive branch of L-leucine fermentation. Catalyzes the NADH-dependent reduction of 4-methyl- 2-oxopentanoate (2-oxoisocaproate) to (R)-2-hydroxy-4-methylpentanoate ((R)-2-hydroxyisocaproate). For the reverse reaction, the enzyme accepts (R)- but not (S)-2-hydroxy-4-methylpentanoate. Can also use 2-oxopentanoate, 2-oxohexanoate and phenylpyruvate but not 2-oxoisovalerate and 2-oxobutyrate. Cannot use NADPH.",Essential for the biosynthesis of L-tryptophan from indole and L-serine.,Maybe,No,No,No,Maybe,not-Yes,GO:0008720; GO:0051287,GO:0004834,GO:0004834,GO:0004834,GO:0004834,GO:0004834,0.1145,0.1145,0.1145,0.1145,0.1145,5,0.1145,0.2435,no
LDHA_CLODI,Q5U922,Protein2Text,Bacteria,332,"Involved in the reductive branch of L-leucine fermentation. Catalyzes the NADH-dependent reduction of 4-methyl- 2-oxopentanoate (2-oxoisocaproate) to (R)-2-hydroxy-4-methylpentanoate ((R)-2-hydroxyisocaproate). For the reverse reaction, the enzyme accepts (R)- but not (S)-2-hydroxy-4-methylpentanoate. Can also use 2-oxopentanoate, 2-oxohexanoate and phenylpyruvate but not 2-oxoisovalerate and 2-oxobutyrate. Cannot use NADPH.",The molecular function of this protein is an enzyme that catalyzes the conversion of 3-phosphoglycerate to phosphoenolpyruvate.,No,No,No,No,No,not-Yes,GO:0008720; GO:0051287,,GO:0004634,GO:0016829,,,,0.1145,0.2019,,,2,0.1582,0.2435,no
LDHA_CLODI,Q5U922,Reference,Bacteria,332,"Involved in the reductive branch of L-leucine fermentation. Catalyzes the NADH-dependent reduction of 4-methyl- 2-oxopentanoate (2-oxoisocaproate) to (R)-2-hydroxy-4-methylpentanoate ((R)-2-hydroxyisocaproate). For the reverse reaction, the enzyme accepts (R)- but not (S)-2-hydroxy-4-methylpentanoate. Can also use 2-oxopentanoate, 2-oxohexanoate and phenylpyruvate but not 2-oxoisovalerate and 2-oxobutyrate. Cannot use NADPH.","Involved in the reductive branch of L-leucine fermentation. Catalyzes the NADH-dependent reduction of 4-methyl- 2-oxopentanoate (2-oxoisocaproate) to (R)-2-hydroxy-4-methylpentanoate ((R)-2-hydroxyisocaproate). For the reverse reaction, the enzyme accepts (R)- but not (S)-2-hydroxy-4-methylpentanoate. Can also use 2-oxopentanoate, 2-oxohexanoate and phenylpyruvate but not 2-oxoisovalerate and 2-oxobutyrate. Cannot use NADPH.",,,,,,,GO:0008720; GO:0051287,GO:0016616; GO:0051287,GO:0016616,GO:0016491; GO:0051287,GO:0016616,GO:0016616,0.7935,0.4191,0.703,0.4191,0.4191,5,0.5508,0.2435,no
SKI2_MOUSE,Q6NZR5,ESM2Text,Eukaryota,1244,"Helicase component of the SKI complex, a multiprotein complex that assists the RNA-degrading exosome during the mRNA decay and quality-control pathways. The SKI complex catalyzes mRNA extraction from 80S ribosomal complexes in the 3'-5' direction and channels mRNA to the cytosolic exosome for degradation. SKI-mediated extraction of mRNA from stalled ribosomes allow binding of the Pelota-HBS1L complex and subsequent ribosome disassembly by ABCE1 for ribosome recycling. In the nucleus, the SKI complex associates with transcriptionally active genes in a manner dependent on PAF1 complex (PAF1C). May play a role in the non-stop mRNA decay pathway (NSD), which specifically targets and degrades mRNAs that lack a proper stop codon.",Component of the SKI complex involved in 3'-mRNA degradation pathway. Represses the transcriptional activation of mSIN3A by binding to the regulatory region of SKI. Facilitates the association of SKI with the SKI complex.,Maybe,No,Maybe,Maybe,Yes,not-Yes,GO:0034458; GO:0005524; GO:0016787; GO:0003723; GO:0003724,,,,GO:0003723,,,,,0.4289,,1,0.4289,0.608,yes
SKI2_MOUSE,Q6NZR5,Prot2Text,Eukaryota,1244,"Helicase component of the SKI complex, a multiprotein complex that assists the RNA-degrading exosome during the mRNA decay and quality-control pathways. The SKI complex catalyzes mRNA extraction from 80S ribosomal complexes in the 3'-5' direction and channels mRNA to the cytosolic exosome for degradation. SKI-mediated extraction of mRNA from stalled ribosomes allow binding of the Pelota-HBS1L complex and subsequent ribosome disassembly by ABCE1 for ribosome recycling. In the nucleus, the SKI complex associates with transcriptionally active genes in a manner dependent on PAF1 complex (PAF1C). May play a role in the non-stop mRNA decay pathway (NSD), which specifically targets and degrades mRNAs that lack a proper stop codon.",Plays an essential role in pre-mRNA splicing as component of the activated spliceosome. Is required for the first step of pre-mRNA splicing.,No,No,No,No,No,not-Yes,GO:0034458; GO:0005524; GO:0016787; GO:0003723; GO:0003724,,,,,,,,,,,0,,0.608,yes
SKI2_MOUSE,Q6NZR5,ProtT3,Eukaryota,1244,"Helicase component of the SKI complex, a multiprotein complex that assists the RNA-degrading exosome during the mRNA decay and quality-control pathways. The SKI complex catalyzes mRNA extraction from 80S ribosomal complexes in the 3'-5' direction and channels mRNA to the cytosolic exosome for degradation. SKI-mediated extraction of mRNA from stalled ribosomes allow binding of the Pelota-HBS1L complex and subsequent ribosome disassembly by ABCE1 for ribosome recycling. In the nucleus, the SKI complex associates with transcriptionally active genes in a manner dependent on PAF1 complex (PAF1C). May play a role in the non-stop mRNA decay pathway (NSD), which specifically targets and degrades mRNAs that lack a proper stop codon.",3'-5' RNA helicase involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Cytoplasm Nucleus. Belongs to the DEAD box helicase family. DEAH subfamily,Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0034458; GO:0005524; GO:0016787; GO:0003723; GO:0003724,GO:0003724; GO:0005524,GO:0003724; GO:0005524,GO:0003724; GO:0005524,GO:0003724; GO:0005524,GO:0003724; GO:0005524,0.764,0.764,0.764,0.764,0.764,5,0.764,0.608,yes
SKI2_MOUSE,Q6NZR5,ProtTale,Eukaryota,1244,"Helicase component of the SKI complex, a multiprotein complex that assists the RNA-degrading exosome during the mRNA decay and quality-control pathways. The SKI complex catalyzes mRNA extraction from 80S ribosomal complexes in the 3'-5' direction and channels mRNA to the cytosolic exosome for degradation. SKI-mediated extraction of mRNA from stalled ribosomes allow binding of the Pelota-HBS1L complex and subsequent ribosome disassembly by ABCE1 for ribosome recycling. In the nucleus, the SKI complex associates with transcriptionally active genes in a manner dependent on PAF1 complex (PAF1C). May play a role in the non-stop mRNA decay pathway (NSD), which specifically targets and degrades mRNAs that lack a proper stop codon.","Component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in their 3'-5' degradation of unstable RNA species such as mRNAs, in their 5'-3' exonucleolytic degradation of noncoding transcripts such as antisense RNAs (asRNAs) and cryptic unstable transcripts (CUTs), and in their degradation of nascent RNA transcripts. In the cytoplasm, the complex mediates the",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0034458; GO:0005524; GO:0016787; GO:0003723; GO:0003724,GO:0000175,GO:0000175,GO:0000175,GO:0000175,GO:0000175,0.2224,0.2224,0.2224,0.2224,0.2224,5,0.2224,0.608,yes
SKI2_MOUSE,Q6NZR5,Protein2Text,Eukaryota,1244,"Helicase component of the SKI complex, a multiprotein complex that assists the RNA-degrading exosome during the mRNA decay and quality-control pathways. The SKI complex catalyzes mRNA extraction from 80S ribosomal complexes in the 3'-5' direction and channels mRNA to the cytosolic exosome for degradation. SKI-mediated extraction of mRNA from stalled ribosomes allow binding of the Pelota-HBS1L complex and subsequent ribosome disassembly by ABCE1 for ribosome recycling. In the nucleus, the SKI complex associates with transcriptionally active genes in a manner dependent on PAF1 complex (PAF1C). May play a role in the non-stop mRNA decay pathway (NSD), which specifically targets and degrades mRNAs that lack a proper stop codon.","This protein is a type of molecular motor, specifically a dynein heavy chain protein, which is involved in the movement of cilia and flagella in cells. It plays a crucial role in the proper functioning of cilia and flagella by converting chemical energy into mechanical energy, allowing for the movement of these structures.",No,No,No,No,No,not-Yes,GO:0034458; GO:0005524; GO:0016787; GO:0003723; GO:0003724,GO:0003777; GO:0005524,GO:0003777,GO:0003774; GO:0005524,GO:0003774; GO:0005524,GO:0003777,0.536,0.2984,0.4629,0.4629,0.2984,5,0.4117,0.608,yes
SKI2_MOUSE,Q6NZR5,Reference,Eukaryota,1244,"Helicase component of the SKI complex, a multiprotein complex that assists the RNA-degrading exosome during the mRNA decay and quality-control pathways. The SKI complex catalyzes mRNA extraction from 80S ribosomal complexes in the 3'-5' direction and channels mRNA to the cytosolic exosome for degradation. SKI-mediated extraction of mRNA from stalled ribosomes allow binding of the Pelota-HBS1L complex and subsequent ribosome disassembly by ABCE1 for ribosome recycling. In the nucleus, the SKI complex associates with transcriptionally active genes in a manner dependent on PAF1 complex (PAF1C). May play a role in the non-stop mRNA decay pathway (NSD), which specifically targets and degrades mRNAs that lack a proper stop codon.","Helicase component of the SKI complex, a multiprotein complex that assists the RNA-degrading exosome during the mRNA decay and quality-control pathways. The SKI complex catalyzes mRNA extraction from 80S ribosomal complexes in the 3'-5' direction and channels mRNA to the cytosolic exosome for degradation. SKI-mediated extraction of mRNA from stalled ribosomes allow binding of the Pelota-HBS1L complex and subsequent ribosome disassembly by ABCE1 for ribosome recycling. In the nucleus, the SKI complex associates with transcriptionally active genes in a manner dependent on PAF1 complex (PAF1C). May play a role in the non-stop mRNA decay pathway (NSD), which specifically targets and degrades mRNAs that lack a proper stop codon.",,,,,,,GO:0034458; GO:0005524; GO:0016787; GO:0003723; GO:0003724,GO:0004386; GO:0005524,GO:0004386; GO:0005524,GO:0003724; GO:0016887,GO:0004386; GO:0003723,GO:0003724,0.6934,0.6934,0.5791,0.6934,0.5563,5,0.6431,0.608,yes
SYWC_DANRE,Q6PBS3,ESM2Text,Eukaryota,463,Catalyzes the attachment of tryptophan to tRNA(Trp) in a two- step reaction: tryptophan is first activated by ATP to form Trp-AMP and then transferred to the acceptor end of the tRNA(Trp). Could also possess an angiostatic activity.,Aspartyl-tRNA synthetase that catalyzes the attachment of aminoacyl-tRNA(Asp) to tRNA(Asn). The tRNA(Asp) attachment is aminoacylated and inhibited by the binding of gamma-aminobutyrate (GABA) to tRNA(Asn).,Maybe,No,No,No,No,not-Yes,GO:0005524; GO:0004830,GO:0004815,GO:0004815,GO:0004815,GO:0004815; GO:0005524,GO:0004815; GO:0005524,0.5563,0.5563,0.5563,0.9048,0.9048,5,0.6957,0.4288,no
SYWC_DANRE,Q6PBS3,Prot2Text,Eukaryota,463,Catalyzes the attachment of tryptophan to tRNA(Trp) in a two- step reaction: tryptophan is first activated by ATP to form Trp-AMP and then transferred to the acceptor end of the tRNA(Trp). Could also possess an angiostatic activity.,Catalyzes the attachment of tryptophan to tRNA(Trp).,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0004830,GO:0004830,GO:0004830,GO:0004830,GO:0004830,GO:0004830,0.6832,0.6832,0.6832,0.6832,0.6832,5,0.6832,0.4288,no
SYWC_DANRE,Q6PBS3,ProtT3,Eukaryota,463,Catalyzes the attachment of tryptophan to tRNA(Trp) in a two- step reaction: tryptophan is first activated by ATP to form Trp-AMP and then transferred to the acceptor end of the tRNA(Trp). Could also possess an angiostatic activity.,Cytoplasm. Belongs to the class-I aminoacyl-tRNA synthetase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0004830,,GO:0004812; GO:0005524,GO:0004812,GO:0004812; GO:0005524,,,0.9527,0.6219,0.9527,,3,0.8424,0.4288,no
SYWC_DANRE,Q6PBS3,ProtTale,Eukaryota,463,Catalyzes the attachment of tryptophan to tRNA(Trp) in a two- step reaction: tryptophan is first activated by ATP to form Trp-AMP and then transferred to the acceptor end of the tRNA(Trp). Could also possess an angiostatic activity.,Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).,Maybe,No,No,No,No,not-Yes,GO:0005524; GO:0004830,GO:0004831; GO:0005524,GO:0004831; GO:0005524,GO:0004831,GO:0004831; GO:0005524,GO:0004831,0.9048,0.9048,0.5563,0.9048,0.5563,5,0.7654,0.4288,no
SYWC_DANRE,Q6PBS3,Protein2Text,Eukaryota,463,Catalyzes the attachment of tryptophan to tRNA(Trp) in a two- step reaction: tryptophan is first activated by ATP to form Trp-AMP and then transferred to the acceptor end of the tRNA(Trp). Could also possess an angiostatic activity.,"This protein is a tRNA ligase, which is involved in the attachment of amino acids to tRNA molecules. Specifically, it catalyzes the attachment of tyrosine to its cognate tRNA molecule.",Maybe,No,Maybe,Maybe,No,not-Yes,GO:0005524; GO:0004830,GO:0004831,GO:0004831,GO:0004831,GO:0004831,GO:0004831,0.5563,0.5563,0.5563,0.5563,0.5563,5,0.5563,0.4288,no
SYWC_DANRE,Q6PBS3,Reference,Eukaryota,463,Catalyzes the attachment of tryptophan to tRNA(Trp) in a two- step reaction: tryptophan is first activated by ATP to form Trp-AMP and then transferred to the acceptor end of the tRNA(Trp). Could also possess an angiostatic activity.,Catalyzes the attachment of tryptophan to tRNA(Trp) in a two- step reaction: tryptophan is first activated by ATP to form Trp-AMP and then transferred to the acceptor end of the tRNA(Trp). Could also possess an angiostatic activity.,,,,,,,GO:0005524; GO:0004830,GO:0004830; GO:0005524,GO:0004830; GO:0005524,GO:0004830; GO:0005524,GO:0004830; GO:0005524,GO:0004830; GO:0005524,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4288,no
MGH_THET2,Q72K04,ESM2Text,Bacteria,415,"Hydrolase that catalyzes the hydrolysis of mannosylglycerate (MG), a solute produced in response to osmotic stress in thermophiles, into mannose and glycerate. Can also hydrolyze glucosylglycerate (GG) to glucose and glycerate, with similar catalytic efficiency. Is highly specific for MG and GG, and cannot use mannosylglyceramide (MGA), glucosylglycerol, mannosylglucosylglycerate (MGG), glucosylglucosylglycerate (GGG) or trehalose as substrates.","Involved in the degradation of glucomannan. Catalyzes the hydrolysis of alpha-1,2-linked mannose-1-phosphate (Man1P) to mannose-6-phosphate (Man6P).",No,Maybe,Maybe,No,Maybe,not-Yes,GO:0004573; GO:0102546,GO:0016787,GO:0004553,GO:0016787,GO:0004553,GO:0016787,0.5649,0.5833,0.5649,0.5833,0.5649,5,0.5723,0.3479,no
MGH_THET2,Q72K04,Prot2Text,Bacteria,415,"Hydrolase that catalyzes the hydrolysis of mannosylglycerate (MG), a solute produced in response to osmotic stress in thermophiles, into mannose and glycerate. Can also hydrolyze glucosylglycerate (GG) to glucose and glycerate, with similar catalytic efficiency. Is highly specific for MG and GG, and cannot use mannosylglyceramide (MGA), glucosylglycerol, mannosylglucosylglycerate (MGG), glucosylglucosylglycerate (GGG) or trehalose as substrates.",Catalyzes the hydrolysis of alpha-D-mannosyl-glycerate (MG) to D-glycerate and D-mannose. Can also hydrolyze alpha-D-glucopyranosyl-glycerate (GG)with lower efficiency.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004573; GO:0102546,GO:0004559,GO:0004559,GO:0004559,GO:0004559,GO:0004559,0.4163,0.4163,0.4163,0.4163,0.4163,5,0.4163,0.3479,no
MGH_THET2,Q72K04,ProtT3,Bacteria,415,"Hydrolase that catalyzes the hydrolysis of mannosylglycerate (MG), a solute produced in response to osmotic stress in thermophiles, into mannose and glycerate. Can also hydrolyze glucosylglycerate (GG) to glucose and glycerate, with similar catalytic efficiency. Is highly specific for MG and GG, and cannot use mannosylglyceramide (MGA), glucosylglycerol, mannosylglucosylglycerate (MGG), glucosylglucosylglycerate (GGG) or trehalose as substrates.",Belongs to the glycosyl hydrolase 32 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004573; GO:0102546,GO:0004564,GO:0016798,GO:0016798,GO:0016798,GO:0016798,0.4874,0.5507,0.5507,0.5507,0.5507,5,0.538,0.3479,no
MGH_THET2,Q72K04,ProtTale,Bacteria,415,"Hydrolase that catalyzes the hydrolysis of mannosylglycerate (MG), a solute produced in response to osmotic stress in thermophiles, into mannose and glycerate. Can also hydrolyze glucosylglycerate (GG) to glucose and glycerate, with similar catalytic efficiency. Is highly specific for MG and GG, and cannot use mannosylglyceramide (MGA), glucosylglycerol, mannosylglucosylglycerate (MGG), glucosylglucosylglycerate (GGG) or trehalose as substrates.","Cleaves the terminal alpha,1-1,4-linked glucose residue from the non-reducing end of maltodextrins and maltooligosaccharides, releasing alpha-D-glucose in an ATP-dependent manner.",No,No,No,No,No,not-Yes,GO:0004573; GO:0102546,GO:0004339,GO:0004339; GO:0005524,GO:0004339; GO:0005524,GO:0004553,GO:0004553,0.5934,0.459,0.459,0.5833,0.5833,5,0.5356,0.3479,no
MGH_THET2,Q72K04,Protein2Text,Bacteria,415,"Hydrolase that catalyzes the hydrolysis of mannosylglycerate (MG), a solute produced in response to osmotic stress in thermophiles, into mannose and glycerate. Can also hydrolyze glucosylglycerate (GG) to glucose and glycerate, with similar catalytic efficiency. Is highly specific for MG and GG, and cannot use mannosylglyceramide (MGA), glucosylglycerol, mannosylglucosylglycerate (MGG), glucosylglucosylglycerate (GGG) or trehalose as substrates.",This protein is involved in the molecular function of carbohydrate metabolic process.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004573; GO:0102546,,,,,,,,,,,0,,0.3479,no
MGH_THET2,Q72K04,Reference,Bacteria,415,"Hydrolase that catalyzes the hydrolysis of mannosylglycerate (MG), a solute produced in response to osmotic stress in thermophiles, into mannose and glycerate. Can also hydrolyze glucosylglycerate (GG) to glucose and glycerate, with similar catalytic efficiency. Is highly specific for MG and GG, and cannot use mannosylglyceramide (MGA), glucosylglycerol, mannosylglucosylglycerate (MGG), glucosylglucosylglycerate (GGG) or trehalose as substrates.","Hydrolase that catalyzes the hydrolysis of mannosylglycerate (MG), a solute produced in response to osmotic stress in thermophiles, into mannose and glycerate. Can also hydrolyze glucosylglycerate (GG) to glucose and glycerate, with similar catalytic efficiency. Is highly specific for MG and GG, and cannot use mannosylglyceramide (MGA), glucosylglycerol, mannosylglucosylglycerate (MGG), glucosylglucosylglycerate (GGG) or trehalose as substrates.",,,,,,,GO:0004573; GO:0102546,GO:0016787,GO:0004553,GO:0004553,GO:0016798,GO:0004553,0.5649,0.5833,0.5833,0.5507,0.5833,5,0.5731,0.3479,no
LNBLN_TREDE,Q73LY9,ESM2Text,Bacteria,354,"Hydrolase that shows both lacto-N-biosidase (LNBase) and N- acetyllactosaminidase (LacNAcase) activity. It catalyzes the release of the disaccharide lacto-N-biose (LNB, Gal- beta1,3-GlcNAc) from the non-reducing end of glycans such as lacto-N- tetraose (LNT). It also catalyzes the release of N- acetyllactosamine (LacNAc, Gal-beta1,4-GlcNAc) from lacto-N-neotetraose (LNnT). Displays activity on the synthetic substrates pNP-LNB (p-nitrophenyl-beta-lacto-N-bioside) and pNP-LacNAc (p- nitrophenyl-beta-N-acetyllactosaminide). Shows weak activity with pNP-6S-GlcNAc and pNP-GalNAc, but cannot use lacto-N- triose II (LNT2, GlcNAc-beta1,3-Gal-beta1,4-Glc) and N,N'- diacetylchitobiose. The low level of activity with LNT and LNnT suggests that they are not the natural substrates for this enzyme.","Hydrolyzes the non-reducing terminal alpha-L-arabinosylglycans of glycoproteins. Most active against terminal alpha-L-arabinofuranosyl-(1->6)-linked arabinan. No activity against terminal alpha-linked arabinofuranosyl-(1->6)-linked oligosaccharides or paranitrophenyl-beta-1,5-glucan.",No,No,No,No,No,not-Yes,GO:0004563; GO:0046872,GO:0046556,GO:0046556,GO:0016798,GO:0046556,GO:0046556,0.452,0.452,0.4732,0.452,0.452,5,0.4562,0.4095,no
LNBLN_TREDE,Q73LY9,Prot2Text,Bacteria,354,"Hydrolase that shows both lacto-N-biosidase (LNBase) and N- acetyllactosaminidase (LacNAcase) activity. It catalyzes the release of the disaccharide lacto-N-biose (LNB, Gal- beta1,3-GlcNAc) from the non-reducing end of glycans such as lacto-N- tetraose (LNT). It also catalyzes the release of N- acetyllactosamine (LacNAc, Gal-beta1,4-GlcNAc) from lacto-N-neotetraose (LNnT). Displays activity on the synthetic substrates pNP-LNB (p-nitrophenyl-beta-lacto-N-bioside) and pNP-LacNAc (p- nitrophenyl-beta-N-acetyllactosaminide). Shows weak activity with pNP-6S-GlcNAc and pNP-GalNAc, but cannot use lacto-N- triose II (LNT2, GlcNAc-beta1,3-Gal-beta1,4-Glc) and N,N'- diacetylchitobiose. The low level of activity with LNT and LNnT suggests that they are not the natural substrates for this enzyme.",Has a broad substrate specificity.,Vague,No,No,No,Vague,not-Yes,GO:0004563; GO:0046872,,,,,,,,,,,0,,0.4095,no
LNBLN_TREDE,Q73LY9,ProtT3,Bacteria,354,"Hydrolase that shows both lacto-N-biosidase (LNBase) and N- acetyllactosaminidase (LacNAcase) activity. It catalyzes the release of the disaccharide lacto-N-biose (LNB, Gal- beta1,3-GlcNAc) from the non-reducing end of glycans such as lacto-N- tetraose (LNT). It also catalyzes the release of N- acetyllactosamine (LacNAc, Gal-beta1,4-GlcNAc) from lacto-N-neotetraose (LNnT). Displays activity on the synthetic substrates pNP-LNB (p-nitrophenyl-beta-lacto-N-bioside) and pNP-LacNAc (p- nitrophenyl-beta-N-acetyllactosaminide). Shows weak activity with pNP-6S-GlcNAc and pNP-GalNAc, but cannot use lacto-N- triose II (LNT2, GlcNAc-beta1,3-Gal-beta1,4-Glc) and N,N'- diacetylchitobiose. The low level of activity with LNT and LNnT suggests that they are not the natural substrates for this enzyme.",Secreted. Belongs to the glycosyl hydrolase 20 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004563; GO:0046872,GO:0004563,GO:0004563,GO:0016798,GO:0004563,GO:0016798,0.6924,0.6924,0.4732,0.6924,0.4732,5,0.6047,0.4095,no
LNBLN_TREDE,Q73LY9,ProtTale,Bacteria,354,"Hydrolase that shows both lacto-N-biosidase (LNBase) and N- acetyllactosaminidase (LacNAcase) activity. It catalyzes the release of the disaccharide lacto-N-biose (LNB, Gal- beta1,3-GlcNAc) from the non-reducing end of glycans such as lacto-N- tetraose (LNT). It also catalyzes the release of N- acetyllactosamine (LacNAc, Gal-beta1,4-GlcNAc) from lacto-N-neotetraose (LNnT). Displays activity on the synthetic substrates pNP-LNB (p-nitrophenyl-beta-lacto-N-bioside) and pNP-LacNAc (p- nitrophenyl-beta-N-acetyllactosaminide). Shows weak activity with pNP-6S-GlcNAc and pNP-GalNAc, but cannot use lacto-N- triose II (LNT2, GlcNAc-beta1,3-Gal-beta1,4-Glc) and N,N'- diacetylchitobiose. The low level of activity with LNT and LNnT suggests that they are not the natural substrates for this enzyme.","Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan. Catalyzes the hydrolysis of 1,5-alpha and 1,4-alpha linkages of terminal L-arabinofuranosyl residues in L-arabinofuranosyl-1,5-alpha-L-arabinofuranosyl xylooligosaccharides (AXOS) and L-arabinofuranosyl-1,4-alpha-L-arabinofuranosyl xylooligosaccharides (AFXOS), respectively.",No,No,No,No,No,not-Yes,GO:0004563; GO:0046872,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0004553,0.452,0.452,0.452,0.452,0.5374,5,0.4691,0.4095,no
LNBLN_TREDE,Q73LY9,Protein2Text,Bacteria,354,"Hydrolase that shows both lacto-N-biosidase (LNBase) and N- acetyllactosaminidase (LacNAcase) activity. It catalyzes the release of the disaccharide lacto-N-biose (LNB, Gal- beta1,3-GlcNAc) from the non-reducing end of glycans such as lacto-N- tetraose (LNT). It also catalyzes the release of N- acetyllactosamine (LacNAc, Gal-beta1,4-GlcNAc) from lacto-N-neotetraose (LNnT). Displays activity on the synthetic substrates pNP-LNB (p-nitrophenyl-beta-lacto-N-bioside) and pNP-LacNAc (p- nitrophenyl-beta-N-acetyllactosaminide). Shows weak activity with pNP-6S-GlcNAc and pNP-GalNAc, but cannot use lacto-N- triose II (LNT2, GlcNAc-beta1,3-Gal-beta1,4-Glc) and N,N'- diacetylchitobiose. The low level of activity with LNT and LNnT suggests that they are not the natural substrates for this enzyme.","The molecular function of this protein is an alpha-L-arabinofuranosidase. It is a type of enzyme that catalyzes the hydrolysis of the alpha-L-arabinofuranosidic linkage in the arabinoxylan backbone of wheat arabinoxylan. This is a key step in the degradation of arabinoxylan, a type of hemicellulose found in plant cell walls. The protein breaks down the arabinose units attached to the xylose backbone, allowing for the subsequent release of xylose and arabinose monomers. This is an important step in the utilization of arabinoxylan as a carbon source. 
The protein also has a role in the breakdown of arabinogalactan (AG), another type of hemicellulose found in plant cell walls. It breaks down the alpha-L-arabinofuranosidic linkages in AG, allowing for the release of arabinose and galactose monomers. This is an important step in the utilization of AG as a carbon source.
In addition to its role in the breakdown of arabinoxylan and AG, this protein has been shown to have a role in the breakdown of arabinan, a type of pectin found in plant cell walls. It breaks down the alpha-L-arabinofuranosidic linkages in arabinan, allowing for the release of arabinose monomers. This is an important step in the utilization of arabinan as a carbon source.
Overall, this protein plays a key role in the breakdown of various types of hemicellulose and pectin found in plant cell walls, allowing for the release of monomers that can be utilized as a carbon source.",No,No,No,No,No,not-Yes,GO:0004563; GO:0046872,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,0.452,0.452,0.452,0.452,0.452,5,0.452,0.4095,no
LNBLN_TREDE,Q73LY9,Reference,Bacteria,354,"Hydrolase that shows both lacto-N-biosidase (LNBase) and N- acetyllactosaminidase (LacNAcase) activity. It catalyzes the release of the disaccharide lacto-N-biose (LNB, Gal- beta1,3-GlcNAc) from the non-reducing end of glycans such as lacto-N- tetraose (LNT). It also catalyzes the release of N- acetyllactosamine (LacNAc, Gal-beta1,4-GlcNAc) from lacto-N-neotetraose (LNnT). Displays activity on the synthetic substrates pNP-LNB (p-nitrophenyl-beta-lacto-N-bioside) and pNP-LacNAc (p- nitrophenyl-beta-N-acetyllactosaminide). Shows weak activity with pNP-6S-GlcNAc and pNP-GalNAc, but cannot use lacto-N- triose II (LNT2, GlcNAc-beta1,3-Gal-beta1,4-Glc) and N,N'- diacetylchitobiose. The low level of activity with LNT and LNnT suggests that they are not the natural substrates for this enzyme.","Hydrolase that shows both lacto-N-biosidase (LNBase) and N- acetyllactosaminidase (LacNAcase) activity. It catalyzes the release of the disaccharide lacto-N-biose (LNB, Gal- beta1,3-GlcNAc) from the non-reducing end of glycans such as lacto-N- tetraose (LNT). It also catalyzes the release of N- acetyllactosamine (LacNAc, Gal-beta1,4-GlcNAc) from lacto-N-neotetraose (LNnT). Displays activity on the synthetic substrates pNP-LNB (p-nitrophenyl-beta-lacto-N-bioside) and pNP-LacNAc (p- nitrophenyl-beta-N-acetyllactosaminide). Shows weak activity with pNP-6S-GlcNAc and pNP-GalNAc, but cannot use lacto-N- triose II (LNT2, GlcNAc-beta1,3-Gal-beta1,4-Glc) and N,N'- diacetylchitobiose. The low level of activity with LNT and LNnT suggests that they are not the natural substrates for this enzyme.",,,,,,,GO:0004563; GO:0046872,GO:0016787,GO:0004553,GO:0004553,GO:0016798,GO:0004553,0.4114,0.5374,0.5374,0.4732,0.5374,5,0.4994,0.4095,no
RGYRB_NANEQ,Q74M79,ESM2Text,Archaea,575,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Binds to single-stranded DNA, transiently cleaves and then rejoins the end, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair or for DNA protection (Probable). Reconstituted holoenzyme binds dsDNA a bit better than ssDNA, this subunit preferentially binds dsDNA. In isolation this subunit has DNA-stimulated ATPase activity that is stimulated by topoisomerase-domain containing RgyA. This subunit inhibits the relaxation activity of the topoisomerase subunit while promoting positive supercoiling.",ATP-dependent DNA helicase. Involved in DNA repair and in translesion synthesis.,Maybe,No,No,No,No,not-Yes,GO:0005524; GO:0003677; GO:0046872; GO:0160097,GO:0003678; GO:0005524,GO:0004003,GO:0004386; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,0.6064,0.2838,0.6148,0.6064,0.6064,5,0.5436,0.519,no
RGYRB_NANEQ,Q74M79,Prot2Text,Archaea,575,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Binds to single-stranded DNA, transiently cleaves and then rejoins the end, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair or for DNA protection (Probable). Reconstituted holoenzyme binds dsDNA a bit better than ssDNA, this subunit preferentially binds dsDNA. In isolation this subunit has DNA-stimulated ATPase activity that is stimulated by topoisomerase-domain containing RgyA. This subunit inhibits the relaxation activity of the topoisomerase subunit while promoting positive supercoiling.","A type II topoisomerase. Despite its similarity to DNA gyrase, this DNA polymerase does not require topoisomerase activity to be active.",Maybe,No,No,No,Maybe,not-Yes,GO:0005524; GO:0003677; GO:0046872; GO:0160097,,,,,,,,,,,0,,0.519,no
RGYRB_NANEQ,Q74M79,ProtT3,Archaea,575,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Binds to single-stranded DNA, transiently cleaves and then rejoins the end, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair or for DNA protection (Probable). Reconstituted holoenzyme binds dsDNA a bit better than ssDNA, this subunit preferentially binds dsDNA. In isolation this subunit has DNA-stimulated ATPase activity that is stimulated by topoisomerase-domain containing RgyA. This subunit inhibits the relaxation activity of the topoisomerase subunit while promoting positive supercoiling.",A DNA-dependent ATPase and a 3'-5' DNA helicase. Belongs to the helicase family. Hel308 subfamily,Maybe,No,No,No,No,not-Yes,GO:0005524; GO:0003677; GO:0046872; GO:0160097,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,0.6064,0.6064,0.6064,0.6064,0.6064,5,0.6064,0.519,no
RGYRB_NANEQ,Q74M79,ProtTale,Archaea,575,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Binds to single-stranded DNA, transiently cleaves and then rejoins the end, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair or for DNA protection (Probable). Reconstituted holoenzyme binds dsDNA a bit better than ssDNA, this subunit preferentially binds dsDNA. In isolation this subunit has DNA-stimulated ATPase activity that is stimulated by topoisomerase-domain containing RgyA. This subunit inhibits the relaxation activity of the topoisomerase subunit while promoting positive supercoiling.","ATP-dependent 3'-5' DNA helicase, unwinds dsDNA in the 3'- to 5'-direction until it encounters a 3'- to 5'-DNA helicase; when it encounters a 3'-to-5'-DNA helicase, releases the unwound strand from the 3'-to-5'-DNA helicase.",No,No,No,No,No,not-Yes,GO:0005524; GO:0003677; GO:0046872; GO:0160097,GO:0003678; GO:0005524,GO:0004386; GO:0005524; GO:0003677,GO:0004386; GO:0003677; GO:0005524,GO:0004386; GO:0005524; GO:0003677,GO:0003678; GO:0016887,0.6064,0.7891,0.7891,0.7891,0.2676,5,0.6483,0.519,no
RGYRB_NANEQ,Q74M79,Protein2Text,Archaea,575,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Binds to single-stranded DNA, transiently cleaves and then rejoins the end, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair or for DNA protection (Probable). Reconstituted holoenzyme binds dsDNA a bit better than ssDNA, this subunit preferentially binds dsDNA. In isolation this subunit has DNA-stimulated ATPase activity that is stimulated by topoisomerase-domain containing RgyA. This subunit inhibits the relaxation activity of the topoisomerase subunit while promoting positive supercoiling.","This protein is a DNA polymerase, which means it is involved in the synthesis of new DNA molecules. Specifically, it is a proofreading polymerase, which means it can also correct errors as it synthesizes DNA.",No,No,No,No,No,not-Yes,GO:0005524; GO:0003677; GO:0046872; GO:0160097,GO:0003887,GO:0003887,GO:0003887,GO:0003887,GO:0003887,0.189,0.189,0.189,0.189,0.189,5,0.189,0.519,no
RGYRB_NANEQ,Q74M79,Reference,Archaea,575,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Binds to single-stranded DNA, transiently cleaves and then rejoins the end, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair or for DNA protection (Probable). Reconstituted holoenzyme binds dsDNA a bit better than ssDNA, this subunit preferentially binds dsDNA. In isolation this subunit has DNA-stimulated ATPase activity that is stimulated by topoisomerase-domain containing RgyA. This subunit inhibits the relaxation activity of the topoisomerase subunit while promoting positive supercoiling.","Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Binds to single-stranded DNA, transiently cleaves and then rejoins the end, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair or for DNA protection (Probable). Reconstituted holoenzyme binds dsDNA a bit better than ssDNA, this subunit preferentially binds dsDNA. In isolation this subunit has DNA-stimulated ATPase activity that is stimulated by topoisomerase-domain containing RgyA. This subunit inhibits the relaxation activity of the topoisomerase subunit while promoting positive supercoiling.",,,,,,,GO:0005524; GO:0003677; GO:0046872; GO:0160097,GO:0003916; GO:0003917; GO:0005524; GO:0003677,GO:0003916; GO:0005524; GO:0003677; GO:0016887,GO:0003916; GO:0016887; GO:0003677,GO:0003916; GO:0005524; GO:0003677; GO:0016887,GO:0003916; GO:0016887; GO:0003677,0.8636,0.7804,0.6292,0.7804,0.6292,5,0.7366,0.519,no
RGYRA_NANEQ,Q74MA4,ESM2Text,Archaea,701,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Binds to single-stranded DNA, transiently cleaves and then rejoins the end, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair or for DNA protection (Probable). Reconstituted holoenzyme binds dsDNA a bit better than ssDNA, this subunit preferentially binds ssDNA. In isolation this subunit relaxes negatively-supercoiled DNA, and stimulates the endogenous ATPase activity of the RgyB subunit.","Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.",Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0003677; GO:0160097; GO:0008270,GO:0003917,GO:0003917,GO:0003917,GO:0003917,GO:0003917,0.4446,0.4446,0.4446,0.4446,0.4446,5,0.4446,0.7097,yes
RGYRA_NANEQ,Q74MA4,Prot2Text,Archaea,701,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Binds to single-stranded DNA, transiently cleaves and then rejoins the end, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair or for DNA protection (Probable). Reconstituted holoenzyme binds dsDNA a bit better than ssDNA, this subunit preferentially binds ssDNA. In isolation this subunit relaxes negatively-supercoiled DNA, and stimulates the endogenous ATPase activity of the RgyB subunit.","Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template.",No,No,No,No,No,not-Yes,GO:0003677; GO:0160097; GO:0008270,GO:0004386,GO:0008186,GO:0008186,GO:0008186,GO:0008186,0.3628,0.1705,0.1705,0.1705,0.1705,5,0.209,0.7097,yes
RGYRA_NANEQ,Q74MA4,ProtT3,Archaea,701,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Binds to single-stranded DNA, transiently cleaves and then rejoins the end, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair or for DNA protection (Probable). Reconstituted holoenzyme binds dsDNA a bit better than ssDNA, this subunit preferentially binds ssDNA. In isolation this subunit relaxes negatively-supercoiled DNA, and stimulates the endogenous ATPase activity of the RgyB subunit.","Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally",Maybe,Maybe,Yes,Yes,Yes,Yes,GO:0003677; GO:0160097; GO:0008270,GO:0003917,GO:0003917,GO:0003917,GO:0003917,GO:0003917,0.4446,0.4446,0.4446,0.4446,0.4446,5,0.4446,0.7097,yes
RGYRA_NANEQ,Q74MA4,ProtTale,Archaea,701,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Binds to single-stranded DNA, transiently cleaves and then rejoins the end, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair or for DNA protection (Probable). Reconstituted holoenzyme binds dsDNA a bit better than ssDNA, this subunit preferentially binds ssDNA. In isolation this subunit relaxes negatively-supercoiled DNA, and stimulates the endogenous ATPase activity of the RgyB subunit.","Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally,",Maybe,Maybe,Yes,Yes,Yes,Yes,GO:0003677; GO:0160097; GO:0008270,GO:0003917,GO:0003917; GO:0003677,GO:0003917,GO:0003917,GO:0003917,0.4446,0.7695,0.4446,0.4446,0.4446,5,0.5096,0.7097,yes
RGYRA_NANEQ,Q74MA4,Protein2Text,Archaea,701,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Binds to single-stranded DNA, transiently cleaves and then rejoins the end, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair or for DNA protection (Probable). Reconstituted holoenzyme binds dsDNA a bit better than ssDNA, this subunit preferentially binds ssDNA. In isolation this subunit relaxes negatively-supercoiled DNA, and stimulates the endogenous ATPase activity of the RgyB subunit.","The molecular function of this protein is DNA replication. Specifically, it is a DNA polymerase, which is an enzyme that synthesizes new DNA molecules by adding nucleotides to a template strand.",No,No,No,No,No,not-Yes,GO:0003677; GO:0160097; GO:0008270,GO:0003887,GO:0003887,GO:0003887,GO:0003887,GO:0003887,0.2198,0.2198,0.2198,0.2198,0.2198,5,0.2198,0.7097,yes
RGYRA_NANEQ,Q74MA4,Reference,Archaea,701,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Binds to single-stranded DNA, transiently cleaves and then rejoins the end, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair or for DNA protection (Probable). Reconstituted holoenzyme binds dsDNA a bit better than ssDNA, this subunit preferentially binds ssDNA. In isolation this subunit relaxes negatively-supercoiled DNA, and stimulates the endogenous ATPase activity of the RgyB subunit.","Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Binds to single-stranded DNA, transiently cleaves and then rejoins the end, introducing a positive supercoil in the process. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate. Probably involved in rewinding DNA strands in regions of the chromosome that have opened up to allow replication, transcription, DNA repair or for DNA protection (Probable). Reconstituted holoenzyme binds dsDNA a bit better than ssDNA, this subunit preferentially binds ssDNA. In isolation this subunit relaxes negatively-supercoiled DNA, and stimulates the endogenous ATPase activity of the RgyB subunit.",,,,,,,GO:0003677; GO:0160097; GO:0008270,GO:0003916; GO:0003917; GO:0005524; GO:0003677,GO:0003917; GO:0003697,GO:0003916; GO:0003677,GO:0003916; GO:0003677,GO:0003916; GO:0003677,0.7256,0.6975,0.8078,0.8078,0.8078,5,0.7693,0.7097,yes
LTN1_NEUCR,Q7S834,ESM2Text,Eukaryota,1600,"E3 ubiquitin-protein ligase component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. Mediates ubiquitination of proteins derived from mRNAs lacking stop codons (non- stop proteins) and other translation arrest products induced by poly- lysine sequences and tandem rare codons. Ubiquitination leads to CDC48 recruitment for extraction and degradation of the incomplete translation product. May indirectly play a role in chromatin function and transcription.","Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to the a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules.",No,No,No,No,No,not-Yes,GO:0043023; GO:0061630; GO:0008270,,,,,,,,,,,0,,0.9124,yes
LTN1_NEUCR,Q7S834,Prot2Text,Eukaryota,1600,"E3 ubiquitin-protein ligase component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. Mediates ubiquitination of proteins derived from mRNAs lacking stop codons (non- stop proteins) and other translation arrest products induced by poly- lysine sequences and tandem rare codons. Ubiquitination leads to CDC48 recruitment for extraction and degradation of the incomplete translation product. May indirectly play a role in chromatin function and transcription.",Involved in DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination.,No,No,No,No,No,not-Yes,GO:0043023; GO:0061630; GO:0008270,,GO:0004519,GO:0004519,GO:0004519,GO:0004520,,0.1379,0.1379,0.1379,0.1009,4,0.1286,0.9124,yes
LTN1_NEUCR,Q7S834,ProtT3,Eukaryota,1600,"E3 ubiquitin-protein ligase component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. Mediates ubiquitination of proteins derived from mRNAs lacking stop codons (non- stop proteins) and other translation arrest products induced by poly- lysine sequences and tandem rare codons. Ubiquitination leads to CDC48 recruitment for extraction and degradation of the incomplete translation product. May indirectly play a role in chromatin function and transcription.",Regulator of protein phosphatase 2A (PP2A) that acts as a negative regulator of the DNA damage response (DDR). Cytoplasm Nucleus. Belongs to the PPP2R2D family,No,No,No,No,No,not-Yes,GO:0043023; GO:0061630; GO:0008270,,,,,,,,,,,0,,0.9124,yes
LTN1_NEUCR,Q7S834,ProtTale,Eukaryota,1600,"E3 ubiquitin-protein ligase component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. Mediates ubiquitination of proteins derived from mRNAs lacking stop codons (non- stop proteins) and other translation arrest products induced by poly- lysine sequences and tandem rare codons. Ubiquitination leads to CDC48 recruitment for extraction and degradation of the incomplete translation product. May indirectly play a role in chromatin function and transcription.","E3 ubiquitin-protein ligase. Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. Ubiquitination leads to polyubiquitination of RPS19 which recruits RPS19 and RPL26 for extraction from the stalled ribosome and subsequent proteasomal degradation.",Yes,Yes,Maybe,Yes,Yes,Yes,GO:0043023; GO:0061630; GO:0008270,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0004842,0.5309,0.5309,0.5309,0.5309,0.454,5,0.5155,0.9124,yes
LTN1_NEUCR,Q7S834,Protein2Text,Eukaryota,1600,"E3 ubiquitin-protein ligase component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. Mediates ubiquitination of proteins derived from mRNAs lacking stop codons (non- stop proteins) and other translation arrest products induced by poly- lysine sequences and tandem rare codons. Ubiquitination leads to CDC48 recruitment for extraction and degradation of the incomplete translation product. May indirectly play a role in chromatin function and transcription.","This protein is a component of the 40S ribosomal subunit, which is a component of the ribosome. The molecular function of this protein is likely to be involved in the assembly and/or stability of the 40S ribosomal subunit.",No,No,No,No,No,not-Yes,GO:0043023; GO:0061630; GO:0008270,GO:0003735,GO:0003735,GO:0003735,GO:0003735,GO:0003735,0.1407,0.1407,0.1407,0.1407,0.1407,5,0.1407,0.9124,yes
LTN1_NEUCR,Q7S834,Reference,Eukaryota,1600,"E3 ubiquitin-protein ligase component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. Mediates ubiquitination of proteins derived from mRNAs lacking stop codons (non- stop proteins) and other translation arrest products induced by poly- lysine sequences and tandem rare codons. Ubiquitination leads to CDC48 recruitment for extraction and degradation of the incomplete translation product. May indirectly play a role in chromatin function and transcription.","E3 ubiquitin-protein ligase component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. Mediates ubiquitination of proteins derived from mRNAs lacking stop codons (non- stop proteins) and other translation arrest products induced by poly- lysine sequences and tandem rare codons. Ubiquitination leads to CDC48 recruitment for extraction and degradation of the incomplete translation product. May indirectly play a role in chromatin function and transcription.",,,,,,,GO:0043023; GO:0061630; GO:0008270,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.5309,0.5309,0.5309,0.5309,0.5309,5,0.5309,0.9124,yes
IREP_ENTFA,Q82ZE0,ESM2Text,Bacteria,249,"Protein phosphatase that dephosphorylates protein kinase IreK and IreB. IreP and IreK are cotranscribed, which suggests that they form a functional couple. Involved in intrinsic cephalosporin antibiotic resistance, probably acting by countering the action of IreK. In part, probably modulates antibiotic resistance by acting in concert with the two-component regulatory system CroS/CroR, via the dephosphorylation of histidine sensor kinase CroS.",Protein phosphatase that dephosphorylates EF-Tu.,Maybe,Yes,Maybe,Yes,Maybe,not-Yes,GO:0046872; GO:0004722,GO:0004721,GO:0004722,GO:0004721,GO:0004721,GO:0004721,0.6347,0.6942,0.6347,0.6347,0.6347,5,0.6466,0.2585,no
IREP_ENTFA,Q82ZE0,Prot2Text,Bacteria,249,"Protein phosphatase that dephosphorylates protein kinase IreK and IreB. IreP and IreK are cotranscribed, which suggests that they form a functional couple. Involved in intrinsic cephalosporin antibiotic resistance, probably acting by countering the action of IreK. In part, probably modulates antibiotic resistance by acting in concert with the two-component regulatory system CroS/CroR, via the dephosphorylation of histidine sensor kinase CroS.",Protein phosphatase that dephosphorylates EF-Tu.,Maybe,Yes,Maybe,Yes,Maybe,not-Yes,GO:0046872; GO:0004722,GO:0004721,GO:0004722,GO:0004722,GO:0004722,GO:0004722,0.6347,0.6942,0.6942,0.6942,0.6942,5,0.6823,0.2585,no
IREP_ENTFA,Q82ZE0,ProtT3,Bacteria,249,"Protein phosphatase that dephosphorylates protein kinase IreK and IreB. IreP and IreK are cotranscribed, which suggests that they form a functional couple. Involved in intrinsic cephalosporin antibiotic resistance, probably acting by countering the action of IreK. In part, probably modulates antibiotic resistance by acting in concert with the two-component regulatory system CroS/CroR, via the dephosphorylation of histidine sensor kinase CroS.",Protein phosphatase that can dephosphorylate both Ser/Thr- and Tyr-phosphorylated proteins. Cell membrane; Lipid-anchor; Cytoplasmic side. Belongs to the PP2C family,Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0046872; GO:0004722,GO:0004721,GO:0004721; GO:0004725,GO:0004721,GO:0004721,GO:0004722,0.6347,0.6784,0.6347,0.6347,0.6942,5,0.6553,0.2585,no
IREP_ENTFA,Q82ZE0,ProtTale,Bacteria,249,"Protein phosphatase that dephosphorylates protein kinase IreK and IreB. IreP and IreK are cotranscribed, which suggests that they form a functional couple. Involved in intrinsic cephalosporin antibiotic resistance, probably acting by countering the action of IreK. In part, probably modulates antibiotic resistance by acting in concert with the two-component regulatory system CroS/CroR, via the dephosphorylation of histidine sensor kinase CroS.",Probably plays a role in the regulation of food intake.,Vague,No,No,No,No,not-Yes,GO:0046872; GO:0004722,,,,,,,,,,,0,,0.2585,no
IREP_ENTFA,Q82ZE0,Protein2Text,Bacteria,249,"Protein phosphatase that dephosphorylates protein kinase IreK and IreB. IreP and IreK are cotranscribed, which suggests that they form a functional couple. Involved in intrinsic cephalosporin antibiotic resistance, probably acting by countering the action of IreK. In part, probably modulates antibiotic resistance by acting in concert with the two-component regulatory system CroS/CroR, via the dephosphorylation of histidine sensor kinase CroS.",The molecular function of this protein is a protein phosphatase activity.,Vague,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0046872; GO:0004722,GO:0004721,GO:0004721,GO:0004721,GO:0004721,GO:0004721,0.6347,0.6347,0.6347,0.6347,0.6347,5,0.6347,0.2585,no
IREP_ENTFA,Q82ZE0,Reference,Bacteria,249,"Protein phosphatase that dephosphorylates protein kinase IreK and IreB. IreP and IreK are cotranscribed, which suggests that they form a functional couple. Involved in intrinsic cephalosporin antibiotic resistance, probably acting by countering the action of IreK. In part, probably modulates antibiotic resistance by acting in concert with the two-component regulatory system CroS/CroR, via the dephosphorylation of histidine sensor kinase CroS.","Protein phosphatase that dephosphorylates protein kinase IreK and IreB. IreP and IreK are cotranscribed, which suggests that they form a functional couple. Involved in intrinsic cephalosporin antibiotic resistance, probably acting by countering the action of IreK. In part, probably modulates antibiotic resistance by acting in concert with the two-component regulatory system CroS/CroR, via the dephosphorylation of histidine sensor kinase CroS.",,,,,,,GO:0046872; GO:0004722,GO:0004721,GO:0004721,GO:0004721,GO:0004721,GO:0004721,0.6347,0.6347,0.6347,0.6347,0.6347,5,0.6347,0.2585,no
HYLA_ENTFA,Q82ZM8,ESM2Text,Bacteria,1372,Has a very modest degradation activity against heparin sodium salt (HS) in vitro. Involved in the pathogenesis of vancomycin- resistant E.faecalis infections.,"Cell-counting factor that limits the maximum size of the multicellular structure during aggregation. Is active against the non-mating type 2,6-dystroglycan, since it is able to bind the murein sacculus-like domain of the sacculus cooperating with its depsipeptide. Is not active against the fructofuranosyl oligosaccharides nor the polymeric murein sacculus-like domain of the human chorionic antigen C3B5. Has no activity against the five major polysaccharide donor-types (C3, C4, C5 and C6) nor the five major hyaluronic acid-domain oligosaccharide donor-types (C1, C3, C4 and C6).",No,No,No,No,No,not-Yes,GO:0030246; GO:0016837,,,,,,,,,,,0,,0.2391,no
HYLA_ENTFA,Q82ZM8,Prot2Text,Bacteria,1372,Has a very modest degradation activity against heparin sodium salt (HS) in vitro. Involved in the pathogenesis of vancomycin- resistant E.faecalis infections.,"Broad-specificity glycosaminoglycan lyase, which acts in an exolytic fashion degrading chondroitin sulfates and dermatan sulfate to yield only disaccharide products. Has a preference for chondroitin 4-sulfate over chondroitin 6-sulfate. Has extremely low activity against hyaluronic acid. Is not active against acharan sulfate, heparin or heparan sulfate.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0030246; GO:0016837,,GO:0016835,GO:0016829,GO:0016829,GO:0047500,,0.6323,0.5473,0.5473,0.2095,4,0.4841,0.2391,no
HYLA_ENTFA,Q82ZM8,ProtT3,Bacteria,1372,Has a very modest degradation activity against heparin sodium salt (HS) in vitro. Involved in the pathogenesis of vancomycin- resistant E.faecalis infections.,Secreted. Belongs to the polysaccharide lyase 9 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0030246; GO:0016837,GO:0030570,GO:0030570,GO:0030570,GO:0030570,GO:0030570,0.6247,0.6247,0.6247,0.6247,0.6247,5,0.6247,0.2391,no
HYLA_ENTFA,Q82ZM8,ProtTale,Bacteria,1372,Has a very modest degradation activity against heparin sodium salt (HS) in vitro. Involved in the pathogenesis of vancomycin- resistant E.faecalis infections.,"Polysaccharide lyase that catalyzes the endolytic cleavage of beta-1,4-glucosidic linkages in laminarin and other beta-1,3-D-glucan substrates. Can also hydrolyze the beta-1,3-D-glucosidic linkages in carboxymethylcellulose (CMC) and in the synthetic substrate 4-methylumbelliferyl-beta-D-glucopyranoside (MUG).",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0030246; GO:0016837,GO:0016837,GO:0016798,GO:0016798; GO:0016837,GO:0016829,GO:0016829,0.727,0.2902,0.6355,0.5473,0.5473,5,0.5495,0.2391,no
HYLA_ENTFA,Q82ZM8,Protein2Text,Bacteria,1372,Has a very modest degradation activity against heparin sodium salt (HS) in vitro. Involved in the pathogenesis of vancomycin- resistant E.faecalis infections.,"This protein is a beta-glucosidase, which means it catalyzes the hydrolysis of beta-glucosidic bonds in a wide variety of glucosides. In particular, it hydrolyzes p-nitrophenyl-beta-D-glucoside and cellobiose, and it is involved in the degradation of cell wall polysaccharides.",No,No,No,No,No,not-Yes,GO:0030246; GO:0016837,GO:0008422,GO:0008422,GO:0008422,GO:0008422,GO:0008422,0.1848,0.1848,0.1848,0.1848,0.1848,5,0.1848,0.2391,no
HYLA_ENTFA,Q82ZM8,Reference,Bacteria,1372,Has a very modest degradation activity against heparin sodium salt (HS) in vitro. Involved in the pathogenesis of vancomycin- resistant E.faecalis infections.,Has a very modest degradation activity against heparin sodium salt (HS) in vitro. Involved in the pathogenesis of vancomycin- resistant E.faecalis infections.,,,,,,,GO:0030246; GO:0016837,GO:0016787,,,,,0.3588,,,,,1,0.3588,0.2391,no
HOPAM_PSESM,Q877R9,ESM2Text,Bacteria,276,"NAD(+) hydrolase (NADase) that cleaves NAD(+) into nicotinamide and 3' cyclic ADP-D-ribose (3'cADPR, v2-cADPR). Upon infiltration of A.thaliana with this bacteria an effector-triggered immunity-like phenotype (ETI- like, cell death with severe chlorosis) is seen, 3'cADPR levels rise while NAD(+) levels remain constant. Plant immune responses are suppressed. Triggers hypersensitive response-like cell death in Nicotiana tabacum cv. Xanthi and N.benthamiana when transiently expressed, depletes NAD(+) in N.benthamiana. Causes cell death upon induction in yeast due to NAD(+) depletion and/or 3'cADPR itself. Transgenic A.thaliana expressing HopAM1 suppresses its plant immune system upon challenge; the plants produce 3'cADPR without significantly depleting NAD(+).","Immunity protein component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion. Neutralizes the toxic activity of cognate toxin CdiA-NC101 (the C-terminal 289 residue CT fragment) upon expression in E.coli. Does not inhibit toxic activity of CdiA from other strains of B.pseudomallei.",No,No,No,No,No,not-Yes,GO:0016787,,,,,,,,,,,0,,0.3158,no
HOPAM_PSESM,Q877R9,Prot2Text,Bacteria,276,"NAD(+) hydrolase (NADase) that cleaves NAD(+) into nicotinamide and 3' cyclic ADP-D-ribose (3'cADPR, v2-cADPR). Upon infiltration of A.thaliana with this bacteria an effector-triggered immunity-like phenotype (ETI- like, cell death with severe chlorosis) is seen, 3'cADPR levels rise while NAD(+) levels remain constant. Plant immune responses are suppressed. Triggers hypersensitive response-like cell death in Nicotiana tabacum cv. Xanthi and N.benthamiana when transiently expressed, depletes NAD(+) in N.benthamiana. Causes cell death upon induction in yeast due to NAD(+) depletion and/or 3'cADPR itself. Transgenic A.thaliana expressing HopAM1 suppresses its plant immune system upon challenge; the plants produce 3'cADPR without significantly depleting NAD(+).",Appears to play some role in the morphogenesis of the spore wall.,No,No,No,No,No,not-Yes,GO:0016787,,,,,,,,,,,0,,0.3158,no
HOPAM_PSESM,Q877R9,ProtT3,Bacteria,276,"NAD(+) hydrolase (NADase) that cleaves NAD(+) into nicotinamide and 3' cyclic ADP-D-ribose (3'cADPR, v2-cADPR). Upon infiltration of A.thaliana with this bacteria an effector-triggered immunity-like phenotype (ETI- like, cell death with severe chlorosis) is seen, 3'cADPR levels rise while NAD(+) levels remain constant. Plant immune responses are suppressed. Triggers hypersensitive response-like cell death in Nicotiana tabacum cv. Xanthi and N.benthamiana when transiently expressed, depletes NAD(+) in N.benthamiana. Causes cell death upon induction in yeast due to NAD(+) depletion and/or 3'cADPR itself. Transgenic A.thaliana expressing HopAM1 suppresses its plant immune system upon challenge; the plants produce 3'cADPR without significantly depleting NAD(+).","NAD(+) hydrolase (NADase) that catalyzes the cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide mononucleotide (NMN) . In addition to NADase activity, also displays ADP-ribosyl cyclase activity, catalyzing the transfer of an ADP-ribose moiety from NAD(+) to a serine or threonine residue of target proteins . In vitro, catalyzes the transfer of an ADP-ribose moiety from NAD(+) to",Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0016787,GO:0003953,GO:0003953; GO:0003952,GO:0003953,GO:0003953,GO:0003953; GO:0061809,0.6019,0.5197,0.6019,0.6019,0.6019,5,0.5855,0.3158,no
HOPAM_PSESM,Q877R9,ProtTale,Bacteria,276,"NAD(+) hydrolase (NADase) that cleaves NAD(+) into nicotinamide and 3' cyclic ADP-D-ribose (3'cADPR, v2-cADPR). Upon infiltration of A.thaliana with this bacteria an effector-triggered immunity-like phenotype (ETI- like, cell death with severe chlorosis) is seen, 3'cADPR levels rise while NAD(+) levels remain constant. Plant immune responses are suppressed. Triggers hypersensitive response-like cell death in Nicotiana tabacum cv. Xanthi and N.benthamiana when transiently expressed, depletes NAD(+) in N.benthamiana. Causes cell death upon induction in yeast due to NAD(+) depletion and/or 3'cADPR itself. Transgenic A.thaliana expressing HopAM1 suppresses its plant immune system upon challenge; the plants produce 3'cADPR without significantly depleting NAD(+).",Probable kinase that may be involved in the regulation of cell morphology and morphogenesis via phosphorylation of a protein or proteins.,No,No,No,No,No,not-Yes,GO:0016787,GO:0016301,GO:0016301,,GO:0016301,GO:0004672,0.4071,0.4071,,0.4071,0.3183,4,0.3849,0.3158,no
HOPAM_PSESM,Q877R9,Protein2Text,Bacteria,276,"NAD(+) hydrolase (NADase) that cleaves NAD(+) into nicotinamide and 3' cyclic ADP-D-ribose (3'cADPR, v2-cADPR). Upon infiltration of A.thaliana with this bacteria an effector-triggered immunity-like phenotype (ETI- like, cell death with severe chlorosis) is seen, 3'cADPR levels rise while NAD(+) levels remain constant. Plant immune responses are suppressed. Triggers hypersensitive response-like cell death in Nicotiana tabacum cv. Xanthi and N.benthamiana when transiently expressed, depletes NAD(+) in N.benthamiana. Causes cell death upon induction in yeast due to NAD(+) depletion and/or 3'cADPR itself. Transgenic A.thaliana expressing HopAM1 suppresses its plant immune system upon challenge; the plants produce 3'cADPR without significantly depleting NAD(+).","This protein is involved in the process of binding and transporting molecules across cell membranes. It is part of a larger family of proteins known as solute carrier proteins (SLCs), which play a crucial role in the transport of various molecules across cell membranes. This specific protein is involved in the transport of glucose, a vital process for cellular energy production and metabolism.",No,No,No,No,No,not-Yes,GO:0016787,GO:0005355,GO:0005215,GO:0005355,GO:0005355,GO:0005355,0.0,0.3396,0.0,0.0,0.0,5,0.0679,0.3158,no
HOPAM_PSESM,Q877R9,Reference,Bacteria,276,"NAD(+) hydrolase (NADase) that cleaves NAD(+) into nicotinamide and 3' cyclic ADP-D-ribose (3'cADPR, v2-cADPR). Upon infiltration of A.thaliana with this bacteria an effector-triggered immunity-like phenotype (ETI- like, cell death with severe chlorosis) is seen, 3'cADPR levels rise while NAD(+) levels remain constant. Plant immune responses are suppressed. Triggers hypersensitive response-like cell death in Nicotiana tabacum cv. Xanthi and N.benthamiana when transiently expressed, depletes NAD(+) in N.benthamiana. Causes cell death upon induction in yeast due to NAD(+) depletion and/or 3'cADPR itself. Transgenic A.thaliana expressing HopAM1 suppresses its plant immune system upon challenge; the plants produce 3'cADPR without significantly depleting NAD(+).","NAD(+) hydrolase (NADase) that cleaves NAD(+) into nicotinamide and 3' cyclic ADP-D-ribose (3'cADPR, v2-cADPR). Upon infiltration of A.thaliana with this bacteria an effector-triggered immunity-like phenotype (ETI- like, cell death with severe chlorosis) is seen, 3'cADPR levels rise while NAD(+) levels remain constant. Plant immune responses are suppressed. Triggers hypersensitive response-like cell death in Nicotiana tabacum cv. Xanthi and N.benthamiana when transiently expressed, depletes NAD(+) in N.benthamiana. Causes cell death upon induction in yeast due to NAD(+) depletion and/or 3'cADPR itself. Transgenic A.thaliana expressing HopAM1 suppresses its plant immune system upon challenge; the plants produce 3'cADPR without significantly depleting NAD(+).",,,,,,,GO:0016787,GO:0016787; GO:0003953,GO:0003953,GO:0003953,GO:0003953,GO:0003953,0.8673,0.6019,0.6019,0.6019,0.6019,5,0.655,0.3158,no
LHRC_PSEPK,Q88NV1,ESM2Text,Bacteria,816,"A single strand (ss)DNA-dependent (d)ATPase probably involved in DNA repair, translocates 3'-to-5' on ssDNA, unwinding any encountered duplex nucleic acid. Unwinds 3'-tailed duplexes; both RNA:DNA hybrids and double-stranded (ds)DNA with a 3'-ssDNA loading strand are unwound, substrates where the helicase loads on a 3'-ssRNA tail (DNA:RNA and RNA:RNA) are not unwound.","CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3 and Cascade participate in CRISPR interference, the third stage of CRISPR immunity (Potential). Involved in the integration of spacer DNA into the CRISPR cassette. Plasmid targeted by Cascade participate in a non DNA-homologous end joining (NHEJ) pathway that may involve anchoring and nuclease activation of target DNA strands. Plasmid targeted by Cascade participate in a DNA repair pathway that involves removal of excised lagging-strand Okazaki fragments. DNA repair is probably guided by an RFC-like protein, which binds to the broken strand and then unwinds the resulting strand. DNA strand-directed degradation is probably guided by a protein that has 3' to 5' DNA terminus and a 3' terminus. Endonuclease activity is stimulated by a protein that has 3",No,No,Maybe,Maybe,No,not-Yes,GO:0043138; GO:0033679; GO:0005524; GO:0016887; GO:0003677,,GO:0004519,GO:0004519,GO:0004519,,,0.2065,0.2065,0.2065,,3,0.2065,0.4819,no
LHRC_PSEPK,Q88NV1,Prot2Text,Bacteria,816,"A single strand (ss)DNA-dependent (d)ATPase probably involved in DNA repair, translocates 3'-to-5' on ssDNA, unwinding any encountered duplex nucleic acid. Unwinds 3'-tailed duplexes; both RNA:DNA hybrids and double-stranded (ds)DNA with a 3'-ssDNA loading strand are unwound, substrates where the helicase loads on a 3'-ssRNA tail (DNA:RNA and RNA:RNA) are not unwound.","Helicase with DNA-dependent ATPase activity that plays key roles in homologous recombination (HR). Binds single-stranded DNA (ssDNA), forked DNA structures containing the sequence 5'-GGATG-3' and other sequences modified by homologous recombination hotspots. Acts in a fashion dependent on the presence of ATP and its helicase activity. Prefers DNA with 5'-overhangs or branched structures. Has DNA-dependent ATPase activity, which is required for DNA binding. May be involved in recombination at ssDNA ends and also in recovery from replication stress.",Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0043138; GO:0033679; GO:0005524; GO:0016887; GO:0003677,GO:0004386; GO:0003678,GO:0003678,GO:0004003; GO:0003677; GO:0005524,GO:0004003,GO:0004003; GO:0008094,0.5518,0.4982,0.854,0.4982,0.5475,5,0.5899,0.4819,no
LHRC_PSEPK,Q88NV1,ProtT3,Bacteria,816,"A single strand (ss)DNA-dependent (d)ATPase probably involved in DNA repair, translocates 3'-to-5' on ssDNA, unwinding any encountered duplex nucleic acid. Unwinds 3'-tailed duplexes; both RNA:DNA hybrids and double-stranded (ds)DNA with a 3'-ssDNA loading strand are unwound, substrates where the helicase loads on a 3'-ssRNA tail (DNA:RNA and RNA:RNA) are not unwound.",Belongs to the helicase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0043138; GO:0033679; GO:0005524; GO:0016887; GO:0003677,,GO:0004386; GO:0005524,,GO:0004386; GO:0005524,,,0.6717,,0.6717,,2,0.6717,0.4819,no
LHRC_PSEPK,Q88NV1,ProtTale,Bacteria,816,"A single strand (ss)DNA-dependent (d)ATPase probably involved in DNA repair, translocates 3'-to-5' on ssDNA, unwinding any encountered duplex nucleic acid. Unwinds 3'-tailed duplexes; both RNA:DNA hybrids and double-stranded (ds)DNA with a 3'-ssDNA loading strand are unwound, substrates where the helicase loads on a 3'-ssRNA tail (DNA:RNA and RNA:RNA) are not unwound.","CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA).",No,No,No,No,No,not-Yes,GO:0043138; GO:0033679; GO:0005524; GO:0016887; GO:0003677,,,,,,,,,,,0,,0.4819,no
LHRC_PSEPK,Q88NV1,Protein2Text,Bacteria,816,"A single strand (ss)DNA-dependent (d)ATPase probably involved in DNA repair, translocates 3'-to-5' on ssDNA, unwinding any encountered duplex nucleic acid. Unwinds 3'-tailed duplexes; both RNA:DNA hybrids and double-stranded (ds)DNA with a 3'-ssDNA loading strand are unwound, substrates where the helicase loads on a 3'-ssRNA tail (DNA:RNA and RNA:RNA) are not unwound.",The molecular function of this protein is an ATP-dependent DNA helicase. It is involved in unwinding DNA during DNA replication and repair.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0043138; GO:0033679; GO:0005524; GO:0016887; GO:0003677,GO:0004003; GO:0005524,GO:0004003; GO:0005524,GO:0004003; GO:0005524,GO:0004003; GO:0005524,GO:0004003,0.7139,0.7139,0.7139,0.7139,0.4982,5,0.6708,0.4819,no
LHRC_PSEPK,Q88NV1,Reference,Bacteria,816,"A single strand (ss)DNA-dependent (d)ATPase probably involved in DNA repair, translocates 3'-to-5' on ssDNA, unwinding any encountered duplex nucleic acid. Unwinds 3'-tailed duplexes; both RNA:DNA hybrids and double-stranded (ds)DNA with a 3'-ssDNA loading strand are unwound, substrates where the helicase loads on a 3'-ssRNA tail (DNA:RNA and RNA:RNA) are not unwound.","A single strand (ss)DNA-dependent (d)ATPase probably involved in DNA repair, translocates 3'-to-5' on ssDNA, unwinding any encountered duplex nucleic acid. Unwinds 3'-tailed duplexes; both RNA:DNA hybrids and double-stranded (ds)DNA with a 3'-ssDNA loading strand are unwound, substrates where the helicase loads on a 3'-ssRNA tail (DNA:RNA and RNA:RNA) are not unwound.",,,,,,,GO:0043138; GO:0033679; GO:0005524; GO:0016887; GO:0003677,GO:0004386; GO:0005524; GO:0003697,GO:0003678; GO:0016887,GO:0003678; GO:0016887,GO:0004386; GO:0016887; GO:0003677,GO:0003678; GO:0016887,0.7775,0.6813,0.6813,0.7984,0.6813,5,0.724,0.4819,no
PI51N_PLAF7,Q8I239,ESM2Text,Eukaryota,1710,"Catalyzes the phosphorylation of phosphatidylinositol 4- phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes.",Acts as a suppressor of cap-dependent translation.,No,No,No,No,No,not-Yes,GO:0016308; GO:0005524; GO:0005509,,,,,,,,,,,0,,0.4108,no
PI51N_PLAF7,Q8I239,Prot2Text,Eukaryota,1710,"Catalyzes the phosphorylation of phosphatidylinositol 4- phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes.",Acts as a docking site for the predominantly cytoplasmic dynein.,No,No,No,No,No,not-Yes,GO:0016308; GO:0005524; GO:0005509,,,,,,,,,,,0,,0.4108,no
PI51N_PLAF7,Q8I239,ProtT3,Eukaryota,1710,"Catalyzes the phosphorylation of phosphatidylinositol 4- phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes.","As part of the membrane-bound complex of cytochrome b561 and b562 (complex III or cytochrome b-c1 complex), part of the respiratory chain that generates an electrochemical potential coupled to ATP synthesis. Endoplasmic reticulum membrane; Single-pass membrane protein. Belongs to the CFB4 family",No,No,No,No,No,not-Yes,GO:0016308; GO:0005524; GO:0005509,GO:0009055,GO:0009055; GO:0008121,GO:0008121,GO:0008121; GO:0009055,GO:0009055,0.1574,0.1407,0.0689,0.1407,0.1574,5,0.133,0.4108,no
PI51N_PLAF7,Q8I239,ProtTale,Eukaryota,1710,"Catalyzes the phosphorylation of phosphatidylinositol 4- phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes.","May play a role in regulating calcium-dependent processes such as cell proliferation, differentiation and virulence. Involved in the regulation of protein phosphatase 2A (PP2A).",Vague,No,No,Maybe,No,not-Yes,GO:0016308; GO:0005524; GO:0005509,,,,,,,,,,,0,,0.4108,no
PI51N_PLAF7,Q8I239,Protein2Text,Eukaryota,1710,"Catalyzes the phosphorylation of phosphatidylinositol 4- phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes.","The molecular function of this protein is not explicitly stated in the provided text. However, it is mentioned that this protein is a serine/threonine-protein kinase, which suggests that its molecular function is related to catalyzing the transfer of a phosphate group from a phosphate donor, such as ATP, to a serine or threonine residue of a target protein.",No,No,No,No,No,not-Yes,GO:0016308; GO:0005524; GO:0005509,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.3024,0.3024,0.3024,0.3024,0.3024,5,0.3024,0.4108,no
PI51N_PLAF7,Q8I239,Reference,Eukaryota,1710,"Catalyzes the phosphorylation of phosphatidylinositol 4- phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes.","Catalyzes the phosphorylation of phosphatidylinositol 4- phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes.",,,,,,,GO:0016308; GO:0005524; GO:0005509,GO:0016307,GO:0016308,GO:0016308,GO:0016308; GO:0005524,GO:0016308,0.0,0.5259,0.5259,0.8511,0.5259,5,0.4858,0.4108,no
EIK2_PLAF7,Q8I265,ESM2Text,Eukaryota,1595,"Phosphorylates translation factor eIF2alpha in salivary gland sporozoites during dormancy, which leads to an inhibition of protein translation and accumulation of stalled mRNAs into granules.",Involved in protein precursor import into chloroplasts. May be part of an intermediate translocation complex acting as a protein-conducting channel at the inner envelope.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004694; GO:0004672; GO:0106310,,,,,,,,,,,0,,0.6251,yes
EIK2_PLAF7,Q8I265,Prot2Text,Eukaryota,1595,"Phosphorylates translation factor eIF2alpha in salivary gland sporozoites during dormancy, which leads to an inhibition of protein translation and accumulation of stalled mRNAs into granules.",Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004694; GO:0004672; GO:0106310,GO:0003720,GO:0003720,GO:0003720,GO:0003720,GO:0003964,0.2538,0.2538,0.2538,0.2538,0.278,5,0.2586,0.6251,yes
EIK2_PLAF7,Q8I265,ProtT3,Eukaryota,1595,"Phosphorylates translation factor eIF2alpha in salivary gland sporozoites during dormancy, which leads to an inhibition of protein translation and accumulation of stalled mRNAs into granules.",Mitochondrion. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0004694; GO:0004672; GO:0106310,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.9253,0.9253,0.9253,0.9253,0.9253,5,0.9253,0.6251,yes
EIK2_PLAF7,Q8I265,ProtTale,Eukaryota,1595,"Phosphorylates translation factor eIF2alpha in salivary gland sporozoites during dormancy, which leads to an inhibition of protein translation and accumulation of stalled mRNAs into granules.","Catalyzes the phosphorylation of phosphatidylinositol (PI) to PI4,5-bisphosphate (PI4,5P2).",No,No,Maybe,Maybe,No,not-Yes,GO:0005524; GO:0004694; GO:0004672; GO:0106310,GO:0016301,GO:0016301; GO:0046934,GO:0016308,GO:0016301,GO:0016301,0.5503,0.5599,0.4585,0.5503,0.5503,5,0.5339,0.6251,yes
EIK2_PLAF7,Q8I265,Protein2Text,Eukaryota,1595,"Phosphorylates translation factor eIF2alpha in salivary gland sporozoites during dormancy, which leads to an inhibition of protein translation and accumulation of stalled mRNAs into granules.","The molecular function of this protein is not specified in the provided text. However, based on the context, it can be inferred that it is involved in a process related to the DNA or chromatin. The protein is described as a ""histone chaperone"" which suggests that it plays a role in the assembly or remodeling of chromatin, specifically in the formation of nucleosomes, which are the building blocks of chromatin.",Vague,No,No,No,Vague,not-Yes,GO:0005524; GO:0004694; GO:0004672; GO:0106310,,,,,,,,,,,0,,0.6251,yes
EIK2_PLAF7,Q8I265,Reference,Eukaryota,1595,"Phosphorylates translation factor eIF2alpha in salivary gland sporozoites during dormancy, which leads to an inhibition of protein translation and accumulation of stalled mRNAs into granules.","Phosphorylates translation factor eIF2alpha in salivary gland sporozoites during dormancy, which leads to an inhibition of protein translation and accumulation of stalled mRNAs into granules.",,,,,,,GO:0005524; GO:0004694; GO:0004672; GO:0106310,GO:0004694,GO:0004694,GO:0004694,GO:0004674; GO:0005524,GO:0004694,0.7267,0.7267,0.7267,0.9253,0.7267,5,0.7664,0.6251,yes
1CPX_PLAF7,Q8IAM2,ESM2Text,Eukaryota,220,"Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (Probable). Exhibits antioxidant activity. Binds ferriprotoporphyrin IX at pH 7.4. Protects parasites against oxidative stresses by slowing the rate of heme degradation and consequent iron generation, thereby preventing damage of the proteins caused by iron-derived reactive oxygen species, and by interfering with formation of membrane- associated ferriprotoporphyrin IX.","Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016209; GO:0004601; GO:0051920,GO:0004601,GO:0008379,GO:0004601,GO:0004601,GO:0004601,0.8527,0.6828,0.8527,0.8527,0.8527,5,0.8187,0.4595,no
1CPX_PLAF7,Q8IAM2,Prot2Text,Eukaryota,220,"Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (Probable). Exhibits antioxidant activity. Binds ferriprotoporphyrin IX at pH 7.4. Protects parasites against oxidative stresses by slowing the rate of heme degradation and consequent iron generation, thereby preventing damage of the proteins caused by iron-derived reactive oxygen species, and by interfering with formation of membrane- associated ferriprotoporphyrin IX.","Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016209; GO:0004601; GO:0051920,GO:0008379,GO:0051920,GO:0004601,GO:0004601,GO:0051920,0.6828,0.8388,0.8527,0.8527,0.8388,5,0.8132,0.4595,no
1CPX_PLAF7,Q8IAM2,ProtT3,Eukaryota,220,"Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (Probable). Exhibits antioxidant activity. Binds ferriprotoporphyrin IX at pH 7.4. Protects parasites against oxidative stresses by slowing the rate of heme degradation and consequent iron generation, thereby preventing damage of the proteins caused by iron-derived reactive oxygen species, and by interfering with formation of membrane- associated ferriprotoporphyrin IX.","Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Cytoplasm Nucleus. Belongs to the peroxiredoxin family. Prx6 subfamily",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016209; GO:0004601; GO:0051920,GO:0051920,GO:0051920,GO:0051920,GO:0051920,GO:0051920,0.8388,0.8388,0.8388,0.8388,0.8388,5,0.8388,0.4595,no
1CPX_PLAF7,Q8IAM2,ProtTale,Eukaryota,220,"Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (Probable). Exhibits antioxidant activity. Binds ferriprotoporphyrin IX at pH 7.4. Protects parasites against oxidative stresses by slowing the rate of heme degradation and consequent iron generation, thereby preventing damage of the proteins caused by iron-derived reactive oxygen species, and by interfering with formation of membrane- associated ferriprotoporphyrin IX.","Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016209; GO:0004601; GO:0051920,GO:0004601,GO:0004601,GO:0004601,GO:0004601,GO:0004601,0.8527,0.8527,0.8527,0.8527,0.8527,5,0.8527,0.4595,no
1CPX_PLAF7,Q8IAM2,Protein2Text,Eukaryota,220,"Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (Probable). Exhibits antioxidant activity. Binds ferriprotoporphyrin IX at pH 7.4. Protects parasites against oxidative stresses by slowing the rate of heme degradation and consequent iron generation, thereby preventing damage of the proteins caused by iron-derived reactive oxygen species, and by interfering with formation of membrane- associated ferriprotoporphyrin IX.",The molecular function of this protein is thiol-disulfide oxidoreductase activity.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016209; GO:0004601; GO:0051920,GO:0015036,GO:0015035,GO:0015035,GO:0015036,GO:0015035,0.3699,0.317,0.317,0.3699,0.317,5,0.3382,0.4595,no
1CPX_PLAF7,Q8IAM2,Reference,Eukaryota,220,"Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (Probable). Exhibits antioxidant activity. Binds ferriprotoporphyrin IX at pH 7.4. Protects parasites against oxidative stresses by slowing the rate of heme degradation and consequent iron generation, thereby preventing damage of the proteins caused by iron-derived reactive oxygen species, and by interfering with formation of membrane- associated ferriprotoporphyrin IX.","Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (Probable). Exhibits antioxidant activity. Binds ferriprotoporphyrin IX at pH 7.4. Protects parasites against oxidative stresses by slowing the rate of heme degradation and consequent iron generation, thereby preventing damage of the proteins caused by iron-derived reactive oxygen species, and by interfering with formation of membrane- associated ferriprotoporphyrin IX.",,,,,,,GO:0016209; GO:0004601; GO:0051920,GO:0004601,GO:0004601,GO:0004601,GO:0004601; GO:0008379,GO:0004601,0.8527,0.8527,0.8527,0.8431,0.8527,5,0.8508,0.4595,no
DDX31_PLAF7,Q8IBN8,ESM2Text,Eukaryota,899,Has DNA helicase activity and may also have RNA helicase activity; the DNA helicase direction was not determined. Shows ssDNA and RNA dependent ATPase activity.,Probable ATP-dependent RNA helicase.,Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0005524; GO:0016887; GO:0003723; GO:0003724,GO:0003724; GO:0005524,GO:0004004,GO:0004386; GO:0005524,GO:0003724; GO:0005524,GO:0004004; GO:0005524,0.735,0.4799,0.6806,0.735,0.735,5,0.6731,0.7198,yes
DDX31_PLAF7,Q8IBN8,Prot2Text,Eukaryota,899,Has DNA helicase activity and may also have RNA helicase activity; the DNA helicase direction was not determined. Shows ssDNA and RNA dependent ATPase activity.,Probable ATP-dependent RNA helicase.,Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0005524; GO:0016887; GO:0003723; GO:0003724,GO:0004004,GO:0004004,GO:0004004,GO:0004004,GO:0004004,0.4799,0.4799,0.4799,0.4799,0.4799,5,0.4799,0.7198,yes
DDX31_PLAF7,Q8IBN8,ProtT3,Eukaryota,899,Has DNA helicase activity and may also have RNA helicase activity; the DNA helicase direction was not determined. Shows ssDNA and RNA dependent ATPase activity.,"ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs. Nucleus, nucleolus. Belongs to the DEAD box helicase family. DDX54/DBP10 subfamily",Maybe,No,Maybe,Maybe,Yes,not-Yes,GO:0005524; GO:0016887; GO:0003723; GO:0003724,GO:0003724; GO:0005524,GO:0003724; GO:0005524,GO:0003724; GO:0005524,GO:0003724; GO:0005524,GO:0003724; GO:0005524,0.735,0.735,0.735,0.735,0.735,5,0.735,0.7198,yes
DDX31_PLAF7,Q8IBN8,ProtTale,Eukaryota,899,Has DNA helicase activity and may also have RNA helicase activity; the DNA helicase direction was not determined. Shows ssDNA and RNA dependent ATPase activity.,"ATP-dependent RNA helicase involved in 40S ribosomal subunit biogenesis. Required for the processing and cleavage of 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA.",Maybe,No,Maybe,Maybe,Yes,not-Yes,GO:0005524; GO:0016887; GO:0003723; GO:0003724,GO:0004004; GO:0005524,GO:0004386; GO:0005524; GO:0003723,GO:0004386; GO:0003723; GO:0005524,GO:0004386; GO:0005524; GO:0003723,GO:0003724; GO:0016887,0.735,0.8454,0.8454,0.8454,0.6975,5,0.7937,0.7198,yes
DDX31_PLAF7,Q8IBN8,Protein2Text,Eukaryota,899,Has DNA helicase activity and may also have RNA helicase activity; the DNA helicase direction was not determined. Shows ssDNA and RNA dependent ATPase activity.,"This protein is a molecular function associated with the catalytic activity of a helicase, which is involved in unwinding DNA or RNA duplexes.",Maybe,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0005524; GO:0016887; GO:0003723; GO:0003724,GO:0004386,GO:0004386,GO:0004386,GO:0004386,GO:0004386,0.4234,0.4234,0.4234,0.4234,0.4234,5,0.4234,0.7198,yes
DDX31_PLAF7,Q8IBN8,Reference,Eukaryota,899,Has DNA helicase activity and may also have RNA helicase activity; the DNA helicase direction was not determined. Shows ssDNA and RNA dependent ATPase activity.,Has DNA helicase activity and may also have RNA helicase activity; the DNA helicase direction was not determined. Shows ssDNA and RNA dependent ATPase activity.,,,,,,,GO:0005524; GO:0016887; GO:0003723; GO:0003724,GO:0004386; GO:0016887,GO:0003678; GO:0016887,GO:0003678; GO:0016887,GO:0004386; GO:0016887; GO:0003677,GO:0003678; GO:0016887,0.6337,0.5806,0.5806,0.7273,0.5806,5,0.6206,0.7198,yes
MNMA_PLAF7,Q8IJK4,ESM2Text,Eukaryota,1084,"Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. Required for apicoplast maintenance.",Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. This is the first step in the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.,No,No,No,No,No,not-Yes,GO:0005524; GO:0000049; GO:0103016,GO:0008175,GO:0008176,GO:0008176,GO:0008176,GO:0008176,0.3008,0.2403,0.2403,0.2403,0.2403,5,0.2524,0.6001,yes
MNMA_PLAF7,Q8IJK4,Prot2Text,Eukaryota,1084,"Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. Required for apicoplast maintenance.",Essential for lysine biosynthesis. Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).,No,No,No,No,No,not-Yes,GO:0005524; GO:0000049; GO:0103016,GO:0004818,GO:0004818,GO:0004818,GO:0004818,GO:0004818,0.2628,0.2628,0.2628,0.2628,0.2628,5,0.2628,0.6001,yes
MNMA_PLAF7,Q8IJK4,ProtT3,Eukaryota,1084,"Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. Required for apicoplast maintenance.","Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly",No,No,No,No,No,not-Yes,GO:0005524; GO:0000049; GO:0103016,GO:0009022,GO:0009022,GO:0009022,GO:0009022,GO:0009022,0.3163,0.3163,0.3163,0.3163,0.3163,5,0.3163,0.6001,yes
MNMA_PLAF7,Q8IJK4,ProtTale,Eukaryota,1084,"Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. Required for apicoplast maintenance.","Involved in tRNA modification. Catalyzes the N(7)-methylguanine (m7G) methylation of the wobble position (U34) of certain tRNAs, forming tRNA-m7G(34). Also catalyzes the formation of s(2)U34 methylation in tmRNA (transfer-mRNA).",No,No,No,No,No,not-Yes,GO:0005524; GO:0000049; GO:0103016,GO:0008176,GO:0008168,GO:0008176,GO:0008176,GO:0008168,0.2403,0.2024,0.2403,0.2403,0.2024,5,0.2251,0.6001,yes
MNMA_PLAF7,Q8IJK4,Protein2Text,Eukaryota,1084,"Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. Required for apicoplast maintenance.","The molecular function of this protein is not explicitly stated in the problem description. However, based on the name ""protein"" and its involvement in a process related to ""mRNA"" and ""DNA"", it can be inferred that this protein is likely involved in a molecular process related to gene expression or transcription.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0000049; GO:0103016,,,,,,,,,,,0,,0.6001,yes
MNMA_PLAF7,Q8IJK4,Reference,Eukaryota,1084,"Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. Required for apicoplast maintenance.","Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. Required for apicoplast maintenance.",,,,,,,GO:0005524; GO:0000049; GO:0103016,GO:0016783,GO:0016783,GO:0016783,GO:0016740,GO:0016783,0.3823,0.3823,0.3823,0.2953,0.3823,5,0.3649,0.6001,yes
PR5X_SOLLC,Q8LPU1,ESM2Text,Eukaryota,230,"Antifungal protein. May bind to beta-glucans and have beta-1,3-D-glucanase activity.",May be involved in disease resistance.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0052736; GO:0052861,,,,,,,,,,,0,,0.2944,no
PR5X_SOLLC,Q8LPU1,Prot2Text,Eukaryota,230,"Antifungal protein. May bind to beta-glucans and have beta-1,3-D-glucanase activity.","Has antifungal activity against P.betae and F.dahliae. Inhibits growth of F.solani and, to a lesser extent, of V.albo-oligosaccharides.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0052736; GO:0052861,,,,,,,,,,,0,,0.2944,no
PR5X_SOLLC,Q8LPU1,ProtT3,Eukaryota,230,"Antifungal protein. May bind to beta-glucans and have beta-1,3-D-glucanase activity.",Belongs to the thaumatin family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0052736; GO:0052861,,,,,,,,,,,0,,0.2944,no
PR5X_SOLLC,Q8LPU1,ProtTale,Eukaryota,230,"Antifungal protein. May bind to beta-glucans and have beta-1,3-D-glucanase activity.",May be involved in protecting the plant body against pathogen attack.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0052736; GO:0052861,,,,,,,,,,,0,,0.2944,no
PR5X_SOLLC,Q8LPU1,Protein2Text,Eukaryota,230,"Antifungal protein. May bind to beta-glucans and have beta-1,3-D-glucanase activity.",The molecular function of this protein is chitinase activity.,No,No,No,No,No,not-Yes,GO:0052736; GO:0052861,GO:0004568,GO:0004568,GO:0004568,GO:0004568,GO:0004568,0.6971,0.6971,0.6971,0.6971,0.6971,5,0.6971,0.2944,no
PR5X_SOLLC,Q8LPU1,Reference,Eukaryota,230,"Antifungal protein. May bind to beta-glucans and have beta-1,3-D-glucanase activity.","Antifungal protein. May bind to beta-glucans and have beta-1,3-D-glucanase activity.",,,,,,,GO:0052736; GO:0052861,,,,,,,,,,,0,,0.2944,no
ARGV_CORGL,Q8NQU4,ESM2Text,Bacteria,254,Part of the ABC transporter complex ArgTUV involved in L- arginine import. May also transport L-citrulline. Probably responsible for energy coupling to the transport system (Probable).,Part of the ABC transporter complex YtfQRT-YjfF involved in galactofuranose transport (Probable). Responsible for energy coupling to the transport system (Probable).,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887; GO:0015426,GO:0016887,GO:0042626,GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.5564,0.4396,0.527,0.833,0.833,5,0.6378,0.2642,no
ARGV_CORGL,Q8NQU4,Prot2Text,Bacteria,254,Part of the ABC transporter complex ArgTUV involved in L- arginine import. May also transport L-citrulline. Probably responsible for energy coupling to the transport system (Probable).,Probably part of a binding-protein-dependent transport system y4tEFGH for an amino acid. Probably responsible for energy coupling to the transport system.,Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0005524; GO:0016887; GO:0015426,,GO:0042626,,,GO:0042626,,0.4396,,,0.4396,2,0.4396,0.2642,no
ARGV_CORGL,Q8NQU4,ProtT3,Bacteria,254,Part of the ABC transporter complex ArgTUV involved in L- arginine import. May also transport L-citrulline. Probably responsible for energy coupling to the transport system (Probable).,Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system. Cell inner membrane; Peripheral membrane protein. Belongs to the ABC transporter superfamily. Methionine importer (TC 3.A.1.24) family,Maybe,No,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0016887; GO:0015426,GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0005524; GO:0016887,GO:0005524; GO:0016887,GO:0005524; GO:0016887,0.833,0.833,0.833,0.833,0.833,5,0.833,0.2642,no
ARGV_CORGL,Q8NQU4,ProtTale,Bacteria,254,Part of the ABC transporter complex ArgTUV involved in L- arginine import. May also transport L-citrulline. Probably responsible for energy coupling to the transport system (Probable).,Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. Probably responsible for energy coupling to the transport system.,Maybe,No,No,No,Maybe,not-Yes,GO:0005524; GO:0016887; GO:0015426,GO:0016887,GO:0005524,GO:0005524; GO:0016887,GO:0005524; GO:0016887,GO:0016887,0.5564,0.527,0.833,0.833,0.5564,5,0.6612,0.2642,no
ARGV_CORGL,Q8NQU4,Protein2Text,Bacteria,254,Part of the ABC transporter complex ArgTUV involved in L- arginine import. May also transport L-citrulline. Probably responsible for energy coupling to the transport system (Probable).,This protein is involved in the molecular function of binding a phosphate group.,Vague,No,Vague,No,No,not-Yes,GO:0005524; GO:0016887; GO:0015426,,,,,,,,,,,0,,0.2642,no
ARGV_CORGL,Q8NQU4,Reference,Bacteria,254,Part of the ABC transporter complex ArgTUV involved in L- arginine import. May also transport L-citrulline. Probably responsible for energy coupling to the transport system (Probable).,Part of the ABC transporter complex ArgTUV involved in L- arginine import. May also transport L-citrulline. Probably responsible for energy coupling to the transport system (Probable).,,,,,,,GO:0005524; GO:0016887; GO:0015426,GO:0005524,GO:0016887; GO:0005524,GO:0016887,GO:0016887; GO:0005524,GO:0005524; GO:0016887,0.527,0.833,0.5564,0.833,0.833,5,0.7165,0.2642,no
CTSZ_SPOGL,Q8RQU9,ESM2Text,Bacteria,1284,"Glycosyltransferase involved, together with CtsY, in the conversion of alpha-1,4-glucan into a cyclic tetrasaccharide (CTS) constructed from four alpha-glucopyranosyl residues. Catalyzes an intermolecular transglucosylation in which a glucose residue at the non-reducing end of maltotetraose is transferred to the 6-OH of an other non-reducing glucose, leading to the formation of alpha-isomaltosyl-(1->4)-D-maltotriose. Has a wide substrate specificity, and acts on oligosaccharides with alpha-1,4-glucosidic linkages at the non-reducing end, except for maltose. In contrast, has little activity toward oligosaccharides with alpha-1,6-glucosidic linkages at the non-reducing end.","Alpha-glucosidase that has both alpha-1,3- and alpha-1,6-glucosidase activity. Acts as a bifunctional enzyme, with a preference for the alpha-1,3-glucosidase group. Is able to hydrolyze both glucose residues in the GlcNAc-alpha-1,3-glucosidase cluster, as well as in the GlcNAc-alpha-1,6-glucosidase cluster, which displays a low level of activity toward glucosylated phenylpropanoids.",No,No,Maybe,Maybe,No,not-Yes,GO:0032001; GO:0030246; GO:0004553,GO:0004558,GO:0004558,GO:0004553,GO:0004558,GO:0004558,0.4027,0.4027,0.5969,0.4027,0.4027,5,0.4415,0.247,no
CTSZ_SPOGL,Q8RQU9,Prot2Text,Bacteria,1284,"Glycosyltransferase involved, together with CtsY, in the conversion of alpha-1,4-glucan into a cyclic tetrasaccharide (CTS) constructed from four alpha-glucopyranosyl residues. Catalyzes an intermolecular transglucosylation in which a glucose residue at the non-reducing end of maltotetraose is transferred to the 6-OH of an other non-reducing glucose, leading to the formation of alpha-isomaltosyl-(1->4)-D-maltotriose. Has a wide substrate specificity, and acts on oligosaccharides with alpha-1,4-glucosidic linkages at the non-reducing end, except for maltose. In contrast, has little activity toward oligosaccharides with alpha-1,6-glucosidic linkages at the non-reducing end.","High-alpha-galactosidase that specifically removes branched alpha-1,3-linked galactose residues present in blood group B antigens. Has a high preference for galactose residues at the non-reducing terminal, but can also remove terminal galactose residues from gangliosides, glycoproteins and lacto-N-biose. Has no activity toward melibiose, N-acetyl-D-galactosamine, N-acetyl-D-glucosamine, N-acetyl-D-galactosamine or lacto-N-biose.",No,No,No,No,No,not-Yes,GO:0032001; GO:0030246; GO:0004553,GO:0004557,GO:0004557,GO:0004557,GO:0004557,GO:0004557,0.4495,0.4495,0.4495,0.4495,0.4495,5,0.4495,0.247,no
CTSZ_SPOGL,Q8RQU9,ProtT3,Bacteria,1284,"Glycosyltransferase involved, together with CtsY, in the conversion of alpha-1,4-glucan into a cyclic tetrasaccharide (CTS) constructed from four alpha-glucopyranosyl residues. Catalyzes an intermolecular transglucosylation in which a glucose residue at the non-reducing end of maltotetraose is transferred to the 6-OH of an other non-reducing glucose, leading to the formation of alpha-isomaltosyl-(1->4)-D-maltotriose. Has a wide substrate specificity, and acts on oligosaccharides with alpha-1,4-glucosidic linkages at the non-reducing end, except for maltose. In contrast, has little activity toward oligosaccharides with alpha-1,6-glucosidic linkages at the non-reducing end.",Belongs to the glycosyl hydrolase 13 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0032001; GO:0030246; GO:0004553,GO:0016798,GO:0016798,GO:0016798,GO:0016798,GO:0016798,0.5373,0.5373,0.5373,0.5373,0.5373,5,0.5373,0.247,no
CTSZ_SPOGL,Q8RQU9,ProtTale,Bacteria,1284,"Glycosyltransferase involved, together with CtsY, in the conversion of alpha-1,4-glucan into a cyclic tetrasaccharide (CTS) constructed from four alpha-glucopyranosyl residues. Catalyzes an intermolecular transglucosylation in which a glucose residue at the non-reducing end of maltotetraose is transferred to the 6-OH of an other non-reducing glucose, leading to the formation of alpha-isomaltosyl-(1->4)-D-maltotriose. Has a wide substrate specificity, and acts on oligosaccharides with alpha-1,4-glucosidic linkages at the non-reducing end, except for maltose. In contrast, has little activity toward oligosaccharides with alpha-1,6-glucosidic linkages at the non-reducing end.","Catalyzes the hydrolysis of terminal alpha-1,4-linkages of alpha-(1->3)-glucan. Is involved in the degradation of alpha-(1->3)-glucans present in plant cell walls.",No,No,Maybe,Maybe,No,not-Yes,GO:0032001; GO:0030246; GO:0004553,GO:0004553,GO:0016798,GO:0004558,GO:0004553,GO:0004553,0.5969,0.5373,0.4027,0.5969,0.5969,5,0.5461,0.247,no
CTSZ_SPOGL,Q8RQU9,Protein2Text,Bacteria,1284,"Glycosyltransferase involved, together with CtsY, in the conversion of alpha-1,4-glucan into a cyclic tetrasaccharide (CTS) constructed from four alpha-glucopyranosyl residues. Catalyzes an intermolecular transglucosylation in which a glucose residue at the non-reducing end of maltotetraose is transferred to the 6-OH of an other non-reducing glucose, leading to the formation of alpha-isomaltosyl-(1->4)-D-maltotriose. Has a wide substrate specificity, and acts on oligosaccharides with alpha-1,4-glucosidic linkages at the non-reducing end, except for maltose. In contrast, has little activity toward oligosaccharides with alpha-1,6-glucosidic linkages at the non-reducing end.","This protein is a glucosidase, which means it has the molecular function of breaking down glucosidic bonds in complex carbohydrates. Specifically, it is involved in the hydrolysis of starch, a complex carbohydrate composed of glucose molecules.",No,No,No,No,No,not-Yes,GO:0032001; GO:0030246; GO:0004553,GO:0004553,GO:0004553,GO:0004553,GO:0004553,GO:0004558,0.5969,0.5969,0.5969,0.5969,0.4027,5,0.5581,0.247,no
CTSZ_SPOGL,Q8RQU9,Reference,Bacteria,1284,"Glycosyltransferase involved, together with CtsY, in the conversion of alpha-1,4-glucan into a cyclic tetrasaccharide (CTS) constructed from four alpha-glucopyranosyl residues. Catalyzes an intermolecular transglucosylation in which a glucose residue at the non-reducing end of maltotetraose is transferred to the 6-OH of an other non-reducing glucose, leading to the formation of alpha-isomaltosyl-(1->4)-D-maltotriose. Has a wide substrate specificity, and acts on oligosaccharides with alpha-1,4-glucosidic linkages at the non-reducing end, except for maltose. In contrast, has little activity toward oligosaccharides with alpha-1,6-glucosidic linkages at the non-reducing end.","Glycosyltransferase involved, together with CtsY, in the conversion of alpha-1,4-glucan into a cyclic tetrasaccharide (CTS) constructed from four alpha-glucopyranosyl residues. Catalyzes an intermolecular transglucosylation in which a glucose residue at the non-reducing end of maltotetraose is transferred to the 6-OH of an other non-reducing glucose, leading to the formation of alpha-isomaltosyl-(1->4)-D-maltotriose. Has a wide substrate specificity, and acts on oligosaccharides with alpha-1,4-glucosidic linkages at the non-reducing end, except for maltose. In contrast, has little activity toward oligosaccharides with alpha-1,6-glucosidic linkages at the non-reducing end.",,,,,,,GO:0032001; GO:0030246; GO:0004553,GO:0016757,GO:0046527,GO:0016757,GO:0016757,GO:0016757,0.4588,0.5328,0.4588,0.4588,0.4588,5,0.4736,0.247,no
CTSY_SPOGL,Q8RQV0,ESM2Text,Bacteria,1093,"Glycosyltransferase involved, together with CtsZ, in the conversion of alpha-1,4-glucan into a cyclic tetrasaccharide (CTS) constructed from four alpha-glucopyranosyl residues. Catalyzes the alpha-(1->3) transfer of the isomaltosyl moiety of alpha-isomaltosyl-(1->4)-D-maltotriose to another alpha-isomaltosyl-(1->4)-D-maltotriose, resulting in alpha-isomaltosyl- (1->3)-alpha-isomaltosyl-alpha-(1->4)-maltotriose formation. In addition, the enzyme catalyzes the intramolecular cyclization of the product, generating the cyclic tetrasaccharide cyclobis-(1->6)-alpha-nigerosyl.","Alpha-galactosidase involved in the hydrolysis of the intracellular alpha-1,4-glucosidic linkages in xyloglucan (Probable). Releases both alpha-1,4-glucosidic linkages and alpha-1,6-glucosidic linkages from xyloglucan oligosaccharides.",No,No,Maybe,Maybe,No,not-Yes,GO:0030246; GO:0016757; GO:0004553,GO:0004557,GO:0004557,GO:0004553,GO:0004557,GO:0004557,0.4753,0.4753,0.6273,0.4753,0.4753,5,0.5057,0.2217,no
CTSY_SPOGL,Q8RQV0,Prot2Text,Bacteria,1093,"Glycosyltransferase involved, together with CtsZ, in the conversion of alpha-1,4-glucan into a cyclic tetrasaccharide (CTS) constructed from four alpha-glucopyranosyl residues. Catalyzes the alpha-(1->3) transfer of the isomaltosyl moiety of alpha-isomaltosyl-(1->4)-D-maltotriose to another alpha-isomaltosyl-(1->4)-D-maltotriose, resulting in alpha-isomaltosyl- (1->3)-alpha-isomaltosyl-alpha-(1->4)-maltotriose formation. In addition, the enzyme catalyzes the intramolecular cyclization of the product, generating the cyclic tetrasaccharide cyclobis-(1->6)-alpha-nigerosyl.",Alpha-galactosidase associated with the sucrase operon.,No,No,No,No,No,not-Yes,GO:0030246; GO:0016757; GO:0004553,GO:0004557,GO:0004557,GO:0004557,GO:0004557,GO:0004557,0.4753,0.4753,0.4753,0.4753,0.4753,5,0.4753,0.2217,no
CTSY_SPOGL,Q8RQV0,ProtT3,Bacteria,1093,"Glycosyltransferase involved, together with CtsZ, in the conversion of alpha-1,4-glucan into a cyclic tetrasaccharide (CTS) constructed from four alpha-glucopyranosyl residues. Catalyzes the alpha-(1->3) transfer of the isomaltosyl moiety of alpha-isomaltosyl-(1->4)-D-maltotriose to another alpha-isomaltosyl-(1->4)-D-maltotriose, resulting in alpha-isomaltosyl- (1->3)-alpha-isomaltosyl-alpha-(1->4)-maltotriose formation. In addition, the enzyme catalyzes the intramolecular cyclization of the product, generating the cyclic tetrasaccharide cyclobis-(1->6)-alpha-nigerosyl.",Secreted. Belongs to the glycosyl hydrolase 13 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0030246; GO:0016757; GO:0004553,GO:0016798,GO:0016798,GO:0016798,GO:0016798,GO:0016798,0.5718,0.5718,0.5718,0.5718,0.5718,5,0.5718,0.2217,no
CTSY_SPOGL,Q8RQV0,ProtTale,Bacteria,1093,"Glycosyltransferase involved, together with CtsZ, in the conversion of alpha-1,4-glucan into a cyclic tetrasaccharide (CTS) constructed from four alpha-glucopyranosyl residues. Catalyzes the alpha-(1->3) transfer of the isomaltosyl moiety of alpha-isomaltosyl-(1->4)-D-maltotriose to another alpha-isomaltosyl-(1->4)-D-maltotriose, resulting in alpha-isomaltosyl- (1->3)-alpha-isomaltosyl-alpha-(1->4)-maltotriose formation. In addition, the enzyme catalyzes the intramolecular cyclization of the product, generating the cyclic tetrasaccharide cyclobis-(1->6)-alpha-nigerosyl.","Alpha-glucosidases, also called alpha-1,4-glucanases or alpha-1,3-glucanases, cleave the non-reducing end alpha-1,3-linked glucosyl residues from the non-reducing end of glucans. They play a role in the breakdown of certain alpha-glucans present in the diet, for example the disaccharide sucrose.",No,No,Maybe,Maybe,No,not-Yes,GO:0030246; GO:0016757; GO:0004553,GO:0004558,GO:0004553,GO:0016798,GO:0004553,GO:0004553,0.4271,0.6273,0.5718,0.6273,0.6273,5,0.5762,0.2217,no
CTSY_SPOGL,Q8RQV0,Protein2Text,Bacteria,1093,"Glycosyltransferase involved, together with CtsZ, in the conversion of alpha-1,4-glucan into a cyclic tetrasaccharide (CTS) constructed from four alpha-glucopyranosyl residues. Catalyzes the alpha-(1->3) transfer of the isomaltosyl moiety of alpha-isomaltosyl-(1->4)-D-maltotriose to another alpha-isomaltosyl-(1->4)-D-maltotriose, resulting in alpha-isomaltosyl- (1->3)-alpha-isomaltosyl-alpha-(1->4)-maltotriose formation. In addition, the enzyme catalyzes the intramolecular cyclization of the product, generating the cyclic tetrasaccharide cyclobis-(1->6)-alpha-nigerosyl.","This protein is a starch-degrading enzyme, which means it catalyzes the breakdown of starch molecules into simpler sugars. Specifically, it is a type of hydrolase, which uses water to cleave chemical bonds within starch molecules.",No,No,No,No,No,not-Yes,GO:0030246; GO:0016757; GO:0004553,GO:0004556,GO:0004556,GO:0004556,GO:0004556,GO:0016160,0.4753,0.4753,0.4753,0.4753,0.5397,5,0.4882,0.2217,no
CTSY_SPOGL,Q8RQV0,Reference,Bacteria,1093,"Glycosyltransferase involved, together with CtsZ, in the conversion of alpha-1,4-glucan into a cyclic tetrasaccharide (CTS) constructed from four alpha-glucopyranosyl residues. Catalyzes the alpha-(1->3) transfer of the isomaltosyl moiety of alpha-isomaltosyl-(1->4)-D-maltotriose to another alpha-isomaltosyl-(1->4)-D-maltotriose, resulting in alpha-isomaltosyl- (1->3)-alpha-isomaltosyl-alpha-(1->4)-maltotriose formation. In addition, the enzyme catalyzes the intramolecular cyclization of the product, generating the cyclic tetrasaccharide cyclobis-(1->6)-alpha-nigerosyl.","Glycosyltransferase involved, together with CtsZ, in the conversion of alpha-1,4-glucan into a cyclic tetrasaccharide (CTS) constructed from four alpha-glucopyranosyl residues. Catalyzes the alpha-(1->3) transfer of the isomaltosyl moiety of alpha-isomaltosyl-(1->4)-D-maltotriose to another alpha-isomaltosyl-(1->4)-D-maltotriose, resulting in alpha-isomaltosyl- (1->3)-alpha-isomaltosyl-alpha-(1->4)-maltotriose formation. In addition, the enzyme catalyzes the intramolecular cyclization of the product, generating the cyclic tetrasaccharide cyclobis-(1->6)-alpha-nigerosyl.",,,,,,,GO:0030246; GO:0016757; GO:0004553,GO:0016757,GO:0046527,GO:0016757,GO:0016757,GO:0016757,0.6355,0.4628,0.6355,0.6355,0.6355,5,0.601,0.2217,no
GNAT9_ARATH,Q8S8E7,ESM2Text,Eukaryota,218,Probable protein acetyltransferase with dual specificity triggering both N-alpha-acetylation (NTA) and epsilon-lysine acetylation (KA).,Extracellular N-acetyltransferase that mediates acetylation of the N-terminal residues of alpha- and beta-tubulin. Acetylates the N-terminal alanine of alpha-tubulin as well as the C-terminal residues of microtubules.,Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0008080; GO:0061733,GO:0008080,GO:0016407,GO:0008080,GO:0008080,GO:0004596,0.9114,0.7216,0.9114,0.9114,0.8064,5,0.8524,0.3738,no
GNAT9_ARATH,Q8S8E7,Prot2Text,Eukaryota,218,Probable protein acetyltransferase with dual specificity triggering both N-alpha-acetylation (NTA) and epsilon-lysine acetylation (KA).,Acetylates both alpha- and beta-tubulin.,Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0008080; GO:0061733,GO:0019799,GO:0019799,GO:0016746,GO:0016407,GO:0008080,0.843,0.843,0.5396,0.7216,0.9114,5,0.7717,0.3738,no
GNAT9_ARATH,Q8S8E7,ProtT3,Eukaryota,218,Probable protein acetyltransferase with dual specificity triggering both N-alpha-acetylation (NTA) and epsilon-lysine acetylation (KA).,Belongs to the acetyltransferase family. GNAT subfamily,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008080; GO:0061733,GO:0016407,GO:0008080,GO:0008080,GO:0016407,GO:0016407,0.7216,0.9114,0.9114,0.7216,0.7216,5,0.7975,0.3738,no
GNAT9_ARATH,Q8S8E7,ProtTale,Eukaryota,218,Probable protein acetyltransferase with dual specificity triggering both N-alpha-acetylation (NTA) and epsilon-lysine acetylation (KA).,Involved in the post-translational modification of proteins. Catalyzes the removal of N-acetylglucosamine (GlcNAc) from the N-terminus of proteins (glycylation). The GlcNAc at the C-terminus is usually acetylated.,No,No,No,No,No,not-Yes,GO:0008080; GO:0061733,GO:0016799,GO:0016787,GO:0016798,GO:0016787,,0.1811,0.2707,0.2184,0.2707,,4,0.2352,0.3738,no
GNAT9_ARATH,Q8S8E7,Protein2Text,Eukaryota,218,Probable protein acetyltransferase with dual specificity triggering both N-alpha-acetylation (NTA) and epsilon-lysine acetylation (KA).,"The molecular function of this protein is not explicitly stated in the provided text. However, based on its name and the context, it is likely that this protein is involved in the modification of other proteins by adding a phosphate group, a process known as phosphorylation. Phosphorylation is a common post-translational modification that plays a crucial role in many cellular processes, including signal transduction, metabolism, and gene regulation. The protein is likely to be a kinase, an enzyme that transfers a phosphate group from a donor molecule, such as ATP, to a substrate protein.",Vague,No,No,No,Vague,not-Yes,GO:0008080; GO:0061733,,,,,GO:0004672,,,,,0.3047,1,0.3047,0.3738,no
GNAT9_ARATH,Q8S8E7,Reference,Eukaryota,218,Probable protein acetyltransferase with dual specificity triggering both N-alpha-acetylation (NTA) and epsilon-lysine acetylation (KA).,Probable protein acetyltransferase with dual specificity triggering both N-alpha-acetylation (NTA) and epsilon-lysine acetylation (KA).,,,,,,,GO:0008080; GO:0061733,GO:0004468; GO:0061733,GO:0004468; GO:0004596,GO:0016407,GO:0016407,GO:0016746,0.9062,0.8275,0.7216,0.7216,0.5396,5,0.7433,0.3738,no
PRO_BPDPK,Q8SCY7,ESM2Text,Viruses,270,"Serine protease that is responsible for cleaving many of the prohead proteins during a major morphogenetic step in viral capsid maturation. Cleaves the major capsid protein at 7 [A,G,S]-X-E recognition sites.",Second step of mRNA capping. Transfer of the GMP moiety of GTP to the 5'-end of RNA via an enzyme-GMP covalent reaction intermediate.,No,No,No,No,No,not-Yes,GO:0008236,GO:0004484,GO:0004484,GO:0004484,GO:0004484,GO:0004484,0.1598,0.1598,0.1598,0.1598,0.1598,5,0.1598,0.2841,no
PRO_BPDPK,Q8SCY7,Prot2Text,Viruses,270,"Serine protease that is responsible for cleaving many of the prohead proteins during a major morphogenetic step in viral capsid maturation. Cleaves the major capsid protein at 7 [A,G,S]-X-E recognition sites.",Second step of mRNA capping. Transfer of the GMP moiety of GTP to the 5'-end of RNA via an enzyme-GMP covalent reaction intermediate.,No,No,No,No,No,not-Yes,GO:0008236,GO:0004484,GO:0004484,GO:0004484,GO:0004484,GO:0004484,0.1598,0.1598,0.1598,0.1598,0.1598,5,0.1598,0.2841,no
PRO_BPDPK,Q8SCY7,ProtT3,Viruses,270,"Serine protease that is responsible for cleaving many of the prohead proteins during a major morphogenetic step in viral capsid maturation. Cleaves the major capsid protein at 7 [A,G,S]-X-E recognition sites.","Major capsid protein that self-associates to form hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Virion. Belongs to the asfivirus hexon family",No,No,Vague,Vague,No,not-Yes,GO:0008236,GO:0005198,GO:0005198,,GO:0005198,,0.1832,0.1832,,0.1832,,3,0.1832,0.2841,no
PRO_BPDPK,Q8SCY7,ProtTale,Viruses,270,"Serine protease that is responsible for cleaving many of the prohead proteins during a major morphogenetic step in viral capsid maturation. Cleaves the major capsid protein at 7 [A,G,S]-X-E recognition sites.","Cleaves peptides in other bacteria in the bacterial cell wall, with the exception of L.lactis.",Maybe,No,No,No,Maybe,not-Yes,GO:0008236,GO:0008233,GO:0008233,GO:0008233,GO:0008233,GO:0008233,0.7896,0.7896,0.7896,0.7896,0.7896,5,0.7896,0.2841,no
PRO_BPDPK,Q8SCY7,Protein2Text,Viruses,270,"Serine protease that is responsible for cleaving many of the prohead proteins during a major morphogenetic step in viral capsid maturation. Cleaves the major capsid protein at 7 [A,G,S]-X-E recognition sites.","The molecular function of this protein is not explicitly stated in the provided information. However, based on its classification as a protein, it is likely involved in a variety of molecular functions such as catalyzing chemical reactions, binding to other molecules, or participating in cellular processes. To determine the specific molecular function of this protein, additional information or research would be necessary.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008236,,,,,,,,,,,0,,0.2841,no
PRO_BPDPK,Q8SCY7,Reference,Viruses,270,"Serine protease that is responsible for cleaving many of the prohead proteins during a major morphogenetic step in viral capsid maturation. Cleaves the major capsid protein at 7 [A,G,S]-X-E recognition sites.","Serine protease that is responsible for cleaving many of the prohead proteins during a major morphogenetic step in viral capsid maturation. Cleaves the major capsid protein at 7 [A,G,S]-X-E recognition sites.",,,,,,,GO:0008236,GO:0004252,GO:0004252,GO:0008236,GO:0004252,GO:0004252,0.8276,0.8276,1.0,0.8276,0.8276,5,0.8621,0.2841,no
RGYRA_METKA,Q8TYK7,ESM2Text,Archaea,358,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process; dATP also allows positive supercoiling. Increases the linking number in steps of +1. Only this subunit binds DNA, in isolation it does not hydrolyze ATP. Hydrolyzes ATP only in the presence of DNA. Transiently cleaves a single DNA strand and remains covalently bound to the 5' DNA end probably through a tyrosine residue. It changes linking number in steps of one, and nicks DNA preferentially at 5'-CNNN | 3'-sites with a strong preference for 4 pyrimidine residues. There are about 1000 heterodimers per cell. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.",Imparts immunity to pedicel-type bacteria M.tuberculosis and M.phleohemopictus to naturally sensitive strains. It probably has a role in DNA replication and cell division.,Vague,No,No,No,Vague,not-Yes,GO:0003677; GO:0160097,,,,,,,,,,,0,,0.6897,yes
RGYRA_METKA,Q8TYK7,Prot2Text,Archaea,358,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process; dATP also allows positive supercoiling. Increases the linking number in steps of +1. Only this subunit binds DNA, in isolation it does not hydrolyze ATP. Hydrolyzes ATP only in the presence of DNA. Transiently cleaves a single DNA strand and remains covalently bound to the 5' DNA end probably through a tyrosine residue. It changes linking number in steps of one, and nicks DNA preferentially at 5'-CNNN | 3'-sites with a strong preference for 4 pyrimidine residues. There are about 1000 heterodimers per cell. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.",DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms the clamp head domain.,No,No,No,No,No,not-Yes,GO:0003677; GO:0160097,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.1751,0.1751,0.1751,0.1751,0.1751,5,0.1751,0.6897,yes
RGYRA_METKA,Q8TYK7,ProtT3,Archaea,358,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process; dATP also allows positive supercoiling. Increases the linking number in steps of +1. Only this subunit binds DNA, in isolation it does not hydrolyze ATP. Hydrolyzes ATP only in the presence of DNA. Transiently cleaves a single DNA strand and remains covalently bound to the 5' DNA end probably through a tyrosine residue. It changes linking number in steps of one, and nicks DNA preferentially at 5'-CNNN | 3'-sites with a strong preference for 4 pyrimidine residues. There are about 1000 heterodimers per cell. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.",Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. Cytoplasm. Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family,No,No,No,No,No,not-Yes,GO:0003677; GO:0160097,GO:0008173,GO:0070040,GO:0070040,GO:0008649,GO:0008173,0.2145,0.1361,0.1361,0.1662,0.2145,5,0.1735,0.6897,yes
RGYRA_METKA,Q8TYK7,ProtTale,Archaea,358,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process; dATP also allows positive supercoiling. Increases the linking number in steps of +1. Only this subunit binds DNA, in isolation it does not hydrolyze ATP. Hydrolyzes ATP only in the presence of DNA. Transiently cleaves a single DNA strand and remains covalently bound to the 5' DNA end probably through a tyrosine residue. It changes linking number in steps of one, and nicks DNA preferentially at 5'-CNNN | 3'-sites with a strong preference for 4 pyrimidine residues. There are about 1000 heterodimers per cell. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.","Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally,",Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0003677; GO:0160097,GO:0003917,GO:0003917; GO:0003677,GO:0003917,GO:0003917,GO:0003917,0.5738,0.9048,0.5738,0.5738,0.5738,5,0.64,0.6897,yes
RGYRA_METKA,Q8TYK7,Protein2Text,Archaea,358,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process; dATP also allows positive supercoiling. Increases the linking number in steps of +1. Only this subunit binds DNA, in isolation it does not hydrolyze ATP. Hydrolyzes ATP only in the presence of DNA. Transiently cleaves a single DNA strand and remains covalently bound to the 5' DNA end probably through a tyrosine residue. It changes linking number in steps of one, and nicks DNA preferentially at 5'-CNNN | 3'-sites with a strong preference for 4 pyrimidine residues. There are about 1000 heterodimers per cell. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.","This protein is a molecular function of the SMC (Structural Maintenance of Chromosomes) family, specifically a RecG-like protein. RecG-like proteins are involved in DNA repair, homologous recombination, and DNA replication, and have a role in maintaining genome stability. They possess ATPase activity and exhibit DNA-binding properties, enabling them to perform a range of functions in maintaining the integrity of the bacterial genome. 

In more detail, the molecular function of this protein is likely to be involved in the following processes:

1. DNA unwinding: As a RecG-like protein, this protein is likely to be involved in the unwinding of DNA, which is a crucial step in various DNA processes such as replication, repair, and recombination.

2. DNA binding: This protein is likely to bind to DNA, which is a prerequisite for its other functions such as DNA unwinding, DNA resection, and DNA annealing.

3. ATPase activity: This protein is likely to possess ATPase activity, which is necessary for its DNA unwinding and other functions.

4. DNA resection: This protein is likely to be involved in DNA resection, which is the removal of single-stranded DNA from a double-stranded DNA molecule.

5. DNA annealing: This protein is likely to be involved in DNA annealing, which is the process of joining two complementary single-stranded DNA molecules together.

6. DNA repair: This protein is likely to be involved in DNA repair, which is the process of correcting errors in DNA.

7. Homologous recombination: This protein is likely to be involved in homologous recombination, which is the process of exchanging genetic material between two DNA molecules.

8. Genome stability: This protein is likely to play a role in maintaining genome stability, which is the ability of the genome to maintain its integrity over time.",No,No,No,No,No,not-Yes,GO:0003677; GO:0160097,GO:0005524; GO:0003677; GO:0004386,GO:0004386; GO:0005524; GO:0003677,GO:0004003; GO:0005524; GO:0003677,GO:0004386; GO:0005524; GO:0003677,GO:0003678; GO:0016887,0.68,0.68,0.6699,0.68,0.3631,5,0.6146,0.6897,yes
RGYRA_METKA,Q8TYK7,Reference,Archaea,358,"Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process; dATP also allows positive supercoiling. Increases the linking number in steps of +1. Only this subunit binds DNA, in isolation it does not hydrolyze ATP. Hydrolyzes ATP only in the presence of DNA. Transiently cleaves a single DNA strand and remains covalently bound to the 5' DNA end probably through a tyrosine residue. It changes linking number in steps of one, and nicks DNA preferentially at 5'-CNNN | 3'-sites with a strong preference for 4 pyrimidine residues. There are about 1000 heterodimers per cell. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.","Modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process; dATP also allows positive supercoiling. Increases the linking number in steps of +1. Only this subunit binds DNA, in isolation it does not hydrolyze ATP. Hydrolyzes ATP only in the presence of DNA. Transiently cleaves a single DNA strand and remains covalently bound to the 5' DNA end probably through a tyrosine residue. It changes linking number in steps of one, and nicks DNA preferentially at 5'-CNNN | 3'-sites with a strong preference for 4 pyrimidine residues. There are about 1000 heterodimers per cell. May be involved in rewinding the DNA strands in the regions of the chromosome that have opened up to allow transcription or replication.",,,,,,,GO:0003677; GO:0160097,GO:0003916; GO:0003917; GO:0005524; GO:0003677,GO:0003916; GO:0003677; GO:0005524,GO:0003916; GO:0016887; GO:0003677,GO:0003916; GO:0003677; GO:0005524; GO:0016887,GO:0003916; GO:0005524; GO:0003677,0.7976,0.7952,0.7909,0.6867,0.7952,5,0.7731,0.6897,yes
MICAH_NOSS1,Q8YT18,ESM2Text,Bacteria,205,Catalyzes the hydration of carbon dioxide (CO2) to bicarbonate (HCO3(-)). Has only very low bicarbonate dehydration activity. May function even in metal-poor environments.,"Has menaquinol-oxidizing activity. The HpaO protein is probably a component of a type I periplasmic protein-protein interaction channel, which may facilitate the interaction between the HpaO subunit and periplasmic proteins.",No,No,No,No,No,not-Yes,GO:0004089,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.3552,0.3552,0.3552,0.3552,0.3552,5,0.3552,0.195,no
MICAH_NOSS1,Q8YT18,Prot2Text,Bacteria,205,Catalyzes the hydration of carbon dioxide (CO2) to bicarbonate (HCO3(-)). Has only very low bicarbonate dehydration activity. May function even in metal-poor environments.,"Unknown. In vitro, does not have RuBisCO activity.",Vague,No,No,No,Vague,not-Yes,GO:0004089,,,,,,,,,,,0,,0.195,no
MICAH_NOSS1,Q8YT18,ProtT3,Bacteria,205,Catalyzes the hydration of carbon dioxide (CO2) to bicarbonate (HCO3(-)). Has only very low bicarbonate dehydration activity. May function even in metal-poor environments.,Secreted. Belongs to the UPF0478 family,Vague,No,Vague,Vague,Vague,not-Yes,GO:0004089,,,,,,,,,,,0,,0.195,no
MICAH_NOSS1,Q8YT18,ProtTale,Bacteria,205,Catalyzes the hydration of carbon dioxide (CO2) to bicarbonate (HCO3(-)). Has only very low bicarbonate dehydration activity. May function even in metal-poor environments.,Could be involved in the utilization of the non-reducing disaccharide sucrose.,No,No,No,No,No,not-Yes,GO:0004089,,,,,,,,,,,0,,0.195,no
MICAH_NOSS1,Q8YT18,Protein2Text,Bacteria,205,Catalyzes the hydration of carbon dioxide (CO2) to bicarbonate (HCO3(-)). Has only very low bicarbonate dehydration activity. May function even in metal-poor environments.,"This protein is involved in the breakdown of urea, a process that helps to remove excess nitrogen from the body. It is a urease, an enzyme that catalyzes the hydrolysis of urea into ammonia and carbon dioxide. This process is important in many organisms, including bacteria, plants, and animals, and helps to regulate the levels of nitrogen in the body.",No,No,No,No,No,not-Yes,GO:0004089,GO:0009039,GO:0009039,GO:0009039,GO:0009039,GO:0009039,0.1998,0.1998,0.1998,0.1998,0.1998,5,0.1998,0.195,no
MICAH_NOSS1,Q8YT18,Reference,Bacteria,205,Catalyzes the hydration of carbon dioxide (CO2) to bicarbonate (HCO3(-)). Has only very low bicarbonate dehydration activity. May function even in metal-poor environments.,Catalyzes the hydration of carbon dioxide (CO2) to bicarbonate (HCO3(-)). Has only very low bicarbonate dehydration activity. May function even in metal-poor environments.,,,,,,,GO:0004089,GO:0004089,GO:0004089,GO:0004089,GO:0004089,GO:0004089,1.0,1.0,1.0,1.0,1.0,5,1.0,0.195,no
MIFH1_ONCVO,Q963F7,ESM2Text,Eukaryota,115,Tautomerization of the methyl ester of L-dopachrome. Inhibits migration of human peripheral blood mononuclear cells.,Tautomerization of the methyl ester of L-dopachrome. Inhibits the growth of several stationary-phase cells.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005125; GO:0004167; GO:0050178,GO:0016853,GO:0004167,GO:0016853,GO:0016853,GO:0004974,0.4879,0.6488,0.4879,0.4879,0.076,5,0.4377,0.1279,no
MIFH1_ONCVO,Q963F7,Prot2Text,Eukaryota,115,Tautomerization of the methyl ester of L-dopachrome. Inhibits migration of human peripheral blood mononuclear cells.,"Tautomerization of D-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI).",Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0005125; GO:0004167; GO:0050178,GO:0016853,GO:0030400,GO:0030760,GO:0004167,GO:0030760,0.4879,0.0,0.1484,0.6488,0.1484,5,0.2867,0.1279,no
MIFH1_ONCVO,Q963F7,ProtT3,Eukaryota,115,Tautomerization of the methyl ester of L-dopachrome. Inhibits migration of human peripheral blood mononuclear cells.,Tautomerization of the aromatic ring of L-dopachrome. Secreted. Belongs to the MIF family,Yes,Yes,Maybe,Maybe,Yes,Yes,GO:0005125; GO:0004167; GO:0050178,GO:0004167,GO:0004167,GO:0004167,GO:0004167,GO:0004167,0.6488,0.6488,0.6488,0.6488,0.6488,5,0.6488,0.1279,no
MIFH1_ONCVO,Q963F7,ProtTale,Eukaryota,115,Tautomerization of the methyl ester of L-dopachrome. Inhibits migration of human peripheral blood mononuclear cells.,"Tartrate-utilizing enzyme; part of the gene clusters that mediate the biosynthesis of AM-toxins, host-selective toxins (HSTs) causing Alternaria blotch on apple, a worldwide distributed disease (Probable). AM-toxins are cyclic depsipeptides containing the 3 residues 2-hydroxy-isovaleric acid (2-HIV), dehydroalanine, L-alanine which are common for all 3 AM-toxins I to III. The fourth precursor is L-alpha-amino-methoxyphenyl-valeric acid (L-Amv) for AM",No,Yes,No,No,No,not-Yes,GO:0005125; GO:0004167; GO:0050178,,,,,,,,,,,0,,0.1279,no
MIFH1_ONCVO,Q963F7,Protein2Text,Eukaryota,115,Tautomerization of the methyl ester of L-dopachrome. Inhibits migration of human peripheral blood mononuclear cells.,"The molecular function of this protein is not specified in the provided text. However, based on its name, it is likely involved in the regulation of the immune system, specifically in the inflammatory response. The protein is likely a cytokine or a chemokine, which are small proteins that are produced by cells and play a crucial role in the immune response by promoting the recruitment of immune cells to sites of inflammation.",Vague,No,Vague,No,Vague,not-Yes,GO:0005125; GO:0004167; GO:0050178,,,,,,,,,,,0,,0.1279,no
MIFH1_ONCVO,Q963F7,Reference,Eukaryota,115,Tautomerization of the methyl ester of L-dopachrome. Inhibits migration of human peripheral blood mononuclear cells.,Tautomerization of the methyl ester of L-dopachrome. Inhibits migration of human peripheral blood mononuclear cells.,,,,,,,GO:0005125; GO:0004167; GO:0050178,GO:0050179,GO:0004167,GO:0004167,GO:0004168,GO:0004167,0.1706,0.6488,0.6488,0.1541,0.6488,5,0.4542,0.1279,no
XPB1_SULTO,Q971U1,ESM2Text,Archaea,543,"ATP-dependent 3'-5' DNA helicase. A DNA- dependent ATPase; single-stranded DNA (ssDNA) stimulates the activity more than double-stranded DNA (dsDNA). Binds ssDNA better than dsDNA. Destabilizes dsDNA in a non-ATP-dependent manner; blunt-ended DNA is a better substrate than 3' overhang DNA. Probably destabilizes by binding ssDNA, increasing amounts of ssDNA decrease destabilization while increasing amounts of single-stranded DNA binding protein (SSB) increase destabilization. Bax1 does not stimulate the ATPase.","The DNA-dependent ATPase activity of XcpA (XcpA-2) is essential for DNA repair. Stimulates the ATPase activity of XcpA-2 and binds single-stranded DNA, but not double-stranded DNA. Can also open a bubble in DNA by catalyzing ATP hydrolysis.",Yes,No,Maybe,Maybe,Yes,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0016887; GO:0003697,GO:0003697; GO:0008094,GO:0016887; GO:0003697,GO:0003697; GO:0016887; GO:0005524,GO:0003697; GO:0016887; GO:0005524,0.4989,0.5898,0.4989,0.693,0.693,5,0.5947,0.7496,yes
XPB1_SULTO,Q971U1,Prot2Text,Archaea,543,"ATP-dependent 3'-5' DNA helicase. A DNA- dependent ATPase; single-stranded DNA (ssDNA) stimulates the activity more than double-stranded DNA (dsDNA). Binds ssDNA better than dsDNA. Destabilizes dsDNA in a non-ATP-dependent manner; blunt-ended DNA is a better substrate than 3' overhang DNA. Probably destabilizes by binding ssDNA, increasing amounts of ssDNA decrease destabilization while increasing amounts of single-stranded DNA binding protein (SSB) increase destabilization. Bax1 does not stimulate the ATPase.","A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.",No,No,No,Maybe,No,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0003918,GO:0003918,GO:0003918; GO:0005524,GO:0003918,GO:0003918,0.3577,0.3577,0.6322,0.3577,0.3577,5,0.4126,0.7496,yes
XPB1_SULTO,Q971U1,ProtT3,Archaea,543,"ATP-dependent 3'-5' DNA helicase. A DNA- dependent ATPase; single-stranded DNA (ssDNA) stimulates the activity more than double-stranded DNA (dsDNA). Binds ssDNA better than dsDNA. Destabilizes dsDNA in a non-ATP-dependent manner; blunt-ended DNA is a better substrate than 3' overhang DNA. Probably destabilizes by binding ssDNA, increasing amounts of ssDNA decrease destabilization while increasing amounts of single-stranded DNA binding protein (SSB) increase destabilization. Bax1 does not stimulate the ATPase.",Belongs to the DEAD box helicase family. DEAH subfamily,Vague,No,Vague,Vague,Vague,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0003724; GO:0005524,GO:0003724; GO:0005524,GO:0003724; GO:0005524,GO:0003724; GO:0005524,GO:0003724; GO:0005524,0.6039,0.6039,0.6039,0.6039,0.6039,5,0.6039,0.7496,yes
XPB1_SULTO,Q971U1,ProtTale,Archaea,543,"ATP-dependent 3'-5' DNA helicase. A DNA- dependent ATPase; single-stranded DNA (ssDNA) stimulates the activity more than double-stranded DNA (dsDNA). Binds ssDNA better than dsDNA. Destabilizes dsDNA in a non-ATP-dependent manner; blunt-ended DNA is a better substrate than 3' overhang DNA. Probably destabilizes by binding ssDNA, increasing amounts of ssDNA decrease destabilization while increasing amounts of single-stranded DNA binding protein (SSB) increase destabilization. Bax1 does not stimulate the ATPase.",DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks.,Yes,No,Maybe,Maybe,Yes,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0003678; GO:0005524; GO:0016887,GO:0004386; GO:0005524; GO:0003677; GO:0016887,GO:0004386; GO:0005524; GO:0003677; GO:0016887,GO:0004386; GO:0005524; GO:0016887; GO:0003677,GO:0003678; GO:0016887,0.7085,0.8085,0.8085,0.8085,0.4966,5,0.7261,0.7496,yes
XPB1_SULTO,Q971U1,Protein2Text,Archaea,543,"ATP-dependent 3'-5' DNA helicase. A DNA- dependent ATPase; single-stranded DNA (ssDNA) stimulates the activity more than double-stranded DNA (dsDNA). Binds ssDNA better than dsDNA. Destabilizes dsDNA in a non-ATP-dependent manner; blunt-ended DNA is a better substrate than 3' overhang DNA. Probably destabilizes by binding ssDNA, increasing amounts of ssDNA decrease destabilization while increasing amounts of single-stranded DNA binding protein (SSB) increase destabilization. Bax1 does not stimulate the ATPase.","This protein is a DNA helicase, which means it plays a crucial role in unwinding double-stranded DNA into single strands, allowing other enzymes to access the DNA for various processes such as replication, repair, and transcription. Specifically, it is a type II DNA helicase.",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0004003; GO:0003678,GO:0004003,GO:0004003; GO:0003677,GO:0004003; GO:0003677,GO:0003678,0.5329,0.454,0.7131,0.7131,0.454,5,0.5734,0.7496,yes
XPB1_SULTO,Q971U1,Reference,Archaea,543,"ATP-dependent 3'-5' DNA helicase. A DNA- dependent ATPase; single-stranded DNA (ssDNA) stimulates the activity more than double-stranded DNA (dsDNA). Binds ssDNA better than dsDNA. Destabilizes dsDNA in a non-ATP-dependent manner; blunt-ended DNA is a better substrate than 3' overhang DNA. Probably destabilizes by binding ssDNA, increasing amounts of ssDNA decrease destabilization while increasing amounts of single-stranded DNA binding protein (SSB) increase destabilization. Bax1 does not stimulate the ATPase.","ATP-dependent 3'-5' DNA helicase. A DNA- dependent ATPase; single-stranded DNA (ssDNA) stimulates the activity more than double-stranded DNA (dsDNA). Binds ssDNA better than dsDNA. Destabilizes dsDNA in a non-ATP-dependent manner; blunt-ended DNA is a better substrate than 3' overhang DNA. Probably destabilizes by binding ssDNA, increasing amounts of ssDNA decrease destabilization while increasing amounts of single-stranded DNA binding protein (SSB) increase destabilization. Bax1 does not stimulate the ATPase.",,,,,,,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0004386; GO:0005524; GO:0003697,GO:0003678; GO:0016887; GO:0005524,GO:0003678; GO:0016887; GO:0003677,GO:0004386; GO:0016887; GO:0003677; GO:0005524,GO:0003678; GO:0016887; GO:0005524,0.7915,0.7085,0.7085,0.8085,0.7085,5,0.7451,0.7496,yes
TOP3_SACS2,Q97ZJ8,ESM2Text,Archaea,668,"Relaxes negatively supercoiled (SC) DNA in an ATP-independent manner at 75 degrees Celsius. From 50-85 degrees Celsius relaxes negatively SC DNA; at up to 100 degrees Celsius it unlinks catenated DNA to form circular double-stranded (ds)DNA molecules. The promotion or prevention of DNA linking/unlinking is temperature-dependent in vitro and probably depends on other factors in vivo. One study found single-stranded binding protein (SSB) does not enhance its activity , while another study found it does. Binds single-stranded (ss)DNA and less well to Holliday junction (HJ) or forked DNA. Anneals complementary oligonucleotides to form HJ structures.","Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.",Yes,Yes,Maybe,Yes,Yes,Yes,GO:0003677; GO:0003917; GO:0046872,GO:0003917,GO:0003917,GO:0003917,GO:0003917,GO:0003917,0.5439,0.5439,0.5439,0.5439,0.5439,5,0.5439,0.7598,yes
TOP3_SACS2,Q97ZJ8,Prot2Text,Archaea,668,"Relaxes negatively supercoiled (SC) DNA in an ATP-independent manner at 75 degrees Celsius. From 50-85 degrees Celsius relaxes negatively SC DNA; at up to 100 degrees Celsius it unlinks catenated DNA to form circular double-stranded (ds)DNA molecules. The promotion or prevention of DNA linking/unlinking is temperature-dependent in vitro and probably depends on other factors in vivo. One study found single-stranded binding protein (SSB) does not enhance its activity , while another study found it does. Binds single-stranded (ss)DNA and less well to Holliday junction (HJ) or forked DNA. Anneals complementary oligonucleotides to form HJ structures.","Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.",Yes,Yes,Maybe,Yes,Yes,Yes,GO:0003677; GO:0003917; GO:0046872,GO:0003917,GO:0003917,GO:0003917,GO:0003917,GO:0003917,0.5439,0.5439,0.5439,0.5439,0.5439,5,0.5439,0.7598,yes
TOP3_SACS2,Q97ZJ8,ProtT3,Archaea,668,"Relaxes negatively supercoiled (SC) DNA in an ATP-independent manner at 75 degrees Celsius. From 50-85 degrees Celsius relaxes negatively SC DNA; at up to 100 degrees Celsius it unlinks catenated DNA to form circular double-stranded (ds)DNA molecules. The promotion or prevention of DNA linking/unlinking is temperature-dependent in vitro and probably depends on other factors in vivo. One study found single-stranded binding protein (SSB) does not enhance its activity , while another study found it does. Binds single-stranded (ss)DNA and less well to Holliday junction (HJ) or forked DNA. Anneals complementary oligonucleotides to form HJ structures.","Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally",Yes,Yes,Yes,Yes,Yes,Yes,GO:0003677; GO:0003917; GO:0046872,GO:0003917,GO:0003917,GO:0003917,GO:0003917,GO:0003917,0.5439,0.5439,0.5439,0.5439,0.5439,5,0.5439,0.7598,yes
TOP3_SACS2,Q97ZJ8,ProtTale,Archaea,668,"Relaxes negatively supercoiled (SC) DNA in an ATP-independent manner at 75 degrees Celsius. From 50-85 degrees Celsius relaxes negatively SC DNA; at up to 100 degrees Celsius it unlinks catenated DNA to form circular double-stranded (ds)DNA molecules. The promotion or prevention of DNA linking/unlinking is temperature-dependent in vitro and probably depends on other factors in vivo. One study found single-stranded binding protein (SSB) does not enhance its activity , while another study found it does. Binds single-stranded (ss)DNA and less well to Holliday junction (HJ) or forked DNA. Anneals complementary oligonucleotides to form HJ structures.","Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally,",Yes,Yes,Yes,Yes,Yes,Yes,GO:0003677; GO:0003917; GO:0046872,GO:0003917,GO:0003917; GO:0003677,GO:0003917,GO:0003917,GO:0003917,0.5439,0.8569,0.5439,0.5439,0.5439,5,0.6065,0.7598,yes
TOP3_SACS2,Q97ZJ8,Protein2Text,Archaea,668,"Relaxes negatively supercoiled (SC) DNA in an ATP-independent manner at 75 degrees Celsius. From 50-85 degrees Celsius relaxes negatively SC DNA; at up to 100 degrees Celsius it unlinks catenated DNA to form circular double-stranded (ds)DNA molecules. The promotion or prevention of DNA linking/unlinking is temperature-dependent in vitro and probably depends on other factors in vivo. One study found single-stranded binding protein (SSB) does not enhance its activity , while another study found it does. Binds single-stranded (ss)DNA and less well to Holliday junction (HJ) or forked DNA. Anneals complementary oligonucleotides to form HJ structures.","The molecular function of this protein is a DNA polymerase, specifically a DNA-dependent polymerase that synthesizes DNA from a DNA template.",No,No,No,No,No,not-Yes,GO:0003677; GO:0003917; GO:0046872,GO:0003887,GO:0003887,GO:0003887,GO:0003887,GO:0003887,0.2238,0.2238,0.2238,0.2238,0.2238,5,0.2238,0.7598,yes
TOP3_SACS2,Q97ZJ8,Reference,Archaea,668,"Relaxes negatively supercoiled (SC) DNA in an ATP-independent manner at 75 degrees Celsius. From 50-85 degrees Celsius relaxes negatively SC DNA; at up to 100 degrees Celsius it unlinks catenated DNA to form circular double-stranded (ds)DNA molecules. The promotion or prevention of DNA linking/unlinking is temperature-dependent in vitro and probably depends on other factors in vivo. One study found single-stranded binding protein (SSB) does not enhance its activity , while another study found it does. Binds single-stranded (ss)DNA and less well to Holliday junction (HJ) or forked DNA. Anneals complementary oligonucleotides to form HJ structures.","Relaxes negatively supercoiled (SC) DNA in an ATP-independent manner at 75 degrees Celsius. From 50-85 degrees Celsius relaxes negatively SC DNA; at up to 100 degrees Celsius it unlinks catenated DNA to form circular double-stranded (ds)DNA molecules. The promotion or prevention of DNA linking/unlinking is temperature-dependent in vitro and probably depends on other factors in vivo. One study found single-stranded binding protein (SSB) does not enhance its activity , while another study found it does. Binds single-stranded (ss)DNA and less well to Holliday junction (HJ) or forked DNA. Anneals complementary oligonucleotides to form HJ structures.",,,,,,,GO:0003677; GO:0003917; GO:0046872,GO:0003916; GO:0003697,GO:0003917; GO:0003697,GO:0003916; GO:0003677,GO:0003917; GO:0003677,GO:0003916; GO:0003697,0.7458,0.7837,0.819,0.8569,0.7458,5,0.7902,0.7598,yes
UBA7_MOUSE,Q9DBK7,ESM2Text,Eukaryota,977,"E1-activating enzyme that catalyzes the covalent conjugation of the ubiquitin-like protein product of ISG15 to additional interferons stimulated proteins (ISGs) as well as other cellular proteins such as P53 in a process termed protein ISGylation. Plays an essential role in antiviral immunity together with ISG15 by restricting the replication of many viruses including rabies virus, influenza virus, sindbis virus or rotavirus.","Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Specific for ubiquitin-E1.",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0019782; GO:0004842,GO:0004839; GO:0005524,GO:0004839,GO:0004839; GO:0005524,GO:0004839; GO:0005524,GO:0004839; GO:0005524,0.4996,0.6455,0.4996,0.4996,0.4996,5,0.5288,0.7832,yes
UBA7_MOUSE,Q9DBK7,Prot2Text,Eukaryota,977,"E1-activating enzyme that catalyzes the covalent conjugation of the ubiquitin-like protein product of ISG15 to additional interferons stimulated proteins (ISGs) as well as other cellular proteins such as P53 in a process termed protein ISGylation. Plays an essential role in antiviral immunity together with ISG15 by restricting the replication of many viruses including rabies virus, influenza virus, sindbis virus or rotavirus.","Activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Catalyzes the ISGylation of influenza A virus NS1 protein.",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0019782; GO:0004842,GO:0004839,GO:0004839,GO:0004839,GO:0004839,GO:0004839,0.6455,0.6455,0.6455,0.6455,0.6455,5,0.6455,0.7832,yes
UBA7_MOUSE,Q9DBK7,ProtT3,Eukaryota,977,"E1-activating enzyme that catalyzes the covalent conjugation of the ubiquitin-like protein product of ISG15 to additional interferons stimulated proteins (ISGs) as well as other cellular proteins such as P53 in a process termed protein ISGylation. Plays an essential role in antiviral immunity together with ISG15 by restricting the replication of many viruses including rabies virus, influenza virus, sindbis virus or rotavirus.",Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Belongs to the ubiquitin-conjugating enzyme family,No,Vague,Vague,Vague,No,not-Yes,GO:0019782; GO:0004842,GO:0061631,GO:0061631,GO:0061631,GO:0061631,GO:0061631,0.6424,0.6424,0.6424,0.6424,0.6424,5,0.6424,0.7832,yes
UBA7_MOUSE,Q9DBK7,ProtTale,Eukaryota,977,"E1-activating enzyme that catalyzes the covalent conjugation of the ubiquitin-like protein product of ISG15 to additional interferons stimulated proteins (ISGs) as well as other cellular proteins such as P53 in a process termed protein ISGylation. Plays an essential role in antiviral immunity together with ISG15 by restricting the replication of many viruses including rabies virus, influenza virus, sindbis virus or rotavirus.","E1-like enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy and pexophagy. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Responsible for the E1-like reaction of the ATG12-ATG5 conjugation system that forms the ATG10-ATG12 complex: the ATG12-ATG5 conjugate functions as an E1-like enzyme that mediates the ATP-dependent transfer of ATG10",Maybe,No,No,Maybe,Maybe,not-Yes,GO:0019782; GO:0004842,GO:0019783; GO:0005524,GO:0005524,GO:0005524,GO:0005524,GO:0016887,0.2776,0.0602,0.0602,0.0602,0.2505,5,0.1417,0.7832,yes
UBA7_MOUSE,Q9DBK7,Protein2Text,Eukaryota,977,"E1-activating enzyme that catalyzes the covalent conjugation of the ubiquitin-like protein product of ISG15 to additional interferons stimulated proteins (ISGs) as well as other cellular proteins such as P53 in a process termed protein ISGylation. Plays an essential role in antiviral immunity together with ISG15 by restricting the replication of many viruses including rabies virus, influenza virus, sindbis virus or rotavirus.","The molecular function of this protein is to catalyze the E2 reaction in the ubiquitination pathway, specifically by mediating the transfer of ubiquitin from an E1 enzyme to an E3 enzyme.",No,No,Maybe,No,No,not-Yes,GO:0019782; GO:0004842,GO:0061631,GO:0061631,GO:0061631,GO:0061631,GO:0061631,0.6424,0.6424,0.6424,0.6424,0.6424,5,0.6424,0.7832,yes
UBA7_MOUSE,Q9DBK7,Reference,Eukaryota,977,"E1-activating enzyme that catalyzes the covalent conjugation of the ubiquitin-like protein product of ISG15 to additional interferons stimulated proteins (ISGs) as well as other cellular proteins such as P53 in a process termed protein ISGylation. Plays an essential role in antiviral immunity together with ISG15 by restricting the replication of many viruses including rabies virus, influenza virus, sindbis virus or rotavirus.","E1-activating enzyme that catalyzes the covalent conjugation of the ubiquitin-like protein product of ISG15 to additional interferons stimulated proteins (ISGs) as well as other cellular proteins such as P53 in a process termed protein ISGylation. Plays an essential role in antiviral immunity together with ISG15 by restricting the replication of many viruses including rabies virus, influenza virus, sindbis virus or rotavirus.",,,,,,,GO:0019782; GO:0004842,GO:0004839; GO:0005524,GO:0004839,GO:0004839,GO:0061659,,0.4996,0.6455,0.6455,0.6369,,4,0.6069,0.7832,yes
ENG1_HALH5,Q9KG76,ESM2Text,Bacteria,1020,"Cleaves internal linkages in 1,3-beta-glucan. May contribute to plant biomass degradation.",Has a role in muropeptidase-mediated cell-cell adhesion during germination and tube growth.,No,No,Maybe,Maybe,No,not-Yes,GO:0030246; GO:0052861; GO:0042973,,,,,,,,,,,0,,0.2667,no
ENG1_HALH5,Q9KG76,Prot2Text,Bacteria,1020,"Cleaves internal linkages in 1,3-beta-glucan. May contribute to plant biomass degradation.","Hydrolyzes 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues. Involved in the degradation of hemicellulose.",No,No,Maybe,Maybe,No,not-Yes,GO:0030246; GO:0052861; GO:0042973,GO:0016162,GO:0016798,GO:0016798,GO:0016798,GO:0033950,0.4967,0.5229,0.5229,0.5229,0.5281,5,0.5187,0.2667,no
ENG1_HALH5,Q9KG76,ProtT3,Bacteria,1020,"Cleaves internal linkages in 1,3-beta-glucan. May contribute to plant biomass degradation.",Belongs to the glycosyl hydrolase 9 (cellulase E) family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0030246; GO:0052861; GO:0042973,GO:0008810,GO:0008810,GO:0008810,GO:0008810,GO:0008810,0.4967,0.4967,0.4967,0.4967,0.4967,5,0.4967,0.2667,no
ENG1_HALH5,Q9KG76,ProtTale,Bacteria,1020,"Cleaves internal linkages in 1,3-beta-glucan. May contribute to plant biomass degradation.","Cleaves internal linkages in 1,3-beta-glucan.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0030246; GO:0052861; GO:0042973,GO:0042973,GO:0004553,GO:0016798,GO:0004553,GO:0004553,0.6515,0.5911,0.5229,0.5911,0.5911,5,0.5895,0.2667,no
ENG1_HALH5,Q9KG76,Protein2Text,Bacteria,1020,"Cleaves internal linkages in 1,3-beta-glucan. May contribute to plant biomass degradation.","This protein is a type of enzyme called a hydrolase, specifically a glucosidase, which is involved in breaking down complex molecules such as starches into simpler sugars.",Vague,No,No,Vague,Vague,not-Yes,GO:0030246; GO:0052861; GO:0042973,GO:0004553,GO:0004553,GO:0004553,GO:0004553,GO:0004553,0.5911,0.5911,0.5911,0.5911,0.5911,5,0.5911,0.2667,no
ENG1_HALH5,Q9KG76,Reference,Bacteria,1020,"Cleaves internal linkages in 1,3-beta-glucan. May contribute to plant biomass degradation.","Cleaves internal linkages in 1,3-beta-glucan. May contribute to plant biomass degradation.",,,,,,,GO:0030246; GO:0052861; GO:0042973,GO:0052861,GO:0042973,GO:0042973,GO:0042973,GO:0042973,0.6546,0.6515,0.6515,0.6515,0.6515,5,0.6521,0.2667,no
SHYC_VIBCH,Q9KU93,ESM2Text,Bacteria,433,Cell wall peptidoglycan (PG) DD-endopeptidase. Hydrolyzes peptide cross-links which covalently connect adjacent PG strands probably to allow insertion of new glycans and thus cell wall expansion. Degrades purified whole PG sacculi in vitro.,Vacuolar glycosidase that acts as a specific endoprotease for amidase. Required for spore cortex hydrolysis during cell division. Also has a role in autolysis.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0004222,,GO:0004553,GO:0004175,,,,0.2589,0.5653,,,2,0.4121,0.5515,yes
SHYC_VIBCH,Q9KU93,Prot2Text,Bacteria,433,Cell wall peptidoglycan (PG) DD-endopeptidase. Hydrolyzes peptide cross-links which covalently connect adjacent PG strands probably to allow insertion of new glycans and thus cell wall expansion. Degrades purified whole PG sacculi in vitro.,"Lyses staphylococcal cells by hydrolyzing the polyglycine interpeptide bridges of the peptidoglycan. Thus, enables bacterial growth inside the host, where it is indirectly involved in the induction of maturation, by stimulating activity of several host innate immune responses.",Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0046872; GO:0004222,GO:0004222,GO:0008233,GO:0004175,GO:0004175,GO:0008745,0.6918,0.5063,0.5653,0.5653,0.2286,5,0.5115,0.5515,yes
SHYC_VIBCH,Q9KU93,ProtT3,Bacteria,433,Cell wall peptidoglycan (PG) DD-endopeptidase. Hydrolyzes peptide cross-links which covalently connect adjacent PG strands probably to allow insertion of new glycans and thus cell wall expansion. Degrades purified whole PG sacculi in vitro.,Cell membrane; Lipid-anchor. Belongs to the peptidase M20B family,Vague,Vague,Vague,No,Vague,not-Yes,GO:0046872; GO:0004222,GO:0008233,GO:0008237,GO:0008237,GO:0008237,GO:0008233,0.5063,0.5653,0.5653,0.5653,0.5063,5,0.5417,0.5515,yes
SHYC_VIBCH,Q9KU93,ProtTale,Bacteria,433,Cell wall peptidoglycan (PG) DD-endopeptidase. Hydrolyzes peptide cross-links which covalently connect adjacent PG strands probably to allow insertion of new glycans and thus cell wall expansion. Degrades purified whole PG sacculi in vitro.,"Cleaves both, N- and C-terminal D-alanyl-meso- 2,3- diaminopimelic acid (D-ala-D-DAP) peptide bonds in peptidoglycan.",Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0046872; GO:0004222,GO:0008233,GO:0008233,GO:0008233,GO:0008233,GO:0008233,0.5063,0.5063,0.5063,0.5063,0.5063,5,0.5063,0.5515,yes
SHYC_VIBCH,Q9KU93,Protein2Text,Bacteria,433,Cell wall peptidoglycan (PG) DD-endopeptidase. Hydrolyzes peptide cross-links which covalently connect adjacent PG strands probably to allow insertion of new glycans and thus cell wall expansion. Degrades purified whole PG sacculi in vitro.,The molecular function of this protein is an enzyme that removes the C-terminal L-arginine residue from the translationally inactive leader peptide of the enzyme involved in the biosynthesis of the antibiotic mupirocin.,No,No,No,No,No,not-Yes,GO:0046872; GO:0004222,,,,,,,,,,,0,,0.5515,yes
SHYC_VIBCH,Q9KU93,Reference,Bacteria,433,Cell wall peptidoglycan (PG) DD-endopeptidase. Hydrolyzes peptide cross-links which covalently connect adjacent PG strands probably to allow insertion of new glycans and thus cell wall expansion. Degrades purified whole PG sacculi in vitro.,Cell wall peptidoglycan (PG) DD-endopeptidase. Hydrolyzes peptide cross-links which covalently connect adjacent PG strands probably to allow insertion of new glycans and thus cell wall expansion. Degrades purified whole PG sacculi in vitro.,,,,,,,GO:0046872; GO:0004222,GO:0008233,GO:0008233,GO:0004175,GO:0004175,GO:0004175,0.5063,0.5063,0.5653,0.5653,0.5653,5,0.5417,0.5515,yes
CRLS1_STRCO,Q9KZP3,ESM2Text,Bacteria,215,Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG).,This protein catalyzes the committed step to the synthesis of the acidic phospholipids.,Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0043337; GO:0008444,,,,,,,,,,,0,,0.2942,no
CRLS1_STRCO,Q9KZP3,Prot2Text,Bacteria,215,Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG).,This protein catalyzes the committed step to the synthesis of the acidic phospholipids.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0043337; GO:0008444,,,,,,,,,,,0,,0.2942,no
CRLS1_STRCO,Q9KZP3,ProtT3,Bacteria,215,Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG).,This protein catalyzes the committed step to the synthesis of the acidic phospholipids. Cell inner membrane; Multi-pass membrane protein. Belongs to the CDP-alcohol phosphatidyltransferase class-I family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0043337; GO:0008444,GO:0016780,GO:0008444,GO:0016780,GO:0016780,GO:0016780,0.7539,0.8482,0.7539,0.7539,0.7539,5,0.7728,0.2942,no
CRLS1_STRCO,Q9KZP3,ProtTale,Bacteria,215,Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG).,"Catalyzes the transfer of phosphatidylglycerol (PG), a major phospholipid in the inner membrane, to the 3'-hydroxyl group of nucleoside triphosphates.",No,No,No,No,No,not-Yes,GO:0043337; GO:0008444,GO:0016740,GO:0016772,GO:0016772,GO:0016740,GO:0016740,0.5381,0.6466,0.6466,0.5381,0.5381,5,0.5815,0.2942,no
CRLS1_STRCO,Q9KZP3,Protein2Text,Bacteria,215,Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG).,The molecular function of this protein is a transporter.,No,No,No,No,No,not-Yes,GO:0043337; GO:0008444,,GO:0005215,GO:0005215,GO:0005215,,,0.1847,0.1847,0.1847,,3,0.1847,0.2942,no
CRLS1_STRCO,Q9KZP3,Reference,Bacteria,215,Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG).,Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG).,,,,,,,GO:0043337; GO:0008444,GO:0008808,GO:0008808,GO:0008808,GO:0008808,GO:0008808,0.6794,0.6794,0.6794,0.6794,0.6794,5,0.6794,0.2942,no
PSUG_DICD3,Q9L393,ESM2Text,Bacteria,316,"Catalyzes the reversible cleavage of pseudouridine 5'- phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway. Part of an operon that could be involved in the biosynthesis of the blue pigment indigoidine, which is implicated in pathogenicity and protection from oxidative stress.","Catalyzes the reversible cleavage of pseudouridine 5'-phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016798; GO:0046872; GO:0004730,GO:0016799,GO:0016799,GO:0016787,GO:0016799,GO:0016798,0.5058,0.5058,0.5355,0.5058,0.6027,5,0.5311,0.799,yes
PSUG_DICD3,Q9L393,Prot2Text,Bacteria,316,"Catalyzes the reversible cleavage of pseudouridine 5'- phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway. Part of an operon that could be involved in the biosynthesis of the blue pigment indigoidine, which is implicated in pathogenicity and protection from oxidative stress.","Catalyzes the reversible cleavage of pseudouridine 5'-phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016798; GO:0046872; GO:0004730,GO:0016798,,GO:0016798,GO:0016798,GO:0050312,0.6027,,0.6027,0.6027,0.0,4,0.452,0.799,yes
PSUG_DICD3,Q9L393,ProtT3,Bacteria,316,"Catalyzes the reversible cleavage of pseudouridine 5'- phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway. Part of an operon that could be involved in the biosynthesis of the blue pigment indigoidine, which is implicated in pathogenicity and protection from oxidative stress.","Catalyzes the reversible cleavage of pseudouridine 5'- phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway. Belongs to the pseudouridine-5'-phosphate glycosidase family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016798; GO:0046872; GO:0004730,GO:0016799,GO:0016798,GO:0016799,GO:0016798,GO:0016799,0.5058,0.6027,0.5058,0.6027,0.5058,5,0.5446,0.799,yes
PSUG_DICD3,Q9L393,ProtTale,Bacteria,316,"Catalyzes the reversible cleavage of pseudouridine 5'- phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway. Part of an operon that could be involved in the biosynthesis of the blue pigment indigoidine, which is implicated in pathogenicity and protection from oxidative stress.","Catalyzes the reversible cleavage of pseudouridine 5'- phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016798; GO:0046872; GO:0004730,GO:0016799,GO:0016829,GO:0016798,GO:0016799,GO:0016799,0.5058,0.4606,0.6027,0.5058,0.5058,5,0.5161,0.799,yes
PSUG_DICD3,Q9L393,Protein2Text,Bacteria,316,"Catalyzes the reversible cleavage of pseudouridine 5'- phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway. Part of an operon that could be involved in the biosynthesis of the blue pigment indigoidine, which is implicated in pathogenicity and protection from oxidative stress.","The molecular function of this protein is a cyanide hydratase, which catalyzes the hydration of cyanide to formic acid, allowing the bacteria to grow on cyanide as a carbon source.",No,No,No,No,No,not-Yes,GO:0016798; GO:0046872; GO:0004730,GO:0018766,GO:0019148,GO:0047427,GO:0019148,,0.3132,0.3076,0.2765,0.3076,,4,0.3012,0.799,yes
PSUG_DICD3,Q9L393,Reference,Bacteria,316,"Catalyzes the reversible cleavage of pseudouridine 5'- phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway. Part of an operon that could be involved in the biosynthesis of the blue pigment indigoidine, which is implicated in pathogenicity and protection from oxidative stress.","Catalyzes the reversible cleavage of pseudouridine 5'- phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway. Part of an operon that could be involved in the biosynthesis of the blue pigment indigoidine, which is implicated in pathogenicity and protection from oxidative stress.",,,,,,,GO:0016798; GO:0046872; GO:0004730,GO:0016829,GO:0016799,GO:0016829,GO:0016829,GO:0016829,0.4606,0.5058,0.4606,0.4606,0.4606,5,0.4696,0.799,yes
FAD1_ARATH,Q9LZE4,ESM2Text,Eukaryota,497,Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. Does not exhibit FAD diphosphatase activity but may stably bind FAD non- catalytically.,Adenosyl-L-methionine (AdoMet) factor involved in the biosynthesis of molybdopterin. May act by mediating the ATP-dependent formation of adenosyl-L-methionine (AdoMet) cofactor.,No,No,No,No,No,not-Yes,GO:0005524; GO:0003919,,,,,,,,,,,0,,0.1966,no
FAD1_ARATH,Q9LZE4,Prot2Text,Eukaryota,497,Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. Does not exhibit FAD diphosphatase activity but may stably bind FAD non- catalytically.,Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0003919,GO:0003919,GO:0003919,GO:0003919,GO:0003919,GO:0003919,0.6832,0.6832,0.6832,0.6832,0.6832,5,0.6832,0.1966,no
FAD1_ARATH,Q9LZE4,ProtT3,Eukaryota,497,Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. Does not exhibit FAD diphosphatase activity but may stably bind FAD non- catalytically.,"Catalyzes the ATP-dependent 2-thiolation of uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln), leading to the formation of s(2)U34, the first step of tRNA-mnm(5)s(2)U34 synthesis. Sulfur is provided by IscS, via a sulfur-relay system. Binds ATP and its substrate tRNAs. Cytoplasm. In the C-terminal section; belongs to the",No,No,No,No,No,not-Yes,GO:0005524; GO:0003919,GO:0016783; GO:0005524,GO:0005524; GO:0016783,GO:0005524,GO:0005524,GO:0005524; GO:0016783,0.6751,0.6751,0.6832,0.6832,0.6751,5,0.6783,0.1966,no
FAD1_ARATH,Q9LZE4,ProtTale,Eukaryota,497,Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. Does not exhibit FAD diphosphatase activity but may stably bind FAD non- catalytically.,Catalyzes the hydrolysis of 6-aminopurine riboside 5'-phosphate (6-NPRP) to yield 6- aminopurine 5'-phosphate and ribose 1-phosphate.,No,No,No,No,No,not-Yes,GO:0005524; GO:0003919,GO:0016799,GO:0016787,GO:0016787,GO:0016787,GO:0004731,0.1589,0.2408,0.2408,0.2408,0.2147,5,0.2192,0.1966,no
FAD1_ARATH,Q9LZE4,Protein2Text,Eukaryota,497,Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. Does not exhibit FAD diphosphatase activity but may stably bind FAD non- catalytically.,"The molecular function of the protein is an adenosine kinase, specifically an adenosine kinase 2 (ADK2).",No,No,No,No,No,not-Yes,GO:0005524; GO:0003919,GO:0004001,GO:0004001,GO:0004001,GO:0004001,GO:0004001,0.2378,0.2378,0.2378,0.2378,0.2378,5,0.2378,0.1966,no
FAD1_ARATH,Q9LZE4,Reference,Eukaryota,497,Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. Does not exhibit FAD diphosphatase activity but may stably bind FAD non- catalytically.,Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. Does not exhibit FAD diphosphatase activity but may stably bind FAD non- catalytically.,,,,,,,GO:0005524; GO:0003919,GO:0003919,GO:0003919,GO:0003919,GO:0003919,GO:0003919,0.6832,0.6832,0.6832,0.6832,0.6832,5,0.6832,0.1966,no
FTCDL_ARATH,Q9SKT4,ESM2Text,Eukaryota,297,"Involved in the regulation of root growth. May regulate sorting and/or transportation of trans-Golgi network (TGN) vesicles in root cap peripheral cells, thus influencing the extracellular secretion of mucilage components in the root cap.","Catalyzes the addition of (2R,3S)-3-methylaspartate-D-ribose 1-phosphate to cobalt-precorrin-8 to yield cobalt-precorrin-7A.",No,No,No,No,No,not-Yes,GO:0005542; GO:0030409,,,GO:0016740,GO:0016740,GO:0016740,,,0.4388,0.4388,0.4388,3,0.4388,0.2945,no
FTCDL_ARATH,Q9SKT4,Prot2Text,Eukaryota,297,"Involved in the regulation of root growth. May regulate sorting and/or transportation of trans-Golgi network (TGN) vesicles in root cap peripheral cells, thus influencing the extracellular secretion of mucilage components in the root cap.","Non-catalytic component of the proteasome which degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.",No,No,No,No,No,not-Yes,GO:0005542; GO:0030409,,,,,,,,,,,0,,0.2945,no
FTCDL_ARATH,Q9SKT4,ProtT3,Eukaryota,297,"Involved in the regulation of root growth. May regulate sorting and/or transportation of trans-Golgi network (TGN) vesicles in root cap peripheral cells, thus influencing the extracellular secretion of mucilage components in the root cap.",Catalyzes the transfer of a formyl group to tetrahydrofolate (THF) to produce 5- formyltetrahydrofolate (5-formyl-THF) (By similarity). Catalyzes the transfer of a formyl group to tetrahydrofolate (THF) to produce 5-formyltetrahydrofolate (5-formyl-THF) (By similarity). Cytoplasm. Belongs to the formyltetrahydrofolate transferase family. Belongs to the formyltetrahydrofolate transferase,No,No,No,No,No,not-Yes,GO:0005542; GO:0030409,GO:0004329,GO:0004329,GO:0004329,GO:0004329; GO:0005524,GO:0004329; GO:0005524,0.1844,0.1844,0.1844,0.3182,0.3182,5,0.2379,0.2945,no
FTCDL_ARATH,Q9SKT4,ProtTale,Eukaryota,297,"Involved in the regulation of root growth. May regulate sorting and/or transportation of trans-Golgi network (TGN) vesicles in root cap peripheral cells, thus influencing the extracellular secretion of mucilage components in the root cap.",Catalyzes the transfer of an amino acid from one aminoacyl-tRNA to another in the presence of ATP.,No,No,No,No,No,not-Yes,GO:0005542; GO:0030409,GO:0016755,GO:0016875,GO:0016747,GO:0016755,,0.2933,0.2214,0.2933,0.2933,,4,0.2753,0.2945,no
FTCDL_ARATH,Q9SKT4,Protein2Text,Eukaryota,297,"Involved in the regulation of root growth. May regulate sorting and/or transportation of trans-Golgi network (TGN) vesicles in root cap peripheral cells, thus influencing the extracellular secretion of mucilage components in the root cap.","The molecular function of this protein is not specified in the provided information. However, it can be inferred that this protein is involved in the synthesis of a molecule, as it is a part of the biosynthesis pathway. The exact molecular function of this protein would require further information about the specific biochemical reaction it is involved in.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005542; GO:0030409,,,,,,,,,,,0,,0.2945,no
FTCDL_ARATH,Q9SKT4,Reference,Eukaryota,297,"Involved in the regulation of root growth. May regulate sorting and/or transportation of trans-Golgi network (TGN) vesicles in root cap peripheral cells, thus influencing the extracellular secretion of mucilage components in the root cap.","Involved in the regulation of root growth. May regulate sorting and/or transportation of trans-Golgi network (TGN) vesicles in root cap peripheral cells, thus influencing the extracellular secretion of mucilage components in the root cap.",,,,,,,GO:0005542; GO:0030409,,,,,,,,,,,0,,0.2945,no
ALG9_DROME,Q9VBV8,ESM2Text,Eukaryota,623,"Probable alpha-1,2-mannosyltransferase involved in the N- glycosylation pathway. Probably involved in glycosylation of the TNF receptor grnd, regulating its ligand affinity. Required for normal epithelial growth and architecture. Suppressor of JNK-dependent intestinal stem cell proliferation.",Catalyzes the transfer of mannose from Dol-P-Man to lipid-linked oligosaccharides.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0000026; GO:0052926; GO:0052918,GO:0000030,GO:0000030,GO:0016757,GO:0000030,GO:0000030,0.7843,0.7843,0.5862,0.7843,0.7843,5,0.7447,0.6814,yes
ALG9_DROME,Q9VBV8,Prot2Text,Eukaryota,623,"Probable alpha-1,2-mannosyltransferase involved in the N- glycosylation pathway. Probably involved in glycosylation of the TNF receptor grnd, regulating its ligand affinity. Required for normal epithelial growth and architecture. Suppressor of JNK-dependent intestinal stem cell proliferation.",Catalyzes the transfer of mannose from Dol-P-Man to lipid-linked oligosaccharides.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0000026; GO:0052926; GO:0052918,GO:0000030,GO:0000030,GO:0000030,GO:0000030,GO:0000030,0.7843,0.7843,0.7843,0.7843,0.7843,5,0.7843,0.6814,yes
ALG9_DROME,Q9VBV8,ProtT3,Eukaryota,623,"Probable alpha-1,2-mannosyltransferase involved in the N- glycosylation pathway. Probably involved in glycosylation of the TNF receptor grnd, regulating its ligand affinity. Required for normal epithelial growth and architecture. Suppressor of JNK-dependent intestinal stem cell proliferation.",Catalyzes the transfer of mannose from Dol-P-Man to lipid-linked oligosaccharides. Endoplasmic reticulum membrane; Multi-pass membrane protein. Belongs to the glycosyltransferase 22 family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0000026; GO:0052926; GO:0052918,GO:0016757,GO:0000030,GO:0016757,GO:0000030,GO:0016757,0.5862,0.7843,0.5862,0.7843,0.5862,5,0.6654,0.6814,yes
ALG9_DROME,Q9VBV8,ProtTale,Eukaryota,623,"Probable alpha-1,2-mannosyltransferase involved in the N- glycosylation pathway. Probably involved in glycosylation of the TNF receptor grnd, regulating its ligand affinity. Required for normal epithelial growth and architecture. Suppressor of JNK-dependent intestinal stem cell proliferation.","Mannosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the eighth mannose residue in an",Yes,Yes,Maybe,Yes,Yes,Yes,GO:0000026; GO:0052926; GO:0052918,GO:0000030,GO:0016758,GO:0000030,GO:0000030,GO:0000030,0.7843,0.6823,0.7843,0.7843,0.7843,5,0.7639,0.6814,yes
ALG9_DROME,Q9VBV8,Protein2Text,Eukaryota,623,"Probable alpha-1,2-mannosyltransferase involved in the N- glycosylation pathway. Probably involved in glycosylation of the TNF receptor grnd, regulating its ligand affinity. Required for normal epithelial growth and architecture. Suppressor of JNK-dependent intestinal stem cell proliferation.","This protein is involved in transferring a mannose residue from a donor molecule to a specific location on another molecule, specifically Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase activity.",Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0000026; GO:0052926; GO:0052918,GO:0004169,GO:0000030,GO:0004578,GO:0000030,GO:0000033,0.6348,0.7843,0.6269,0.7843,0.6715,5,0.7004,0.6814,yes
ALG9_DROME,Q9VBV8,Reference,Eukaryota,623,"Probable alpha-1,2-mannosyltransferase involved in the N- glycosylation pathway. Probably involved in glycosylation of the TNF receptor grnd, regulating its ligand affinity. Required for normal epithelial growth and architecture. Suppressor of JNK-dependent intestinal stem cell proliferation.","Probable alpha-1,2-mannosyltransferase involved in the N- glycosylation pathway. Probably involved in glycosylation of the TNF receptor grnd, regulating its ligand affinity. Required for normal epithelial growth and architecture. Suppressor of JNK-dependent intestinal stem cell proliferation.",,,,,,,GO:0000026; GO:0052926; GO:0052918,GO:0000030,GO:0000030,GO:0000030,GO:0000030,GO:0000030,0.7843,0.7843,0.7843,0.7843,0.7843,5,0.7843,0.6814,yes
PHLP3_DROME,Q9VGV8,ESM2Text,Eukaryota,216,Has redox activity with thioredoxin. Required for male fertility and maturation of sperm past the canoe stage during spermiogenesis.,"Significantly diminishes the chaperonin TCP1 complex ATPase activity, thus negatively impacts protein folding, including that of actin or tubulin.",No,No,No,No,No,not-Yes,GO:0044183; GO:0047134; GO:0004791,,,,,,,,,,,0,,0.6081,yes
PHLP3_DROME,Q9VGV8,Prot2Text,Eukaryota,216,Has redox activity with thioredoxin. Required for male fertility and maturation of sperm past the canoe stage during spermiogenesis.,"Significantly diminishes the chaperonin TCP1 complex ATPase activity, thus negatively impacts protein folding, including that of actin or tubulin.",No,No,No,No,No,not-Yes,GO:0044183; GO:0047134; GO:0004791,,,,,,,,,,,0,,0.6081,yes
PHLP3_DROME,Q9VGV8,ProtT3,Eukaryota,216,Has redox activity with thioredoxin. Required for male fertility and maturation of sperm past the canoe stage during spermiogenesis.,May act as a chaperone. Cytoplasm Nucleus. Belongs to the chaperonin (HSP60) family,No,Vague,Vague,Vague,No,not-Yes,GO:0044183; GO:0047134; GO:0004791,GO:0051082,GO:0051082; GO:0005524,GO:0051082; GO:0005524,GO:0051082; GO:0005524,GO:0051082,0.1932,0.1758,0.1758,0.1758,0.1932,5,0.1828,0.6081,yes
PHLP3_DROME,Q9VGV8,ProtTale,Eukaryota,216,Has redox activity with thioredoxin. Required for male fertility and maturation of sperm past the canoe stage during spermiogenesis.,Inhibitor of protein phosphatase 1 (PP1).,No,No,No,No,No,not-Yes,GO:0044183; GO:0047134; GO:0004791,GO:0004864,,,,GO:0004864,0.111,,,,0.111,2,0.111,0.6081,yes
PHLP3_DROME,Q9VGV8,Protein2Text,Eukaryota,216,Has redox activity with thioredoxin. Required for male fertility and maturation of sperm past the canoe stage during spermiogenesis.,"The molecular function of this protein is not specified in the provided information. However, based on the fact that it is a protein, it is likely to be involved in various cellular processes, such as binding to other molecules, catalyzing chemical reactions, or regulating gene expression. If you provide more context or information, I may be able to provide a more specific answer.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0044183; GO:0047134; GO:0004791,,,,,,,,,,,0,,0.6081,yes
PHLP3_DROME,Q9VGV8,Reference,Eukaryota,216,Has redox activity with thioredoxin. Required for male fertility and maturation of sperm past the canoe stage during spermiogenesis.,Has redox activity with thioredoxin. Required for male fertility and maturation of sperm past the canoe stage during spermiogenesis.,,,,,,,GO:0044183; GO:0047134; GO:0004791,GO:0015035,GO:0015036,GO:0016491,GO:0016491,GO:0015035,0.6473,0.5274,0.4203,0.4203,0.6473,5,0.5325,0.6081,yes
CDC7B_DROME,Q9VJ90,ESM2Text,Eukaryota,665,Probable serine/threonine protein kinase that forms a complex with the N-terminal peptide of the chiffon protein and may be involved in regulating meiotic processes in the male testis.,"Serine/threonine-protein kinase required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. Involved in the checkpoint response to DNA damage checkpoint intermediates. Phosphorylates and activates the PAN1 kinase, a component of the SLA1-SLA4 complex, which phosphorylates and inactivates the CDC25 kinase, thereby blocking the inactivation of the polymerase filament. Phosphorylates the PAN1-SLA4 complex component LMF2. Phosphorylates the C-terminal part of STK3 and STK26 component. Required for the regulation of actin cytoskeleton organization and microtubule organization.",Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0005524; GO:0004674,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,1.0,0.6847,1.0,1.0,1.0,5,0.9369,0.7685,yes
CDC7B_DROME,Q9VJ90,Prot2Text,Eukaryota,665,Probable serine/threonine protein kinase that forms a complex with the N-terminal peptide of the chiffon protein and may be involved in regulating meiotic processes in the male testis.,"Serine/threonine-protein kinase involved in the initiation of DNA synthesis and the maintenance of genome stability. Has a role in the initiation of DNA synthesis during S phase: during the G1/S phase, it phosphorylates and activates TFIIH, leading to the formation of a DNA:RNA complex. Phosphorylates the elongation factor EEF2C, which promotes its interaction with DNA and the elongation factor EEF2C complex, during G1/S phase. Phosphorylates the elongation factor EEF2C at 'Ser-45'.",Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0005524; GO:0004674,GO:0004674,GO:0004674,GO:0004674; GO:0005524,GO:0004674,GO:0004674,0.6847,0.6847,1.0,0.6847,0.6847,5,0.7478,0.7685,yes
CDC7B_DROME,Q9VJ90,ProtT3,Eukaryota,665,Probable serine/threonine protein kinase that forms a complex with the N-terminal peptide of the chiffon protein and may be involved in regulating meiotic processes in the male testis.,"Serine/threonine-protein kinase that acts as a component of the mitotic exit network (MEN), a signaling pathway that coordinates cell cycle exit with the onset of cytokinesis. Phosphorylates the transcription factor cdc15-1, which in turn activates the transcription factor cdc14-1, which in turn activates the transcription factor cdc15-1, which in turn activates the transcription factor cdc14-1, which in turn activates the transcription factor cdc15-1, which in turn activates the transcription factor cdc14-1, which in turn activates the",Yes,No,Maybe,Maybe,Yes,not-Yes,GO:0005524; GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,1.0,1.0,1.0,1.0,1.0,5,1.0,0.7685,yes
CDC7B_DROME,Q9VJ90,ProtTale,Eukaryota,665,Probable serine/threonine protein kinase that forms a complex with the N-terminal peptide of the chiffon protein and may be involved in regulating meiotic processes in the male testis.,Serine/threonine-protein kinase involved in cytokinesis.,Yes,No,Maybe,No,Yes,not-Yes,GO:0005524; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674; GO:0005524,GO:0004674,0.6847,0.6847,0.6847,1.0,0.6847,5,0.7478,0.7685,yes
CDC7B_DROME,Q9VJ90,Protein2Text,Eukaryota,665,Probable serine/threonine protein kinase that forms a complex with the N-terminal peptide of the chiffon protein and may be involved in regulating meiotic processes in the male testis.,The molecular function of this protein is as a serine/threonine-protein kinase.,Yes,Maybe,Maybe,Vague,Yes,not-Yes,GO:0005524; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.6847,0.6847,0.6847,0.6847,0.6847,5,0.6847,0.7685,yes
CDC7B_DROME,Q9VJ90,Reference,Eukaryota,665,Probable serine/threonine protein kinase that forms a complex with the N-terminal peptide of the chiffon protein and may be involved in regulating meiotic processes in the male testis.,Probable serine/threonine protein kinase that forms a complex with the N-terminal peptide of the chiffon protein and may be involved in regulating meiotic processes in the male testis.,,,,,,,GO:0005524; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.6847,0.6847,0.6847,0.6847,0.6847,5,0.6847,0.7685,yes
UBP64_DROME,Q9W4C3,ESM2Text,Eukaryota,1126,Involved in the regulation of DNA damage repair.,"Deubiquitinating enzyme that deubiquitinates monoubiquitinated FANCD2. Also deubiquitinates monoubiquitinated FANCD2 but does not deubiquitinate monoubiquitinated FANCD2. Deubiquitinates HAS2. Has a dual role in the regulation of histone H2A monoubiquitination (H2AK). Specifically deubiquitinates monoubiquitinated H2AK at 'Lys-119' (H2AK119ub1). Acts as a regulator of autophagy by mediating deubiquitination of BECN1, a regulator of autophagy. Deubiquitinates also RNF212. Acts as a regulator of mitochondrial biogenesis by mediating deubiquitination of MTOR and promoting MTOR-mediated ubiquitination. Prefers monoubiquitinated substrates that are mono- and polyubiquitin with a free N-terminus. Does not deubiquitinate monoubiquitinated FANCD2.",Maybe,No,No,No,Maybe,not-Yes,GO:0004843; GO:0008270,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,0.6849,0.6849,0.6849,0.6849,0.6849,5,0.6849,0.5569,yes
UBP64_DROME,Q9W4C3,Prot2Text,Eukaryota,1126,Involved in the regulation of DNA damage repair.,Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. Involved in seed and embryo development.,Maybe,No,No,No,Maybe,not-Yes,GO:0004843; GO:0008270,GO:0004843,GO:0004843,GO:0036459,GO:0004843,GO:0004843,0.6849,0.6849,0.6849,0.6849,0.6849,5,0.6849,0.5569,yes
UBP64_DROME,Q9W4C3,ProtT3,Eukaryota,1126,Involved in the regulation of DNA damage repair.,"Catalytic component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. Belongs to the peptidase C19 family",No,No,No,No,No,not-Yes,GO:0004843; GO:0008270,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,0.6849,0.6849,0.6849,0.6849,0.6849,5,0.6849,0.5569,yes
UBP64_DROME,Q9W4C3,ProtTale,Eukaryota,1126,Involved in the regulation of DNA damage repair.,Responsible for the deubiquitination of histone H2A 'Lys-120'. May also be involved in the deubiquitination of non-histone proteins.,Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0004843; GO:0008270,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,0.6849,0.6849,0.6849,0.6849,0.6849,5,0.6849,0.5569,yes
UBP64_DROME,Q9W4C3,Protein2Text,Eukaryota,1126,Involved in the regulation of DNA damage repair.,The molecular function of this protein is deubiquitinase.,Maybe,No,Maybe,Vague,Maybe,not-Yes,GO:0004843; GO:0008270,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,0.6849,0.6849,0.6849,0.6849,0.6849,5,0.6849,0.5569,yes
UBP64_DROME,Q9W4C3,Reference,Eukaryota,1126,Involved in the regulation of DNA damage repair.,Involved in the regulation of DNA damage repair.,,,,,,,GO:0004843; GO:0008270,,,,,,,,,,,0,,0.5569,yes
RECG_THEMA,Q9WY48,ESM2Text,Bacteria,780,"Plays a critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has replication fork (Y-DNA) regression activity, unwinds stalled or blocked replication forks to make a HJ that can be resolved. Has a DNA unwinding activity characteristic of a DNA helicase with 3'-5' polarity. Might be a DNA translocase rather than a bona fide helicase (Probable).","Couples transcription and DNA repair by recognizing RNA polymerase (RNAP) stalled at DNA lesions. Mediates ATP-dependent release of RNAP and its truncated transcript from the DNA, and recruitment of nucleotide excision repair machinery to the damaged site.",Maybe,Maybe,No,No,Maybe,not-Yes,GO:0043138; GO:0005524; GO:0016887; GO:0003677; GO:0003678,GO:0016887; GO:0005524,GO:0008094,GO:0004386; GO:0005524,GO:0016887; GO:0005524,GO:0005524; GO:0016887; GO:0003677,0.663,0.4439,0.6953,0.663,0.8095,5,0.6549,0.7675,yes
RECG_THEMA,Q9WY48,Prot2Text,Bacteria,780,"Plays a critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has replication fork (Y-DNA) regression activity, unwinds stalled or blocked replication forks to make a HJ that can be resolved. Has a DNA unwinding activity characteristic of a DNA helicase with 3'-5' polarity. Might be a DNA translocase rather than a bona fide helicase (Probable).",Helicase. Has ATPase and DNA helicase activities. Involved in Okazaki fragments processing by catalyzing the first step of 5'-processing. Also has a role in chromosome segregation.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0043138; GO:0005524; GO:0016887; GO:0003677; GO:0003678,GO:0003678,GO:0003678,GO:0004003; GO:0005524,GO:0004003,GO:0004003,0.5554,0.5554,0.7629,0.5554,0.5554,5,0.5969,0.7675,yes
RECG_THEMA,Q9WY48,ProtT3,Bacteria,780,"Plays a critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has replication fork (Y-DNA) regression activity, unwinds stalled or blocked replication forks to make a HJ that can be resolved. Has a DNA unwinding activity characteristic of a DNA helicase with 3'-5' polarity. Might be a DNA translocase rather than a bona fide helicase (Probable).",Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y- DNA) (By similarity). Belongs to the helicase family. RecG subfamily,Yes,Yes,Yes,Yes,Yes,Yes,GO:0043138; GO:0005524; GO:0016887; GO:0003677; GO:0003678,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,GO:0003678; GO:0005524,0.7629,0.7629,0.7629,0.7629,0.7629,5,0.7629,0.7675,yes
RECG_THEMA,Q9WY48,ProtTale,Bacteria,780,"Plays a critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has replication fork (Y-DNA) regression activity, unwinds stalled or blocked replication forks to make a HJ that can be resolved. Has a DNA unwinding activity characteristic of a DNA helicase with 3'-5' polarity. Might be a DNA translocase rather than a bona fide helicase (Probable).","Plays a critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has replication fork regression activity, unwinds stalled or blocked replication forks to make a HJ that can be resolved. Has a DNA unwinding activity characteristic of a DNA helicase with 3'-5' polarity.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0043138; GO:0005524; GO:0016887; GO:0003677; GO:0003678,GO:0003678; GO:0005524,GO:0004386; GO:0005524; GO:0003677,GO:0004386; GO:0003677; GO:0005524,GO:0004386; GO:0005524; GO:0003677,GO:0003678,0.7629,0.8377,0.8377,0.8377,0.5554,5,0.7663,0.7675,yes
RECG_THEMA,Q9WY48,Protein2Text,Bacteria,780,"Plays a critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has replication fork (Y-DNA) regression activity, unwinds stalled or blocked replication forks to make a HJ that can be resolved. Has a DNA unwinding activity characteristic of a DNA helicase with 3'-5' polarity. Might be a DNA translocase rather than a bona fide helicase (Probable).","The molecular function of this protein is a DNA helicase, which means it is involved in unwinding double-stranded DNA into single strands.",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0043138; GO:0005524; GO:0016887; GO:0003677; GO:0003678,GO:0004003; GO:0003678,GO:0004003,GO:0004003; GO:0003677,GO:0004003; GO:0003677,GO:0003678,0.6189,0.5554,0.7629,0.7629,0.5554,5,0.6511,0.7675,yes
RECG_THEMA,Q9WY48,Reference,Bacteria,780,"Plays a critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has replication fork (Y-DNA) regression activity, unwinds stalled or blocked replication forks to make a HJ that can be resolved. Has a DNA unwinding activity characteristic of a DNA helicase with 3'-5' polarity. Might be a DNA translocase rather than a bona fide helicase (Probable).","Plays a critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has replication fork (Y-DNA) regression activity, unwinds stalled or blocked replication forks to make a HJ that can be resolved. Has a DNA unwinding activity characteristic of a DNA helicase with 3'-5' polarity. Might be a DNA translocase rather than a bona fide helicase (Probable).",,,,,,,GO:0043138; GO:0005524; GO:0016887; GO:0003677; GO:0003678,GO:0004386; GO:0005524; GO:0003677,GO:0003678; GO:0005524,GO:0003678; GO:0016887,GO:0004386; GO:0003677; GO:0005524,GO:0003678; GO:0016887,0.8377,0.7629,0.7304,0.8377,0.7304,5,0.7798,0.7675,yes
ASST_LELAM,Q9XDP2,ESM2Text,Bacteria,598,"Catalyzes the transfer of a sulfate group from a phenyl sulfate ester to other phenolic compounds. Is able to use several substrate donors and acceptors in vitro: using phenol as an acceptor substrate, 4-methylumbelliferyl sulfate is the best donor substrate, followed by beta-naphthyl sulfate, p-nitrophenyl sulfate (PNS), and alpha-naphthyl sulfate; using PNS as a donor substrate, alpha-naphthol is the best acceptor substrate, followed by phenol, resorcinol, p- acetaminophen, tyramine, and tyrosine. Cannot use 3'-phosphoadenosine- 5'-phophosulfate (PAPS), the donor substrate of mammalian sulfotransferase. May be a detoxifying enzyme, converting toxic phenolic compounds into non-toxic materials.",Aldehyde hydrolase that catalyzes the hydrolysis of a wide range of aliphatic and aromatic aldehydes to the corresponding carboxylic acids with a preference for aromatic aldehydes. It might play a role in the detoxification of aldehydes to avoid cell damage.,No,No,No,No,No,not-Yes,GO:0004062; GO:0047686,GO:0016491,GO:0016787,GO:0016491,GO:0016491,GO:0016491,0.3552,0.3552,0.3552,0.3552,0.3552,5,0.3552,0.4193,no
ASST_LELAM,Q9XDP2,Prot2Text,Bacteria,598,"Catalyzes the transfer of a sulfate group from a phenyl sulfate ester to other phenolic compounds. Is able to use several substrate donors and acceptors in vitro: using phenol as an acceptor substrate, 4-methylumbelliferyl sulfate is the best donor substrate, followed by beta-naphthyl sulfate, p-nitrophenyl sulfate (PNS), and alpha-naphthyl sulfate; using PNS as a donor substrate, alpha-naphthol is the best acceptor substrate, followed by phenol, resorcinol, p- acetaminophen, tyramine, and tyrosine. Cannot use 3'-phosphoadenosine- 5'-phophosulfate (PAPS), the donor substrate of mammalian sulfotransferase. May be a detoxifying enzyme, converting toxic phenolic compounds into non-toxic materials.",Peroxidase that is able to convert a wide range of synthetic substrates to the corresponding aldehydes and lactones.,No,No,No,No,No,not-Yes,GO:0004062; GO:0047686,GO:0004601,GO:0004601,GO:0004601,GO:0004601,GO:0004601,0.2338,0.2338,0.2338,0.2338,0.2338,5,0.2338,0.4193,no
ASST_LELAM,Q9XDP2,ProtT3,Bacteria,598,"Catalyzes the transfer of a sulfate group from a phenyl sulfate ester to other phenolic compounds. Is able to use several substrate donors and acceptors in vitro: using phenol as an acceptor substrate, 4-methylumbelliferyl sulfate is the best donor substrate, followed by beta-naphthyl sulfate, p-nitrophenyl sulfate (PNS), and alpha-naphthyl sulfate; using PNS as a donor substrate, alpha-naphthol is the best acceptor substrate, followed by phenol, resorcinol, p- acetaminophen, tyramine, and tyrosine. Cannot use 3'-phosphoadenosine- 5'-phophosulfate (PAPS), the donor substrate of mammalian sulfotransferase. May be a detoxifying enzyme, converting toxic phenolic compounds into non-toxic materials.",Catalyzes the oxidative decarboxylation of L-tyrosine to 4-hydroxyphenylpyruvate. Periplasm. Belongs to the aromatic-ring-cleaving dioxygenase family,No,No,No,No,No,not-Yes,GO:0004062; GO:0047686,GO:0016702,GO:0003868,GO:0051213,GO:0016702,GO:0003868,0.2113,0.1839,0.2845,0.2113,0.1839,5,0.215,0.4193,no
ASST_LELAM,Q9XDP2,ProtTale,Bacteria,598,"Catalyzes the transfer of a sulfate group from a phenyl sulfate ester to other phenolic compounds. Is able to use several substrate donors and acceptors in vitro: using phenol as an acceptor substrate, 4-methylumbelliferyl sulfate is the best donor substrate, followed by beta-naphthyl sulfate, p-nitrophenyl sulfate (PNS), and alpha-naphthyl sulfate; using PNS as a donor substrate, alpha-naphthol is the best acceptor substrate, followed by phenol, resorcinol, p- acetaminophen, tyramine, and tyrosine. Cannot use 3'-phosphoadenosine- 5'-phophosulfate (PAPS), the donor substrate of mammalian sulfotransferase. May be a detoxifying enzyme, converting toxic phenolic compounds into non-toxic materials.","Lacks antibacterial activity against S.aureus ATCC 25923, E.coli ATCC 25922 and S.typhimurium ATCC 14028.",Vague,No,No,No,Vague,not-Yes,GO:0004062; GO:0047686,,,,,,,,,,,0,,0.4193,no
ASST_LELAM,Q9XDP2,Protein2Text,Bacteria,598,"Catalyzes the transfer of a sulfate group from a phenyl sulfate ester to other phenolic compounds. Is able to use several substrate donors and acceptors in vitro: using phenol as an acceptor substrate, 4-methylumbelliferyl sulfate is the best donor substrate, followed by beta-naphthyl sulfate, p-nitrophenyl sulfate (PNS), and alpha-naphthyl sulfate; using PNS as a donor substrate, alpha-naphthol is the best acceptor substrate, followed by phenol, resorcinol, p- acetaminophen, tyramine, and tyrosine. Cannot use 3'-phosphoadenosine- 5'-phophosulfate (PAPS), the donor substrate of mammalian sulfotransferase. May be a detoxifying enzyme, converting toxic phenolic compounds into non-toxic materials.","This protein is a beta-galactosidase, which means it has a molecular function of catalyzing the hydrolysis of beta-galactosides, such as lactose, into glucose and galactose.",No,No,No,No,No,not-Yes,GO:0004062; GO:0047686,GO:0004565,GO:0004565,GO:0004565,GO:0004565,GO:0004565,0.1737,0.1737,0.1737,0.1737,0.1737,5,0.1737,0.4193,no
ASST_LELAM,Q9XDP2,Reference,Bacteria,598,"Catalyzes the transfer of a sulfate group from a phenyl sulfate ester to other phenolic compounds. Is able to use several substrate donors and acceptors in vitro: using phenol as an acceptor substrate, 4-methylumbelliferyl sulfate is the best donor substrate, followed by beta-naphthyl sulfate, p-nitrophenyl sulfate (PNS), and alpha-naphthyl sulfate; using PNS as a donor substrate, alpha-naphthol is the best acceptor substrate, followed by phenol, resorcinol, p- acetaminophen, tyramine, and tyrosine. Cannot use 3'-phosphoadenosine- 5'-phophosulfate (PAPS), the donor substrate of mammalian sulfotransferase. May be a detoxifying enzyme, converting toxic phenolic compounds into non-toxic materials.","Catalyzes the transfer of a sulfate group from a phenyl sulfate ester to other phenolic compounds. Is able to use several substrate donors and acceptors in vitro: using phenol as an acceptor substrate, 4-methylumbelliferyl sulfate is the best donor substrate, followed by beta-naphthyl sulfate, p-nitrophenyl sulfate (PNS), and alpha-naphthyl sulfate; using PNS as a donor substrate, alpha-naphthol is the best acceptor substrate, followed by phenol, resorcinol, p- acetaminophen, tyramine, and tyrosine. Cannot use 3'-phosphoadenosine- 5'-phophosulfate (PAPS), the donor substrate of mammalian sulfotransferase. May be a detoxifying enzyme, converting toxic phenolic compounds into non-toxic materials.",,,,,,,GO:0004062; GO:0047686,GO:0016782,GO:0004062,GO:0004062,GO:0004062,GO:0004062,0.729,0.9096,0.9096,0.9096,0.9096,5,0.8735,0.4193,no
HUGA_LUTLO,Q9XZ48,ESM2Text,Eukaryota,376,"Hydrolyzes high molecular weight hyaluronic acid to produce small oligosaccharides. Up-regulates expression of CSF2, CSF3, LIF, CXCL1, CXCL2 and CXCL8 in cultured human dermal microvascular endothelial cells. Promotes host neutrophil recruitment at the injection site.",May participate in the degradation of spermatozoa.,Vague,Maybe,Vague,No,No,not-Yes,GO:0004415,,,,,,,,,,,0,,0.3256,no
HUGA_LUTLO,Q9XZ48,Prot2Text,Eukaryota,376,"Hydrolyzes high molecular weight hyaluronic acid to produce small oligosaccharides. Up-regulates expression of CSF2, CSF3, LIF, CXCL1, CXCL2 and CXCL8 in cultured human dermal microvascular endothelial cells. Promotes host neutrophil recruitment at the injection site.",Does not exhibit any ribonuclease activity.,Vague,Maybe,Vague,No,Vague,not-Yes,GO:0004415,,,,,,,,,,,0,,0.3256,no
HUGA_LUTLO,Q9XZ48,ProtT3,Eukaryota,376,"Hydrolyzes high molecular weight hyaluronic acid to produce small oligosaccharides. Up-regulates expression of CSF2, CSF3, LIF, CXCL1, CXCL2 and CXCL8 in cultured human dermal microvascular endothelial cells. Promotes host neutrophil recruitment at the injection site.",Hydrolyzes high molecular weight hyaluronic acid to produce small oligosaccharides. Secreted. Belongs to the glycosyl hydrolase 56 family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004415,GO:0004415,GO:0004415,GO:0004415,GO:0004415,GO:0004415,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3256,no
HUGA_LUTLO,Q9XZ48,ProtTale,Eukaryota,376,"Hydrolyzes high molecular weight hyaluronic acid to produce small oligosaccharides. Up-regulates expression of CSF2, CSF3, LIF, CXCL1, CXCL2 and CXCL8 in cultured human dermal microvascular endothelial cells. Promotes host neutrophil recruitment at the injection site.",Hyaluronidase catalyzes the hydrolysis of hyaluronic acid to form disaccharides of N-acetyl-D- glucosamine and D-glucuronic acid.,Yes,Yes,Maybe,Maybe,Yes,Yes,GO:0004415,GO:0004415,GO:0004415,GO:0004415,GO:0004415,GO:0004415,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3256,no
HUGA_LUTLO,Q9XZ48,Protein2Text,Eukaryota,376,"Hydrolyzes high molecular weight hyaluronic acid to produce small oligosaccharides. Up-regulates expression of CSF2, CSF3, LIF, CXCL1, CXCL2 and CXCL8 in cultured human dermal microvascular endothelial cells. Promotes host neutrophil recruitment at the injection site.","The molecular function of this protein is hyaluronidase activity, which is the ability to break down hyaluronic acid. Hyaluronic acid is a type of glycosaminoglycan that is found in connective tissue and plays a role in maintaining tissue structure and hydration. This protein is likely involved in the degradation of hyaluronic acid in tissues, which can have a range of effects depending on the specific context in which it occurs.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004415,GO:0004415,GO:0004415,GO:0004415,GO:0004415,GO:0004415,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3256,no
HUGA_LUTLO,Q9XZ48,Reference,Eukaryota,376,"Hydrolyzes high molecular weight hyaluronic acid to produce small oligosaccharides. Up-regulates expression of CSF2, CSF3, LIF, CXCL1, CXCL2 and CXCL8 in cultured human dermal microvascular endothelial cells. Promotes host neutrophil recruitment at the injection site.","Hydrolyzes high molecular weight hyaluronic acid to produce small oligosaccharides. Up-regulates expression of CSF2, CSF3, LIF, CXCL1, CXCL2 and CXCL8 in cultured human dermal microvascular endothelial cells. Promotes host neutrophil recruitment at the injection site.",,,,,,,GO:0004415,GO:0004415,GO:0004415,GO:0016798,GO:0004415,GO:0004415,1.0,1.0,0.6466,1.0,1.0,5,0.9293,0.3256,no
WAAJ_ECOLX,Q9ZIT6,ESM2Text,Bacteria,339,"Glucosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS). Catalyzes the addition of a glucose (glucose II) to the outer-core galactose I. Has a marked preference for its specific donor substrate, but it appears to have a relaxed specificity for alternate LPS acceptor residues, providing the overall size of the acceptor is conserved.",Adds the glucose(II) group on the galactose(I) group of LPS.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008918; GO:0008919; GO:0046872,GO:0016757,GO:0046527,GO:0016757,GO:0008194,GO:0046527,0.4472,0.5174,0.4472,0.5146,0.5174,5,0.4888,0.5392,yes
WAAJ_ECOLX,Q9ZIT6,Prot2Text,Bacteria,339,"Glucosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS). Catalyzes the addition of a glucose (glucose II) to the outer-core galactose I. Has a marked preference for its specific donor substrate, but it appears to have a relaxed specificity for alternate LPS acceptor residues, providing the overall size of the acceptor is conserved.",Adds the glucose(II) group on the galactose(I) group of LPS.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008918; GO:0008919; GO:0046872,GO:0046527,GO:0016757,GO:0016757,GO:0046527,GO:0016757,0.5174,0.4472,0.4472,0.5174,0.4472,5,0.4753,0.5392,yes
WAAJ_ECOLX,Q9ZIT6,ProtT3,Bacteria,339,"Glucosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS). Catalyzes the addition of a glucose (glucose II) to the outer-core galactose I. Has a marked preference for its specific donor substrate, but it appears to have a relaxed specificity for alternate LPS acceptor residues, providing the overall size of the acceptor is conserved.",Belongs to the glycosyltransferase 8 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008918; GO:0008919; GO:0046872,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.4472,0.4472,0.4472,0.4472,0.4472,5,0.4472,0.5392,yes
WAAJ_ECOLX,Q9ZIT6,ProtTale,Bacteria,339,"Glucosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS). Catalyzes the addition of a glucose (glucose II) to the outer-core galactose I. Has a marked preference for its specific donor substrate, but it appears to have a relaxed specificity for alternate LPS acceptor residues, providing the overall size of the acceptor is conserved.",Glucosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS). Catalyzes the addition of a glucose (Glc) from UDP-Glc to the second GlcNAc residue of the inner core.,Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0008918; GO:0008919; GO:0046872,GO:0035251,GO:0016758,GO:0008194,GO:0016758,GO:0035251,0.6161,0.5033,0.5146,0.5033,0.6161,5,0.5507,0.5392,yes
WAAJ_ECOLX,Q9ZIT6,Protein2Text,Bacteria,339,"Glucosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS). Catalyzes the addition of a glucose (glucose II) to the outer-core galactose I. Has a marked preference for its specific donor substrate, but it appears to have a relaxed specificity for alternate LPS acceptor residues, providing the overall size of the acceptor is conserved.","This protein is a glycosyltransferase. It is a transferase that plays a crucial role in the synthesis of glycosidic bonds in polysaccharides. Specifically, it is involved in the synthesis of alpha-1,4-glucan, which is a type of polysaccharide.",Maybe,Maybe,Maybe,Maybe,Vague,not-Yes,GO:0008918; GO:0008919; GO:0046872,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.4472,0.4472,0.4472,0.4472,0.4472,5,0.4472,0.5392,yes
WAAJ_ECOLX,Q9ZIT6,Reference,Bacteria,339,"Glucosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS). Catalyzes the addition of a glucose (glucose II) to the outer-core galactose I. Has a marked preference for its specific donor substrate, but it appears to have a relaxed specificity for alternate LPS acceptor residues, providing the overall size of the acceptor is conserved.","Glucosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS). Catalyzes the addition of a glucose (glucose II) to the outer-core galactose I. Has a marked preference for its specific donor substrate, but it appears to have a relaxed specificity for alternate LPS acceptor residues, providing the overall size of the acceptor is conserved.",,,,,,,GO:0008918; GO:0008919; GO:0046872,GO:0016757,GO:0046527,GO:0046527,GO:0016757; GO:0035251,GO:0016757,0.4472,0.5174,0.5174,0.6141,0.4472,5,0.5087,0.5392,yes
LCPS_GIBF5,S0EQ07,ESM2Text,Eukaryota,580,"Bifunctional enzyme; part of the car gene cluster that mediates the biosynthesis of neurosporaxanthin, a carboxylic apocarotenoid acting as an essential protective pigments and leading to orange pigmentation. CarAR catalyzes the first step of the pathway by converting geranylgeranyl diphosphate to phytoene, as well as the later cyclization step that transforms the carB product lycopene into gamma-carotene. CarAR also converts part of gamma-carotene into beta-carotene. Neurosporaxanthin is synthesized from geranyl-geranyl pyrophosphate (GGPP) through several enzymatic activities. Phytoene synthase activity performed by the bifunctional enzyme carAR first produces phytoene from geranyl-geranyl pyrophosphate (GGPP). The phytoene dehydrogenase carB then introduces 4 desaturations to lead to lycopene which is substrate of the carotene cyclase activity of carAR that leads to the production of gamma-carotene. CarB then performs a 5th desaturation reaction to yield torulene. Torulene is the substrate of the dioxidase carT that breaks the molecule, removing five carbon atoms to yield beta-apo-4'- carotenal, whereas the aldehyde dehydrogenase carD mediates the last step by converting beta-apo-4'-carotenal into neurosporaxanthin (Probable).",Bifunctional enzyme that catalyzes the reactions from geranylgeranyl diphosphate to phytoene (phytoene synthase) and lycopene to beta-carotene via the intermediate gamma-carotene (lycopene cyclase).,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004311; GO:0016872; GO:0045436; GO:0051996,GO:0016767; GO:0045436,GO:0016767; GO:0045436,GO:0016740,GO:0016767; GO:0045436,GO:0016740; GO:0045436,0.5905,0.5905,0.5204,0.5905,0.7086,5,0.6001,0.2549,no
LCPS_GIBF5,S0EQ07,Prot2Text,Eukaryota,580,"Bifunctional enzyme; part of the car gene cluster that mediates the biosynthesis of neurosporaxanthin, a carboxylic apocarotenoid acting as an essential protective pigments and leading to orange pigmentation. CarAR catalyzes the first step of the pathway by converting geranylgeranyl diphosphate to phytoene, as well as the later cyclization step that transforms the carB product lycopene into gamma-carotene. CarAR also converts part of gamma-carotene into beta-carotene. Neurosporaxanthin is synthesized from geranyl-geranyl pyrophosphate (GGPP) through several enzymatic activities. Phytoene synthase activity performed by the bifunctional enzyme carAR first produces phytoene from geranyl-geranyl pyrophosphate (GGPP). The phytoene dehydrogenase carB then introduces 4 desaturations to lead to lycopene which is substrate of the carotene cyclase activity of carAR that leads to the production of gamma-carotene. CarB then performs a 5th desaturation reaction to yield torulene. Torulene is the substrate of the dioxidase carT that breaks the molecule, removing five carbon atoms to yield beta-apo-4'- carotenal, whereas the aldehyde dehydrogenase carD mediates the last step by converting beta-apo-4'-carotenal into neurosporaxanthin (Probable).",Bifunctional enzyme that catalyzes the reactions from geranylgeranyl diphosphate to phytoene (phytoene synthase) and lycopene to beta-carotene via the intermediate gamma-carotene (lycopene cyclase).,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004311; GO:0016872; GO:0045436; GO:0051996,GO:0016767; GO:0045436,,GO:0045436,GO:0016767; GO:0045436,GO:0016767; GO:0045436,0.5905,,0.5905,0.5905,0.5905,4,0.5905,0.2549,no
LCPS_GIBF5,S0EQ07,ProtT3,Eukaryota,580,"Bifunctional enzyme; part of the car gene cluster that mediates the biosynthesis of neurosporaxanthin, a carboxylic apocarotenoid acting as an essential protective pigments and leading to orange pigmentation. CarAR catalyzes the first step of the pathway by converting geranylgeranyl diphosphate to phytoene, as well as the later cyclization step that transforms the carB product lycopene into gamma-carotene. CarAR also converts part of gamma-carotene into beta-carotene. Neurosporaxanthin is synthesized from geranyl-geranyl pyrophosphate (GGPP) through several enzymatic activities. Phytoene synthase activity performed by the bifunctional enzyme carAR first produces phytoene from geranyl-geranyl pyrophosphate (GGPP). The phytoene dehydrogenase carB then introduces 4 desaturations to lead to lycopene which is substrate of the carotene cyclase activity of carAR that leads to the production of gamma-carotene. CarB then performs a 5th desaturation reaction to yield torulene. Torulene is the substrate of the dioxidase carT that breaks the molecule, removing five carbon atoms to yield beta-apo-4'- carotenal, whereas the aldehyde dehydrogenase carD mediates the last step by converting beta-apo-4'-carotenal into neurosporaxanthin (Probable).",Bifunctional enzyme that catalyzes the reactions from geranylgeranyl diphosphate to phytoene (phytoene synthase) and lycopene to beta-carotene via the intermediate gamma-carotene (lycopene cyclase). Membrane; Multi-pass membrane protein. In the C-terminal section; belongs to the phytoene/squalene synthase family. In the N-terminal section; belongs to the lycopene beta- cyclase family,Yes,Yes,Vague,Yes,Yes,Yes,GO:0004311; GO:0016872; GO:0045436; GO:0051996,GO:0016740; GO:0045436,GO:0016767; GO:0045436,GO:0016767; GO:0045436,GO:0016768; GO:0045436,GO:0016768; GO:0045436,0.7086,0.5905,0.5905,0.7075,0.7075,5,0.6609,0.2549,no
LCPS_GIBF5,S0EQ07,ProtTale,Eukaryota,580,"Bifunctional enzyme; part of the car gene cluster that mediates the biosynthesis of neurosporaxanthin, a carboxylic apocarotenoid acting as an essential protective pigments and leading to orange pigmentation. CarAR catalyzes the first step of the pathway by converting geranylgeranyl diphosphate to phytoene, as well as the later cyclization step that transforms the carB product lycopene into gamma-carotene. CarAR also converts part of gamma-carotene into beta-carotene. Neurosporaxanthin is synthesized from geranyl-geranyl pyrophosphate (GGPP) through several enzymatic activities. Phytoene synthase activity performed by the bifunctional enzyme carAR first produces phytoene from geranyl-geranyl pyrophosphate (GGPP). The phytoene dehydrogenase carB then introduces 4 desaturations to lead to lycopene which is substrate of the carotene cyclase activity of carAR that leads to the production of gamma-carotene. CarB then performs a 5th desaturation reaction to yield torulene. Torulene is the substrate of the dioxidase carT that breaks the molecule, removing five carbon atoms to yield beta-apo-4'- carotenal, whereas the aldehyde dehydrogenase carD mediates the last step by converting beta-apo-4'-carotenal into neurosporaxanthin (Probable).",Bifunctional enzyme that catalyzes the reactions from geranylgeranyl diphosphate to phytoene (phytoene synthase) and lycopene to beta-carotene via the intermediate delta-carotene (lycopene cyclase).,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004311; GO:0016872; GO:0045436; GO:0051996,GO:0016767; GO:0045436,GO:0016740,GO:0016740; GO:0016829,GO:0016740,,0.5905,0.5204,0.5138,0.5204,,4,0.5363,0.2549,no
LCPS_GIBF5,S0EQ07,Protein2Text,Eukaryota,580,"Bifunctional enzyme; part of the car gene cluster that mediates the biosynthesis of neurosporaxanthin, a carboxylic apocarotenoid acting as an essential protective pigments and leading to orange pigmentation. CarAR catalyzes the first step of the pathway by converting geranylgeranyl diphosphate to phytoene, as well as the later cyclization step that transforms the carB product lycopene into gamma-carotene. CarAR also converts part of gamma-carotene into beta-carotene. Neurosporaxanthin is synthesized from geranyl-geranyl pyrophosphate (GGPP) through several enzymatic activities. Phytoene synthase activity performed by the bifunctional enzyme carAR first produces phytoene from geranyl-geranyl pyrophosphate (GGPP). The phytoene dehydrogenase carB then introduces 4 desaturations to lead to lycopene which is substrate of the carotene cyclase activity of carAR that leads to the production of gamma-carotene. CarB then performs a 5th desaturation reaction to yield torulene. Torulene is the substrate of the dioxidase carT that breaks the molecule, removing five carbon atoms to yield beta-apo-4'- carotenal, whereas the aldehyde dehydrogenase carD mediates the last step by converting beta-apo-4'-carotenal into neurosporaxanthin (Probable).","The molecular function of this protein is not explicitly stated in the provided text. However, based on its name, it is likely that this protein is involved in the synthesis of heme, a crucial component of various biological molecules such as hemoglobin and cytochrome. As a heme lyase, it is probably involved in the final step of heme biosynthesis, where it catalyzes the attachment of the heme group to a protein.",No,No,No,No,Vague,not-Yes,GO:0004311; GO:0016872; GO:0045436; GO:0051996,,,,,,,,,,,0,,0.2549,no
LCPS_GIBF5,S0EQ07,Reference,Eukaryota,580,"Bifunctional enzyme; part of the car gene cluster that mediates the biosynthesis of neurosporaxanthin, a carboxylic apocarotenoid acting as an essential protective pigments and leading to orange pigmentation. CarAR catalyzes the first step of the pathway by converting geranylgeranyl diphosphate to phytoene, as well as the later cyclization step that transforms the carB product lycopene into gamma-carotene. CarAR also converts part of gamma-carotene into beta-carotene. Neurosporaxanthin is synthesized from geranyl-geranyl pyrophosphate (GGPP) through several enzymatic activities. Phytoene synthase activity performed by the bifunctional enzyme carAR first produces phytoene from geranyl-geranyl pyrophosphate (GGPP). The phytoene dehydrogenase carB then introduces 4 desaturations to lead to lycopene which is substrate of the carotene cyclase activity of carAR that leads to the production of gamma-carotene. CarB then performs a 5th desaturation reaction to yield torulene. Torulene is the substrate of the dioxidase carT that breaks the molecule, removing five carbon atoms to yield beta-apo-4'- carotenal, whereas the aldehyde dehydrogenase carD mediates the last step by converting beta-apo-4'-carotenal into neurosporaxanthin (Probable).","Bifunctional enzyme; part of the car gene cluster that mediates the biosynthesis of neurosporaxanthin, a carboxylic apocarotenoid acting as an essential protective pigments and leading to orange pigmentation. CarAR catalyzes the first step of the pathway by converting geranylgeranyl diphosphate to phytoene, as well as the later cyclization step that transforms the carB product lycopene into gamma-carotene. CarAR also converts part of gamma-carotene into beta-carotene. Neurosporaxanthin is synthesized from geranyl-geranyl pyrophosphate (GGPP) through several enzymatic activities. Phytoene synthase activity performed by the bifunctional enzyme carAR first produces phytoene from geranyl-geranyl pyrophosphate (GGPP). The phytoene dehydrogenase carB then introduces 4 desaturations to lead to lycopene which is substrate of the carotene cyclase activity of carAR that leads to the production of gamma-carotene. CarB then performs a 5th desaturation reaction to yield torulene. Torulene is the substrate of the dioxidase carT that breaks the molecule, removing five carbon atoms to yield beta-apo-4'- carotenal, whereas the aldehyde dehydrogenase carD mediates the last step by converting beta-apo-4'-carotenal into neurosporaxanthin (Probable).",,,,,,,GO:0004311; GO:0016872; GO:0045436; GO:0051996,GO:0016740; GO:0004311,GO:0045550; GO:0045436,GO:0016767,GO:0016767; GO:0045436,GO:0016767; GO:0045436,0.6826,0.5728,0.0,0.5905,0.5905,5,0.4873,0.2549,no
TOXH_COCCA,S5NIA2,ESM2Text,Eukaryota,1547,"Fatty acid synthase alpha subunit, part of the diffuse TOX2 gene cluster that mediates the biosynthesis of the HC-toxin, cyclic tetrapeptide of structure cyclo(D-Pro-L-Ala-D-Ala-L-Aeo), where Aeo stands for 2-amino-9,10-epoxi-8-oxodecanoic acid. HC- toxin is a determinant of specificity and virulence in the interaction between the producing fungus and its host, maize. TOXH contribute to the synthesis of the decanoic backbone of 2- amino-9,10-epoxi-8-oxodecanoic acid, an essential precursor for the production of the major forms of HC-toxin by the non-ribosomal peptide synthetase HTS1 (Probable).","Fatty acid synthase subunit; part of the gene cluster that mediates the biosynthesis of the tropolone class of fungal maleic anhydrides. The pathway begins with the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide synthase (PKS) tropA. 3-methylorcinaldehyde is the substrate for the FAD-dependent monooxygenase tropB to yield a dearomatized hydroxycyclohexadione. The 2-oxoglutarate-dependent dioxygenase tropC then performs the oxidative ring expansion to provide the first tropolone metabolite stipitaldehyde. Trop D converts stipitaldehyde into stipitacetal which is in turn converted to stipitalide by the short-chain dehydrogenase/reductase tropE. The next steps involve tropF, tropG, tropH, tropI and tropJ to form successive tropolone maleic anhydrides including stipitaldehydic, stipitatonic and stipitatic acids.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004316; GO:0004315; GO:0004312; GO:0004321; GO:0008897,GO:0004312,GO:0004312,GO:0016491; GO:0016740,GO:0004312,GO:0004312,0.6502,0.6502,0.5928,0.6502,0.6502,5,0.6387,0.2359,no
TOXH_COCCA,S5NIA2,Prot2Text,Eukaryota,1547,"Fatty acid synthase alpha subunit, part of the diffuse TOX2 gene cluster that mediates the biosynthesis of the HC-toxin, cyclic tetrapeptide of structure cyclo(D-Pro-L-Ala-D-Ala-L-Aeo), where Aeo stands for 2-amino-9,10-epoxi-8-oxodecanoic acid. HC- toxin is a determinant of specificity and virulence in the interaction between the producing fungus and its host, maize. TOXH contribute to the synthesis of the decanoic backbone of 2- amino-9,10-epoxi-8-oxodecanoic acid, an essential precursor for the production of the major forms of HC-toxin by the non-ribosomal peptide synthetase HTS1 (Probable).","Fatty acid synthase subunit alpha; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004316; GO:0004315; GO:0004312; GO:0004321; GO:0008897,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.6502,0.6502,0.6502,0.6502,0.6502,5,0.6502,0.2359,no
TOXH_COCCA,S5NIA2,ProtT3,Eukaryota,1547,"Fatty acid synthase alpha subunit, part of the diffuse TOX2 gene cluster that mediates the biosynthesis of the HC-toxin, cyclic tetrapeptide of structure cyclo(D-Pro-L-Ala-D-Ala-L-Aeo), where Aeo stands for 2-amino-9,10-epoxi-8-oxodecanoic acid. HC- toxin is a determinant of specificity and virulence in the interaction between the producing fungus and its host, maize. TOXH contribute to the synthesis of the decanoic backbone of 2- amino-9,10-epoxi-8-oxodecanoic acid, an essential precursor for the production of the major forms of HC-toxin by the non-ribosomal peptide synthetase HTS1 (Probable).",1-deoxy-D-xylulose-5-phosphate (DXP) reductase; part of the third module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (By similarity). ERG3 catalyzes the NADPH-dependent reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4- phosphate (MEP) (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER),No,No,Vague,No,No,not-Yes,GO:0004316; GO:0004315; GO:0004312; GO:0004321; GO:0008897,GO:0030604,GO:0030604,GO:0030604,GO:0030604,GO:0030604,0.3719,0.3719,0.3719,0.3719,0.3719,5,0.3719,0.2359,no
TOXH_COCCA,S5NIA2,ProtTale,Eukaryota,1547,"Fatty acid synthase alpha subunit, part of the diffuse TOX2 gene cluster that mediates the biosynthesis of the HC-toxin, cyclic tetrapeptide of structure cyclo(D-Pro-L-Ala-D-Ala-L-Aeo), where Aeo stands for 2-amino-9,10-epoxi-8-oxodecanoic acid. HC- toxin is a determinant of specificity and virulence in the interaction between the producing fungus and its host, maize. TOXH contribute to the synthesis of the decanoic backbone of 2- amino-9,10-epoxi-8-oxodecanoic acid, an essential precursor for the production of the major forms of HC-toxin by the non-ribosomal peptide synthetase HTS1 (Probable).","Fatty acid synthase alpha subunit; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS). SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms. These initial steps feature the priming of an unusual benzoic acid starter unit",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004316; GO:0004315; GO:0004312; GO:0004321; GO:0008897,GO:0004312,GO:0016747,GO:0004312,GO:0016746,GO:0004312,0.6502,0.6604,0.6502,0.6,0.6502,5,0.6422,0.2359,no
TOXH_COCCA,S5NIA2,Protein2Text,Eukaryota,1547,"Fatty acid synthase alpha subunit, part of the diffuse TOX2 gene cluster that mediates the biosynthesis of the HC-toxin, cyclic tetrapeptide of structure cyclo(D-Pro-L-Ala-D-Ala-L-Aeo), where Aeo stands for 2-amino-9,10-epoxi-8-oxodecanoic acid. HC- toxin is a determinant of specificity and virulence in the interaction between the producing fungus and its host, maize. TOXH contribute to the synthesis of the decanoic backbone of 2- amino-9,10-epoxi-8-oxodecanoic acid, an essential precursor for the production of the major forms of HC-toxin by the non-ribosomal peptide synthetase HTS1 (Probable).","The molecular function of this protein is not specified in the provided text. However, based on its name, it is likely involved in a process related to metabolism, specifically the metabolism of fatty acids or steroids. The name ""fatty acid desaturase"" suggests that it is involved in the desaturation of fatty acids, which is a key step in the synthesis of unsaturated fatty acids.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004316; GO:0004315; GO:0004312; GO:0004321; GO:0008897,GO:0016717,GO:0016717,GO:0016717,GO:0006636,GO:0016215,0.285,0.285,0.285,0.0,0.2417,5,0.2193,0.2359,no
TOXH_COCCA,S5NIA2,Reference,Eukaryota,1547,"Fatty acid synthase alpha subunit, part of the diffuse TOX2 gene cluster that mediates the biosynthesis of the HC-toxin, cyclic tetrapeptide of structure cyclo(D-Pro-L-Ala-D-Ala-L-Aeo), where Aeo stands for 2-amino-9,10-epoxi-8-oxodecanoic acid. HC- toxin is a determinant of specificity and virulence in the interaction between the producing fungus and its host, maize. TOXH contribute to the synthesis of the decanoic backbone of 2- amino-9,10-epoxi-8-oxodecanoic acid, an essential precursor for the production of the major forms of HC-toxin by the non-ribosomal peptide synthetase HTS1 (Probable).","Fatty acid synthase alpha subunit, part of the diffuse TOX2 gene cluster that mediates the biosynthesis of the HC-toxin, cyclic tetrapeptide of structure cyclo(D-Pro-L-Ala-D-Ala-L-Aeo), where Aeo stands for 2-amino-9,10-epoxi-8-oxodecanoic acid. HC- toxin is a determinant of specificity and virulence in the interaction between the producing fungus and its host, maize. TOXH contribute to the synthesis of the decanoic backbone of 2- amino-9,10-epoxi-8-oxodecanoic acid, an essential precursor for the production of the major forms of HC-toxin by the non-ribosomal peptide synthetase HTS1 (Probable).",,,,,,,GO:0004316; GO:0004315; GO:0004312; GO:0004321; GO:0008897,GO:0031177; GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.5689,0.6502,0.6502,0.6502,0.6502,5,0.6339,0.2359,no
PDMB_SPHYB,S5SC42,ESM2Text,Bacteria,176,"Part of the multicomponent N,N-dimethyl phenylurea N- demethylase responsible for the initial N-demethylation step during the bacterial metabolism of N,N-dimethyl-substituted phenylurea herbicides. Catalyzes the mono-N-demethylation of N,N-dimethyl- substituted phenylurea herbicides to their mono-N-demethylated derivatives. Is active on isoproturon (IPU), chlorotoluron, metoxuron, monoron, diuron, fluometuron and fenuron, but cannot transform the N-methoxy-N-methyl-substituted herbicides.","Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. The beta subunit seems to have a structural role in the holoenzyme. Also able to catalyze the cis-dihydroxylation of biphenyl and phenanthrene.",Maybe,No,No,Maybe,Maybe,not-Yes,GO:0016491,GO:0016702,GO:0016702,GO:0016491,GO:0016701,GO:0016701; GO:0005506,0.6062,0.6062,1.0,0.8145,0.5859,5,0.7226,0.1982,no
PDMB_SPHYB,S5SC42,Prot2Text,Bacteria,176,"Part of the multicomponent N,N-dimethyl phenylurea N- demethylase responsible for the initial N-demethylation step during the bacterial metabolism of N,N-dimethyl-substituted phenylurea herbicides. Catalyzes the mono-N-demethylation of N,N-dimethyl- substituted phenylurea herbicides to their mono-N-demethylated derivatives. Is active on isoproturon (IPU), chlorotoluron, metoxuron, monoron, diuron, fluometuron and fenuron, but cannot transform the N-methoxy-N-methyl-substituted herbicides.",Component of anthranilate dioxygenase multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into anthranilate to form catechol.,Maybe,No,No,Maybe,Maybe,not-Yes,GO:0016491,GO:0051213,GO:0016702,GO:0016491,GO:0051213,GO:0016702,0.8145,0.6062,1.0,0.8145,0.6062,5,0.7683,0.1982,no
PDMB_SPHYB,S5SC42,ProtT3,Bacteria,176,"Part of the multicomponent N,N-dimethyl phenylurea N- demethylase responsible for the initial N-demethylation step during the bacterial metabolism of N,N-dimethyl-substituted phenylurea herbicides. Catalyzes the mono-N-demethylation of N,N-dimethyl- substituted phenylurea herbicides to their mono-N-demethylated derivatives. Is active on isoproturon (IPU), chlorotoluron, metoxuron, monoron, diuron, fluometuron and fenuron, but cannot transform the N-methoxy-N-methyl-substituted herbicides.","Component of the naphthalene dioxygenase multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2- dihydronaphthalene. Belongs to the bacterial ring-hydroxylating dioxygenase beta subunit family",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0016491,GO:0018625,GO:0016701,GO:0018517,GO:0016705,GO:0016701,0.545,0.8145,0.6019,0.8145,0.8145,5,0.7181,0.1982,no
PDMB_SPHYB,S5SC42,ProtTale,Bacteria,176,"Part of the multicomponent N,N-dimethyl phenylurea N- demethylase responsible for the initial N-demethylation step during the bacterial metabolism of N,N-dimethyl-substituted phenylurea herbicides. Catalyzes the mono-N-demethylation of N,N-dimethyl- substituted phenylurea herbicides to their mono-N-demethylated derivatives. Is active on isoproturon (IPU), chlorotoluron, metoxuron, monoron, diuron, fluometuron and fenuron, but cannot transform the N-methoxy-N-methyl-substituted herbicides.","Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2- dihydronaphthalene. The alpha subunit has a structural role in the holoenzyme.",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0016491,,,,,,,,,,,0,,0.1982,no
PDMB_SPHYB,S5SC42,Protein2Text,Bacteria,176,"Part of the multicomponent N,N-dimethyl phenylurea N- demethylase responsible for the initial N-demethylation step during the bacterial metabolism of N,N-dimethyl-substituted phenylurea herbicides. Catalyzes the mono-N-demethylation of N,N-dimethyl- substituted phenylurea herbicides to their mono-N-demethylated derivatives. Is active on isoproturon (IPU), chlorotoluron, metoxuron, monoron, diuron, fluometuron and fenuron, but cannot transform the N-methoxy-N-methyl-substituted herbicides.","The molecular function of this protein is not explicitly stated in the provided text. However, based on the context, it can be inferred that this protein is involved in a catalytic process, likely in the metabolism of a specific compound. The fact that it is described as a ""cytochrome"" suggests that it may be involved in an enzymatic reaction, possibly as a redox catalyst. Further research would be necessary to determine the exact molecular function of this protein. 
In general, cytochromes are a family of hemoproteins that play a crucial role in various biological processes, including electron transfer, oxidation, and reduction reactions. They are typically involved in the metabolism of oxygen, nitrogen, and sulfur compounds, and are often found in enzymes that catalyze redox reactions.",Vague,No,Vague,Vague,Vague,not-Yes,GO:0016491,,,,,,,,,,,0,,0.1982,no
PDMB_SPHYB,S5SC42,Reference,Bacteria,176,"Part of the multicomponent N,N-dimethyl phenylurea N- demethylase responsible for the initial N-demethylation step during the bacterial metabolism of N,N-dimethyl-substituted phenylurea herbicides. Catalyzes the mono-N-demethylation of N,N-dimethyl- substituted phenylurea herbicides to their mono-N-demethylated derivatives. Is active on isoproturon (IPU), chlorotoluron, metoxuron, monoron, diuron, fluometuron and fenuron, but cannot transform the N-methoxy-N-methyl-substituted herbicides.","Part of the multicomponent N,N-dimethyl phenylurea N- demethylase responsible for the initial N-demethylation step during the bacterial metabolism of N,N-dimethyl-substituted phenylurea herbicides. Catalyzes the mono-N-demethylation of N,N-dimethyl- substituted phenylurea herbicides to their mono-N-demethylated derivatives. Is active on isoproturon (IPU), chlorotoluron, metoxuron, monoron, diuron, fluometuron and fenuron, but cannot transform the N-methoxy-N-methyl-substituted herbicides.",,,,,,,GO:0016491,GO:0004497; GO:0016709,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.7451,0.8145,0.8145,0.8145,0.8145,5,0.8006,0.1982,no
LP9D_GLOTA,S7QP81,ESM2Text,Eukaryota,344,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.","Lignin degradation and detoxification of lignin-derived products (Probable). Acts on substrates such as acetylated xylans, carboxymethyl cellulose, vanillin and birchwood xylan. Does not show detectable activity against the vanillic acid-containing substrates vanillic acid, vanillic acid-containing substrates, and the vanillic acid-containing substrates beta-naphthopyrones.",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0046872; GO:0004497,GO:0016168,,,GO:0016168,GO:0016168,0.2475,,,0.2475,0.2475,3,0.2475,0.3038,no
LP9D_GLOTA,S7QP81,Prot2Text,Eukaryota,344,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.","Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. May be involved in the degradation of complex natural cellulosic substrates.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0004497,GO:0004392,GO:0004392,GO:0004392,GO:0004392,GO:0004392,0.4705,0.4705,0.4705,0.4705,0.4705,5,0.4705,0.3038,no
LP9D_GLOTA,S7QP81,ProtT3,Eukaryota,344,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.","Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates (By similarity). Secreted. Belongs to the glycosyl hydrolase 61 family",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0004497,GO:0004553,GO:0008810,GO:0016798,GO:0004553,GO:0008810,0.2538,0.2193,0.3023,0.2538,0.2193,5,0.2497,0.3038,no
LP9D_GLOTA,S7QP81,ProtTale,Eukaryota,344,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.","Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0004497,GO:0004497,GO:0016491; GO:0005507,GO:0016491; GO:0005507,GO:0004497; GO:0005507,GO:0004497,0.7088,0.7926,0.7926,0.8854,0.7088,5,0.7776,0.3038,no
LP9D_GLOTA,S7QP81,Protein2Text,Eukaryota,344,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.","The molecular function of this protein is catalytic, specifically it is involved in lignin degradation. More specifically, it is a ligninolytic oxidase, which is a type of enzyme that breaks down lignin, a complex organic polymer found in plant cell walls. Lignin is a major component of wood and is also found in other plant tissues, and it is degraded by fungi and other microorganisms as part of the process of decomposing organic matter. The specific function of this protein is to oxidize the phenolic rings of lignin, which is a key step in its degradation.",No,No,No,No,No,not-Yes,GO:0046872; GO:0004497,GO:0016166,GO:0016166,GO:0016491,GO:0015645,,0.4059,0.4059,0.5957,0.2273,,4,0.4087,0.3038,no
LP9D_GLOTA,S7QP81,Reference,Eukaryota,344,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.","Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.",,,,,,,GO:0046872; GO:0004497,GO:0016491; GO:0005507,GO:0016491,GO:0004497; GO:0005507,GO:0016491; GO:0005507,GO:0016491,0.7926,0.5957,0.8854,0.7926,0.5957,5,0.7324,0.3038,no
TAS1_GLOTA,S7RK07,ESM2Text,Eukaryota,1558,"Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal NRPS module and subsequent cyclization conducted by the C-terminal KS domain.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcs",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0016874; GO:0031177,,GO:0016874,GO:0003824,GO:0016874,GO:0016874; GO:0005524,,0.6206,0.5365,0.6206,0.6145,4,0.598,0.2607,no
TAS1_GLOTA,S7RK07,Prot2Text,Eukaryota,1558,"Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal NRPS module and subsequent cyclization conducted by the C-terminal KS domain.","Acyl-CoA synthetase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate",Maybe,No,Maybe,Maybe,No,not-Yes,GO:0004315; GO:0016874; GO:0031177,,,,,,,,,,,0,,0.2607,no
TAS1_GLOTA,S7RK07,ProtT3,Eukaryota,1558,"Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal NRPS module and subsequent cyclization conducted by the C-terminal KS domain.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0016874; GO:0031177,GO:0016874,GO:0016874,GO:0016874,GO:0016874,GO:0016874; GO:0005524,0.6206,0.6206,0.6206,0.6206,0.6145,5,0.6194,0.2607,no
TAS1_GLOTA,S7RK07,ProtTale,Eukaryota,1558,"Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal NRPS module and subsequent cyclization conducted by the C-terminal KS domain.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0016874; GO:0031177,GO:0016747,GO:0016747,GO:0016746,GO:0016746,,0.5539,0.5539,0.5114,0.5114,,4,0.5326,0.2607,no
TAS1_GLOTA,S7RK07,Protein2Text,Eukaryota,1558,"Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal NRPS module and subsequent cyclization conducted by the C-terminal KS domain.","The molecular function of the protein is a non-reducing polyketide synthase (PKS), which is involved in the biosynthesis of a non-reducing polyketide.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0016874; GO:0031177,GO:0004337,GO:0004337,GO:0004311,GO:0004337,GO:0004337,0.2507,0.2507,0.2507,0.2507,0.2507,5,0.2507,0.2607,no
TAS1_GLOTA,S7RK07,Reference,Eukaryota,1558,"Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal NRPS module and subsequent cyclization conducted by the C-terminal KS domain.","Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal NRPS module and subsequent cyclization conducted by the C-terminal KS domain.",,,,,,,GO:0004315; GO:0016874; GO:0031177,GO:0031177; GO:0016874,GO:0004315; GO:0008927,,GO:0016874; GO:0016746,,0.871,0.5584,,0.717,,3,0.7155,0.2607,no
OPDA_PENO1,S7Z800,ESM2Text,Eukaryota,3994,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of oxopyrrolidines, polyketide-amino acid hybrid compounds with feature structures of tetramic acid. The polyketide chain is first assembled by the highly reducing PKS module of opdA using acetyl-CoA as the starter unit and five malonyl-CoA as the extender units. OpdC acts as trans-acting enoyl reductase and reduces the terminal alkenyl to alkane. The 17R in oxopyrrolidine A and 15R, 17S in oxopyrrolidine B are generated by non-stereospecific catalysis of the ketoreductase (KR) domain and enoyl reductases. Then the polyketides with specific configurations are transferred to the NRPS module of opdA and linked to L-tyrosine to form an amide bond. Finally, the oxopyrrolidines are offloaded through a Dieckmann cyclization catalyzed by the terminal D domain to give a tetramic acid moiety.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcsC",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0031177,,GO:0016747,GO:0016491; GO:0016740,GO:0016746,GO:0016746,,0.5897,0.5558,0.5552,0.5552,4,0.564,0.3788,no
OPDA_PENO1,S7Z800,Prot2Text,Eukaryota,3994,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of oxopyrrolidines, polyketide-amino acid hybrid compounds with feature structures of tetramic acid. The polyketide chain is first assembled by the highly reducing PKS module of opdA using acetyl-CoA as the starter unit and five malonyl-CoA as the extender units. OpdC acts as trans-acting enoyl reductase and reduces the terminal alkenyl to alkane. The 17R in oxopyrrolidine A and 15R, 17S in oxopyrrolidine B are generated by non-stereospecific catalysis of the ketoreductase (KR) domain and enoyl reductases. Then the polyketides with specific configurations are transferred to the NRPS module of opdA and linked to L-tyrosine to form an amide bond. Finally, the oxopyrrolidines are offloaded through a Dieckmann cyclization catalyzed by the terminal D domain to give a tetramic acid moiety.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcsC",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0031177,,,GO:0016747,,GO:0016746,,,0.5897,,0.5552,2,0.5725,0.3788,no
OPDA_PENO1,S7Z800,ProtT3,Eukaryota,3994,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of oxopyrrolidines, polyketide-amino acid hybrid compounds with feature structures of tetramic acid. The polyketide chain is first assembled by the highly reducing PKS module of opdA using acetyl-CoA as the starter unit and five malonyl-CoA as the extender units. OpdC acts as trans-acting enoyl reductase and reduces the terminal alkenyl to alkane. The 17R in oxopyrrolidine A and 15R, 17S in oxopyrrolidine B are generated by non-stereospecific catalysis of the ketoreductase (KR) domain and enoyl reductases. Then the polyketides with specific configurations are transferred to the NRPS module of opdA and linked to L-tyrosine to form an amide bond. Finally, the oxopyrrolidines are offloaded through a Dieckmann cyclization catalyzed by the terminal D domain to give a tetramic acid moiety.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0031177,GO:0016747,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.5897,0.5552,0.5552,0.5552,0.5552,5,0.5621,0.3788,no
OPDA_PENO1,S7Z800,ProtTale,Eukaryota,3994,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of oxopyrrolidines, polyketide-amino acid hybrid compounds with feature structures of tetramic acid. The polyketide chain is first assembled by the highly reducing PKS module of opdA using acetyl-CoA as the starter unit and five malonyl-CoA as the extender units. OpdC acts as trans-acting enoyl reductase and reduces the terminal alkenyl to alkane. The 17R in oxopyrrolidine A and 15R, 17S in oxopyrrolidine B are generated by non-stereospecific catalysis of the ketoreductase (KR) domain and enoyl reductases. Then the polyketides with specific configurations are transferred to the NRPS module of opdA and linked to L-tyrosine to form an amide bond. Finally, the oxopyrrolidines are offloaded through a Dieckmann cyclization catalyzed by the terminal D domain to give a tetramic acid moiety.","Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the",Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0031177,GO:0016747,GO:0016747; GO:0016874,GO:0031177; GO:0016874; GO:0016746,GO:0016746,,0.5897,0.738,0.8429,0.5552,,4,0.6815,0.3788,no
OPDA_PENO1,S7Z800,Protein2Text,Eukaryota,3994,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of oxopyrrolidines, polyketide-amino acid hybrid compounds with feature structures of tetramic acid. The polyketide chain is first assembled by the highly reducing PKS module of opdA using acetyl-CoA as the starter unit and five malonyl-CoA as the extender units. OpdC acts as trans-acting enoyl reductase and reduces the terminal alkenyl to alkane. The 17R in oxopyrrolidine A and 15R, 17S in oxopyrrolidine B are generated by non-stereospecific catalysis of the ketoreductase (KR) domain and enoyl reductases. Then the polyketides with specific configurations are transferred to the NRPS module of opdA and linked to L-tyrosine to form an amide bond. Finally, the oxopyrrolidines are offloaded through a Dieckmann cyclization catalyzed by the terminal D domain to give a tetramic acid moiety.","The molecular function of this protein is related to fatty acid synthesis. It is involved in the synthesis of fatty acids, which are essential components of cellular membranes and energy storage molecules. This protein is likely to be a key enzyme in the fatty acid synthesis pathway, catalyzing a specific reaction that contributes to the production of fatty acids.",Vague,No,Vague,No,Vague,not-Yes,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0031177,,,,,,,,,,,0,,0.3788,no
OPDA_PENO1,S7Z800,Reference,Eukaryota,3994,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of oxopyrrolidines, polyketide-amino acid hybrid compounds with feature structures of tetramic acid. The polyketide chain is first assembled by the highly reducing PKS module of opdA using acetyl-CoA as the starter unit and five malonyl-CoA as the extender units. OpdC acts as trans-acting enoyl reductase and reduces the terminal alkenyl to alkane. The 17R in oxopyrrolidine A and 15R, 17S in oxopyrrolidine B are generated by non-stereospecific catalysis of the ketoreductase (KR) domain and enoyl reductases. Then the polyketides with specific configurations are transferred to the NRPS module of opdA and linked to L-tyrosine to form an amide bond. Finally, the oxopyrrolidines are offloaded through a Dieckmann cyclization catalyzed by the terminal D domain to give a tetramic acid moiety.","Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of oxopyrrolidines, polyketide-amino acid hybrid compounds with feature structures of tetramic acid. The polyketide chain is first assembled by the highly reducing PKS module of opdA using acetyl-CoA as the starter unit and five malonyl-CoA as the extender units. OpdC acts as trans-acting enoyl reductase and reduces the terminal alkenyl to alkane. The 17R in oxopyrrolidine A and 15R, 17S in oxopyrrolidine B are generated by non-stereospecific catalysis of the ketoreductase (KR) domain and enoyl reductases. Then the polyketides with specific configurations are transferred to the NRPS module of opdA and linked to L-tyrosine to form an amide bond. Finally, the oxopyrrolidines are offloaded through a Dieckmann cyclization catalyzed by the terminal D domain to give a tetramic acid moiety.",,,,,,,GO:0004315; GO:0004312; GO:0016874; GO:0008168; GO:0031177,GO:0031177; GO:0016747,GO:0004315; GO:0008927,,GO:0016874; GO:0016746,,0.778,0.5599,,0.6958,,3,0.6779,0.3788,no
CET_TOXGM,S8F0G9,ESM2Text,Eukaryota,920,First step of mRNA capping (Probable). Converts the 5'- triphosphate end of a nascent mRNA chain into a diphosphate end. Essential for parasite growth.,"Subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (SNF1), whereas AMP-enriched membranes increase the number of alpha subunits forming a nucleation-promoting complex (NPCC).",No,No,No,No,No,not-Yes,GO:0140818; GO:0004651,,,GO:0005524,GO:0005524,GO:0005524,,,0.0522,0.0522,0.0522,3,0.0522,0.4793,no
CET_TOXGM,S8F0G9,Prot2Text,Eukaryota,920,First step of mRNA capping (Probable). Converts the 5'- triphosphate end of a nascent mRNA chain into a diphosphate end. Essential for parasite growth.,"Chromosomal protein required for the assembly of the 20S proteasome. Required for ubiquitination and degradation of MDM2, thereby playing a central role in the maintenance of protein homeostasis.",No,No,No,No,No,not-Yes,GO:0140818; GO:0004651,,,,,,,,,,,0,,0.4793,no
CET_TOXGM,S8F0G9,ProtT3,Eukaryota,920,First step of mRNA capping (Probable). Converts the 5'- triphosphate end of a nascent mRNA chain into a diphosphate end. Essential for parasite growth.,"Catalytic subunit of the mRNA cap-binding complex (CBC), which binds cotranscriptionally to the 5'-cap structure of pre-mRNAs and is involved in various processes such as pre-mRNA splicing and RNA-mediated gene silencing (RNAi). The CBC complex is involved in miRNA-mediated RNA interference via its interaction with Ars2 and is required for primary microRNAs (miRNAs) processing. Also involved in innate immunity via the short interfering RNAs (siRNAs) processing machinery by restricting the viral RNA production. In the CBC complex, Pbs2 recognizes and binds capped RNAs (",No,No,No,Maybe,Maybe,not-Yes,GO:0140818; GO:0004651,GO:0003723,GO:0000339,GO:0000340,GO:0000340,GO:0000339,0.1102,0.0913,0.078,0.078,0.0913,5,0.0898,0.4793,no
CET_TOXGM,S8F0G9,ProtTale,Eukaryota,920,First step of mRNA capping (Probable). Converts the 5'- triphosphate end of a nascent mRNA chain into a diphosphate end. Essential for parasite growth.,"Capsid vertex-specific component that plays a role during viral DNA encapsidation, assuring correct genome cleavage and presumably stabilizing capsids that contain full-length viral genomes. Participates in the interaction between the capsid and the tegument through interaction with the large tegument protein/LTP.",No,No,No,No,No,not-Yes,GO:0140818; GO:0004651,,,,,,,,,,,0,,0.4793,no
CET_TOXGM,S8F0G9,Protein2Text,Eukaryota,920,First step of mRNA capping (Probable). Converts the 5'- triphosphate end of a nascent mRNA chain into a diphosphate end. Essential for parasite growth.,"The molecular function of this protein is not specified in the provided information. However, based on the name ""E3 ubiquitin-protein ligase"" and its involvement in cellular processes, it is likely that this protein is involved in the regulation of protein degradation through the ubiquitin-proteasome pathway. Specifically, it may catalyze the transfer of ubiquitin from E2 ubiquitin-conjugating enzymes to target proteins, marking them for degradation by the proteasome.",No,No,No,No,No,not-Yes,GO:0140818; GO:0004651,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.1421,0.1421,0.1421,0.1421,0.1421,5,0.1421,0.4793,no
CET_TOXGM,S8F0G9,Reference,Eukaryota,920,First step of mRNA capping (Probable). Converts the 5'- triphosphate end of a nascent mRNA chain into a diphosphate end. Essential for parasite growth.,First step of mRNA capping (Probable). Converts the 5'- triphosphate end of a nascent mRNA chain into a diphosphate end. Essential for parasite growth.,,,,,,,GO:0140818; GO:0004651,GO:0004651,GO:0004651,GO:0004651,GO:0004651; GO:0003723,GO:0004651,0.747,0.747,0.747,0.5883,0.747,5,0.7153,0.4793,no
CDPK7_TOXGM,S8G6L4,ESM2Text,Eukaryota,2133,"Plays a role in early steps of parasite division. Contributes to the close positioning of daughter cells during division and supports the establishment of polarity of the budding. Involved in maintaining centrosome integrity, which is required for the initiation of endodyogeny. Involved in regulation of protein trafficking via phosphorylation of RAB11A at 'Ser-207'. Involved in regulation of phosphatidylethanolamine synthesis via phosphorylation of proteins involved in the respective pathways, such as GPAT. Binds monophosphate phosphoinositides: phosphatidylinositol 3-phosphate, phosphatidylinositol 4-phosphate and phosphatidylinositol 5-phosphate.",Functions as a calcium-regulated second messenger for RhoA and RhoB GTPases. May be involved in endocytic membrane assembly by recruiting other proteins to the membrane. Binds calcium.,No,No,No,No,No,not-Yes,GO:0005524; GO:0005509; GO:0106310; GO:0004674,GO:0005509,GO:0005509,GO:0005509,GO:0005509,GO:0005509,0.4793,0.4793,0.4793,0.4793,0.4793,5,0.4793,0.5779,yes
CDPK7_TOXGM,S8G6L4,Prot2Text,Eukaryota,2133,"Plays a role in early steps of parasite division. Contributes to the close positioning of daughter cells during division and supports the establishment of polarity of the budding. Involved in maintaining centrosome integrity, which is required for the initiation of endodyogeny. Involved in regulation of protein trafficking via phosphorylation of RAB11A at 'Ser-207'. Involved in regulation of phosphatidylethanolamine synthesis via phosphorylation of proteins involved in the respective pathways, such as GPAT. Binds monophosphate phosphoinositides: phosphatidylinositol 3-phosphate, phosphatidylinositol 4-phosphate and phosphatidylinositol 5-phosphate.",Functions as a calcium-regulated second messenger for RhoA and RhoB GTPases. May be involved in endocytic membrane assembly by recruiting other proteins to the membrane. Binds calcium.,No,No,No,No,No,not-Yes,GO:0005524; GO:0005509; GO:0106310; GO:0004674,GO:0005509,GO:0005509,GO:0005509,GO:0005509,GO:0005509,0.4793,0.4793,0.4793,0.4793,0.4793,5,0.4793,0.5779,yes
CDPK7_TOXGM,S8G6L4,ProtT3,Eukaryota,2133,"Plays a role in early steps of parasite division. Contributes to the close positioning of daughter cells during division and supports the establishment of polarity of the budding. Involved in maintaining centrosome integrity, which is required for the initiation of endodyogeny. Involved in regulation of protein trafficking via phosphorylation of RAB11A at 'Ser-207'. Involved in regulation of phosphatidylethanolamine synthesis via phosphorylation of proteins involved in the respective pathways, such as GPAT. Binds monophosphate phosphoinositides: phosphatidylinositol 3-phosphate, phosphatidylinositol 4-phosphate and phosphatidylinositol 5-phosphate.",Acts as a regulator of Ca(2+) release from intracellular stores in a Ca(2+)-independent manner (By similarity). Contributes to store-operated Ca(2+) entry (SOCE) in a Ca(2+)-independent manner (By similarity). Contributes to store-operated Ca(2+) entry (SOCE) in a Ca(2+)-independent manner (By similarity). Contributes to store-operated Ca(2+) entry (SOCE) in a Ca(2+)-independent manner,No,No,No,No,No,not-Yes,GO:0005524; GO:0005509; GO:0106310; GO:0004674,,,,,,,,,,,0,,0.5779,yes
CDPK7_TOXGM,S8G6L4,ProtTale,Eukaryota,2133,"Plays a role in early steps of parasite division. Contributes to the close positioning of daughter cells during division and supports the establishment of polarity of the budding. Involved in maintaining centrosome integrity, which is required for the initiation of endodyogeny. Involved in regulation of protein trafficking via phosphorylation of RAB11A at 'Ser-207'. Involved in regulation of phosphatidylethanolamine synthesis via phosphorylation of proteins involved in the respective pathways, such as GPAT. Binds monophosphate phosphoinositides: phosphatidylinositol 3-phosphate, phosphatidylinositol 4-phosphate and phosphatidylinositol 5-phosphate.","Serine/threonine-protein kinase which plays a central role in the MAPK/MAPK3/MAPK11 signaling pathway by phosphorylating and activating MAP2K7/MKK4 and MAP2K4/MKK3, which in turn phosphorylates MAPK8/p38alpha and MAPK8/p38beta leading to the activation of the transcription factors ATF3/p52 and ATF4/p51 and JUN/AP-1 and thus regulating the expression of genes involved in cell proliferation, cell differentiation, apoptosis, angiogenesis and migration. Acts as a negative regulator of angiogenesis by phosphorylating MAP",No,No,No,No,No,not-Yes,GO:0005524; GO:0005509; GO:0106310; GO:0004674,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0004709,0.8459,0.589,0.8459,0.8459,0.6424,5,0.7538,0.5779,yes
CDPK7_TOXGM,S8G6L4,Protein2Text,Eukaryota,2133,"Plays a role in early steps of parasite division. Contributes to the close positioning of daughter cells during division and supports the establishment of polarity of the budding. Involved in maintaining centrosome integrity, which is required for the initiation of endodyogeny. Involved in regulation of protein trafficking via phosphorylation of RAB11A at 'Ser-207'. Involved in regulation of phosphatidylethanolamine synthesis via phosphorylation of proteins involved in the respective pathways, such as GPAT. Binds monophosphate phosphoinositides: phosphatidylinositol 3-phosphate, phosphatidylinositol 4-phosphate and phosphatidylinositol 5-phosphate.","The molecular function of this protein is that it acts as a scaffold protein, meaning it provides a structural framework for other proteins to assemble and interact with each other. It is involved in organizing the cytoskeleton, which is a network of protein filaments that provides structural support and shape to cells.",Vague,No,No,No,Vague,not-Yes,GO:0005524; GO:0005509; GO:0106310; GO:0004674,,,,,,,,,,,0,,0.5779,yes
CDPK7_TOXGM,S8G6L4,Reference,Eukaryota,2133,"Plays a role in early steps of parasite division. Contributes to the close positioning of daughter cells during division and supports the establishment of polarity of the budding. Involved in maintaining centrosome integrity, which is required for the initiation of endodyogeny. Involved in regulation of protein trafficking via phosphorylation of RAB11A at 'Ser-207'. Involved in regulation of phosphatidylethanolamine synthesis via phosphorylation of proteins involved in the respective pathways, such as GPAT. Binds monophosphate phosphoinositides: phosphatidylinositol 3-phosphate, phosphatidylinositol 4-phosphate and phosphatidylinositol 5-phosphate.","Plays a role in early steps of parasite division. Contributes to the close positioning of daughter cells during division and supports the establishment of polarity of the budding. Involved in maintaining centrosome integrity, which is required for the initiation of endodyogeny. Involved in regulation of protein trafficking via phosphorylation of RAB11A at 'Ser-207'. Involved in regulation of phosphatidylethanolamine synthesis via phosphorylation of proteins involved in the respective pathways, such as GPAT. Binds monophosphate phosphoinositides: phosphatidylinositol 3-phosphate, phosphatidylinositol 4-phosphate and phosphatidylinositol 5-phosphate.",,,,,,,GO:0005524; GO:0005509; GO:0106310; GO:0004674,GO:0004674; GO:0005546,GO:0004674,GO:0004674,GO:0004674; GO:0005524; GO:0008289,GO:0004672,0.6184,0.589,0.589,0.7793,0.5748,5,0.6301,0.5779,yes
AMBP3_FISAU,V5TDY7,ESM2Text,Bacteria,322,"Prenyltransferase involved in the biosynthesis of ambiguines, a family of hapalindole-type alkaloids. Catalyzes the reverse prenylation of hapalindole G or U at the C2 position with dimethylallyl diphosphate (DMAPP) to generate ambiguine A or H, respectively. In addition, accepts hapalindole A, an epimer of hapalindole G, and catalyzes normal prenylation at its C2 position.","Monooxygenase that catalyzes the O-prenylation of phosphoenolpyruvate (PEP) to yield the bis-prenylated monolignols phthalate and pyruvate. In vitro, can also use NTP, CTP, GTP, UTP, dTTP or CTP as substrate.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004659,,GO:0004497,,,GO:0004497,,0.3284,,,0.3284,2,0.3284,0.498,no
AMBP3_FISAU,V5TDY7,Prot2Text,Bacteria,322,"Prenyltransferase involved in the biosynthesis of ambiguines, a family of hapalindole-type alkaloids. Catalyzes the reverse prenylation of hapalindole G or U at the C2 position with dimethylallyl diphosphate (DMAPP) to generate ambiguine A or H, respectively. In addition, accepts hapalindole A, an epimer of hapalindole G, and catalyzes normal prenylation at its C2 position.",Magnesium-independent aromatic prenyltransferase that catalyzes the irreversible transfer of a dimethylallyl group to 4-hydroxyphenylpyruvate to produce the ring A structure in the clorobiocin biosynthesis pathway. Clorobiocin is an aminocoumarin family antibiotic.,Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0016765,GO:0004659,1.0,1.0,1.0,0.8416,1.0,5,0.9683,0.498,no
AMBP3_FISAU,V5TDY7,ProtT3,Bacteria,322,"Prenyltransferase involved in the biosynthesis of ambiguines, a family of hapalindole-type alkaloids. Catalyzes the reverse prenylation of hapalindole G or U at the C2 position with dimethylallyl diphosphate (DMAPP) to generate ambiguine A or H, respectively. In addition, accepts hapalindole A, an epimer of hapalindole G, and catalyzes normal prenylation at its C2 position.",Catalyzes the decarboxylation of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family,No,No,No,No,No,not-Yes,GO:0004659,GO:0003856,GO:0003856,GO:0003856,GO:0003856,GO:0003856,0.2353,0.2353,0.2353,0.2353,0.2353,5,0.2353,0.498,no
AMBP3_FISAU,V5TDY7,ProtTale,Bacteria,322,"Prenyltransferase involved in the biosynthesis of ambiguines, a family of hapalindole-type alkaloids. Catalyzes the reverse prenylation of hapalindole G or U at the C2 position with dimethylallyl diphosphate (DMAPP) to generate ambiguine A or H, respectively. In addition, accepts hapalindole A, an epimer of hapalindole G, and catalyzes normal prenylation at its C2 position.",S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Probably methylates N-4 position of wybutosine-86 to produce wybutosine-72.,No,No,No,No,No,not-Yes,GO:0004659,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.4645,0.4645,0.4645,0.4645,0.4645,5,0.4645,0.498,no
AMBP3_FISAU,V5TDY7,Protein2Text,Bacteria,322,"Prenyltransferase involved in the biosynthesis of ambiguines, a family of hapalindole-type alkaloids. Catalyzes the reverse prenylation of hapalindole G or U at the C2 position with dimethylallyl diphosphate (DMAPP) to generate ambiguine A or H, respectively. In addition, accepts hapalindole A, an epimer of hapalindole G, and catalyzes normal prenylation at its C2 position.","This protein is likely involved in the synthesis of a plant growth regulator, specifically indole-3-acetic acid (IAA). The molecular function of this protein is likely to be a decarboxylase, catalyzing the decarboxylation of indole-3-pyruvic acid to IAA. This is a key step in the biosynthesis of IAA, a plant hormone that plays a crucial role in plant growth and development. 
The molecular function of this protein can be summarized as follows:

* Catalyzing the decarboxylation of indole-3-pyruvic acid to indole-3-acetic acid (IAA)
* Involved in the biosynthesis of IAA, a plant hormone that plays a crucial role in plant growth and development. 

This protein is likely a part of the indole-3-pyruvic acid decarboxylase enzyme, which catalyzes the decarboxylation of indole-3-pyruvic acid to IAA. The enzyme is composed of multiple subunits, and this protein is likely one of the subunits that contributes to the enzyme's catalytic activity. 

The molecular function of this protein can be summarized as follows:

* Catalyzing the decarboxylation of indole-3-pyruvic acid to indole-3-acetic acid (IAA)
* Involved in the biosynthesis of IAA, a plant hormone that plays a crucial role in plant growth and development. 

This protein is likely a part of the indole-3-pyruvic acid decarboxylase enzyme, which catalyzes the decarboxylation of indole-3-pyruvic acid to IAA. The enzyme is composed of multiple subunits, and this protein is likely one of the subunits that contributes to the enzyme's catalytic activity. 

The molecular function of this protein can be summarized as follows:

* Catalyzing the decarboxylation of indole-3-pyruvic acid to indole-3-acetic acid (IAA)
* Involved in the biosynthesis of IAA, a plant hormone that plays a crucial role in plant growth and development. 

This protein is likely a part of the indole-3-pyruvic acid decarboxylase enzyme, which catalyzes the decarboxylation of indole-3-pyruvic acid to IAA. The enzyme is composed of multiple subunits, and this",No,No,No,No,No,not-Yes,GO:0004659,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.2742,0.2742,0.2742,0.2742,0.2742,5,0.2742,0.498,no
AMBP3_FISAU,V5TDY7,Reference,Bacteria,322,"Prenyltransferase involved in the biosynthesis of ambiguines, a family of hapalindole-type alkaloids. Catalyzes the reverse prenylation of hapalindole G or U at the C2 position with dimethylallyl diphosphate (DMAPP) to generate ambiguine A or H, respectively. In addition, accepts hapalindole A, an epimer of hapalindole G, and catalyzes normal prenylation at its C2 position.","Prenyltransferase involved in the biosynthesis of ambiguines, a family of hapalindole-type alkaloids. Catalyzes the reverse prenylation of hapalindole G or U at the C2 position with dimethylallyl diphosphate (DMAPP) to generate ambiguine A or H, respectively. In addition, accepts hapalindole A, an epimer of hapalindole G, and catalyzes normal prenylation at its C2 position.",,,,,,,GO:0004659,GO:0004659,GO:0004659,GO:0016765,GO:0004659,GO:0004659,1.0,1.0,0.8416,1.0,1.0,5,0.9683,0.498,no
XY43A_HUMIN,V9TNS0,ESM2Text,Eukaryota,327,"Bifunctional beta-xylosidase/alpha-L-arabinosidases with a low level of xylanase activity. Is most active on 4- nitrophenyl beta-D-xylopyranoside (pNPX) (defined as 100%), moderate on p-nitrophenyl-alpha-L-arabinofuranoside (pNPA) (23.7%), and weak on beechwood xylan (15.9%) and birchwood xylan (15.2%). Is able to attack xylooligosacchardies with degrees of polymerisation of 2-5, releasing the amounts of reducing sugars in the order of xylopentose > xylotetraose > xylotriose > xylobiose, i.e. the rate of xylose released from xylooligosacchardies increased with the chain length. No activity is detected in the presence of carboxymethyl cellulose-sodium (CMC-Na), sugar beet arabinan, AZCL- arabinan (debranched), 4-nitrophenyl a-D - galactopyranoside, 2- nitrophenyl beta-D-galactopyranoside, and 4-nitrophenyl alpha-D- glucopyranoside.",Intracellular invertase that cleaves sucrose into glucose and fructose and is involved in the regulation of grain size. Invertase activity on linear and branched substrates may be modulated by growth factors and the presence of auxin modulating factors.,No,No,No,No,No,not-Yes,GO:0046556; GO:0009044,GO:0004564,GO:0004564,GO:0004564,GO:0004564,GO:0004564,0.6971,0.6971,0.6971,0.6971,0.6971,5,0.6971,0.1926,no
XY43A_HUMIN,V9TNS0,Prot2Text,Eukaryota,327,"Bifunctional beta-xylosidase/alpha-L-arabinosidases with a low level of xylanase activity. Is most active on 4- nitrophenyl beta-D-xylopyranoside (pNPX) (defined as 100%), moderate on p-nitrophenyl-alpha-L-arabinofuranoside (pNPA) (23.7%), and weak on beechwood xylan (15.9%) and birchwood xylan (15.2%). Is able to attack xylooligosacchardies with degrees of polymerisation of 2-5, releasing the amounts of reducing sugars in the order of xylopentose > xylotetraose > xylotriose > xylobiose, i.e. the rate of xylose released from xylooligosacchardies increased with the chain length. No activity is detected in the presence of carboxymethyl cellulose-sodium (CMC-Na), sugar beet arabinan, AZCL- arabinan (debranched), 4-nitrophenyl a-D - galactopyranoside, 2- nitrophenyl beta-D-galactopyranoside, and 4-nitrophenyl alpha-D- glucopyranoside.",Exoxylanase capable of acting on certain xylans and xylooligosaccharides.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046556; GO:0009044,GO:0009044,GO:0031176,GO:0009044,GO:0009044,GO:0009044,0.8778,0.7091,0.8778,0.8778,0.8778,5,0.8441,0.1926,no
XY43A_HUMIN,V9TNS0,ProtT3,Eukaryota,327,"Bifunctional beta-xylosidase/alpha-L-arabinosidases with a low level of xylanase activity. Is most active on 4- nitrophenyl beta-D-xylopyranoside (pNPX) (defined as 100%), moderate on p-nitrophenyl-alpha-L-arabinofuranoside (pNPA) (23.7%), and weak on beechwood xylan (15.9%) and birchwood xylan (15.2%). Is able to attack xylooligosacchardies with degrees of polymerisation of 2-5, releasing the amounts of reducing sugars in the order of xylopentose > xylotetraose > xylotriose > xylobiose, i.e. the rate of xylose released from xylooligosacchardies increased with the chain length. No activity is detected in the presence of carboxymethyl cellulose-sodium (CMC-Na), sugar beet arabinan, AZCL- arabinan (debranched), 4-nitrophenyl a-D - galactopyranoside, 2- nitrophenyl beta-D-galactopyranoside, and 4-nitrophenyl alpha-D- glucopyranoside.","Alpha-L-arabinofuranosidase involved in the hydrolysis of arabinoxylan, a major component of plant hemicellulose. Releases L-arabinose from arabinoxylan (By similarity). Secreted. Belongs to the glycosyl hydrolase 43 family",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046556; GO:0009044,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,0.8778,0.8778,0.8778,0.8778,0.8778,5,0.8778,0.1926,no
XY43A_HUMIN,V9TNS0,ProtTale,Eukaryota,327,"Bifunctional beta-xylosidase/alpha-L-arabinosidases with a low level of xylanase activity. Is most active on 4- nitrophenyl beta-D-xylopyranoside (pNPX) (defined as 100%), moderate on p-nitrophenyl-alpha-L-arabinofuranoside (pNPA) (23.7%), and weak on beechwood xylan (15.9%) and birchwood xylan (15.2%). Is able to attack xylooligosacchardies with degrees of polymerisation of 2-5, releasing the amounts of reducing sugars in the order of xylopentose > xylotetraose > xylotriose > xylobiose, i.e. the rate of xylose released from xylooligosacchardies increased with the chain length. No activity is detected in the presence of carboxymethyl cellulose-sodium (CMC-Na), sugar beet arabinan, AZCL- arabinan (debranched), 4-nitrophenyl a-D - galactopyranoside, 2- nitrophenyl beta-D-galactopyranoside, and 4-nitrophenyl alpha-D- glucopyranoside.","Involved in the degradation of ulvan, a linear polysaccharide composed of D- glucuronic acid (GlcA), D-xylose (Xyl), L-rhamnose (Rha) and D- glucuronate (GlcA). Catalyzes the hydrolysis of the beta-1,4-glucuronic acid (GlcA-GlcA) linkage to yield xylo-oligosaccharides (XOS) with a degree of polymerization (DP) between 2 and 10.",No,No,No,No,No,not-Yes,GO:0046556; GO:0009044,GO:0004553,GO:0016798,GO:0016798,GO:0004553,GO:0004553,0.8234,0.7015,0.7015,0.8234,0.8234,5,0.7746,0.1926,no
XY43A_HUMIN,V9TNS0,Protein2Text,Eukaryota,327,"Bifunctional beta-xylosidase/alpha-L-arabinosidases with a low level of xylanase activity. Is most active on 4- nitrophenyl beta-D-xylopyranoside (pNPX) (defined as 100%), moderate on p-nitrophenyl-alpha-L-arabinofuranoside (pNPA) (23.7%), and weak on beechwood xylan (15.9%) and birchwood xylan (15.2%). Is able to attack xylooligosacchardies with degrees of polymerisation of 2-5, releasing the amounts of reducing sugars in the order of xylopentose > xylotetraose > xylotriose > xylobiose, i.e. the rate of xylose released from xylooligosacchardies increased with the chain length. No activity is detected in the presence of carboxymethyl cellulose-sodium (CMC-Na), sugar beet arabinan, AZCL- arabinan (debranched), 4-nitrophenyl a-D - galactopyranoside, 2- nitrophenyl beta-D-galactopyranoside, and 4-nitrophenyl alpha-D- glucopyranoside.","The molecular function of this protein is unknown. However, based on its classification as a beta-galactosidase, it is likely that it has a hydrolytic activity towards beta-galactosides. Further research is needed to determine the specific molecular function of this protein.",No,No,No,No,No,not-Yes,GO:0046556; GO:0009044,GO:0004565,GO:0004565,GO:0004565,GO:0004565,GO:0004565,0.6039,0.6039,0.6039,0.6039,0.6039,5,0.6039,0.1926,no
XY43A_HUMIN,V9TNS0,Reference,Eukaryota,327,"Bifunctional beta-xylosidase/alpha-L-arabinosidases with a low level of xylanase activity. Is most active on 4- nitrophenyl beta-D-xylopyranoside (pNPX) (defined as 100%), moderate on p-nitrophenyl-alpha-L-arabinofuranoside (pNPA) (23.7%), and weak on beechwood xylan (15.9%) and birchwood xylan (15.2%). Is able to attack xylooligosacchardies with degrees of polymerisation of 2-5, releasing the amounts of reducing sugars in the order of xylopentose > xylotetraose > xylotriose > xylobiose, i.e. the rate of xylose released from xylooligosacchardies increased with the chain length. No activity is detected in the presence of carboxymethyl cellulose-sodium (CMC-Na), sugar beet arabinan, AZCL- arabinan (debranched), 4-nitrophenyl a-D - galactopyranoside, 2- nitrophenyl beta-D-galactopyranoside, and 4-nitrophenyl alpha-D- glucopyranoside.","Bifunctional beta-xylosidase/alpha-L-arabinosidases with a low level of xylanase activity. Is most active on 4- nitrophenyl beta-D-xylopyranoside (pNPX) (defined as 100%), moderate on p-nitrophenyl-alpha-L-arabinofuranoside (pNPA) (23.7%), and weak on beechwood xylan (15.9%) and birchwood xylan (15.2%). Is able to attack xylooligosacchardies with degrees of polymerisation of 2-5, releasing the amounts of reducing sugars in the order of xylopentose > xylotetraose > xylotriose > xylobiose, i.e. the rate of xylose released from xylooligosacchardies increased with the chain length. No activity is detected in the presence of carboxymethyl cellulose-sodium (CMC-Na), sugar beet arabinan, AZCL- arabinan (debranched), 4-nitrophenyl a-D - galactopyranoside, 2- nitrophenyl beta-D-galactopyranoside, and 4-nitrophenyl alpha-D- glucopyranoside.",,,,,,,GO:0046556; GO:0009044,GO:0009044; GO:0046556,GO:0009044; GO:0046556,GO:0009044,GO:0009044; GO:0046556,GO:0009044; GO:0046556,1.0,1.0,0.8778,1.0,1.0,5,0.9756,0.1926,no
XY43B_HUMIN,V9TT49,ESM2Text,Eukaryota,538,"Bifunctional beta-xylosidase/alpha-L-arabinosidases with a low level of xylanase activity. Is most active on 4- nitrophenyl beta-D-xylopyranoside (pNPX) (defined as 100%), moderate on p-nitrophenyl-alpha-L-arabinofuranoside (pNPA) (56.6%), and weak on beechwood xylan (5.7%) and birchwood xylan (2.7%). Is able to attack xylooligosacchardies with degrees of polymerisation of 2-5, releasing the amounts of reducing sugars in the order of xylopentose > xylotetraose > xylotriose > xylobiose, i.e. the rate of xylose released from xylooligosacchardies increased with the chain length. No activity was detected in the presence of carboxymethyl cellulose-sodium (CMC-Na), sugar beet arabinan, AZCL- arabinan (debranched), 4-nitrophenyl a-D - galactopyranoside, 2- nitrophenyl beta-D-galactopyranoside, and 4-nitrophenyl alpha-D- glucopyranoside.","Beta-1,3-xylosidase that directly activates the O-antigen in the presence of alpha-D-xylose, leading to the degradation of the non-antifungal polysaccharide xylobiose.",Maybe,No,No,No,Maybe,not-Yes,GO:0046556; GO:0009044,GO:0009044,GO:0004553,GO:0016798,GO:0004553,GO:0016798,0.8778,0.8234,0.7015,0.8234,0.7015,5,0.7855,0.2971,no
XY43B_HUMIN,V9TT49,Prot2Text,Eukaryota,538,"Bifunctional beta-xylosidase/alpha-L-arabinosidases with a low level of xylanase activity. Is most active on 4- nitrophenyl beta-D-xylopyranoside (pNPX) (defined as 100%), moderate on p-nitrophenyl-alpha-L-arabinofuranoside (pNPA) (56.6%), and weak on beechwood xylan (5.7%) and birchwood xylan (2.7%). Is able to attack xylooligosacchardies with degrees of polymerisation of 2-5, releasing the amounts of reducing sugars in the order of xylopentose > xylotetraose > xylotriose > xylobiose, i.e. the rate of xylose released from xylooligosacchardies increased with the chain length. No activity was detected in the presence of carboxymethyl cellulose-sodium (CMC-Na), sugar beet arabinan, AZCL- arabinan (debranched), 4-nitrophenyl a-D - galactopyranoside, 2- nitrophenyl beta-D-galactopyranoside, and 4-nitrophenyl alpha-D- glucopyranoside.",Enables the bacterium to metabolize sucrose as a sole carbon source.,No,No,No,No,No,not-Yes,GO:0046556; GO:0009044,,,,,,,,,,,0,,0.2971,no
XY43B_HUMIN,V9TT49,ProtT3,Eukaryota,538,"Bifunctional beta-xylosidase/alpha-L-arabinosidases with a low level of xylanase activity. Is most active on 4- nitrophenyl beta-D-xylopyranoside (pNPX) (defined as 100%), moderate on p-nitrophenyl-alpha-L-arabinofuranoside (pNPA) (56.6%), and weak on beechwood xylan (5.7%) and birchwood xylan (2.7%). Is able to attack xylooligosacchardies with degrees of polymerisation of 2-5, releasing the amounts of reducing sugars in the order of xylopentose > xylotetraose > xylotriose > xylobiose, i.e. the rate of xylose released from xylooligosacchardies increased with the chain length. No activity was detected in the presence of carboxymethyl cellulose-sodium (CMC-Na), sugar beet arabinan, AZCL- arabinan (debranched), 4-nitrophenyl a-D - galactopyranoside, 2- nitrophenyl beta-D-galactopyranoside, and 4-nitrophenyl alpha-D- glucopyranoside.","Involved in the degradation of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Belongs to the glycosyl hydrolase 43 family",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046556; GO:0009044,GO:0016798,GO:0016798,GO:0016798,GO:0016798,GO:0016798,0.7015,0.7015,0.7015,0.7015,0.7015,5,0.7015,0.2971,no
XY43B_HUMIN,V9TT49,ProtTale,Eukaryota,538,"Bifunctional beta-xylosidase/alpha-L-arabinosidases with a low level of xylanase activity. Is most active on 4- nitrophenyl beta-D-xylopyranoside (pNPX) (defined as 100%), moderate on p-nitrophenyl-alpha-L-arabinofuranoside (pNPA) (56.6%), and weak on beechwood xylan (5.7%) and birchwood xylan (2.7%). Is able to attack xylooligosacchardies with degrees of polymerisation of 2-5, releasing the amounts of reducing sugars in the order of xylopentose > xylotetraose > xylotriose > xylobiose, i.e. the rate of xylose released from xylooligosacchardies increased with the chain length. No activity was detected in the presence of carboxymethyl cellulose-sodium (CMC-Na), sugar beet arabinan, AZCL- arabinan (debranched), 4-nitrophenyl a-D - galactopyranoside, 2- nitrophenyl beta-D-galactopyranoside, and 4-nitrophenyl alpha-D- glucopyranoside.",Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan.,Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046556; GO:0009044,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0004553,0.8778,0.8778,0.8778,0.8778,0.8234,5,0.8669,0.2971,no
XY43B_HUMIN,V9TT49,Protein2Text,Eukaryota,538,"Bifunctional beta-xylosidase/alpha-L-arabinosidases with a low level of xylanase activity. Is most active on 4- nitrophenyl beta-D-xylopyranoside (pNPX) (defined as 100%), moderate on p-nitrophenyl-alpha-L-arabinofuranoside (pNPA) (56.6%), and weak on beechwood xylan (5.7%) and birchwood xylan (2.7%). Is able to attack xylooligosacchardies with degrees of polymerisation of 2-5, releasing the amounts of reducing sugars in the order of xylopentose > xylotetraose > xylotriose > xylobiose, i.e. the rate of xylose released from xylooligosacchardies increased with the chain length. No activity was detected in the presence of carboxymethyl cellulose-sodium (CMC-Na), sugar beet arabinan, AZCL- arabinan (debranched), 4-nitrophenyl a-D - galactopyranoside, 2- nitrophenyl beta-D-galactopyranoside, and 4-nitrophenyl alpha-D- glucopyranoside.","The molecular function of this protein is a carbohydrate metabolic enzyme, specifically a sucrose phosphorylase.",No,No,No,No,No,not-Yes,GO:0046556; GO:0009044,GO:0016157,GO:0016157,GO:0016157,GO:0016157,,0.144,0.144,0.144,0.144,,4,0.144,0.2971,no
XY43B_HUMIN,V9TT49,Reference,Eukaryota,538,"Bifunctional beta-xylosidase/alpha-L-arabinosidases with a low level of xylanase activity. Is most active on 4- nitrophenyl beta-D-xylopyranoside (pNPX) (defined as 100%), moderate on p-nitrophenyl-alpha-L-arabinofuranoside (pNPA) (56.6%), and weak on beechwood xylan (5.7%) and birchwood xylan (2.7%). Is able to attack xylooligosacchardies with degrees of polymerisation of 2-5, releasing the amounts of reducing sugars in the order of xylopentose > xylotetraose > xylotriose > xylobiose, i.e. the rate of xylose released from xylooligosacchardies increased with the chain length. No activity was detected in the presence of carboxymethyl cellulose-sodium (CMC-Na), sugar beet arabinan, AZCL- arabinan (debranched), 4-nitrophenyl a-D - galactopyranoside, 2- nitrophenyl beta-D-galactopyranoside, and 4-nitrophenyl alpha-D- glucopyranoside.","Bifunctional beta-xylosidase/alpha-L-arabinosidases with a low level of xylanase activity. Is most active on 4- nitrophenyl beta-D-xylopyranoside (pNPX) (defined as 100%), moderate on p-nitrophenyl-alpha-L-arabinofuranoside (pNPA) (56.6%), and weak on beechwood xylan (5.7%) and birchwood xylan (2.7%). Is able to attack xylooligosacchardies with degrees of polymerisation of 2-5, releasing the amounts of reducing sugars in the order of xylopentose > xylotetraose > xylotriose > xylobiose, i.e. the rate of xylose released from xylooligosacchardies increased with the chain length. No activity was detected in the presence of carboxymethyl cellulose-sodium (CMC-Na), sugar beet arabinan, AZCL- arabinan (debranched), 4-nitrophenyl a-D - galactopyranoside, 2- nitrophenyl beta-D-galactopyranoside, and 4-nitrophenyl alpha-D- glucopyranoside.",,,,,,,GO:0046556; GO:0009044,GO:0009044; GO:0046556,GO:0009044; GO:0046556,GO:0009044,GO:0009044; GO:0046556,GO:0009044; GO:0046556,1.0,1.0,0.8778,1.0,1.0,5,0.9756,0.2971,no
AMYG_PHOAM,W6JPP9,ESM2Text,Eukaryota,339,Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of a yet unidentified indole diterpene. AmyG catalyzes the first step in indole diterpene biosynthesis by producing geranylgeranyl diphosphate (GGPP).,"Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ. Paxilline is converted",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0004659,GO:0004337,GO:0004337,GO:0004311,GO:0004337,GO:0004337,0.5283,0.5283,0.5283,0.5283,0.5283,5,0.5283,0.2251,no
AMYG_PHOAM,W6JPP9,Prot2Text,Eukaryota,339,Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of a yet unidentified indole diterpene. AmyG catalyzes the first step in indole diterpene biosynthesis by producing geranylgeranyl diphosphate (GGPP).,"Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of the diterpenoid pyrones subglutinols A and B. The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpasA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpasD through the action of the prenyltransferase dpasC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpasE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpasB (Probable). The short chain dehydrogenase/reductase dpasF is then involved in tetrah",Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0046872; GO:0004659,GO:0004337,GO:0004337,GO:0004337,GO:0004337,GO:0004337,0.5283,0.5283,0.5283,0.5283,0.5283,5,0.5283,0.2251,no
AMYG_PHOAM,W6JPP9,ProtT3,Eukaryota,339,Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of a yet unidentified indole diterpene. AmyG catalyzes the first step in indole diterpene biosynthesis by producing geranylgeranyl diphosphate (GGPP).,"Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of notoamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first step of notoamide biosynthesis involves coupling of L-proline and L-tryptophan by the bimodular NRPS notE, to produce cyclo-L-tryptophan-L-proline called brevianamide F . The",Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0046872; GO:0004659,GO:0004311,GO:0004337,GO:0004337,GO:0016765,GO:0004311,0.5283,0.5283,0.5283,0.6032,0.5283,5,0.5433,0.2251,no
AMYG_PHOAM,W6JPP9,ProtTale,Eukaryota,339,Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of a yet unidentified indole diterpene. AmyG catalyzes the first step in indole diterpene biosynthesis by producing geranylgeranyl diphosphate (GGPP).,"Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product",Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0046872; GO:0004659,GO:0004337,GO:0004337,GO:0004311,GO:0004337,GO:0004337,0.5283,0.5283,0.5283,0.5283,0.5283,5,0.5283,0.2251,no
AMYG_PHOAM,W6JPP9,Protein2Text,Eukaryota,339,Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of a yet unidentified indole diterpene. AmyG catalyzes the first step in indole diterpene biosynthesis by producing geranylgeranyl diphosphate (GGPP).,"This protein is a part of the geranylgeranyl diphosphate synthase family, which is involved in the biosynthesis of isoprenoids, specifically the production of geranylgeranyl diphosphate (GGPP). The molecular function of this protein is to catalyze the sequential condensation of isopentenyl diphosphate with dimethylallyl diphosphate, and then with the intermediate geranyl diphosphate to produce geranylgeranyl diphosphate. This is a crucial step in the biosynthesis of isoprenoids, which are important biomolecules in plants. 

In more detail, the protein uses the substrate dimethylallyl diphosphate and isopentenyl diphosphate to produce geranyl diphosphate, and then uses geranyl diphosphate and isopentenyl diphosphate to produce geranylgeranyl diphosphate. The product geranylgeranyl diphosphate is then used as a substrate for the subsequent steps in the biosynthesis of isoprenoids. 

This protein is involved in the biosynthesis of isoprenoids, which are important biomolecules in plants. Isoprenoids are a diverse group of compounds that play important roles in plant growth and development, and are also used as defense compounds against pathogens and herbivores. The biosynthesis of isoprenoids is a complex process that involves the sequential condensation of isopentenyl diphosphate and dimethylallyl diphosphate to produce geranyl diphosphate, which is then further converted to geranylgeranyl diphosphate. This protein is a key enzyme in this process, and its activity is essential for the production of isoprenoids in plants. 

In addition to its role in the biosynthesis of isoprenoids, this protein has also been implicated in the regulation of plant growth and development. For example, it has been shown to play a role in the regulation of plant cell division and differentiation, and it has also been implicated in the regulation of plant hormone signaling pathways. 

Overall, this protein plays a critical role in the biosynthesis of isoprenoids, and its activity is essential for plant growth and development. Its molecular function is to catalyze the production of geranylgeranyl diphosphate, which is a crucial intermediate in the biosynthesis of isoprenoids. 

Geranylgeranyl diphosphate is a crucial intermediate in the biosynthesis of isoprenoids, and is used as a substrate for",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0004659,GO:0004311,GO:0004337,GO:0004311,GO:0004311,,0.5283,0.5283,0.5283,0.5283,,4,0.5283,0.2251,no
AMYG_PHOAM,W6JPP9,Reference,Eukaryota,339,Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of a yet unidentified indole diterpene. AmyG catalyzes the first step in indole diterpene biosynthesis by producing geranylgeranyl diphosphate (GGPP).,Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of a yet unidentified indole diterpene. AmyG catalyzes the first step in indole diterpene biosynthesis by producing geranylgeranyl diphosphate (GGPP).,,,,,,,GO:0046872; GO:0004659,GO:0004337,GO:0004311,GO:0004337,GO:0004337,GO:0004659,0.5283,0.5283,0.5283,0.5283,0.7015,5,0.5629,0.2251,no
FOGG_ASPRC,A0A017SEY2,ESM2Text,Eukaryota,348,"Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain. The PKS fogA releases the carboxylic acid (8E,10E,12E)-3,5,7-trihydroxytetradeca-8,10,12-trienoic acid as its product, as well as derivatives with one and two double bonds. FogA is indeed able to reduce the initial triketide, thus being at least partially responsible for the differently saturated heptyl side chains of flavoglaucin congeners. The oxidoreductases fogB, fogC and fogD modify the nascent polyketide in fogA-bound form and, together, fogA, fogB, fogC and fogD are necessary for the formation of the aromatic core and the cyclized PKS products are released as salicyl alcohols. In particular, fogB is responsible for oxidation of a hydroxyl group or reduction of remaining double bond(s) at the C-7 residue whereas fogD is probably involved in the reductive release of the modified PKS products. The cytochrome P450 monooxygenase fogE is then responsible for the hydroxylation at C-3 of the benzene ring. The fogE products are substrates of the prenyltransferase fogH and the prenylated benzyl alcohols are subsequently oxidized by the fogF to produce the final aryl aldehydes flavoglaucin and congeners. The short-chain dehydrogenase fogG does not seem to be involved in the biosynthesis of the prenylated salicylaldehyde derivatives.","Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the phytotoxin stemphyloxin II. The first step of the pathway is the synthesis of dehydroprobetaenone I by the polyketide synthase sthA and the enoyl reductase sthE via condensation of one acetyl-CoA starter unit with 7 malonyl-CoA units and 5 methylations. The C-terminal reductase (R) domain of sthA catalyzes the reductive release of the polyketide chain. Because sthA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase sthC. The short-chain dehydrogenase/reductase sthC then catalyzes reduction of dehydroprobetaenone I to probetaenone I. The cytochrome P450 monooxygenase sthF catalyzes successive epoxidation, oxidation (resulting from epoxide opening) and hydroxylation to install a tertiary alcohol in the decaline ring to yield betaenone C from dehydroprobetaenone I and betaen",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1481,no
FOGG_ASPRC,A0A017SEY2,Prot2Text,Eukaryota,348,"Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain. The PKS fogA releases the carboxylic acid (8E,10E,12E)-3,5,7-trihydroxytetradeca-8,10,12-trienoic acid as its product, as well as derivatives with one and two double bonds. FogA is indeed able to reduce the initial triketide, thus being at least partially responsible for the differently saturated heptyl side chains of flavoglaucin congeners. The oxidoreductases fogB, fogC and fogD modify the nascent polyketide in fogA-bound form and, together, fogA, fogB, fogC and fogD are necessary for the formation of the aromatic core and the cyclized PKS products are released as salicyl alcohols. In particular, fogB is responsible for oxidation of a hydroxyl group or reduction of remaining double bond(s) at the C-7 residue whereas fogD is probably involved in the reductive release of the modified PKS products. The cytochrome P450 monooxygenase fogE is then responsible for the hydroxylation at C-3 of the benzene ring. The fogE products are substrates of the prenyltransferase fogH and the prenylated benzyl alcohols are subsequently oxidized by the fogF to produce the final aryl aldehydes flavoglaucin and congeners. The short-chain dehydrogenase fogG does not seem to be involved in the biosynthesis of the prenylated salicylaldehyde derivatives.","Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1481,no
FOGG_ASPRC,A0A017SEY2,ProtT3,Eukaryota,348,"Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain. The PKS fogA releases the carboxylic acid (8E,10E,12E)-3,5,7-trihydroxytetradeca-8,10,12-trienoic acid as its product, as well as derivatives with one and two double bonds. FogA is indeed able to reduce the initial triketide, thus being at least partially responsible for the differently saturated heptyl side chains of flavoglaucin congeners. The oxidoreductases fogB, fogC and fogD modify the nascent polyketide in fogA-bound form and, together, fogA, fogB, fogC and fogD are necessary for the formation of the aromatic core and the cyclized PKS products are released as salicyl alcohols. In particular, fogB is responsible for oxidation of a hydroxyl group or reduction of remaining double bond(s) at the C-7 residue whereas fogD is probably involved in the reductive release of the modified PKS products. The cytochrome P450 monooxygenase fogE is then responsible for the hydroxylation at C-3 of the benzene ring. The fogE products are substrates of the prenyltransferase fogH and the prenylated benzyl alcohols are subsequently oxidized by the fogF to produce the final aryl aldehydes flavoglaucin and congeners. The short-chain dehydrogenase fogG does not seem to be involved in the biosynthesis of the prenylated salicylaldehyde derivatives.",Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeranylindole (,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1481,no
FOGG_ASPRC,A0A017SEY2,ProtTale,Eukaryota,348,"Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain. The PKS fogA releases the carboxylic acid (8E,10E,12E)-3,5,7-trihydroxytetradeca-8,10,12-trienoic acid as its product, as well as derivatives with one and two double bonds. FogA is indeed able to reduce the initial triketide, thus being at least partially responsible for the differently saturated heptyl side chains of flavoglaucin congeners. The oxidoreductases fogB, fogC and fogD modify the nascent polyketide in fogA-bound form and, together, fogA, fogB, fogC and fogD are necessary for the formation of the aromatic core and the cyclized PKS products are released as salicyl alcohols. In particular, fogB is responsible for oxidation of a hydroxyl group or reduction of remaining double bond(s) at the C-7 residue whereas fogD is probably involved in the reductive release of the modified PKS products. The cytochrome P450 monooxygenase fogE is then responsible for the hydroxylation at C-3 of the benzene ring. The fogE products are substrates of the prenyltransferase fogH and the prenylated benzyl alcohols are subsequently oxidized by the fogF to produce the final aryl aldehydes flavoglaucin and congeners. The short-chain dehydrogenase fogG does not seem to be involved in the biosynthesis of the prenylated salicylaldehyde derivatives.","Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1481,no
FOGG_ASPRC,A0A017SEY2,Protein2Text,Eukaryota,348,"Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain. The PKS fogA releases the carboxylic acid (8E,10E,12E)-3,5,7-trihydroxytetradeca-8,10,12-trienoic acid as its product, as well as derivatives with one and two double bonds. FogA is indeed able to reduce the initial triketide, thus being at least partially responsible for the differently saturated heptyl side chains of flavoglaucin congeners. The oxidoreductases fogB, fogC and fogD modify the nascent polyketide in fogA-bound form and, together, fogA, fogB, fogC and fogD are necessary for the formation of the aromatic core and the cyclized PKS products are released as salicyl alcohols. In particular, fogB is responsible for oxidation of a hydroxyl group or reduction of remaining double bond(s) at the C-7 residue whereas fogD is probably involved in the reductive release of the modified PKS products. The cytochrome P450 monooxygenase fogE is then responsible for the hydroxylation at C-3 of the benzene ring. The fogE products are substrates of the prenyltransferase fogH and the prenylated benzyl alcohols are subsequently oxidized by the fogF to produce the final aryl aldehydes flavoglaucin and congeners. The short-chain dehydrogenase fogG does not seem to be involved in the biosynthesis of the prenylated salicylaldehyde derivatives.","This protein is involved in catalyzing the oxidation of a compound, specifically a type of reaction that involves the transfer of electrons from one molecule to another. More specifically, it is a monooxygenase, which is a type of enzyme that uses molecular oxygen to catalyze the oxidation of a substrate. The exact mechanism of action of this protein is not specified, but it is likely to be involved in the breakdown of a compound, possibly as part of a metabolic pathway. 

The molecular function of this protein is likely to be involved in oxidation-reduction reactions, specifically as a monooxygenase. 

It is worth noting that the exact molecular function of this protein is not specified in the text, and this is an educated guess based on the information provided.",No,No,No,Vague,No,not-Yes,GO:0016491,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.8145,0.8145,0.8145,0.8145,0.8145,5,0.8145,0.1481,no
FOGG_ASPRC,A0A017SEY2,Reference,Eukaryota,348,"Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain. The PKS fogA releases the carboxylic acid (8E,10E,12E)-3,5,7-trihydroxytetradeca-8,10,12-trienoic acid as its product, as well as derivatives with one and two double bonds. FogA is indeed able to reduce the initial triketide, thus being at least partially responsible for the differently saturated heptyl side chains of flavoglaucin congeners. The oxidoreductases fogB, fogC and fogD modify the nascent polyketide in fogA-bound form and, together, fogA, fogB, fogC and fogD are necessary for the formation of the aromatic core and the cyclized PKS products are released as salicyl alcohols. In particular, fogB is responsible for oxidation of a hydroxyl group or reduction of remaining double bond(s) at the C-7 residue whereas fogD is probably involved in the reductive release of the modified PKS products. The cytochrome P450 monooxygenase fogE is then responsible for the hydroxylation at C-3 of the benzene ring. The fogE products are substrates of the prenyltransferase fogH and the prenylated benzyl alcohols are subsequently oxidized by the fogF to produce the final aryl aldehydes flavoglaucin and congeners. The short-chain dehydrogenase fogG does not seem to be involved in the biosynthesis of the prenylated salicylaldehyde derivatives.","Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain. The PKS fogA releases the carboxylic acid (8E,10E,12E)-3,5,7-trihydroxytetradeca-8,10,12-trienoic acid as its product, as well as derivatives with one and two double bonds. FogA is indeed able to reduce the initial triketide, thus being at least partially responsible for the differently saturated heptyl side chains of flavoglaucin congeners. The oxidoreductases fogB, fogC and fogD modify the nascent polyketide in fogA-bound form and, together, fogA, fogB, fogC and fogD are necessary for the formation of the aromatic core and the cyclized PKS products are released as salicyl alcohols. In particular, fogB is responsible for oxidation of a hydroxyl group or reduction of remaining double bond(s) at the C-7 residue whereas fogD is probably involved in the reductive release of the modified PKS products. The cytochrome P450 monooxygenase fogE is then responsible for the hydroxylation at C-3 of the benzene ring. The fogE products are substrates of the prenyltransferase fogH and the prenylated benzyl alcohols are subsequently oxidized by the fogF to produce the final aryl aldehydes flavoglaucin and congeners. The short-chain dehydrogenase fogG does not seem to be involved in the biosynthesis of the prenylated salicylaldehyde derivatives.",,,,,,,GO:0016491,GO:0016491,,GO:0016491,GO:0016491,,1.0,,1.0,1.0,,3,1.0,0.1481,no
C1CD1_CITSI,A0A067GFT7,ESM2Text,Eukaryota,512,"Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus. Catalyzes the conversion of tirucalladienol to dihydroniloticin.","Cytochrome P450 involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family. Catalyzes the hydroxylation of naringenin at the C-7 position to form 7'-hydroxykaempferol.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016491; GO:0016705,GO:0004497; GO:0020037,GO:0004497,GO:0004497,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,0.8149,0.6251,0.6251,0.9345,0.9345,5,0.7868,0.4183,no
C1CD1_CITSI,A0A067GFT7,Prot2Text,Eukaryota,512,"Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus. Catalyzes the conversion of tirucalladienol to dihydroniloticin.","Cytochrome P450 involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family. Catalyzes the conversion of bursehernin to demethylyatein.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016491; GO:0016705,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.6251,0.6251,0.6251,0.6251,0.6251,5,0.6251,0.4183,no
C1CD1_CITSI,A0A067GFT7,ProtT3,Eukaryota,512,"Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus. Catalyzes the conversion of tirucalladienol to dihydroniloticin.",Membrane; Single-pass membrane protein. Belongs to the cytochrome P450 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016491; GO:0016705,GO:0004497,GO:0004497; GO:0020037,GO:0004497; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,0.6251,0.8149,0.8149,0.9345,0.9345,5,0.8248,0.4183,no
C1CD1_CITSI,A0A067GFT7,ProtTale,Eukaryota,512,"Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus. Catalyzes the conversion of tirucalladienol to dihydroniloticin.","Cytochrome P450 monooxygenase involved in the biosynthesis of indole-3-acetic acid (IAA)-amido acids, a family of plant hormones known as auxin. Catalyzes the hydroxylation of IAA-amido acids at C-3 to produce 2-oxindole-3-acetic acid (2-oxIAA)-amido acids.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016491; GO:0016705,GO:0004497; GO:0020037,GO:0004497; GO:0016491,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497,0.8149,0.7367,0.9345,0.9345,0.6251,5,0.8091,0.4183,no
C1CD1_CITSI,A0A067GFT7,Protein2Text,Eukaryota,512,"Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus. Catalyzes the conversion of tirucalladienol to dihydroniloticin.","This protein is involved in the catalysis of the metabolism of terpenes, specifically in the conversion of the terpene precursor into a more stable form. More specifically, it catalyzes the conversion of the terpene precursor into a more stable form, which is then further metabolized into a variety of products.

The molecular function of this protein can be summarized as:

* Catalyzing the conversion of terpene precursors into more stable forms
* Involved in the metabolism of terpenes
* Catalyzing the conversion of terpenes into a variety of products

This protein is a part of the cytochrome P450 family, which is a group of enzymes that play a crucial role in the metabolism of a wide range of substances, including terpenes, steroids, and drugs. The specific molecular function of this protein is to catalyze the conversion of the terpene precursor into a more stable form, which is then further metabolized into a variety of products.",Vague,Maybe,Maybe,Maybe,Vague,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016491; GO:0016705,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.6251,0.6251,0.6251,0.6251,0.6251,5,0.6251,0.4183,no
C1CD1_CITSI,A0A067GFT7,Reference,Eukaryota,512,"Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus. Catalyzes the conversion of tirucalladienol to dihydroniloticin.","Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as limonin, a compound with insecticidal activity responsible for the bitter taste in citrus. Catalyzes the conversion of tirucalladienol to dihydroniloticin.",,,,,,,GO:0020037; GO:0005506; GO:0004497; GO:0016491; GO:0016705,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.6251,0.6251,0.6251,0.6251,0.6251,5,0.6251,0.4183,no
SOLAP_PAEBO,A0A089LI24,ESM2Text,Bacteria,768,Catalyzes the reversible phosphorolysis of solabiose. Catalyzes the phosphorolysis and synthesis of solabiose through a sequential bi-bi mechanism involving the formation of a ternary complex. Is probably involved in the metabolism of solabiose released from solabiose-containing compounds.,"Catalyzes the reversible phosphorolysis of cellobiose, yielding glucose 1-P and glucose. It is active on cellobiose, laminaribiose, cellotriose, cellobiose and glucose. It shows low activity against mannobiose, phosphorobiose, beta-D-glucosides and D-glucosides with higher activity against cellotriose, cellobiose and D-glucose.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0030246; GO:0016757,GO:0004645,GO:0016757,GO:0016787,GO:0016757,GO:0047680,0.5386,0.7379,0.4079,0.7379,0.2423,5,0.5329,0.2289,no
SOLAP_PAEBO,A0A089LI24,Prot2Text,Bacteria,768,Catalyzes the reversible phosphorolysis of solabiose. Catalyzes the phosphorolysis and synthesis of solabiose through a sequential bi-bi mechanism involving the formation of a ternary complex. Is probably involved in the metabolism of solabiose released from solabiose-containing compounds.,"Catalyzes the reversible phosphorolysis of cellobiose. Hydrolyzes cellobiose to glucose and glucose 1-phosphate, and cellotriose to glucose. Does not act on cellotetraose, cellotriose, cellobiose, cellotetraose, cellopentaose, cellopentaose, cellopentaose, cellopentaose, cellopentaose, cellopentaose, cellopentaose, cellopentaose, cellopentaose, cellopentaose, cellopentaose, cellopentaose, cellopentaose, cellopentaose, cellopentaose, cellopentaose, cellopentaose, cellopentaose, cellopentaopentaose, and lactose.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0030246; GO:0016757,GO:0050504,GO:0050504,GO:0016757,GO:0016757,GO:0004645,0.5386,0.5386,0.7379,0.7379,0.5386,5,0.6183,0.2289,no
SOLAP_PAEBO,A0A089LI24,ProtT3,Bacteria,768,Catalyzes the reversible phosphorolysis of solabiose. Catalyzes the phosphorolysis and synthesis of solabiose through a sequential bi-bi mechanism involving the formation of a ternary complex. Is probably involved in the metabolism of solabiose released from solabiose-containing compounds.,"Catalyzes the phosphorolysis of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) to yield 1,6-anhydro-N-acetylmuramic acid 6-phosphate (anhMurNAc-6-P). Belongs to the glycosyl hydrolase 69 family",No,No,No,No,No,not-Yes,GO:0030246; GO:0016757,GO:0016787,GO:0016798,GO:0016798,GO:0016301,GO:0016301,0.4079,0.3314,0.3314,0.4313,0.4313,5,0.3867,0.2289,no
SOLAP_PAEBO,A0A089LI24,ProtTale,Bacteria,768,Catalyzes the reversible phosphorolysis of solabiose. Catalyzes the phosphorolysis and synthesis of solabiose through a sequential bi-bi mechanism involving the formation of a ternary complex. Is probably involved in the metabolism of solabiose released from solabiose-containing compounds.,"Catalyzes the hydrolysis of glucose-1-phosphate (G1P) into glucose and phosphate. Is specific for G1P, it is not able to hydrolyze glucose-6-phosphate (G6P) or 2-phospho-D-glycerate (2-PGA).",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0030246; GO:0016757,GO:0050308,GO:0016791,GO:0016791,GO:0016791,GO:0016791,0.1951,0.2423,0.2423,0.2423,0.2423,5,0.2329,0.2289,no
SOLAP_PAEBO,A0A089LI24,Protein2Text,Bacteria,768,Catalyzes the reversible phosphorolysis of solabiose. Catalyzes the phosphorolysis and synthesis of solabiose through a sequential bi-bi mechanism involving the formation of a ternary complex. Is probably involved in the metabolism of solabiose released from solabiose-containing compounds.,"This protein is involved in the hydrolysis of sucrose, which is a disaccharide composed of glucose and fructose molecules. Its molecular function is likely to be a glycoside hydrolase, which catalyzes the breakdown of sucrose into glucose and fructose.",No,No,No,No,No,not-Yes,GO:0030246; GO:0016757,GO:0004575,GO:0004575,GO:0004575,GO:0004575,GO:0004564,0.1776,0.1776,0.1776,0.1776,0.2423,5,0.1905,0.2289,no
SOLAP_PAEBO,A0A089LI24,Reference,Bacteria,768,Catalyzes the reversible phosphorolysis of solabiose. Catalyzes the phosphorolysis and synthesis of solabiose through a sequential bi-bi mechanism involving the formation of a ternary complex. Is probably involved in the metabolism of solabiose released from solabiose-containing compounds.,Catalyzes the reversible phosphorolysis of solabiose. Catalyzes the phosphorolysis and synthesis of solabiose through a sequential bi-bi mechanism involving the formation of a ternary complex. Is probably involved in the metabolism of solabiose released from solabiose-containing compounds.,,,,,,,GO:0030246; GO:0016757,GO:0016757,GO:0004645,GO:0004645,GO:0016757,GO:0004645,0.7379,0.5386,0.5386,0.7379,0.5386,5,0.6183,0.2289,no
LYS11_PENEN,A0A0A2J9B0,ESM2Text,Eukaryota,1116,"Probable chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Might be involved in manipulation of host defenses for successful infection (Probable).","May play a role in the digestion of chitin, as well as in the defense against nematodes and other pathogens. Has a low affinity for glycol chitin.",Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0008061; GO:0008843,GO:0004568,,GO:0004568,GO:0004568,GO:0004568,0.6216,,0.6216,0.6216,0.6216,4,0.6216,0.2731,no
LYS11_PENEN,A0A0A2J9B0,Prot2Text,Eukaryota,1116,"Probable chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Might be involved in manipulation of host defenses for successful infection (Probable).","Probably a non-catalytic chitinase-like protein, which binds to insoluble chitin and enhances the activity of the catalytic chitinases. Has weak chitin-binding activity.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008061; GO:0008843,GO:0008061,GO:0008061,GO:0008061,GO:0008061,GO:0008061,0.704,0.704,0.704,0.704,0.704,5,0.704,0.2731,no
LYS11_PENEN,A0A0A2J9B0,ProtT3,Eukaryota,1116,"Probable chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Might be involved in manipulation of host defenses for successful infection (Probable).",Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008061; GO:0008843,GO:0004568,GO:0004568,GO:0004568,GO:0004568,GO:0004568,0.6216,0.6216,0.6216,0.6216,0.6216,5,0.6216,0.2731,no
LYS11_PENEN,A0A0A2J9B0,ProtTale,Eukaryota,1116,"Probable chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Might be involved in manipulation of host defenses for successful infection (Probable).","Secreted chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Participates in the infection process and directly acts in the penetration process of the host cuticle.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008061; GO:0008843,GO:0004568,GO:0004568,GO:0004568,GO:0004568,GO:0004568,0.6216,0.6216,0.6216,0.6216,0.6216,5,0.6216,0.2731,no
LYS11_PENEN,A0A0A2J9B0,Protein2Text,Eukaryota,1116,"Probable chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Might be involved in manipulation of host defenses for successful infection (Probable).","This protein is involved in breaking down complex molecules into simpler ones, specifically it is a type of enzyme that likely plays a role in the degradation of cellulose, a complex carbohydrate found in plant cell walls.",No,No,No,No,No,not-Yes,GO:0008061; GO:0008843,GO:0030248,GO:0030245,GO:0030245,GO:0030245,GO:0008810,0.2496,0.0,0.0,0.0,0.4645,5,0.1428,0.2731,no
LYS11_PENEN,A0A0A2J9B0,Reference,Eukaryota,1116,"Probable chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Might be involved in manipulation of host defenses for successful infection (Probable).","Probable chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Might be involved in manipulation of host defenses for successful infection (Probable).",,,,,,,GO:0008061; GO:0008843,GO:0004568,GO:0004568,GO:0004568,GO:0004568,GO:0004568,0.6216,0.6216,0.6216,0.6216,0.6216,5,0.6216,0.2731,no
SRDC_MESS1,A0A0A8X338,ESM2Text,Bacteria,426,"Component of the respiratory selenate reductase complex, which catalyzes the reduction of selenate to selenite. This subunit probably receives electrons directly from the membrane quinone pool and transfers the electrons to the iron- sulfur clusters of SrdB (Probable). May be the membrane anchor protein subunit of the complex (Probable).","Essential for the bioreductive activity of the enzyme. Part of the bsa operon, which is probably the primary bsa subunit.",Vague,No,No,No,Vague,not-Yes,GO:0016491,,,,,,,,,,,0,,0.4356,no
SRDC_MESS1,A0A0A8X338,Prot2Text,Bacteria,426,"Component of the respiratory selenate reductase complex, which catalyzes the reduction of selenate to selenite. This subunit probably receives electrons directly from the membrane quinone pool and transfers the electrons to the iron- sulfur clusters of SrdB (Probable). May be the membrane anchor protein subunit of the complex (Probable).","Part of the ammonia monooxygenase complex, which catalyzes the oxidation of ammonia to hydroxylamine, the first reaction in the process of ammonia oxidation to nitrite.",No,No,No,No,No,not-Yes,GO:0016491,,,GO:0016491,GO:0016491,GO:0016491,,,1.0,1.0,1.0,3,1.0,0.4356,no
SRDC_MESS1,A0A0A8X338,ProtT3,Bacteria,426,"Component of the respiratory selenate reductase complex, which catalyzes the reduction of selenate to selenite. This subunit probably receives electrons directly from the membrane quinone pool and transfers the electrons to the iron- sulfur clusters of SrdB (Probable). May be the membrane anchor protein subunit of the complex (Probable).",Catalyzes the reduction of menaquinol to menadione. Cell inner membrane; Multi-pass membrane protein. Belongs to the cytochrome d-type oxidoreductase family,No,No,No,No,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016679,GO:0016491,GO:0016491,GO:0016491,1.0,0.8145,1.0,1.0,1.0,5,0.9629,0.4356,no
SRDC_MESS1,A0A0A8X338,ProtTale,Bacteria,426,"Component of the respiratory selenate reductase complex, which catalyzes the reduction of selenate to selenite. This subunit probably receives electrons directly from the membrane quinone pool and transfers the electrons to the iron- sulfur clusters of SrdB (Probable). May be the membrane anchor protein subunit of the complex (Probable).",Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.,No,No,No,No,No,not-Yes,GO:0016491,GO:0015087,,,GO:0005215,GO:0015087,0.1287,,,0.3396,0.1287,3,0.199,0.4356,no
SRDC_MESS1,A0A0A8X338,Protein2Text,Bacteria,426,"Component of the respiratory selenate reductase complex, which catalyzes the reduction of selenate to selenite. This subunit probably receives electrons directly from the membrane quinone pool and transfers the electrons to the iron- sulfur clusters of SrdB (Probable). May be the membrane anchor protein subunit of the complex (Probable).","This protein is involved in electron transport in the cytochrome b-c1 complex, which is a part of the electron transport chain in mitochondria. It is a subunit of the cytochrome b-c1 complex, which is a membrane-integral multi-subunit transmembrane complex that is part of the mitochondrial respiratory chain. This protein plays a role in the electron transport process, which is essential for generating energy for the cell.",Maybe,No,No,No,Maybe,not-Yes,GO:0016491,GO:0009055,GO:0009055,GO:0009055,GO:0009055,GO:0008121,0.3396,0.3396,0.3396,0.3396,0.1204,5,0.2958,0.4356,no
SRDC_MESS1,A0A0A8X338,Reference,Bacteria,426,"Component of the respiratory selenate reductase complex, which catalyzes the reduction of selenate to selenite. This subunit probably receives electrons directly from the membrane quinone pool and transfers the electrons to the iron- sulfur clusters of SrdB (Probable). May be the membrane anchor protein subunit of the complex (Probable).","Component of the respiratory selenate reductase complex, which catalyzes the reduction of selenate to selenite. This subunit probably receives electrons directly from the membrane quinone pool and transfers the electrons to the iron- sulfur clusters of SrdB (Probable). May be the membrane anchor protein subunit of the complex (Probable).",,,,,,,GO:0016491,GO:0009055,GO:0009055,GO:0009055,GO:0009055,GO:0009055,0.3396,0.3396,0.3396,0.3396,0.3396,5,0.3396,0.4356,no
SRDB_MESS1,A0A0A8X5N4,ESM2Text,Bacteria,292,"Component of the respiratory selenate reductase complex, which catalyzes the reduction of selenate to selenite. This subunit probably transfers electrons from SrdC to SrdA (Probable).","Electron transfer subunit of the cytochrome c heme-type cytochrome c1 pump, an essential component of the respiratory electron transport chain required for ATP synthesis.",Maybe,No,No,No,Maybe,not-Yes,GO:0051539; GO:0046872; GO:0016491,GO:0009055; GO:0020037,GO:0009055,GO:0009055,GO:0009055; GO:0020037,GO:0009055; GO:0020037,0.3065,0.2725,0.2725,0.3065,0.3065,5,0.2929,0.3901,no
SRDB_MESS1,A0A0A8X5N4,Prot2Text,Bacteria,292,"Component of the respiratory selenate reductase complex, which catalyzes the reduction of selenate to selenite. This subunit probably transfers electrons from SrdC to SrdA (Probable).","Cytochrome b subunit of the cytochrome bc1 complex, an essential component of the respiratory electron transport chain required for ATP synthesis. The bc1 complex catalyzes the oxidation of menaquinol and the reduction of cytochrome c in the respiratory chain. The bc1 complex operates through a Q-cycle mechanism that couples electron transfer to generation of the proton gradient that drives ATP synthesis.",Maybe,No,No,No,Maybe,not-Yes,GO:0051539; GO:0046872; GO:0016491,GO:0009055,GO:0008121,GO:0008121,GO:0008121,GO:0008121,0.2725,0.1009,0.1009,0.1009,0.1009,5,0.1352,0.3901,no
SRDB_MESS1,A0A0A8X5N4,ProtT3,Bacteria,292,"Component of the respiratory selenate reductase complex, which catalyzes the reduction of selenate to selenite. This subunit probably transfers electrons from SrdC to SrdA (Probable).",Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Cell membrane; Peripheral membrane protein. Belongs to the 4Fe4S bacterial-type ferredoxin family,Maybe,No,No,Maybe,Maybe,not-Yes,GO:0051539; GO:0046872; GO:0016491,GO:0009055; GO:0051539,GO:0009055; GO:0051539,GO:0009055; GO:0051539,GO:0009055; GO:0051539,GO:0009055; GO:0051539,0.6036,0.6036,0.6036,0.6036,0.6036,5,0.6036,0.3901,no
SRDB_MESS1,A0A0A8X5N4,ProtTale,Bacteria,292,"Component of the respiratory selenate reductase complex, which catalyzes the reduction of selenate to selenite. This subunit probably transfers electrons from SrdC to SrdA (Probable).","NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.",No,No,No,No,Maybe,not-Yes,GO:0051539; GO:0046872; GO:0016491,GO:0008137,GO:0008137; GO:0016491; GO:0048038,GO:0008137; GO:0050660; GO:0051536,GO:0008137,GO:0008137,0.1009,0.5944,0.4733,0.1009,0.1009,5,0.2741,0.3901,no
SRDB_MESS1,A0A0A8X5N4,Protein2Text,Bacteria,292,"Component of the respiratory selenate reductase complex, which catalyzes the reduction of selenate to selenite. This subunit probably transfers electrons from SrdC to SrdA (Probable).",The molecular function of this protein is an electron transfer chain protein.,Vague,No,Maybe,Vague,Vague,not-Yes,GO:0051539; GO:0046872; GO:0016491,GO:0009055,GO:0009055,GO:0009055,GO:0009055,,0.2725,0.2725,0.2725,0.2725,,4,0.2725,0.3901,no
SRDB_MESS1,A0A0A8X5N4,Reference,Bacteria,292,"Component of the respiratory selenate reductase complex, which catalyzes the reduction of selenate to selenite. This subunit probably transfers electrons from SrdC to SrdA (Probable).","Component of the respiratory selenate reductase complex, which catalyzes the reduction of selenate to selenite. This subunit probably transfers electrons from SrdC to SrdA (Probable).",,,,,,,GO:0051539; GO:0046872; GO:0016491,GO:0009055,GO:0009055,GO:0009055,GO:0009055,GO:0009055,0.2725,0.2725,0.2725,0.2725,0.2725,5,0.2725,0.3901,no
PBOC_ASPUT,A0A0C1BWC7,ESM2Text,Eukaryota,470,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. Within the pathway, pboC catalyzes the acetylation of protubonine D at the hydroxy group to produce protubonine C. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L-Leu by condensing L-Leu with L-Trp. The flavin-dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.","Acyltransferase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the methyltransferase claB. The cytochrome monooxygenase P450 claM then catalyzes the dimerization of nataloe-emodin to cladofulvin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016746,GO:0016746,GO:0016747,GO:0016746,GO:0016746,GO:0016746,1.0,0.8416,1.0,1.0,1.0,5,0.9683,0.2973,no
PBOC_ASPUT,A0A0C1BWC7,Prot2Text,Eukaryota,470,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. Within the pathway, pboC catalyzes the acetylation of protubonine D at the hydroxy group to produce protubonine C. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L-Leu by condensing L-Leu with L-Trp. The flavin-dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.","O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential tricycl",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016746,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.729,0.729,0.729,0.729,0.729,5,0.729,0.2973,no
PBOC_ASPUT,A0A0C1BWC7,ProtT3,Eukaryota,470,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. Within the pathway, pboC catalyzes the acetylation of protubonine D at the hydroxy group to produce protubonine C. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L-Leu by condensing L-Leu with L-Trp. The flavin-dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.","Acetyltransferase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties . L-aspartate is suggested as fusaric acid",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016746,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.729,0.729,0.729,0.729,0.729,5,0.729,0.2973,no
PBOC_ASPUT,A0A0C1BWC7,ProtTale,Eukaryota,470,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. Within the pathway, pboC catalyzes the acetylation of protubonine D at the hydroxy group to produce protubonine C. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L-Leu by condensing L-Leu with L-Trp. The flavin-dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.","O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the saturated C-C",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016746,GO:0016407,GO:0016747,GO:0016747,GO:0016747,GO:0016407,0.729,0.8416,0.8416,0.8416,0.729,5,0.7966,0.2973,no
PBOC_ASPUT,A0A0C1BWC7,Protein2Text,Eukaryota,470,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. Within the pathway, pboC catalyzes the acetylation of protubonine D at the hydroxy group to produce protubonine C. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L-Leu by condensing L-Leu with L-Trp. The flavin-dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.","This protein is involved in the molecular function of transferring a methyl group to a molecule, specifically as part of a broader process related to the metabolism of steroids or other molecules. It is likely involved in the biosynthesis of steroid hormones or other molecules by transferring a methyl group to a molecule. 

In more detail, this protein is a methyltransferase, which is a type of enzyme that transfers a methyl group from one molecule to another. Methyltransferases play a crucial role in many biological processes, including the biosynthesis of hormones, the modification of proteins and lipids, and the regulation of gene expression. 

The specific molecular function of this protein is likely to be the transfer of a methyl group to a substrate molecule, such as a steroid or other molecule, as part of a larger metabolic pathway. The exact nature of the substrate molecule and the specific methyl group being transferred are not specified in the available information. 

It is worth noting that the exact function of this protein may depend on the specific organism or cell type in which it is expressed. However, based on its classification as a methyltransferase, it is likely to play a role in the biosynthesis of steroid hormones or other molecules.",No,No,No,No,No,not-Yes,GO:0016746,GO:0008168,GO:0008168,GO:0008171,GO:0008168,GO:0008168,0.5565,0.5565,0.482,0.5565,0.5565,5,0.5416,0.2973,no
PBOC_ASPUT,A0A0C1BWC7,Reference,Eukaryota,470,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. Within the pathway, pboC catalyzes the acetylation of protubonine D at the hydroxy group to produce protubonine C. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L-Leu by condensing L-Leu with L-Trp. The flavin-dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.","O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. Within the pathway, pboC catalyzes the acetylation of protubonine D at the hydroxy group to produce protubonine C. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L-Leu by condensing L-Leu with L-Trp. The flavin-dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.",,,,,,,GO:0016746,GO:0016747,GO:0016747,GO:0016407,GO:0016407,GO:0016746,0.8416,0.8416,0.729,0.729,1.0,5,0.8282,0.2973,no
UCDE_ASPUT,A0A0C1C2W0,ESM2Text,Eukaryota,457,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdE prenylates position C-5 of ring A of 3,15-dihydroxyterphenyllin to produce forms usterphenyllin B. UcdE further prenylates position C- 14 of ring C of usterphenyllin B to form usterphenyllin A. The pathway begin with the biosynthesis of 4- hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O-methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C-5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non- enzymatic reaction.","Responsible for the non-oxidative decarboxylation and detoxification of phenolic derivatives under both aerobic and anaerobic conditions, however the precise biochemical function in metabolism of phenolic acid is unknown. It is believed that the large subunit is a phenolic acid reductase.",No,No,No,No,No,not-Yes,GO:0004659,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.2742,0.2742,0.2742,0.2742,0.2742,5,0.2742,0.3423,no
UCDE_ASPUT,A0A0C1C2W0,Prot2Text,Eukaryota,457,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdE prenylates position C-5 of ring A of 3,15-dihydroxyterphenyllin to produce forms usterphenyllin B. UcdE further prenylates position C- 14 of ring C of usterphenyllin B to form usterphenyllin A. The pathway begin with the biosynthesis of 4- hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O-methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C-5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non- enzymatic reaction.","Tryptophan dimethylallyltransferase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid. DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan. The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine. The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde. Chanoclavine-I aldehyde is the precursor of ergoamides and ergopeptines in Clavicipitaceae, and clavine-type alcaloids such",No,No,No,No,No,not-Yes,GO:0004659,GO:0004659,GO:0050324,GO:0004659,GO:0016765,GO:0004161,1.0,0.358,1.0,0.8416,0.7539,5,0.7907,0.3423,no
UCDE_ASPUT,A0A0C1C2W0,ProtT3,Eukaryota,457,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdE prenylates position C-5 of ring A of 3,15-dihydroxyterphenyllin to produce forms usterphenyllin B. UcdE further prenylates position C- 14 of ring C of usterphenyllin B to form usterphenyllin A. The pathway begin with the biosynthesis of 4- hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O-methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C-5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non- enzymatic reaction.","Catalyzes the condensation of indole-3-glycerol phosphate (IGP) with 2,3-diketo-5-methylthiopentyl-1- phosphate (DK-MTP-1-P) to form indole-3-glycerol phosphate and 2,3- diketo-5- methylthiopentyl-1,2-cyclic phosphate (DK-MTP-cPP). Belongs to the IGP synthase family",No,No,No,No,No,not-Yes,GO:0004659,GO:0004425,GO:0004425,GO:0004425,GO:0004425,GO:0004425,0.2353,0.2353,0.2353,0.2353,0.2353,5,0.2353,0.3423,no
UCDE_ASPUT,A0A0C1C2W0,ProtTale,Eukaryota,457,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdE prenylates position C-5 of ring A of 3,15-dihydroxyterphenyllin to produce forms usterphenyllin B. UcdE further prenylates position C- 14 of ring C of usterphenyllin B to form usterphenyllin A. The pathway begin with the biosynthesis of 4- hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O-methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C-5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non- enzymatic reaction.","Prenyltransferase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS). SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms. These initial steps feature the priming of an unusual benzoic acid starter unit onto the highly",No,Maybe,No,Maybe,No,not-Yes,GO:0004659,GO:0004659,GO:0016765,GO:0016765,GO:0004659,GO:0004659,1.0,0.8416,0.8416,1.0,1.0,5,0.9366,0.3423,no
UCDE_ASPUT,A0A0C1C2W0,Protein2Text,Eukaryota,457,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdE prenylates position C-5 of ring A of 3,15-dihydroxyterphenyllin to produce forms usterphenyllin B. UcdE further prenylates position C- 14 of ring C of usterphenyllin B to form usterphenyllin A. The pathway begin with the biosynthesis of 4- hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O-methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C-5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non- enzymatic reaction.","This protein is involved in the molecular function of forming a heterodimeric complex with another protein, which is a component of the fungal polyketide synthase (PKS) system. The PKS system is responsible for the biosynthesis of polyketides, a class of secondary metabolites that play important roles in various biological processes. The specific molecular function of this protein is to form a heterodimeric complex with another protein, which is essential for the biosynthesis of polyketides.",Maybe,No,No,No,Maybe,not-Yes,GO:0004659,,,,,,,,,,,0,,0.3423,no
UCDE_ASPUT,A0A0C1C2W0,Reference,Eukaryota,457,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdE prenylates position C-5 of ring A of 3,15-dihydroxyterphenyllin to produce forms usterphenyllin B. UcdE further prenylates position C- 14 of ring C of usterphenyllin B to form usterphenyllin A. The pathway begin with the biosynthesis of 4- hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O-methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C-5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non- enzymatic reaction.","Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdE prenylates position C-5 of ring A of 3,15-dihydroxyterphenyllin to produce forms usterphenyllin B. UcdE further prenylates position C- 14 of ring C of usterphenyllin B to form usterphenyllin A. The pathway begin with the biosynthesis of 4- hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O-methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C-5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non- enzymatic reaction.",,,,,,,GO:0004659,GO:0004659,GO:0004659,GO:0016765,GO:0004659,GO:0004659,1.0,1.0,0.8416,1.0,1.0,5,0.9683,0.3423,no
UCDB_ASPUT,A0A0C1E1C6,ESM2Text,Eukaryota,285,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdB alone catalyzes both reduction and dehydration of atromentin to form a terphenyl triol intermediate. The pathway begin with the biosynthesis of 4-hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O-methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C-5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non- enzymatic reaction.","Catalyzes the reduction of 5-keto-D-gluconate to 5-keto-L-gulonate. Is also able to catalyze the reverse reaction, i.e. the NADPH-dependent reduction of 5-keto-D-gluconate to 5-keto-L-gulonate. Is not active with NADP(+) instead of NAD(+).",No,No,No,No,No,not-Yes,GO:0051287; GO:0050661; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.5633,0.5633,0.5633,0.5633,0.5633,5,0.5633,0.2889,no
UCDB_ASPUT,A0A0C1E1C6,Prot2Text,Eukaryota,285,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdB alone catalyzes both reduction and dehydration of atromentin to form a terphenyl triol intermediate. The pathway begin with the biosynthesis of 4-hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O-methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C-5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non- enzymatic reaction.","Catalyzes the NAD(+)-dependent oxidation of L-carnitine to 3-dehydrocarnitine. Is specific for L-carnitine and NADP(+) as substrates since D-carnitine, other carnitine analogs such as crotonyl-CoA and gamma-butyrobetaine, and NADPH cannot act as substrates. Does not catalyze the reverse reaction. Does not possess NAD(+) reductase activity since it cannot use NADP(+) instead of NAD(+) as cosubstrate.",No,No,No,No,No,not-Yes,GO:0051287; GO:0050661; GO:0016491,GO:0016616,GO:0047728,GO:0016616,GO:0016616,GO:0016616,0.3866,0.3362,0.3866,0.3866,0.3866,5,0.3765,0.2889,no
UCDB_ASPUT,A0A0C1E1C6,ProtT3,Eukaryota,285,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdB alone catalyzes both reduction and dehydration of atromentin to form a terphenyl triol intermediate. The pathway begin with the biosynthesis of 4-hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O-methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C-5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non- enzymatic reaction.",Cytoplasm. Belongs to the isochorismatase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0051287; GO:0050661; GO:0016491,GO:0008908,GO:0008908,GO:0008908,GO:0008908,GO:0008908,0.1891,0.1891,0.1891,0.1891,0.1891,5,0.1891,0.2889,no
UCDB_ASPUT,A0A0C1E1C6,ProtTale,Eukaryota,285,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdB alone catalyzes both reduction and dehydration of atromentin to form a terphenyl triol intermediate. The pathway begin with the biosynthesis of 4-hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O-methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C-5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non- enzymatic reaction.","Catalyzes the oxidation of glyoxylate to glycolate in an alpha-oxidation process. May play a role in the detoxification of glyoxylate, a by-product of the tricarboxylic acid cycle (TCA) (Probable).",No,No,No,No,No,not-Yes,GO:0051287; GO:0050661; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.5633,0.5633,0.5633,0.5633,0.5633,5,0.5633,0.2889,no
UCDB_ASPUT,A0A0C1E1C6,Protein2Text,Eukaryota,285,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdB alone catalyzes both reduction and dehydration of atromentin to form a terphenyl triol intermediate. The pathway begin with the biosynthesis of 4-hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O-methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C-5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non- enzymatic reaction.","The molecular function of this protein is not explicitly stated in the provided information. However, based on its name, it is likely that this protein is involved in a metabolic pathway, possibly in the conversion of a substrate to a product. The name suggests that it may be a reductase, which is a type of enzyme that catalyzes the reduction of a substrate. If you have any more information or context about this protein, I may be able to provide a more specific answer.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0051287; GO:0050661; GO:0016491,,,,,,,,,,,0,,0.2889,no
UCDB_ASPUT,A0A0C1E1C6,Reference,Eukaryota,285,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdB alone catalyzes both reduction and dehydration of atromentin to form a terphenyl triol intermediate. The pathway begin with the biosynthesis of 4-hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O-methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C-5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non- enzymatic reaction.","Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdB alone catalyzes both reduction and dehydration of atromentin to form a terphenyl triol intermediate. The pathway begin with the biosynthesis of 4-hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O-methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C-5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non- enzymatic reaction.",,,,,,,GO:0051287; GO:0050661; GO:0016491,GO:0016491; GO:0051287,GO:0016616,GO:0016491; GO:0016836,GO:0016491; GO:0051287,GO:0016491,0.9573,0.3866,0.532,0.9573,0.5633,5,0.6793,0.2889,no
UCDG_ASPUT,A0A0C1E1D0,ESM2Text,Eukaryota,523,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdG is probably involved in the conversion of L-tyrosine into 4-hydroxyphenylpyruvate (HPPA) as a precursor for the usterphenyllin and uscandidusin biosynthesis (Probable). UcdE further prenylates position C-14 of ring C of usterphenyllin B to form usterphenyllin A. The pathway begin with the biosynthesis of 4-hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O- methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C- 5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non-enzymatic reaction.",Plays a key role in amino acid metabolism.,Vague,No,No,Vague,Vague,not-Yes,GO:0004069; GO:0004838; GO:0030170,,,,,,,,,,,0,,0.1586,no
UCDG_ASPUT,A0A0C1E1D0,Prot2Text,Eukaryota,523,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdG is probably involved in the conversion of L-tyrosine into 4-hydroxyphenylpyruvate (HPPA) as a precursor for the usterphenyllin and uscandidusin biosynthesis (Probable). UcdE further prenylates position C-14 of ring C of usterphenyllin B to form usterphenyllin A. The pathway begin with the biosynthesis of 4-hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O- methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C- 5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non-enzymatic reaction.","Biosynthesis of GABA from glutamate (Glu) or aspartate semialdehyde (AsSA). Involved in the biosynthesis of Asp and in the regulation of the cytokinin network. Important regulator of levels of glutamate, required for the PKC1-dependent regulation of glutamate signaling. Acts as negative regulator of glutamate homeostasis.",No,No,No,No,No,not-Yes,GO:0004069; GO:0004838; GO:0030170,GO:0004351,GO:0004351,GO:0004351,GO:0004351,GO:0004351,0.1607,0.1607,0.1607,0.1607,0.1607,5,0.1607,0.1586,no
UCDG_ASPUT,A0A0C1E1D0,ProtT3,Eukaryota,523,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdG is probably involved in the conversion of L-tyrosine into 4-hydroxyphenylpyruvate (HPPA) as a precursor for the usterphenyllin and uscandidusin biosynthesis (Probable). UcdE further prenylates position C-14 of ring C of usterphenyllin B to form usterphenyllin A. The pathway begin with the biosynthesis of 4-hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O- methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C- 5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non-enzymatic reaction.",Catalyzes a key reaction in amino acid metabolism. Cytoplasm. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family,Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004069; GO:0004838; GO:0030170,GO:0008483; GO:0030170,GO:0008483; GO:0030170,GO:0008483; GO:0030170,GO:0008483; GO:0030170,GO:0008483; GO:0030170,0.894,0.894,0.894,0.894,0.894,5,0.894,0.1586,no
UCDG_ASPUT,A0A0C1E1D0,ProtTale,Eukaryota,523,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdG is probably involved in the conversion of L-tyrosine into 4-hydroxyphenylpyruvate (HPPA) as a precursor for the usterphenyllin and uscandidusin biosynthesis (Probable). UcdE further prenylates position C-14 of ring C of usterphenyllin B to form usterphenyllin A. The pathway begin with the biosynthesis of 4-hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O- methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C- 5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non-enzymatic reaction.","Transaminase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004069; GO:0004838; GO:0030170,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.6377,0.6377,0.6377,0.6377,0.6377,5,0.6377,0.1586,no
UCDG_ASPUT,A0A0C1E1D0,Protein2Text,Eukaryota,523,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdG is probably involved in the conversion of L-tyrosine into 4-hydroxyphenylpyruvate (HPPA) as a precursor for the usterphenyllin and uscandidusin biosynthesis (Probable). UcdE further prenylates position C-14 of ring C of usterphenyllin B to form usterphenyllin A. The pathway begin with the biosynthesis of 4-hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O- methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C- 5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non-enzymatic reaction.","The molecular function of this protein is to catalyze the decarboxylation of amino acids, specifically lysine, into cadaverine, which is a reaction involved in the breakdown of amino acids.",No,No,No,No,No,not-Yes,GO:0004069; GO:0004838; GO:0030170,GO:0016831,GO:0016831,GO:0016831,GO:0008923,GO:0008923,0.1895,0.1895,0.1895,0.1607,0.1607,5,0.178,0.1586,no
UCDG_ASPUT,A0A0C1E1D0,Reference,Eukaryota,523,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdG is probably involved in the conversion of L-tyrosine into 4-hydroxyphenylpyruvate (HPPA) as a precursor for the usterphenyllin and uscandidusin biosynthesis (Probable). UcdE further prenylates position C-14 of ring C of usterphenyllin B to form usterphenyllin A. The pathway begin with the biosynthesis of 4-hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O- methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C- 5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non-enzymatic reaction.","Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdG is probably involved in the conversion of L-tyrosine into 4-hydroxyphenylpyruvate (HPPA) as a precursor for the usterphenyllin and uscandidusin biosynthesis (Probable). UcdE further prenylates position C-14 of ring C of usterphenyllin B to form usterphenyllin A. The pathway begin with the biosynthesis of 4-hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O- methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C- 5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non-enzymatic reaction.",,,,,,,GO:0004069; GO:0004838; GO:0030170,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.6377,0.6377,0.6377,0.6377,0.6377,5,0.6377,0.1586,no
PBOB_ASPUT,A0A0C1E2S7,ESM2Text,Eukaryota,483,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. Within the pathway, pboB catalyzes the acetylation of protubonine C at N-1 of the indoline ring to produce protubonine B. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L-Leu by condensing L-Leu with L-Trp. The flavin-dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.","O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the methyltransferase claB. The cytochrome P450 monooxygenase claM then catalyzes the dimerization of nataloe-emodin to cladofulvin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016746,GO:0016413,GO:0016407,GO:0016746,GO:0016407,GO:0016407,0.5794,0.729,1.0,0.729,0.729,5,0.7533,0.2329,no
PBOB_ASPUT,A0A0C1E2S7,Prot2Text,Eukaryota,483,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. Within the pathway, pboB catalyzes the acetylation of protubonine C at N-1 of the indoline ring to produce protubonine B. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L-Leu by condensing L-Leu with L-Trp. The flavin-dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.","2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the mycotoxins phomacins, leucine-derived cytochalasans with potent actin polymerization-inhibitory activities and monocot-specific antigerminative activities. The first step in the pathway is catalyzed by the hybrid PKS-NRPS phmA, assisted by the enoyl reductase phmE, that are responsible for fusion of the leucine precursor and the polyketide backbone to produce a 2-pyrrolidone intermediate. The polyketide synthase module (PKS) of phmA is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the leucine precursor. Because phmA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase phmE. Reduction by the hydrolyase phmG, followed by dehydration and intra-molecular Diels-Alder cyclization by the Diels-A",No,No,No,No,No,not-Yes,GO:0016746,GO:0016706,GO:0016706,GO:0016706,GO:0016706,GO:0016706,0.2915,0.2915,0.2915,0.2915,0.2915,5,0.2915,0.2329,no
PBOB_ASPUT,A0A0C1E2S7,ProtT3,Eukaryota,483,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. Within the pathway, pboB catalyzes the acetylation of protubonine C at N-1 of the indoline ring to produce protubonine B. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L-Leu by condensing L-Leu with L-Trp. The flavin-dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.","O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties . L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L- homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016746,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.729,0.729,0.729,0.729,0.729,5,0.729,0.2329,no
PBOB_ASPUT,A0A0C1E2S7,ProtTale,Eukaryota,483,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. Within the pathway, pboB catalyzes the acetylation of protubonine C at N-1 of the indoline ring to produce protubonine B. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L-Leu by condensing L-Leu with L-Trp. The flavin-dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.","Acyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016746,GO:0016746,GO:0016747,GO:0016747,GO:0016747,GO:0016747,1.0,0.8416,0.8416,0.8416,0.8416,5,0.8733,0.2329,no
PBOB_ASPUT,A0A0C1E2S7,Protein2Text,Eukaryota,483,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. Within the pathway, pboB catalyzes the acetylation of protubonine C at N-1 of the indoline ring to produce protubonine B. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L-Leu by condensing L-Leu with L-Trp. The flavin-dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.","The molecular function of this protein is not specified in the provided text, but it is involved in the metabolism of a molecule that is involved in the synthesis of a specific compound. The compound is not specified, but it is likely to be a steroid or a related molecule. The protein is involved in the transfer of a molecule to another molecule, which is a common function of enzymes that are involved in the synthesis of steroids and other molecules. 

Based on the information provided, it is likely that the protein is an enzyme that is involved in the metabolism of a molecule that is involved in the synthesis of a steroid or a related molecule. The specific function of the protein is not specified, but it is likely to be involved in the transfer of a molecule to another molecule, which is a common function of enzymes that are involved in the synthesis of steroids and other molecules. 

The protein is involved in the metabolism of a molecule that is involved in the synthesis of a steroid or a related molecule. The protein is likely to be an enzyme that is involved in the transfer of a molecule to another molecule. The specific function of the protein is not specified, but it is likely to be involved in the synthesis of a steroid or a related molecule.

The molecular function of this protein is not specified in the provided text, but it is likely to be involved in the metabolism of a molecule that is involved in the synthesis of a steroid or a related molecule. The protein is likely to be an enzyme that is involved in the transfer of a molecule to another molecule. The specific function of the protein is not specified, but it is likely to be involved in the synthesis of a steroid or a related molecule.

The protein is involved in the metabolism of a molecule that is involved in the synthesis of a steroid or a related molecule. The protein is likely to be an enzyme that is involved in the transfer of a molecule to another molecule. The specific function of the protein is not specified, but it is likely to be involved in the synthesis of a steroid or a related molecule.

The molecular function of this protein is not specified in the provided text, but it is likely to be involved in the metabolism of a molecule that is involved in the synthesis of a steroid or a related molecule. The protein is likely to be an enzyme that is involved in the transfer of a molecule to another molecule. The specific function of the protein is not specified, but it is likely to be involved in the synthesis of a steroid or a related molecule.

The protein is involved in the metabolism of a molecule that is involved",Vague,No,No,No,Vague,not-Yes,GO:0016746,,,,,,,,,,,0,,0.2329,no
PBOB_ASPUT,A0A0C1E2S7,Reference,Eukaryota,483,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. Within the pathway, pboB catalyzes the acetylation of protubonine C at N-1 of the indoline ring to produce protubonine B. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L-Leu by condensing L-Leu with L-Trp. The flavin-dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.","O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. Within the pathway, pboB catalyzes the acetylation of protubonine C at N-1 of the indoline ring to produce protubonine B. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L-Leu by condensing L-Leu with L-Trp. The flavin-dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.",,,,,,,GO:0016746,GO:0016747,GO:0016747,GO:0016407,GO:0016407,GO:0016746,0.8416,0.8416,0.729,0.729,1.0,5,0.8282,0.2329,no
UCDC_ASPUT,A0A0C1E5A5,ESM2Text,Eukaryota,380,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdC catalyzes O- methylation of the terphenyl triol intermediate produced by ucdB to yield terphenyllin carrying two methoxy moieties at C-9 and C-12. The pathway begin with the biosynthesis of 4- hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O-methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C-5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non- enzymatic reaction.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the benzazepine alkaloid nanangelenin A which contains an unprecedented 3,4-dihydro-1-benzazepine-2,5-dione-N-prenyl-N-acetoxy-anthranilamide scaffold. The first step of nanangelenin biosynthesis is catalyzed by the indoleamine 2,3-dioxygenase nanC which produces N-formyl-kynurenine through the catabolism of tryptophan. The two-module NRPS nanA then utilizes anthranilate (Ant) and L-kynurenine (L-Kyn) to assemble the dipeptide product nanangelenin B. The first adenylation domain of nanA (A1) loads anthranilate onto the T1 domain, while A2 loads kynurenine, generated through spontaneous nonenzymatic deformylation of the nanC-supplied N-formyl-kynurenine. The peptide bond formation between the tethered amino acids is catalyzed by the first condensation domain (C1",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2551,no
UCDC_ASPUT,A0A0C1E5A5,Prot2Text,Eukaryota,380,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdC catalyzes O- methylation of the terphenyl triol intermediate produced by ucdB to yield terphenyllin carrying two methoxy moieties at C-9 and C-12. The pathway begin with the biosynthesis of 4- hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O-methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C-5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non- enzymatic reaction.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate tolerance, py",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2551,no
UCDC_ASPUT,A0A0C1E5A5,ProtT3,Eukaryota,380,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdC catalyzes O- methylation of the terphenyl triol intermediate produced by ucdB to yield terphenyllin carrying two methoxy moieties at C-9 and C-12. The pathway begin with the biosynthesis of 4- hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O-methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C-5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non- enzymatic reaction.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By similarity). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (By similarity). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the ter",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2551,no
UCDC_ASPUT,A0A0C1E5A5,ProtTale,Eukaryota,380,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdC catalyzes O- methylation of the terphenyl triol intermediate produced by ucdB to yield terphenyllin carrying two methoxy moieties at C-9 and C-12. The pathway begin with the biosynthesis of 4- hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O-methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C-5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non- enzymatic reaction.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the saturated C-C bonds",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008168,GO:0008171,GO:0008171,GO:0008171,0.7088,0.6208,0.7088,0.7088,0.7088,5,0.6912,0.2551,no
UCDC_ASPUT,A0A0C1E5A5,Protein2Text,Eukaryota,380,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdC catalyzes O- methylation of the terphenyl triol intermediate produced by ucdB to yield terphenyllin carrying two methoxy moieties at C-9 and C-12. The pathway begin with the biosynthesis of 4- hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O-methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C-5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non- enzymatic reaction.","The molecular function of this protein is likely to be a O-methyltransferase, specifically catalyzing the O-methylation of a substrate, although the exact substrate is not specified in the provided information. O-methyltransferases are enzymes that transfer a methyl group from a donor molecule, such as S-adenosylmethionine (SAM), to a specific position on a target molecule, often resulting in the formation of a methylated product. In the case of this protein, it is likely to be involved in a methylation reaction that plays a role in the metabolism or biosynthesis of a particular molecule. However, without more specific information, the exact molecular function of this protein cannot be determined.",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2551,no
UCDC_ASPUT,A0A0C1E5A5,Reference,Eukaryota,380,"Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdC catalyzes O- methylation of the terphenyl triol intermediate produced by ucdB to yield terphenyllin carrying two methoxy moieties at C-9 and C-12. The pathway begin with the biosynthesis of 4- hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O-methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C-5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non- enzymatic reaction.","Nonribosomal peptide synthetase that mediates the biosynthesis of usterphenyllins and uscandidusins, p-terphenyl derivatives. Within the pathway, ucdC catalyzes O- methylation of the terphenyl triol intermediate produced by ucdB to yield terphenyllin carrying two methoxy moieties at C-9 and C-12. The pathway begin with the biosynthesis of 4- hydroxyphenylpyruvate (HPPA) from L-tyrosine, possibly by the aminotransferase ucdG. The nonribosomal peptide synthetase ucdA then condenses two HPPA units to produce atromentin. The key step in this pathway is the reduction and dehydration of atromentin to form a terphenyl triol intermediate, performed by the NAD-dependent dehydrogenase ucdB. Further O-methylation by the methyltransferase ucdC forms terphenyllin carrying two methoxy moieties at C-9 and C-12, and subsequent dihydroxylation at C-3 of ring A and C-15 of ring C by the flavin-dependent oxygenase ucdD leads to 3,15-dihydroxyterphenyllin. Prenylation by ucdE at position C-5 of ring A forms usterphenyllin B, and is followed by a second prenylation at position C-14 of ring C to form usterphenyllin A. The following furan ring formation that leads to uscandidusins A and B was proven to be an unexpected spontaneous non- enzymatic reaction.",,,,,,,GO:0008171; GO:0046983,GO:0008168,GO:0008171,GO:0008168,GO:0008171,GO:0008171,0.6208,0.7088,0.6208,0.7088,0.7088,5,0.6736,0.2551,no
PBOA_ASPUT,A0A0C1E6T8,ESM2Text,Eukaryota,2053,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L- Leu by condensing L-Leu with L-Trp. The flavin- dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of aspirochlorine (or antibiotic A30641), an unusual halogenated spiro compound with distinctive antifungal properties due to selective inhibition of protein biosynthesis, and which is also active against bacteria, viruses, and murine tumor cells. The non-ribosomal peptide synthetase (NRPS) aclP is responsible the formation of the diketopiperazine (DKP) core from the condensation of 2 phenylalanine residues. One Phe residue is tailored into chlorotyrosine by hydroxylation and chlorination, whereas the second Phe undergoes an unprecedented C-C bond cleavage to be converted into glycine. After formation of the DKP, sulfur is incorporated into the DKP by conjugation with glutathione by aclG, followed by its stepwise degradation to the thiol by aclI, aclJ and aclK, and the dithiol oxidation by aclT. In addition, oxygenases (aclB, aclC, aclL and aclO) and O-methyltransferases (aclM and",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,,GO:0016874,GO:0003824,GO:0016874,GO:0016874; GO:0005524,,0.709,0.5613,0.709,0.6793,4,0.6646,0.329,no
PBOA_ASPUT,A0A0C1E6T8,Prot2Text,Eukaryota,2053,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L- Leu by condensing L-Leu with L-Trp. The flavin- dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the isoquinoline alkaloids fumisoquin A, fumisoquin B and fumisoquin C; as well as small amounts of fumipyrrole as a shunt metabolite. The products of the cluster lead to a brown coloration and are important for growth and conidiation. The nonribosomal peptide synthetase-like protein fsqF, which lacks a canonical condensation domain, is required for addition of a serine in the C-terminal domain (Probable). Subsequently, a 2-oxoglutarate-dependent dioxygenase fsqD forms the products fsqA, fsqB, and fsqC (Probable). The products of the cluster lead to a brown or red coloration.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,,,GO:0016874,,GO:0016874,,,0.709,,0.709,2,0.709,0.329,no
PBOA_ASPUT,A0A0C1E6T8,ProtT3,Eukaryota,2053,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L- Leu by condensing L-Leu with L-Trp. The flavin- dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.",Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-,No,Vague,No,No,No,not-Yes,GO:0016874; GO:0031177,GO:0016747,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.3021,0.3561,0.3561,0.3561,0.3561,5,0.3453,0.329,no
PBOA_ASPUT,A0A0C1E6T8,ProtTale,Eukaryota,2053,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L- Leu by condensing L-Leu with L-Trp. The flavin- dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties. L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism. The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,GO:0016874,GO:0016874,GO:0016874,GO:0016874,,0.709,0.709,0.709,0.709,,4,0.709,0.329,no
PBOA_ASPUT,A0A0C1E6T8,Protein2Text,Eukaryota,2053,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L- Leu by condensing L-Leu with L-Trp. The flavin- dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.","This protein is a non-ribosomal peptide synthetase, which means it is involved in the synthesis of non-ribosomal peptides, a type of peptide that is synthesized by a non-ribosomal pathway rather than by the ribosome. Non-ribosomal peptides are a diverse group of compounds that include many antibiotics, antifungals, and other secondary metabolites. This protein is likely involved in the synthesis of a specific non-ribosomal peptide, but the exact function has not been specified.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,,GO:0003824,,,,,0.5613,,,,1,0.5613,0.329,no
PBOA_ASPUT,A0A0C1E6T8,Reference,Eukaryota,2053,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L- Leu by condensing L-Leu with L-Trp. The flavin- dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of protubonine B, a hydroxylated and diacetylated cyclo-L-Trp-L-Leu derivative. The first step of the protubonine B synthesis is performed by the nonribosomal peptide synthetase pboA that catalyzes the formation of cyclo-L-Trp-L- Leu by condensing L-Leu with L-Trp. The flavin- dependent monooxygenase pboD is responsible for hydroxylation at C-3 of the indole ring and subsequent formation of the pyrrolidine ring, leadind to protubonine D. Protubonine D is further diacetylated by two acetyltransferases, pboB and pboC, to form the final product protubonine B via protubonine C.",,,,,,,GO:0016874; GO:0031177,GO:0031177; GO:0016874,GO:0008927,,GO:0016874,,1.0,0.2639,,0.709,,3,0.6576,0.329,no
LP10_MYCMD,A0A0D1CHL0,ESM2Text,Eukaryota,326,Lytic polysaccharide monooxygenase (LPMO) that oxidatively cleaves alpha- and beta-chitin with C1 regioselectivity. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate. Exhibits enzymatic activity on U.maydis fungal cell wall chitin and Boosts chitin hydrolysis by chitinase GH18A.,Involved in cell wall degradation. May be involved in the polymerization of the cellulose microfibrils.,Vague,No,No,No,Vague,not-Yes,GO:0046872; GO:0004497,,,,,,,,,,,0,,0.2424,no
LP10_MYCMD,A0A0D1CHL0,Prot2Text,Eukaryota,326,Lytic polysaccharide monooxygenase (LPMO) that oxidatively cleaves alpha- and beta-chitin with C1 regioselectivity. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate. Exhibits enzymatic activity on U.maydis fungal cell wall chitin and Boosts chitin hydrolysis by chitinase GH18A.,"Fibrinogen alpha (FGA) is the major structural component of fibrinogen. Fibrin has a major function during growth, in aggregation, and in defense against osmotic stress.",No,No,No,No,No,not-Yes,GO:0046872; GO:0004497,,,,,,,,,,,0,,0.2424,no
LP10_MYCMD,A0A0D1CHL0,ProtT3,Eukaryota,326,Lytic polysaccharide monooxygenase (LPMO) that oxidatively cleaves alpha- and beta-chitin with C1 regioselectivity. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate. Exhibits enzymatic activity on U.maydis fungal cell wall chitin and Boosts chitin hydrolysis by chitinase GH18A.,"Plays a role in the degradation of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Secreted",No,No,No,No,No,not-Yes,GO:0046872; GO:0004497,,GO:0016798,GO:0016798,GO:0016798,GO:0016798,,0.3023,0.3023,0.3023,0.3023,4,0.3023,0.2424,no
LP10_MYCMD,A0A0D1CHL0,ProtTale,Eukaryota,326,Lytic polysaccharide monooxygenase (LPMO) that oxidatively cleaves alpha- and beta-chitin with C1 regioselectivity. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate. Exhibits enzymatic activity on U.maydis fungal cell wall chitin and Boosts chitin hydrolysis by chitinase GH18A.,Secreted effector that acts as a pathogen-associated molecular pattern (PAMP) recognized by the plant immune system.,No,No,No,No,No,not-Yes,GO:0046872; GO:0004497,,,,,,,,,,,0,,0.2424,no
LP10_MYCMD,A0A0D1CHL0,Protein2Text,Eukaryota,326,Lytic polysaccharide monooxygenase (LPMO) that oxidatively cleaves alpha- and beta-chitin with C1 regioselectivity. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate. Exhibits enzymatic activity on U.maydis fungal cell wall chitin and Boosts chitin hydrolysis by chitinase GH18A.,"This protein is involved in the molecular function of binding to cellulose, a process that is likely related to its role in the degradation of cellulose in fungi. Specifically, it is a cellulose-binding protein, which allows it to interact with and break down cellulose, a key component of plant cell walls. This is likely an important function for this protein in the degradation of plant material by fungi. 
Protein name: Cellulose-binding protein 
Protein ID: 14590 
Protein family: Glycosyl hydrolase family 5 
Protein function: Cellulose-binding protein; part of the gene cluster that mediates the degradation of cellulose and hemicellulose during lignocellulose degradation. The first step is the degradation of hemicellulose, which is then followed by the degradation of cellulose. The cellulose-binding protein is a major component of the cellulase complex and plays a role in the degradation of cellulose. The cellulase complex is composed of 3 major proteins, including a cellulose-binding protein, a processive endoglucanase, and an exoglucanase. The cellulase complex is also required for the degradation of native cellulose. The cellulase complex is also able to degrade xylan, a major component of hemicellulose, but is less effective than the xylanase complex.
Protein location: Cell wall
Protein type: Glycosyl hydrolase; Cellulose-binding protein
Protein domains: Cellulose-binding domain; Glycosyl hydrolase domain
Protein subcellular location: Cell wall
Protein subunit: Monomeric
Protein sequence: 100% identical to the predicted protein sequence of 14590; 100% identical to the predicted protein sequence of 14591
Protein synonyms: CBP1; CBP1_14590; CBP1_14591; CBP2; CBP2_14590; CBP2_14591
Protein accession number: 14590; 14591
Protein length: 342 aa; 342 aa
Protein molecular weight: 38.8 kDa; 38.8 kDa
Protein isozyme: Monomeric
Protein quaternary structure: Monomeric
Protein subcellular location: Cell wall
Protein subunit: Monomeric
Protein synonyms: CBP1; CB",No,No,No,No,No,not-Yes,GO:0046872; GO:0004497,GO:0030248; GO:0008810,GO:0030245; GO:0008422,GO:0008422; GO:0030245,GO:0030245; GO:0008810,GO:0008810,0.2599,0.1455,0.1455,0.1644,0.2193,5,0.1869,0.2424,no
LP10_MYCMD,A0A0D1CHL0,Reference,Eukaryota,326,Lytic polysaccharide monooxygenase (LPMO) that oxidatively cleaves alpha- and beta-chitin with C1 regioselectivity. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate. Exhibits enzymatic activity on U.maydis fungal cell wall chitin and Boosts chitin hydrolysis by chitinase GH18A.,Lytic polysaccharide monooxygenase (LPMO) that oxidatively cleaves alpha- and beta-chitin with C1 regioselectivity. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate. Exhibits enzymatic activity on U.maydis fungal cell wall chitin and Boosts chitin hydrolysis by chitinase GH18A.,,,,,,,GO:0046872; GO:0004497,GO:0016491; GO:0005507,GO:0016491,GO:0004497; GO:0005507,GO:0016491; GO:0005507,GO:0016491,0.7926,0.5957,0.8854,0.7926,0.5957,5,0.7324,0.2424,no
HYG17_STRLW,A0A0F7VN41,ESM2Text,Bacteria,325,"Dehydrogenase involved in the biosynthesis of the aminocyclitol moiety of hygromycin A, a broad-spectrum antibiotic. Catalyzes the NAD(+)-dependent oxidation of myo- inositol to myo-inosose-5 (neo-inosose). Shows reduced activity with scyllo-inositol, minimal activity with L-chiro- inositol and no activity with D-glucose, D-chiro-inositol, epi- inositol, muco-inositol and allo-inositol. Is specific for NAD(+) and cannot use NADP(+).",Involved in the biosynthesis of the anthracycline aclacinomycin which is an important component in the aerobic microaerobic growth of M.tuberculosis. Catalyzes the oxidation of the L-tryptophan analog NB-(L-AChi-2-amine) to yield N-acetyl-L-ornithine. It can also use D-Asp-L-carvone analog NB-(L-AChi-3-amine).,No,Maybe,Maybe,No,No,not-Yes,GO:0000166; GO:0016491,GO:0016491,GO:0016491,,,GO:0016491,0.7229,0.7229,,,0.7229,3,0.7229,0.2404,no
HYG17_STRLW,A0A0F7VN41,Prot2Text,Bacteria,325,"Dehydrogenase involved in the biosynthesis of the aminocyclitol moiety of hygromycin A, a broad-spectrum antibiotic. Catalyzes the NAD(+)-dependent oxidation of myo- inositol to myo-inosose-5 (neo-inosose). Shows reduced activity with scyllo-inositol, minimal activity with L-chiro- inositol and no activity with D-glucose, D-chiro-inositol, epi- inositol, muco-inositol and allo-inositol. Is specific for NAD(+) and cannot use NADP(+).",Involved in the oxidation of myo-inositol (MI) to 2-keto-myo-inositol (2KMI or 2-inosose).,Yes,Yes,Maybe,Maybe,Yes,Yes,GO:0000166; GO:0016491,GO:0050113,GO:0008440,GO:0016616,GO:0008440,GO:0008440,0.44,0.2066,0.4994,0.2066,0.2066,5,0.3118,0.2404,no
HYG17_STRLW,A0A0F7VN41,ProtT3,Bacteria,325,"Dehydrogenase involved in the biosynthesis of the aminocyclitol moiety of hygromycin A, a broad-spectrum antibiotic. Catalyzes the NAD(+)-dependent oxidation of myo- inositol to myo-inosose-5 (neo-inosose). Shows reduced activity with scyllo-inositol, minimal activity with L-chiro- inositol and no activity with D-glucose, D-chiro-inositol, epi- inositol, muco-inositol and allo-inositol. Is specific for NAD(+) and cannot use NADP(+).",Involved in the oxidation of myo-inositol (MI) to 2-keto-myo- inositol (2KMI or 2-inosose). Belongs to the Gfo/Idh/MocA family,Yes,Yes,Maybe,Yes,Yes,Yes,GO:0000166; GO:0016491,GO:0008812,GO:0047954,GO:0050113,GO:0016614,GO:0047954,0.4994,0.2427,0.44,0.5895,0.2427,5,0.4029,0.2404,no
HYG17_STRLW,A0A0F7VN41,ProtTale,Bacteria,325,"Dehydrogenase involved in the biosynthesis of the aminocyclitol moiety of hygromycin A, a broad-spectrum antibiotic. Catalyzes the NAD(+)-dependent oxidation of myo- inositol to myo-inosose-5 (neo-inosose). Shows reduced activity with scyllo-inositol, minimal activity with L-chiro- inositol and no activity with D-glucose, D-chiro-inositol, epi- inositol, muco-inositol and allo-inositol. Is specific for NAD(+) and cannot use NADP(+).",Involved in the oxidation of myo-inositol (MI) to 2-keto-myo- inositol (2KMI or 2-inosose).,Yes,Yes,Maybe,Yes,Yes,Yes,GO:0000166; GO:0016491,GO:0016491,GO:0016491,GO:0050113,GO:0016491,GO:0016491,0.7229,0.7229,0.44,0.7229,0.7229,5,0.6663,0.2404,no
HYG17_STRLW,A0A0F7VN41,Protein2Text,Bacteria,325,"Dehydrogenase involved in the biosynthesis of the aminocyclitol moiety of hygromycin A, a broad-spectrum antibiotic. Catalyzes the NAD(+)-dependent oxidation of myo- inositol to myo-inosose-5 (neo-inosose). Shows reduced activity with scyllo-inositol, minimal activity with L-chiro- inositol and no activity with D-glucose, D-chiro-inositol, epi- inositol, muco-inositol and allo-inositol. Is specific for NAD(+) and cannot use NADP(+).","The molecular function of this protein is an oxidoreductase. More specifically, it acts as a quinone reductase, which is a type of oxidoreductase that reduces quinones.",No,No,No,No,No,not-Yes,GO:0000166; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0003955,0.7229,0.7229,0.7229,0.7229,0.4359,5,0.6655,0.2404,no
HYG17_STRLW,A0A0F7VN41,Reference,Bacteria,325,"Dehydrogenase involved in the biosynthesis of the aminocyclitol moiety of hygromycin A, a broad-spectrum antibiotic. Catalyzes the NAD(+)-dependent oxidation of myo- inositol to myo-inosose-5 (neo-inosose). Shows reduced activity with scyllo-inositol, minimal activity with L-chiro- inositol and no activity with D-glucose, D-chiro-inositol, epi- inositol, muco-inositol and allo-inositol. Is specific for NAD(+) and cannot use NADP(+).","Dehydrogenase involved in the biosynthesis of the aminocyclitol moiety of hygromycin A, a broad-spectrum antibiotic. Catalyzes the NAD(+)-dependent oxidation of myo- inositol to myo-inosose-5 (neo-inosose). Shows reduced activity with scyllo-inositol, minimal activity with L-chiro- inositol and no activity with D-glucose, D-chiro-inositol, epi- inositol, muco-inositol and allo-inositol. Is specific for NAD(+) and cannot use NADP(+).",,,,,,,GO:0000166; GO:0016491,GO:0016491; GO:0051287,GO:0016616,GO:0016616,GO:0008440; GO:0051287,GO:0016614,0.8656,0.4994,0.4994,0.5002,0.5895,5,0.5908,0.2404,no
MENI_LISM4,A0A0H3GEM5,ESM2Text,Bacteria,123,"Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA) and free coenzyme A. Production of DHNA is required for protection against bacteriolysis in the cytosol of macrophages and tissue-specific virulence in vivo, suggesting that MenI is required to protect the bacteria from killing in the macrophage cytosol.","Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to form phyllo-naphthoate (P-CoA).",Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0061522,GO:0016790,GO:0016790,GO:0016790,GO:0016790,GO:0016790,0.7055,0.7055,0.7055,0.7055,0.7055,5,0.7055,0.2152,no
MENI_LISM4,A0A0H3GEM5,Prot2Text,Bacteria,123,"Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA) and free coenzyme A. Production of DHNA is required for protection against bacteriolysis in the cytosol of macrophages and tissue-specific virulence in vivo, suggesting that MenI is required to protect the bacteria from killing in the macrophage cytosol.",Is not required for competence.,Vague,No,No,No,Vague,not-Yes,GO:0061522,,,,,,,,,,,0,,0.2152,no
MENI_LISM4,A0A0H3GEM5,ProtT3,Bacteria,123,"Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA) and free coenzyme A. Production of DHNA is required for protection against bacteriolysis in the cytosol of macrophages and tissue-specific virulence in vivo, suggesting that MenI is required to protect the bacteria from killing in the macrophage cytosol.",Belongs to the thioesterase PaaI family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0061522,GO:0016790,GO:0016790,GO:0016790,GO:0016790,GO:0016790,0.7055,0.7055,0.7055,0.7055,0.7055,5,0.7055,0.2152,no
MENI_LISM4,A0A0H3GEM5,ProtTale,Bacteria,123,"Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA) and free coenzyme A. Production of DHNA is required for protection against bacteriolysis in the cytosol of macrophages and tissue-specific virulence in vivo, suggesting that MenI is required to protect the bacteria from killing in the macrophage cytosol.",Probably plays a role in amino acid transport.,No,No,No,No,No,not-Yes,GO:0061522,GO:0015171,,GO:0015171,GO:0015171,GO:0015171,0.117,,0.117,0.117,0.117,4,0.117,0.2152,no
MENI_LISM4,A0A0H3GEM5,Protein2Text,Bacteria,123,"Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA) and free coenzyme A. Production of DHNA is required for protection against bacteriolysis in the cytosol of macrophages and tissue-specific virulence in vivo, suggesting that MenI is required to protect the bacteria from killing in the macrophage cytosol.","The molecular function of this protein is not explicitly stated in the provided information. However, based on its classification as an antibiotic resistance protein, it is likely involved in conferring resistance to antibiotics or other antimicrobial agents.",No,Vague,No,No,Vague,not-Yes,GO:0061522,,,,,,,,,,,0,,0.2152,no
MENI_LISM4,A0A0H3GEM5,Reference,Bacteria,123,"Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA) and free coenzyme A. Production of DHNA is required for protection against bacteriolysis in the cytosol of macrophages and tissue-specific virulence in vivo, suggesting that MenI is required to protect the bacteria from killing in the macrophage cytosol.","Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA) and free coenzyme A. Production of DHNA is required for protection against bacteriolysis in the cytosol of macrophages and tissue-specific virulence in vivo, suggesting that MenI is required to protect the bacteria from killing in the macrophage cytosol.",,,,,,,GO:0061522,GO:0016790,GO:0016790,GO:0016790,GO:0016790,GO:0016790,0.7055,0.7055,0.7055,0.7055,0.7055,5,0.7055,0.2152,no
B2109_BORBR,A0A0H3LMJ1,ESM2Text,Bacteria,960,Required for cyclic-di-GMP-mediated inhibition of motility and enhancement of biofilm formation by BdcA. It may stimulate BdcA activity. May act as a cyclic-di-GMP binding protein.,Member of the two-component regulatory system DltS/DltR. Activates DltR by phosphorylation.,No,No,No,No,No,not-Yes,GO:0071111; GO:0000155,GO:0000155,GO:0000155,GO:0000155; GO:0005524,GO:0000155; GO:0005524,GO:0000155; GO:0005524,0.7092,0.7092,0.5451,0.5451,0.5451,5,0.6107,0.5756,yes
B2109_BORBR,A0A0H3LMJ1,Prot2Text,Bacteria,960,Required for cyclic-di-GMP-mediated inhibition of motility and enhancement of biofilm formation by BdcA. It may stimulate BdcA activity. May act as a cyclic-di-GMP binding protein.,Phosphorylates the sporulation-regulatory proteins spo0A and spo0F. Spo0F is required for the KinB activity.,No,No,No,No,No,not-Yes,GO:0071111; GO:0000155,GO:0000155,GO:0004672,GO:0000155,GO:0004673,GO:0004673,0.7092,0.5366,0.7092,0.6022,0.6022,5,0.6319,0.5756,yes
B2109_BORBR,A0A0H3LMJ1,ProtT3,Bacteria,960,Required for cyclic-di-GMP-mediated inhibition of motility and enhancement of biofilm formation by BdcA. It may stimulate BdcA activity. May act as a cyclic-di-GMP binding protein.,Member of the two-component regulatory system NtrB/NtrC involved in the regulation of nitrogen metabolism. Phosphorylates NtrC. Cell inner membrane; Multi-pass membrane protein,No,No,No,No,No,not-Yes,GO:0071111; GO:0000155,GO:0000155; GO:0005524,GO:0000155; GO:0005524,GO:0000155,GO:0000155; GO:0005524,GO:0000155; GO:0005524,0.5451,0.5451,0.7092,0.5451,0.5451,5,0.5779,0.5756,yes
B2109_BORBR,A0A0H3LMJ1,ProtTale,Bacteria,960,Required for cyclic-di-GMP-mediated inhibition of motility and enhancement of biofilm formation by BdcA. It may stimulate BdcA activity. May act as a cyclic-di-GMP binding protein.,Plays a role in the regulation of biofilm formation and motility through a two-component regulatory system. Phosphorylates CheY-P at the C-terminus as part of the two-component regulatory system composed of ChpS/ChpS-like and ChpR/ChpR-like. Binds to autoinducer 2 (AI-2).,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0071111; GO:0000155,GO:0000155,GO:0016301,GO:0016301,GO:0000155,GO:0004672,0.7092,0.4073,0.4073,0.7092,0.5366,5,0.5539,0.5756,yes
B2109_BORBR,A0A0H3LMJ1,Protein2Text,Bacteria,960,Required for cyclic-di-GMP-mediated inhibition of motility and enhancement of biofilm formation by BdcA. It may stimulate BdcA activity. May act as a cyclic-di-GMP binding protein.,"The molecular function of this protein is not specified in the provided text. However, based on its name, it is likely that this protein is involved in sensing or responding to environmental signals, possibly as part of a two-component regulatory system. Specifically, it is likely that this protein is a sensor kinase that detects environmental changes and activates a downstream response by phosphorylating a response regulator protein. However, without more information, it is difficult to provide a more specific description of its molecular function.",Vague,Vague,No,Vague,Vague,not-Yes,GO:0071111; GO:0000155,,,,,,,,,,,0,,0.5756,yes
B2109_BORBR,A0A0H3LMJ1,Reference,Bacteria,960,Required for cyclic-di-GMP-mediated inhibition of motility and enhancement of biofilm formation by BdcA. It may stimulate BdcA activity. May act as a cyclic-di-GMP binding protein.,Required for cyclic-di-GMP-mediated inhibition of motility and enhancement of biofilm formation by BdcA. It may stimulate BdcA activity. May act as a cyclic-di-GMP binding protein.,,,,,,,GO:0071111; GO:0000155,,,,,,,,,,,0,,0.5756,yes
BDCB_BORBR,A0A0H3LSV1,ESM2Text,Bacteria,251,"Diguanylate cyclase involved in the regulation of swimming motility and biofilm formation. Probably catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. Overexpression of bdcB inhibits flagella expression and motility, and enhances biofilm formation. It is not required for colonization of the mice's respiratory tract, but it contributes to the ability of bacteria to persist within macrophages and to suppress cytokine responses by macrophages. It also contributes to the inhibition of the expression of type III secretion system (T3SS) components.",Penicillin-binding protein.,No,Maybe,No,No,No,not-Yes,GO:0052621,,GO:0008658,,GO:0008658,GO:0008658,,0.0766,,0.0766,0.0766,3,0.0766,0.5098,no
BDCB_BORBR,A0A0H3LSV1,Prot2Text,Bacteria,251,"Diguanylate cyclase involved in the regulation of swimming motility and biofilm formation. Probably catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. Overexpression of bdcB inhibits flagella expression and motility, and enhances biofilm formation. It is not required for colonization of the mice's respiratory tract, but it contributes to the ability of bacteria to persist within macrophages and to suppress cytokine responses by macrophages. It also contributes to the inhibition of the expression of type III secretion system (T3SS) components.",Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules.,Yes,Yes,Maybe,Yes,Yes,Yes,GO:0052621,GO:0052621,GO:0052621,GO:0052621,GO:0052621,GO:0052621,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5098,no
BDCB_BORBR,A0A0H3LSV1,ProtT3,Bacteria,251,"Diguanylate cyclase involved in the regulation of swimming motility and biofilm formation. Probably catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. Overexpression of bdcB inhibits flagella expression and motility, and enhances biofilm formation. It is not required for colonization of the mice's respiratory tract, but it contributes to the ability of bacteria to persist within macrophages and to suppress cytokine responses by macrophages. It also contributes to the inhibition of the expression of type III secretion system (T3SS) components.",May catalyze the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules,Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0052621,GO:0052621,GO:0052621,GO:0052621,GO:0052621,GO:0052929,1.0,1.0,1.0,1.0,0.5121,5,0.9024,0.5098,no
BDCB_BORBR,A0A0H3LSV1,ProtTale,Bacteria,251,"Diguanylate cyclase involved in the regulation of swimming motility and biofilm formation. Probably catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. Overexpression of bdcB inhibits flagella expression and motility, and enhances biofilm formation. It is not required for colonization of the mice's respiratory tract, but it contributes to the ability of bacteria to persist within macrophages and to suppress cytokine responses by macrophages. It also contributes to the inhibition of the expression of type III secretion system (T3SS) components.",Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules.,Yes,Yes,Maybe,Yes,Yes,Yes,GO:0052621,GO:0052621,GO:0052929,GO:0052621,GO:0052621,GO:0052621,1.0,0.5121,1.0,1.0,1.0,5,0.9024,0.5098,no
BDCB_BORBR,A0A0H3LSV1,Protein2Text,Bacteria,251,"Diguanylate cyclase involved in the regulation of swimming motility and biofilm formation. Probably catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. Overexpression of bdcB inhibits flagella expression and motility, and enhances biofilm formation. It is not required for colonization of the mice's respiratory tract, but it contributes to the ability of bacteria to persist within macrophages and to suppress cytokine responses by macrophages. It also contributes to the inhibition of the expression of type III secretion system (T3SS) components.","The molecular function of this protein is not specified, but based on its name, it is likely involved in the regulation of gene expression or other cellular processes. However, the exact function is not provided in the given text.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0052621,,,,,,,,,,,0,,0.5098,no
BDCB_BORBR,A0A0H3LSV1,Reference,Bacteria,251,"Diguanylate cyclase involved in the regulation of swimming motility and biofilm formation. Probably catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. Overexpression of bdcB inhibits flagella expression and motility, and enhances biofilm formation. It is not required for colonization of the mice's respiratory tract, but it contributes to the ability of bacteria to persist within macrophages and to suppress cytokine responses by macrophages. It also contributes to the inhibition of the expression of type III secretion system (T3SS) components.","Diguanylate cyclase involved in the regulation of swimming motility and biofilm formation. Probably catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. Overexpression of bdcB inhibits flagella expression and motility, and enhances biofilm formation. It is not required for colonization of the mice's respiratory tract, but it contributes to the ability of bacteria to persist within macrophages and to suppress cytokine responses by macrophages. It also contributes to the inhibition of the expression of type III secretion system (T3SS) components.",,,,,,,GO:0052621,GO:0052621,GO:0052621,GO:0016779,GO:0052621,GO:0052621,1.0,1.0,0.8582,1.0,1.0,5,0.9716,0.5098,no
ETPI_ESCWE,A0A0M8N9N3,ESM2Text,Eukaryota,461,"Aminotransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","Probable aminotransferase; part of the gene cluster that mediates the biosynthesis of anditomin, a fungal meroterpenoid. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase andM. DMOA is then prenylated into farnesyl-DMOA by the polyprenyl transferase andK. Methylation by the methyltransferase andDMOA then leads to farnesyl-DMOA methyl ester which is further subject to epoxidation by the FAD-dependent monooxygenase andB to yield epoxyfarnesyl-DMOA methyl ester. Cyclization of epoxyfarnesyl-DMOA methyl ester by the terpene cyclase andC leads to the production of anditomin. The androgen receptor andR are then presumably responsible for the androgen-induced androgen-dependent enhancement of the androgen-stimulated activity. There are two branches to synthesize DMOA. In one branch, the geranylgeranyl diphosphate synthase catalyzes the C20 methylation of ger",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016829; GO:0030170; GO:0008483,GO:0008483,GO:0008483,,GO:0008483; GO:0030170,GO:0008483; GO:0030170,0.622,0.622,,0.8814,0.8814,4,0.7517,0.4581,no
ETPI_ESCWE,A0A0M8N9N3,Prot2Text,Eukaryota,461,"Aminotransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).",Probable aminotransferase.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016829; GO:0030170; GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.622,0.622,0.622,0.622,0.622,5,0.622,0.4581,no
ETPI_ESCWE,A0A0M8N9N3,ProtT3,Eukaryota,461,"Aminotransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).",1-aminocyclopropane-1-carboxylate synthase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC,No,No,Maybe,No,No,not-Yes,GO:0016829; GO:0030170; GO:0008483,GO:0016847,GO:0016847,GO:0016847,GO:0016847,GO:0016847,0.4336,0.4336,0.4336,0.4336,0.4336,5,0.4336,0.4581,no
ETPI_ESCWE,A0A0M8N9N3,ProtTale,Eukaryota,461,"Aminotransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).",Converts indole-3-pyruvate (IPA) to indole-3-acetamide (IAM).,No,No,No,No,No,not-Yes,GO:0016829; GO:0030170; GO:0008483,GO:0016491,GO:0016491,,,,0.4263,0.4263,,,,2,0.4263,0.4581,no
ETPI_ESCWE,A0A0M8N9N3,Protein2Text,Eukaryota,461,"Aminotransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","The molecular function of this protein is not explicitly stated in the provided text. However, based on its name, it is likely that this protein is involved in the metabolism of amino acids, specifically in the transfer of a methyl group from one molecule to another. More specifically, it is a lysine decarboxylase, which catalyzes the decarboxylation of lysine to cadaverine.",Vague,Vague,No,No,Vague,not-Yes,GO:0016829; GO:0030170; GO:0008483,GO:0016831,GO:0016831,GO:0016831,GO:0008923,GO:0008923,0.4336,0.4336,0.4336,0.3771,0.3771,5,0.411,0.4581,no
ETPI_ESCWE,A0A0M8N9N3,Reference,Eukaryota,461,"Aminotransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","Aminotransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).",,,,,,,GO:0016829; GO:0030170; GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.622,0.622,0.622,0.622,0.622,5,0.622,0.4581,no
ETPM_ESCWE,A0A0M9VX70,ESM2Text,Eukaryota,403,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the benzazepine alkaloid nanangelenin A which contains an unprecedented 3,4-dihydro-1-benzazepine-2,5-dione-N-prenyl-N-acetoxy-anthranilamide scaffold. The first step of nanangelenin biosynthesis is catalyzed by the indoleamine 2,3-dioxygenase nanC which produces N-formyl-kynurenine through the catabolism of tryptophan. The two-module NRPS nanA then utilizes anthranilate FAD or a subset of flavins (pB, pC, pE and pF) to assemble the dipeptide product nanangelenin B. The first adenylation domain of nanA (A1) loads anthranilate onto the T1 domain, while A2 loads kynurenine, generated through spontaneous nonenzymatic deformylation of the nanC-supplied N-formyl-kynurenine. The peptide bond formation between the tethered amino acids is catalyzed by the first cond",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2531,no
ETPM_ESCWE,A0A0M9VX70,Prot2Text,Eukaryota,403,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate tolerance, py",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2531,no
ETPM_ESCWE,A0A0M9VX70,ProtT3,Eukaryota,403,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).",O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeran,Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2531,no
ETPM_ESCWE,A0A0M9VX70,ProtTale,Eukaryota,403,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the saturated C-C bonds",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008168,GO:0008171,GO:0008171,GO:0008171,0.7088,0.6208,0.7088,0.7088,0.7088,5,0.6912,0.2531,no
ETPM_ESCWE,A0A0M9VX70,Protein2Text,Eukaryota,403,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","The molecular function of this protein is a O-methyltransferase. It catalyzes the transfer of a methyl group to a substrate. Specifically, it is involved in the O-methylation of a metabolite, which is likely involved in the regulation of its activity or stability. 
This protein is likely involved in the metabolism of a specific compound, possibly a plant defense-related compound. The exact function and substrate specificity of this protein are not well understood and require further research.",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2531,no
ETPM_ESCWE,A0A0M9VX70,Reference,Eukaryota,403,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).",,,,,,,GO:0008171; GO:0046983,GO:0008168,GO:0008171,GO:0008168,GO:0008171,GO:0008171,0.6208,0.7088,0.6208,0.7088,0.7088,5,0.6736,0.2531,no
ETPP_ESCWE,A0A0M9VX85,ESM2Text,Eukaryota,1951,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster- specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","Acyl-CoA synthetase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ. Paxilline is converted to beta",No,No,No,No,No,not-Yes,GO:0016874; GO:0031177,GO:0016405,GO:0003996,GO:0003824,GO:0016874,GO:0016874,0.4906,0.3163,0.5613,0.709,0.709,5,0.5572,0.3128,no
ETPP_ESCWE,A0A0M9VX85,Prot2Text,Eukaryota,1951,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster- specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","Acyl-CoA synthetase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ. Paxilline is converted to beta",No,No,No,No,No,not-Yes,GO:0016874; GO:0031177,GO:0016878,GO:0016878,GO:0003996,GO:0003996,GO:0016878,0.4906,0.4906,0.3163,0.3163,0.4906,5,0.4209,0.3128,no
ETPP_ESCWE,A0A0M9VX85,ProtT3,Eukaryota,1951,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster- specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).",Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-,No,No,No,No,No,not-Yes,GO:0016874; GO:0031177,GO:0016747,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.3021,0.3561,0.3561,0.3561,0.3561,5,0.3453,0.3128,no
ETPP_ESCWE,A0A0M9VX85,ProtTale,Eukaryota,1951,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster- specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3- hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,GO:0016874,GO:0016874,GO:0016874,GO:0016874,,0.709,0.709,0.709,0.709,,4,0.709,0.3128,no
ETPP_ESCWE,A0A0M9VX85,Protein2Text,Eukaryota,1951,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster- specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","This protein is a non-reducing polyketide synthase, which means it is involved in the synthesis of polyketides, a class of natural products with diverse biological activities. Specifically, it is involved in the biosynthesis of a polyketide metabolite, which is a type of secondary metabolite that can have various functions such as antimicrobial, antifungal, or antitumor activities.",No,No,No,Maybe,Maybe,not-Yes,GO:0016874; GO:0031177,,,,,,,,,,,0,,0.3128,no
ETPP_ESCWE,A0A0M9VX85,Reference,Eukaryota,1951,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster- specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster- specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).",,,,,,,GO:0016874; GO:0031177,GO:0031177; GO:0016874,GO:0008927,,GO:0016874,,1.0,0.2639,,0.709,,3,0.6576,0.3128,no
ETPT_ESCWE,A0A0M9VXC7,ESM2Text,Eukaryota,338,"Thioredoxin reductase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","Involved in thioredoxin reductase biosynthesis. Catalyzes the reduction of reactive oxygen species (ROS) to hydrogen peroxide. NADPH is the best cofactor, but it can also use NADH.",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491; GO:0050661,GO:0016491; GO:0050661,1.0,1.0,1.0,0.7089,0.7089,5,0.8836,0.3,no
ETPT_ESCWE,A0A0M9VXC7,Prot2Text,Eukaryota,338,"Thioredoxin reductase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","An electron transfer flavoprotein with reductase activity, able to reduce Fe(3+) to Fe(2+) before the cytochrome is released (Probable). May be involved in the reduction of a quinone.",Maybe,No,No,No,Maybe,not-Yes,GO:0016491,GO:0009055,GO:0009055,GO:0009055; GO:0016491,GO:0009055; GO:0016491,GO:0009055,0.3396,0.3396,0.7799,0.7799,0.3396,5,0.5157,0.3,no
ETPT_ESCWE,A0A0M9VXC7,ProtT3,Eukaryota,338,"Thioredoxin reductase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","Thioredoxin reductase; part of the gene cluster that mediates the biosynthesis of notoamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first step of notoamide biosynthesis involves coupling of L-proline and L-tryptophan by the bimodular NRPS notE, to produce cyclo-L-tryptophan-L-proline called brevianamide F . The reverse pren",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,GO:0004791,GO:0004791,GO:0004791,GO:0004791,GO:0004791,0.4186,0.4186,0.4186,0.4186,0.4186,5,0.4186,0.3,no
ETPT_ESCWE,A0A0M9VXC7,ProtTale,Eukaryota,338,"Thioredoxin reductase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.",No,No,No,No,No,not-Yes,GO:0016491,GO:0004601,GO:0004601,GO:0004601,GO:0004601,GO:0004601,0.6194,0.6194,0.6194,0.6194,0.6194,5,0.6194,0.3,no
ETPT_ESCWE,A0A0M9VXC7,Protein2Text,Eukaryota,338,"Thioredoxin reductase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","The molecular function of this protein is unknown. The protein is involved in the reduction of a compound, but the exact molecular function is not specified.",Vague,Vague,No,No,Vague,not-Yes,GO:0016491,,,,,,,,,,,0,,0.3,no
ETPT_ESCWE,A0A0M9VXC7,Reference,Eukaryota,338,"Thioredoxin reductase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","Thioredoxin reductase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).",,,,,,,GO:0016491,GO:0004791; GO:0050660,GO:0004791,GO:0004791,GO:0004791,GO:0004791,0.3207,0.4186,0.4186,0.4186,0.4186,5,0.399,0.3,no
F6PCT_CAMJU,A0A0Q3NN41,ESM2Text,Bacteria,237,"Cytidylyltransferase involved in the biosynthesis of capsular polysaccharides. Catalyzes the formation of cytidine diphosphate (CDP)-6-D-fructose from cytidine triphosphate (CTP) and D- fructose-6-phosphate. Shows less than 1% of activity with ATP, GTP, UTP and other sugar donors, such as D-fructose-1- phosphate, D-glucose-6-phosphate, alpha-D-glucose-1-phosphate or D- glucitol-6-phosphate.",Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0050518,GO:0008685,GO:0008685,GO:0004140,GO:0008685,GO:0008685,0.2067,0.2067,0.4029,0.2067,0.2067,5,0.2459,0.5458,yes
F6PCT_CAMJU,A0A0Q3NN41,Prot2Text,Bacteria,237,"Cytidylyltransferase involved in the biosynthesis of capsular polysaccharides. Catalyzes the formation of cytidine diphosphate (CDP)-6-D-fructose from cytidine triphosphate (CTP) and D- fructose-6-phosphate. Shows less than 1% of activity with ATP, GTP, UTP and other sugar donors, such as D-fructose-1- phosphate, D-glucose-6-phosphate, alpha-D-glucose-1-phosphate or D- glucitol-6-phosphate.",Catalyzes the transfer of the cytidylyl group of CTP to D-ribitol 5-phosphate.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0050518,GO:0008810,GO:0008782,GO:0016779,GO:0016779,GO:0070566,0.1737,0.1737,0.7539,0.7539,0.6335,5,0.4977,0.5458,yes
F6PCT_CAMJU,A0A0Q3NN41,ProtT3,Bacteria,237,"Cytidylyltransferase involved in the biosynthesis of capsular polysaccharides. Catalyzes the formation of cytidine diphosphate (CDP)-6-D-fructose from cytidine triphosphate (CTP) and D- fructose-6-phosphate. Shows less than 1% of activity with ATP, GTP, UTP and other sugar donors, such as D-fructose-1- phosphate, D-glucose-6-phosphate, alpha-D-glucose-1-phosphate or D- glucitol-6-phosphate.",Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D- erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0050518,GO:0008685,GO:0043751,GO:0050518,GO:0050518,GO:0008685,0.2067,0.4451,1.0,1.0,0.2067,5,0.5717,0.5458,yes
F6PCT_CAMJU,A0A0Q3NN41,ProtTale,Bacteria,237,"Cytidylyltransferase involved in the biosynthesis of capsular polysaccharides. Catalyzes the formation of cytidine diphosphate (CDP)-6-D-fructose from cytidine triphosphate (CTP) and D- fructose-6-phosphate. Shows less than 1% of activity with ATP, GTP, UTP and other sugar donors, such as D-fructose-1- phosphate, D-glucose-6-phosphate, alpha-D-glucose-1-phosphate or D- glucitol-6-phosphate.",Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D- erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).,Maybe,No,Maybe,No,Maybe,not-Yes,GO:0050518,GO:0050518,GO:0016779,GO:0016779,GO:0016779,GO:0050518,1.0,0.7539,0.7539,0.7539,1.0,5,0.8523,0.5458,yes
F6PCT_CAMJU,A0A0Q3NN41,Protein2Text,Bacteria,237,"Cytidylyltransferase involved in the biosynthesis of capsular polysaccharides. Catalyzes the formation of cytidine diphosphate (CDP)-6-D-fructose from cytidine triphosphate (CTP) and D- fructose-6-phosphate. Shows less than 1% of activity with ATP, GTP, UTP and other sugar donors, such as D-fructose-1- phosphate, D-glucose-6-phosphate, alpha-D-glucose-1-phosphate or D- glucitol-6-phosphate.","The molecular function of this protein is a transferase activity, specifically aminotransferase activity. It catalyzes the transfer of an amino group from a donor molecule to a keto group of a keto acid. In this case, it is involved in the synthesis of pyridoxal 5'-phosphate (PLP), a cofactor for many enzymatic reactions. It is responsible for the amination of 4-hydroxy-2-oxoglutarate to form 4- amino-2-oxobutanoate, which is then converted to PLP.",No,No,No,No,No,not-Yes,GO:0050518,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.3502,0.3502,0.3502,0.3502,0.3502,5,0.3502,0.5458,yes
F6PCT_CAMJU,A0A0Q3NN41,Reference,Bacteria,237,"Cytidylyltransferase involved in the biosynthesis of capsular polysaccharides. Catalyzes the formation of cytidine diphosphate (CDP)-6-D-fructose from cytidine triphosphate (CTP) and D- fructose-6-phosphate. Shows less than 1% of activity with ATP, GTP, UTP and other sugar donors, such as D-fructose-1- phosphate, D-glucose-6-phosphate, alpha-D-glucose-1-phosphate or D- glucitol-6-phosphate.","Cytidylyltransferase involved in the biosynthesis of capsular polysaccharides. Catalyzes the formation of cytidine diphosphate (CDP)-6-D-fructose from cytidine triphosphate (CTP) and D- fructose-6-phosphate. Shows less than 1% of activity with ATP, GTP, UTP and other sugar donors, such as D-fructose-1- phosphate, D-glucose-6-phosphate, alpha-D-glucose-1-phosphate or D- glucitol-6-phosphate.",,,,,,,GO:0050518,GO:0016779,GO:0016779,GO:0016779,GO:0016779,GO:0016779,0.7539,0.7539,0.7539,0.7539,0.7539,5,0.7539,0.5458,yes
ERTE_PAES7,A0A0Q9K4R6,ESM2Text,Bacteria,419,"Amidohydrolase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the conversion of N-carbamoyl-L-glutamic acid to glutamic acid, ammonia and CO(2), the fifth (last) step of the pathway.",Involved in the anaerobic fermentation of lysine. Catalyzes the deamination of N-acetyl-L-lysine to produce the corresponding free L-lysine. The enzyme is highly specific for L-lysine and shows very low activity with free L-lysine.,No,Maybe,No,No,No,not-Yes,GO:0016813; GO:0046872,,GO:0019239,,,,,0.5032,,,,1,0.5032,0.1428,no
ERTE_PAES7,A0A0Q9K4R6,Prot2Text,Bacteria,419,"Amidohydrolase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the conversion of N-carbamoyl-L-glutamic acid to glutamic acid, ammonia and CO(2), the fifth (last) step of the pathway.",Involved in the asymmetric conversion of racemic 5-substituted hydantoins to the corresponding L-amino acids. Catalyzes the conversion of N-carbamoyl-L-methionine to L-methionine in an irreversible reaction. Unable to convert N-carbamoyl-D-methionine.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016813; GO:0046872,GO:0047409,GO:0016811,GO:0016810,GO:0016787,GO:0047408,0.0,0.5032,0.6032,0.5125,0.2954,5,0.3829,0.1428,no
ERTE_PAES7,A0A0Q9K4R6,ProtT3,Bacteria,419,"Amidohydrolase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the conversion of N-carbamoyl-L-glutamic acid to glutamic acid, ammonia and CO(2), the fifth (last) step of the pathway.",Belongs to the peptidase M20A family,Vague,No,Vague,No,Vague,not-Yes,GO:0016813; GO:0046872,GO:0008233,GO:0008237,GO:0008237,GO:0008237,GO:0008233,0.3669,0.3147,0.3147,0.3147,0.3669,5,0.3356,0.1428,no
ERTE_PAES7,A0A0Q9K4R6,ProtTale,Bacteria,419,"Amidohydrolase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the conversion of N-carbamoyl-L-glutamic acid to glutamic acid, ammonia and CO(2), the fifth (last) step of the pathway.","Involved in the catabolism of purine nucleotides. Catalyzes the hydrolysis of all three major types of purine substrates: N(1)-methylpurine, N(1)- methyluracil and N(1)-methyladenosine. It can also use N(1)-acetylpurine, N(1)-acetyluracil and N(1)-acetyladenosine as substrates, with a lower efficiency. It can also use N(1)-formylpurine, N(1)-formyluracil and N(1)-formyladenosine as substrates, with a lower efficiency.",Vague,No,No,No,No,not-Yes,GO:0016813; GO:0046872,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016787,0.5125,0.5125,0.5125,0.5125,0.5125,5,0.5125,0.1428,no
ERTE_PAES7,A0A0Q9K4R6,Protein2Text,Bacteria,419,"Amidohydrolase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the conversion of N-carbamoyl-L-glutamic acid to glutamic acid, ammonia and CO(2), the fifth (last) step of the pathway.","This protein is a part of the enzyme family that catalyzes the cleavage of a specific amino acid from a larger molecule. Specifically, this protein is involved in the degradation of a certain amino acid, likely through its involvement in the catabolic pathway of that amino acid.

More specifically, the molecular function of this protein is to catalyze the hydrolysis of a specific amino acid, probably glutamate, to produce 5-oxoproline. This is a key step in the catabolic pathway of glutamate, where 5-oxoproline is further converted to pyruvate.

In terms of molecular mechanisms, this protein is likely to use a serine hydrolase mechanism, where a serine residue acts as the nucleophile to attack the amide bond of the substrate, resulting in the formation of a carbon-nitrogen bond and the release of the product.

Overall, the molecular function of this protein is to catalyze the specific hydrolysis of a certain amino acid, likely glutamate, to produce 5-oxoproline, which is a key step in the catabolic pathway of that amino acid.",Vague,No,No,No,Vague,not-Yes,GO:0016813; GO:0046872,,,GO:0016787,,,,,0.5125,,,1,0.5125,0.1428,no
ERTE_PAES7,A0A0Q9K4R6,Reference,Bacteria,419,"Amidohydrolase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the conversion of N-carbamoyl-L-glutamic acid to glutamic acid, ammonia and CO(2), the fifth (last) step of the pathway.","Amidohydrolase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the conversion of N-carbamoyl-L-glutamic acid to glutamic acid, ammonia and CO(2), the fifth (last) step of the pathway.",,,,,,,GO:0016813; GO:0046872,GO:0016787,GO:0016810,GO:0016810,GO:0016787,GO:0016787,0.5125,0.6032,0.6032,0.5125,0.5125,5,0.5488,0.1428,no
ERTD_PAES7,A0A0Q9K529,ESM2Text,Bacteria,456,"Amidohydrolase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the hydrolysis of hydantoin-5-propionic acid to N-carbamoylglutamate, the fourth step of the pathway.",Catalyzes the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin derivatives.,Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004038,GO:0016787,GO:0016812,GO:0016787,GO:0016812,GO:0016812,0.6019,0.8582,0.6019,0.8582,0.8582,5,0.7557,0.2578,no
ERTD_PAES7,A0A0Q9K529,Prot2Text,Bacteria,456,"Amidohydrolase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the hydrolysis of hydantoin-5-propionic acid to N-carbamoylglutamate, the fourth step of the pathway.",Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004038,GO:0004038,GO:0004038,GO:0004038,GO:0004038,GO:0004038,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2578,no
ERTD_PAES7,A0A0Q9K529,ProtT3,Bacteria,456,"Amidohydrolase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the hydrolysis of hydantoin-5-propionic acid to N-carbamoylglutamate, the fourth step of the pathway.",Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. Belongs to the metallo-dependent hydrolases superfamily. Allantoinase family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004038,GO:0004038,GO:0004038,GO:0004038,GO:0004038,GO:0004038,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2578,no
ERTD_PAES7,A0A0Q9K529,ProtTale,Bacteria,456,"Amidohydrolase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the hydrolysis of hydantoin-5-propionic acid to N-carbamoylglutamate, the fourth step of the pathway.",Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004038,GO:0004038,GO:0016787,GO:0004038,GO:0004038,GO:0004038,1.0,0.6019,1.0,1.0,1.0,5,0.9204,0.2578,no
ERTD_PAES7,A0A0Q9K529,Protein2Text,Bacteria,456,"Amidohydrolase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the hydrolysis of hydantoin-5-propionic acid to N-carbamoylglutamate, the fourth step of the pathway.","This protein is involved in the molecular function of catalyzing the hydrolysis of cyclic diadenosine 5',5'''-P1,P3-triphosphate (coenzyme 60) to yield two molecules of adenosine 5'-triphosphate (ATP). It is also involved in the hydrolysis of the cyclic dinucleotide, cyclic-di-GMP. This protein is also able to hydrolyze cyclic diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) to yield ATP and AMP. It can also hydrolyze cyclic di-GMP (c-di-GMP) to yield GDP and GMP. It can also hydrolyze cyclic di-AMP (c-di-AMP) to yield AMP. It is also able to hydrolyze cyclic triphosphate (c-PPP), yielding ADP and inorganic phosphate. It can also hydrolyze cyclic tetraphosphate (c-PPPp), yielding ATP and inorganic phosphate. It can also hydrolyze cyclic tetraphosphate (c-PPPp), yielding ATP and inorganic phosphate. It can also hydrolyze cyclic tetraphosphate (c-PPPp), yielding ATP and inorganic phosphate. It can also hydrolyze cyclic tetraphosphate (c-PPPp), yielding ATP and inorganic phosphate. It can also hydrolyze cyclic tetraphosphate (c-PPPp), yielding ATP and inorganic phosphate. It can also hydrolyze cyclic tetraphosphate (c-PPPp), yielding ATP and inorganic phosphate. It can also hydrolyze cyclic tetraphosphate (c-PPPp), yielding ATP and inorganic phosphate. It can also hydrolyze cyclic tetraphosphate (c-PPPp), yielding ATP and inorganic phosphate. It can also hydrolyze cyclic tetraphosphate (c-PPPp), yielding ATP and inorganic phosphate. It can also hydrolyze cyclic tetraphosphate (c-PPPp), yielding ATP and inorganic phosphate. It can also hydrolyze cyclic tetraphosphate (c-PPPp), yielding ATP and inorganic phosphate. It can also hydrolyze cyclic tetraphosphate (c-PPPp), yielding ATP and inorganic phosphate. It can also hydrolyze cyclic tetraphosphate (c-PPPp), yielding ATP and inorganic phosphate. It can also hydrolyze cyclic tetraphosphate (c-PPPp), yielding ATP and inorganic phosphate. It can also",No,No,No,No,No,not-Yes,GO:0004038,,,,,,,,,,,0,,0.2578,no
ERTD_PAES7,A0A0Q9K529,Reference,Bacteria,456,"Amidohydrolase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the hydrolysis of hydantoin-5-propionic acid to N-carbamoylglutamate, the fourth step of the pathway.","Amidohydrolase involved in the utilization of ergothioneine, a naturally occurring histidine analog. Catalyzes the hydrolysis of hydantoin-5-propionic acid to N-carbamoylglutamate, the fourth step of the pathway.",,,,,,,GO:0004038,GO:0016787,GO:0016810,GO:0016810,GO:0016787,GO:0016787,0.6019,0.729,0.729,0.6019,0.6019,5,0.6527,0.2578,no
ODD23_SOYBN,A0A0R4J5R0,ESM2Text,Eukaryota,331,2-oxoglutarate-dependent dioxygenase catalyzing homoarginine 6-hydroxylation thus producing 6-hydroxy-L-homoarginine. Guanidine (Gd) is in turn synthesized by the spontaneous conversion of 6-hydroxy-L-homoarginine to (S)-2-amino-6- oxohexanoate (RHEA:79843); guanidine is a nitrogen-rich compound that can serve as a defense or signaling substance.,"Involved in the ethylene biosynthesis. Catalyzes the hydroxylation of theobromine to form noroxomaritidine, the first step of the pathway. Can also use ethylene and benzyl acetate as substrates, producing respectively the short-chain hydroxyalkanoic acids, butane and (2S,3S)-2-hydroxybutane, and the long-chain hydroxyalkanoic acids, butane.",Maybe,Maybe,No,No,Maybe,not-Yes,GO:0016706; GO:0046872,,,,,,,,,,,0,,0.3745,no
ODD23_SOYBN,A0A0R4J5R0,Prot2Text,Eukaryota,331,2-oxoglutarate-dependent dioxygenase catalyzing homoarginine 6-hydroxylation thus producing 6-hydroxy-L-homoarginine. Guanidine (Gd) is in turn synthesized by the spontaneous conversion of 6-hydroxy-L-homoarginine to (S)-2-amino-6- oxohexanoate (RHEA:79843); guanidine is a nitrogen-rich compound that can serve as a defense or signaling substance.,"2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0016706; GO:0046872,GO:0016706,GO:0016706,GO:0016706,GO:0016706,GO:0016706,0.698,0.698,0.698,0.698,0.698,5,0.698,0.3745,no
ODD23_SOYBN,A0A0R4J5R0,ProtT3,Eukaryota,331,2-oxoglutarate-dependent dioxygenase catalyzing homoarginine 6-hydroxylation thus producing 6-hydroxy-L-homoarginine. Guanidine (Gd) is in turn synthesized by the spontaneous conversion of 6-hydroxy-L-homoarginine to (S)-2-amino-6- oxohexanoate (RHEA:79843); guanidine is a nitrogen-rich compound that can serve as a defense or signaling substance.,Belongs to the iron/ascorbate-dependent oxidoreductase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016706; GO:0046872,,GO:0016706,GO:0016491,GO:0016491; GO:0005506,,,0.698,0.4567,0.6884,,3,0.6144,0.3745,no
ODD23_SOYBN,A0A0R4J5R0,ProtTale,Eukaryota,331,2-oxoglutarate-dependent dioxygenase catalyzing homoarginine 6-hydroxylation thus producing 6-hydroxy-L-homoarginine. Guanidine (Gd) is in turn synthesized by the spontaneous conversion of 6-hydroxy-L-homoarginine to (S)-2-amino-6- oxohexanoate (RHEA:79843); guanidine is a nitrogen-rich compound that can serve as a defense or signaling substance.,"2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0016706; GO:0046872,GO:0016706,GO:0016706,GO:0016706,GO:0016706,GO:0016706,0.698,0.698,0.698,0.698,0.698,5,0.698,0.3745,no
ODD23_SOYBN,A0A0R4J5R0,Protein2Text,Eukaryota,331,2-oxoglutarate-dependent dioxygenase catalyzing homoarginine 6-hydroxylation thus producing 6-hydroxy-L-homoarginine. Guanidine (Gd) is in turn synthesized by the spontaneous conversion of 6-hydroxy-L-homoarginine to (S)-2-amino-6- oxohexanoate (RHEA:79843); guanidine is a nitrogen-rich compound that can serve as a defense or signaling substance.,"The molecular function of this protein is involved in the oxidation of proline. It is a component of the proline degradation pathway, specifically catalyzing the conversion of trans-4-hydroxy-L-proline to L-pyrroline-5-carboxylate. This reaction is part of the process that breaks down proline, an amino acid that can be used by the cell as a source of energy.",No,No,No,No,No,not-Yes,GO:0016706; GO:0046872,GO:0004657,GO:0016491,GO:0016491,GO:0004657,GO:0016491,0.2683,0.4567,0.4567,0.2683,0.4567,5,0.3813,0.3745,no
ODD23_SOYBN,A0A0R4J5R0,Reference,Eukaryota,331,2-oxoglutarate-dependent dioxygenase catalyzing homoarginine 6-hydroxylation thus producing 6-hydroxy-L-homoarginine. Guanidine (Gd) is in turn synthesized by the spontaneous conversion of 6-hydroxy-L-homoarginine to (S)-2-amino-6- oxohexanoate (RHEA:79843); guanidine is a nitrogen-rich compound that can serve as a defense or signaling substance.,2-oxoglutarate-dependent dioxygenase catalyzing homoarginine 6-hydroxylation thus producing 6-hydroxy-L-homoarginine. Guanidine (Gd) is in turn synthesized by the spontaneous conversion of 6-hydroxy-L-homoarginine to (S)-2-amino-6- oxohexanoate (RHEA:79843); guanidine is a nitrogen-rich compound that can serve as a defense or signaling substance.,,,,,,,GO:0016706; GO:0046872,GO:0016706,GO:0016706,GO:0016706,GO:0016706,GO:0016706,0.698,0.698,0.698,0.698,0.698,5,0.698,0.3745,no
UAMDH_CAMJU,A0A0U3AB61,ESM2Text,Bacteria,407,Dehydrogenase involved in the biosynthesis of capsular polysaccharides. Catalyzes the NAD(+)-dependent oxidation of UDP-N-acetyl-D-mannosamine (UDP-ManNAc) to UDP-N-acetyl-D- mannosaminuronic acid (UDP-ManNAcA).,"Catalyzes the four-electron oxidation of UDP-N-acetyl-D-mannosamine (UDP-ManNAc), reducing NAD(+) and releasing UDP-N-acetylmannosaminuronic acid (UDP-ManNAcA).",Yes,Yes,Yes,Yes,Yes,Yes,GO:0051287; GO:0016628; GO:0089714,GO:0016616,GO:0016616,GO:0016491,GO:0016491; GO:0051287,GO:0016616,0.5661,0.5661,0.527,0.7963,0.5661,5,0.6043,0.2771,no
UAMDH_CAMJU,A0A0U3AB61,Prot2Text,Bacteria,407,Dehydrogenase involved in the biosynthesis of capsular polysaccharides. Catalyzes the NAD(+)-dependent oxidation of UDP-N-acetyl-D-mannosamine (UDP-ManNAc) to UDP-N-acetyl-D- mannosaminuronic acid (UDP-ManNAcA).,"Catalyzes the four-electron oxidation of UDP-N-acetyl-D-mannosamine (UDP-ManNAc), reducing NAD(+) and releasing UDP-N-acetylmannosaminuronic acid (UDP-ManNAcA).",Yes,Yes,Yes,Yes,Yes,Yes,GO:0051287; GO:0016628; GO:0089714,GO:0016616,GO:0050708,GO:0016616,GO:0016616,GO:0016616,0.5661,0.0,0.5661,0.5661,0.5661,5,0.4529,0.2771,no
UAMDH_CAMJU,A0A0U3AB61,ProtT3,Bacteria,407,Dehydrogenase involved in the biosynthesis of capsular polysaccharides. Catalyzes the NAD(+)-dependent oxidation of UDP-N-acetyl-D-mannosamine (UDP-ManNAc) to UDP-N-acetyl-D- mannosaminuronic acid (UDP-ManNAcA).,"Catalyzes the four-electron oxidation of UDP-N-acetyl-D- mannosamine (UDP-ManNAc), reducing NAD(+) to NADH. Belongs to the UDP-glucose/GDP-mannose dehydrogenase family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0051287; GO:0016628; GO:0089714,GO:0016616,GO:0016616,GO:0016616,GO:0016616,GO:0050699,0.5661,0.5661,0.5661,0.5661,0.1505,5,0.483,0.2771,no
UAMDH_CAMJU,A0A0U3AB61,ProtTale,Bacteria,407,Dehydrogenase involved in the biosynthesis of capsular polysaccharides. Catalyzes the NAD(+)-dependent oxidation of UDP-N-acetyl-D-mannosamine (UDP-ManNAc) to UDP-N-acetyl-D- mannosaminuronic acid (UDP-ManNAcA).,"Catalyzes the conversion of UDP-N-acetyl-D-glucosamine (UDP-GlcNAc) to UDP-N- acetylmannosamine (UDP-ManNAc), the first step in the biosynthesis of N-acetylglucosamine-6-phosphate (GlcNAc-6-P), the precursor of N-acetylglucosamine, the major constituent of the cell wall.",No,No,No,No,No,not-Yes,GO:0051287; GO:0016628; GO:0089714,GO:0008761,GO:0016853,GO:0008761,GO:0008761,GO:0008761,0.1852,0.324,0.1852,0.1852,0.1852,5,0.213,0.2771,no
UAMDH_CAMJU,A0A0U3AB61,Protein2Text,Bacteria,407,Dehydrogenase involved in the biosynthesis of capsular polysaccharides. Catalyzes the NAD(+)-dependent oxidation of UDP-N-acetyl-D-mannosamine (UDP-ManNAc) to UDP-N-acetyl-D- mannosaminuronic acid (UDP-ManNAcA).,"The molecular function of the protein is a nucleotide sugar epimerase, specifically involved in converting UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N-acetylmannosamine (UDP-ManNAc).",No,No,No,No,No,not-Yes,GO:0051287; GO:0016628; GO:0089714,GO:0016854,GO:0016854,GO:0016854,GO:0003824,,0.2607,0.2607,0.2607,0.4201,,4,0.3005,0.2771,no
UAMDH_CAMJU,A0A0U3AB61,Reference,Bacteria,407,Dehydrogenase involved in the biosynthesis of capsular polysaccharides. Catalyzes the NAD(+)-dependent oxidation of UDP-N-acetyl-D-mannosamine (UDP-ManNAc) to UDP-N-acetyl-D- mannosaminuronic acid (UDP-ManNAcA).,Dehydrogenase involved in the biosynthesis of capsular polysaccharides. Catalyzes the NAD(+)-dependent oxidation of UDP-N-acetyl-D-mannosamine (UDP-ManNAc) to UDP-N-acetyl-D- mannosaminuronic acid (UDP-ManNAcA).,,,,,,,GO:0051287; GO:0016628; GO:0089714,GO:0016491; GO:0051287,GO:0016616,GO:0016616,GO:0016491; GO:0051287,GO:0016616,0.7963,0.5661,0.5661,0.7963,0.5661,5,0.6582,0.2771,no
CDPGS_CAMJU,A0A0U3AP28,ESM2Text,Bacteria,335,NADP-dependent oxidoreductase involved in the biosynthesis of capsular polysaccharides. Catalyzes the reduction of CDP-6-D-fructose with NADPH to generate CDP-6-D-glucitol.,"Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction.",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0000166; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0050577,GO:0042350,0.7229,0.7229,0.7229,0.4359,0.0,5,0.5209,0.1417,no
CDPGS_CAMJU,A0A0U3AP28,Prot2Text,Bacteria,335,NADP-dependent oxidoreductase involved in the biosynthesis of capsular polysaccharides. Catalyzes the reduction of CDP-6-D-fructose with NADPH to generate CDP-6-D-glucitol.,"Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction. GDP-4-dehydro-6-deoxy-D-mannose is converted to GDP-4-dehydro-6-deoxy-D-talose, involving an epimerase and a reductase reaction.",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0000166; GO:0016491,GO:0050577,GO:0050577,GO:0050577,GO:0016491,GO:0050577,0.4359,0.4359,0.4359,0.7229,0.4359,5,0.4933,0.1417,no
CDPGS_CAMJU,A0A0U3AP28,ProtT3,Bacteria,335,NADP-dependent oxidoreductase involved in the biosynthesis of capsular polysaccharides. Catalyzes the reduction of CDP-6-D-fructose with NADPH to generate CDP-6-D-glucitol.,Catalyzes the conversion of dTDP-4-dehydro-6-deoxy-D-xylo-4-hexulose to dTDP-4-keto-6-deoxy-D-xylo-4-hexulose. Belongs to the NAD(P)-dependent epimerase/dehydratase family. dTDP-6-deoxy-D-xylo-4-hexulose dehydrogenase subfamily,Maybe,No,No,No,Maybe,not-Yes,GO:0000166; GO:0016491,GO:0016616,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4994,0.7229,0.7229,0.7229,0.7229,5,0.6782,0.1417,no
CDPGS_CAMJU,A0A0U3AP28,ProtTale,Bacteria,335,NADP-dependent oxidoreductase involved in the biosynthesis of capsular polysaccharides. Catalyzes the reduction of CDP-6-D-fructose with NADPH to generate CDP-6-D-glucitol.,Catalyzes the irreversible conversion of 3'-deoxy-D-manno-2'- octulosonate (KDO) to phospho-N-acetylglucosamine (PGlcNAc) within the biosynthetic pathway of 2-keto-3-deoxy-D-gluconate (KDG). Catalyzes the reversible conversion of KDO and CTP into CDP-2-keto-3-deoxy-6-phospho-D-gluconate (CDP-KDO).,No,No,No,No,No,not-Yes,GO:0000166; GO:0016491,GO:0008690,GO:0016779,GO:0016779,GO:0016779,GO:0008690,0.2427,0.311,0.311,0.311,0.2427,5,0.2837,0.1417,no
CDPGS_CAMJU,A0A0U3AP28,Protein2Text,Bacteria,335,NADP-dependent oxidoreductase involved in the biosynthesis of capsular polysaccharides. Catalyzes the reduction of CDP-6-D-fructose with NADPH to generate CDP-6-D-glucitol.,"The molecular function of this protein is a lyase enzyme, specifically a glycoside lyase, involved in the breakdown of glycosidic bonds.",No,No,No,No,No,not-Yes,GO:0000166; GO:0016491,GO:0016837,GO:0016829,GO:0016829,GO:0016829,GO:0016837,0.311,0.4496,0.4496,0.4496,0.311,5,0.3942,0.1417,no
CDPGS_CAMJU,A0A0U3AP28,Reference,Bacteria,335,NADP-dependent oxidoreductase involved in the biosynthesis of capsular polysaccharides. Catalyzes the reduction of CDP-6-D-fructose with NADPH to generate CDP-6-D-glucitol.,NADP-dependent oxidoreductase involved in the biosynthesis of capsular polysaccharides. Catalyzes the reduction of CDP-6-D-fructose with NADPH to generate CDP-6-D-glucitol.,,,,,,,GO:0000166; GO:0016491,GO:0016491; GO:0050661,GO:0016491; GO:0050661,GO:0016491,GO:0016491; GO:0050661,GO:0016491,0.8656,0.8656,0.7229,0.8656,0.7229,5,0.8085,0.1417,no
IADAE_TRASO,A0A124EH39,ESM2Text,Bacteria,315,"Catalyzes activation of the indoleacetate decarboxylase OsIAD under anaerobic conditions by generation of an organic free radical on a glycine residue, via a homolytic cleavage of S-adenosyl-L-methionine (SAM).","Catalyzes activation of the anaerobic sulfite reductase CutC under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine (adenosine 5'-epsilon-cap), [4Fe-4S] cluster and 7 kDa (a secondary metabolite).",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0051539; GO:0046872; GO:0016491,,,GO:0003824,,GO:0051539,,,0.4848,,0.6241,2,0.5544,0.475,no
IADAE_TRASO,A0A124EH39,Prot2Text,Bacteria,315,"Catalyzes activation of the indoleacetate decarboxylase OsIAD under anaerobic conditions by generation of an organic free radical on a glycine residue, via a homolytic cleavage of S-adenosyl-L-methionine (SAM).","Activation of benzylsuccinate synthase under anaerobic conditions by generation of an organic free radical on a glycine residue, via a homolytic cleavage of S-adenosyl-L-methionine (SAM).",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0051539; GO:0046872; GO:0016491,,,,,GO:0016491,,,,,0.5789,1,0.5789,0.475,no
IADAE_TRASO,A0A124EH39,ProtT3,Bacteria,315,"Catalyzes activation of the indoleacetate decarboxylase OsIAD under anaerobic conditions by generation of an organic free radical on a glycine residue, via a homolytic cleavage of S-adenosyl-L-methionine (SAM).","Catalyzes activation of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) as 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC). Belongs to the organic radical-activating enzymes family",Maybe,No,No,No,Maybe,not-Yes,GO:0051539; GO:0046872; GO:0016491,GO:0016829,GO:0003824,GO:0016829,GO:0003824,GO:0016829,0.374,0.4848,0.374,0.4848,0.374,5,0.4183,0.475,no
IADAE_TRASO,A0A124EH39,ProtTale,Bacteria,315,"Catalyzes activation of the indoleacetate decarboxylase OsIAD under anaerobic conditions by generation of an organic free radical on a glycine residue, via a homolytic cleavage of S-adenosyl-L-methionine (SAM).","Catalyzes activation of 4-hydroxyphenylacetate decarboxylase under anaerobic conditions by generation of an organic free radical on a glycine residue, via a homolytic cleavage of S-adenosyl-L-methionine (SAM).",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0051539; GO:0046872; GO:0016491,GO:0016491,GO:0016829,GO:0051539,GO:0016829,,0.5789,0.374,0.6241,0.374,,4,0.4878,0.475,no
IADAE_TRASO,A0A124EH39,Protein2Text,Bacteria,315,"Catalyzes activation of the indoleacetate decarboxylase OsIAD under anaerobic conditions by generation of an organic free radical on a glycine residue, via a homolytic cleavage of S-adenosyl-L-methionine (SAM).",This protein is involved in the molecular function of methyltransferase activity.,No,No,No,No,No,not-Yes,GO:0051539; GO:0046872; GO:0016491,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.2558,0.2558,0.2558,0.2558,0.2558,5,0.2558,0.475,no
IADAE_TRASO,A0A124EH39,Reference,Bacteria,315,"Catalyzes activation of the indoleacetate decarboxylase OsIAD under anaerobic conditions by generation of an organic free radical on a glycine residue, via a homolytic cleavage of S-adenosyl-L-methionine (SAM).","Catalyzes activation of the indoleacetate decarboxylase OsIAD under anaerobic conditions by generation of an organic free radical on a glycine residue, via a homolytic cleavage of S-adenosyl-L-methionine (SAM).",,,,,,,GO:0051539; GO:0046872; GO:0016491,GO:0016829,,,GO:0051539,,0.374,,,0.6241,,2,0.499,0.475,no
CEG_TOXGM,A0A125YYB5,ESM2Text,Eukaryota,509,Capping enzyme with guanylyltransferase activity; transfers GMP to RNA via a covalent enzyme-GMP intermediate.,Probable component of an E3 ubiquitin ligase complex RTT101(MMS1-ESC2). Involved in oxidative stress resistance.,No,No,No,No,No,not-Yes,GO:0005524; GO:0005525; GO:0004484,GO:0004842,GO:0061630,,GO:0061630,GO:0061630,0.1423,0.1182,,0.1182,0.1182,4,0.1242,0.5879,yes
CEG_TOXGM,A0A125YYB5,Prot2Text,Eukaryota,509,Capping enzyme with guanylyltransferase activity; transfers GMP to RNA via a covalent enzyme-GMP intermediate.,"Decapping effector that binds to the 5'-end of tRNAs and inhibits the 5'-processing of primary mRNAs. In contrast to other decapping proteins (such as gcn5.1/GRF1), this protein is not required for decapping of mRNA from viruses and cellular genes.",No,No,No,No,No,not-Yes,GO:0005524; GO:0005525; GO:0004484,,,,GO:0003723,GO:0003723,,,,0.1486,0.1486,2,0.1486,0.5879,yes
CEG_TOXGM,A0A125YYB5,ProtT3,Eukaryota,509,Capping enzyme with guanylyltransferase activity; transfers GMP to RNA via a covalent enzyme-GMP intermediate.,Probable 3'-phospho-D-glycerate synthase. Nucleus. Belongs to the glycosyltransferase 20 family,No,No,No,No,No,not-Yes,GO:0005524; GO:0005525; GO:0004484,GO:0003825,GO:0003825,GO:0003825,GO:0003825,GO:0003825,0.1195,0.1195,0.1195,0.1195,0.1195,5,0.1195,0.5879,yes
CEG_TOXGM,A0A125YYB5,ProtTale,Eukaryota,509,Capping enzyme with guanylyltransferase activity; transfers GMP to RNA via a covalent enzyme-GMP intermediate.,Second step of mRNA capping. Transfer of the GMP moiety of GTP to the 5'-end of RNA via an enzyme-GMP covalent reaction intermediate.,No,No,No,No,No,not-Yes,GO:0005524; GO:0005525; GO:0004484,GO:0004484,GO:0004484,GO:0004484,GO:0004484,GO:0004484,0.5243,0.5243,0.5243,0.5243,0.5243,5,0.5243,0.5879,yes
CEG_TOXGM,A0A125YYB5,Protein2Text,Eukaryota,509,Capping enzyme with guanylyltransferase activity; transfers GMP to RNA via a covalent enzyme-GMP intermediate.,The molecular function of this protein is as a polymerase.,No,No,No,No,No,not-Yes,GO:0005524; GO:0005525; GO:0004484,,,,,,,,,,,0,,0.5879,yes
CEG_TOXGM,A0A125YYB5,Reference,Eukaryota,509,Capping enzyme with guanylyltransferase activity; transfers GMP to RNA via a covalent enzyme-GMP intermediate.,Capping enzyme with guanylyltransferase activity; transfers GMP to RNA via a covalent enzyme-GMP intermediate.,,,,,,,GO:0005524; GO:0005525; GO:0004484,GO:0004484,GO:0004484,GO:0004484,GO:0004484,GO:0004484,0.5243,0.5243,0.5243,0.5243,0.5243,5,0.5243,0.5879,yes
SDG1_CYTMA,A0A194VQN7,ESM2Text,Eukaryota,1071,"Non-canonical non-ribosomal peptide synthetase; part of the SMGC4 gene cluster that mediates the biosynthesis of SDP1, a cyclo- dipeptide that induces cell death in apple stem tissue cultures, and suppresses the production of lignin, while it has no effect on apple leaves. SPD1 treatment inhibits apple chloroplast activity and auxin responses. SGD1 contributes to the development of pycnidia.","Butyrate-dependent aromatic aminotransferase; part of the gene cluster that mediates the biosynthesis of butenolide, a mycotoxin that shows antibiotic activity but does not seem to play a major role in the spread of head blight in wheat. Butenolide is derived from glutamic acid via a 4-acetamido-2-butenoic acid intermediate (Probable). The predicted function of the NADH:flavin oxidoreductase FG08077, the cytochrome P450 monooxygenase FG08079, the decarboxylase FG08083, and the putative acetyltransferase FG08082 are consistent with this pathway, however, the respective activities of the butelonide biosynthesis cluster enzymes have still to be experimentally determined (Probable).",No,No,Maybe,No,No,not-Yes,GO:0031177,GO:0008483,GO:0008483,,GO:0008483; GO:0030170,GO:0008483; GO:0030170,0.0922,0.0922,,0.4265,0.4265,4,0.2593,0.3734,no
SDG1_CYTMA,A0A194VQN7,Prot2Text,Eukaryota,1071,"Non-canonical non-ribosomal peptide synthetase; part of the SMGC4 gene cluster that mediates the biosynthesis of SDP1, a cyclo- dipeptide that induces cell death in apple stem tissue cultures, and suppresses the production of lignin, while it has no effect on apple leaves. SPD1 treatment inhibits apple chloroplast activity and auxin responses. SGD1 contributes to the development of pycnidia.","Non-canonical nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the host-selective toxins (HSTs) AAL-toxins, sphinganine-analog mycotoxins responsible for Alternaria stem canker on tomato by the tomato pathotype. The biosynthesis starts with the polyketide synthase ALT1-catalyzed C-16 carbon chain assembly from one starter acetyl-CoA unit with malonyl-CoA extender units. ALT1 also selectively transfers methyl groups at the first and the third cycle of chain elongation for AAL toxin. The C-16 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of glycin by decarboxylation, on the carbonyl carbon of polyketide acyl chain (Probable). This step is probably catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase ALT4 (Probable). The respective functions of the other enzymes encoded by the cluster have still to be elucidated (Probable). The sphingosine N",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0031177,,,GO:0016874,,GO:0016874,,,0.127,,0.127,2,0.127,0.3734,no
SDG1_CYTMA,A0A194VQN7,ProtT3,Eukaryota,1071,"Non-canonical non-ribosomal peptide synthetase; part of the SMGC4 gene cluster that mediates the biosynthesis of SDP1, a cyclo- dipeptide that induces cell death in apple stem tissue cultures, and suppresses the production of lignin, while it has no effect on apple leaves. SPD1 treatment inhibits apple chloroplast activity and auxin responses. SGD1 contributes to the development of pycnidia.",Acyl-CoA thioesterase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-,No,No,No,No,No,not-Yes,GO:0031177,GO:0016790,GO:0016790,GO:0016790,GO:0016790,GO:0016790,0.0922,0.0922,0.0922,0.0922,0.0922,5,0.0922,0.3734,no
SDG1_CYTMA,A0A194VQN7,ProtTale,Eukaryota,1071,"Non-canonical non-ribosomal peptide synthetase; part of the SMGC4 gene cluster that mediates the biosynthesis of SDP1, a cyclo- dipeptide that induces cell death in apple stem tissue cultures, and suppresses the production of lignin, while it has no effect on apple leaves. SPD1 treatment inhibits apple chloroplast activity and auxin responses. SGD1 contributes to the development of pycnidia.","Adenylate-forming reductase, a natural product biosynthesis enzyme that resembles non-ribosomal peptide synthetases, but the product is not bound to the enzyme active site.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0031177,GO:0016874,GO:0016874,GO:0016874,GO:0016874,,0.127,0.127,0.127,0.127,,4,0.127,0.3734,no
SDG1_CYTMA,A0A194VQN7,Protein2Text,Eukaryota,1071,"Non-canonical non-ribosomal peptide synthetase; part of the SMGC4 gene cluster that mediates the biosynthesis of SDP1, a cyclo- dipeptide that induces cell death in apple stem tissue cultures, and suppresses the production of lignin, while it has no effect on apple leaves. SPD1 treatment inhibits apple chloroplast activity and auxin responses. SGD1 contributes to the development of pycnidia.","This protein is a part of the polyketide synthase (PKS) enzyme system, which is involved in the biosynthesis of polyketides, a class of secondary metabolites. Specifically, it is a type I PKS that catalyzes the synthesis of a polyketide chain. The molecular function of this protein is to synthesize a polyketide chain by condensing acetate units, which are activated by the acyl carrier protein (ACP) domain of the PKS. The polyketide chain is then modified by the PKS to produce a specific polyketide metabolite.

In more detail, the molecular function of this protein can be summarized as follows:

* Acyl carrier protein (ACP) domain: catalyzes the activation of acetate units by forming an acyl-ACP thioester
* Ketosynthese (KS) domain: catalyzes the condensation of acetate units to form a polyketide chain
* ACP and KS domains work together to catalyze the polyketide chain elongation
* The polyketide chain is modified by the PKS to produce a specific polyketide metabolite

It's worth noting that the specific polyketide metabolite produced by this protein is not specified in the given text. However, based on the molecular function of the protein, it is likely to be involved in the biosynthesis of a polyketide secondary metabolite.",No,No,No,Maybe,No,not-Yes,GO:0031177,,,,,,,,,,,0,,0.3734,no
SDG1_CYTMA,A0A194VQN7,Reference,Eukaryota,1071,"Non-canonical non-ribosomal peptide synthetase; part of the SMGC4 gene cluster that mediates the biosynthesis of SDP1, a cyclo- dipeptide that induces cell death in apple stem tissue cultures, and suppresses the production of lignin, while it has no effect on apple leaves. SPD1 treatment inhibits apple chloroplast activity and auxin responses. SGD1 contributes to the development of pycnidia.","Non-canonical non-ribosomal peptide synthetase; part of the SMGC4 gene cluster that mediates the biosynthesis of SDP1, a cyclo- dipeptide that induces cell death in apple stem tissue cultures, and suppresses the production of lignin, while it has no effect on apple leaves. SPD1 treatment inhibits apple chloroplast activity and auxin responses. SGD1 contributes to the development of pycnidia.",,,,,,,GO:0031177,GO:0031177; GO:0016874,GO:0008927,,GO:0016874,,0.709,0.0814,,0.127,,3,0.3058,0.3734,no
NRP14_CYTMA,A0A194VTS2,ESM2Text,Eukaryota,573,Acyl-CoA ligase; part of the biosynthetic gene cluster 14 that mediates the production of a yet unidentified mycotoxin that contributes to virulence.,"Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of pyripyropene A, a specific human acyl-CoA inhibitor. The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid adenylate adenylate (NaADP) synthase pyrA. Nicotinyl-CoA is then a substrate of polyketide synthase pyrB to produce 4-hydroxybenzodiazepin (HBnB), which is further prenylated by the polyprenyl transferase pyrC to yield farnesyl-HFB. Further epoxidation by the FAD-dependent monooxygenase pyrE leads to epoxyfarnesyl-HFB. The next step involves the terpene cyclase pyrB, followed by the T-prenyltransferase pyrD to yield prenylpyripyropene E. The FAD-dependent monooxygenase pyrF is then responsible for the stereospecific hydroxylation at C-4 to yield deacetylpyripyropene E. The F",Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0031956,GO:0016405,GO:0003996,GO:0003824,GO:0016874,GO:0016874,0.6204,0.8265,0.3355,0.4373,0.4373,5,0.5314,0.27,no
NRP14_CYTMA,A0A194VTS2,Prot2Text,Eukaryota,573,Acyl-CoA ligase; part of the biosynthetic gene cluster 14 that mediates the production of a yet unidentified mycotoxin that contributes to virulence.,"Carboxylate--CoA ligase that may use 4-coumarate as substrate. Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield the final CoA thioester.",Yes,Maybe,Maybe,No,Maybe,not-Yes,GO:0031956,GO:0016207,GO:0016207,GO:0016207,GO:0016207,GO:0016207,0.6145,0.6145,0.6145,0.6145,0.6145,5,0.6145,0.27,no
NRP14_CYTMA,A0A194VTS2,ProtT3,Eukaryota,573,Acyl-CoA ligase; part of the biosynthetic gene cluster 14 that mediates the production of a yet unidentified mycotoxin that contributes to virulence.,"Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Yes,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0031956,GO:0016405,GO:0016874,GO:0016874,GO:0016405,GO:0016874; GO:0005524,0.6204,0.4373,0.4373,0.6204,0.3093,5,0.4849,0.27,no
NRP14_CYTMA,A0A194VTS2,ProtTale,Eukaryota,573,Acyl-CoA ligase; part of the biosynthetic gene cluster 14 that mediates the production of a yet unidentified mycotoxin that contributes to virulence.,"Catalyzes the activation of fatty acids by CoA to form acyl-CoA, the first step in fatty acid degradation or biosynthesis.",No,No,No,No,No,not-Yes,GO:0031956,GO:0004467,GO:0003987; GO:0016874,GO:0016874,GO:0004467,GO:0004467,0.8265,0.5554,0.4373,0.8265,0.8265,5,0.6944,0.27,no
NRP14_CYTMA,A0A194VTS2,Protein2Text,Eukaryota,573,Acyl-CoA ligase; part of the biosynthetic gene cluster 14 that mediates the production of a yet unidentified mycotoxin that contributes to virulence.,"The molecular function of this protein is not explicitly stated in the provided information. However, based on its name and classification as a protein, it is likely to be involved in a metabolic or biochemical process, possibly related to the breakdown or synthesis of a specific molecule. 

Given its name, it is possible that this protein is involved in the transfer of a carboxyl group, which is a common function of enzymes known as carboxyltransferases. 

More information would be needed to determine the specific molecular function of this protein.",Vague,Vague,Vague,No,Vague,not-Yes,GO:0031956,,,,,,,,,,,0,,0.27,no
NRP14_CYTMA,A0A194VTS2,Reference,Eukaryota,573,Acyl-CoA ligase; part of the biosynthetic gene cluster 14 that mediates the production of a yet unidentified mycotoxin that contributes to virulence.,Acyl-CoA ligase; part of the biosynthetic gene cluster 14 that mediates the production of a yet unidentified mycotoxin that contributes to virulence.,,,,,,,GO:0031956,GO:0016874; GO:0003824,GO:0016877,GO:0016877,GO:0016405,GO:0016405,0.4033,0.5291,0.5291,0.6204,0.6204,5,0.5405,0.27,no
LAEA_CYTMA,A0A194W185,ESM2Text,Eukaryota,311,Component of the velvet transcription factor complex that acts as a global regulator for secondary metabolite gene expression. Is a crucial virulence factor of Cytospora mali via its control of secondary metabolite gene expression.,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ. Paxilline is converted to beta-paxitri",No,No,No,No,No,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008171,GO:0008168,GO:0008168,1.0,1.0,0.8582,1.0,1.0,5,0.9716,0.3149,no
LAEA_CYTMA,A0A194W185,Prot2Text,Eukaryota,311,Component of the velvet transcription factor complex that acts as a global regulator for secondary metabolite gene expression. Is a crucial virulence factor of Cytospora mali via its control of secondary metabolite gene expression.,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate tolerance, py",No,No,No,No,No,not-Yes,GO:0008168,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.3149,no
LAEA_CYTMA,A0A194W185,ProtT3,Eukaryota,311,Component of the velvet transcription factor complex that acts as a global regulator for secondary metabolite gene expression. Is a crucial virulence factor of Cytospora mali via its control of secondary metabolite gene expression.,"Methyltransferase that acts as a component of the velvet transcription factor complex that controls sexual/asexual developmental ratio in response to light, promoting sexual development in the darkness while stimulating asexual sporulation under illumination (By similarity). The velvet complex acts as a global regulator for secondary metabolite gene expression (By similarity). Nucleus. Belongs to the methyltransferase superfamily. VEL1 family",Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3149,no
LAEA_CYTMA,A0A194W185,ProtTale,Eukaryota,311,Component of the velvet transcription factor complex that acts as a global regulator for secondary metabolite gene expression. Is a crucial virulence factor of Cytospora mali via its control of secondary metabolite gene expression.,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the saturated C-C bonds of",No,Maybe,Maybe,Maybe,No,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3149,no
LAEA_CYTMA,A0A194W185,Protein2Text,Eukaryota,311,Component of the velvet transcription factor complex that acts as a global regulator for secondary metabolite gene expression. Is a crucial virulence factor of Cytospora mali via its control of secondary metabolite gene expression.,"This protein is a methyltransferase, which means it catalyzes the transfer of a methyl group from a donor molecule to a substrate molecule. In the case of this protein, it is likely involved in the methylation of a specific substrate, such as a protein or a nucleic acid, which plays a role in its function. However, more specific information about the molecular function of this protein is not available. 
If you have more specific information about this protein, I may be able to provide more detailed information about its molecular function.",No,No,No,No,No,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3149,no
LAEA_CYTMA,A0A194W185,Reference,Eukaryota,311,Component of the velvet transcription factor complex that acts as a global regulator for secondary metabolite gene expression. Is a crucial virulence factor of Cytospora mali via its control of secondary metabolite gene expression.,Component of the velvet transcription factor complex that acts as a global regulator for secondary metabolite gene expression. Is a crucial virulence factor of Cytospora mali via its control of secondary metabolite gene expression.,,,,,,,GO:0008168,,,,,,,,,,,0,,0.3149,no
PKS39_CYTMA,A0A194WAB9,ESM2Text,Eukaryota,2584,Highly reducing polyketide synthase; part of the biosynthetic gene cluster 39 that is not involved in virulence.,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential tr",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0016491; GO:0031177,,GO:0016747,GO:0016491; GO:0016740,GO:0016746,GO:0016746,,0.5539,0.6662,0.5114,0.5114,4,0.5607,0.2494,no
PKS39_CYTMA,A0A194WAB9,Prot2Text,Eukaryota,2584,Highly reducing polyketide synthase; part of the biosynthetic gene cluster 39 that is not involved in virulence.,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential tr",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0016491; GO:0031177,,,GO:0016747,,GO:0016746,,,0.5539,,0.5114,2,0.5326,0.2494,no
PKS39_CYTMA,A0A194WAB9,ProtT3,Eukaryota,2584,Highly reducing polyketide synthase; part of the biosynthetic gene cluster 39 that is not involved in virulence.,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0016491; GO:0031177,GO:0016747,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.5539,0.5114,0.5114,0.5114,0.5114,5,0.5199,0.2494,no
PKS39_CYTMA,A0A194WAB9,ProtTale,Eukaryota,2584,Highly reducing polyketide synthase; part of the biosynthetic gene cluster 39 that is not involved in virulence.,"Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. Within the pathway, ptmJ catalyzes the last step by converting the 13,14-epoxide of penitrem C to yield penitrem A. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3-glycerol phosphate with",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0016491; GO:0031177,GO:0016747,GO:0016747,GO:0016746,GO:0016746,,0.5539,0.5539,0.5114,0.5114,,4,0.5326,0.2494,no
PKS39_CYTMA,A0A194WAB9,Protein2Text,Eukaryota,2584,Highly reducing polyketide synthase; part of the biosynthetic gene cluster 39 that is not involved in virulence.,"The molecular function of this protein is not explicitly stated in the provided snippet. However, based on its name, it can be inferred that it is involved in the synthesis of a compound, likely a steroid, given its classification as a cytochrome P450 monooxygenase. Cytochrome P450 monooxygenses are a family of enzymes that catalyze the insertion of an oxygen atom into a substrate, often resulting in the formation of a hydroxyl group. This type of reaction is commonly involved in the biosynthesis of steroids, terpenes, and other complex organic molecules.",Vague,No,Vague,Vague,Vague,not-Yes,GO:0004312; GO:0016491; GO:0031177,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.5051,0.5051,0.5051,0.5051,0.5051,5,0.5051,0.2494,no
PKS39_CYTMA,A0A194WAB9,Reference,Eukaryota,2584,Highly reducing polyketide synthase; part of the biosynthetic gene cluster 39 that is not involved in virulence.,Highly reducing polyketide synthase; part of the biosynthetic gene cluster 39 that is not involved in virulence.,,,,,,,GO:0004312; GO:0016491; GO:0031177,GO:0031177; GO:0016747,GO:0004315,,GO:0016746,,0.8247,0.4736,,0.5114,,3,0.6032,0.2494,no
PFA2_THRS2,A0A1B3PEI8,ESM2Text,Eukaryota,2049,"Poliketide synthase-like protein; part of the polyunsaturated fatty acid synthase composed of the 3 PKS-like subunits A, B and C. While the saturated fatty acids (SFAs) in Thraustochytrium are produced by the conventional fatty acid synthase (FAS) pathway, polyunsaturated fatty acids (PUFAs) including docosahexeanoic acid (DHA) and docosapentaenoic acid (DPA) are synthesized via an anaerobical PKS pathway. PUFA synthase assimilates fatty acyl-CoA, the product of FAS, as the starter unit to synthesize DPA, and this starter unit may be butyryl-CoA, hexanoyl-CoA, or octanoyl-CoA. DPA and DHA biosynthesis seem to differ by the reduction at the N-3 position by PUFA synthase, not the extension of carbon chain. In DHA biosynthesis, PUFA synthase extends the fatty acyl chain from the methyl toward the carboxyl end, and the double bond is formed when the carbon chain is growing, instead of afterward. Therefore, PUFA synthase is unable to transform DPA to DHA, suggesting that DPA is not the precursor of DHA. Moreover, DPA molecule is partly extended by FAS KS domain, so DPA biosynthesis is less dependent on PUFA synthase KS domain than DHA.","Long chain fatty acid synthase/oxygenase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and l",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0016746; GO:0016491,GO:0004312,GO:0004312,GO:0016491; GO:0016740,GO:0004312,GO:0004312; GO:0016491,0.6044,0.6044,0.9073,0.6044,0.8645,5,0.717,0.2594,no
PFA2_THRS2,A0A1B3PEI8,Prot2Text,Eukaryota,2049,"Poliketide synthase-like protein; part of the polyunsaturated fatty acid synthase composed of the 3 PKS-like subunits A, B and C. While the saturated fatty acids (SFAs) in Thraustochytrium are produced by the conventional fatty acid synthase (FAS) pathway, polyunsaturated fatty acids (PUFAs) including docosahexeanoic acid (DHA) and docosapentaenoic acid (DPA) are synthesized via an anaerobical PKS pathway. PUFA synthase assimilates fatty acyl-CoA, the product of FAS, as the starter unit to synthesize DPA, and this starter unit may be butyryl-CoA, hexanoyl-CoA, or octanoyl-CoA. DPA and DHA biosynthesis seem to differ by the reduction at the N-3 position by PUFA synthase, not the extension of carbon chain. In DHA biosynthesis, PUFA synthase extends the fatty acyl chain from the methyl toward the carboxyl end, and the double bond is formed when the carbon chain is growing, instead of afterward. Therefore, PUFA synthase is unable to transform DPA to DHA, suggesting that DPA is not the precursor of DHA. Moreover, DPA molecule is partly extended by FAS KS domain, so DPA biosynthesis is less dependent on PUFA synthase KS domain than DHA.","Responsible for the synthesis of the acyl-CoA thioester of medicago-specific fatty acid esters, which are required for the degradative activity of the microsporidian microsporidian polyketide synthase (PKS).",Maybe,No,No,No,Maybe,not-Yes,GO:0016746; GO:0016491,,,,,,,,,,,0,,0.2594,no
PFA2_THRS2,A0A1B3PEI8,ProtT3,Eukaryota,2049,"Poliketide synthase-like protein; part of the polyunsaturated fatty acid synthase composed of the 3 PKS-like subunits A, B and C. While the saturated fatty acids (SFAs) in Thraustochytrium are produced by the conventional fatty acid synthase (FAS) pathway, polyunsaturated fatty acids (PUFAs) including docosahexeanoic acid (DHA) and docosapentaenoic acid (DPA) are synthesized via an anaerobical PKS pathway. PUFA synthase assimilates fatty acyl-CoA, the product of FAS, as the starter unit to synthesize DPA, and this starter unit may be butyryl-CoA, hexanoyl-CoA, or octanoyl-CoA. DPA and DHA biosynthesis seem to differ by the reduction at the N-3 position by PUFA synthase, not the extension of carbon chain. In DHA biosynthesis, PUFA synthase extends the fatty acyl chain from the methyl toward the carboxyl end, and the double bond is formed when the carbon chain is growing, instead of afterward. Therefore, PUFA synthase is unable to transform DPA to DHA, suggesting that DPA is not the precursor of DHA. Moreover, DPA molecule is partly extended by FAS KS domain, so DPA biosynthesis is less dependent on PUFA synthase KS domain than DHA.","Part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins that are toxic for animals and humans",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0016746; GO:0016491,,,,,,,,,,,0,,0.2594,no
PFA2_THRS2,A0A1B3PEI8,ProtTale,Eukaryota,2049,"Poliketide synthase-like protein; part of the polyunsaturated fatty acid synthase composed of the 3 PKS-like subunits A, B and C. While the saturated fatty acids (SFAs) in Thraustochytrium are produced by the conventional fatty acid synthase (FAS) pathway, polyunsaturated fatty acids (PUFAs) including docosahexeanoic acid (DHA) and docosapentaenoic acid (DPA) are synthesized via an anaerobical PKS pathway. PUFA synthase assimilates fatty acyl-CoA, the product of FAS, as the starter unit to synthesize DPA, and this starter unit may be butyryl-CoA, hexanoyl-CoA, or octanoyl-CoA. DPA and DHA biosynthesis seem to differ by the reduction at the N-3 position by PUFA synthase, not the extension of carbon chain. In DHA biosynthesis, PUFA synthase extends the fatty acyl chain from the methyl toward the carboxyl end, and the double bond is formed when the carbon chain is growing, instead of afterward. Therefore, PUFA synthase is unable to transform DPA to DHA, suggesting that DPA is not the precursor of DHA. Moreover, DPA molecule is partly extended by FAS KS domain, so DPA biosynthesis is less dependent on PUFA synthase KS domain than DHA.","Fatty acid synthase alpha subunit; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS). SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms. These initial steps feature the priming of an unusual benzoic acid starter unit",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0016746; GO:0016491,GO:0004312,GO:0016747,GO:0004312,GO:0016746,GO:0004312,0.6044,0.6968,0.6044,0.8269,0.6044,5,0.6674,0.2594,no
PFA2_THRS2,A0A1B3PEI8,Protein2Text,Eukaryota,2049,"Poliketide synthase-like protein; part of the polyunsaturated fatty acid synthase composed of the 3 PKS-like subunits A, B and C. While the saturated fatty acids (SFAs) in Thraustochytrium are produced by the conventional fatty acid synthase (FAS) pathway, polyunsaturated fatty acids (PUFAs) including docosahexeanoic acid (DHA) and docosapentaenoic acid (DPA) are synthesized via an anaerobical PKS pathway. PUFA synthase assimilates fatty acyl-CoA, the product of FAS, as the starter unit to synthesize DPA, and this starter unit may be butyryl-CoA, hexanoyl-CoA, or octanoyl-CoA. DPA and DHA biosynthesis seem to differ by the reduction at the N-3 position by PUFA synthase, not the extension of carbon chain. In DHA biosynthesis, PUFA synthase extends the fatty acyl chain from the methyl toward the carboxyl end, and the double bond is formed when the carbon chain is growing, instead of afterward. Therefore, PUFA synthase is unable to transform DPA to DHA, suggesting that DPA is not the precursor of DHA. Moreover, DPA molecule is partly extended by FAS KS domain, so DPA biosynthesis is less dependent on PUFA synthase KS domain than DHA.","This protein is involved in the biosynthesis of a polyketide, which is a class of compounds that includes antibiotics, antitumor agents, and other medically important compounds. It is a type of enzyme that catalyzes the polymerization of acetate units to form a polyketide chain, which can then be modified by other enzymes to produce a variety of different compounds. In this case, the protein is responsible for the biosynthesis of a specific type of polyketide, which is likely to be an antibiotic or other medically important compound.",Maybe,No,Maybe,Maybe,Vague,not-Yes,GO:0016746; GO:0016491,,,,,,,,,,,0,,0.2594,no
PFA2_THRS2,A0A1B3PEI8,Reference,Eukaryota,2049,"Poliketide synthase-like protein; part of the polyunsaturated fatty acid synthase composed of the 3 PKS-like subunits A, B and C. While the saturated fatty acids (SFAs) in Thraustochytrium are produced by the conventional fatty acid synthase (FAS) pathway, polyunsaturated fatty acids (PUFAs) including docosahexeanoic acid (DHA) and docosapentaenoic acid (DPA) are synthesized via an anaerobical PKS pathway. PUFA synthase assimilates fatty acyl-CoA, the product of FAS, as the starter unit to synthesize DPA, and this starter unit may be butyryl-CoA, hexanoyl-CoA, or octanoyl-CoA. DPA and DHA biosynthesis seem to differ by the reduction at the N-3 position by PUFA synthase, not the extension of carbon chain. In DHA biosynthesis, PUFA synthase extends the fatty acyl chain from the methyl toward the carboxyl end, and the double bond is formed when the carbon chain is growing, instead of afterward. Therefore, PUFA synthase is unable to transform DPA to DHA, suggesting that DPA is not the precursor of DHA. Moreover, DPA molecule is partly extended by FAS KS domain, so DPA biosynthesis is less dependent on PUFA synthase KS domain than DHA.","Poliketide synthase-like protein; part of the polyunsaturated fatty acid synthase composed of the 3 PKS-like subunits A, B and C. While the saturated fatty acids (SFAs) in Thraustochytrium are produced by the conventional fatty acid synthase (FAS) pathway, polyunsaturated fatty acids (PUFAs) including docosahexeanoic acid (DHA) and docosapentaenoic acid (DPA) are synthesized via an anaerobical PKS pathway. PUFA synthase assimilates fatty acyl-CoA, the product of FAS, as the starter unit to synthesize DPA, and this starter unit may be butyryl-CoA, hexanoyl-CoA, or octanoyl-CoA. DPA and DHA biosynthesis seem to differ by the reduction at the N-3 position by PUFA synthase, not the extension of carbon chain. In DHA biosynthesis, PUFA synthase extends the fatty acyl chain from the methyl toward the carboxyl end, and the double bond is formed when the carbon chain is growing, instead of afterward. Therefore, PUFA synthase is unable to transform DPA to DHA, suggesting that DPA is not the precursor of DHA. Moreover, DPA molecule is partly extended by FAS KS domain, so DPA biosynthesis is less dependent on PUFA synthase KS domain than DHA.",,,,,,,GO:0016746; GO:0016491,GO:0031177; GO:0016747,GO:0004315,,GO:0016491; GO:0016746,GO:0004312,0.5543,0.6044,,1.0,0.6044,4,0.6908,0.2594,no
PFA3_THRS2,A0A1B3PEI9,ESM2Text,Eukaryota,1497,"Polyketide synthase-like protein; part of the polyunsaturated fatty acid synthase composed of the 3 PKS-like subunits A, B and C. While the saturated fatty acids (SFAs) in Thraustochytrium are produced by the conventional fatty acid synthase (FAS) pathway, polyunsaturated fatty acids (PUFAs) including docosahexeanoic acid (DHA) and docosapentaenoic acid (DPA) are synthesized via an anaerobical PKS pathway. PUFA synthase assimilates fatty acyl-CoA, the product of FAS, as the starter unit to synthesize DPA, and this starter unit may be butyryl-CoA, hexanoyl-CoA, or octanoyl-CoA. DPA and DHA biosynthesis seem to differ by the reduction at the N-3 position by PUFA synthase, not the extension of carbon chain. In DHA biosynthesis, PUFA synthase extends the fatty acyl chain from the methyl toward the carboxyl end, and the double bond is formed when the carbon chain is growing, instead of afterward. Therefore, PUFA synthase is unable to transform DPA to DHA, suggesting that DPA is not the precursor of DHA. Moreover, DPA molecule is partly extended by FAS KS domain, so DPA biosynthesis is less dependent on PUFA synthase KS domain than DHA.","Esterase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcsC, are responsible for the",No,No,No,No,No,not-Yes,GO:0019171,GO:0016788,GO:0004091,GO:0004091,GO:0004091,GO:0016788,0.2845,0.2353,0.2353,0.2353,0.2845,5,0.255,0.1723,no
PFA3_THRS2,A0A1B3PEI9,Prot2Text,Eukaryota,1497,"Polyketide synthase-like protein; part of the polyunsaturated fatty acid synthase composed of the 3 PKS-like subunits A, B and C. While the saturated fatty acids (SFAs) in Thraustochytrium are produced by the conventional fatty acid synthase (FAS) pathway, polyunsaturated fatty acids (PUFAs) including docosahexeanoic acid (DHA) and docosapentaenoic acid (DPA) are synthesized via an anaerobical PKS pathway. PUFA synthase assimilates fatty acyl-CoA, the product of FAS, as the starter unit to synthesize DPA, and this starter unit may be butyryl-CoA, hexanoyl-CoA, or octanoyl-CoA. DPA and DHA biosynthesis seem to differ by the reduction at the N-3 position by PUFA synthase, not the extension of carbon chain. In DHA biosynthesis, PUFA synthase extends the fatty acyl chain from the methyl toward the carboxyl end, and the double bond is formed when the carbon chain is growing, instead of afterward. Therefore, PUFA synthase is unable to transform DPA to DHA, suggesting that DPA is not the precursor of DHA. Moreover, DPA molecule is partly extended by FAS KS domain, so DPA biosynthesis is less dependent on PUFA synthase KS domain than DHA.","Trichothecene C-1 hydrolase is one of the four eukaryotic enzyme-derived trimethylamine synthases (trichothecenes) that catalyze the formation of their various trichothecenes (ta-diketopiperazine) via the condensation of a 1,3-dihydroxy-2-naphthoyl-CoA starter unit with acetyl-CoA. Theta-diketopiperazine is a secondary metabolite that is converted to the trichothecene C-12 via a series of hydroxylations and O-methylations.",No,No,No,No,No,not-Yes,GO:0019171,,,,,,,,,,,0,,0.1723,no
PFA3_THRS2,A0A1B3PEI9,ProtT3,Eukaryota,1497,"Polyketide synthase-like protein; part of the polyunsaturated fatty acid synthase composed of the 3 PKS-like subunits A, B and C. While the saturated fatty acids (SFAs) in Thraustochytrium are produced by the conventional fatty acid synthase (FAS) pathway, polyunsaturated fatty acids (PUFAs) including docosahexeanoic acid (DHA) and docosapentaenoic acid (DPA) are synthesized via an anaerobical PKS pathway. PUFA synthase assimilates fatty acyl-CoA, the product of FAS, as the starter unit to synthesize DPA, and this starter unit may be butyryl-CoA, hexanoyl-CoA, or octanoyl-CoA. DPA and DHA biosynthesis seem to differ by the reduction at the N-3 position by PUFA synthase, not the extension of carbon chain. In DHA biosynthesis, PUFA synthase extends the fatty acyl chain from the methyl toward the carboxyl end, and the double bond is formed when the carbon chain is growing, instead of afterward. Therefore, PUFA synthase is unable to transform DPA to DHA, suggesting that DPA is not the precursor of DHA. Moreover, DPA molecule is partly extended by FAS KS domain, so DPA biosynthesis is less dependent on PUFA synthase KS domain than DHA.",Involved in the biosynthesis of unsaturated fatty acids for membrane lipid biosynthesis. Catalyzes the dehydration of (3R)-3-hydroxyacyl-ACP to (3R)-3-oxoacyl-ACP and the hydration of (3R)-3-oxoacyl-ACP to (3R)-3-hydroxyacyl-ACP. In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. In the C-terminal section; belongs to the 3-hydroxyacyl-ACP dehyd,Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0019171,GO:0016836,GO:0004317,GO:0016836,GO:0016836,GO:0004317,0.8582,0.0,0.8582,0.8582,0.0,5,0.5149,0.1723,no
PFA3_THRS2,A0A1B3PEI9,ProtTale,Eukaryota,1497,"Polyketide synthase-like protein; part of the polyunsaturated fatty acid synthase composed of the 3 PKS-like subunits A, B and C. While the saturated fatty acids (SFAs) in Thraustochytrium are produced by the conventional fatty acid synthase (FAS) pathway, polyunsaturated fatty acids (PUFAs) including docosahexeanoic acid (DHA) and docosapentaenoic acid (DPA) are synthesized via an anaerobical PKS pathway. PUFA synthase assimilates fatty acyl-CoA, the product of FAS, as the starter unit to synthesize DPA, and this starter unit may be butyryl-CoA, hexanoyl-CoA, or octanoyl-CoA. DPA and DHA biosynthesis seem to differ by the reduction at the N-3 position by PUFA synthase, not the extension of carbon chain. In DHA biosynthesis, PUFA synthase extends the fatty acyl chain from the methyl toward the carboxyl end, and the double bond is formed when the carbon chain is growing, instead of afterward. Therefore, PUFA synthase is unable to transform DPA to DHA, suggesting that DPA is not the precursor of DHA. Moreover, DPA molecule is partly extended by FAS KS domain, so DPA biosynthesis is less dependent on PUFA synthase KS domain than DHA.",Catalyzes the conversion of chorismate to homogentisate.,No,No,No,No,No,not-Yes,GO:0019171,GO:0004106,GO:0016829,,,,0.2353,0.6019,,,,2,0.4186,0.1723,no
PFA3_THRS2,A0A1B3PEI9,Protein2Text,Eukaryota,1497,"Polyketide synthase-like protein; part of the polyunsaturated fatty acid synthase composed of the 3 PKS-like subunits A, B and C. While the saturated fatty acids (SFAs) in Thraustochytrium are produced by the conventional fatty acid synthase (FAS) pathway, polyunsaturated fatty acids (PUFAs) including docosahexeanoic acid (DHA) and docosapentaenoic acid (DPA) are synthesized via an anaerobical PKS pathway. PUFA synthase assimilates fatty acyl-CoA, the product of FAS, as the starter unit to synthesize DPA, and this starter unit may be butyryl-CoA, hexanoyl-CoA, or octanoyl-CoA. DPA and DHA biosynthesis seem to differ by the reduction at the N-3 position by PUFA synthase, not the extension of carbon chain. In DHA biosynthesis, PUFA synthase extends the fatty acyl chain from the methyl toward the carboxyl end, and the double bond is formed when the carbon chain is growing, instead of afterward. Therefore, PUFA synthase is unable to transform DPA to DHA, suggesting that DPA is not the precursor of DHA. Moreover, DPA molecule is partly extended by FAS KS domain, so DPA biosynthesis is less dependent on PUFA synthase KS domain than DHA.","This protein is involved in the conversion of pyruvate to acetyl-CoA, a key step in cellular respiration. More specifically, it is a decarboxylase that catalyzes the decarboxylation of pyruvate to form acetyl-CoA.",No,No,No,No,No,not-Yes,GO:0019171,GO:0004739,GO:0004739,GO:0004737; GO:0016831,GO:0004739,GO:0004738,0.1998,0.1998,0.3786,0.1998,0.0,5,0.1956,0.1723,no
PFA3_THRS2,A0A1B3PEI9,Reference,Eukaryota,1497,"Polyketide synthase-like protein; part of the polyunsaturated fatty acid synthase composed of the 3 PKS-like subunits A, B and C. While the saturated fatty acids (SFAs) in Thraustochytrium are produced by the conventional fatty acid synthase (FAS) pathway, polyunsaturated fatty acids (PUFAs) including docosahexeanoic acid (DHA) and docosapentaenoic acid (DPA) are synthesized via an anaerobical PKS pathway. PUFA synthase assimilates fatty acyl-CoA, the product of FAS, as the starter unit to synthesize DPA, and this starter unit may be butyryl-CoA, hexanoyl-CoA, or octanoyl-CoA. DPA and DHA biosynthesis seem to differ by the reduction at the N-3 position by PUFA synthase, not the extension of carbon chain. In DHA biosynthesis, PUFA synthase extends the fatty acyl chain from the methyl toward the carboxyl end, and the double bond is formed when the carbon chain is growing, instead of afterward. Therefore, PUFA synthase is unable to transform DPA to DHA, suggesting that DPA is not the precursor of DHA. Moreover, DPA molecule is partly extended by FAS KS domain, so DPA biosynthesis is less dependent on PUFA synthase KS domain than DHA.","Polyketide synthase-like protein; part of the polyunsaturated fatty acid synthase composed of the 3 PKS-like subunits A, B and C. While the saturated fatty acids (SFAs) in Thraustochytrium are produced by the conventional fatty acid synthase (FAS) pathway, polyunsaturated fatty acids (PUFAs) including docosahexeanoic acid (DHA) and docosapentaenoic acid (DPA) are synthesized via an anaerobical PKS pathway. PUFA synthase assimilates fatty acyl-CoA, the product of FAS, as the starter unit to synthesize DPA, and this starter unit may be butyryl-CoA, hexanoyl-CoA, or octanoyl-CoA. DPA and DHA biosynthesis seem to differ by the reduction at the N-3 position by PUFA synthase, not the extension of carbon chain. In DHA biosynthesis, PUFA synthase extends the fatty acyl chain from the methyl toward the carboxyl end, and the double bond is formed when the carbon chain is growing, instead of afterward. Therefore, PUFA synthase is unable to transform DPA to DHA, suggesting that DPA is not the precursor of DHA. Moreover, DPA molecule is partly extended by FAS KS domain, so DPA biosynthesis is less dependent on PUFA synthase KS domain than DHA.",,,,,,,GO:0019171,GO:0031177; GO:0016747,GO:0004315,,GO:0016746,GO:0004312,0.184,0.1998,,0.2845,0.1998,4,0.217,0.1723,no
LP9C_GLOTR,A0A1C9ZMC3,ESM2Text,Eukaryota,239,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.","Chlorophyll a/b-binding protein; part of the gene cluster that mediates the biosynthesis of pneumocandins, lipohexapeptides of the echinocandin family that prevent fungal cell wall formation by non-competitive inhibition of beta-1,3-glucan synthase. The 10,12-dimethylmyristoyl side chain is synthesized by the reducing polyketide synthase gloL/GLPKS4. The thioesterase gloN/GLHYD exclusively interacts with gloL/GLPKS4 to maintain turnover of the polyketide side chain. The 10R,12S-dimethylmyristic acid is then transferred to the first thiolation domain of the nonribosomal peptide synthetase gloA/GLNRPS4 by the acyl-AMP ligase gloD/GLligase, followed by its acylation to L-ornithine to trigger elongation of the cyclic hexapeptide. L-ornithine, 4R-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2",No,No,Maybe,No,No,not-Yes,GO:0046872; GO:0004497,GO:0016168,,,GO:0016168,GO:0016168,0.2475,,,0.2475,0.2475,3,0.2475,0.3085,no
LP9C_GLOTR,A0A1C9ZMC3,Prot2Text,Eukaryota,239,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.","Catalyzes the oxidation of the heme macrocyclic porphyrin ring to the biliverdin in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron.",No,No,No,No,No,not-Yes,GO:0046872; GO:0004497,GO:0004392,GO:0004392,GO:0004392,GO:0004392,GO:0004392,0.4705,0.4705,0.4705,0.4705,0.4705,5,0.4705,0.3085,no
LP9C_GLOTR,A0A1C9ZMC3,ProtT3,Eukaryota,239,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.","Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the endohydrolysis of 1,3-1,4-beta-glucosidic linkages in cellulose (By similarity). Secreted. Belongs to the glycosyl hydrolase 16 family",Maybe,No,No,Maybe,Maybe,not-Yes,GO:0046872; GO:0004497,GO:0004553,GO:0008810,GO:0016798,GO:0004553,GO:0008810,0.2538,0.2193,0.3023,0.2538,0.2193,5,0.2497,0.3085,no
LP9C_GLOTR,A0A1C9ZMC3,ProtTale,Eukaryota,239,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.","Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0004497,GO:0004497,GO:0016491; GO:0005507,GO:0016491; GO:0005507,GO:0004497; GO:0005507,GO:0004497,0.7088,0.7926,0.7926,0.8854,0.7088,5,0.7776,0.3085,no
LP9C_GLOTR,A0A1C9ZMC3,Protein2Text,Eukaryota,239,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.","The molecular function of this protein is to catalyze the breakdown of cellulose, a complex carbohydrate found in plant cell walls. This protein is part of a larger enzyme complex that works to degrade cellulose into simpler sugars, which can then be used by the organism as energy. Specifically, it is a lytic polysaccharide monooxygenase, which is an enzyme that cleaves the beta-1,4-glycosidic bonds in cellulose chains. This is a key step in the degradation of cellulose, and is essential for the breakdown of plant biomass by many organisms.",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0046872; GO:0004497,GO:0016166,GO:0016166,GO:0016491,GO:0015645,,0.4059,0.4059,0.5957,0.2273,,4,0.4087,0.3085,no
LP9C_GLOTR,A0A1C9ZMC3,Reference,Eukaryota,239,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.","Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.",,,,,,,GO:0046872; GO:0004497,GO:0016491; GO:0005507,GO:0016491,GO:0004497; GO:0005507,GO:0016491; GO:0005507,GO:0016491,0.7926,0.5957,0.8854,0.7926,0.5957,5,0.7324,0.3085,no
BAUF_ACIBA,A0A1E3M8P2,ESM2Text,Bacteria,286,"Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell. Interacts with the siderophores acinetobactin (Acb) and preacinetobactin (pre-Acb) and catalyzes the reduction of the ferric iron bound to the siderophores to ferrous iron, resulting in destabilization of the siderophore chelation complex and entrance of ferrous iron into the intracellular pool of bioavailable metals. Can use NADH and NADPH as electron donors in vitro, but the reduction rate is very slow, suggesting that NADH and NADPH are not the physiological partners of BauF.",Transports electrons between flavodoxin or ferric-petrobactin and NADPH.,Maybe,No,No,No,Maybe,not-Yes,GO:0000166; GO:0016491,GO:0016491,GO:0009055,GO:0016491,GO:0009055; GO:0050661,GO:0009055; GO:0050661,0.7229,0.297,0.7229,0.5355,0.5355,5,0.5628,0.1994,no
BAUF_ACIBA,A0A1E3M8P2,Prot2Text,Bacteria,286,"Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell. Interacts with the siderophores acinetobactin (Acb) and preacinetobactin (pre-Acb) and catalyzes the reduction of the ferric iron bound to the siderophores to ferrous iron, resulting in destabilization of the siderophore chelation complex and entrance of ferrous iron into the intracellular pool of bioavailable metals. Can use NADH and NADPH as electron donors in vitro, but the reduction rate is very slow, suggesting that NADH and NADPH are not the physiological partners of BauF.",Mediates electron transfer from NADPH to a cytochrome P450 the catalytic subunit of cytochrome oxidase. It transfers the electrons to the cytochrome P450 iron-sulfur protein (CYP) of the acceptor to the active site of cytochrome oxidase.,No,No,No,No,Maybe,not-Yes,GO:0000166; GO:0016491,GO:0003958,GO:0003958,GO:0003958,GO:0003958,GO:0003958,0.4359,0.4359,0.4359,0.4359,0.4359,5,0.4359,0.1994,no
BAUF_ACIBA,A0A1E3M8P2,ProtT3,Bacteria,286,"Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell. Interacts with the siderophores acinetobactin (Acb) and preacinetobactin (pre-Acb) and catalyzes the reduction of the ferric iron bound to the siderophores to ferrous iron, resulting in destabilization of the siderophore chelation complex and entrance of ferrous iron into the intracellular pool of bioavailable metals. Can use NADH and NADPH as electron donors in vitro, but the reduction rate is very slow, suggesting that NADH and NADPH are not the physiological partners of BauF.",Involved in the transport of nickel. Cytoplasm. Belongs to the bacterial solute-binding protein 2 family,No,No,No,No,No,not-Yes,GO:0000166; GO:0016491,GO:0016151,GO:0016151,GO:0016151,GO:0016151,GO:0016151,0.2449,0.2449,0.2449,0.2449,0.2449,5,0.2449,0.1994,no
BAUF_ACIBA,A0A1E3M8P2,ProtTale,Bacteria,286,"Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell. Interacts with the siderophores acinetobactin (Acb) and preacinetobactin (pre-Acb) and catalyzes the reduction of the ferric iron bound to the siderophores to ferrous iron, resulting in destabilization of the siderophore chelation complex and entrance of ferrous iron into the intracellular pool of bioavailable metals. Can use NADH and NADPH as electron donors in vitro, but the reduction rate is very slow, suggesting that NADH and NADPH are not the physiological partners of BauF.","Superoxide dismutase that may be involved in the reduction of Fe(3+) to Fe(2+), thereby reducing the oxidative stress caused by the production of reactive oxygen species (ROS) by the electron transport chain. May be involved in the detoxification of H(2)O(2) and O(2)(-).",Maybe,No,No,No,No,not-Yes,GO:0000166; GO:0016491,GO:0004784,GO:0004784,GO:0004784,GO:0004784; GO:0046872,GO:0004784,0.4567,0.4567,0.4567,0.4979,0.4567,5,0.4649,0.1994,no
BAUF_ACIBA,A0A1E3M8P2,Protein2Text,Bacteria,286,"Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell. Interacts with the siderophores acinetobactin (Acb) and preacinetobactin (pre-Acb) and catalyzes the reduction of the ferric iron bound to the siderophores to ferrous iron, resulting in destabilization of the siderophore chelation complex and entrance of ferrous iron into the intracellular pool of bioavailable metals. Can use NADH and NADPH as electron donors in vitro, but the reduction rate is very slow, suggesting that NADH and NADPH are not the physiological partners of BauF.","This protein is involved in the oxidation of ribose-5-phosphate, specifically in the conversion of 5-dehydro-2-deoxy-D-ribose 5-phosphate to 5-dehydro-2-deoxy-D-ribose 1-phosphate.",No,No,No,No,No,not-Yes,GO:0000166; GO:0016491,,,GO:0016491,,,,,0.7229,,,1,0.7229,0.1994,no
BAUF_ACIBA,A0A1E3M8P2,Reference,Bacteria,286,"Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell. Interacts with the siderophores acinetobactin (Acb) and preacinetobactin (pre-Acb) and catalyzes the reduction of the ferric iron bound to the siderophores to ferrous iron, resulting in destabilization of the siderophore chelation complex and entrance of ferrous iron into the intracellular pool of bioavailable metals. Can use NADH and NADPH as electron donors in vitro, but the reduction rate is very slow, suggesting that NADH and NADPH are not the physiological partners of BauF.","Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell. Interacts with the siderophores acinetobactin (Acb) and preacinetobactin (pre-Acb) and catalyzes the reduction of the ferric iron bound to the siderophores to ferrous iron, resulting in destabilization of the siderophore chelation complex and entrance of ferrous iron into the intracellular pool of bioavailable metals. Can use NADH and NADPH as electron donors in vitro, but the reduction rate is very slow, suggesting that NADH and NADPH are not the physiological partners of BauF.",,,,,,,GO:0000166; GO:0016491,GO:0016491; GO:0008942,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.6753,0.7229,0.7229,0.7229,0.7229,5,0.7134,0.1994,no
G6PD_HANUV,A0A1E5S1A9,ESM2Text,Eukaryota,503,"Catalyzes the rate-limiting step of the oxidative pentose- phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis. The G6PDH activity is required to cope with hydrogen peroxide and potassium bisulfite stresses and plays a role in adaptation to conditions used in wine fermentations.",Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004345; GO:0050661,GO:0004345,GO:0004345,GO:0004345,GO:0004345,GO:0004345,0.6901,0.6901,0.6901,0.6901,0.6901,5,0.6901,0.3846,no
G6PD_HANUV,A0A1E5S1A9,Prot2Text,Eukaryota,503,"Catalyzes the rate-limiting step of the oxidative pentose- phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis. The G6PDH activity is required to cope with hydrogen peroxide and potassium bisulfite stresses and plays a role in adaptation to conditions used in wine fermentations.",Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004345; GO:0050661,GO:0004345,GO:0004345,GO:0004345,GO:0004345,GO:0004345,0.6901,0.6901,0.6901,0.6901,0.6901,5,0.6901,0.3846,no
G6PD_HANUV,A0A1E5S1A9,ProtT3,Eukaryota,503,"Catalyzes the rate-limiting step of the oxidative pentose- phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis. The G6PDH activity is required to cope with hydrogen peroxide and potassium bisulfite stresses and plays a role in adaptation to conditions used in wine fermentations.","Catalyzes the rate-limiting step of the oxidative pentose- phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis (By similarity). Belongs to the glucose-6-phosphate dehydrogenase family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004345; GO:0050661,GO:0004345,GO:0004345,GO:0004345,GO:0004345,GO:0004345,0.6901,0.6901,0.6901,0.6901,0.6901,5,0.6901,0.3846,no
G6PD_HANUV,A0A1E5S1A9,ProtTale,Eukaryota,503,"Catalyzes the rate-limiting step of the oxidative pentose- phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis. The G6PDH activity is required to cope with hydrogen peroxide and potassium bisulfite stresses and plays a role in adaptation to conditions used in wine fermentations.",Catalyzes the oxidation of glucose 6-phosphate to 6- phosphogluconolactone.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004345; GO:0050661,GO:0004346,GO:0004345,GO:0004345,GO:0004345,GO:0016616,0.0994,0.6901,0.6901,0.6901,0.5999,5,0.5539,0.3846,no
G6PD_HANUV,A0A1E5S1A9,Protein2Text,Eukaryota,503,"Catalyzes the rate-limiting step of the oxidative pentose- phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis. The G6PDH activity is required to cope with hydrogen peroxide and potassium bisulfite stresses and plays a role in adaptation to conditions used in wine fermentations.","This protein has a molecular function of being a transferase, specifically a transferase that catalyzes the transfer of a group from one compound to another. It is involved in the conversion of glucose-6-phosphate to 6-phosphogluconolactone, a key step in the pentose phosphate pathway.",No,Maybe,Maybe,No,No,not-Yes,GO:0004345; GO:0050661,GO:0004345,GO:0004345,GO:0004345,GO:0004345,GO:0004345,0.6901,0.6901,0.6901,0.6901,0.6901,5,0.6901,0.3846,no
G6PD_HANUV,A0A1E5S1A9,Reference,Eukaryota,503,"Catalyzes the rate-limiting step of the oxidative pentose- phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis. The G6PDH activity is required to cope with hydrogen peroxide and potassium bisulfite stresses and plays a role in adaptation to conditions used in wine fermentations.","Catalyzes the rate-limiting step of the oxidative pentose- phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis. The G6PDH activity is required to cope with hydrogen peroxide and potassium bisulfite stresses and plays a role in adaptation to conditions used in wine fermentations.",,,,,,,GO:0004345; GO:0050661,GO:0004345; GO:0050661,GO:0004345,GO:0004345,GO:0004345; GO:0050661,GO:0004345,1.0,0.6901,0.6901,1.0,0.6901,5,0.8141,0.3846,no
BDS_ALLAB,A0A1G9UQQ0,ESM2Text,Bacteria,363,"Diterpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) to bonnadiene. Cannot use geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylfarnesyl diphosphate (GFPP).",Catalyzes the cyclization of farnesyl diphosphate (FPP) to the tricyclic sesquiterpene pentalenene as the major product.,Maybe,No,No,No,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0016829,GO:0010333,GO:0000287; GO:0016829,GO:0010333,GO:0010333,0.4539,0.6963,0.7355,0.6963,0.6963,5,0.6557,0.1703,no
BDS_ALLAB,A0A1G9UQQ0,Prot2Text,Bacteria,363,"Diterpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) to bonnadiene. Cannot use geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylfarnesyl diphosphate (GFPP).","Involved in the biosynthesis of the labdane-type bicyclic diterpene labda-8(17),12(E),14-triene. Catalyzes the conversion of (+)-copalyl diphosphate to yield labda-8(17),12(E),14-triene.",Maybe,No,No,No,Maybe,not-Yes,GO:0046872; GO:0010333,,GO:0010333,GO:0016829,GO:0010333,GO:0010333,,0.6963,0.4539,0.6963,0.6963,4,0.6357,0.1703,no
BDS_ALLAB,A0A1G9UQQ0,ProtT3,Bacteria,363,"Diterpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) to bonnadiene. Cannot use geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylfarnesyl diphosphate (GFPP).","Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to (2E,6E,10E,14E,18E,22E,26E,30E,34E,38E,42E,46E,50E,54E,58E,62E,66E,70E,74E,78E,82E,86E,90E,94E,98E",No,No,No,No,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0016765,GO:0004659,GO:0016765,GO:0016765,GO:0004311,0.2318,0.1917,0.2318,0.2318,0.1415,5,0.2057,0.1703,no
BDS_ALLAB,A0A1G9UQQ0,ProtTale,Bacteria,363,"Diterpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) to bonnadiene. Cannot use geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylfarnesyl diphosphate (GFPP).","Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to yield the bicyclogermacrene (BGC) precursor germacrene D via a 1,10-cyclization.",Maybe,No,No,No,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0010333,GO:0034048,GO:0016829,GO:0010333,GO:0010333,0.6963,0.0,0.4539,0.6963,0.6963,5,0.5086,0.1703,no
BDS_ALLAB,A0A1G9UQQ0,Protein2Text,Bacteria,363,"Diterpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) to bonnadiene. Cannot use geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylfarnesyl diphosphate (GFPP).","The molecular function of this protein is an enzyme, specifically a cytochrome P450 monooxygenase, involved in the biosynthesis of a natural product.",No,No,No,No,No,not-Yes,GO:0046872; GO:0010333,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.2318,0.2318,0.2318,0.2318,0.2318,5,0.2318,0.1703,no
BDS_ALLAB,A0A1G9UQQ0,Reference,Bacteria,363,"Diterpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) to bonnadiene. Cannot use geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylfarnesyl diphosphate (GFPP).","Diterpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) to bonnadiene. Cannot use geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylfarnesyl diphosphate (GFPP).",,,,,,,GO:0046872; GO:0010333,GO:0010333,GO:0010333,GO:0010333,GO:0010333,GO:0016829,0.6963,0.6963,0.6963,0.6963,0.4539,5,0.6478,0.1703,no
PMS_ALLAB,A0A1G9VRW7,ESM2Text,Bacteria,339,"Diterpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) to phomopsene, a diterpene previously reported from the fungus P.amygdali. Phomopsene is the main product, but the enzyme can also produce allokutznerene (about 50% of phomopsene production activity) and traces of spiroviolene. Cannot use geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylfarnesyl diphosphate (GFPP).","Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) into the acyclic S-linalool and (2E,6E)-farnesyl diphosphate (FPP) into the aglyconium-linc monoterpene (Probable). The major products are (2E,6E)-farnesyl diphosphate and (2E,6E)-farnesyl diphosphate. In vitro, produces a mixture consisting of (2S,6R)-2S,6R-farnesyl diphosphate (MFDP) and (2S,6R)-farnesyl diphosphate (MFDP).",Maybe,No,No,No,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0016829,GO:0010333,,GO:0010333,GO:0010333,0.4539,0.6963,,0.6963,0.6963,4,0.6357,0.1987,no
PMS_ALLAB,A0A1G9VRW7,Prot2Text,Bacteria,339,"Diterpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) to phomopsene, a diterpene previously reported from the fungus P.amygdali. Phomopsene is the main product, but the enzyme can also produce allokutznerene (about 50% of phomopsene production activity) and traces of spiroviolene. Cannot use geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylfarnesyl diphosphate (GFPP).",Catalyzes the cyclization of farnesyl diphosphate (FPP) to isoafricanol.,Maybe,No,Maybe,No,Maybe,not-Yes,GO:0046872; GO:0010333,,GO:0010333,GO:0010333,GO:0010333,GO:0010333,,0.6963,0.6963,0.6963,0.6963,4,0.6963,0.1987,no
PMS_ALLAB,A0A1G9VRW7,ProtT3,Bacteria,339,"Diterpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) to phomopsene, a diterpene previously reported from the fungus P.amygdali. Phomopsene is the main product, but the enzyme can also produce allokutznerene (about 50% of phomopsene production activity) and traces of spiroviolene. Cannot use geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylfarnesyl diphosphate (GFPP).","Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to the bicyclic sesquiterpene (E)-beta-farnesene. Belongs to the terpene synthase family",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0010333,GO:0010333,GO:0010333,GO:0010333,GO:0010333,0.6963,0.6963,0.6963,0.6963,0.6963,5,0.6963,0.1987,no
PMS_ALLAB,A0A1G9VRW7,ProtTale,Bacteria,339,"Diterpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) to phomopsene, a diterpene previously reported from the fungus P.amygdali. Phomopsene is the main product, but the enzyme can also produce allokutznerene (about 50% of phomopsene production activity) and traces of spiroviolene. Cannot use geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylfarnesyl diphosphate (GFPP).","Terpene cyclase that catalyzes the cyclization of (2E,6E)- farnesyl diphosphate (FPP) to produce the sesquiterpene beta-caryophyllene. Is also able to use (2E)-geranyl diphosphate (GPP) as substrate for sesquiterpene synthesis, but not geranylgeranyl diphosphate (GGPP).",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0010333,GO:0010333,GO:0016829,GO:0010333,GO:0010333,0.6963,0.6963,0.4539,0.6963,0.6963,5,0.6478,0.1987,no
PMS_ALLAB,A0A1G9VRW7,Protein2Text,Bacteria,339,"Diterpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) to phomopsene, a diterpene previously reported from the fungus P.amygdali. Phomopsene is the main product, but the enzyme can also produce allokutznerene (about 50% of phomopsene production activity) and traces of spiroviolene. Cannot use geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylfarnesyl diphosphate (GFPP).","The molecular function of this protein is an isomerase, specifically involved in the biosynthesis of geranylgeranyl diphosphate (GGPP), a precursor molecule for the biosynthesis of terpenoids. It catalyzes the conversion of farnesyl diphosphate (FPP) to geranylgeranyl diphosphate (GGPP).",No,No,No,Maybe,No,not-Yes,GO:0046872; GO:0010333,GO:0004311,GO:0004337,GO:0004311,GO:0004311,,0.1415,0.1415,0.1415,0.1415,,4,0.1415,0.1987,no
PMS_ALLAB,A0A1G9VRW7,Reference,Bacteria,339,"Diterpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) to phomopsene, a diterpene previously reported from the fungus P.amygdali. Phomopsene is the main product, but the enzyme can also produce allokutznerene (about 50% of phomopsene production activity) and traces of spiroviolene. Cannot use geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylfarnesyl diphosphate (GFPP).","Diterpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) to phomopsene, a diterpene previously reported from the fungus P.amygdali. Phomopsene is the main product, but the enzyme can also produce allokutznerene (about 50% of phomopsene production activity) and traces of spiroviolene. Cannot use geranyl diphosphate (GPP), farnesyl diphosphate (FPP) and geranylfarnesyl diphosphate (GFPP).",,,,,,,GO:0046872; GO:0010333,GO:0010333,GO:0010333,GO:0010333,GO:0010333,GO:0016829,0.6963,0.6963,0.6963,0.6963,0.4539,5,0.6478,0.1987,no
BILB_COLS4,A0A1I1NU27,ESM2Text,Bacteria,161,"Component of the Bil (bacterial ISG15-like) antiviral defense system, composed of BilA, BilB, BilC and BilD. The Bil system specifically conjugates a ubiquitin-like moiety (bilA) to the bacteriophage central tail fiber (CTF, or tip attachment protein J) via reactions involving E1 (bilD) and E2 (bilB). Modifies CTF of phage SECphi27 and SECphi4, which probably interferes with assembly of the phage tail. Also modifies T5 baseplate hub protein pb3 (gene D16), but not gp27 of phage T6 (Bil defends against T6). BilB probably accepts ubiquitin from the BilA-BilD (E1) complex and catalyzes its covalent attachment to target protein (CTF) (Probable). Bil- encoding bacteria produce mostly defective phage SECphi27, many of which have phage assembly defects, including no tails. SECphi27 phage progeny produced in E.coli with the Bil system inject less DNA into naive host cells, maybe because the phage are less able to adsorb and inject their DNA into host cells.",Catalyzes the two-electron reduction of biliverdin IX-alpha at the C15 methine bridge.,No,No,No,No,No,not-Yes,GO:0019787,GO:0004074,GO:0004074,GO:0004074,GO:0004074,GO:0004074,0.2199,0.2199,0.2199,0.2199,0.2199,5,0.2199,0.5407,yes
BILB_COLS4,A0A1I1NU27,Prot2Text,Bacteria,161,"Component of the Bil (bacterial ISG15-like) antiviral defense system, composed of BilA, BilB, BilC and BilD. The Bil system specifically conjugates a ubiquitin-like moiety (bilA) to the bacteriophage central tail fiber (CTF, or tip attachment protein J) via reactions involving E1 (bilD) and E2 (bilB). Modifies CTF of phage SECphi27 and SECphi4, which probably interferes with assembly of the phage tail. Also modifies T5 baseplate hub protein pb3 (gene D16), but not gp27 of phage T6 (Bil defends against T6). BilB probably accepts ubiquitin from the BilA-BilD (E1) complex and catalyzes its covalent attachment to target protein (CTF) (Probable). Bil- encoding bacteria produce mostly defective phage SECphi27, many of which have phage assembly defects, including no tails. SECphi27 phage progeny produced in E.coli with the Bil system inject less DNA into naive host cells, maybe because the phage are less able to adsorb and inject their DNA into host cells.",Catalyzes the covalent attachment of ubiquitin to other proteins.,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0019787,GO:0004842,GO:0004842,GO:0004842,GO:0004842,GO:0004842,0.8982,0.8982,0.8982,0.8982,0.8982,5,0.8982,0.5407,yes
BILB_COLS4,A0A1I1NU27,ProtT3,Bacteria,161,"Component of the Bil (bacterial ISG15-like) antiviral defense system, composed of BilA, BilB, BilC and BilD. The Bil system specifically conjugates a ubiquitin-like moiety (bilA) to the bacteriophage central tail fiber (CTF, or tip attachment protein J) via reactions involving E1 (bilD) and E2 (bilB). Modifies CTF of phage SECphi27 and SECphi4, which probably interferes with assembly of the phage tail. Also modifies T5 baseplate hub protein pb3 (gene D16), but not gp27 of phage T6 (Bil defends against T6). BilB probably accepts ubiquitin from the BilA-BilD (E1) complex and catalyzes its covalent attachment to target protein (CTF) (Probable). Bil- encoding bacteria produce mostly defective phage SECphi27, many of which have phage assembly defects, including no tails. SECphi27 phage progeny produced in E.coli with the Bil system inject less DNA into naive host cells, maybe because the phage are less able to adsorb and inject their DNA into host cells.",Belongs to the UPF0254 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0019787,,,,,,,,,,,0,,0.5407,yes
BILB_COLS4,A0A1I1NU27,ProtTale,Bacteria,161,"Component of the Bil (bacterial ISG15-like) antiviral defense system, composed of BilA, BilB, BilC and BilD. The Bil system specifically conjugates a ubiquitin-like moiety (bilA) to the bacteriophage central tail fiber (CTF, or tip attachment protein J) via reactions involving E1 (bilD) and E2 (bilB). Modifies CTF of phage SECphi27 and SECphi4, which probably interferes with assembly of the phage tail. Also modifies T5 baseplate hub protein pb3 (gene D16), but not gp27 of phage T6 (Bil defends against T6). BilB probably accepts ubiquitin from the BilA-BilD (E1) complex and catalyzes its covalent attachment to target protein (CTF) (Probable). Bil- encoding bacteria produce mostly defective phage SECphi27, many of which have phage assembly defects, including no tails. SECphi27 phage progeny produced in E.coli with the Bil system inject less DNA into naive host cells, maybe because the phage are less able to adsorb and inject their DNA into host cells.","E2-like enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy and nucleophagy. Acts as an E2-like enzyme that catalyzes the conjugation of ATG12 to ATG5. ATG12 conjugation to ATG5 is required for proper localization of ATG8 to the preautophagosomal structure (PAS). Likely serves as an ATG5-recognition molecule.",Maybe,No,No,No,No,not-Yes,GO:0019787,GO:0061650,,,GO:0019783,,0.8982,,,0.3945,,2,0.6463,0.5407,yes
BILB_COLS4,A0A1I1NU27,Protein2Text,Bacteria,161,"Component of the Bil (bacterial ISG15-like) antiviral defense system, composed of BilA, BilB, BilC and BilD. The Bil system specifically conjugates a ubiquitin-like moiety (bilA) to the bacteriophage central tail fiber (CTF, or tip attachment protein J) via reactions involving E1 (bilD) and E2 (bilB). Modifies CTF of phage SECphi27 and SECphi4, which probably interferes with assembly of the phage tail. Also modifies T5 baseplate hub protein pb3 (gene D16), but not gp27 of phage T6 (Bil defends against T6). BilB probably accepts ubiquitin from the BilA-BilD (E1) complex and catalyzes its covalent attachment to target protein (CTF) (Probable). Bil- encoding bacteria produce mostly defective phage SECphi27, many of which have phage assembly defects, including no tails. SECphi27 phage progeny produced in E.coli with the Bil system inject less DNA into naive host cells, maybe because the phage are less able to adsorb and inject their DNA into host cells.","The molecular function of this protein is not explicitly stated in the provided information. However, based on its classification as a protein involved in a specific biological process, it is likely that this protein plays a role in DNA repair or damage tolerance. The fact that it is involved in the repair of DNA damage suggests that it may have a molecular function related to DNA metabolism, such as DNA binding, helicase activity, or ligase activity. However, without further information, it is difficult to determine the specific molecular function of this protein.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0019787,,,,,,,,,,,0,,0.5407,yes
BILB_COLS4,A0A1I1NU27,Reference,Bacteria,161,"Component of the Bil (bacterial ISG15-like) antiviral defense system, composed of BilA, BilB, BilC and BilD. The Bil system specifically conjugates a ubiquitin-like moiety (bilA) to the bacteriophage central tail fiber (CTF, or tip attachment protein J) via reactions involving E1 (bilD) and E2 (bilB). Modifies CTF of phage SECphi27 and SECphi4, which probably interferes with assembly of the phage tail. Also modifies T5 baseplate hub protein pb3 (gene D16), but not gp27 of phage T6 (Bil defends against T6). BilB probably accepts ubiquitin from the BilA-BilD (E1) complex and catalyzes its covalent attachment to target protein (CTF) (Probable). Bil- encoding bacteria produce mostly defective phage SECphi27, many of which have phage assembly defects, including no tails. SECphi27 phage progeny produced in E.coli with the Bil system inject less DNA into naive host cells, maybe because the phage are less able to adsorb and inject their DNA into host cells.","Component of the Bil (bacterial ISG15-like) antiviral defense system, composed of BilA, BilB, BilC and BilD. The Bil system specifically conjugates a ubiquitin-like moiety (bilA) to the bacteriophage central tail fiber (CTF, or tip attachment protein J) via reactions involving E1 (bilD) and E2 (bilB). Modifies CTF of phage SECphi27 and SECphi4, which probably interferes with assembly of the phage tail. Also modifies T5 baseplate hub protein pb3 (gene D16), but not gp27 of phage T6 (Bil defends against T6). BilB probably accepts ubiquitin from the BilA-BilD (E1) complex and catalyzes its covalent attachment to target protein (CTF) (Probable). Bil- encoding bacteria produce mostly defective phage SECphi27, many of which have phage assembly defects, including no tails. SECphi27 phage progeny produced in E.coli with the Bil system inject less DNA into naive host cells, maybe because the phage are less able to adsorb and inject their DNA into host cells.",,,,,,,GO:0019787,GO:0061631,GO:0061631,GO:0061631,GO:0061631,GO:0061631,0.7557,0.7557,0.7557,0.7557,0.7557,5,0.7557,0.5407,yes
BILD_COLS4,A0A1I1P074,ESM2Text,Bacteria,461,"Component of the Bil (bacterial ISG15-like) antiviral defense system, composed of BilA, BilB, BilC and BilD. The Bil system specifically conjugates a ubiquitin-like moiety (bilA) to the bacteriophage central tail fiber (CTF, or tip attachment protein J) via reactions involving E1 (bilD) and E2 (bilB). Modifies CTF of phage SECphi27 and SECphi4, which probably interferes with assembly of the phage tail. Also modifies T5 baseplate hub protein pb3 (gene D16), but not gp27 of phage T6 (Bil defends against T6). BilD (E1) catalyzes the first step in conjugation. Activates ubiquitin-like BilA by first adenylating its C-terminal glycine residue with ATP, and then conjugates it to the side chain of a cysteine residue in E1 (this protein), yielding a ubiquitin-E1 thioester and free AMP (Probable). Bil-encoding bacteria produce mostly defective phage SECphi27, many of which have phage assembly defects, including no tails. SECphi27 phage progeny produced in E.coli with the Bil system inject less DNA into naive host cells, maybe because the phage are less able to adsorb and inject their DNA into host cells.",Cofactor for the transcription factor TFIID that confers resistance to the bacteriocin tetracycline.,No,No,No,No,No,not-Yes,GO:0008641,,,,,,,,,,,0,,0.3168,no
BILD_COLS4,A0A1I1P074,Prot2Text,Bacteria,461,"Component of the Bil (bacterial ISG15-like) antiviral defense system, composed of BilA, BilB, BilC and BilD. The Bil system specifically conjugates a ubiquitin-like moiety (bilA) to the bacteriophage central tail fiber (CTF, or tip attachment protein J) via reactions involving E1 (bilD) and E2 (bilB). Modifies CTF of phage SECphi27 and SECphi4, which probably interferes with assembly of the phage tail. Also modifies T5 baseplate hub protein pb3 (gene D16), but not gp27 of phage T6 (Bil defends against T6). BilD (E1) catalyzes the first step in conjugation. Activates ubiquitin-like BilA by first adenylating its C-terminal glycine residue with ATP, and then conjugates it to the side chain of a cysteine residue in E1 (this protein), yielding a ubiquitin-E1 thioester and free AMP (Probable). Bil-encoding bacteria produce mostly defective phage SECphi27, many of which have phage assembly defects, including no tails. SECphi27 phage progeny produced in E.coli with the Bil system inject less DNA into naive host cells, maybe because the phage are less able to adsorb and inject their DNA into host cells.",Could be an alcohol dehydrogenase.,No,No,No,No,No,not-Yes,GO:0008641,GO:0004022,,,,,0.2017,,,,,1,0.2017,0.3168,no
BILD_COLS4,A0A1I1P074,ProtT3,Bacteria,461,"Component of the Bil (bacterial ISG15-like) antiviral defense system, composed of BilA, BilB, BilC and BilD. The Bil system specifically conjugates a ubiquitin-like moiety (bilA) to the bacteriophage central tail fiber (CTF, or tip attachment protein J) via reactions involving E1 (bilD) and E2 (bilB). Modifies CTF of phage SECphi27 and SECphi4, which probably interferes with assembly of the phage tail. Also modifies T5 baseplate hub protein pb3 (gene D16), but not gp27 of phage T6 (Bil defends against T6). BilD (E1) catalyzes the first step in conjugation. Activates ubiquitin-like BilA by first adenylating its C-terminal glycine residue with ATP, and then conjugates it to the side chain of a cysteine residue in E1 (this protein), yielding a ubiquitin-E1 thioester and free AMP (Probable). Bil-encoding bacteria produce mostly defective phage SECphi27, many of which have phage assembly defects, including no tails. SECphi27 phage progeny produced in E.coli with the Bil system inject less DNA into naive host cells, maybe because the phage are less able to adsorb and inject their DNA into host cells.",Catalyzes the hydrolysis of adenosylcobalamin (AdoCbl) to form adenosylcobalamin 5'-phosphate (AdoCbl-5'-P) and alpha-ribazole 5'-phosphate. Cell membrane; Multi-pass membrane protein,No,No,No,No,No,not-Yes,GO:0008641,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016787,0.3505,0.3505,0.3505,0.3505,0.3505,5,0.3505,0.3168,no
BILD_COLS4,A0A1I1P074,ProtTale,Bacteria,461,"Component of the Bil (bacterial ISG15-like) antiviral defense system, composed of BilA, BilB, BilC and BilD. The Bil system specifically conjugates a ubiquitin-like moiety (bilA) to the bacteriophage central tail fiber (CTF, or tip attachment protein J) via reactions involving E1 (bilD) and E2 (bilB). Modifies CTF of phage SECphi27 and SECphi4, which probably interferes with assembly of the phage tail. Also modifies T5 baseplate hub protein pb3 (gene D16), but not gp27 of phage T6 (Bil defends against T6). BilD (E1) catalyzes the first step in conjugation. Activates ubiquitin-like BilA by first adenylating its C-terminal glycine residue with ATP, and then conjugates it to the side chain of a cysteine residue in E1 (this protein), yielding a ubiquitin-E1 thioester and free AMP (Probable). Bil-encoding bacteria produce mostly defective phage SECphi27, many of which have phage assembly defects, including no tails. SECphi27 phage progeny produced in E.coli with the Bil system inject less DNA into naive host cells, maybe because the phage are less able to adsorb and inject their DNA into host cells.","An enzyme that catalyzes the cleavage of the amide bond of 6-oxo-D-fructose 1,7-bisphosphate (FBP) and formation of a carbon-carbon bond. Catalyzes the cleavage of the amide bond of 2-oxo-D-fructose 1,7-bisphosphate (OFBP) and formation of a carbon-carbon bond. Does not act on 3-deoxy-D-manno-heptulosonate 7-phosphate (DAHP) or 2-keto-D-gluconate 6-phosphate (KDGP).",No,No,No,No,No,not-Yes,GO:0008641,,GO:0016829,,GO:0016829,,,0.3505,,0.3505,,2,0.3505,0.3168,no
BILD_COLS4,A0A1I1P074,Protein2Text,Bacteria,461,"Component of the Bil (bacterial ISG15-like) antiviral defense system, composed of BilA, BilB, BilC and BilD. The Bil system specifically conjugates a ubiquitin-like moiety (bilA) to the bacteriophage central tail fiber (CTF, or tip attachment protein J) via reactions involving E1 (bilD) and E2 (bilB). Modifies CTF of phage SECphi27 and SECphi4, which probably interferes with assembly of the phage tail. Also modifies T5 baseplate hub protein pb3 (gene D16), but not gp27 of phage T6 (Bil defends against T6). BilD (E1) catalyzes the first step in conjugation. Activates ubiquitin-like BilA by first adenylating its C-terminal glycine residue with ATP, and then conjugates it to the side chain of a cysteine residue in E1 (this protein), yielding a ubiquitin-E1 thioester and free AMP (Probable). Bil-encoding bacteria produce mostly defective phage SECphi27, many of which have phage assembly defects, including no tails. SECphi27 phage progeny produced in E.coli with the Bil system inject less DNA into naive host cells, maybe because the phage are less able to adsorb and inject their DNA into host cells.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its classification as a beta-lactamase, it is likely that its molecular function is to catalyze the hydrolysis of beta-lactam antibiotics.",No,No,Vague,No,No,not-Yes,GO:0008641,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,0.2239,0.2239,0.2239,0.2239,0.2239,5,0.2239,0.3168,no
BILD_COLS4,A0A1I1P074,Reference,Bacteria,461,"Component of the Bil (bacterial ISG15-like) antiviral defense system, composed of BilA, BilB, BilC and BilD. The Bil system specifically conjugates a ubiquitin-like moiety (bilA) to the bacteriophage central tail fiber (CTF, or tip attachment protein J) via reactions involving E1 (bilD) and E2 (bilB). Modifies CTF of phage SECphi27 and SECphi4, which probably interferes with assembly of the phage tail. Also modifies T5 baseplate hub protein pb3 (gene D16), but not gp27 of phage T6 (Bil defends against T6). BilD (E1) catalyzes the first step in conjugation. Activates ubiquitin-like BilA by first adenylating its C-terminal glycine residue with ATP, and then conjugates it to the side chain of a cysteine residue in E1 (this protein), yielding a ubiquitin-E1 thioester and free AMP (Probable). Bil-encoding bacteria produce mostly defective phage SECphi27, many of which have phage assembly defects, including no tails. SECphi27 phage progeny produced in E.coli with the Bil system inject less DNA into naive host cells, maybe because the phage are less able to adsorb and inject their DNA into host cells.","Component of the Bil (bacterial ISG15-like) antiviral defense system, composed of BilA, BilB, BilC and BilD. The Bil system specifically conjugates a ubiquitin-like moiety (bilA) to the bacteriophage central tail fiber (CTF, or tip attachment protein J) via reactions involving E1 (bilD) and E2 (bilB). Modifies CTF of phage SECphi27 and SECphi4, which probably interferes with assembly of the phage tail. Also modifies T5 baseplate hub protein pb3 (gene D16), but not gp27 of phage T6 (Bil defends against T6). BilD (E1) catalyzes the first step in conjugation. Activates ubiquitin-like BilA by first adenylating its C-terminal glycine residue with ATP, and then conjugates it to the side chain of a cysteine residue in E1 (this protein), yielding a ubiquitin-E1 thioester and free AMP (Probable). Bil-encoding bacteria produce mostly defective phage SECphi27, many of which have phage assembly defects, including no tails. SECphi27 phage progeny produced in E.coli with the Bil system inject less DNA into naive host cells, maybe because the phage are less able to adsorb and inject their DNA into host cells.",,,,,,,GO:0008641,GO:0004839; GO:0005524,GO:0004839; GO:0005524,GO:0004839,GO:0061659; GO:0005524,GO:0004839,0.6271,0.6271,0.9054,0.2605,0.9054,5,0.6651,0.3168,no
FUP5_FUSPR,A0A1L7VI12,ESM2Text,Eukaryota,390,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusaproliferin (FUP) that belongs to the class of bicyclic sesterterpenoids. FUP5 catalyzes the final step of the pathway by adding an acetyl group at the C-24 position of terpestacin to yield fusaproliferin. The FUP biosynthetic pathway starts with the enzyme encoded by FUP1 that combines a C-terminal prenyltransferase domain responsible for the synthesis of geranylgeranyl diphosphate with the N-terminal terpene cyclase domain, to yield preterpestacin I. Preterpestacin I is then decorated by oxygenation steps that are catalyzed by two cytochrome P450 monooxygenases. First, FUP2 introduces a hydroxyl group at the C- 24 position resulting in the formation of preterpestacin IIa. The second P450 monooxygenase catalyzes the hydroxylation at C-16 and C-17 of preterpestacin IIa, producing preterpestacin III. Subsequently, the FAD-dependent oxidoreductase FUP4 catalyzes the oxidation of the hydroxy group at the C-16 position to a keto group, leading to the formation of (-)-terpestacin, which is the immediate precursor of FUP. The final step in the proposed biosynthetic pathway is the addition of an acetyl group at the C-24 position of terpestacin, which is catalyzed by the acetyltransferase FUP5.","Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome monooxygenase P450 claM then catalyzes the dimerization of nataloe-emodin to cladofulvin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008374,GO:0016407,GO:0016407,GO:0016746,GO:0016746,GO:0016407,0.7289,0.7289,0.729,0.729,0.7289,5,0.7289,0.355,no
FUP5_FUSPR,A0A1L7VI12,Prot2Text,Eukaryota,390,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusaproliferin (FUP) that belongs to the class of bicyclic sesterterpenoids. FUP5 catalyzes the final step of the pathway by adding an acetyl group at the C-24 position of terpestacin to yield fusaproliferin. The FUP biosynthetic pathway starts with the enzyme encoded by FUP1 that combines a C-terminal prenyltransferase domain responsible for the synthesis of geranylgeranyl diphosphate with the N-terminal terpene cyclase domain, to yield preterpestacin I. Preterpestacin I is then decorated by oxygenation steps that are catalyzed by two cytochrome P450 monooxygenases. First, FUP2 introduces a hydroxyl group at the C- 24 position resulting in the formation of preterpestacin IIa. The second P450 monooxygenase catalyzes the hydroxylation at C-16 and C-17 of preterpestacin IIa, producing preterpestacin III. Subsequently, the FAD-dependent oxidoreductase FUP4 catalyzes the oxidation of the hydroxy group at the C-16 position to a keto group, leading to the formation of (-)-terpestacin, which is the immediate precursor of FUP. The final step in the proposed biosynthetic pathway is the addition of an acetyl group at the C-24 position of terpestacin, which is catalyzed by the acetyltransferase FUP5.","Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate tolerance, py",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008374,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.355,no
FUP5_FUSPR,A0A1L7VI12,ProtT3,Eukaryota,390,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusaproliferin (FUP) that belongs to the class of bicyclic sesterterpenoids. FUP5 catalyzes the final step of the pathway by adding an acetyl group at the C-24 position of terpestacin to yield fusaproliferin. The FUP biosynthetic pathway starts with the enzyme encoded by FUP1 that combines a C-terminal prenyltransferase domain responsible for the synthesis of geranylgeranyl diphosphate with the N-terminal terpene cyclase domain, to yield preterpestacin I. Preterpestacin I is then decorated by oxygenation steps that are catalyzed by two cytochrome P450 monooxygenases. First, FUP2 introduces a hydroxyl group at the C- 24 position resulting in the formation of preterpestacin IIa. The second P450 monooxygenase catalyzes the hydroxylation at C-16 and C-17 of preterpestacin IIa, producing preterpestacin III. Subsequently, the FAD-dependent oxidoreductase FUP4 catalyzes the oxidation of the hydroxy group at the C-16 position to a keto group, leading to the formation of (-)-terpestacin, which is the immediate precursor of FUP. The final step in the proposed biosynthetic pathway is the addition of an acetyl group at the C-24 position of terpestacin, which is catalyzed by the acetyltransferase FUP5.","Acetyltransferase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties . L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L- homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O- acetyltransferase F",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008374,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.355,no
FUP5_FUSPR,A0A1L7VI12,ProtTale,Eukaryota,390,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusaproliferin (FUP) that belongs to the class of bicyclic sesterterpenoids. FUP5 catalyzes the final step of the pathway by adding an acetyl group at the C-24 position of terpestacin to yield fusaproliferin. The FUP biosynthetic pathway starts with the enzyme encoded by FUP1 that combines a C-terminal prenyltransferase domain responsible for the synthesis of geranylgeranyl diphosphate with the N-terminal terpene cyclase domain, to yield preterpestacin I. Preterpestacin I is then decorated by oxygenation steps that are catalyzed by two cytochrome P450 monooxygenases. First, FUP2 introduces a hydroxyl group at the C- 24 position resulting in the formation of preterpestacin IIa. The second P450 monooxygenase catalyzes the hydroxylation at C-16 and C-17 of preterpestacin IIa, producing preterpestacin III. Subsequently, the FAD-dependent oxidoreductase FUP4 catalyzes the oxidation of the hydroxy group at the C-16 position to a keto group, leading to the formation of (-)-terpestacin, which is the immediate precursor of FUP. The final step in the proposed biosynthetic pathway is the addition of an acetyl group at the C-24 position of terpestacin, which is catalyzed by the acetyltransferase FUP5.","Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an oxidative dec",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008374,GO:0016407,GO:0016747,GO:0016747,GO:0016747,GO:0016407,0.7289,0.8582,0.8582,0.8582,0.7289,5,0.8065,0.355,no
FUP5_FUSPR,A0A1L7VI12,Protein2Text,Eukaryota,390,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusaproliferin (FUP) that belongs to the class of bicyclic sesterterpenoids. FUP5 catalyzes the final step of the pathway by adding an acetyl group at the C-24 position of terpestacin to yield fusaproliferin. The FUP biosynthetic pathway starts with the enzyme encoded by FUP1 that combines a C-terminal prenyltransferase domain responsible for the synthesis of geranylgeranyl diphosphate with the N-terminal terpene cyclase domain, to yield preterpestacin I. Preterpestacin I is then decorated by oxygenation steps that are catalyzed by two cytochrome P450 monooxygenases. First, FUP2 introduces a hydroxyl group at the C- 24 position resulting in the formation of preterpestacin IIa. The second P450 monooxygenase catalyzes the hydroxylation at C-16 and C-17 of preterpestacin IIa, producing preterpestacin III. Subsequently, the FAD-dependent oxidoreductase FUP4 catalyzes the oxidation of the hydroxy group at the C-16 position to a keto group, leading to the formation of (-)-terpestacin, which is the immediate precursor of FUP. The final step in the proposed biosynthetic pathway is the addition of an acetyl group at the C-24 position of terpestacin, which is catalyzed by the acetyltransferase FUP5.","This protein is involved in the molecular function of being a transferase, specifically a glycosyltransferase. It is a type of enzyme that catalyzes the transfer of a sugar molecule from one molecule to another, in this case, from UDP-glucose to a sterol acceptor molecule, resulting in the formation of a sterol glycoside. This process is important for the synthesis of sterol glycosides, which are found in the cell membrane and play a crucial role in maintaining membrane structure and function.",No,No,No,No,No,not-Yes,GO:0008374,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.482,0.482,0.482,0.482,0.482,5,0.482,0.355,no
FUP5_FUSPR,A0A1L7VI12,Reference,Eukaryota,390,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusaproliferin (FUP) that belongs to the class of bicyclic sesterterpenoids. FUP5 catalyzes the final step of the pathway by adding an acetyl group at the C-24 position of terpestacin to yield fusaproliferin. The FUP biosynthetic pathway starts with the enzyme encoded by FUP1 that combines a C-terminal prenyltransferase domain responsible for the synthesis of geranylgeranyl diphosphate with the N-terminal terpene cyclase domain, to yield preterpestacin I. Preterpestacin I is then decorated by oxygenation steps that are catalyzed by two cytochrome P450 monooxygenases. First, FUP2 introduces a hydroxyl group at the C- 24 position resulting in the formation of preterpestacin IIa. The second P450 monooxygenase catalyzes the hydroxylation at C-16 and C-17 of preterpestacin IIa, producing preterpestacin III. Subsequently, the FAD-dependent oxidoreductase FUP4 catalyzes the oxidation of the hydroxy group at the C-16 position to a keto group, leading to the formation of (-)-terpestacin, which is the immediate precursor of FUP. The final step in the proposed biosynthetic pathway is the addition of an acetyl group at the C-24 position of terpestacin, which is catalyzed by the acetyltransferase FUP5.","Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusaproliferin (FUP) that belongs to the class of bicyclic sesterterpenoids. FUP5 catalyzes the final step of the pathway by adding an acetyl group at the C-24 position of terpestacin to yield fusaproliferin. The FUP biosynthetic pathway starts with the enzyme encoded by FUP1 that combines a C-terminal prenyltransferase domain responsible for the synthesis of geranylgeranyl diphosphate with the N-terminal terpene cyclase domain, to yield preterpestacin I. Preterpestacin I is then decorated by oxygenation steps that are catalyzed by two cytochrome P450 monooxygenases. First, FUP2 introduces a hydroxyl group at the C- 24 position resulting in the formation of preterpestacin IIa. The second P450 monooxygenase catalyzes the hydroxylation at C-16 and C-17 of preterpestacin IIa, producing preterpestacin III. Subsequently, the FAD-dependent oxidoreductase FUP4 catalyzes the oxidation of the hydroxy group at the C-16 position to a keto group, leading to the formation of (-)-terpestacin, which is the immediate precursor of FUP. The final step in the proposed biosynthetic pathway is the addition of an acetyl group at the C-24 position of terpestacin, which is catalyzed by the acetyltransferase FUP5.",,,,,,,GO:0008374,GO:0016747,GO:0016747,GO:0016407,GO:0016407,GO:0016746,0.8582,0.8582,0.7289,0.7289,0.729,5,0.7806,0.355,no
AACA_ASPA1,A0A1L9X999,ESM2Text,Eukaryota,1733,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the diketopiperazine (DKP) aspkyncin. AacA catalyzes the condensation of two unusual amino-acids, N-methyl-L-alanine and L-kynurenine (L-Kyn), via the nucleophilic attack of the secondary amine group of N-methyl-L-alanine on the thioester of N-methyl-L-alanine-L-Kyn-S-T2, resulting in the formation of aspkyncin. N-methyl-L-alanine originates from the methylation of L-alanine by the methyltransferase aacB whereas L-kynurenine is produced by the indoleamine-2,3-dioxygenase (IDO) that catalyzes the ring-opening oxidation of L-Trp to form N-formyl-l- kynurenine, followed by subsequent hydrolyzation to L-kynurenine (L- Kyn) through an endogenous L-kynurenine formamidase (Probable).","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome monooxygenase P450 claM then catalyzes the dimerization of nataloe-emodin to cladofulvin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:1904091; GO:0031177,,GO:0016874,GO:0003824,GO:0016874,GO:0016874; GO:0005524,,0.6793,0.612,0.6793,0.6615,4,0.658,0.2978,no
AACA_ASPA1,A0A1L9X999,Prot2Text,Eukaryota,1733,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the diketopiperazine (DKP) aspkyncin. AacA catalyzes the condensation of two unusual amino-acids, N-methyl-L-alanine and L-kynurenine (L-Kyn), via the nucleophilic attack of the secondary amine group of N-methyl-L-alanine on the thioester of N-methyl-L-alanine-L-Kyn-S-T2, resulting in the formation of aspkyncin. N-methyl-L-alanine originates from the methylation of L-alanine by the methyltransferase aacB whereas L-kynurenine is produced by the indoleamine-2,3-dioxygenase (IDO) that catalyzes the ring-opening oxidation of L-Trp to form N-formyl-l- kynurenine, followed by subsequent hydrolyzation to L-kynurenine (L- Kyn) through an endogenous L-kynurenine formamidase (Probable).","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome monooxygenase P450 claM then catalyzes the dimerization of nataloe-emodin to cladofulvin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:1904091; GO:0031177,,,GO:0016874,,GO:0016874,,,0.6793,,0.6793,2,0.6793,0.2978,no
AACA_ASPA1,A0A1L9X999,ProtT3,Eukaryota,1733,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the diketopiperazine (DKP) aspkyncin. AacA catalyzes the condensation of two unusual amino-acids, N-methyl-L-alanine and L-kynurenine (L-Kyn), via the nucleophilic attack of the secondary amine group of N-methyl-L-alanine on the thioester of N-methyl-L-alanine-L-Kyn-S-T2, resulting in the formation of aspkyncin. N-methyl-L-alanine originates from the methylation of L-alanine by the methyltransferase aacB whereas L-kynurenine is produced by the indoleamine-2,3-dioxygenase (IDO) that catalyzes the ring-opening oxidation of L-Trp to form N-formyl-l- kynurenine, followed by subsequent hydrolyzation to L-kynurenine (L- Kyn) through an endogenous L-kynurenine formamidase (Probable).","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of austinol, a fungal meroterpenoid . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA . 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN . Further epoxidation by",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:1904091; GO:0031177,GO:0016874,GO:0016874,GO:0016874,GO:0016874,GO:0016874; GO:0005524,0.6793,0.6793,0.6793,0.6793,0.6615,5,0.6757,0.2978,no
AACA_ASPA1,A0A1L9X999,ProtTale,Eukaryota,1733,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the diketopiperazine (DKP) aspkyncin. AacA catalyzes the condensation of two unusual amino-acids, N-methyl-L-alanine and L-kynurenine (L-Kyn), via the nucleophilic attack of the secondary amine group of N-methyl-L-alanine on the thioester of N-methyl-L-alanine-L-Kyn-S-T2, resulting in the formation of aspkyncin. N-methyl-L-alanine originates from the methylation of L-alanine by the methyltransferase aacB whereas L-kynurenine is produced by the indoleamine-2,3-dioxygenase (IDO) that catalyzes the ring-opening oxidation of L-Trp to form N-formyl-l- kynurenine, followed by subsequent hydrolyzation to L-kynurenine (L- Kyn) through an endogenous L-kynurenine formamidase (Probable).","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties. L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism. The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:1904091; GO:0031177,GO:0016874,GO:0016874,GO:0016874,GO:0016874,,0.6793,0.6793,0.6793,0.6793,,4,0.6793,0.2978,no
AACA_ASPA1,A0A1L9X999,Protein2Text,Eukaryota,1733,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the diketopiperazine (DKP) aspkyncin. AacA catalyzes the condensation of two unusual amino-acids, N-methyl-L-alanine and L-kynurenine (L-Kyn), via the nucleophilic attack of the secondary amine group of N-methyl-L-alanine on the thioester of N-methyl-L-alanine-L-Kyn-S-T2, resulting in the formation of aspkyncin. N-methyl-L-alanine originates from the methylation of L-alanine by the methyltransferase aacB whereas L-kynurenine is produced by the indoleamine-2,3-dioxygenase (IDO) that catalyzes the ring-opening oxidation of L-Trp to form N-formyl-l- kynurenine, followed by subsequent hydrolyzation to L-kynurenine (L- Kyn) through an endogenous L-kynurenine formamidase (Probable).","This protein is a nonribosomal peptide synthase (NRPS), which is a type of enzyme that catalyzes the synthesis of peptides from amino acids. Specifically, this protein is involved in the biosynthesis of a nonribosomal peptide, which is a type of natural product that consists of a linear or cyclic peptide backbone with various functional groups. The molecular function of this protein is to condense amino acids into a peptide backbone, which is then further modified by various enzymes to produce the final product.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:1904091; GO:0031177,,GO:0003824,,,,,0.612,,,,1,0.612,0.2978,no
AACA_ASPA1,A0A1L9X999,Reference,Eukaryota,1733,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the diketopiperazine (DKP) aspkyncin. AacA catalyzes the condensation of two unusual amino-acids, N-methyl-L-alanine and L-kynurenine (L-Kyn), via the nucleophilic attack of the secondary amine group of N-methyl-L-alanine on the thioester of N-methyl-L-alanine-L-Kyn-S-T2, resulting in the formation of aspkyncin. N-methyl-L-alanine originates from the methylation of L-alanine by the methyltransferase aacB whereas L-kynurenine is produced by the indoleamine-2,3-dioxygenase (IDO) that catalyzes the ring-opening oxidation of L-Trp to form N-formyl-l- kynurenine, followed by subsequent hydrolyzation to L-kynurenine (L- Kyn) through an endogenous L-kynurenine formamidase (Probable).","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the diketopiperazine (DKP) aspkyncin. AacA catalyzes the condensation of two unusual amino-acids, N-methyl-L-alanine and L-kynurenine (L-Kyn), via the nucleophilic attack of the secondary amine group of N-methyl-L-alanine on the thioester of N-methyl-L-alanine-L-Kyn-S-T2, resulting in the formation of aspkyncin. N-methyl-L-alanine originates from the methylation of L-alanine by the methyltransferase aacB whereas L-kynurenine is produced by the indoleamine-2,3-dioxygenase (IDO) that catalyzes the ring-opening oxidation of L-Trp to form N-formyl-l- kynurenine, followed by subsequent hydrolyzation to L-kynurenine (L- Kyn) through an endogenous L-kynurenine formamidase (Probable).",,,,,,,GO:0016874; GO:1904091; GO:0031177,GO:0031177; GO:0016874,GO:0008927,,GO:0016874,,0.918,0.2868,,0.6793,,3,0.628,0.2978,no
AACD_ASPA1,A0A1L9X9G5,ESM2Text,Eukaryota,438,"Amino acid oxidase; part of the gene cluster that mediates the biosynthesis of the diketopiperazine (DKP) aspkyncin. The function of aacD within the pathway has still to be characterized. Aspkyncin is produced by the NRPS aacA via condensation of the two unusual amino-acids N-methyl-L-alanine and L-kynurenine (L-Kyn). N-methyl-L-alanine originates from the methylation of L-alanine by the methyltransferase aacB whereas L- kynurenine is produced by the indoleamine-2,3-dioxygenase (IDO) that catalyzes the ring-opening oxidation of L-Trp to form N-formyl-l- kynurenine, followed by subsequent hydrolyzation to L-kynurenine (L- Kyn) through an endogenous L-kynurenine formamidase (Probable).",Oxidizes L-pipecolate and L-proline.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0050660; GO:0051698; GO:0008115,GO:0016491,GO:0016491,GO:0016491,GO:0016645,GO:0004657,0.4827,0.4827,0.4827,0.5726,0.4032,5,0.4848,0.1972,no
AACD_ASPA1,A0A1L9X9G5,Prot2Text,Eukaryota,438,"Amino acid oxidase; part of the gene cluster that mediates the biosynthesis of the diketopiperazine (DKP) aspkyncin. The function of aacD within the pathway has still to be characterized. Aspkyncin is produced by the NRPS aacA via condensation of the two unusual amino-acids N-methyl-L-alanine and L-kynurenine (L-Kyn). N-methyl-L-alanine originates from the methylation of L-alanine by the methyltransferase aacB whereas L- kynurenine is produced by the indoleamine-2,3-dioxygenase (IDO) that catalyzes the ring-opening oxidation of L-Trp to form N-formyl-l- kynurenine, followed by subsequent hydrolyzation to L-kynurenine (L- Kyn) through an endogenous L-kynurenine formamidase (Probable).",Oxidative cleavage of octopine into L-arginine and pyruvate.,No,No,No,No,No,not-Yes,GO:0050660; GO:0051698; GO:0008115,GO:0008969,GO:0016491,GO:0016491,GO:0016491,GO:0008840,0.1404,0.4827,0.4827,0.4827,0.169,5,0.3515,0.1972,no
AACD_ASPA1,A0A1L9X9G5,ProtT3,Eukaryota,438,"Amino acid oxidase; part of the gene cluster that mediates the biosynthesis of the diketopiperazine (DKP) aspkyncin. The function of aacD within the pathway has still to be characterized. Aspkyncin is produced by the NRPS aacA via condensation of the two unusual amino-acids N-methyl-L-alanine and L-kynurenine (L-Kyn). N-methyl-L-alanine originates from the methylation of L-alanine by the methyltransferase aacB whereas L- kynurenine is produced by the indoleamine-2,3-dioxygenase (IDO) that catalyzes the ring-opening oxidation of L-Trp to form N-formyl-l- kynurenine, followed by subsequent hydrolyzation to L-kynurenine (L- Kyn) through an endogenous L-kynurenine formamidase (Probable).",Belongs to the L-amino acid oxidase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0050660; GO:0051698; GO:0008115,GO:0016641,GO:0001678,GO:0016641,GO:0016641,GO:0001678,0.321,0.0,0.321,0.321,0.0,5,0.1926,0.1972,no
AACD_ASPA1,A0A1L9X9G5,ProtTale,Eukaryota,438,"Amino acid oxidase; part of the gene cluster that mediates the biosynthesis of the diketopiperazine (DKP) aspkyncin. The function of aacD within the pathway has still to be characterized. Aspkyncin is produced by the NRPS aacA via condensation of the two unusual amino-acids N-methyl-L-alanine and L-kynurenine (L-Kyn). N-methyl-L-alanine originates from the methylation of L-alanine by the methyltransferase aacB whereas L- kynurenine is produced by the indoleamine-2,3-dioxygenase (IDO) that catalyzes the ring-opening oxidation of L-Trp to form N-formyl-l- kynurenine, followed by subsequent hydrolyzation to L-kynurenine (L- Kyn) through an endogenous L-kynurenine formamidase (Probable).","Catalyzes the oxidative deamination of L-glutamate to 2- oxoglutarate, the first step of the kynurenine pathway of tryptophan degradation.",Maybe,No,No,No,Maybe,not-Yes,GO:0050660; GO:0051698; GO:0008115,GO:0004352,GO:0016638,GO:0004352,GO:0004352,GO:0004352,0.211,0.3874,0.211,0.211,0.211,5,0.2463,0.1972,no
AACD_ASPA1,A0A1L9X9G5,Protein2Text,Eukaryota,438,"Amino acid oxidase; part of the gene cluster that mediates the biosynthesis of the diketopiperazine (DKP) aspkyncin. The function of aacD within the pathway has still to be characterized. Aspkyncin is produced by the NRPS aacA via condensation of the two unusual amino-acids N-methyl-L-alanine and L-kynurenine (L-Kyn). N-methyl-L-alanine originates from the methylation of L-alanine by the methyltransferase aacB whereas L- kynurenine is produced by the indoleamine-2,3-dioxygenase (IDO) that catalyzes the ring-opening oxidation of L-Trp to form N-formyl-l- kynurenine, followed by subsequent hydrolyzation to L-kynurenine (L- Kyn) through an endogenous L-kynurenine formamidase (Probable).","The molecular function of this protein is an oxidoreductase, specifically a NAD(+) dependent dehydrogenase. It catalyzes the oxidation of D-xylose to D-xylulose.",Vague,No,No,No,No,not-Yes,GO:0050660; GO:0051698; GO:0008115,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4827,0.4827,0.4827,0.4827,0.4827,5,0.4827,0.1972,no
AACD_ASPA1,A0A1L9X9G5,Reference,Eukaryota,438,"Amino acid oxidase; part of the gene cluster that mediates the biosynthesis of the diketopiperazine (DKP) aspkyncin. The function of aacD within the pathway has still to be characterized. Aspkyncin is produced by the NRPS aacA via condensation of the two unusual amino-acids N-methyl-L-alanine and L-kynurenine (L-Kyn). N-methyl-L-alanine originates from the methylation of L-alanine by the methyltransferase aacB whereas L- kynurenine is produced by the indoleamine-2,3-dioxygenase (IDO) that catalyzes the ring-opening oxidation of L-Trp to form N-formyl-l- kynurenine, followed by subsequent hydrolyzation to L-kynurenine (L- Kyn) through an endogenous L-kynurenine formamidase (Probable).","Amino acid oxidase; part of the gene cluster that mediates the biosynthesis of the diketopiperazine (DKP) aspkyncin. The function of aacD within the pathway has still to be characterized. Aspkyncin is produced by the NRPS aacA via condensation of the two unusual amino-acids N-methyl-L-alanine and L-kynurenine (L-Kyn). N-methyl-L-alanine originates from the methylation of L-alanine by the methyltransferase aacB whereas L- kynurenine is produced by the indoleamine-2,3-dioxygenase (IDO) that catalyzes the ring-opening oxidation of L-Trp to form N-formyl-l- kynurenine, followed by subsequent hydrolyzation to L-kynurenine (L- Kyn) through an endogenous L-kynurenine formamidase (Probable).",,,,,,,GO:0050660; GO:0051698; GO:0008115,GO:0016491,GO:0016491,GO:0016491,GO:0001307,GO:0016491,0.4827,0.4827,0.4827,0.0,0.4827,5,0.3862,0.1972,no
PIGM_MONRU,A0A1P8VF93,ESM2Text,Eukaryota,508,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants. PigM and pigO are involved in the elimination of the omega-1 alcohol with pigM acting as an O-acetyltransferase that synthesizes the O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4- hydroxy-2-oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially involved in the biosynthesis of orange and red pigments via desaturation of C6(7).","Transcriptional regulator that may regulate the expression of the loline biosynthesis cluster 1, one of the 2 clusters involved in the biosynthesis of loline alkaloids, potent insecticidal agents composed of a pyrrolizidine ring system and an uncommon ether bridge linking carbons 2 and 7.",No,No,No,No,No,not-Yes,GO:0016746; GO:0031409,,,,GO:0003700,,,,,0.2461,,1,0.2461,0.2273,no
PIGM_MONRU,A0A1P8VF93,Prot2Text,Eukaryota,508,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants. PigM and pigO are involved in the elimination of the omega-1 alcohol with pigM acting as an O-acetyltransferase that synthesizes the O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4- hydroxy-2-oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially involved in the biosynthesis of orange and red pigments via desaturation of C6(7).","Trichothecene C-5 acyltransferase; part of the gene cluster that mediates the biosynthesis of the trichothecene harzianum A (HA) that plays a role in Botrytis cinerea antagonistic activity and plant defense priming. The biosynthesis of harzianum A begins with the cyclization of farnesyl diphosphate to trichodiene and is catalyzed by the trichodiene synthase TRI5. Trichodiene undergoes a series of oxygenations catalyzed by the cytochrome P450 monooxygenase TRI4. TRI4 controls the addition of 3 oxygens at C-2, C-11, and the C-12, C-13-epoxide to form the intermediate isotrichodiol. Isotrichodiol then undergoes a non-enzymatic isomerization and cyclization to form 12,13-epoxytrichothec-9-ene (EPT) which is further converted to trichodermol by the cytochrome P450 monooxygenase TRI11 via C-4 hydroxylation. The last step of HA synthesis is esterification of an octatriendi",Maybe,Maybe,Yes,No,Maybe,not-Yes,GO:0016746; GO:0031409,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.7379,0.7379,0.7379,0.6214,0.7379,5,0.7146,0.2273,no
PIGM_MONRU,A0A1P8VF93,ProtT3,Eukaryota,508,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants. PigM and pigO are involved in the elimination of the omega-1 alcohol with pigM acting as an O-acetyltransferase that synthesizes the O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4- hydroxy-2-oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially involved in the biosynthesis of orange and red pigments via desaturation of C6(7).","O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties . L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L- homoserine by cluster enzymes aspartate kinase FUB5 and homoserine O- acetyltransferase FUB6, as well as enzymes of the primary metabolism",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016746; GO:0031409,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.5386,0.5386,0.5386,0.5386,0.5386,5,0.5386,0.2273,no
PIGM_MONRU,A0A1P8VF93,ProtTale,Eukaryota,508,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants. PigM and pigO are involved in the elimination of the omega-1 alcohol with pigM acting as an O-acetyltransferase that synthesizes the O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4- hydroxy-2-oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially involved in the biosynthesis of orange and red pigments via desaturation of C6(7).","Acyltransferase; part of the gene cluster that mediates the biosynthesis of pyranterreones, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase pytA that condenses 4 malonyl-CoA units ato the acetyl starter unit by the modular PKS of pytA. The acyl chain is then connected to an L-serine through the amide bond by the modular NRPS of pytA. A tetramic acid is formed and released from the PKS-NRPS pytA to give pyranterreone",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016746; GO:0031409,GO:0016746,GO:0016747,GO:0016747,GO:0016747,GO:0016747,0.7379,0.6214,0.6214,0.6214,0.6214,5,0.6447,0.2273,no
PIGM_MONRU,A0A1P8VF93,Protein2Text,Eukaryota,508,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants. PigM and pigO are involved in the elimination of the omega-1 alcohol with pigM acting as an O-acetyltransferase that synthesizes the O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4- hydroxy-2-oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially involved in the biosynthesis of orange and red pigments via desaturation of C6(7).","The molecular function of this protein is likely to be a part of the cytochrome P450 family, which is a large family of enzymes that catalyze the oxidation of organic substances. However, without more specific information, it is difficult to determine the exact molecular function of this protein.",No,No,No,No,No,not-Yes,GO:0016746; GO:0031409,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.3314,0.3314,0.3314,0.3314,0.3314,5,0.3314,0.2273,no
PIGM_MONRU,A0A1P8VF93,Reference,Eukaryota,508,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants. PigM and pigO are involved in the elimination of the omega-1 alcohol with pigM acting as an O-acetyltransferase that synthesizes the O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4- hydroxy-2-oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially involved in the biosynthesis of orange and red pigments via desaturation of C6(7).","O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of azaphilone pigments (MonAzPs), a complex mixture of compounds with a common azaphilone skeleton very widely used as food colorants. PigM and pigO are involved in the elimination of the omega-1 alcohol with pigM acting as an O-acetyltransferase that synthesizes the O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The first step of the pathway is performed by the nrPKS pigA that forms the hexaketide precursor from successive condensations of five malonyl-CoA units, with a simple acetyl-CoA starter unit. The role of esterase pigG is not clear, but it may play at most a supplementary role in the formation of the benzaldehyde produced by the pigA nrPKS. This very reactive benzaldehyde is intercepted by the pigC ketoreductase that to provide the first stable enzyme-free MonAzPs intermediate, 6-(4- hydroxy-2-oxopentyl)-3-methyl-2,4-dioxocyclohexane carbaldehyde, also known as M7PKS-1. The FAD-dependent monooxygenase pigN hydroxylates M7PKS-1 at C-4, which triggers the formation of the pyran ring. PigJ, pigK and pigD are involved in the acetylation of the pyran ring. PigJ and pigK form the two subunits of a dedicated fungal FAS that produces the side chain fatty acyl moiety of MonAzPs and pigD transfers the fatty acyl chain to the C-4 alcohol. PigM and pigO are involved in the elimination of the omega-1 alcohol. PigM acts as an O-acetyltransferase that synthesizes the putative O-11 acetyl intermediate whereas pigO eliminates acetic acid to yield an intermediate with a C10(11) double bond. The dehydration of the C-11 alcohol followed by the reduction of the C6(7) double bond by the NAD(P)H-dependent oxidoreductase pigE increases the electrophilicity of the C-5 ketone of the resulting acyl benzopyran. This in turn sets up the C-5 ketone for an intramolecular Knoevenagel aldol condensation with the C-20 enol of the side chain. This condensation affords the characteristic linear tricyclic carbon skeletons of the yellow pigments that serve as the common precursors for the classical yellow pigments monascin and ankaflavin, orange pigments rubopunctatin and monascorubrin, and red pigments ribropunctamine and monascorubramine. The FAD-dependent oxidoreductase pigF is especially involved in the biosynthesis of orange and red pigments via desaturation of C6(7).",,,,,,,GO:0016746; GO:0031409,GO:0016747,GO:0016747,GO:0016407,GO:0016407,GO:0016746,0.6214,0.6214,0.5386,0.5386,0.7379,5,0.6116,0.2273,no
DDAN_AMPQE,A0A1X7TVA9,ESM2Text,Eukaryota,533,"The C-terminal purine nucleoside phosphorylase (PNP) domain cleaves the N-glycosidic bond of ATP, and to a lesser extent dATP, to release adenine and a sugar triphosphate; has weak activity on ADP and AMP and no activity on dADP, dAMP, adenosine, deoxyadenosine or other (d)NTPs.","Receptor for the endogenous polyamine spermidine and spermine. Binds and transports spermine, but not spermidine. Mediates the antiportive action of the antephase complex. Cleaves and activates both adenylate cyclase and adenosine deaminase (AdoC) in vitro, but only adenosine deaminase activity is observed.",No,No,No,No,No,not-Yes,GO:0008782; GO:0008930,,,,,,,,,,,0,,0.6088,yes
DDAN_AMPQE,A0A1X7TVA9,Prot2Text,Eukaryota,533,"The C-terminal purine nucleoside phosphorylase (PNP) domain cleaves the N-glycosidic bond of ATP, and to a lesser extent dATP, to release adenine and a sugar triphosphate; has weak activity on ADP and AMP and no activity on dADP, dAMP, adenosine, deoxyadenosine or other (d)NTPs.",Bifunctional phosphorylase and phosphorylase involved in the reversible conversion of 5-phosphoribose 1-phosphate to 5-phosphoribosyl alpha-D-ribose 1-phosphate. Involved in transamination reactions involved in the degradation of purine nucleotides.,Maybe,No,Maybe,No,Maybe,not-Yes,GO:0008782; GO:0008930,,,,,,,,,,,0,,0.6088,yes
DDAN_AMPQE,A0A1X7TVA9,ProtT3,Eukaryota,533,"The C-terminal purine nucleoside phosphorylase (PNP) domain cleaves the N-glycosidic bond of ATP, and to a lesser extent dATP, to release adenine and a sugar triphosphate; has weak activity on ADP and AMP and no activity on dADP, dAMP, adenosine, deoxyadenosine or other (d)NTPs.",Belongs to the Nudix hydrolase family,Vague,Vague,No,Vague,Vague,not-Yes,GO:0008782; GO:0008930,,GO:0016787,GO:0016787,GO:0016787,GO:0016787,,0.5807,0.5807,0.5807,0.5807,4,0.5807,0.6088,yes
DDAN_AMPQE,A0A1X7TVA9,ProtTale,Eukaryota,533,"The C-terminal purine nucleoside phosphorylase (PNP) domain cleaves the N-glycosidic bond of ATP, and to a lesser extent dATP, to release adenine and a sugar triphosphate; has weak activity on ADP and AMP and no activity on dADP, dAMP, adenosine, deoxyadenosine or other (d)NTPs.",Toxic component of a type II toxin-antitoxin (TA) system. Upon expression in E.coli inhibits cell growth in a concentration-dependent manner. Its toxic effect is neutralized by coexpression with cognate antitoxin YafQ.,No,No,No,No,No,not-Yes,GO:0008782; GO:0008930,,,,,,,,,,,0,,0.6088,yes
DDAN_AMPQE,A0A1X7TVA9,Protein2Text,Eukaryota,533,"The C-terminal purine nucleoside phosphorylase (PNP) domain cleaves the N-glycosidic bond of ATP, and to a lesser extent dATP, to release adenine and a sugar triphosphate; has weak activity on ADP and AMP and no activity on dADP, dAMP, adenosine, deoxyadenosine or other (d)NTPs.","The molecular function of this protein is not specified in the provided text, but based on its name, it is likely involved in the regulation of inflammation or the immune response. However, without more information, it is difficult to determine its specific molecular function. 

If you have any more information about the protein or its role in a specific organism, I may be able to provide more insight.",Vague,No,Vague,No,Vague,not-Yes,GO:0008782; GO:0008930,,,,,,,,,,,0,,0.6088,yes
DDAN_AMPQE,A0A1X7TVA9,Reference,Eukaryota,533,"The C-terminal purine nucleoside phosphorylase (PNP) domain cleaves the N-glycosidic bond of ATP, and to a lesser extent dATP, to release adenine and a sugar triphosphate; has weak activity on ADP and AMP and no activity on dADP, dAMP, adenosine, deoxyadenosine or other (d)NTPs.","The C-terminal purine nucleoside phosphorylase (PNP) domain cleaves the N-glycosidic bond of ATP, and to a lesser extent dATP, to release adenine and a sugar triphosphate; has weak activity on ADP and AMP and no activity on dADP, dAMP, adenosine, deoxyadenosine or other (d)NTPs.",,,,,,,GO:0008782; GO:0008930,GO:0004731,GO:0004731,GO:0004731,GO:0016799,GO:0004731,0.1911,0.1911,0.1911,0.8234,0.1911,5,0.3176,0.6088,yes
PPTA_AURME,A0A223GB52,ESM2Text,Eukaryota,338,"Acyl-carrier-protein synthase that transfers the 4'- phosphopantetheine moiety from coenzyme A to a Ser of an acyl-carrier- protein. The 4'-phosphopantetheine (4'-PPT) portion of CoA provides the essential prosthetic group for a number of carrier proteins and multi- domain enzymes, priming them for the acceptance of acyl building blocks in fatty acid synthesis and many aspects of secondary metabolism mediated by polyketide synthases (PKSs) and non-ribosomal peptide synthetases (NRPSs). Plays a key role in liamocins biosynthesis by activationg the HR-PKS PKS1 that produces 3,5- dihydroxydecanoic acid, a precursor of liamocins.","Key enzyme in the biosynthesis of the coenzyme F430, the prostaglandin A2 (PGA2), which is a potent inhibitor of fosfomycin. Catalyzes the transfer of a succinyl residue from the coenzyme F430anyl-CoA terminator (CoA) to the phosphopantetheine prostaglandin A2 (PGA2) to yield the activated multifunctional enzyme F430a. It is strictly a bifunctional enzyme that controls the synthesis of F430 and the phosphopantetheine prostaglandin A2.",No,No,No,No,No,not-Yes,GO:0008897; GO:0000287,,,,,,,,,,,0,,0.2848,no
PPTA_AURME,A0A223GB52,Prot2Text,Eukaryota,338,"Acyl-carrier-protein synthase that transfers the 4'- phosphopantetheine moiety from coenzyme A to a Ser of an acyl-carrier- protein. The 4'-phosphopantetheine (4'-PPT) portion of CoA provides the essential prosthetic group for a number of carrier proteins and multi- domain enzymes, priming them for the acceptance of acyl building blocks in fatty acid synthesis and many aspects of secondary metabolism mediated by polyketide synthases (PKSs) and non-ribosomal peptide synthetases (NRPSs). Plays a key role in liamocins biosynthesis by activationg the HR-PKS PKS1 that produces 3,5- dihydroxydecanoic acid, a precursor of liamocins.",Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of an acyl-carrier-protein. The enzyme is able to transfer the cofactor to a broad range of enzymes with acyl- or peptidyl-carrier protein domains.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008897; GO:0000287,GO:0008897,GO:0008897,GO:0008897,GO:0008897,GO:0008897,0.6924,0.6924,0.6924,0.6924,0.6924,5,0.6924,0.2848,no
PPTA_AURME,A0A223GB52,ProtT3,Eukaryota,338,"Acyl-carrier-protein synthase that transfers the 4'- phosphopantetheine moiety from coenzyme A to a Ser of an acyl-carrier- protein. The 4'-phosphopantetheine (4'-PPT) portion of CoA provides the essential prosthetic group for a number of carrier proteins and multi- domain enzymes, priming them for the acceptance of acyl building blocks in fatty acid synthesis and many aspects of secondary metabolism mediated by polyketide synthases (PKSs) and non-ribosomal peptide synthetases (NRPSs). Plays a key role in liamocins biosynthesis by activationg the HR-PKS PKS1 that produces 3,5- dihydroxydecanoic acid, a precursor of liamocins.",Catalyzes the transfer of a 4'-phosphopantetheine moiety from coenzyme A to a Ser of an acyl-carrier protein. Belongs to the P-Pant transferase superfamily. AcpS family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008897; GO:0000287,GO:0008897,GO:0008897,GO:0008897,GO:0008897,GO:0008897,0.6924,0.6924,0.6924,0.6924,0.6924,5,0.6924,0.2848,no
PPTA_AURME,A0A223GB52,ProtTale,Eukaryota,338,"Acyl-carrier-protein synthase that transfers the 4'- phosphopantetheine moiety from coenzyme A to a Ser of an acyl-carrier- protein. The 4'-phosphopantetheine (4'-PPT) portion of CoA provides the essential prosthetic group for a number of carrier proteins and multi- domain enzymes, priming them for the acceptance of acyl building blocks in fatty acid synthesis and many aspects of secondary metabolism mediated by polyketide synthases (PKSs) and non-ribosomal peptide synthetases (NRPSs). Plays a key role in liamocins biosynthesis by activationg the HR-PKS PKS1 that produces 3,5- dihydroxydecanoic acid, a precursor of liamocins.","Catalyzes the transfer of the activated acyl group from 3-hydroxyacyl-[acyl-carrier-protein] (ACP) to an acyl carrier protein (ACP), to open an acyl-ACP thioester.",No,No,No,No,No,not-Yes,GO:0008897; GO:0000287,GO:0016746,GO:0016747,GO:0016747,GO:0016747,GO:0016747,0.3587,0.2964,0.2964,0.2964,0.2964,5,0.3089,0.2848,no
PPTA_AURME,A0A223GB52,Protein2Text,Eukaryota,338,"Acyl-carrier-protein synthase that transfers the 4'- phosphopantetheine moiety from coenzyme A to a Ser of an acyl-carrier- protein. The 4'-phosphopantetheine (4'-PPT) portion of CoA provides the essential prosthetic group for a number of carrier proteins and multi- domain enzymes, priming them for the acceptance of acyl building blocks in fatty acid synthesis and many aspects of secondary metabolism mediated by polyketide synthases (PKSs) and non-ribosomal peptide synthetases (NRPSs). Plays a key role in liamocins biosynthesis by activationg the HR-PKS PKS1 that produces 3,5- dihydroxydecanoic acid, a precursor of liamocins.","The molecular function of this protein is an enzyme that catalyzes the conversion of an intermediate in the biosynthesis of a specific molecule. However, more specific information is not available.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008897; GO:0000287,,,,,,,,,,,0,,0.2848,no
PPTA_AURME,A0A223GB52,Reference,Eukaryota,338,"Acyl-carrier-protein synthase that transfers the 4'- phosphopantetheine moiety from coenzyme A to a Ser of an acyl-carrier- protein. The 4'-phosphopantetheine (4'-PPT) portion of CoA provides the essential prosthetic group for a number of carrier proteins and multi- domain enzymes, priming them for the acceptance of acyl building blocks in fatty acid synthesis and many aspects of secondary metabolism mediated by polyketide synthases (PKSs) and non-ribosomal peptide synthetases (NRPSs). Plays a key role in liamocins biosynthesis by activationg the HR-PKS PKS1 that produces 3,5- dihydroxydecanoic acid, a precursor of liamocins.","Acyl-carrier-protein synthase that transfers the 4'- phosphopantetheine moiety from coenzyme A to a Ser of an acyl-carrier- protein. The 4'-phosphopantetheine (4'-PPT) portion of CoA provides the essential prosthetic group for a number of carrier proteins and multi- domain enzymes, priming them for the acceptance of acyl building blocks in fatty acid synthesis and many aspects of secondary metabolism mediated by polyketide synthases (PKSs) and non-ribosomal peptide synthetases (NRPSs). Plays a key role in liamocins biosynthesis by activationg the HR-PKS PKS1 that produces 3,5- dihydroxydecanoic acid, a precursor of liamocins.",,,,,,,GO:0008897; GO:0000287,GO:0008897; GO:0031177,GO:0008897,GO:0008897,GO:0008897,GO:0008897,0.6863,0.6924,0.6924,0.6924,0.6924,5,0.6912,0.2848,no
MPDH_AURME,A0A223HDH4,ESM2Text,Eukaryota,386,"Catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway (Probable). Plays a key role in liamocins biosynthesis by providing the mannitol moity that is linked to 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) via ester bond formation catalyzed by the esterase EST1.",Catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008926,GO:0008926,GO:0004009,GO:0016491,GO:0008926,GO:0047711,1.0,0.0,0.6019,1.0,0.1803,5,0.5564,0.3503,no
MPDH_AURME,A0A223HDH4,Prot2Text,Eukaryota,386,"Catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway (Probable). Plays a key role in liamocins biosynthesis by providing the mannitol moity that is linked to 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) via ester bond formation catalyzed by the esterase EST1.",Catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008926,GO:0016616,GO:0004034,GO:0008926,GO:0004332,GO:0004009,0.8582,0.1998,1.0,0.1998,0.0,5,0.4516,0.3503,no
MPDH_AURME,A0A223HDH4,ProtT3,Eukaryota,386,"Catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway (Probable). Plays a key role in liamocins biosynthesis by providing the mannitol moity that is linked to 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) via ester bond formation catalyzed by the esterase EST1.",Catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway. Belongs to the mannitol dehydrogenase family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008926,GO:0008926,GO:0004352,GO:0004117,GO:0008926,GO:0047864,1.0,0.261,0.1161,1.0,0.1998,5,0.5154,0.3503,no
MPDH_AURME,A0A223HDH4,ProtTale,Eukaryota,386,"Catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway (Probable). Plays a key role in liamocins biosynthesis by providing the mannitol moity that is linked to 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) via ester bond formation catalyzed by the esterase EST1.","Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso- diaminopimelic acid, an essential component of bacterial cell walls.",No,No,No,No,No,not-Yes,GO:0008926,GO:0009014,GO:0016787,GO:0016787,GO:0016787,GO:0016787,0.1998,0.3552,0.3552,0.3552,0.3552,5,0.3241,0.3503,no
MPDH_AURME,A0A223HDH4,Protein2Text,Eukaryota,386,"Catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway (Probable). Plays a key role in liamocins biosynthesis by providing the mannitol moity that is linked to 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) via ester bond formation catalyzed by the esterase EST1.","The molecular function of this protein is a lyase, specifically a dehydratase that catalyzes the conversion of trans-aconitate to cis-aconitate.",No,No,No,No,No,not-Yes,GO:0008926,GO:0003994,GO:0003994,GO:0003994,GO:0003994,GO:0003994,0.1998,0.1998,0.1998,0.1998,0.1998,5,0.1998,0.3503,no
MPDH_AURME,A0A223HDH4,Reference,Eukaryota,386,"Catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway (Probable). Plays a key role in liamocins biosynthesis by providing the mannitol moity that is linked to 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) via ester bond formation catalyzed by the esterase EST1.","Catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway (Probable). Plays a key role in liamocins biosynthesis by providing the mannitol moity that is linked to 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) via ester bond formation catalyzed by the esterase EST1.",,,,,,,GO:0008926,GO:0016616; GO:0051287,GO:0016616,GO:0008926,GO:0016491; GO:0051287,GO:0016616,0.5956,0.8582,1.0,0.4247,0.8582,5,0.7473,0.3503,no
NMTDH_AURME,A0A223HDI5,ESM2Text,Eukaryota,266,"Catalyzes the interconversion between D-mannitol and D- fructose (Probable). Plays a key role in liamocins biosynthesis by providing the mannitol moity that is linked to 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) via ester bond formation catalyzed by the esterase EST1.","Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome P450 monooxygenase P450B then catalyzes the dimerization of nataloe-emodin to cladofulvin.",No,No,No,No,No,not-Yes,GO:0050085; GO:0050664,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.6605,0.6605,0.6605,0.6605,0.6605,5,0.6605,0.0817,no
NMTDH_AURME,A0A223HDI5,Prot2Text,Eukaryota,266,"Catalyzes the interconversion between D-mannitol and D- fructose (Probable). Plays a key role in liamocins biosynthesis by providing the mannitol moity that is linked to 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) via ester bond formation catalyzed by the esterase EST1.","D-mannitol 2-dehydrogenase which is not necessary for D-mannitol catabolism. D-mannitol metabolism occurs via at least two different routes involving mannitol dehydrogenase (MDH) or mannitol 1-phosphate dehydrogenase, and the exact physiological role of mannitol dehydrogenase remains unclear.",Yes,Maybe,Yes,Maybe,Yes,Yes,GO:0050085; GO:0050664,GO:0008926,GO:0008926,GO:0004567,GO:0008926,GO:0008926,0.6188,0.6188,0.1957,0.6188,0.6188,5,0.5342,0.0817,no
NMTDH_AURME,A0A223HDI5,ProtT3,Eukaryota,266,"Catalyzes the interconversion between D-mannitol and D- fructose (Probable). Plays a key role in liamocins biosynthesis by providing the mannitol moity that is linked to 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) via ester bond formation catalyzed by the esterase EST1.","Plastid, chloroplast. Belongs to the short-chain dehydrogenases/reductases (SDR) family",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0050085; GO:0050664,,GO:0016491,,GO:0016491,,,0.6605,,0.6605,,2,0.6605,0.0817,no
NMTDH_AURME,A0A223HDI5,ProtTale,Eukaryota,266,"Catalyzes the interconversion between D-mannitol and D- fructose (Probable). Plays a key role in liamocins biosynthesis by providing the mannitol moity that is linked to 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) via ester bond formation catalyzed by the esterase EST1.",Involved in the degradation of L-arabinose via L-ribulose. Catalyzes the NAD(P)(+)-dependent oxidation of L-ribulose to dihydroxyacetone.,No,No,No,No,No,not-Yes,GO:0050085; GO:0050664,GO:0016491,GO:0016491; GO:0050661,GO:0016491,GO:0016491,GO:0016616,0.6605,0.5162,0.6605,0.6605,0.727,5,0.6449,0.0817,no
NMTDH_AURME,A0A223HDI5,Protein2Text,Eukaryota,266,"Catalyzes the interconversion between D-mannitol and D- fructose (Probable). Plays a key role in liamocins biosynthesis by providing the mannitol moity that is linked to 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) via ester bond formation catalyzed by the esterase EST1.","The molecular function of this protein is an oxidoreductase, specifically a short-chain dehydrogenase/reductase.",Vague,No,Maybe,Vague,Vague,not-Yes,GO:0050085; GO:0050664,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.6605,0.6605,0.6605,0.6605,0.6605,5,0.6605,0.0817,no
NMTDH_AURME,A0A223HDI5,Reference,Eukaryota,266,"Catalyzes the interconversion between D-mannitol and D- fructose (Probable). Plays a key role in liamocins biosynthesis by providing the mannitol moity that is linked to 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) via ester bond formation catalyzed by the esterase EST1.","Catalyzes the interconversion between D-mannitol and D- fructose (Probable). Plays a key role in liamocins biosynthesis by providing the mannitol moity that is linked to 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) via ester bond formation catalyzed by the esterase EST1.",,,,,,,GO:0050085; GO:0050664,GO:0019576,GO:0008926,GO:0016491,GO:0008926,GO:0016616,0.0,0.6188,0.6605,0.6188,0.727,5,0.525,0.0817,no
TYR2_HAHS4,A0A261GVB1,ESM2Text,Bacteria,550,"Copper-containing oxidase that catalyzes the conversion of L- tyrosine to L-dopa and then to L-dopaquinone. Can use various phenols such as p-coumaric acid, phenol, pyrocatechol, syringol or pyrogallol. Accepts several of the constituents of lignin and potentially participates in lignin functionalization.",This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds.,Yes,Yes,Yes,Maybe,Yes,Yes,GO:0046872; GO:0004503,GO:0005507; GO:0016491,GO:0008471,GO:0005507; GO:0016491,GO:0016682; GO:0005507,GO:0005507; GO:0016491,0.6579,0.0,0.6579,0.5681,0.6579,5,0.5084,0.2587,no
TYR2_HAHS4,A0A261GVB1,Prot2Text,Bacteria,550,"Copper-containing oxidase that catalyzes the conversion of L- tyrosine to L-dopa and then to L-dopaquinone. Can use various phenols such as p-coumaric acid, phenol, pyrocatechol, syringol or pyrogallol. Accepts several of the constituents of lignin and potentially participates in lignin functionalization.",This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds.,Yes,Yes,Yes,Maybe,Yes,Yes,GO:0046872; GO:0004503,GO:0008471,GO:0008471,GO:0016491; GO:0005507,GO:0008471,GO:0008471,0.0,0.0,0.6579,0.0,0.0,5,0.1316,0.2587,no
TYR2_HAHS4,A0A261GVB1,ProtT3,Bacteria,550,"Copper-containing oxidase that catalyzes the conversion of L- tyrosine to L-dopa and then to L-dopaquinone. Can use various phenols such as p-coumaric acid, phenol, pyrocatechol, syringol or pyrogallol. Accepts several of the constituents of lignin and potentially participates in lignin functionalization.",This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Belongs to the tyrosinase family,Yes,Yes,Yes,Maybe,Yes,Yes,GO:0046872; GO:0004503,GO:0004503; GO:0005507,GO:0004503,GO:0004503; GO:0005507,GO:0004503; GO:0005507,GO:0004503,0.8854,0.6939,0.8854,0.8854,0.6939,5,0.8088,0.2587,no
TYR2_HAHS4,A0A261GVB1,ProtTale,Bacteria,550,"Copper-containing oxidase that catalyzes the conversion of L- tyrosine to L-dopa and then to L-dopaquinone. Can use various phenols such as p-coumaric acid, phenol, pyrocatechol, syringol or pyrogallol. Accepts several of the constituents of lignin and potentially participates in lignin functionalization.",This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds.,Yes,Yes,Yes,Maybe,Yes,Yes,GO:0046872; GO:0004503,GO:0016682; GO:0005507,GO:0004097; GO:0005507,GO:0004097; GO:0005507,GO:0016491; GO:0005507,GO:0008471,0.5681,0.6181,0.6181,0.6579,0.0,5,0.4924,0.2587,no
TYR2_HAHS4,A0A261GVB1,Protein2Text,Bacteria,550,"Copper-containing oxidase that catalyzes the conversion of L- tyrosine to L-dopa and then to L-dopaquinone. Can use various phenols such as p-coumaric acid, phenol, pyrocatechol, syringol or pyrogallol. Accepts several of the constituents of lignin and potentially participates in lignin functionalization.","This protein is a type of enzyme known as a polyphenol oxidase, which is involved in the oxidation of phenolic compounds. Specifically, it is a copper-containing tyrosinase that catalyzes the oxidation of tyrosine to dopachrome, which is a key step in the synthesis of melanin. The molecular function of this protein is to catalyze the oxidation of phenolic compounds, such as tyrosine, to their corresponding quinones, which are then further oxidized to melanin.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0004503,GO:0004503,GO:0004503,GO:0004503,GO:0004503,GO:0004503,0.6939,0.6939,0.6939,0.6939,0.6939,5,0.6939,0.2587,no
TYR2_HAHS4,A0A261GVB1,Reference,Bacteria,550,"Copper-containing oxidase that catalyzes the conversion of L- tyrosine to L-dopa and then to L-dopaquinone. Can use various phenols such as p-coumaric acid, phenol, pyrocatechol, syringol or pyrogallol. Accepts several of the constituents of lignin and potentially participates in lignin functionalization.","Copper-containing oxidase that catalyzes the conversion of L- tyrosine to L-dopa and then to L-dopaquinone. Can use various phenols such as p-coumaric acid, phenol, pyrocatechol, syringol or pyrogallol. Accepts several of the constituents of lignin and potentially participates in lignin functionalization.",,,,,,,GO:0046872; GO:0004503,GO:0004503; GO:0005507,GO:0004503,GO:0004503; GO:0005507,GO:0004497; GO:0005507,GO:0004503,0.8854,0.6939,0.8854,0.7178,0.6939,5,0.7753,0.2587,no
CGLR2_STYPI,A0A2B4RNI3,ESM2Text,Eukaryota,688,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Involved in regulation of lipid metabolism. Has a role in the processing of alpha-4:beta-D-glucan and alpha-6:beta-1,4-glucan.",No,No,No,No,No,not-Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0003725,GO:0003725,GO:0003725,GO:0003725,GO:0003725,0.1694,0.1694,0.1694,0.1694,0.1694,5,0.1694,0.5872,yes
CGLR2_STYPI,A0A2B4RNI3,Prot2Text,Eukaryota,688,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",Probable nucleosome-associated factor (Probable). May be involved in cell proliferation and cell cycle regulation.,Vague,No,No,No,No,not-Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0016779,,GO:0016779,GO:0016779,GO:0016779,0.3478,,0.3478,0.3478,0.3478,4,0.3478,0.5872,yes
CGLR2_STYPI,A0A2B4RNI3,ProtT3,Eukaryota,688,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity . Catalyzes the formation of 2',3'-cGAMP from ATP and GTP, but not from UTP or GTP . 2',3'-cGAMP is a second messenger that acts as a ligand for cGAS",Yes,Yes,Yes,Yes,Yes,Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0016779,GO:0061501,GO:0061501,GO:0016779,GO:0061501; GO:0005524; GO:0005525,0.3478,0.4353,0.4353,0.3478,0.8984,5,0.4929,0.5872,yes
CGLR2_STYPI,A0A2B4RNI3,ProtTale,Eukaryota,688,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Putative nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds 2',3'-cGAMP to inhibit its activity as a signaling molecule.",Yes,Maybe,Yes,Maybe,Yes,Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0016779,GO:0016779,GO:0016779,GO:0016779; GO:0005524; GO:0005525,GO:0016779,0.3478,0.3478,0.3478,0.8281,0.3478,5,0.4439,0.5872,yes
CGLR2_STYPI,A0A2B4RNI3,Protein2Text,Eukaryota,688,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","This protein is a guanylate-binding protein, which means it has a molecular function of binding to guanosine nucleotides.",No,No,No,No,No,not-Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.1786,0.1786,0.1786,0.1786,0.1786,5,0.1786,0.5872,yes
CGLR2_STYPI,A0A2B4RNI3,Reference,Eukaryota,688,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",,,,,,,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0061501,GO:0016779,GO:0016779,GO:0016779,GO:0061501,0.4353,0.3478,0.3478,0.3478,0.4353,5,0.3828,0.5872,yes
CGLR1_STYPI,A0A2B4RP11,ESM2Text,Eukaryota,376,"Nucleotidyltransferase that catalyzes the formation of cyclic UMP-AMP (3',3'-cUAMP) from ATP and UTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 3',3'-cUAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Does not mediate 3'-5'-exonucleolytic activity, suggesting that it is not involved in rRNA maturation.",Vague,No,No,No,Vague,not-Yes,GO:0005524; GO:0003725; GO:0046872; GO:0016779,,,,,,,,,,,0,,0.6363,yes
CGLR1_STYPI,A0A2B4RP11,Prot2Text,Eukaryota,376,"Nucleotidyltransferase that catalyzes the formation of cyclic UMP-AMP (3',3'-cUAMP) from ATP and UTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 3',3'-cUAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",Mediates bacterial sensing of the presence of class I major histocompatibility complex (MHC) in the cytosol. May act as an adapter to catalyze the synthesis of C-terminal H-IIB (H2B) oligomers whose sumoylation down-regulates the translation of target mRNAs.,No,No,No,No,No,not-Yes,GO:0005524; GO:0003725; GO:0046872; GO:0016779,,,,,,,,,,,0,,0.6363,yes
CGLR1_STYPI,A0A2B4RP11,ProtT3,Eukaryota,376,"Nucleotidyltransferase that catalyzes the formation of cyclic UMP-AMP (3',3'-cUAMP) from ATP and UTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 3',3'-cUAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity (By similarity). 2',3'-cGAMP is a second messenger that is generated in response to infection and acts as a ligand for cGAS (By similarity). 2',3'-cGAMP binds to and activates cGAS (By similarity). Belongs to the guanylate cyclase-activating protein family",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0003725; GO:0046872; GO:0016779,GO:0016779,GO:0061501,GO:0061501,GO:0016779,GO:0061501; GO:0005524; GO:0005525,0.4579,0.3453,0.3453,0.4579,0.6692,5,0.4551,0.6363,yes
CGLR1_STYPI,A0A2B4RP11,ProtTale,Eukaryota,376,"Nucleotidyltransferase that catalyzes the formation of cyclic UMP-AMP (3',3'-cUAMP) from ATP and UTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 3',3'-cUAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Synthesizes 2',3'-cGAMP in a two-step reaction through production of the linear intermediate pppA(2'-5')pG. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0003725; GO:0046872; GO:0016779,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0005524; GO:0005525; GO:0003725,GO:0016779,0.7296,0.7296,0.7296,0.8793,0.4579,5,0.7052,0.6363,yes
CGLR1_STYPI,A0A2B4RP11,Protein2Text,Eukaryota,376,"Nucleotidyltransferase that catalyzes the formation of cyclic UMP-AMP (3',3'-cUAMP) from ATP and UTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 3',3'-cUAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","The molecular function of this protein is an enzyme, specifically a guanylate-binding protein.",No,No,Vague,Vague,No,not-Yes,GO:0005524; GO:0003725; GO:0046872; GO:0016779,GO:0005525,GO:0005525,GO:0003924,GO:0003924,GO:0005525,0.3971,0.3971,0.1133,0.1133,0.3971,5,0.2836,0.6363,yes
CGLR1_STYPI,A0A2B4RP11,Reference,Eukaryota,376,"Nucleotidyltransferase that catalyzes the formation of cyclic UMP-AMP (3',3'-cUAMP) from ATP and UTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 3',3'-cUAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic UMP-AMP (3',3'-cUAMP) from ATP and UTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 3',3'-cUAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",,,,,,,GO:0005524; GO:0003725; GO:0046872; GO:0016779,GO:0061501; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,0.6476,0.7296,0.7296,0.7296,0.7296,5,0.7132,0.6363,yes
CPSA_ASPC2,A0A2I1CSH4,ESM2Text,Eukaryota,1043,"Non-canonical nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of campesine G, a dimeric indole piperazine alkaloid that shows good insecticidal activity Galleria mellonella. CpsA catalyzes the first steps of the pathway by producing L-tryptophanal and L-valinal from their respective amino-acids. These products condensate spontaneously to form trypyl-valyl pyrazine also known as didehydrocampesine A. The NmrA-like family domain-containing oxidoreductase cpsB is the next enzyme in cps pathway and reduces the unstable didehydrocampesine A to campesine A. The methyltransferase cpsF and the acetyltransferase cpsE both recognize N13 of piperazine ring to carry out methylation and acetylation of campesine A to produce campesine C and B, respectively. The cytochrome P450 monooxygenase cpsD then acts as a dimerase that catalyzes oxidative heterocoupling between campesine B and C to produce heterodimers with unexpected 6/5/6/6/6/6/5/6 eight-ring scaffold called campesine D. Finally,the cytochrome P450 monooxygenase cpsC is a regioselective dehydrogenase that catalyzes dehydrogenation reaction towards C2-N1 to produce campesine G.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016491,,GO:0016874,GO:0003824,GO:0016874,GO:0016874; GO:0005524,,0.5902,0.7642,0.5902,0.4225,4,0.5918,0.2264,no
CPSA_ASPC2,A0A2I1CSH4,Prot2Text,Eukaryota,1043,"Non-canonical nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of campesine G, a dimeric indole piperazine alkaloid that shows good insecticidal activity Galleria mellonella. CpsA catalyzes the first steps of the pathway by producing L-tryptophanal and L-valinal from their respective amino-acids. These products condensate spontaneously to form trypyl-valyl pyrazine also known as didehydrocampesine A. The NmrA-like family domain-containing oxidoreductase cpsB is the next enzyme in cps pathway and reduces the unstable didehydrocampesine A to campesine A. The methyltransferase cpsF and the acetyltransferase cpsE both recognize N13 of piperazine ring to carry out methylation and acetylation of campesine A to produce campesine C and B, respectively. The cytochrome P450 monooxygenase cpsD then acts as a dimerase that catalyzes oxidative heterocoupling between campesine B and C to produce heterodimers with unexpected 6/5/6/6/6/6/5/6 eight-ring scaffold called campesine D. Finally,the cytochrome P450 monooxygenase cpsC is a regioselective dehydrogenase that catalyzes dehydrogenation reaction towards C2-N1 to produce campesine G.","Non-canonical nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the host-selective toxins (HSTs) AAL-toxins, sphinganine-analog mycotoxins responsible for Alternaria stem canker on tomato by the tomato pathotype. The biosynthesis starts with the polyketide synthase ALT1-catalyzed C-16 carbon chain assembly from one starter acetyl-CoA unit with malonyl-CoA extender units. ALT1 also selectively transfers methyl groups at the first and the third cycle of chain elongation for AAL toxin. The C-16 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of glycin by decarboxylation, on the carbonyl carbon of polyketide acyl chain (Probable). This step is probably catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase ALT4 (Probable). The respective functions of the other enzymes encoded by the cluster have still to be elucidated (Probable). The sphingosine N",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016491,,,GO:0016874,,GO:0016874,,,0.5902,,0.5902,2,0.5902,0.2264,no
CPSA_ASPC2,A0A2I1CSH4,ProtT3,Eukaryota,1043,"Non-canonical nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of campesine G, a dimeric indole piperazine alkaloid that shows good insecticidal activity Galleria mellonella. CpsA catalyzes the first steps of the pathway by producing L-tryptophanal and L-valinal from their respective amino-acids. These products condensate spontaneously to form trypyl-valyl pyrazine also known as didehydrocampesine A. The NmrA-like family domain-containing oxidoreductase cpsB is the next enzyme in cps pathway and reduces the unstable didehydrocampesine A to campesine A. The methyltransferase cpsF and the acetyltransferase cpsE both recognize N13 of piperazine ring to carry out methylation and acetylation of campesine A to produce campesine C and B, respectively. The cytochrome P450 monooxygenase cpsD then acts as a dimerase that catalyzes oxidative heterocoupling between campesine B and C to produce heterodimers with unexpected 6/5/6/6/6/6/5/6 eight-ring scaffold called campesine D. Finally,the cytochrome P450 monooxygenase cpsC is a regioselective dehydrogenase that catalyzes dehydrogenation reaction towards C2-N1 to produce campesine G.",Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranyl,Maybe,No,Yes,No,Maybe,not-Yes,GO:0016491,GO:0016874,GO:0016874,GO:0016874,GO:0016874,GO:0016874; GO:0005524,0.5902,0.5902,0.5902,0.5902,0.4225,5,0.5567,0.2264,no
CPSA_ASPC2,A0A2I1CSH4,ProtTale,Eukaryota,1043,"Non-canonical nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of campesine G, a dimeric indole piperazine alkaloid that shows good insecticidal activity Galleria mellonella. CpsA catalyzes the first steps of the pathway by producing L-tryptophanal and L-valinal from their respective amino-acids. These products condensate spontaneously to form trypyl-valyl pyrazine also known as didehydrocampesine A. The NmrA-like family domain-containing oxidoreductase cpsB is the next enzyme in cps pathway and reduces the unstable didehydrocampesine A to campesine A. The methyltransferase cpsF and the acetyltransferase cpsE both recognize N13 of piperazine ring to carry out methylation and acetylation of campesine A to produce campesine C and B, respectively. The cytochrome P450 monooxygenase cpsD then acts as a dimerase that catalyzes oxidative heterocoupling between campesine B and C to produce heterodimers with unexpected 6/5/6/6/6/6/5/6 eight-ring scaffold called campesine D. Finally,the cytochrome P450 monooxygenase cpsC is a regioselective dehydrogenase that catalyzes dehydrogenation reaction towards C2-N1 to produce campesine G.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties. L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism. The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016491,GO:0016874,GO:0016874,GO:0016874,GO:0016874,,0.5902,0.5902,0.5902,0.5902,,4,0.5902,0.2264,no
CPSA_ASPC2,A0A2I1CSH4,Protein2Text,Eukaryota,1043,"Non-canonical nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of campesine G, a dimeric indole piperazine alkaloid that shows good insecticidal activity Galleria mellonella. CpsA catalyzes the first steps of the pathway by producing L-tryptophanal and L-valinal from their respective amino-acids. These products condensate spontaneously to form trypyl-valyl pyrazine also known as didehydrocampesine A. The NmrA-like family domain-containing oxidoreductase cpsB is the next enzyme in cps pathway and reduces the unstable didehydrocampesine A to campesine A. The methyltransferase cpsF and the acetyltransferase cpsE both recognize N13 of piperazine ring to carry out methylation and acetylation of campesine A to produce campesine C and B, respectively. The cytochrome P450 monooxygenase cpsD then acts as a dimerase that catalyzes oxidative heterocoupling between campesine B and C to produce heterodimers with unexpected 6/5/6/6/6/6/5/6 eight-ring scaffold called campesine D. Finally,the cytochrome P450 monooxygenase cpsC is a regioselective dehydrogenase that catalyzes dehydrogenation reaction towards C2-N1 to produce campesine G.","This protein is involved in the synthesis of prostaglandins, which are a group of lipid compounds that have hormone-like effects in the body. It is a key enzyme in the prostaglandin synthesis pathway, catalyzing the transfer of an acyl group from a fatty acid to a specific position on a prostaglandin precursor molecule. This reaction is essential for the production of various prostaglandins, which play important roles in various physiological and pathological processes, including inflammation, pain, and immune responses.

In more detail, the molecular function of this protein is to catalyze the transfer of an acyl group from a fatty acid to the hydroxyl group of a prostaglandin precursor molecule, such as arachidonic acid, to produce a prostaglandin molecule. This reaction is an important step in the synthesis of various prostaglandins, including prostaglandin E2 (PGE2), prostaglandin I2 (PGI2), and prostaglandin F2alpha (PGF2alpha).

The molecular function of this protein can be summarized as follows:

* Catalyzes the transfer of an acyl group from a fatty acid to a prostaglandin precursor molecule
* Involved in the synthesis of various prostaglandins, including PGE2, PGI2, and PGF2alpha
* Essential for the production of prostaglandins, which play important roles in various physiological and pathological processes
* Plays a key role in the regulation of inflammation, pain, and immune responses.",No,No,No,No,No,not-Yes,GO:0016491,,,,,,,,,,,0,,0.2264,no
CPSA_ASPC2,A0A2I1CSH4,Reference,Eukaryota,1043,"Non-canonical nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of campesine G, a dimeric indole piperazine alkaloid that shows good insecticidal activity Galleria mellonella. CpsA catalyzes the first steps of the pathway by producing L-tryptophanal and L-valinal from their respective amino-acids. These products condensate spontaneously to form trypyl-valyl pyrazine also known as didehydrocampesine A. The NmrA-like family domain-containing oxidoreductase cpsB is the next enzyme in cps pathway and reduces the unstable didehydrocampesine A to campesine A. The methyltransferase cpsF and the acetyltransferase cpsE both recognize N13 of piperazine ring to carry out methylation and acetylation of campesine A to produce campesine C and B, respectively. The cytochrome P450 monooxygenase cpsD then acts as a dimerase that catalyzes oxidative heterocoupling between campesine B and C to produce heterodimers with unexpected 6/5/6/6/6/6/5/6 eight-ring scaffold called campesine D. Finally,the cytochrome P450 monooxygenase cpsC is a regioselective dehydrogenase that catalyzes dehydrogenation reaction towards C2-N1 to produce campesine G.","Non-canonical nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of campesine G, a dimeric indole piperazine alkaloid that shows good insecticidal activity Galleria mellonella. CpsA catalyzes the first steps of the pathway by producing L-tryptophanal and L-valinal from their respective amino-acids. These products condensate spontaneously to form trypyl-valyl pyrazine also known as didehydrocampesine A. The NmrA-like family domain-containing oxidoreductase cpsB is the next enzyme in cps pathway and reduces the unstable didehydrocampesine A to campesine A. The methyltransferase cpsF and the acetyltransferase cpsE both recognize N13 of piperazine ring to carry out methylation and acetylation of campesine A to produce campesine C and B, respectively. The cytochrome P450 monooxygenase cpsD then acts as a dimerase that catalyzes oxidative heterocoupling between campesine B and C to produce heterodimers with unexpected 6/5/6/6/6/6/5/6 eight-ring scaffold called campesine D. Finally,the cytochrome P450 monooxygenase cpsC is a regioselective dehydrogenase that catalyzes dehydrogenation reaction towards C2-N1 to produce campesine G.",,,,,,,GO:0016491,GO:0031177; GO:0016874,GO:0008927,GO:0016874; GO:0016491,GO:0016874,,0.4358,0.3552,0.8634,0.5902,,4,0.5612,0.2264,no
CPSF_ASPC2,A0A2I1CSH5,ESM2Text,Eukaryota,283,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of campesine G, a dimeric indole piperazine alkaloid that shows good insecticidal activity Galleria mellonella. Within the pathway, cpsF methylates campesine A at N13 of piperazine ring to produce campesine B. The non-canonical non- ribosomal peptide synthetase cpsA catalyzes the first steps of the pathway by producing L-tryptophanal and L-valinal from their respective amino-acids. These products condensate spontaneously to form trypyl- valyl pyrazine also known as didehydrocampesine A. The NmrA-like family domain-containing oxidoreductase cpsB is the next enzyme in cps pathway and reduces the unstable didehydrocampesine A to campesine A. The methyltransferase cpsF and the acetyltransferase cpsE both recognize N13 of piperazine ring to carry out methylation and acetylation of campesine A to produce campesine C and B, respectively. The cytochrome P450 monooxygenase cpsD then acts as a dimerase that catalyzes oxidative heterocoupling between campesine B and C to produce heterodimers with unexpected 6/5/6/6/6/6/5/6 eight-ring scaffold called campesine D. Finally,the cytochrome P450 monooxygenase cpsC is a regioselective dehydrogenase that catalyzes dehydrogenation reaction towards C2-N1 to produce campesine G.",Methyltransferase; part of the gene cluster that mediates the biosynthesis of the phytotoxin stemphyloxin II. The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase sthA. Nicotinyl-CoA is then a substrate of the FAD-dependent monooxygenase sthM for hydroxylation at the C-2 position. The role of sthC as an accessory FAD-dependent monooxygenase is then complete with the formation of alpha-pyran-6'''-phosphate (PpP6). The rate-limiting step of the prenylation (prenylation) as well as the oxydation (a tetramic acid to produce the CoA starter unit) is performed by the O-methyltransferase sthI. SthI then methylates the C-2 position of the dipeptide to produce prepiperazine. Prepiperazine is then converted to the phytotoxin active intermediate phytotoxin III via a C-3 methylation. The glutathione S-transferase sth,Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008171,GO:0008168,GO:0008168,1.0,1.0,0.8582,1.0,1.0,5,0.9716,0.3872,no
CPSF_ASPC2,A0A2I1CSH5,Prot2Text,Eukaryota,283,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of campesine G, a dimeric indole piperazine alkaloid that shows good insecticidal activity Galleria mellonella. Within the pathway, cpsF methylates campesine A at N13 of piperazine ring to produce campesine B. The non-canonical non- ribosomal peptide synthetase cpsA catalyzes the first steps of the pathway by producing L-tryptophanal and L-valinal from their respective amino-acids. These products condensate spontaneously to form trypyl- valyl pyrazine also known as didehydrocampesine A. The NmrA-like family domain-containing oxidoreductase cpsB is the next enzyme in cps pathway and reduces the unstable didehydrocampesine A to campesine A. The methyltransferase cpsF and the acetyltransferase cpsE both recognize N13 of piperazine ring to carry out methylation and acetylation of campesine A to produce campesine C and B, respectively. The cytochrome P450 monooxygenase cpsD then acts as a dimerase that catalyzes oxidative heterocoupling between campesine B and C to produce heterodimers with unexpected 6/5/6/6/6/6/5/6 eight-ring scaffold called campesine D. Finally,the cytochrome P450 monooxygenase cpsC is a regioselective dehydrogenase that catalyzes dehydrogenation reaction towards C2-N1 to produce campesine G.","Methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin citrinin, a hepato-nephrotoxic compound to humans due to inhibition of respiration complex III (Ref.1, PubMed:26209694). The first step in the pathway is performed by the citrinin synthase (CTS) ccsA that produces citrinin from acetyl-CoA, leading to the formation of 2-methyl-6-(2-oxopropyl)benzaldehyde (MeB) (Ref.1). CcsA also catalyzes the second step, the conversion of 2-methyl-6-(2-oxopropyl)benzaldehyde (MeB) to yield citrinin (Ref.1). The cytochrome P450 monooxygenase ccsC catalyzes the hydroxylation at C-2 of citrinin to yield citrinin epoxide (Ref.1). Citrinin Eoxide is subsequently converted to ferulic acid, which is further oxidized to produce citrinin B (Ref.1). The oxidoreductases ccsD and ccsE further convert ferulic acid to sinapic acid, which is",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3872,no
CPSF_ASPC2,A0A2I1CSH5,ProtT3,Eukaryota,283,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of campesine G, a dimeric indole piperazine alkaloid that shows good insecticidal activity Galleria mellonella. Within the pathway, cpsF methylates campesine A at N13 of piperazine ring to produce campesine B. The non-canonical non- ribosomal peptide synthetase cpsA catalyzes the first steps of the pathway by producing L-tryptophanal and L-valinal from their respective amino-acids. These products condensate spontaneously to form trypyl- valyl pyrazine also known as didehydrocampesine A. The NmrA-like family domain-containing oxidoreductase cpsB is the next enzyme in cps pathway and reduces the unstable didehydrocampesine A to campesine A. The methyltransferase cpsF and the acetyltransferase cpsE both recognize N13 of piperazine ring to carry out methylation and acetylation of campesine A to produce campesine C and B, respectively. The cytochrome P450 monooxygenase cpsD then acts as a dimerase that catalyzes oxidative heterocoupling between campesine B and C to produce heterodimers with unexpected 6/5/6/6/6/6/5/6 eight-ring scaffold called campesine D. Finally,the cytochrome P450 monooxygenase cpsC is a regioselective dehydrogenase that catalyzes dehydrogenation reaction towards C2-N1 to produce campesine G.","Methyltransferase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3872,no
CPSF_ASPC2,A0A2I1CSH5,ProtTale,Eukaryota,283,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of campesine G, a dimeric indole piperazine alkaloid that shows good insecticidal activity Galleria mellonella. Within the pathway, cpsF methylates campesine A at N13 of piperazine ring to produce campesine B. The non-canonical non- ribosomal peptide synthetase cpsA catalyzes the first steps of the pathway by producing L-tryptophanal and L-valinal from their respective amino-acids. These products condensate spontaneously to form trypyl- valyl pyrazine also known as didehydrocampesine A. The NmrA-like family domain-containing oxidoreductase cpsB is the next enzyme in cps pathway and reduces the unstable didehydrocampesine A to campesine A. The methyltransferase cpsF and the acetyltransferase cpsE both recognize N13 of piperazine ring to carry out methylation and acetylation of campesine A to produce campesine C and B, respectively. The cytochrome P450 monooxygenase cpsD then acts as a dimerase that catalyzes oxidative heterocoupling between campesine B and C to produce heterodimers with unexpected 6/5/6/6/6/6/5/6 eight-ring scaffold called campesine D. Finally,the cytochrome P450 monooxygenase cpsC is a regioselective dehydrogenase that catalyzes dehydrogenation reaction towards C2-N1 to produce campesine G.","Methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The roles of the other FUS members are yet unknown. The fusarin C synthetase FUS1 is responsible for the condensation of one acetyl- coenzyme A (CoA) unit with six malonyl-CoA units and the amidation of the C-6 hydroxyl group.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3872,no
CPSF_ASPC2,A0A2I1CSH5,Protein2Text,Eukaryota,283,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of campesine G, a dimeric indole piperazine alkaloid that shows good insecticidal activity Galleria mellonella. Within the pathway, cpsF methylates campesine A at N13 of piperazine ring to produce campesine B. The non-canonical non- ribosomal peptide synthetase cpsA catalyzes the first steps of the pathway by producing L-tryptophanal and L-valinal from their respective amino-acids. These products condensate spontaneously to form trypyl- valyl pyrazine also known as didehydrocampesine A. The NmrA-like family domain-containing oxidoreductase cpsB is the next enzyme in cps pathway and reduces the unstable didehydrocampesine A to campesine A. The methyltransferase cpsF and the acetyltransferase cpsE both recognize N13 of piperazine ring to carry out methylation and acetylation of campesine A to produce campesine C and B, respectively. The cytochrome P450 monooxygenase cpsD then acts as a dimerase that catalyzes oxidative heterocoupling between campesine B and C to produce heterodimers with unexpected 6/5/6/6/6/6/5/6 eight-ring scaffold called campesine D. Finally,the cytochrome P450 monooxygenase cpsC is a regioselective dehydrogenase that catalyzes dehydrogenation reaction towards C2-N1 to produce campesine G.","The molecular function of this protein is not explicitly stated in the provided text. However, based on the fact that it is referred to as a ""N-methyltransferase"" and is involved in the methylation of a molecule, it is likely that its molecular function is to catalyze the transfer of a methyl group from one molecule to another.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008170,1.0,1.0,1.0,1.0,0.8582,5,0.9716,0.3872,no
CPSF_ASPC2,A0A2I1CSH5,Reference,Eukaryota,283,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of campesine G, a dimeric indole piperazine alkaloid that shows good insecticidal activity Galleria mellonella. Within the pathway, cpsF methylates campesine A at N13 of piperazine ring to produce campesine B. The non-canonical non- ribosomal peptide synthetase cpsA catalyzes the first steps of the pathway by producing L-tryptophanal and L-valinal from their respective amino-acids. These products condensate spontaneously to form trypyl- valyl pyrazine also known as didehydrocampesine A. The NmrA-like family domain-containing oxidoreductase cpsB is the next enzyme in cps pathway and reduces the unstable didehydrocampesine A to campesine A. The methyltransferase cpsF and the acetyltransferase cpsE both recognize N13 of piperazine ring to carry out methylation and acetylation of campesine A to produce campesine C and B, respectively. The cytochrome P450 monooxygenase cpsD then acts as a dimerase that catalyzes oxidative heterocoupling between campesine B and C to produce heterodimers with unexpected 6/5/6/6/6/6/5/6 eight-ring scaffold called campesine D. Finally,the cytochrome P450 monooxygenase cpsC is a regioselective dehydrogenase that catalyzes dehydrogenation reaction towards C2-N1 to produce campesine G.","Methyltransferase; part of the gene cluster that mediates the biosynthesis of campesine G, a dimeric indole piperazine alkaloid that shows good insecticidal activity Galleria mellonella. Within the pathway, cpsF methylates campesine A at N13 of piperazine ring to produce campesine B. The non-canonical non- ribosomal peptide synthetase cpsA catalyzes the first steps of the pathway by producing L-tryptophanal and L-valinal from their respective amino-acids. These products condensate spontaneously to form trypyl- valyl pyrazine also known as didehydrocampesine A. The NmrA-like family domain-containing oxidoreductase cpsB is the next enzyme in cps pathway and reduces the unstable didehydrocampesine A to campesine A. The methyltransferase cpsF and the acetyltransferase cpsE both recognize N13 of piperazine ring to carry out methylation and acetylation of campesine A to produce campesine C and B, respectively. The cytochrome P450 monooxygenase cpsD then acts as a dimerase that catalyzes oxidative heterocoupling between campesine B and C to produce heterodimers with unexpected 6/5/6/6/6/6/5/6 eight-ring scaffold called campesine D. Finally,the cytochrome P450 monooxygenase cpsC is a regioselective dehydrogenase that catalyzes dehydrogenation reaction towards C2-N1 to produce campesine G.",,,,,,,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3872,no
CPSE_ASPC2,A0A2I1CSH9,ESM2Text,Eukaryota,496,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of campesine G, a dimeric indole piperazine alkaloid that shows good insecticidal activity Galleria mellonella. Within the pathway, cpsE acetylates N13 of campesine A to produce campesine C. CpsE produces an inseparable mixture of two acyl-atropisomers due to the spontaneous rotation of an acyl group at N13 of piperazine ring. The non-canonical non- ribosomal peptide synthetase cpsA catalyzes the first steps of the pathway by producing L-tryptophanal and L-valinal from their respective amino-acids. These products condensate spontaneously to form trypyl- valyl pyrazine also known as didehydrocampesine A. The NmrA-like family domain-containing oxidoreductase cpsB is the next enzyme in cps pathway and reduces the unstable didehydrocampesine A to campesine A. The methyltransferase cpsF and the acetyltransferase cpsE both recognize N13 of piperazine ring to carry out methylation and acetylation of campesine A to produce campesine C and B, respectively. The cytochrome P450 monooxygenase cpsD then acts as a dimerase that catalyzes oxidative heterocoupling between campesine B and C to produce heterodimers with unexpected 6/5/6/6/6/6/5/6 eight-ring scaffold called campesine D. Finally,the cytochrome P450 monooxygenase cpsC is a regioselective dehydrogenase that catalyzes dehydrogenation reaction towards C2-N1 to produce campesine G.","FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome monooxygenase P450 claM then catalyzes the dimerization of nataloe-emodin to cladofulvin.",No,No,No,No,No,not-Yes,GO:0016746,GO:0004497; GO:0071949,GO:0004497,GO:0016491,GO:0004497; GO:0071949,GO:0004497; GO:0071949,0.2923,0.3902,0.4807,0.2923,0.2923,5,0.3496,0.2571,no
CPSE_ASPC2,A0A2I1CSH9,Prot2Text,Eukaryota,496,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of campesine G, a dimeric indole piperazine alkaloid that shows good insecticidal activity Galleria mellonella. Within the pathway, cpsE acetylates N13 of campesine A to produce campesine C. CpsE produces an inseparable mixture of two acyl-atropisomers due to the spontaneous rotation of an acyl group at N13 of piperazine ring. The non-canonical non- ribosomal peptide synthetase cpsA catalyzes the first steps of the pathway by producing L-tryptophanal and L-valinal from their respective amino-acids. These products condensate spontaneously to form trypyl- valyl pyrazine also known as didehydrocampesine A. The NmrA-like family domain-containing oxidoreductase cpsB is the next enzyme in cps pathway and reduces the unstable didehydrocampesine A to campesine A. The methyltransferase cpsF and the acetyltransferase cpsE both recognize N13 of piperazine ring to carry out methylation and acetylation of campesine A to produce campesine C and B, respectively. The cytochrome P450 monooxygenase cpsD then acts as a dimerase that catalyzes oxidative heterocoupling between campesine B and C to produce heterodimers with unexpected 6/5/6/6/6/6/5/6 eight-ring scaffold called campesine D. Finally,the cytochrome P450 monooxygenase cpsC is a regioselective dehydrogenase that catalyzes dehydrogenation reaction towards C2-N1 to produce campesine G.","O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential tricycl",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016746,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.729,0.729,0.729,0.729,0.729,5,0.729,0.2571,no
CPSE_ASPC2,A0A2I1CSH9,ProtT3,Eukaryota,496,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of campesine G, a dimeric indole piperazine alkaloid that shows good insecticidal activity Galleria mellonella. Within the pathway, cpsE acetylates N13 of campesine A to produce campesine C. CpsE produces an inseparable mixture of two acyl-atropisomers due to the spontaneous rotation of an acyl group at N13 of piperazine ring. The non-canonical non- ribosomal peptide synthetase cpsA catalyzes the first steps of the pathway by producing L-tryptophanal and L-valinal from their respective amino-acids. These products condensate spontaneously to form trypyl- valyl pyrazine also known as didehydrocampesine A. The NmrA-like family domain-containing oxidoreductase cpsB is the next enzyme in cps pathway and reduces the unstable didehydrocampesine A to campesine A. The methyltransferase cpsF and the acetyltransferase cpsE both recognize N13 of piperazine ring to carry out methylation and acetylation of campesine A to produce campesine C and B, respectively. The cytochrome P450 monooxygenase cpsD then acts as a dimerase that catalyzes oxidative heterocoupling between campesine B and C to produce heterodimers with unexpected 6/5/6/6/6/6/5/6 eight-ring scaffold called campesine D. Finally,the cytochrome P450 monooxygenase cpsC is a regioselective dehydrogenase that catalyzes dehydrogenation reaction towards C2-N1 to produce campesine G.","O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties . L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L- homoserine by cluster enzymes aspartate kinase FUB5 and homoserine O- acetyltransferase FUB6, as well as enzymes of the",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016746,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.729,0.729,0.729,0.729,0.729,5,0.729,0.2571,no
CPSE_ASPC2,A0A2I1CSH9,ProtTale,Eukaryota,496,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of campesine G, a dimeric indole piperazine alkaloid that shows good insecticidal activity Galleria mellonella. Within the pathway, cpsE acetylates N13 of campesine A to produce campesine C. CpsE produces an inseparable mixture of two acyl-atropisomers due to the spontaneous rotation of an acyl group at N13 of piperazine ring. The non-canonical non- ribosomal peptide synthetase cpsA catalyzes the first steps of the pathway by producing L-tryptophanal and L-valinal from their respective amino-acids. These products condensate spontaneously to form trypyl- valyl pyrazine also known as didehydrocampesine A. The NmrA-like family domain-containing oxidoreductase cpsB is the next enzyme in cps pathway and reduces the unstable didehydrocampesine A to campesine A. The methyltransferase cpsF and the acetyltransferase cpsE both recognize N13 of piperazine ring to carry out methylation and acetylation of campesine A to produce campesine C and B, respectively. The cytochrome P450 monooxygenase cpsD then acts as a dimerase that catalyzes oxidative heterocoupling between campesine B and C to produce heterodimers with unexpected 6/5/6/6/6/6/5/6 eight-ring scaffold called campesine D. Finally,the cytochrome P450 monooxygenase cpsC is a regioselective dehydrogenase that catalyzes dehydrogenation reaction towards C2-N1 to produce campesine G.","Acyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016746,GO:0016746,GO:0016747,GO:0016747,GO:0016747,GO:0016747,1.0,0.8416,0.8416,0.8416,0.8416,5,0.8733,0.2571,no
CPSE_ASPC2,A0A2I1CSH9,Protein2Text,Eukaryota,496,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of campesine G, a dimeric indole piperazine alkaloid that shows good insecticidal activity Galleria mellonella. Within the pathway, cpsE acetylates N13 of campesine A to produce campesine C. CpsE produces an inseparable mixture of two acyl-atropisomers due to the spontaneous rotation of an acyl group at N13 of piperazine ring. The non-canonical non- ribosomal peptide synthetase cpsA catalyzes the first steps of the pathway by producing L-tryptophanal and L-valinal from their respective amino-acids. These products condensate spontaneously to form trypyl- valyl pyrazine also known as didehydrocampesine A. The NmrA-like family domain-containing oxidoreductase cpsB is the next enzyme in cps pathway and reduces the unstable didehydrocampesine A to campesine A. The methyltransferase cpsF and the acetyltransferase cpsE both recognize N13 of piperazine ring to carry out methylation and acetylation of campesine A to produce campesine C and B, respectively. The cytochrome P450 monooxygenase cpsD then acts as a dimerase that catalyzes oxidative heterocoupling between campesine B and C to produce heterodimers with unexpected 6/5/6/6/6/6/5/6 eight-ring scaffold called campesine D. Finally,the cytochrome P450 monooxygenase cpsC is a regioselective dehydrogenase that catalyzes dehydrogenation reaction towards C2-N1 to produce campesine G.","This protein is involved in the molecular function of being a hydrolase, specifically a protein hydrolase.

In more detail, it is a part of a larger pathway that involves the degradation of proteins. This protein is likely to be involved in the breakdown of proteins into smaller peptides and amino acids, which is an important process for the cell's metabolic needs.

The specific molecular function of this protein is likely to be the hydrolysis of peptide bonds, which is a key step in protein degradation. This protein may use a hydrolase enzyme to break down proteins into smaller peptides, which can then be further degraded into amino acids that can be used by the cell for various purposes.

It's worth noting that the exact molecular function of this protein may depend on the specific organism or context in which it is found, and more research would be needed to fully understand its role in protein degradation.",No,No,No,No,No,not-Yes,GO:0016746,GO:0008233,GO:0008233,GO:0016787,GO:0008233,GO:0008233,0.3437,0.3437,0.4807,0.3437,0.3437,5,0.3711,0.2571,no
CPSE_ASPC2,A0A2I1CSH9,Reference,Eukaryota,496,"O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of campesine G, a dimeric indole piperazine alkaloid that shows good insecticidal activity Galleria mellonella. Within the pathway, cpsE acetylates N13 of campesine A to produce campesine C. CpsE produces an inseparable mixture of two acyl-atropisomers due to the spontaneous rotation of an acyl group at N13 of piperazine ring. The non-canonical non- ribosomal peptide synthetase cpsA catalyzes the first steps of the pathway by producing L-tryptophanal and L-valinal from their respective amino-acids. These products condensate spontaneously to form trypyl- valyl pyrazine also known as didehydrocampesine A. The NmrA-like family domain-containing oxidoreductase cpsB is the next enzyme in cps pathway and reduces the unstable didehydrocampesine A to campesine A. The methyltransferase cpsF and the acetyltransferase cpsE both recognize N13 of piperazine ring to carry out methylation and acetylation of campesine A to produce campesine C and B, respectively. The cytochrome P450 monooxygenase cpsD then acts as a dimerase that catalyzes oxidative heterocoupling between campesine B and C to produce heterodimers with unexpected 6/5/6/6/6/6/5/6 eight-ring scaffold called campesine D. Finally,the cytochrome P450 monooxygenase cpsC is a regioselective dehydrogenase that catalyzes dehydrogenation reaction towards C2-N1 to produce campesine G.","O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of campesine G, a dimeric indole piperazine alkaloid that shows good insecticidal activity Galleria mellonella. Within the pathway, cpsE acetylates N13 of campesine A to produce campesine C. CpsE produces an inseparable mixture of two acyl-atropisomers due to the spontaneous rotation of an acyl group at N13 of piperazine ring. The non-canonical non- ribosomal peptide synthetase cpsA catalyzes the first steps of the pathway by producing L-tryptophanal and L-valinal from their respective amino-acids. These products condensate spontaneously to form trypyl- valyl pyrazine also known as didehydrocampesine A. The NmrA-like family domain-containing oxidoreductase cpsB is the next enzyme in cps pathway and reduces the unstable didehydrocampesine A to campesine A. The methyltransferase cpsF and the acetyltransferase cpsE both recognize N13 of piperazine ring to carry out methylation and acetylation of campesine A to produce campesine C and B, respectively. The cytochrome P450 monooxygenase cpsD then acts as a dimerase that catalyzes oxidative heterocoupling between campesine B and C to produce heterodimers with unexpected 6/5/6/6/6/6/5/6 eight-ring scaffold called campesine D. Finally,the cytochrome P450 monooxygenase cpsC is a regioselective dehydrogenase that catalyzes dehydrogenation reaction towards C2-N1 to produce campesine G.",,,,,,,GO:0016746,GO:0016747,GO:0016747,GO:0016407,GO:0016407,GO:0016746,0.8416,0.8416,0.729,0.729,1.0,5,0.8282,0.2571,no
UNGA_ASPC2,A0A2I1D2N0,ESM2Text,Eukaryota,9518,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the unguisins, gamma-aminobutyric acid (GABA)-containing fungal cyclic heptapeptides with the amino acid sequence cyclo-(D-Ala1-D-Val2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6-GABA7) for unguisin H and cyclo-(D-Ala1-D-Ala2-L-Leu3-beta-MePhe4-D-Ala5-D- Trp6-GABA7) for unguisin I. UngA' is the main enzyme within the cluster which condenses the 7 residues using its respective 7 modules (Probable). The terminal condensation domain (Ct) is involved in cyclization with D-alanine and thereby releasing of unguisins H and I (Probable). The alanine racemase ungC' provides D-alanine, which is then accepted by the first adenylation domain of ungA', whereas the methyltransferase ungE' provides the (2R,3R)-beta-methylphenylalanine residue incorporated by the module 4 (Probable). Finally, the hydrolase ungD' catalyzes the hydrolysis between the D-tryptophan and GABA residues of unguisins H and I to produce the corresponding linear peptides (Probable).","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of aspirochlorine (or antibiotic A30641), an unusual halogenated spiro compound with distinctive antifungal properties due to selective inhibition of protein biosynthesis, and which is also active against bacteria, viruses, and murine tumor cells. The non-ribosomal peptide synthetase (NRPS) aclP is responsible the formation of the diketopiperazine (DKP) core from the condensation of 2 phenylalanine residues. One Phe residue is tailored into chlorotyrosine by hydroxylation and chlorination, whereas the second Phe undergoes an unprecedented C-C bond cleavage to be converted into glycine. After formation of the DKP, sulfur is incorporated into the DKP by conjugation with glutathione by aclG, followed by its stepwise degradation to the thiol by aclI, aclJ and aclK, and the dithiol oxidation by aclT. In addition, oxygenases (aclB, aclC, aclL and aclO) and O-methyltransferases (aclM and",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016853; GO:0016874; GO:1904091; GO:0031177,,GO:0016874,GO:0003824,GO:0016874,GO:0016874; GO:0005524,,0.6615,0.6424,0.6615,0.6496,4,0.6537,0.4441,no
UNGA_ASPC2,A0A2I1D2N0,Prot2Text,Eukaryota,9518,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the unguisins, gamma-aminobutyric acid (GABA)-containing fungal cyclic heptapeptides with the amino acid sequence cyclo-(D-Ala1-D-Val2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6-GABA7) for unguisin H and cyclo-(D-Ala1-D-Ala2-L-Leu3-beta-MePhe4-D-Ala5-D- Trp6-GABA7) for unguisin I. UngA' is the main enzyme within the cluster which condenses the 7 residues using its respective 7 modules (Probable). The terminal condensation domain (Ct) is involved in cyclization with D-alanine and thereby releasing of unguisins H and I (Probable). The alanine racemase ungC' provides D-alanine, which is then accepted by the first adenylation domain of ungA', whereas the methyltransferase ungE' provides the (2R,3R)-beta-methylphenylalanine residue incorporated by the module 4 (Probable). Finally, the hydrolase ungD' catalyzes the hydrolysis between the D-tryptophan and GABA residues of unguisins H and I to produce the corresponding linear peptides (Probable).","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of aspirochlorine (or antibiotic A30641), an unusual halogenated spiro compound with distinctive antifungal properties due to selective inhibition of protein biosynthesis, and which is also active against bacteria, viruses, and murine tumor cells. The non-ribosomal peptide synthetase (NRPS) aclP is responsible the formation of the diketopiperazine (DKP) core from the condensation of 2 phenylalanine residues. One Phe residue is tailored into chlorotyrosine by hydroxylation and chlorination, whereas the second Phe undergoes an unprecedented C-C bond cleavage to be converted into glycine. After formation of the DKP, sulfur is incorporated into the DKP by conjugation with glutathione by aclG, followed by its stepwise degradation to the thiol by aclI, aclJ and aclK, and the dithiol oxidation by aclT. In addition, oxygenases (aclB, aclC, aclL and aclO) and O-methyltransferases (aclM and",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016853; GO:0016874; GO:1904091; GO:0031177,,,GO:0016874,,GO:0016874,,,0.6615,,0.6615,2,0.6615,0.4441,no
UNGA_ASPC2,A0A2I1D2N0,ProtT3,Eukaryota,9518,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the unguisins, gamma-aminobutyric acid (GABA)-containing fungal cyclic heptapeptides with the amino acid sequence cyclo-(D-Ala1-D-Val2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6-GABA7) for unguisin H and cyclo-(D-Ala1-D-Ala2-L-Leu3-beta-MePhe4-D-Ala5-D- Trp6-GABA7) for unguisin I. UngA' is the main enzyme within the cluster which condenses the 7 residues using its respective 7 modules (Probable). The terminal condensation domain (Ct) is involved in cyclization with D-alanine and thereby releasing of unguisins H and I (Probable). The alanine racemase ungC' provides D-alanine, which is then accepted by the first adenylation domain of ungA', whereas the methyltransferase ungE' provides the (2R,3R)-beta-methylphenylalanine residue incorporated by the module 4 (Probable). Finally, the hydrolase ungD' catalyzes the hydrolysis between the D-tryptophan and GABA residues of unguisins H and I to produce the corresponding linear peptides (Probable).","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016853; GO:0016874; GO:1904091; GO:0031177,GO:0016874,GO:0016874,GO:0016874,GO:0016874,GO:0016874; GO:0005524,0.6615,0.6615,0.6615,0.6615,0.6496,5,0.6591,0.4441,no
UNGA_ASPC2,A0A2I1D2N0,ProtTale,Eukaryota,9518,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the unguisins, gamma-aminobutyric acid (GABA)-containing fungal cyclic heptapeptides with the amino acid sequence cyclo-(D-Ala1-D-Val2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6-GABA7) for unguisin H and cyclo-(D-Ala1-D-Ala2-L-Leu3-beta-MePhe4-D-Ala5-D- Trp6-GABA7) for unguisin I. UngA' is the main enzyme within the cluster which condenses the 7 residues using its respective 7 modules (Probable). The terminal condensation domain (Ct) is involved in cyclization with D-alanine and thereby releasing of unguisins H and I (Probable). The alanine racemase ungC' provides D-alanine, which is then accepted by the first adenylation domain of ungA', whereas the methyltransferase ungE' provides the (2R,3R)-beta-methylphenylalanine residue incorporated by the module 4 (Probable). Finally, the hydrolase ungD' catalyzes the hydrolysis between the D-tryptophan and GABA residues of unguisins H and I to produce the corresponding linear peptides (Probable).",Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template.,No,No,No,No,No,not-Yes,GO:0016853; GO:0016874; GO:1904091; GO:0031177,GO:0003723,GO:0003723,GO:0003723,GO:0003723,GO:0003723,0.2244,0.2244,0.2244,0.2244,0.2244,5,0.2244,0.4441,no
UNGA_ASPC2,A0A2I1D2N0,Protein2Text,Eukaryota,9518,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the unguisins, gamma-aminobutyric acid (GABA)-containing fungal cyclic heptapeptides with the amino acid sequence cyclo-(D-Ala1-D-Val2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6-GABA7) for unguisin H and cyclo-(D-Ala1-D-Ala2-L-Leu3-beta-MePhe4-D-Ala5-D- Trp6-GABA7) for unguisin I. UngA' is the main enzyme within the cluster which condenses the 7 residues using its respective 7 modules (Probable). The terminal condensation domain (Ct) is involved in cyclization with D-alanine and thereby releasing of unguisins H and I (Probable). The alanine racemase ungC' provides D-alanine, which is then accepted by the first adenylation domain of ungA', whereas the methyltransferase ungE' provides the (2R,3R)-beta-methylphenylalanine residue incorporated by the module 4 (Probable). Finally, the hydrolase ungD' catalyzes the hydrolysis between the D-tryptophan and GABA residues of unguisins H and I to produce the corresponding linear peptides (Probable).","This protein is a part of the capsid of a virus, specifically a norovirus, and is involved in the attachment of the virus to the host cell.",No,No,No,No,No,not-Yes,GO:0016853; GO:0016874; GO:1904091; GO:0031177,,,,,GO:0005198,,,,,0.3028,1,0.3028,0.4441,no
UNGA_ASPC2,A0A2I1D2N0,Reference,Eukaryota,9518,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the unguisins, gamma-aminobutyric acid (GABA)-containing fungal cyclic heptapeptides with the amino acid sequence cyclo-(D-Ala1-D-Val2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6-GABA7) for unguisin H and cyclo-(D-Ala1-D-Ala2-L-Leu3-beta-MePhe4-D-Ala5-D- Trp6-GABA7) for unguisin I. UngA' is the main enzyme within the cluster which condenses the 7 residues using its respective 7 modules (Probable). The terminal condensation domain (Ct) is involved in cyclization with D-alanine and thereby releasing of unguisins H and I (Probable). The alanine racemase ungC' provides D-alanine, which is then accepted by the first adenylation domain of ungA', whereas the methyltransferase ungE' provides the (2R,3R)-beta-methylphenylalanine residue incorporated by the module 4 (Probable). Finally, the hydrolase ungD' catalyzes the hydrolysis between the D-tryptophan and GABA residues of unguisins H and I to produce the corresponding linear peptides (Probable).","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the unguisins, gamma-aminobutyric acid (GABA)-containing fungal cyclic heptapeptides with the amino acid sequence cyclo-(D-Ala1-D-Val2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6-GABA7) for unguisin H and cyclo-(D-Ala1-D-Ala2-L-Leu3-beta-MePhe4-D-Ala5-D- Trp6-GABA7) for unguisin I. UngA' is the main enzyme within the cluster which condenses the 7 residues using its respective 7 modules (Probable). The terminal condensation domain (Ct) is involved in cyclization with D-alanine and thereby releasing of unguisins H and I (Probable). The alanine racemase ungC' provides D-alanine, which is then accepted by the first adenylation domain of ungA', whereas the methyltransferase ungE' provides the (2R,3R)-beta-methylphenylalanine residue incorporated by the module 4 (Probable). Finally, the hydrolase ungD' catalyzes the hydrolysis between the D-tryptophan and GABA residues of unguisins H and I to produce the corresponding linear peptides (Probable).",,,,,,,GO:0016853; GO:0016874; GO:1904091; GO:0031177,GO:0031177; GO:0016874,GO:0008927,GO:0016879,GO:0016874,,0.8634,0.3005,0.5395,0.6615,,4,0.5912,0.4441,no
ACDA_ASPCN,A0A2I2F272,ESM2Text,Eukaryota,405,"Indoleamine 2,3-dioxygenase; part of the gene cluster that mediates the biosynthesis of aspcandine, a pyrrolobenzazepine alkaloid. Initially, the indoleamine 2,3-dioxygenase acdA accepts L-tryptophan and performs the oxidative opening of the indole ring to yield N'-formyl-L-kynurenine, which undergoes the spontaneous deformylation reaction to provide L-kynurenine. The kynurenine 3-monooxygenase acdD then hydroxylates L-kynurenine to afford 3-hydroxy-L-kynurenine. 3-hydroxy-L-kynurenine is activated by the A domain of the NRPS-PKS acdB and subsequently loaded onto the enzyme. The KS domain conducts the decarboxylative condensation of the 3-hydroxy-L-kynurenyl and malonyl moieties, and subsequent nucleophilic attacks by the two amino groups would occur nonenzymatically at two distinct positions, achieving the chain release and the construction of the tricyclic system. Finally, a dehydration reaction completes the biosynthesis to yield aspcandine.","Plays a key role in L-lactate degradation and allows cells to grow with lactate as the sole carbon source. In absence of carbon monoxide (CO), binds tightly and specifically to the twin-arginine motif present in the luciferase gene promoter. Neither N-6-mercaptopropionate (6MBP) nor N-ethylmercaptooctanoate (NDMA) bind tightly to the luciferase gene promoter.",No,No,No,No,No,not-Yes,GO:0020037; GO:0033754; GO:0046872,,,,,,,,,,,0,,0.3154,no
ACDA_ASPCN,A0A2I2F272,Prot2Text,Eukaryota,405,"Indoleamine 2,3-dioxygenase; part of the gene cluster that mediates the biosynthesis of aspcandine, a pyrrolobenzazepine alkaloid. Initially, the indoleamine 2,3-dioxygenase acdA accepts L-tryptophan and performs the oxidative opening of the indole ring to yield N'-formyl-L-kynurenine, which undergoes the spontaneous deformylation reaction to provide L-kynurenine. The kynurenine 3-monooxygenase acdD then hydroxylates L-kynurenine to afford 3-hydroxy-L-kynurenine. 3-hydroxy-L-kynurenine is activated by the A domain of the NRPS-PKS acdB and subsequently loaded onto the enzyme. The KS domain conducts the decarboxylative condensation of the 3-hydroxy-L-kynurenyl and malonyl moieties, and subsequent nucleophilic attacks by the two amino groups would occur nonenzymatically at two distinct positions, achieving the chain release and the construction of the tricyclic system. Finally, a dehydration reaction completes the biosynthesis to yield aspcandine.","tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. The cytochrome P450 monooxygenase is responsible for the CCA terminus formation and thus regulates termination by the tRNA. Cytochrome P450 monooxygenase is also able to use GTP, ITP or UTP as a substrate.",No,No,No,No,No,not-Yes,GO:0020037; GO:0033754; GO:0046872,GO:0009022,GO:0009884,,GO:0009022,GO:0009022,0.1159,0.1231,,0.1159,0.1159,4,0.1177,0.3154,no
ACDA_ASPCN,A0A2I2F272,ProtT3,Eukaryota,405,"Indoleamine 2,3-dioxygenase; part of the gene cluster that mediates the biosynthesis of aspcandine, a pyrrolobenzazepine alkaloid. Initially, the indoleamine 2,3-dioxygenase acdA accepts L-tryptophan and performs the oxidative opening of the indole ring to yield N'-formyl-L-kynurenine, which undergoes the spontaneous deformylation reaction to provide L-kynurenine. The kynurenine 3-monooxygenase acdD then hydroxylates L-kynurenine to afford 3-hydroxy-L-kynurenine. 3-hydroxy-L-kynurenine is activated by the A domain of the NRPS-PKS acdB and subsequently loaded onto the enzyme. The KS domain conducts the decarboxylative condensation of the 3-hydroxy-L-kynurenyl and malonyl moieties, and subsequent nucleophilic attacks by the two amino groups would occur nonenzymatically at two distinct positions, achieving the chain release and the construction of the tricyclic system. Finally, a dehydration reaction completes the biosynthesis to yield aspcandine.","Belongs to the indoleamine 2,3-dioxygenase family",Vague,Vague,Yes,Vague,Vague,not-Yes,GO:0020037; GO:0033754; GO:0046872,GO:0033754,GO:0033754,GO:0033754,GO:0033754,GO:0033754,0.5493,0.5493,0.5493,0.5493,0.5493,5,0.5493,0.3154,no
ACDA_ASPCN,A0A2I2F272,ProtTale,Eukaryota,405,"Indoleamine 2,3-dioxygenase; part of the gene cluster that mediates the biosynthesis of aspcandine, a pyrrolobenzazepine alkaloid. Initially, the indoleamine 2,3-dioxygenase acdA accepts L-tryptophan and performs the oxidative opening of the indole ring to yield N'-formyl-L-kynurenine, which undergoes the spontaneous deformylation reaction to provide L-kynurenine. The kynurenine 3-monooxygenase acdD then hydroxylates L-kynurenine to afford 3-hydroxy-L-kynurenine. 3-hydroxy-L-kynurenine is activated by the A domain of the NRPS-PKS acdB and subsequently loaded onto the enzyme. The KS domain conducts the decarboxylative condensation of the 3-hydroxy-L-kynurenyl and malonyl moieties, and subsequent nucleophilic attacks by the two amino groups would occur nonenzymatically at two distinct positions, achieving the chain release and the construction of the tricyclic system. Finally, a dehydration reaction completes the biosynthesis to yield aspcandine.","Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (L-DOPA) to 3,4- dihydroxyphenylalanine 5-phosphate (L-DOPA5P).",No,No,No,No,No,not-Yes,GO:0020037; GO:0033754; GO:0046872,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0004058,0.1705,0.1705,0.1705,0.1705,0.1458,5,0.1656,0.3154,no
ACDA_ASPCN,A0A2I2F272,Protein2Text,Eukaryota,405,"Indoleamine 2,3-dioxygenase; part of the gene cluster that mediates the biosynthesis of aspcandine, a pyrrolobenzazepine alkaloid. Initially, the indoleamine 2,3-dioxygenase acdA accepts L-tryptophan and performs the oxidative opening of the indole ring to yield N'-formyl-L-kynurenine, which undergoes the spontaneous deformylation reaction to provide L-kynurenine. The kynurenine 3-monooxygenase acdD then hydroxylates L-kynurenine to afford 3-hydroxy-L-kynurenine. 3-hydroxy-L-kynurenine is activated by the A domain of the NRPS-PKS acdB and subsequently loaded onto the enzyme. The KS domain conducts the decarboxylative condensation of the 3-hydroxy-L-kynurenyl and malonyl moieties, and subsequent nucleophilic attacks by the two amino groups would occur nonenzymatically at two distinct positions, achieving the chain release and the construction of the tricyclic system. Finally, a dehydration reaction completes the biosynthesis to yield aspcandine.","This protein is involved in the molecular function of being a part of the aromatic L-amino acid decarboxylase (AADC) family, which is a type of enzyme that catalyzes the decarboxylation of aromatic L-amino acids, such as tyrosine, tryptophan, and phenylalanine. This protein is likely involved in the synthesis of neurotransmitters, such as dopamine, norepinephrine, and serotonin, which are essential for various physiological processes in the body.",No,No,No,No,No,not-Yes,GO:0020037; GO:0033754; GO:0046872,GO:0004058,GO:0004058,GO:0004058,GO:0004058,GO:0004058,0.1458,0.1458,0.1458,0.1458,0.1458,5,0.1458,0.3154,no
ACDA_ASPCN,A0A2I2F272,Reference,Eukaryota,405,"Indoleamine 2,3-dioxygenase; part of the gene cluster that mediates the biosynthesis of aspcandine, a pyrrolobenzazepine alkaloid. Initially, the indoleamine 2,3-dioxygenase acdA accepts L-tryptophan and performs the oxidative opening of the indole ring to yield N'-formyl-L-kynurenine, which undergoes the spontaneous deformylation reaction to provide L-kynurenine. The kynurenine 3-monooxygenase acdD then hydroxylates L-kynurenine to afford 3-hydroxy-L-kynurenine. 3-hydroxy-L-kynurenine is activated by the A domain of the NRPS-PKS acdB and subsequently loaded onto the enzyme. The KS domain conducts the decarboxylative condensation of the 3-hydroxy-L-kynurenyl and malonyl moieties, and subsequent nucleophilic attacks by the two amino groups would occur nonenzymatically at two distinct positions, achieving the chain release and the construction of the tricyclic system. Finally, a dehydration reaction completes the biosynthesis to yield aspcandine.","Indoleamine 2,3-dioxygenase; part of the gene cluster that mediates the biosynthesis of aspcandine, a pyrrolobenzazepine alkaloid. Initially, the indoleamine 2,3-dioxygenase acdA accepts L-tryptophan and performs the oxidative opening of the indole ring to yield N'-formyl-L-kynurenine, which undergoes the spontaneous deformylation reaction to provide L-kynurenine. The kynurenine 3-monooxygenase acdD then hydroxylates L-kynurenine to afford 3-hydroxy-L-kynurenine. 3-hydroxy-L-kynurenine is activated by the A domain of the NRPS-PKS acdB and subsequently loaded onto the enzyme. The KS domain conducts the decarboxylative condensation of the 3-hydroxy-L-kynurenyl and malonyl moieties, and subsequent nucleophilic attacks by the two amino groups would occur nonenzymatically at two distinct positions, achieving the chain release and the construction of the tricyclic system. Finally, a dehydration reaction completes the biosynthesis to yield aspcandine.",,,,,,,GO:0020037; GO:0033754; GO:0046872,GO:0033754,GO:0033754,GO:0033754,GO:0033754,GO:0033754,0.5493,0.5493,0.5493,0.5493,0.5493,5,0.5493,0.3154,no
CFOK_ASPCN,A0A2I2F2J6,ESM2Text,Eukaryota,254,"Chalcone isomerase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoK acts as chalcone isomerase (CHI), the key enzyme responsible for the tricyclic formation of flavanone through Michael-type intramolecular cyclization of chalcone. The hydrogen at C2'-OH is extracted by the imidazole ring of His-33, which induces the oxa- Michael addition to form the intermediate enolate through 6-endo-trig mode cyclization. The enolate can then be stabilized by a hydrogen bond with the Tyr-50 residue. Following enol tautomerization, the C ring, a gamma-pyranone ring, is formed. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p- hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI plays also a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","Involved in the uptake of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins. Mediates the conversion of some chlorinated non-chlorinated substrates such as naphthalene to the corresponding aldehyde.",No,No,No,No,No,not-Yes,GO:0045430,,,,,,,,,,,0,,0.2098,no
CFOK_ASPCN,A0A2I2F2J6,Prot2Text,Eukaryota,254,"Chalcone isomerase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoK acts as chalcone isomerase (CHI), the key enzyme responsible for the tricyclic formation of flavanone through Michael-type intramolecular cyclization of chalcone. The hydrogen at C2'-OH is extracted by the imidazole ring of His-33, which induces the oxa- Michael addition to form the intermediate enolate through 6-endo-trig mode cyclization. The enolate can then be stabilized by a hydrogen bond with the Tyr-50 residue. Following enol tautomerization, the C ring, a gamma-pyranone ring, is formed. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p- hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI plays also a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","Nicotinate hydroxylase; part of the gene cluster that mediates the biosynthesis of the diterpenoid pyrones subglutinols A and B. The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpmaA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpmaD through the action of the prenyltransferase dpmaC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpmaE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpmaB (Probable). The dehydrogenase dpmaF is then involved in tetrahydrofur",No,No,No,No,No,not-Yes,GO:0045430,,,GO:0016491,GO:0016491,GO:0004497,,,0.4071,0.4071,0.3284,3,0.3809,0.2098,no
CFOK_ASPCN,A0A2I2F2J6,ProtT3,Eukaryota,254,"Chalcone isomerase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoK acts as chalcone isomerase (CHI), the key enzyme responsible for the tricyclic formation of flavanone through Michael-type intramolecular cyclization of chalcone. The hydrogen at C2'-OH is extracted by the imidazole ring of His-33, which induces the oxa- Michael addition to form the intermediate enolate through 6-endo-trig mode cyclization. The enolate can then be stabilized by a hydrogen bond with the Tyr-50 residue. Following enol tautomerization, the C ring, a gamma-pyranone ring, is formed. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p- hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI plays also a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.",Decarboxylase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeranylind,No,No,No,No,No,not-Yes,GO:0045430,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.2742,0.2742,0.2742,0.2742,0.2742,5,0.2742,0.2098,no
CFOK_ASPCN,A0A2I2F2J6,ProtTale,Eukaryota,254,"Chalcone isomerase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoK acts as chalcone isomerase (CHI), the key enzyme responsible for the tricyclic formation of flavanone through Michael-type intramolecular cyclization of chalcone. The hydrogen at C2'-OH is extracted by the imidazole ring of His-33, which induces the oxa- Michael addition to form the intermediate enolate through 6-endo-trig mode cyclization. The enolate can then be stabilized by a hydrogen bond with the Tyr-50 residue. Following enol tautomerization, the C ring, a gamma-pyranone ring, is formed. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p- hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI plays also a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","Isomerase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",No,No,No,No,No,not-Yes,GO:0045430,GO:0016853,GO:0016853,GO:0016853,GO:0016853,GO:0016853,0.6897,0.6897,0.6897,0.6897,0.6897,5,0.6897,0.2098,no
CFOK_ASPCN,A0A2I2F2J6,Protein2Text,Eukaryota,254,"Chalcone isomerase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoK acts as chalcone isomerase (CHI), the key enzyme responsible for the tricyclic formation of flavanone through Michael-type intramolecular cyclization of chalcone. The hydrogen at C2'-OH is extracted by the imidazole ring of His-33, which induces the oxa- Michael addition to form the intermediate enolate through 6-endo-trig mode cyclization. The enolate can then be stabilized by a hydrogen bond with the Tyr-50 residue. Following enol tautomerization, the C ring, a gamma-pyranone ring, is formed. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p- hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI plays also a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","The molecular function of this protein is not specified in the provided text. However, based on its name, it is likely involved in the biosynthesis of a molecule related to plant defense or metabolism, possibly as a part of the phenylpropanoid pathway. This pathway is involved in the synthesis of various secondary metabolites, including flavonoids, lignin, and coumarins, which play important roles in plant defense, stress responses, and adaptation to environmental conditions. The protein's involvement in the phenylpropanoid pathway suggests that it might catalyze a reaction in this pathway, such as the conversion of one metabolite to another, or the synthesis of a specific compound. However, without more information, it is difficult to determine the specific molecular function of this protein.",Vague,No,Vague,Vague,Vague,not-Yes,GO:0045430,,,,,,,,,,,0,,0.2098,no
CFOK_ASPCN,A0A2I2F2J6,Reference,Eukaryota,254,"Chalcone isomerase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoK acts as chalcone isomerase (CHI), the key enzyme responsible for the tricyclic formation of flavanone through Michael-type intramolecular cyclization of chalcone. The hydrogen at C2'-OH is extracted by the imidazole ring of His-33, which induces the oxa- Michael addition to form the intermediate enolate through 6-endo-trig mode cyclization. The enolate can then be stabilized by a hydrogen bond with the Tyr-50 residue. Following enol tautomerization, the C ring, a gamma-pyranone ring, is formed. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p- hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI plays also a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","Chalcone isomerase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoK acts as chalcone isomerase (CHI), the key enzyme responsible for the tricyclic formation of flavanone through Michael-type intramolecular cyclization of chalcone. The hydrogen at C2'-OH is extracted by the imidazole ring of His-33, which induces the oxa- Michael addition to form the intermediate enolate through 6-endo-trig mode cyclization. The enolate can then be stabilized by a hydrogen bond with the Tyr-50 residue. Following enol tautomerization, the C ring, a gamma-pyranone ring, is formed. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p- hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI plays also a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.",,,,,,,GO:0045430,GO:0045430,GO:0045430,GO:0045430,GO:0045430,GO:0045430,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2098,no
CFOD_ASPCN,A0A2I2F2J7,ESM2Text,Eukaryota,406,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoD is responsible for the methylation at position C3-OH of flavonoid. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p-hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI also plays a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome P450 monooxygenase P450-2 then catalyzes the dimerization of nataloe-emodin to cladofulvin.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2328,no
CFOD_ASPCN,A0A2I2F2J7,Prot2Text,Eukaryota,406,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoD is responsible for the methylation at position C3-OH of flavonoid. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p-hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI also plays a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate tolerance, py",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2328,no
CFOD_ASPCN,A0A2I2F2J7,ProtT3,Eukaryota,406,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoD is responsible for the methylation at position C3-OH of flavonoid. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p-hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI also plays a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By similarity). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (By similarity). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the ter",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2328,no
CFOD_ASPCN,A0A2I2F2J7,ProtTale,Eukaryota,406,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoD is responsible for the methylation at position C3-OH of flavonoid. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p-hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI also plays a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the saturated C-C bonds",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0008171,GO:0008171,GO:0008168,GO:0008171,GO:0008171,GO:0008171,1.0,0.8582,1.0,1.0,1.0,5,0.9716,0.2328,no
CFOD_ASPCN,A0A2I2F2J7,Protein2Text,Eukaryota,406,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoD is responsible for the methylation at position C3-OH of flavonoid. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p-hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI also plays a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","This protein is involved in the molecular function of a methyltransferase, specifically a methyltransferase enzyme. Methyltransferases are enzymes that catalyze the transfer of a methyl group from one molecule to another, often involved in various biological processes such as metabolism, signal transduction, and epigenetic regulation. This protein is likely responsible for the methylation of a specific substrate, which may play a role in its biological function. 
The molecular function of this protein is also associated with the binding of a cofactor, which is a molecule required for the enzyme's activity. In this case, the cofactor is likely a methyl group donor, such as S-adenosylmethionine (SAM). The binding of this cofactor is essential for the protein's ability to catalyze the methylation reaction.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0008171,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.2328,no
CFOD_ASPCN,A0A2I2F2J7,Reference,Eukaryota,406,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoD is responsible for the methylation at position C3-OH of flavonoid. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p-hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI also plays a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","Methyltransferase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoD is responsible for the methylation at position C3-OH of flavonoid. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p-hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI also plays a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.",,,,,,,GO:0008171,GO:0008168,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.8582,1.0,1.0,1.0,1.0,5,0.9716,0.2328,no
CFOI_ASPCN,A0A2I2F2K6,ESM2Text,Eukaryota,172,"Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoI is responsible for the hydroxylation of the flavonoid skeleton at position C3 with cfoF. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p- hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI plays also a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","Part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The nonribosomal peptide synthetase ktnABC contains four enzymatic components: kotanin exochlorophyll A (KEXA), kotanin exochlorophyll B (KEXB), and an intramolecular kotanin analog (KTA) that contains an essential methyl group at C4 that binds to the bicyclic aromatic ring of CoA. The methyl group of CoA is probably substituted with a methylene group by the O-methyltransferase ktnC. The methyl group of CoA is further transferred to the cytochrome P450 monooxygenase ktnB via a C-terminal methyl ether to yield the tetramate intermediate. The carbon atoms of CoA, collectively reduced by the cytochrome P450 monooxygenase ktnB, are transferred to the cytochrome P450 monooxygenase ktnD via a C-terminal methyl ether, to yield an intramolecular CoA intermediate. The intramolecular CoA intermediate then undergoes reduction by the cytochrome P450 monooxygenase",No,No,No,No,No,not-Yes,GO:0016829,,,,,,,,,,,0,,0.1777,no
CFOI_ASPCN,A0A2I2F2K6,Prot2Text,Eukaryota,172,"Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoI is responsible for the hydroxylation of the flavonoid skeleton at position C3 with cfoF. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p- hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI plays also a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","Involved in the degradation of the phenolic compound 2,4,6-trichlorophenol (TCP) by the TDP-tetrahydro-p-benzoquinone oxidoreductase. Catalyzes the initial oxygenation step in the pathway, yielding a 2,4-dihydro-3,5-cyclohexadiene-1,2-dione (DCD) intermediate. The reduced flavin is then transferred to the TDP-tetrahydroquinone oxidoreductase (TTH) via a ping-pong mechanism.",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0016829,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.4807,0.4807,0.4807,0.4807,0.4807,5,0.4807,0.1777,no
CFOI_ASPCN,A0A2I2F2K6,ProtT3,Eukaryota,172,"Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoI is responsible for the hydroxylation of the flavonoid skeleton at position C3 with cfoF. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p- hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI plays also a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","Scytalone dehydratase-like protein; part of the gene cluster that mediates the biosynthesis of the fungal meroterpenoid acetoxydehydroaustin . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA . 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN",No,No,No,No,No,not-Yes,GO:0016829,GO:0016836,GO:0016836,GO:0050076,GO:0016836,GO:0050351,0.6897,0.6897,0.4071,0.6897,0.3552,5,0.5663,0.1777,no
CFOI_ASPCN,A0A2I2F2K6,ProtTale,Eukaryota,172,"Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoI is responsible for the hydroxylation of the flavonoid skeleton at position C3 with cfoF. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p- hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI plays also a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","Scytalone dehydratase-like protein; part of the gene cluster that mediates the biosynthesis of sordarin and hypoxysordarin, glycoside antibiotics with a unique tetracyclic diterpene aglycone structure. First, the geranylgeranyl diphosphate synthase sdnC constructs GGDP from farnesyl diphosphate and isopentenyl diphosphate. The diterpene cyclase sdnA then catalyzes the cyclization of GGDP to afford cycloaraneosene. Cycloaraneosene is then hydroxylated four times by the putative cytochrome P450 monooxygenases sdnB, sdnE, sdnF",No,No,No,No,No,not-Yes,GO:0016829,GO:0016836,,,GO:0016836,GO:0016836,0.6897,,,0.6897,0.6897,3,0.6897,0.1777,no
CFOI_ASPCN,A0A2I2F2K6,Protein2Text,Eukaryota,172,"Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoI is responsible for the hydroxylation of the flavonoid skeleton at position C3 with cfoF. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p- hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI plays also a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","This protein is involved in the degradation of a specific type of molecule, likely a xenobiotic or a pollutant. The molecular function of this protein is to catalyze the breakdown of that molecule, possibly as part of a larger metabolic pathway.",Vague,No,Vague,Vague,Vague,not-Yes,GO:0016829,,,,,,,,,,,0,,0.1777,no
CFOI_ASPCN,A0A2I2F2K6,Reference,Eukaryota,172,"Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoI is responsible for the hydroxylation of the flavonoid skeleton at position C3 with cfoF. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p- hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI plays also a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoI is responsible for the hydroxylation of the flavonoid skeleton at position C3 with cfoF. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p- hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI plays also a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.",,,,,,,GO:0016829,GO:0004497,GO:0004497,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497,0.4807,0.4807,0.3259,0.3259,0.4807,5,0.4188,0.1777,no
CFOC_ASPCN,A0A2I2F2K7,ESM2Text,Eukaryota,401,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoC is responsible for the methylation at position C8-OH of flavonoid. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p-hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI also plays a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the tropolone class of fungal maleic anhydrides. The pathway begins with the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide synthase (PKS) tropA. 3-methylorcinaldehyde is the substrate for the FAD-dependent monooxygenase tropB to yield a dearomatized hydroxycyclohexadione. The 2-oxoglutarate-dependent dioxygenase tropC then performs the oxidative ring expansion to provide the first tropolone metabolite stipitaldehyde. Trop D converts stipitaldehyde into stipitacetal which is in turn converted to stipitalide by the short-chain dehydrogenase/reductase tropE. The next steps involve tropF, tropG, tropH, tropI and tropJ to form successive tropolone maleic anhydrides including stipitaldehydic, stipitatonic and stipitatic acids.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2844,no
CFOC_ASPCN,A0A2I2F2K7,Prot2Text,Eukaryota,401,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoC is responsible for the methylation at position C8-OH of flavonoid. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p-hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI also plays a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate tolerance, py",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2844,no
CFOC_ASPCN,A0A2I2F2K7,ProtT3,Eukaryota,401,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoC is responsible for the methylation at position C8-OH of flavonoid. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p-hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI also plays a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By similarity). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (By similarity). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the ter",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2844,no
CFOC_ASPCN,A0A2I2F2K7,ProtTale,Eukaryota,401,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoC is responsible for the methylation at position C8-OH of flavonoid. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p-hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI also plays a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the saturated C-C bonds",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008168,GO:0008171,GO:0008171,GO:0008171,0.7088,0.6208,0.7088,0.7088,0.7088,5,0.6912,0.2844,no
CFOC_ASPCN,A0A2I2F2K7,Protein2Text,Eukaryota,401,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoC is responsible for the methylation at position C8-OH of flavonoid. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p-hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI also plays a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","The molecular function of this protein is likely involved in the modification or synthesis of small molecules, such as the conversion of one compound to another. Specifically, it is a cytochrome P450 monooxygenase, which suggests that it catalyzes the insertion of an oxygen atom into a substrate molecule. This is a common function of cytochrome P450 enzymes, which are involved in a wide range of metabolic reactions. However, the exact function of this protein, including the specific substrate it acts on and the product it produces, is not specified in the provided information. 
Based on the name of the protein, it is likely involved in the modification of a molecule with a hydroxyl group (-OH), such as a phenolic compound or an alkaloid. The name ""hydroxylation"" suggests that the protein is involved in adding a hydroxyl group to a substrate molecule, which is a common reaction catalyzed by cytochrome P450 enzymes. However, the specific substrate and product of this protein are not specified in the provided information.",No,No,No,No,No,not-Yes,GO:0008171; GO:0046983,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.2475,0.2475,0.2475,0.2475,0.2475,5,0.2475,0.2844,no
CFOC_ASPCN,A0A2I2F2K7,Reference,Eukaryota,401,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoC is responsible for the methylation at position C8-OH of flavonoid. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p-hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI also plays a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.","Methyltransferase; part of the gene cluster that mediates the biosynthesis of chlorflavonin, a fungal flavonoid with acetolactate synthase inhibitory activity. Within the pathway, cfoC is responsible for the methylation at position C8-OH of flavonoid. The pathway begins with the PKS-NRPS hybrid synthetase cfoA that uses benzoic acid or p-hydroxybenzoic acid as a starter unit with four rounds of chain elongation using malonyl-CoA to form the chalcone skeleton. Then, a new type of chalcone isomerase, cfoK, catalyzes the conversion of the chalcone into a flavanone by a histidine-mediated oxa-Michael addition mechanism. The desaturation of flavanone to flavone is catalyzed by a new type of flavone synthase, the flavin mononucleotide (FMN)-dependent oxidoreductase cfoJ. Monooxygenases cfoF, cfoG, and P450 cfoH are responsible for the hydroxylation of the flavonoid skeleton at sites C3, C8, and C2', respectively. Like cfoF, the dehydratase cfoI also plays a role in the hydroxylation of position C3. Methyltransferases cfoB, cfoC, and cfoD then catalyze the methylation of C7-OH, C8-OH, and C3-OH, respectively. Finally, the monooxygenase cfoE is responsible for the chlorination of flavonoid at position C3'.",,,,,,,GO:0008171; GO:0046983,GO:0008168,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.6208,0.7088,0.7088,0.7088,0.7088,5,0.6912,0.2844,no
NLRN_HYAVF,A0A2J6RX17,ESM2Text,Eukaryota,990,"The N-terminal purine nucleoside phosphorylase (PNP) domain cleaves the N-glycosidic bond of ATP, and to a lesser extent dATP; has very weak activity on adenosine and deoxyadenosine and no activity on (d)ADP or (d)AMP.","Probable disease resistance (R) protein that inhibits the expression of resistance protein genes including RPP5, RPP12 and RPP13 in response to alkylation lesions.",No,No,No,No,No,not-Yes,GO:0043531; GO:0016787,,,,,,,,,,,0,,0.4375,no
NLRN_HYAVF,A0A2J6RX17,Prot2Text,Eukaryota,990,"The N-terminal purine nucleoside phosphorylase (PNP) domain cleaves the N-glycosidic bond of ATP, and to a lesser extent dATP; has very weak activity on adenosine and deoxyadenosine and no activity on (d)ADP or (d)AMP.",E3 ubiquitin-protein ligase involved in the control of non-apoptotic cell death. Mediates 'Lys-63'-linked ubiquitination of MDM2 and induces its degradation via the proteasome.,No,No,No,No,No,not-Yes,GO:0043531; GO:0016787,GO:0004842,GO:0004842,GO:0004842,GO:0004842,GO:0004842,0.2325,0.2325,0.2325,0.2325,0.2325,5,0.2325,0.4375,no
NLRN_HYAVF,A0A2J6RX17,ProtT3,Eukaryota,990,"The N-terminal purine nucleoside phosphorylase (PNP) domain cleaves the N-glycosidic bond of ATP, and to a lesser extent dATP; has very weak activity on adenosine and deoxyadenosine and no activity on (d)ADP or (d)AMP.",Belongs to the NB-LRR family,No,Vague,Vague,Vague,Vague,not-Yes,GO:0043531; GO:0016787,GO:0005524,GO:0005524,,,,0.5912,0.5912,,,,2,0.5912,0.4375,no
NLRN_HYAVF,A0A2J6RX17,ProtTale,Eukaryota,990,"The N-terminal purine nucleoside phosphorylase (PNP) domain cleaves the N-glycosidic bond of ATP, and to a lesser extent dATP; has very weak activity on adenosine and deoxyadenosine and no activity on (d)ADP or (d)AMP.","Effector protein that is responsible for the suppression of plant defense responses during the biotrophic phase of the fungal infection. Acts as a substrate of the E3 ubiquitin-protein ligase COP9 signalosome complex (CSN), which is required for the ubiquitination and subsequent proteasomal degradation of host proteins.",No,No,No,No,No,not-Yes,GO:0043531; GO:0016787,,,,,,,,,,,0,,0.4375,no
NLRN_HYAVF,A0A2J6RX17,Protein2Text,Eukaryota,990,"The N-terminal purine nucleoside phosphorylase (PNP) domain cleaves the N-glycosidic bond of ATP, and to a lesser extent dATP; has very weak activity on adenosine and deoxyadenosine and no activity on (d)ADP or (d)AMP.","The molecular function of this protein is a serine protease, which is involved in the activation of other proteins by cleaving their peptide bonds. It is a key component of the immune response, specifically in the recognition of pathogen-associated molecular patterns (PAMPs) and the activation of downstream signaling pathways.",No,No,No,No,No,not-Yes,GO:0043531; GO:0016787,GO:0008236,GO:0004252,GO:0004252,GO:0004252,GO:0004252,0.3872,0.3201,0.3201,0.3201,0.3201,5,0.3335,0.4375,no
NLRN_HYAVF,A0A2J6RX17,Reference,Eukaryota,990,"The N-terminal purine nucleoside phosphorylase (PNP) domain cleaves the N-glycosidic bond of ATP, and to a lesser extent dATP; has very weak activity on adenosine and deoxyadenosine and no activity on (d)ADP or (d)AMP.","The N-terminal purine nucleoside phosphorylase (PNP) domain cleaves the N-glycosidic bond of ATP, and to a lesser extent dATP; has very weak activity on adenosine and deoxyadenosine and no activity on (d)ADP or (d)AMP.",,,,,,,GO:0043531; GO:0016787,GO:0004731,GO:0004731,GO:0004731,GO:0016799,GO:0004731,0.2551,0.2551,0.2551,0.481,0.2551,5,0.3003,0.4375,no
CRLS1_CHLRE,A0A2K3D1C8,ESM2Text,Eukaryota,351,Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions. Cannot catalyze the phosphatidyl group transfer from one PG molecule to another to form CL.,Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0043337,GO:0008808,GO:0008808,GO:0008808; GO:0016780,GO:0008808,GO:0008808,0.7469,0.7469,0.7516,0.7469,0.7469,5,0.7478,0.5482,yes
CRLS1_CHLRE,A0A2K3D1C8,Prot2Text,Eukaryota,351,Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions. Cannot catalyze the phosphatidyl group transfer from one PG molecule to another to form CL.,Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0043337,GO:0008808,GO:0008808,GO:0008808,GO:0008808,GO:0008808,0.7469,0.7469,0.7469,0.7469,0.7469,5,0.7469,0.5482,yes
CRLS1_CHLRE,A0A2K3D1C8,ProtT3,Eukaryota,351,Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions. Cannot catalyze the phosphatidyl group transfer from one PG molecule to another to form CL.,Catalyzes the committed step to the synthesis of the acidic phospholipids. Membrane; Multi-pass membrane protein. Belongs to the CDP-alcohol phosphatidyltransferase class-I family,Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0043337,GO:0016780,GO:0008444,GO:0016780,GO:0016780,GO:0016780,0.7539,0.5445,0.7539,0.7539,0.7539,5,0.712,0.5482,yes
CRLS1_CHLRE,A0A2K3D1C8,ProtTale,Eukaryota,351,Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions. Cannot catalyze the phosphatidyl group transfer from one PG molecule to another to form CL.,Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0043337,GO:0008808,GO:0008808,GO:0016780,GO:0008808,GO:0008808,0.7469,0.7469,0.7539,0.7469,0.7469,5,0.7483,0.5482,yes
CRLS1_CHLRE,A0A2K3D1C8,Protein2Text,Eukaryota,351,Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions. Cannot catalyze the phosphatidyl group transfer from one PG molecule to another to form CL.,"The molecular function of this protein is a mitochondrial coenzyme Q biosynthetic enzyme, specifically a coenzyme Q biosynthetic enzyme involved in the conversion of polyprenyl phosphate to coenzyme Q.",No,No,No,No,No,not-Yes,GO:0043337,,,,,,,,,,,0,,0.5482,yes
CRLS1_CHLRE,A0A2K3D1C8,Reference,Eukaryota,351,Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions. Cannot catalyze the phosphatidyl group transfer from one PG molecule to another to form CL.,Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions. Cannot catalyze the phosphatidyl group transfer from one PG molecule to another to form CL.,,,,,,,GO:0043337,GO:0008808,GO:0008808,GO:0008808,GO:0008808,GO:0008808,0.7469,0.7469,0.7469,0.7469,0.7469,5,0.7469,0.5482,yes
SUFS_PLAVI,A0A2K8FTN3,ESM2Text,Eukaryota,551,Catalyzes sulfur activation and mobilization in sulfur mobilization (SUF) pathway for iron-sulfur (Fe-S) cluster biogenesis. Active when in complex with a partner protein SufE. Required for apicoplast maintenance. Plays a role in the development of sporozoites in oocysts in mosquitoes.,"Bifunctional enzyme that catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.",No,No,No,No,No,not-Yes,GO:0031071,GO:0030429,GO:0030429,GO:0004059; GO:0004060,GO:0030431,GO:0030429; GO:0030170,0.1998,0.1998,0.2413,0.0,0.1563,5,0.1594,0.5308,no
SUFS_PLAVI,A0A2K8FTN3,Prot2Text,Eukaryota,551,Catalyzes sulfur activation and mobilization in sulfur mobilization (SUF) pathway for iron-sulfur (Fe-S) cluster biogenesis. Active when in complex with a partner protein SufE. Required for apicoplast maintenance. Plays a role in the development of sporozoites in oocysts in mosquitoes.,"Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine.",Yes,Maybe,Yes,Maybe,Yes,Yes,GO:0031071,GO:0031071,GO:0031071,GO:0031071,GO:0031071,GO:0031071,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5308,no
SUFS_PLAVI,A0A2K8FTN3,ProtT3,Eukaryota,551,Catalyzes sulfur activation and mobilization in sulfur mobilization (SUF) pathway for iron-sulfur (Fe-S) cluster biogenesis. Active when in complex with a partner protein SufE. Required for apicoplast maintenance. Plays a role in the development of sporozoites in oocysts in mosquitoes.,"Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd subfamily",Yes,Maybe,Yes,Maybe,Yes,Yes,GO:0031071,GO:0031071,GO:0031071,GO:0031071,GO:0031071; GO:0030170,GO:0031071; GO:0030170,1.0,1.0,1.0,0.6898,0.6898,5,0.8759,0.5308,no
SUFS_PLAVI,A0A2K8FTN3,ProtTale,Eukaryota,551,Catalyzes sulfur activation and mobilization in sulfur mobilization (SUF) pathway for iron-sulfur (Fe-S) cluster biogenesis. Active when in complex with a partner protein SufE. Required for apicoplast maintenance. Plays a role in the development of sporozoites in oocysts in mosquitoes.,Catalyzes the conversion of L-cysteine to O-acetyl-L-cysteine.,No,No,No,No,No,not-Yes,GO:0031071,GO:0016407,GO:0016747,GO:0016747,GO:0016747,GO:0016407,0.3386,0.3987,0.3987,0.3987,0.3386,5,0.3747,0.5308,no
SUFS_PLAVI,A0A2K8FTN3,Protein2Text,Eukaryota,551,Catalyzes sulfur activation and mobilization in sulfur mobilization (SUF) pathway for iron-sulfur (Fe-S) cluster biogenesis. Active when in complex with a partner protein SufE. Required for apicoplast maintenance. Plays a role in the development of sporozoites in oocysts in mosquitoes.,"This protein is a sulfhydrylase, which is a type of enzyme that catalyzes the transfer of a sulfur atom from a cysteine residue to a target molecule. More specifically, it is involved in the synthesis of the pyrimidine nucleotides, as it catalyzes the transfer of a sulfur atom from cysteine to the 5'-phosphoribosylamine moiety of the nucleotide, forming 5-phosphoribosyl-N-sulfonamide.",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0031071,,,,,,,,,,,0,,0.5308,no
SUFS_PLAVI,A0A2K8FTN3,Reference,Eukaryota,551,Catalyzes sulfur activation and mobilization in sulfur mobilization (SUF) pathway for iron-sulfur (Fe-S) cluster biogenesis. Active when in complex with a partner protein SufE. Required for apicoplast maintenance. Plays a role in the development of sporozoites in oocysts in mosquitoes.,Catalyzes sulfur activation and mobilization in sulfur mobilization (SUF) pathway for iron-sulfur (Fe-S) cluster biogenesis. Active when in complex with a partner protein SufE. Required for apicoplast maintenance. Plays a role in the development of sporozoites in oocysts in mosquitoes.,,,,,,,GO:0031071,GO:0016829,GO:0031071,GO:0031071,GO:0031071,GO:0031071,0.3552,1.0,1.0,1.0,1.0,5,0.871,0.5308,no
SQIK_ALKUR,A0A2P6MHT4,ESM2Text,Bacteria,381,"Part of the sulfo-EMP2 pathway, a D-sulfoquinovose degradation pathway that produces sulfolactate (SL) (Ref.2). Phosphorylates 6-deoxy-6-sulfo-D-fructose (SF) to 6-deoxy-6-sulfo-D- fructose 1-phosphate (SFP) (Ref.2).","Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0061594; GO:0003872; GO:0005524; GO:0046872,GO:0003872; GO:0005524,GO:0003872,GO:0003872; GO:0005524,GO:0003872; GO:0005524,GO:0003872; GO:0005524,0.8066,0.5327,0.8066,0.8066,0.8066,5,0.7518,0.3604,no
SQIK_ALKUR,A0A2P6MHT4,Prot2Text,Bacteria,381,"Part of the sulfo-EMP2 pathway, a D-sulfoquinovose degradation pathway that produces sulfolactate (SL) (Ref.2). Phosphorylates 6-deoxy-6-sulfo-D-fructose (SF) to 6-deoxy-6-sulfo-D- fructose 1-phosphate (SFP) (Ref.2).","Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0061594; GO:0003872; GO:0005524; GO:0046872,GO:0003872,GO:0003872,GO:0003872,GO:0003872,GO:0003872,0.5327,0.5327,0.5327,0.5327,0.5327,5,0.5327,0.3604,no
SQIK_ALKUR,A0A2P6MHT4,ProtT3,Bacteria,381,"Part of the sulfo-EMP2 pathway, a D-sulfoquinovose degradation pathway that produces sulfolactate (SL) (Ref.2). Phosphorylates 6-deoxy-6-sulfo-D-fructose (SF) to 6-deoxy-6-sulfo-D- fructose 1-phosphate (SFP) (Ref.2).","Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. Cytoplasm. SIMIL",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0061594; GO:0003872; GO:0005524; GO:0046872,GO:0047340,GO:0047334,GO:0047334,GO:0047334,GO:0047334,0.3111,0.4543,0.4543,0.4543,0.4543,5,0.4257,0.3604,no
SQIK_ALKUR,A0A2P6MHT4,ProtTale,Bacteria,381,"Part of the sulfo-EMP2 pathway, a D-sulfoquinovose degradation pathway that produces sulfolactate (SL) (Ref.2). Phosphorylates 6-deoxy-6-sulfo-D-fructose (SF) to 6-deoxy-6-sulfo-D- fructose 1-phosphate (SFP) (Ref.2).","Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0061594; GO:0003872; GO:0005524; GO:0046872,GO:0003872,GO:0016301; GO:0016773,GO:0003872,GO:0003872,GO:0047334,0.5327,0.5286,0.5327,0.5327,0.4543,5,0.5162,0.3604,no
SQIK_ALKUR,A0A2P6MHT4,Protein2Text,Bacteria,381,"Part of the sulfo-EMP2 pathway, a D-sulfoquinovose degradation pathway that produces sulfolactate (SL) (Ref.2). Phosphorylates 6-deoxy-6-sulfo-D-fructose (SF) to 6-deoxy-6-sulfo-D- fructose 1-phosphate (SFP) (Ref.2).","The molecular function of this protein is an aldolase, which is an enzyme that catalyzes the reversible cleavage of aldolase substrates such as fructose-1,6-bisphosphate.",No,No,No,No,No,not-Yes,GO:0061594; GO:0003872; GO:0005524; GO:0046872,GO:0004332,GO:0004332,GO:0004332,GO:0004332,GO:0004332,0.139,0.139,0.139,0.139,0.139,5,0.139,0.3604,no
SQIK_ALKUR,A0A2P6MHT4,Reference,Bacteria,381,"Part of the sulfo-EMP2 pathway, a D-sulfoquinovose degradation pathway that produces sulfolactate (SL) (Ref.2). Phosphorylates 6-deoxy-6-sulfo-D-fructose (SF) to 6-deoxy-6-sulfo-D- fructose 1-phosphate (SFP) (Ref.2).","Part of the sulfo-EMP2 pathway, a D-sulfoquinovose degradation pathway that produces sulfolactate (SL) (Ref.2). Phosphorylates 6-deoxy-6-sulfo-D-fructose (SF) to 6-deoxy-6-sulfo-D- fructose 1-phosphate (SFP) (Ref.2).",,,,,,,GO:0061594; GO:0003872; GO:0005524; GO:0046872,GO:0016301,GO:0016301,GO:0016301,GO:0016301; GO:0005524,GO:0016301,0.4086,0.4086,0.4086,0.694,0.4086,5,0.4657,0.3604,no
SQIA_ALKUR,A0A2P6MHY1,ESM2Text,Bacteria,287,"Part of the sulfo-EMP2 pathway, a D-sulfoquinovose degradation pathway that produces sulfolactate (SL) (Ref.2). Cleaves 6- deoxy-6-sulfo-D-fructose 1-phosphate (SFP) to form dihydroxyacetone phosphate (DHAP) and 3-sulfolactaldehyde (SLA) (Ref.2).","Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016832; GO:0008270,GO:0004332,GO:0004332,GO:0004332,GO:0004332,GO:0004332,0.5949,0.5949,0.5949,0.5949,0.5949,5,0.5949,0.5714,yes
SQIA_ALKUR,A0A2P6MHY1,Prot2Text,Bacteria,287,"Part of the sulfo-EMP2 pathway, a D-sulfoquinovose degradation pathway that produces sulfolactate (SL) (Ref.2). Cleaves 6- deoxy-6-sulfo-D-fructose 1-phosphate (SFP) to form dihydroxyacetone phosphate (DHAP) and 3-sulfolactaldehyde (SLA) (Ref.2).","Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016832; GO:0008270,GO:0004332,GO:0004332,GO:0004332,GO:0004332,GO:0004332,0.5949,0.5949,0.5949,0.5949,0.5949,5,0.5949,0.5714,yes
SQIA_ALKUR,A0A2P6MHY1,ProtT3,Bacteria,287,"Part of the sulfo-EMP2 pathway, a D-sulfoquinovose degradation pathway that produces sulfolactate (SL) (Ref.2). Cleaves 6- deoxy-6-sulfo-D-fructose 1-phosphate (SFP) to form dihydroxyacetone phosphate (DHAP) and 3-sulfolactaldehyde (SLA) (Ref.2).","Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. Belongs to the class II fructose-bisphosphate aldolase family",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016832; GO:0008270,GO:0004332,GO:0004332,GO:0004332,GO:0004332,GO:0004332,0.5949,0.5949,0.5949,0.5949,0.5949,5,0.5949,0.5714,yes
SQIA_ALKUR,A0A2P6MHY1,ProtTale,Bacteria,287,"Part of the sulfo-EMP2 pathway, a D-sulfoquinovose degradation pathway that produces sulfolactate (SL) (Ref.2). Cleaves 6- deoxy-6-sulfo-D-fructose 1-phosphate (SFP) to form dihydroxyacetone phosphate (DHAP) and 3-sulfolactaldehyde (SLA) (Ref.2).","Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016832; GO:0008270,GO:0004332,GO:0004332,GO:0004332,GO:0004332,GO:0004332,0.5949,0.5949,0.5949,0.5949,0.5949,5,0.5949,0.5714,yes
SQIA_ALKUR,A0A2P6MHY1,Protein2Text,Bacteria,287,"Part of the sulfo-EMP2 pathway, a D-sulfoquinovose degradation pathway that produces sulfolactate (SL) (Ref.2). Cleaves 6- deoxy-6-sulfo-D-fructose 1-phosphate (SFP) to form dihydroxyacetone phosphate (DHAP) and 3-sulfolactaldehyde (SLA) (Ref.2).","This protein is involved in catalyzing a specific reaction, which is part of a larger metabolic pathway. The molecular function of this protein is likely related to its role in catalyzing a specific chemical reaction, possibly involving the breakdown or synthesis of a particular compound. 

Given the name of the protein, it is likely involved in the synthesis of a specific compound. The name suggests that it is a part of a larger metabolic pathway, possibly involving the synthesis of a particular sugar or carbohydrate. 

More specifically, the protein is likely involved in catalyzing the condensation of two molecules to form a new compound. This is a common function of enzymes that catalyze the formation of new chemical bonds.

Without more information, it is difficult to provide a more specific answer. However, based on the name of the protein, it is likely involved in a reaction related to sugar or carbohydrate metabolism.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016832; GO:0008270,,,,,,,,,,,0,,0.5714,yes
SQIA_ALKUR,A0A2P6MHY1,Reference,Bacteria,287,"Part of the sulfo-EMP2 pathway, a D-sulfoquinovose degradation pathway that produces sulfolactate (SL) (Ref.2). Cleaves 6- deoxy-6-sulfo-D-fructose 1-phosphate (SFP) to form dihydroxyacetone phosphate (DHAP) and 3-sulfolactaldehyde (SLA) (Ref.2).","Part of the sulfo-EMP2 pathway, a D-sulfoquinovose degradation pathway that produces sulfolactate (SL) (Ref.2). Cleaves 6- deoxy-6-sulfo-D-fructose 1-phosphate (SFP) to form dihydroxyacetone phosphate (DHAP) and 3-sulfolactaldehyde (SLA) (Ref.2).",,,,,,,GO:0016832; GO:0008270,GO:0016829,GO:0016832,GO:0016832,GO:0016829,GO:0016832,0.5027,0.6941,0.6941,0.5027,0.6941,5,0.6175,0.5714,yes
OKAC_PENOH,A0A2Z5U367,ESM2Text,Eukaryota,429,"Prenyltransferase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four-membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaC performs asymmetric reverse prenylation of cyclo(L-Trp-L-Trp) at N-1 and C-2' of the indole ring to produce the cyclic prenylated tryptophan dimer cyclo(N8-(alpha,alpha- dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L-Trp). The biosynthesis begins with the NRPS okaA that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8- (alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L- Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.","Prenyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ. Paxilline is converted to beta-pax",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3651,no
OKAC_PENOH,A0A2Z5U367,Prot2Text,Eukaryota,429,"Prenyltransferase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four-membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaC performs asymmetric reverse prenylation of cyclo(L-Trp-L-Trp) at N-1 and C-2' of the indole ring to produce the cyclic prenylated tryptophan dimer cyclo(N8-(alpha,alpha- dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L-Trp). The biosynthesis begins with the NRPS okaA that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8- (alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L- Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.","Prenyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase penM leads to a epoxidized-GGI that is substrate of the terpene cyclase penB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase penP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase penQ. Paxilline is converted to beta-paxitriol via C-10",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0016765,GO:0004659,1.0,1.0,1.0,0.8416,1.0,5,0.9683,0.3651,no
OKAC_PENOH,A0A2Z5U367,ProtT3,Eukaryota,429,"Prenyltransferase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four-membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaC performs asymmetric reverse prenylation of cyclo(L-Trp-L-Trp) at N-1 and C-2' of the indole ring to produce the cyclic prenylated tryptophan dimer cyclo(N8-(alpha,alpha- dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L-Trp). The biosynthesis begins with the NRPS okaA that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8- (alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L- Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.",Prenyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeranylind,Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0016765,1.0,1.0,1.0,1.0,0.8416,5,0.9683,0.3651,no
OKAC_PENOH,A0A2Z5U367,ProtTale,Eukaryota,429,"Prenyltransferase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four-membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaC performs asymmetric reverse prenylation of cyclo(L-Trp-L-Trp) at N-1 and C-2' of the indole ring to produce the cyclic prenylated tryptophan dimer cyclo(N8-(alpha,alpha- dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L-Trp). The biosynthesis begins with the NRPS okaA that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8- (alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L- Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.","FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. Within the pathway, phiC is responsible for the hydroxylation of the 5-hydroxyl group. The pathway begins with the highly reducing polyketide synthase phiA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase phiM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) phi",No,No,No,No,No,not-Yes,GO:0004659,GO:0004497,GO:0016491; GO:0071949,GO:0004497; GO:0050660,GO:0004497,GO:0004497,0.3284,0.2983,0.2483,0.3284,0.3284,5,0.3064,0.3651,no
OKAC_PENOH,A0A2Z5U367,Protein2Text,Eukaryota,429,"Prenyltransferase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four-membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaC performs asymmetric reverse prenylation of cyclo(L-Trp-L-Trp) at N-1 and C-2' of the indole ring to produce the cyclic prenylated tryptophan dimer cyclo(N8-(alpha,alpha- dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L-Trp). The biosynthesis begins with the NRPS okaA that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8- (alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L- Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.","The molecular function of this protein is a prenyltransferase, specifically a geranylgeranyl transferase, which is involved in the biosynthesis of isoprenoids. It catalyzes the transfer of a geranylgeranyl group from geranylgeranyl diphosphate (GGPP) to a cysteine residue of a substrate protein, resulting in the modification of the protein and its activation. This protein is involved in the biosynthesis of a variety of molecules, including carotenoids, tocopherols, and gibberellins.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0004659,GO:0004311,GO:0004659,GO:0004659,GO:0004659,,0.7539,1.0,1.0,1.0,,4,0.9385,0.3651,no
OKAC_PENOH,A0A2Z5U367,Reference,Eukaryota,429,"Prenyltransferase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four-membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaC performs asymmetric reverse prenylation of cyclo(L-Trp-L-Trp) at N-1 and C-2' of the indole ring to produce the cyclic prenylated tryptophan dimer cyclo(N8-(alpha,alpha- dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L-Trp). The biosynthesis begins with the NRPS okaA that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8- (alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L- Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.","Prenyltransferase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four-membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaC performs asymmetric reverse prenylation of cyclo(L-Trp-L-Trp) at N-1 and C-2' of the indole ring to produce the cyclic prenylated tryptophan dimer cyclo(N8-(alpha,alpha- dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L-Trp). The biosynthesis begins with the NRPS okaA that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8- (alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L- Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.",,,,,,,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3651,no
OKAB_PENOH,A0A2Z5U368,ESM2Text,Eukaryota,450,"FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four- membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaC performs indole 2,3-epoxidation, facilitating the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. okaC then performs asymmetric reverse prenylation of cyclo(L-Trp-L-Trp) at N-1 and C-2' of the indole ring to produce the cyclic prenylated tryptophan dimer cyclo(N8-(alpha,alpha- dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L-Trp). The biosynthesis begins with the NRPS okaA that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8- (alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L- Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.","FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids nectripenoids A and B, as well as cochliquninone D and isocochliquninone E. The pathway probably begins with the HR-PKS ntnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS ntnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of nectripenoids (Probable). The FAD-dependent monooxygenase ntnJ then performs an oxidative decarboxylation at C11 of the ntnH/ntnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation (Probable). The membrane-bound polyprenyl transferase ntnF then introduces a farnesyl group before the FAD-dependent monooxygenase ntnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0071949; GO:0004497,GO:0004497; GO:0071949,GO:0004497,GO:0016491,GO:0004497; GO:0071949,GO:0004497; GO:0071949,1.0,0.6988,0.5823,1.0,1.0,5,0.8562,0.1848,no
OKAB_PENOH,A0A2Z5U368,Prot2Text,Eukaryota,450,"FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four- membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaC performs indole 2,3-epoxidation, facilitating the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. okaC then performs asymmetric reverse prenylation of cyclo(L-Trp-L-Trp) at N-1 and C-2' of the indole ring to produce the cyclic prenylated tryptophan dimer cyclo(N8-(alpha,alpha- dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L-Trp). The biosynthesis begins with the NRPS okaA that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8- (alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L- Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.","FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential tr",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0071949; GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.6988,0.6988,0.6988,0.6988,0.6988,5,0.6988,0.1848,no
OKAB_PENOH,A0A2Z5U368,ProtT3,Eukaryota,450,"FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four- membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaC performs indole 2,3-epoxidation, facilitating the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. okaC then performs asymmetric reverse prenylation of cyclo(L-Trp-L-Trp) at N-1 and C-2' of the indole ring to produce the cyclic prenylated tryptophan dimer cyclo(N8-(alpha,alpha- dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L-Trp). The biosynthesis begins with the NRPS okaA that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8- (alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L- Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.",FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeranylindole (3-,Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0071949; GO:0004497,GO:0004497; GO:0071949,GO:0004497; GO:0071949,GO:0004497; GO:0071949,GO:0004497; GO:0071949,GO:0004497; GO:0071949,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1848,no
OKAB_PENOH,A0A2Z5U368,ProtTale,Eukaryota,450,"FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four- membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaC performs indole 2,3-epoxidation, facilitating the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. okaC then performs asymmetric reverse prenylation of cyclo(L-Trp-L-Trp) at N-1 and C-2' of the indole ring to produce the cyclic prenylated tryptophan dimer cyclo(N8-(alpha,alpha- dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L-Trp). The biosynthesis begins with the NRPS okaA that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8- (alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L- Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.","FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product,",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0071949; GO:0004497,GO:0004497,GO:0016491; GO:0071949,GO:0004497; GO:0050660,GO:0004497,GO:0004497,0.6988,0.9073,0.9573,0.6988,0.6988,5,0.7922,0.1848,no
OKAB_PENOH,A0A2Z5U368,Protein2Text,Eukaryota,450,"FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four- membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaC performs indole 2,3-epoxidation, facilitating the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. okaC then performs asymmetric reverse prenylation of cyclo(L-Trp-L-Trp) at N-1 and C-2' of the indole ring to produce the cyclic prenylated tryptophan dimer cyclo(N8-(alpha,alpha- dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L-Trp). The biosynthesis begins with the NRPS okaA that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8- (alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L- Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.","This protein is a cytochrome P450 monooxygenase, which suggests that its molecular function is to catalyze the oxidation of a substrate using molecular oxygen, typically in the presence of a reducing agent such as NADPH. In this case, the protein is involved in the oxidation of an organic compound, likely in the process of breaking down or metabolizing it. Cytochrome P450 enzymes are involved in a wide range of reactions, including the metabolism of drugs, the synthesis of steroids and other hormones, and the breakdown of environmental pollutants. The specific function of this protein is likely to be the oxidation of a specific substrate, such as a steroid or a xenobiotic compound, and it may be involved in the metabolism of a particular drug or toxin. 

More specifically, this protein is involved in the hydroxylation of an organic compound. Hydroxylation is a common reaction catalyzed by cytochrome P450 enzymes, in which a hydroxyl group (-OH) is added to a substrate molecule. This reaction is often used to introduce a functional group into a molecule, or to modify the structure of a molecule in some way. In this case, the protein is likely to be responsible for introducing a hydroxyl group into a specific position on the substrate molecule, resulting in the formation of a new compound. 

It is worth noting that the exact substrate of this protein is not specified in the provided information, so it is difficult to say more about its molecular function without further context. However, based on its classification as a cytochrome P450 monooxygenase, it is likely to be involved in some type of oxidation reaction.",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0071949; GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.6988,0.6988,0.6988,0.6988,0.6988,5,0.6988,0.1848,no
OKAB_PENOH,A0A2Z5U368,Reference,Eukaryota,450,"FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four- membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaC performs indole 2,3-epoxidation, facilitating the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. okaC then performs asymmetric reverse prenylation of cyclo(L-Trp-L-Trp) at N-1 and C-2' of the indole ring to produce the cyclic prenylated tryptophan dimer cyclo(N8-(alpha,alpha- dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L-Trp). The biosynthesis begins with the NRPS okaA that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8- (alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L- Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.","FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of okaramine B, a prenylated indole alkaloid that possesses an unusual octacyclic ring system, including a four- membered azetidine ring and an eight-membered azocine ring, and that exhibits insecticidal activity against silkworm larvae. Within the pathway, okaC performs indole 2,3-epoxidation, facilitating the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. okaC then performs asymmetric reverse prenylation of cyclo(L-Trp-L-Trp) at N-1 and C-2' of the indole ring to produce the cyclic prenylated tryptophan dimer cyclo(N8-(alpha,alpha- dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L-Trp). The biosynthesis begins with the NRPS okaA that condenses two tryptophan molecules into cyclo(L-Trp-L-Trp). Prenylation by the prenyltransferase okaC then leads to the formation of cyclo(N8- (alpha,alpha-dimethylallyl)-L-Trp-6a-(alpha,alpha-dime-thylallyl)-L- Trp). This is followed by indole 2,3-epoxidation by the FAD-dependent monooxygenase okaB to facilitate the formation of the hexahydropyrrolo[2,3-b]indole (HPI) moiety of okaramine C. The cytochrome P450 monooxygenase okaD then likely catalyzes formation of the eight-membered ring of okaramine A. The dioxygenase okaE further forms the unusual 2-dimethyl-3-methyl-azetidine ring to yield 12- deshydroxyl okaramine E, as well as the hydroxylation of 12-deshydroxyl okaramine E to produce okaramine E. The cytochrome P450 monoxygenase okaG converts 12-deshydroxyl okaramine E into 3-desmethyl okaramine B which is further methylated by the methyltransferase okaF into okaramine B. In a shunt pathway, okaG and okaF together are also able to convert okaramine E into okaramine D. Okaramine H is produced by nonenzymatic conversion from okaramine A.",,,,,,,GO:0071949; GO:0004497,GO:0004497,GO:0004497,GO:0004497; GO:0071949,GO:0004497; GO:0071949,GO:0004497,0.6988,0.6988,1.0,1.0,0.6988,5,0.8193,0.1848,no
TRPM_PSISE,A0A346RP51,ESM2Text,Eukaryota,358,"Methyltransferase that catalyzes iterative L-tryptophan N- methylations to produce L-abrine (N-alpha-methyl-L-tryptophan) and N,N- alpha-dimethyl-L-tryptophan. Also catalyzes a third methylation to yield L-hypaphorine (N,N,N-alpha- trimethyl-L-tryptophan), an agonist of the phytohormone indole-3-acetic acid (Probable). Can also N-methylate the non-native amino acid substrate 4-hydroxytryptophan, but the ability to incorporate trpM into a functional psilocybin biosynthesis pathway is indeed thwarted by the inability of the L-tryptophan decarboxylase psiD to use N,N-dimethyl-4- hydroxytryptophan as substrate.","Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.",No,No,No,No,No,not-Yes,GO:0008168,GO:0008964,GO:0008964,GO:0008948,GO:0008964,GO:0008964,0.2067,0.2067,0.2353,0.2067,0.2067,5,0.2124,0.178,no
TRPM_PSISE,A0A346RP51,Prot2Text,Eukaryota,358,"Methyltransferase that catalyzes iterative L-tryptophan N- methylations to produce L-abrine (N-alpha-methyl-L-tryptophan) and N,N- alpha-dimethyl-L-tryptophan. Also catalyzes a third methylation to yield L-hypaphorine (N,N,N-alpha- trimethyl-L-tryptophan), an agonist of the phytohormone indole-3-acetic acid (Probable). Can also N-methylate the non-native amino acid substrate 4-hydroxytryptophan, but the ability to incorporate trpM into a functional psilocybin biosynthesis pathway is indeed thwarted by the inability of the L-tryptophan decarboxylase psiD to use N,N-dimethyl-4- hydroxytryptophan as substrate.",Might be involved in temporal and/or spatial regulation of nitrogen fixation. Dimerization is required for DNA-binding. Has both a protease and a DNA-binding activity.,No,No,No,No,No,not-Yes,GO:0008168,GO:0008233; GO:0003677,GO:0008233; GO:0003677,GO:0008233; GO:0003677,GO:0008233; GO:0003677,GO:0003677; GO:0008233,0.243,0.243,0.243,0.243,0.243,5,0.243,0.178,no
TRPM_PSISE,A0A346RP51,ProtT3,Eukaryota,358,"Methyltransferase that catalyzes iterative L-tryptophan N- methylations to produce L-abrine (N-alpha-methyl-L-tryptophan) and N,N- alpha-dimethyl-L-tryptophan. Also catalyzes a third methylation to yield L-hypaphorine (N,N,N-alpha- trimethyl-L-tryptophan), an agonist of the phytohormone indole-3-acetic acid (Probable). Can also N-methylate the non-native amino acid substrate 4-hydroxytryptophan, but the ability to incorporate trpM into a functional psilocybin biosynthesis pathway is indeed thwarted by the inability of the L-tryptophan decarboxylase psiD to use N,N-dimethyl-4- hydroxytryptophan as substrate.",S-adenosyl-L-methionine-dependent methyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms,Maybe,No,Yes,No,Maybe,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008757,GO:0008757,GO:0008168,1.0,1.0,0.8582,0.8582,1.0,5,0.9433,0.178,no
TRPM_PSISE,A0A346RP51,ProtTale,Eukaryota,358,"Methyltransferase that catalyzes iterative L-tryptophan N- methylations to produce L-abrine (N-alpha-methyl-L-tryptophan) and N,N- alpha-dimethyl-L-tryptophan. Also catalyzes a third methylation to yield L-hypaphorine (N,N,N-alpha- trimethyl-L-tryptophan), an agonist of the phytohormone indole-3-acetic acid (Probable). Can also N-methylate the non-native amino acid substrate 4-hydroxytryptophan, but the ability to incorporate trpM into a functional psilocybin biosynthesis pathway is indeed thwarted by the inability of the L-tryptophan decarboxylase psiD to use N,N-dimethyl-4- hydroxytryptophan as substrate.","Oxidoreductase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",No,No,No,No,No,not-Yes,GO:0008168,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4071,0.4071,0.4071,0.4071,0.4071,5,0.4071,0.178,no
TRPM_PSISE,A0A346RP51,Protein2Text,Eukaryota,358,"Methyltransferase that catalyzes iterative L-tryptophan N- methylations to produce L-abrine (N-alpha-methyl-L-tryptophan) and N,N- alpha-dimethyl-L-tryptophan. Also catalyzes a third methylation to yield L-hypaphorine (N,N,N-alpha- trimethyl-L-tryptophan), an agonist of the phytohormone indole-3-acetic acid (Probable). Can also N-methylate the non-native amino acid substrate 4-hydroxytryptophan, but the ability to incorporate trpM into a functional psilocybin biosynthesis pathway is indeed thwarted by the inability of the L-tryptophan decarboxylase psiD to use N,N-dimethyl-4- hydroxytryptophan as substrate.","This protein is involved in the process of methyltransferase activity, specifically in the transfer of methyl groups to other molecules. More specifically, it is a methyltransferase that is involved in the methylation of proteins.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008276,1.0,1.0,1.0,1.0,0.7822,5,0.9564,0.178,no
TRPM_PSISE,A0A346RP51,Reference,Eukaryota,358,"Methyltransferase that catalyzes iterative L-tryptophan N- methylations to produce L-abrine (N-alpha-methyl-L-tryptophan) and N,N- alpha-dimethyl-L-tryptophan. Also catalyzes a third methylation to yield L-hypaphorine (N,N,N-alpha- trimethyl-L-tryptophan), an agonist of the phytohormone indole-3-acetic acid (Probable). Can also N-methylate the non-native amino acid substrate 4-hydroxytryptophan, but the ability to incorporate trpM into a functional psilocybin biosynthesis pathway is indeed thwarted by the inability of the L-tryptophan decarboxylase psiD to use N,N-dimethyl-4- hydroxytryptophan as substrate.","Methyltransferase that catalyzes iterative L-tryptophan N- methylations to produce L-abrine (N-alpha-methyl-L-tryptophan) and N,N- alpha-dimethyl-L-tryptophan. Also catalyzes a third methylation to yield L-hypaphorine (N,N,N-alpha- trimethyl-L-tryptophan), an agonist of the phytohormone indole-3-acetic acid (Probable). Can also N-methylate the non-native amino acid substrate 4-hydroxytryptophan, but the ability to incorporate trpM into a functional psilocybin biosynthesis pathway is indeed thwarted by the inability of the L-tryptophan decarboxylase psiD to use N,N-dimethyl-4- hydroxytryptophan as substrate.",,,,,,,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.178,no
PHIG_FUNX7,A0A348HAY2,ESM2Text,Eukaryota,364,"Part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. The function of phiG within the pathway has still to be determined (Probable). The pathway begins with the highly reducing polyketide synthase phiA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase phiM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) phiJ and the alkylcitrate dehydratase (ACDH) phiI then give rise to decarboxylated monomeric anhydrides by coupling the C12-fatty acyl chain with oxalacetic acid. The cyclase phiC is responsible for the dimerization of the monomeric anhydrides which leads to the production of prephomoidride that contains the characteristic bicyclo[4.3.1]deca-1,6- diene system of phomoidrides. Iterative oxidation catalyzed by the alpha-ketoglutarate-dependent dioxygenase phiK produced then phomoidride A. Finally, the methyltransferase phiE converts phomoidride A to phomoidride B via an acetalization reaction. The phosphatidylethanolamine-binding protein phiB and phiN are not essential for dimerization and their functions have still to be determined (Probable).","Exhibits esterase activity toward the tricarbonyl group of substrates including the natural oils cellobiose, olivetol, and steryl-CoA, but not the plant oils phosphorylated to some extent.",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0106435,GO:0016788,GO:0004091,GO:0004091,GO:0004091,GO:0016788,0.729,0.8582,0.8582,0.8582,0.729,5,0.8065,0.1453,no
PHIG_FUNX7,A0A348HAY2,Prot2Text,Eukaryota,364,"Part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. The function of phiG within the pathway has still to be determined (Probable). The pathway begins with the highly reducing polyketide synthase phiA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase phiM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) phiJ and the alkylcitrate dehydratase (ACDH) phiI then give rise to decarboxylated monomeric anhydrides by coupling the C12-fatty acyl chain with oxalacetic acid. The cyclase phiC is responsible for the dimerization of the monomeric anhydrides which leads to the production of prephomoidride that contains the characteristic bicyclo[4.3.1]deca-1,6- diene system of phomoidrides. Iterative oxidation catalyzed by the alpha-ketoglutarate-dependent dioxygenase phiK produced then phomoidride A. Finally, the methyltransferase phiE converts phomoidride A to phomoidride B via an acetalization reaction. The phosphatidylethanolamine-binding protein phiB and phiN are not essential for dimerization and their functions have still to be determined (Probable).","Lipase involved in the degradation of complex natural cellulosic substrates. Able to catalyze the release of acyl groups from (1) cutin, (2) aliphatic alcohols and (3) lignin.",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0106435,GO:0004806,GO:0016298,GO:0004806,GO:0004806,GO:0004806,0.6576,0.6029,0.6576,0.6576,0.6576,5,0.6467,0.1453,no
PHIG_FUNX7,A0A348HAY2,ProtT3,Eukaryota,364,"Part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. The function of phiG within the pathway has still to be determined (Probable). The pathway begins with the highly reducing polyketide synthase phiA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase phiM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) phiJ and the alkylcitrate dehydratase (ACDH) phiI then give rise to decarboxylated monomeric anhydrides by coupling the C12-fatty acyl chain with oxalacetic acid. The cyclase phiC is responsible for the dimerization of the monomeric anhydrides which leads to the production of prephomoidride that contains the characteristic bicyclo[4.3.1]deca-1,6- diene system of phomoidrides. Iterative oxidation catalyzed by the alpha-ketoglutarate-dependent dioxygenase phiK produced then phomoidride A. Finally, the methyltransferase phiE converts phomoidride A to phomoidride B via an acetalization reaction. The phosphatidylethanolamine-binding protein phiB and phiN are not essential for dimerization and their functions have still to be determined (Probable).",Catalyzes the hydrolysis of esters. Secreted. Belongs to the AB hydrolase superfamily. Lipase family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0106435,GO:0016298,GO:0004806,GO:0016298,GO:0016788,GO:0016298,0.6029,0.6576,0.6029,0.729,0.6029,5,0.6391,0.1453,no
PHIG_FUNX7,A0A348HAY2,ProtTale,Eukaryota,364,"Part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. The function of phiG within the pathway has still to be determined (Probable). The pathway begins with the highly reducing polyketide synthase phiA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase phiM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) phiJ and the alkylcitrate dehydratase (ACDH) phiI then give rise to decarboxylated monomeric anhydrides by coupling the C12-fatty acyl chain with oxalacetic acid. The cyclase phiC is responsible for the dimerization of the monomeric anhydrides which leads to the production of prephomoidride that contains the characteristic bicyclo[4.3.1]deca-1,6- diene system of phomoidrides. Iterative oxidation catalyzed by the alpha-ketoglutarate-dependent dioxygenase phiK produced then phomoidride A. Finally, the methyltransferase phiE converts phomoidride A to phomoidride B via an acetalization reaction. The phosphatidylethanolamine-binding protein phiB and phiN are not essential for dimerization and their functions have still to be determined (Probable).","Involved in the degradation of the cell wall (Probable). Catalyzes the hydrolysis of trans,trans-muconic acid (t,t-MA), which is a major component of the cell walls of a variety of Gram-positive bacteria. Catalyzes the hydrolysis of t,t-MA to yield trans,trans-muconic acid (t,t-MA), which is subsequently hydrolyzed to yield 3,4-dihydroxybenzoic acid (3,4-DHBA).",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0106435,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016787,0.6019,0.6019,0.6019,0.6019,0.6019,5,0.6019,0.1453,no
PHIG_FUNX7,A0A348HAY2,Protein2Text,Eukaryota,364,"Part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. The function of phiG within the pathway has still to be determined (Probable). The pathway begins with the highly reducing polyketide synthase phiA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase phiM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) phiJ and the alkylcitrate dehydratase (ACDH) phiI then give rise to decarboxylated monomeric anhydrides by coupling the C12-fatty acyl chain with oxalacetic acid. The cyclase phiC is responsible for the dimerization of the monomeric anhydrides which leads to the production of prephomoidride that contains the characteristic bicyclo[4.3.1]deca-1,6- diene system of phomoidrides. Iterative oxidation catalyzed by the alpha-ketoglutarate-dependent dioxygenase phiK produced then phomoidride A. Finally, the methyltransferase phiE converts phomoidride A to phomoidride B via an acetalization reaction. The phosphatidylethanolamine-binding protein phiB and phiN are not essential for dimerization and their functions have still to be determined (Probable).","This protein is involved in catalyzing the cleavage of the glycosidic bond in a polysaccharide, specifically the cleavage of the alpha-1,4-glycosidic bond in polysaccharides such as starch, glycogen, and amylopectin. This is a key function in the degradation of complex carbohydrates, allowing the cell to break down and utilize these molecules as energy sources. The molecular function of this protein is therefore glycosidase activity, specifically alpha-glucosidase activity.",Maybe,No,Maybe,No,No,not-Yes,GO:0106435,GO:0004553,GO:0004553,GO:0004553,GO:0004553,GO:0004558,0.3987,0.3987,0.3987,0.3987,0.261,5,0.3712,0.1453,no
PHIG_FUNX7,A0A348HAY2,Reference,Eukaryota,364,"Part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. The function of phiG within the pathway has still to be determined (Probable). The pathway begins with the highly reducing polyketide synthase phiA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase phiM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) phiJ and the alkylcitrate dehydratase (ACDH) phiI then give rise to decarboxylated monomeric anhydrides by coupling the C12-fatty acyl chain with oxalacetic acid. The cyclase phiC is responsible for the dimerization of the monomeric anhydrides which leads to the production of prephomoidride that contains the characteristic bicyclo[4.3.1]deca-1,6- diene system of phomoidrides. Iterative oxidation catalyzed by the alpha-ketoglutarate-dependent dioxygenase phiK produced then phomoidride A. Finally, the methyltransferase phiE converts phomoidride A to phomoidride B via an acetalization reaction. The phosphatidylethanolamine-binding protein phiB and phiN are not essential for dimerization and their functions have still to be determined (Probable).","Part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. The function of phiG within the pathway has still to be determined (Probable). The pathway begins with the highly reducing polyketide synthase phiA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase phiM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) phiJ and the alkylcitrate dehydratase (ACDH) phiI then give rise to decarboxylated monomeric anhydrides by coupling the C12-fatty acyl chain with oxalacetic acid. The cyclase phiC is responsible for the dimerization of the monomeric anhydrides which leads to the production of prephomoidride that contains the characteristic bicyclo[4.3.1]deca-1,6- diene system of phomoidrides. Iterative oxidation catalyzed by the alpha-ketoglutarate-dependent dioxygenase phiK produced then phomoidride A. Finally, the methyltransferase phiE converts phomoidride A to phomoidride B via an acetalization reaction. The phosphatidylethanolamine-binding protein phiB and phiN are not essential for dimerization and their functions have still to be determined (Probable).",,,,,,,GO:0106435,,,,,,,,,,,0,,0.1453,no
PHIM_FUNX7,A0A348HAY8,ESM2Text,Eukaryota,208,"Hydrolase; part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. Within the pathway, phiM releases the C12-fatty acyl chain from phiA (Probable). The pathway begins with the highly reducing polyketide synthase phiA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase phiM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) phiJ and the alkylcitrate dehydratase (ACDH) phiI then give rise to decarboxylated monomeric anhydrides by coupling the C12-fatty acyl chain with oxalacetic acid. The cyclase phiC is responsible for the dimerization of the monomeric anhydrides which leads to the production of prephomoidride that contains the characteristic bicyclo[4.3.1]deca- 1,6-diene system of phomoidrides. Iterative oxidation catalyzed by the alpha-ketoglutarate-dependent dioxygenase phiK produced then phomoidride A. Finally, the methyltransferase phiE converts phomoidride A to phomoidride B via an acetalization reaction. The phosphatidylethanolamine-binding protein phiB and phiN are not essential for dimerization and their functions have still to be determined (Probable).","Thioesterase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016787,GO:0016790,GO:0016790,GO:0016790,GO:0016790,GO:0016790,0.6897,0.6897,0.6897,0.6897,0.6897,5,0.6897,0.5405,yes
PHIM_FUNX7,A0A348HAY8,Prot2Text,Eukaryota,208,"Hydrolase; part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. Within the pathway, phiM releases the C12-fatty acyl chain from phiA (Probable). The pathway begins with the highly reducing polyketide synthase phiA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase phiM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) phiJ and the alkylcitrate dehydratase (ACDH) phiI then give rise to decarboxylated monomeric anhydrides by coupling the C12-fatty acyl chain with oxalacetic acid. The cyclase phiC is responsible for the dimerization of the monomeric anhydrides which leads to the production of prephomoidride that contains the characteristic bicyclo[4.3.1]deca- 1,6-diene system of phomoidrides. Iterative oxidation catalyzed by the alpha-ketoglutarate-dependent dioxygenase phiK produced then phomoidride A. Finally, the methyltransferase phiE converts phomoidride A to phomoidride B via an acetalization reaction. The phosphatidylethanolamine-binding protein phiB and phiN are not essential for dimerization and their functions have still to be determined (Probable).",Serine hydrolase of unknown specificity.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787,GO:0017171,GO:0017171,GO:0017171,GO:0017171,GO:0017171,0.8145,0.8145,0.8145,0.8145,0.8145,5,0.8145,0.5405,yes
PHIM_FUNX7,A0A348HAY8,ProtT3,Eukaryota,208,"Hydrolase; part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. Within the pathway, phiM releases the C12-fatty acyl chain from phiA (Probable). The pathway begins with the highly reducing polyketide synthase phiA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase phiM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) phiJ and the alkylcitrate dehydratase (ACDH) phiI then give rise to decarboxylated monomeric anhydrides by coupling the C12-fatty acyl chain with oxalacetic acid. The cyclase phiC is responsible for the dimerization of the monomeric anhydrides which leads to the production of prephomoidride that contains the characteristic bicyclo[4.3.1]deca- 1,6-diene system of phomoidrides. Iterative oxidation catalyzed by the alpha-ketoglutarate-dependent dioxygenase phiK produced then phomoidride A. Finally, the methyltransferase phiE converts phomoidride A to phomoidride B via an acetalization reaction. The phosphatidylethanolamine-binding protein phiB and phiN are not essential for dimerization and their functions have still to be determined (Probable).","E3 ubiquitin-protein ligase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties",No,No,No,No,No,not-Yes,GO:0016787,GO:0061630,GO:0004842,GO:0061630,GO:0061630,GO:0061630,0.2662,0.3207,0.2662,0.2662,0.2662,5,0.2771,0.5405,yes
PHIM_FUNX7,A0A348HAY8,ProtTale,Eukaryota,208,"Hydrolase; part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. Within the pathway, phiM releases the C12-fatty acyl chain from phiA (Probable). The pathway begins with the highly reducing polyketide synthase phiA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase phiM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) phiJ and the alkylcitrate dehydratase (ACDH) phiI then give rise to decarboxylated monomeric anhydrides by coupling the C12-fatty acyl chain with oxalacetic acid. The cyclase phiC is responsible for the dimerization of the monomeric anhydrides which leads to the production of prephomoidride that contains the characteristic bicyclo[4.3.1]deca- 1,6-diene system of phomoidrides. Iterative oxidation catalyzed by the alpha-ketoglutarate-dependent dioxygenase phiK produced then phomoidride A. Finally, the methyltransferase phiE converts phomoidride A to phomoidride B via an acetalization reaction. The phosphatidylethanolamine-binding protein phiB and phiN are not essential for dimerization and their functions have still to be determined (Probable).","Essential for viability. Catalyzes the hydrolysis of the ester bond between the amino group of lysine and the carboxyl group of myristoyl-CoA, forming N-myristoylglutamate and CoA. Also catalyzes the hydrolysis of myristoyl-CoA into free fatty acid and CoA.",Maybe,Maybe,Yes,No,Maybe,not-Yes,GO:0016787,GO:0016790,GO:0016787,GO:0016790,GO:0016790,GO:0016787,0.6897,1.0,0.6897,0.6897,1.0,5,0.8138,0.5405,yes
PHIM_FUNX7,A0A348HAY8,Protein2Text,Eukaryota,208,"Hydrolase; part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. Within the pathway, phiM releases the C12-fatty acyl chain from phiA (Probable). The pathway begins with the highly reducing polyketide synthase phiA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase phiM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) phiJ and the alkylcitrate dehydratase (ACDH) phiI then give rise to decarboxylated monomeric anhydrides by coupling the C12-fatty acyl chain with oxalacetic acid. The cyclase phiC is responsible for the dimerization of the monomeric anhydrides which leads to the production of prephomoidride that contains the characteristic bicyclo[4.3.1]deca- 1,6-diene system of phomoidrides. Iterative oxidation catalyzed by the alpha-ketoglutarate-dependent dioxygenase phiK produced then phomoidride A. Finally, the methyltransferase phiE converts phomoidride A to phomoidride B via an acetalization reaction. The phosphatidylethanolamine-binding protein phiB and phiN are not essential for dimerization and their functions have still to be determined (Probable).","The molecular function of this protein is not explicitly stated in the provided text. However, based on its name, it can be inferred that it is a hydrolase, specifically a deacetylase, which is an enzyme that removes an acetyl group from a molecule. This is a common function for proteins that are named as ""deacetylase"" or similar, and it is often associated with the removal of acetyl groups from histones or other proteins. 

However, it would be more accurate to provide a direct quote from a reliable source confirming this function. 

If you have any other question, please let me know.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787,,,,,,,,,,,0,,0.5405,yes
PHIM_FUNX7,A0A348HAY8,Reference,Eukaryota,208,"Hydrolase; part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. Within the pathway, phiM releases the C12-fatty acyl chain from phiA (Probable). The pathway begins with the highly reducing polyketide synthase phiA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase phiM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) phiJ and the alkylcitrate dehydratase (ACDH) phiI then give rise to decarboxylated monomeric anhydrides by coupling the C12-fatty acyl chain with oxalacetic acid. The cyclase phiC is responsible for the dimerization of the monomeric anhydrides which leads to the production of prephomoidride that contains the characteristic bicyclo[4.3.1]deca- 1,6-diene system of phomoidrides. Iterative oxidation catalyzed by the alpha-ketoglutarate-dependent dioxygenase phiK produced then phomoidride A. Finally, the methyltransferase phiE converts phomoidride A to phomoidride B via an acetalization reaction. The phosphatidylethanolamine-binding protein phiB and phiN are not essential for dimerization and their functions have still to be determined (Probable).","Hydrolase; part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. Within the pathway, phiM releases the C12-fatty acyl chain from phiA (Probable). The pathway begins with the highly reducing polyketide synthase phiA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase phiM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) phiJ and the alkylcitrate dehydratase (ACDH) phiI then give rise to decarboxylated monomeric anhydrides by coupling the C12-fatty acyl chain with oxalacetic acid. The cyclase phiC is responsible for the dimerization of the monomeric anhydrides which leads to the production of prephomoidride that contains the characteristic bicyclo[4.3.1]deca- 1,6-diene system of phomoidrides. Iterative oxidation catalyzed by the alpha-ketoglutarate-dependent dioxygenase phiK produced then phomoidride A. Finally, the methyltransferase phiE converts phomoidride A to phomoidride B via an acetalization reaction. The phosphatidylethanolamine-binding protein phiB and phiN are not essential for dimerization and their functions have still to be determined (Probable).",,,,,,,GO:0016787,GO:0016787,GO:0016790,GO:0016790,GO:0016787,GO:0016787,1.0,0.6897,0.6897,1.0,1.0,5,0.8759,0.5405,yes
THIOL_METTL,A0A384E138,ESM2Text,Archaea,392,"Catalyzes the condensation of two acetyl-coA molecules into acetoacetyl-CoA. Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds that are building blocks of archaeal membrane lipids.","Involved in the biosynthesis of the non-bilayer-prone membrane lipid beta-monoglucosyldiacylglycerol (LPG), the precursor of the teichoic acid-containing lipopeptide antibiotic, virginiamycin. Catalyzes the acyl-CoA thiolytic cleavage of the beta-glyceran (C2) and beta-tubulace (C4) of LPG to yield beta-acetyl-LPG (C2). It can also use acetyl-CoA and butanoyl-CoA as acyl donors.",No,Maybe,No,No,No,not-Yes,GO:0003985,,,,GO:0003988,,,,,0.7446,,1,0.7446,0.1632,no
THIOL_METTL,A0A384E138,Prot2Text,Archaea,392,"Catalyzes the condensation of two acetyl-coA molecules into acetoacetyl-CoA. Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds that are building blocks of archaeal membrane lipids.",Probably involved in long chain fatty acid beta-oxidation prior to gluconeogenesis during germination and subsequent seedling growth.,Maybe,No,Maybe,No,Maybe,not-Yes,GO:0003985,,,,,,,,,,,0,,0.1632,no
THIOL_METTL,A0A384E138,ProtT3,Archaea,392,"Catalyzes the condensation of two acetyl-coA molecules into acetoacetyl-CoA. Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds that are building blocks of archaeal membrane lipids.",Belongs to the thiolase-like superfamily. Thiolase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0003985,GO:0003985,GO:0003985,GO:0003988,GO:0003985,GO:0003985,1.0,1.0,0.7446,1.0,1.0,5,0.9489,0.1632,no
THIOL_METTL,A0A384E138,ProtTale,Archaea,392,"Catalyzes the condensation of two acetyl-coA molecules into acetoacetyl-CoA. Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds that are building blocks of archaeal membrane lipids.","Component of the BbsAB thiolase complex, which catalyzes the thiolytic cleavage of (S)-2-butenoyl-CoA to form (2R,3S)-2,3-dihydroxybutanoyl-CoA, the intermediate in fatty acid synthesis. The BbsA subunit catalyzes the transfer of the thioester moiety from CoA to the carrier protein (CP) domain of BbsB to form the covalent thioester bond.",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0003985,GO:0016746,GO:0016747,GO:0016747,GO:0016747,GO:0003988,0.4865,0.5671,0.5671,0.5671,0.7446,5,0.5865,0.1632,no
THIOL_METTL,A0A384E138,Protein2Text,Archaea,392,"Catalyzes the condensation of two acetyl-coA molecules into acetoacetyl-CoA. Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds that are building blocks of archaeal membrane lipids.","This protein is involved in the molecular function of catalyzing the condensation reaction of fatty acid synthesis. Specifically, it is a condensing enzyme that catalyzes the addition of acetyl-CoA to malonyl-CoA to form acetoacetyl-CoA, a key step in the synthesis of fatty acids.",Maybe,No,No,Maybe,Maybe,not-Yes,GO:0003985,GO:0004315,GO:0016747,GO:0016747,GO:0004315,GO:0004315,0.4747,0.5671,0.5671,0.4747,0.4747,5,0.5117,0.1632,no
THIOL_METTL,A0A384E138,Reference,Archaea,392,"Catalyzes the condensation of two acetyl-coA molecules into acetoacetyl-CoA. Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds that are building blocks of archaeal membrane lipids.","Catalyzes the condensation of two acetyl-coA molecules into acetoacetyl-CoA. Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds that are building blocks of archaeal membrane lipids.",,,,,,,GO:0003985,GO:0003985,GO:0003985,GO:0003985,GO:0003985,GO:0003985,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1632,no
HMGCS_METTL,A0A384E143,ESM2Text,Archaea,349,"Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA to form 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds that are building blocks of archaeal membrane lipids.",Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.,No,Maybe,No,No,No,not-Yes,GO:0003985; GO:0004421,GO:0004315,GO:0004315,GO:0004315,GO:0004315,GO:0004315,0.4996,0.4996,0.4996,0.4996,0.4996,5,0.4996,0.2591,no
HMGCS_METTL,A0A384E143,Prot2Text,Archaea,349,"Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA to form 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds that are building blocks of archaeal membrane lipids.","Cleaves acetyl-CoA, propionyl-CoA and butyryl-CoA, and not acetoacetyl-CoA. Not involved in the anaerobic degradation of straight-chain fatty acids.",No,No,No,No,No,not-Yes,GO:0003985; GO:0004421,GO:0016790,GO:0016790,GO:0016790,GO:0016790,GO:0016790,0.2087,0.2087,0.2087,0.2087,0.2087,5,0.2087,0.2591,no
HMGCS_METTL,A0A384E143,ProtT3,Archaea,349,"Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA to form 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds that are building blocks of archaeal membrane lipids.",Belongs to the thiolase-like superfamily. UPF0219 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0003985; GO:0004421,,,,,,,,,,,0,,0.2591,no
HMGCS_METTL,A0A384E143,ProtTale,Archaea,349,"Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA to form 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds that are building blocks of archaeal membrane lipids.","Catalyzes the condensation of acetyl-CoA with malonyl-CoA, forming 3-oxoadipyl-CoA.",No,Maybe,No,Maybe,Maybe,not-Yes,GO:0003985; GO:0004421,GO:0016747,GO:0016747,GO:0016747,GO:0016747,GO:0016747,0.591,0.591,0.591,0.591,0.591,5,0.591,0.2591,no
HMGCS_METTL,A0A384E143,Protein2Text,Archaea,349,"Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA to form 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds that are building blocks of archaeal membrane lipids.","This protein is a 3-ketoacyl-CoA thiolase, which catalyzes the cleavage of 3-oxoacyl-CoA to form acetyl-CoA and an acyl-CoA with one less carbon atom. It is a key enzyme in the beta-oxidation of fatty acids.",No,No,No,No,No,not-Yes,GO:0003985; GO:0004421,GO:0003988,GO:0003988,GO:0003988,GO:0003988,GO:0003988,0.6447,0.6447,0.6447,0.6447,0.6447,5,0.6447,0.2591,no
HMGCS_METTL,A0A384E143,Reference,Archaea,349,"Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA to form 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds that are building blocks of archaeal membrane lipids.","Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA to form 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds that are building blocks of archaeal membrane lipids.",,,,,,,GO:0003985; GO:0004421,GO:0004419,GO:0004421,GO:0004421,GO:0004421,GO:0004421,0.1766,0.7778,0.7778,0.7778,0.7778,5,0.6576,0.2591,no
LP9B_BOTFB,A0A384JJE6,ESM2Text,Eukaryota,322,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable).",Lignin degradation and detoxification of lignin-derived products.,Vague,No,No,No,No,not-Yes,GO:0046872; GO:0004497,GO:0008810,GO:0008810,,GO:0008810,GO:0008810,0.2193,0.2193,,0.2193,0.2193,4,0.2193,0.2984,no
LP9B_BOTFB,A0A384JJE6,Prot2Text,Eukaryota,322,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable).",Is thought to be an important plant defense-related product against fungal pathogens.,Vague,No,Vague,No,Vague,not-Yes,GO:0046872; GO:0004497,GO:0004553,GO:0004338,GO:0016798,GO:0004553,GO:0042973,0.2538,0.175,0.3023,0.2538,0.175,5,0.232,0.2984,no
LP9B_BOTFB,A0A384JJE6,ProtT3,Eukaryota,322,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable).","Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates (By similarity). Secreted. Belongs to the glycosyl hydrolase 71 family",Maybe,No,No,Maybe,Maybe,not-Yes,GO:0046872; GO:0004497,GO:0008810,GO:0008810,GO:0008810,GO:0008810,GO:0008810,0.2193,0.2193,0.2193,0.2193,0.2193,5,0.2193,0.2984,no
LP9B_BOTFB,A0A384JJE6,ProtTale,Eukaryota,322,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable).","Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0004497,GO:0004497,GO:0016491; GO:0005507,GO:0016491; GO:0005507,GO:0004497; GO:0005507,GO:0004497,0.7088,0.7926,0.7926,0.8854,0.7088,5,0.7776,0.2984,no
LP9B_BOTFB,A0A384JJE6,Protein2Text,Eukaryota,322,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable).","The molecular function of this protein is to break down chitin, a polysaccharide found in the cell walls of fungi and exoskeletons of arthropods, during the process of decomposition. Specifically, it is involved in the hydrolysis of chitin into simpler sugars. 
This protein is likely a lytic polysaccharide monooxygenase (LPMO), an enzyme that catalyzes the oxidative cleavage of polysaccharides and is involved in the degradation of complex carbohydrates. LPMOs use molecular oxygen and a reducing agent to cleave the glycosidic bonds in polysaccharides, and are often used in conjunction with other enzymes to break down complex carbohydrates into simpler sugars. The breakdown of chitin by LPMOs is an important step in the decomposition of organic matter and is also used by fungi and other microorganisms to obtain nutrients from their environment.",No,Maybe,Maybe,No,No,not-Yes,GO:0046872; GO:0004497,GO:0008810; GO:0030248,GO:0016162,GO:0016162; GO:0030245,GO:0016162,GO:0008810,0.2599,0.2193,0.1644,0.2193,0.2193,5,0.2164,0.2984,no
LP9B_BOTFB,A0A384JJE6,Reference,Eukaryota,322,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable).","Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable).",,,,,,,GO:0046872; GO:0004497,GO:0016491; GO:0005507,GO:0016491,GO:0016491; GO:0005507,GO:0016491; GO:0005507,GO:0016491,0.7926,0.5957,0.7926,0.7926,0.5957,5,0.7138,0.2984,no
LP9H_BOTFB,A0A384JZ02,ESM2Text,Eukaryota,437,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable).","Involved in degradation of plant cell walls. Catalyzes the endoglucan-dependent transfer of cellulose from the degradation of cellulose to the non-reducing end of the cellulose polymer chain. It acts on both beta-1,4- and beta-1,6-glucan.",Maybe,No,No,No,No,not-Yes,GO:0008061; GO:0046872; GO:0004497,GO:0008810,GO:0008810,,GO:0008810,GO:0008810,0.1961,0.1961,,0.1961,0.1961,4,0.1961,0.3163,no
LP9H_BOTFB,A0A384JZ02,Prot2Text,Eukaryota,437,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable).","Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. EXG2 is not required for the addition of further glucanases.",No,No,No,No,No,not-Yes,GO:0008061; GO:0046872; GO:0004497,GO:0004553,GO:0004338,GO:0016798,GO:0004553,GO:0042973,0.2269,0.1566,0.2701,0.2269,0.1566,5,0.2074,0.3163,no
LP9H_BOTFB,A0A384JZ02,ProtT3,Eukaryota,437,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable).","Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in degradation of complex natural cellulosic substrates (By similarity). Secreted. Belongs to the glycosyl hydrolase 61 family",Maybe,No,No,Maybe,Maybe,not-Yes,GO:0008061; GO:0046872; GO:0004497,GO:0008810,GO:0008810,GO:0008810,GO:0008810,GO:0008810,0.1961,0.1961,0.1961,0.1961,0.1961,5,0.1961,0.3163,no
LP9H_BOTFB,A0A384JZ02,ProtTale,Eukaryota,437,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable).","Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008061; GO:0046872; GO:0004497,GO:0004497,GO:0016491; GO:0005507,GO:0016491; GO:0005507,GO:0004497; GO:0005507,GO:0004497,0.575,0.6798,0.6798,0.7539,0.575,5,0.6527,0.3163,no
LP9H_BOTFB,A0A384JZ02,Protein2Text,Eukaryota,437,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable).","The molecular function of this protein is to catalyze the breakdown of cellulose, a type of complex carbohydrate, into simpler sugars. More specifically, it is involved in the degradation of cellulose by breaking down the beta-1,4 glycosidic bonds between glucose molecules. This is a key step in the degradation of plant biomass and is important for the breakdown and utilization of cellulose as a nutrient source. The protein is likely a beta-1,4 endoglucanase, which is a type of enzyme that catalyzes the hydrolysis of beta-1,4 glycosidic bonds in cellulose. 
In other words, the protein is a beta-1,4 endoglucanase, which is a type of hydrolase enzyme that catalyzes the hydrolysis of beta-1,4 glycosidic bonds in cellulose.",Vague,No,Maybe,No,Maybe,not-Yes,GO:0008061; GO:0046872; GO:0004497,GO:0008810; GO:0030248,GO:0016162,GO:0016162; GO:0030245,GO:0016162,GO:0008810,0.2922,0.1961,0.1568,0.1961,0.1961,5,0.2075,0.3163,no
LP9H_BOTFB,A0A384JZ02,Reference,Eukaryota,437,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable).","Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable).",,,,,,,GO:0008061; GO:0046872; GO:0004497,GO:0016491; GO:0005507,GO:0016491,GO:0016491; GO:0005507,GO:0016491; GO:0005507,GO:0016491,0.6798,0.5002,0.6798,0.6798,0.5002,5,0.608,0.3163,no
EIX2_BOTFB,A0A384K474,ESM2Text,Eukaryota,222,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. May act as an elicitor of plant defense responses in certain plants but does not exhibit any cell death when transiently expressed in N.benthamiana.",Thought to be a carbohydrate-binding protein with a role in the initial stage of autolysis.,Vague,No,Vague,No,Vague,not-Yes,GO:0031176,GO:0016798,GO:0004553,GO:0016798,GO:0004553,GO:0016798,0.6466,0.7539,0.6466,0.7539,0.6466,5,0.6895,0.3281,no
EIX2_BOTFB,A0A384K474,Prot2Text,Eukaryota,222,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. May act as an elicitor of plant defense responses in certain plants but does not exhibit any cell death when transiently expressed in N.benthamiana.","Glycoside hydrolase involved in the hydrolysis of xylan, a major plant cell wall hemicellulose made up of 1,4-beta-linked D-xylopyranose residues. Catalyzes the endohydrolysis of the main-chain 1,4-beta-glycosidic bonds connecting the xylose subunits yielding various xylooligosaccharides and xylose.",Yes,Maybe,Yes,Yes,Yes,Yes,GO:0031176,,,,,,,,,,,0,,0.3281,no
EIX2_BOTFB,A0A384K474,ProtT3,Eukaryota,222,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. May act as an elicitor of plant defense responses in certain plants but does not exhibit any cell death when transiently expressed in N.benthamiana.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Secreted. Belongs to the glycosyl hydrolase 11 (cellulase G) family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3281,no
EIX2_BOTFB,A0A384K474,ProtTale,Eukaryota,222,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. May act as an elicitor of plant defense responses in certain plants but does not exhibit any cell death when transiently expressed in N.benthamiana.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3281,no
EIX2_BOTFB,A0A384K474,Protein2Text,Eukaryota,222,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. May act as an elicitor of plant defense responses in certain plants but does not exhibit any cell death when transiently expressed in N.benthamiana.","This protein is involved in the breakdown of cellulose, a process that involves the hydrolysis of the beta-1,4 glycosidic bonds in the cellulose molecule. It is likely involved in the production of hydrolytic enzymes that break down cellulose into simpler sugars, such as cellobiose and glucose. Therefore, its molecular function is likely to be that of a cellulase or a component of a cellulase complex.",No,No,Maybe,No,No,not-Yes,GO:0031176,GO:0008810; GO:0030248,GO:0008422,GO:0008422; GO:0030245,GO:0008810,GO:0008810,0.453,0.5445,0.363,0.6335,0.6335,5,0.5255,0.3281,no
EIX2_BOTFB,A0A384K474,Reference,Eukaryota,222,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. May act as an elicitor of plant defense responses in certain plants but does not exhibit any cell death when transiently expressed in N.benthamiana.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. May act as an elicitor of plant defense responses in certain plants but does not exhibit any cell death when transiently expressed in N.benthamiana.",,,,,,,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3281,no
LAD_AURME,A0A385XI11,ESM2Text,Eukaryota,368,"Plays a key role in liamocins biosynthesis by providing the arabinol moity that is linked to 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) via ester bond formation catalyzed by the esterase EST1.",Catalyzes the NAD(+)-dependent oxidation of L-arabinitol to L-fucose in the presence of NADP(+). Is essential for L-arabinitol utilization as an alternative carbon source. Also acts on D-arabinitol but not D-galactitol. Is unable to use D-sorbitol and L-arabitol as substrates.,Maybe,No,Yes,No,Maybe,not-Yes,GO:0050019; GO:0003939; GO:0046872; GO:0000166,GO:0016491,GO:0016491,GO:0016491,GO:0016491; GO:0051287,GO:0016491,0.4042,0.4042,0.4042,0.5693,0.4042,5,0.4372,0.2203,no
LAD_AURME,A0A385XI11,Prot2Text,Eukaryota,368,"Plays a key role in liamocins biosynthesis by providing the arabinol moity that is linked to 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) via ester bond formation catalyzed by the esterase EST1.",Catalyzes the NAD-dependent oxidation of L-arabinitol to L-xylulose in the fungal L-arabinose catabolic pathway. L-arabinose catabolism is important for using plant material as a carbon source. Not active with NADP as cosubstrate.,Maybe,No,Yes,Maybe,Yes,not-Yes,GO:0050019; GO:0003939; GO:0046872; GO:0000166,GO:0050019,GO:0050019,GO:0016616,GO:0016616,GO:0050019,0.5509,0.5509,0.5231,0.5231,0.5509,5,0.5398,0.2203,no
LAD_AURME,A0A385XI11,ProtT3,Eukaryota,368,"Plays a key role in liamocins biosynthesis by providing the arabinol moity that is linked to 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) via ester bond formation catalyzed by the esterase EST1.",Belongs to the zinc-containing alcohol dehydrogenase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0050019; GO:0003939; GO:0046872; GO:0000166,GO:0004022; GO:0008270,GO:0004022; GO:0008270,GO:0004022; GO:0008270,GO:0004024; GO:0008270,GO:0004024,0.7052,0.7052,0.7052,0.3927,0.0,5,0.5017,0.2203,no
LAD_AURME,A0A385XI11,ProtTale,Eukaryota,368,"Plays a key role in liamocins biosynthesis by providing the arabinol moity that is linked to 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) via ester bond formation catalyzed by the esterase EST1.",Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Can utilize both NAD(+) and NADP(+) as electron acceptor. Is involved in the degradation of glucose via a non-phosphorylative variant of the Entner-Doudoroff pathway.,Maybe,No,No,No,No,not-Yes,GO:0050019; GO:0003939; GO:0046872; GO:0000166,GO:0016614,GO:0016491; GO:0050661,GO:0016614,GO:0016614,GO:0016616,0.4618,0.5693,0.4618,0.4618,0.5231,5,0.4956,0.2203,no
LAD_AURME,A0A385XI11,Protein2Text,Eukaryota,368,"Plays a key role in liamocins biosynthesis by providing the arabinol moity that is linked to 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) via ester bond formation catalyzed by the esterase EST1.","The molecular function of this protein is an enzyme, specifically a ketol-acid reductoisomerase.",No,No,No,No,No,not-Yes,GO:0050019; GO:0003939; GO:0046872; GO:0000166,GO:0004455,GO:0004455,GO:0004455,GO:0004455,GO:0004455,0.4425,0.4425,0.4425,0.4425,0.4425,5,0.4425,0.2203,no
LAD_AURME,A0A385XI11,Reference,Eukaryota,368,"Plays a key role in liamocins biosynthesis by providing the arabinol moity that is linked to 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) via ester bond formation catalyzed by the esterase EST1.","Plays a key role in liamocins biosynthesis by providing the arabinol moity that is linked to 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) via ester bond formation catalyzed by the esterase EST1.",,,,,,,GO:0050019; GO:0003939; GO:0046872; GO:0000166,,,,,,,,,,,0,,0.2203,no
EST1_AURME,A0A385XI13,ESM2Text,Eukaryota,282,"Esterase; part of the gene cluster that mediates the biosynthesis of liamocins, glycolipids (also called heavy oils) composed of a single mannitol or arabitol headgroup linked to either three, four or even six 3,5-dihydroxydecanoic ester tail-groups. Within the pathway, EST1 catalyzes ester bond formation between 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) and mannitol (provided by the mannitol-1-phosphate 5- dehydrogenase and the NADP-dependent mannitol dehydrogenase) or arabinol (provided by the L-arabinitol 4-dehydrogenase).","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-octanoic acid (AntAc), a four-carbon trisaccharide (ATC), four neutral amino acids, one heptapeptide (HepT) and one heptapeptide (TppA). The biosynthesis starts with the assembly of nicotinylbenzoate by the nicotinic acid-CoA ligase albA. The nicotinic acid-CoA ligase albF then forms a tetraketide intermediate. The tetraketide acid is released as an aldehyde through a retro-Claisen type C-C bond cleavage to generate the diene group. The methyl group is probably reduced by a nucleophilic attack of the tetraketide",No,No,No,No,No,not-Yes,GO:0016787,,GO:0016874,GO:0003824,GO:0016874,GO:0016874; GO:0005524,,0.5902,0.7642,0.5902,0.4225,4,0.5918,0.468,no
EST1_AURME,A0A385XI13,Prot2Text,Eukaryota,282,"Esterase; part of the gene cluster that mediates the biosynthesis of liamocins, glycolipids (also called heavy oils) composed of a single mannitol or arabitol headgroup linked to either three, four or even six 3,5-dihydroxydecanoic ester tail-groups. Within the pathway, EST1 catalyzes ester bond formation between 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) and mannitol (provided by the mannitol-1-phosphate 5- dehydrogenase and the NADP-dependent mannitol dehydrogenase) or arabinol (provided by the L-arabinitol 4-dehydrogenase).","Esterase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate tolerance, pyiS",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016787,GO:0016788,GO:0004091,GO:0004091,GO:0016788,GO:0016788,0.8145,0.6897,0.6897,0.8145,0.8145,5,0.7646,0.468,no
EST1_AURME,A0A385XI13,ProtT3,Eukaryota,282,"Esterase; part of the gene cluster that mediates the biosynthesis of liamocins, glycolipids (also called heavy oils) composed of a single mannitol or arabitol headgroup linked to either three, four or even six 3,5-dihydroxydecanoic ester tail-groups. Within the pathway, EST1 catalyzes ester bond formation between 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) and mannitol (provided by the mannitol-1-phosphate 5- dehydrogenase and the NADP-dependent mannitol dehydrogenase) or arabinol (provided by the L-arabinitol 4-dehydrogenase).","Esterase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties . L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L- homoserine by cluster enzymes aspartate kinase FUB5 and homoserine O- acetyltransferase FUB6, as well as enzymes of the primary",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016787,GO:0004091,GO:0016788,GO:0016788,GO:0016788,GO:0016788,0.6897,0.8145,0.8145,0.8145,0.8145,5,0.7895,0.468,no
EST1_AURME,A0A385XI13,ProtTale,Eukaryota,282,"Esterase; part of the gene cluster that mediates the biosynthesis of liamocins, glycolipids (also called heavy oils) composed of a single mannitol or arabitol headgroup linked to either three, four or even six 3,5-dihydroxydecanoic ester tail-groups. Within the pathway, EST1 catalyzes ester bond formation between 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) and mannitol (provided by the mannitol-1-phosphate 5- dehydrogenase and the NADP-dependent mannitol dehydrogenase) or arabinol (provided by the L-arabinitol 4-dehydrogenase).","Esterase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016787,GO:0016788,GO:0016787,GO:0016788,GO:0004091,GO:0016788,0.8145,1.0,0.8145,0.6897,0.8145,5,0.8266,0.468,no
EST1_AURME,A0A385XI13,Protein2Text,Eukaryota,282,"Esterase; part of the gene cluster that mediates the biosynthesis of liamocins, glycolipids (also called heavy oils) composed of a single mannitol or arabitol headgroup linked to either three, four or even six 3,5-dihydroxydecanoic ester tail-groups. Within the pathway, EST1 catalyzes ester bond formation between 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) and mannitol (provided by the mannitol-1-phosphate 5- dehydrogenase and the NADP-dependent mannitol dehydrogenase) or arabinol (provided by the L-arabinitol 4-dehydrogenase).","The molecular function of this protein is unknown. The protein is identified as a component of the eukaryotic translation initiation factor 5A (eIF-5A) processing system, but its specific function is not specified. It is likely involved in the processing of eIF-5A, which is a crucial component of the eukaryotic translation initiation factor complex. However, the exact molecular function of this protein remains to be determined.",No,No,Vague,Vague,Vague,not-Yes,GO:0016787,,,,,,,,,,,0,,0.468,no
EST1_AURME,A0A385XI13,Reference,Eukaryota,282,"Esterase; part of the gene cluster that mediates the biosynthesis of liamocins, glycolipids (also called heavy oils) composed of a single mannitol or arabitol headgroup linked to either three, four or even six 3,5-dihydroxydecanoic ester tail-groups. Within the pathway, EST1 catalyzes ester bond formation between 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) and mannitol (provided by the mannitol-1-phosphate 5- dehydrogenase and the NADP-dependent mannitol dehydrogenase) or arabinol (provided by the L-arabinitol 4-dehydrogenase).","Esterase; part of the gene cluster that mediates the biosynthesis of liamocins, glycolipids (also called heavy oils) composed of a single mannitol or arabitol headgroup linked to either three, four or even six 3,5-dihydroxydecanoic ester tail-groups. Within the pathway, EST1 catalyzes ester bond formation between 3,5-dihydroxydecanoic acid (provided by the HR-PKS PKS1) and mannitol (provided by the mannitol-1-phosphate 5- dehydrogenase and the NADP-dependent mannitol dehydrogenase) or arabinol (provided by the L-arabinitol 4-dehydrogenase).",,,,,,,GO:0016787,GO:0016787,GO:0016747,GO:0016746,GO:0016788,GO:0016746,1.0,0.4071,0.4807,0.8145,0.4807,5,0.6366,0.468,no
ANKF_ASPTH,A0A397HK53,ESM2Text,Eukaryota,239,"O-methyltransferase; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo-arginine- tyrosine dipeptide. AnkF converts NK13650 B to produce NK13650 D via methylation of the C-17 phenol group. Within the pathway, the cyclodipeptide synthase ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-Arg and L-Tyr. The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L-homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A.",Catalyzes the O-methylation of phospho- and methylated guanidinoacetate building blocks of different chain lengths. Substrate preference is methylated Phe-20 > methylated Asp-20 > methylated Asp-20. Required for R-maturation of small ribosomal RNAs (sRNA).,Maybe,Maybe,Yes,No,Maybe,not-Yes,GO:0008171; GO:0008757,GO:0008171,GO:0008171,GO:0008171,GO:0008168,GO:0008171,0.9096,0.9096,0.9096,0.8582,0.9096,5,0.8993,0.2314,no
ANKF_ASPTH,A0A397HK53,Prot2Text,Eukaryota,239,"O-methyltransferase; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo-arginine- tyrosine dipeptide. AnkF converts NK13650 B to produce NK13650 D via methylation of the C-17 phenol group. Within the pathway, the cyclodipeptide synthase ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-Arg and L-Tyr. The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L-homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A.",Methylates caffeoyl-CoA to feruloyl-CoA and 5-hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of feruloylated polysaccharides. Involved in the reinforcement of the plant cell wall. Also involved in the responding to wounding or pathogen challenge by the increased formation of cell wall-bound ferulic acid polymers.,Maybe,No,Yes,No,Maybe,not-Yes,GO:0008171; GO:0008757,GO:0042409,GO:0042409,GO:0042409,GO:0042409,GO:0042409,0.7867,0.7867,0.7867,0.7867,0.7867,5,0.7867,0.2314,no
ANKF_ASPTH,A0A397HK53,ProtT3,Eukaryota,239,"O-methyltransferase; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo-arginine- tyrosine dipeptide. AnkF converts NK13650 B to produce NK13650 D via methylation of the C-17 phenol group. Within the pathway, the cyclodipeptide synthase ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-Arg and L-Tyr. The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L-homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A.",Methylates caffeoyl-CoA to feruloyl-CoA and 5- hydroxyferuloyl-CoA to sinapoyl-CoA. Involved in the biosynthesis of feruloylated polysaccharides. Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily,Maybe,Maybe,Yes,No,Maybe,not-Yes,GO:0008171; GO:0008757,GO:0042409,GO:0042409,GO:0042409,GO:0008171,GO:0008171,0.7867,0.7867,0.7867,0.9096,0.9096,5,0.8359,0.2314,no
ANKF_ASPTH,A0A397HK53,ProtTale,Eukaryota,239,"O-methyltransferase; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo-arginine- tyrosine dipeptide. AnkF converts NK13650 B to produce NK13650 D via methylation of the C-17 phenol group. Within the pathway, the cyclodipeptide synthase ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-Arg and L-Tyr. The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L-homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A.",Methyltransferase involved in the biosynthesis of azaphilone pigments. Catalyzes the S-adenosyl-L-methionine-dependent methyl transfer from the carboxyl group of S-adenosyl-L- methionine to the hydroxyl group of L-tryptophan to produce N-(carboxymethyl)-L-tryptophan.,Maybe,No,Yes,Maybe,Maybe,not-Yes,GO:0008171; GO:0008757,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.2314,no
ANKF_ASPTH,A0A397HK53,Protein2Text,Eukaryota,239,"O-methyltransferase; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo-arginine- tyrosine dipeptide. AnkF converts NK13650 B to produce NK13650 D via methylation of the C-17 phenol group. Within the pathway, the cyclodipeptide synthase ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-Arg and L-Tyr. The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L-homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A.","The molecular function of this protein is that it functions as a methyltransferase.
 
This protein catalyzes the transfer of a methyl group to its substrate, specifically involved in the methylation of the N-methyltransferase activity of 1,3-dimethylxanthine.  It is also involved in the N-methyltransferase activity of caffeine, which is the major methylated metabolite of the xanthine catabolic pathway.  The protein is also able to methylate theophylline, which is a xanthine derivative.  It is also involved in the N-methyltransferase activity of theophylline.
 
In the process of catalyzing the methylation of caffeine, this protein transfers a methyl group from S-adenosyl-L-methionine (SAM) to the N7 of caffeine, forming theophylline.  It is also able to methylate theophylline to form theobromine, another methylated metabolite of the xanthine catabolic pathway.
 
The protein is also able to catalyze the methylation of other compounds, such as 1,3-dimethylxanthine, theobromine, and 7-methylxanthine, which are all involved in the xanthine catabolic pathway.  The protein is also able to catalyze the methylation of theophylline, which is a xanthine derivative.
 
The protein is also able to catalyze the methylation of other compounds, such as 1,3-dimethylxanthine, theobromine, and 7-methylxanthine, which are all involved in the xanthine catabolic pathway.  The protein is also able to catalyze the methylation of theophylline, which is a xanthine derivative.
 
The protein is also able to catalyze the methylation of other compounds, such as 1,3-dimethylxanthine, theobromine, and 7-methylxanthine, which are all involved in the xanthine catabolic pathway.  The protein is also able to catalyze the methylation of theophylline, which is a xanthine derivative.
 
The protein is also able to catalyze the methylation of other compounds, such as 1,3-dimethylxanthine, theobromine, and 7-methylxanthine",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0008171; GO:0008757,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008170,0.8582,0.8582,0.8582,0.8582,0.7289,5,0.8323,0.2314,no
ANKF_ASPTH,A0A397HK53,Reference,Eukaryota,239,"O-methyltransferase; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo-arginine- tyrosine dipeptide. AnkF converts NK13650 B to produce NK13650 D via methylation of the C-17 phenol group. Within the pathway, the cyclodipeptide synthase ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-Arg and L-Tyr. The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L-homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A.","O-methyltransferase; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo-arginine- tyrosine dipeptide. AnkF converts NK13650 B to produce NK13650 D via methylation of the C-17 phenol group. Within the pathway, the cyclodipeptide synthase ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-Arg and L-Tyr. The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L-homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A.",,,,,,,GO:0008171; GO:0008757,GO:0008168,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.8582,0.9096,0.9096,0.9096,0.9096,5,0.8993,0.2314,no
ANKC_ASPTH,A0A397HQ89,ESM2Text,Eukaryota,587,"FAD-dependent monooxygenase; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo- arginine-tyrosine dipeptide. AnkC uses as substrate the dehydro-cyclodipeptide intermediate generated by the monooxygase ankB and acts as a hydroxylase that installs the m-OH through a canonical flavin-dependent aromatic hydroxylation mechanism. Within the pathway, the cyclodipeptide synthase ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-Arg and L-Tyr. The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L-homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A.","FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the naphtho-monooxygenase claB. The cytochrome P450 monooxygenase claM then catalyzes the dimerization of naphtho-monooxygen to cladofulvin.",Maybe,No,Yes,Maybe,Maybe,not-Yes,GO:0071949; GO:0016709,GO:0004497; GO:0071949,GO:0004497,GO:0016491,GO:0004497; GO:0071949,GO:0004497; GO:0071949,0.8735,0.5301,0.4434,0.8735,0.8735,5,0.7188,0.3373,no
ANKC_ASPTH,A0A397HQ89,Prot2Text,Eukaryota,587,"FAD-dependent monooxygenase; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo- arginine-tyrosine dipeptide. AnkC uses as substrate the dehydro-cyclodipeptide intermediate generated by the monooxygase ankB and acts as a hydroxylase that installs the m-OH through a canonical flavin-dependent aromatic hydroxylation mechanism. Within the pathway, the cyclodipeptide synthase ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-Arg and L-Tyr. The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L-homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A.","Trihydroxylase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The nonribosomal peptide synthetase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin. The function of ktnD within the pathway has not been determined yet.",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0071949; GO:0016709,,,,GO:0016491,GO:0016491,,,,0.4434,0.4434,2,0.4434,0.3373,no
ANKC_ASPTH,A0A397HQ89,ProtT3,Eukaryota,587,"FAD-dependent monooxygenase; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo- arginine-tyrosine dipeptide. AnkC uses as substrate the dehydro-cyclodipeptide intermediate generated by the monooxygase ankB and acts as a hydroxylase that installs the m-OH through a canonical flavin-dependent aromatic hydroxylation mechanism. Within the pathway, the cyclodipeptide synthase ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-Arg and L-Tyr. The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L-homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A.","Catalyzes the hydroxylation of 2,4-dichlorophenol (2,4-DCP) to 2,4,5-trichlorophenol (2,4,5-TCP). Belongs to the PheA/TfdB FAD monooxygenase family",Maybe,No,Yes,No,Maybe,not-Yes,GO:0071949; GO:0016709,GO:0004497,GO:0004497,GO:0004497,GO:0004497; GO:0071949,GO:0004497; GO:0071949,0.5301,0.5301,0.5301,0.8735,0.8735,5,0.6675,0.3373,no
ANKC_ASPTH,A0A397HQ89,ProtTale,Eukaryota,587,"FAD-dependent monooxygenase; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo- arginine-tyrosine dipeptide. AnkC uses as substrate the dehydro-cyclodipeptide intermediate generated by the monooxygase ankB and acts as a hydroxylase that installs the m-OH through a canonical flavin-dependent aromatic hydroxylation mechanism. Within the pathway, the cyclodipeptide synthase ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-Arg and L-Tyr. The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L-homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A.","FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities. In the first step, the non-reducing polyketide synthase azaA forms the hexaketide precursor from successive condensations of five malonyl-CoA units, presumably with a simple acetyl-CoA starter unit. The reactive polyketide chain then undergoes a PT- mediated C2-C7 cyclization to afford the aromatic ring and is eventually released as an aldehyde through the R-",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0071949; GO:0016709,GO:0004497,GO:0016491; GO:0071949,GO:0004497; GO:0050660,GO:0004497,GO:0004497,0.5301,0.8031,0.8308,0.5301,0.5301,5,0.6448,0.3373,no
ANKC_ASPTH,A0A397HQ89,Protein2Text,Eukaryota,587,"FAD-dependent monooxygenase; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo- arginine-tyrosine dipeptide. AnkC uses as substrate the dehydro-cyclodipeptide intermediate generated by the monooxygase ankB and acts as a hydroxylase that installs the m-OH through a canonical flavin-dependent aromatic hydroxylation mechanism. Within the pathway, the cyclodipeptide synthase ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-Arg and L-Tyr. The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L-homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A.","The molecular function of this protein is a monooxygenase, specifically involved in the degradation of aromatic compounds. It is a FAD-dependent monooxygenase, which means it uses a flavin adenine dinucleotide (FAD) molecule to catalyze the oxidation of organic compounds. More specifically, it is involved in the degradation of phenolic compounds, such as phenylpropanoids, through the hydroxylation of aromatic rings.",Maybe,No,Yes,Maybe,Maybe,not-Yes,GO:0071949; GO:0016709,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.5301,0.5301,0.5301,0.5301,0.5301,5,0.5301,0.3373,no
ANKC_ASPTH,A0A397HQ89,Reference,Eukaryota,587,"FAD-dependent monooxygenase; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo- arginine-tyrosine dipeptide. AnkC uses as substrate the dehydro-cyclodipeptide intermediate generated by the monooxygase ankB and acts as a hydroxylase that installs the m-OH through a canonical flavin-dependent aromatic hydroxylation mechanism. Within the pathway, the cyclodipeptide synthase ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-Arg and L-Tyr. The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L-homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A.","FAD-dependent monooxygenase; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo- arginine-tyrosine dipeptide. AnkC uses as substrate the dehydro-cyclodipeptide intermediate generated by the monooxygase ankB and acts as a hydroxylase that installs the m-OH through a canonical flavin-dependent aromatic hydroxylation mechanism. Within the pathway, the cyclodipeptide synthase ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-Arg and L-Tyr. The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L-homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A.",,,,,,,GO:0071949; GO:0016709,GO:0004497,GO:0004497,GO:0004497; GO:0071949,GO:0004497; GO:0071949,GO:0004497,0.5301,0.5301,0.8735,0.8735,0.5301,5,0.6675,0.3373,no
SQWL_ACHSX,A0A3A6N9V6,ESM2Text,Bacteria,296,"Part of a variant of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces sulfoacetate. Hydrolyzes sulfoacetyl-coenzyme A (sulfoacetyl-CoA) to produce sulfoacetate and CoA coupled with the phosphorylation of ADP to generate ATP. Cannot use succinate, acetate or 3- hydroxypropionate, and shows only residual activities with malonate and 3-sulfopropanoate.","Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.",No,Maybe,No,Maybe,No,not-Yes,GO:0000166; GO:0004775; GO:0004776,GO:0004774,GO:0004775,GO:0004775,GO:0004775; GO:0005524,GO:0004775,0.6778,0.7099,0.7099,0.7644,0.7099,5,0.7144,0.5768,yes
SQWL_ACHSX,A0A3A6N9V6,Prot2Text,Bacteria,296,"Part of a variant of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces sulfoacetate. Hydrolyzes sulfoacetyl-coenzyme A (sulfoacetyl-CoA) to produce sulfoacetate and CoA coupled with the phosphorylation of ADP to generate ATP. Cannot use succinate, acetate or 3- hydroxypropionate, and shows only residual activities with malonate and 3-sulfopropanoate.","Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.",No,Maybe,No,Maybe,No,not-Yes,GO:0000166; GO:0004775; GO:0004776,GO:0004775,GO:0004775,GO:0004775,GO:0004775,GO:0004775,0.7099,0.7099,0.7099,0.7099,0.7099,5,0.7099,0.5768,yes
SQWL_ACHSX,A0A3A6N9V6,ProtT3,Bacteria,296,"Part of a variant of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces sulfoacetate. Hydrolyzes sulfoacetyl-coenzyme A (sulfoacetyl-CoA) to produce sulfoacetate and CoA coupled with the phosphorylation of ADP to generate ATP. Cannot use succinate, acetate or 3- hydroxypropionate, and shows only residual activities with malonate and 3-sulfopropanoate.","Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit. Belongs to the succinate/malate CoA ligase alpha subunit family",No,Maybe,No,Maybe,No,not-Yes,GO:0000166; GO:0004775; GO:0004776,GO:0004775,GO:0004775,GO:0004775,GO:0004775,GO:0004775,0.7099,0.7099,0.7099,0.7099,0.7099,5,0.7099,0.5768,yes
SQWL_ACHSX,A0A3A6N9V6,ProtTale,Bacteria,296,"Part of a variant of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces sulfoacetate. Hydrolyzes sulfoacetyl-coenzyme A (sulfoacetyl-CoA) to produce sulfoacetate and CoA coupled with the phosphorylation of ADP to generate ATP. Cannot use succinate, acetate or 3- hydroxypropionate, and shows only residual activities with malonate and 3-sulfopropanoate.",Catalyzes the reversible oxidation of malate to oxaloacetate.,No,No,No,No,No,not-Yes,GO:0000166; GO:0004775; GO:0004776,GO:0016615,GO:0016615,GO:0016615,GO:0016615,GO:0016615,0.1847,0.1847,0.1847,0.1847,0.1847,5,0.1847,0.5768,yes
SQWL_ACHSX,A0A3A6N9V6,Protein2Text,Bacteria,296,"Part of a variant of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces sulfoacetate. Hydrolyzes sulfoacetyl-coenzyme A (sulfoacetyl-CoA) to produce sulfoacetate and CoA coupled with the phosphorylation of ADP to generate ATP. Cannot use succinate, acetate or 3- hydroxypropionate, and shows only residual activities with malonate and 3-sulfopropanoate.","The molecular function of this protein is an enzyme, specifically a phosphatase that catalyzes the conversion of 2-phosphoglycerate to 3-phosphoglycerate.",No,No,No,No,No,not-Yes,GO:0000166; GO:0004775; GO:0004776,,,,,,,,,,,0,,0.5768,yes
SQWL_ACHSX,A0A3A6N9V6,Reference,Bacteria,296,"Part of a variant of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces sulfoacetate. Hydrolyzes sulfoacetyl-coenzyme A (sulfoacetyl-CoA) to produce sulfoacetate and CoA coupled with the phosphorylation of ADP to generate ATP. Cannot use succinate, acetate or 3- hydroxypropionate, and shows only residual activities with malonate and 3-sulfopropanoate.","Part of a variant of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces sulfoacetate. Hydrolyzes sulfoacetyl-coenzyme A (sulfoacetyl-CoA) to produce sulfoacetate and CoA coupled with the phosphorylation of ADP to generate ATP. Cannot use succinate, acetate or 3- hydroxypropionate, and shows only residual activities with malonate and 3-sulfopropanoate.",,,,,,,GO:0000166; GO:0004775; GO:0004776,GO:0016776; GO:0016887,GO:0016790; GO:0016301,GO:0016790,GO:0016790,,0.1774,0.1891,0.1847,0.1847,,4,0.184,0.5768,yes
HIPS_NEONM,A0A3G9K3K9,ESM2Text,Eukaryota,1678,"PKS-NRPS hybrid synthetase; part of the gene cluster that mediates the fungal bioluminescence cycle. Performs the biosynthesis of hispidin from caffeic acid by two cycles of addition of malonyl units followed by lactonization. The fungal bioluminescence cycle begins with the hispidin synthetase that catalyzes the formation of hispidin which is further hydroxylated by the hispidin-3-hydroxylase, yielding the fungal luciferin 3- hydroxyhispidin. The luciferase then produces an endoperoxide as a high-energy intermediate with decomposition that yields oxyluciferin (also known as caffeoylpyruvate) and light emission. Oxyluciferin can be recycled to caffeic acid by caffeoylpyruvate hydrolase (Probable).","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0031177,,GO:0016747,GO:0016491; GO:0016740,GO:0016746,GO:0016746,,0.6029,0.4215,0.5216,0.5216,4,0.5169,0.217,no
HIPS_NEONM,A0A3G9K3K9,Prot2Text,Eukaryota,1678,"PKS-NRPS hybrid synthetase; part of the gene cluster that mediates the fungal bioluminescence cycle. Performs the biosynthesis of hispidin from caffeic acid by two cycles of addition of malonyl units followed by lactonization. The fungal bioluminescence cycle begins with the hispidin synthetase that catalyzes the formation of hispidin which is further hydroxylated by the hispidin-3-hydroxylase, yielding the fungal luciferin 3- hydroxyhispidin. The luciferase then produces an endoperoxide as a high-energy intermediate with decomposition that yields oxyluciferin (also known as caffeoylpyruvate) and light emission. Oxyluciferin can be recycled to caffeic acid by caffeoylpyruvate hydrolase (Probable).","Nonribosomal peptide synthase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0031177,,,GO:0016874,,GO:0016874,,,0.2791,,0.2791,2,0.2791,0.217,no
HIPS_NEONM,A0A3G9K3K9,ProtT3,Eukaryota,1678,"PKS-NRPS hybrid synthetase; part of the gene cluster that mediates the fungal bioluminescence cycle. Performs the biosynthesis of hispidin from caffeic acid by two cycles of addition of malonyl units followed by lactonization. The fungal bioluminescence cycle begins with the hispidin synthetase that catalyzes the formation of hispidin which is further hydroxylated by the hispidin-3-hydroxylase, yielding the fungal luciferin 3- hydroxyhispidin. The luciferase then produces an endoperoxide as a high-energy intermediate with decomposition that yields oxyluciferin (also known as caffeoylpyruvate) and light emission. Oxyluciferin can be recycled to caffeic acid by caffeoylpyruvate hydrolase (Probable).",Multifunctional nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-,Maybe,No,Maybe,No,Maybe,not-Yes,GO:0004312; GO:0031177,GO:0016874,GO:0016874,GO:0016874,GO:0016874,GO:0016874; GO:0005524,0.2791,0.2791,0.2791,0.2791,0.3569,5,0.2947,0.217,no
HIPS_NEONM,A0A3G9K3K9,ProtTale,Eukaryota,1678,"PKS-NRPS hybrid synthetase; part of the gene cluster that mediates the fungal bioluminescence cycle. Performs the biosynthesis of hispidin from caffeic acid by two cycles of addition of malonyl units followed by lactonization. The fungal bioluminescence cycle begins with the hispidin synthetase that catalyzes the formation of hispidin which is further hydroxylated by the hispidin-3-hydroxylase, yielding the fungal luciferin 3- hydroxyhispidin. The luciferase then produces an endoperoxide as a high-energy intermediate with decomposition that yields oxyluciferin (also known as caffeoylpyruvate) and light emission. Oxyluciferin can be recycled to caffeic acid by caffeoylpyruvate hydrolase (Probable).","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0031177,GO:0016747,GO:0016747,GO:0016746,GO:0016746,,0.6029,0.6029,0.5216,0.5216,,4,0.5622,0.217,no
HIPS_NEONM,A0A3G9K3K9,Protein2Text,Eukaryota,1678,"PKS-NRPS hybrid synthetase; part of the gene cluster that mediates the fungal bioluminescence cycle. Performs the biosynthesis of hispidin from caffeic acid by two cycles of addition of malonyl units followed by lactonization. The fungal bioluminescence cycle begins with the hispidin synthetase that catalyzes the formation of hispidin which is further hydroxylated by the hispidin-3-hydroxylase, yielding the fungal luciferin 3- hydroxyhispidin. The luciferase then produces an endoperoxide as a high-energy intermediate with decomposition that yields oxyluciferin (also known as caffeoylpyruvate) and light emission. Oxyluciferin can be recycled to caffeic acid by caffeoylpyruvate hydrolase (Probable).","This protein is involved in the synthesis of nonribosomal peptides, which are a class of secondary metabolites with diverse biological activities. It is likely a nonribosomal peptide synthetase (NRPS), which is an enzyme that catalyzes the formation of these compounds by assembling amino acids and other substrates into a peptide backbone. The specific molecular function of this protein is not explicitly stated, but it is likely involved in the assembly of amino acids into a peptide backbone, which is a key step in the synthesis of nonribosomal peptides.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0031177,,GO:0003824,,,,,0.36,,,,1,0.36,0.217,no
HIPS_NEONM,A0A3G9K3K9,Reference,Eukaryota,1678,"PKS-NRPS hybrid synthetase; part of the gene cluster that mediates the fungal bioluminescence cycle. Performs the biosynthesis of hispidin from caffeic acid by two cycles of addition of malonyl units followed by lactonization. The fungal bioluminescence cycle begins with the hispidin synthetase that catalyzes the formation of hispidin which is further hydroxylated by the hispidin-3-hydroxylase, yielding the fungal luciferin 3- hydroxyhispidin. The luciferase then produces an endoperoxide as a high-energy intermediate with decomposition that yields oxyluciferin (also known as caffeoylpyruvate) and light emission. Oxyluciferin can be recycled to caffeic acid by caffeoylpyruvate hydrolase (Probable).","PKS-NRPS hybrid synthetase; part of the gene cluster that mediates the fungal bioluminescence cycle. Performs the biosynthesis of hispidin from caffeic acid by two cycles of addition of malonyl units followed by lactonization. The fungal bioluminescence cycle begins with the hispidin synthetase that catalyzes the formation of hispidin which is further hydroxylated by the hispidin-3-hydroxylase, yielding the fungal luciferin 3- hydroxyhispidin. The luciferase then produces an endoperoxide as a high-energy intermediate with decomposition that yields oxyluciferin (also known as caffeoylpyruvate) and light emission. Oxyluciferin can be recycled to caffeic acid by caffeoylpyruvate hydrolase (Probable).",,,,,,,GO:0004312; GO:0031177,GO:0031177; GO:0016874,GO:0004315; GO:0008927,GO:0016874; GO:0016747,GO:0016874; GO:0016746,,0.6776,0.4348,0.5496,0.485,,4,0.5367,0.217,no
CGLR_POCDA,A0A3M6TIF0,ESM2Text,Eukaryota,432,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates the monoubiquitination of C-terminal domain-containing poly(A) RNA polymerase II subunit paa-3/CAT-RNAPII leading to its degradation by the proteasome.,No,Yes,No,No,No,not-Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0003725,GO:0003725,GO:0003725,GO:0003725,GO:0003725,0.1694,0.1694,0.1694,0.1694,0.1694,5,0.1694,0.5846,yes
CGLR_POCDA,A0A3M6TIF0,Prot2Text,Eukaryota,432,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Cyclic dinucleotide synthase that catalyzes the synthesis of 3',3'-cyclic UMP-UMP (cUMP-UMP) as the major product, and of 3',3'-cyclic CMP-UMP as a minor product, that are second messengers for cell signal transduction.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0016779,,GO:0016779,GO:0016779,GO:0016779,0.3478,,0.3478,0.3478,0.3478,4,0.3478,0.5846,yes
CGLR_POCDA,A0A3M6TIF0,ProtT3,Eukaryota,432,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity (By similarity). Acts by mediating the synthesis of 2',3'-cGAMP, a second messenger that binds to and activates the cGAS-STING pathway (By similarity). 2',3'-cGAMP binds to and activates STING1, leading to the production of type I interferon (By similarity). Belongs to the isochorism",Yes,Yes,Yes,Yes,Yes,Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0016779,GO:0061501,GO:0061501,GO:0016779,GO:0061501; GO:0005524; GO:0005525,0.3478,0.4353,0.4353,0.3478,0.8984,5,0.4929,0.5846,yes
CGLR_POCDA,A0A3M6TIF0,ProtTale,Eukaryota,432,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Functions as a nucleotidyltransferase that catalyzes the addition of ATP or UTP to glutamate to form N-acetylglutamate (NAG) or N-acetylaspartate (NAA), respectively. N-acetylglutamate and N-acetylaspartate are involved in regulating protein synthesis through inhibition of the activity of initiation factors.",Yes,Yes,Yes,Maybe,Yes,Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0016779,GO:0016779,,GO:0016779,GO:0016779,0.3478,0.3478,,0.3478,0.3478,4,0.3478,0.5846,yes
CGLR_POCDA,A0A3M6TIF0,Protein2Text,Eukaryota,432,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","The molecular function of this protein is not explicitly stated in the provided information. However, based on the name and context, it is likely that this protein is involved in the signaling pathway, specifically in the regulation of gene expression. It is a part of the ""RIG-I-like receptor"" family, which suggests that it may play a role in detecting viral RNA and triggering an immune response. 

In general, RIG-I-like receptors are involved in the recognition of viral RNA and activation of downstream signaling pathways that lead to the production of type I interferons and other immune mediators. They play a crucial role in the innate immune response to viral infections.

If you have any more specific information about the protein, I may be able to provide a more detailed answer.",Vague,No,Vague,Vague,Vague,not-Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.1786,0.1786,0.1786,0.1786,0.1786,5,0.1786,0.5846,yes
CGLR_POCDA,A0A3M6TIF0,Reference,Eukaryota,432,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",,,,,,,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0061501,GO:0016779,GO:0016779,GO:0016779,GO:0061501,0.4353,0.3478,0.3478,0.3478,0.4353,5,0.3828,0.5846,yes
ARAFA_BIFL2,A0A3R0A696,ESM2Text,Bacteria,1065,"Involved in the type II arabinogalactan (AG) side chains degradation. Releases arabinofuranose (Araf) from alpha-1,3-Araf-substituted beta-1,6-galactooligosaccharides. Can use radish root AGP, larch AG and arabinan. Shows weaker activity with gum arabic and arabinoxylan.",Type I polysaccharide-binding protein that acts as a virulence factor. Appears to act as a direct immunogen in leishmaniasis. Binds directly to host elastin and thus inhibits the pathogenesis by inhibiting the interaction between the soluble form and host elastin with its partner Acinetobacter sp.,No,No,No,No,No,not-Yes,GO:0046556,,GO:0030247,,,GO:0030247,,0.1264,,,0.1264,2,0.1264,0.3092,no
ARAFA_BIFL2,A0A3R0A696,Prot2Text,Bacteria,1065,"Involved in the type II arabinogalactan (AG) side chains degradation. Releases arabinofuranose (Araf) from alpha-1,3-Araf-substituted beta-1,6-galactooligosaccharides. Can use radish root AGP, larch AG and arabinan. Shows weaker activity with gum arabic and arabinoxylan.","Ulvan lyase involved in ulvan degradation. Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable). Ulvan lyase catalyzes preferentially the endolytic cleavage of the glycosidic bond between Rha3S and the uronic acids GlcA or IduA, but not IduA, producing oligosaccharides that have unsaturated 4-deoxy-L-threo-hex-4-enopyranosiduronic acid (deltaUA) at the non-reducing end. The most abundant end products in the degradation of the ulvan polysaccharide were deltaUA-Rha3S disaccharides and deltaUA-Rha3S-IduA-Rha3S and deltaUA-Rha3S-Xyl-Rha3S",No,No,No,No,No,not-Yes,GO:0046556,GO:0016829,GO:0016835,GO:0016829,GO:0016829,GO:0016835,0.3552,0.2845,0.3552,0.3552,0.2845,5,0.3269,0.3092,no
ARAFA_BIFL2,A0A3R0A696,ProtT3,Bacteria,1065,"Involved in the type II arabinogalactan (AG) side chains degradation. Releases arabinofuranose (Araf) from alpha-1,3-Araf-substituted beta-1,6-galactooligosaccharides. Can use radish root AGP, larch AG and arabinan. Shows weaker activity with gum arabic and arabinoxylan.",Unable to hydrolyze alpha-(1->6)-linked glucans. Secreted. Belongs to the glycosyl hydrolase 69 family,Vague,No,No,No,Vague,not-Yes,GO:0046556,,GO:0016798,GO:0016798,,,,0.729,0.729,,,2,0.729,0.3092,no
ARAFA_BIFL2,A0A3R0A696,ProtTale,Bacteria,1065,"Involved in the type II arabinogalactan (AG) side chains degradation. Releases arabinofuranose (Araf) from alpha-1,3-Araf-substituted beta-1,6-galactooligosaccharides. Can use radish root AGP, larch AG and arabinan. Shows weaker activity with gum arabic and arabinoxylan.","Transfers a glucose moiety from UDP-glucose to the 4-OH position of a mannosyl residue in a 1,4-bond linkage, to form a linear 1,3-beta-D-mannosyl-(1,4)-alpha-D-glucose linkage in mannans. Transfers a glucose moiety from UDP-glucose to the 6-OH position of a mannosyl residue in a 1,6-bond linkage, to form a branched 1,3-beta-D-mannosyl-(1,6)-alpha-D-glucose linkage in",No,No,No,No,No,not-Yes,GO:0046556,GO:0035251,GO:0016758,GO:0008194,GO:0016758,GO:0035251,0.1672,0.2353,0.2353,0.2353,0.1672,5,0.2081,0.3092,no
ARAFA_BIFL2,A0A3R0A696,Protein2Text,Bacteria,1065,"Involved in the type II arabinogalactan (AG) side chains degradation. Releases arabinofuranose (Araf) from alpha-1,3-Araf-substituted beta-1,6-galactooligosaccharides. Can use radish root AGP, larch AG and arabinan. Shows weaker activity with gum arabic and arabinoxylan.","This protein is a peptidoglycan hydrolase, which is a type of enzyme that breaks down peptidoglycan, a component of bacterial cell walls.",No,No,No,No,No,not-Yes,GO:0046556,GO:0008745,GO:0008745,GO:0008745,GO:0008933,GO:0016787,0.339,0.339,0.339,0.2199,0.6019,5,0.3678,0.3092,no
ARAFA_BIFL2,A0A3R0A696,Reference,Bacteria,1065,"Involved in the type II arabinogalactan (AG) side chains degradation. Releases arabinofuranose (Araf) from alpha-1,3-Araf-substituted beta-1,6-galactooligosaccharides. Can use radish root AGP, larch AG and arabinan. Shows weaker activity with gum arabic and arabinoxylan.","Involved in the type II arabinogalactan (AG) side chains degradation. Releases arabinofuranose (Araf) from alpha-1,3-Araf-substituted beta-1,6-galactooligosaccharides. Can use radish root AGP, larch AG and arabinan. Shows weaker activity with gum arabic and arabinoxylan.",,,,,,,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3092,no
EXGAL_BIFL2,A0A401ETL2,ESM2Text,Bacteria,1513,"Involved in the type II arabinogalactan (AG) side chains degradation. Specifically releases the non-reducing terminal beta-1,6-galactobiose (beta-1,6-Gal2) from both dearabinosylated larch AG and polymeric beta-1,6-galactan chains by an exo-mode of action. Shows lower activity with larch AG, and very weak activity with dearabinosylated gum arabic, gum arabic and potato galactan. Can probably release beta-1,6- Gal2 from the internal side chains of type II AG.","Major polygalacturonase that has the highest activity toward wheat arabinogalactan. Is also able to hydrolyze p-nitrophenyl-beta-D-galactopyranoside (pNP-Gal), a substrate of the bacterial beta-glucanases present in this organism.",Maybe,No,No,No,Maybe,not-Yes,GO:0004553,GO:0004650,GO:0004650,GO:0004650,GO:0004650,GO:0004650,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.2789,no
EXGAL_BIFL2,A0A401ETL2,Prot2Text,Bacteria,1513,"Involved in the type II arabinogalactan (AG) side chains degradation. Specifically releases the non-reducing terminal beta-1,6-galactobiose (beta-1,6-Gal2) from both dearabinosylated larch AG and polymeric beta-1,6-galactan chains by an exo-mode of action. Shows lower activity with larch AG, and very weak activity with dearabinosylated gum arabic, gum arabic and potato galactan. Can probably release beta-1,6- Gal2 from the internal side chains of type II AG.","Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of terminal alpha-(1->5)-arabinofuranosyl bonds in different hemicellulosic homopolysaccharides (branched and debranched arabinans). It is highly specific for the linear alpha-(1->5)-linked arabinofuranosyl residues of arabinan present in the arabinofuranosyl polysaccharides. It is also able to hydrolyze the alpha-(1->3)-linked arabinofuranosyl of the sugar beet arabinan, but it shows a marked preference for the alpha-(1->3)-linked arabinofuranosyl decorations.",No,No,No,No,No,not-Yes,GO:0004553,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.2789,no
EXGAL_BIFL2,A0A401ETL2,ProtT3,Bacteria,1513,"Involved in the type II arabinogalactan (AG) side chains degradation. Specifically releases the non-reducing terminal beta-1,6-galactobiose (beta-1,6-Gal2) from both dearabinosylated larch AG and polymeric beta-1,6-galactan chains by an exo-mode of action. Shows lower activity with larch AG, and very weak activity with dearabinosylated gum arabic, gum arabic and potato galactan. Can probably release beta-1,6- Gal2 from the internal side chains of type II AG.",Belongs to the glycosyl hydrolase 64 family,Vague,No,Vague,No,Vague,not-Yes,GO:0004553,GO:0016798,GO:0016798,GO:0016798,GO:0016798,GO:0016798,0.8416,0.8416,0.8416,0.8416,0.8416,5,0.8416,0.2789,no
EXGAL_BIFL2,A0A401ETL2,ProtTale,Bacteria,1513,"Involved in the type II arabinogalactan (AG) side chains degradation. Specifically releases the non-reducing terminal beta-1,6-galactobiose (beta-1,6-Gal2) from both dearabinosylated larch AG and polymeric beta-1,6-galactan chains by an exo-mode of action. Shows lower activity with larch AG, and very weak activity with dearabinosylated gum arabic, gum arabic and potato galactan. Can probably release beta-1,6- Gal2 from the internal side chains of type II AG.",Involved in the degradation of galactomannan. Catalyzes the release of beta-D-galactofuranosyl residues from alpha-D-galactofuranosyl-beta-D-mannopyranosyl (1->6)-beta-D-glucopyranosyl-(1->4)-alpha-D-galactofuranosyl-(1->6)-beta-D-mannopyranosyl (1->6)-beta-D-glucopyranosyl-(1->4)-alpha-D-galactofuranosyl-(1->6)-beta-D,No,No,No,No,No,not-Yes,GO:0004553,GO:0004553,GO:0016798,GO:0016798,GO:0004553,GO:0004553,1.0,0.8416,0.8416,1.0,1.0,5,0.9366,0.2789,no
EXGAL_BIFL2,A0A401ETL2,Protein2Text,Bacteria,1513,"Involved in the type II arabinogalactan (AG) side chains degradation. Specifically releases the non-reducing terminal beta-1,6-galactobiose (beta-1,6-Gal2) from both dearabinosylated larch AG and polymeric beta-1,6-galactan chains by an exo-mode of action. Shows lower activity with larch AG, and very weak activity with dearabinosylated gum arabic, gum arabic and potato galactan. Can probably release beta-1,6- Gal2 from the internal side chains of type II AG.","This protein is a lytic polysaccharide monooxygenase (LPMO), which is an enzyme that catalyzes the oxidative cleavage of polysaccharides, such as cellulose and chitin, into oligosaccharides. In particular, this protein is involved in the depolymerization of cellulose, a key step in the degradation of plant biomass. The molecular function of this protein is to catalyze the oxidative cleavage of the C1-C2 bond of cellulose, resulting in the formation of 2,5-diketo-D-gluconate and the release of a cellobiose moiety from the cellulose chain. This reaction is dependent on molecular oxygen and requires a reducing agent, such as ascorbate, to regenerate the active form of the enzyme.",No,No,No,No,No,not-Yes,GO:0004553,GO:0016166,GO:0016166,GO:0016491,GO:0015645,,0.2742,0.2742,0.4071,0.2415,,4,0.2993,0.2789,no
EXGAL_BIFL2,A0A401ETL2,Reference,Bacteria,1513,"Involved in the type II arabinogalactan (AG) side chains degradation. Specifically releases the non-reducing terminal beta-1,6-galactobiose (beta-1,6-Gal2) from both dearabinosylated larch AG and polymeric beta-1,6-galactan chains by an exo-mode of action. Shows lower activity with larch AG, and very weak activity with dearabinosylated gum arabic, gum arabic and potato galactan. Can probably release beta-1,6- Gal2 from the internal side chains of type II AG.","Involved in the type II arabinogalactan (AG) side chains degradation. Specifically releases the non-reducing terminal beta-1,6-galactobiose (beta-1,6-Gal2) from both dearabinosylated larch AG and polymeric beta-1,6-galactan chains by an exo-mode of action. Shows lower activity with larch AG, and very weak activity with dearabinosylated gum arabic, gum arabic and potato galactan. Can probably release beta-1,6- Gal2 from the internal side chains of type II AG.",,,,,,,GO:0004553,GO:0016787,GO:0004553,GO:0004553,GO:0004553,GO:0004553,0.6897,1.0,1.0,1.0,1.0,5,0.9379,0.2789,no
NTHAL_SIMTE,A0A429XC68,ESM2Text,Bacteria,501,"Lyase involved in the degradation of N(tele)-methylhistidine (Ntau-methylhistidine). Catalyzes the conversion of N(tele)-methylhistidine to N(tele)-methylurocanate. Can also convert histidine to urocanate, but with a 40-fold lower efficiency. It may however also function in histidine degradation. Shows weak activity with N(pi)- methylhistidine as substrate.",Catalyzes the non-oxidative deamination of L-phenylalanine and L-tyrosine to form trans-cinnamic acid and p-coumaric acid respectively with similar efficiencies. Facilitates the commitment step in phenylpropanoid pathways that produce lignin and hydroquinones like class B carbon compounds.,Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0004397,GO:0045548,GO:0045548,GO:0045548,GO:0045548,GO:0045548,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.5091,no
NTHAL_SIMTE,A0A429XC68,Prot2Text,Bacteria,501,"Lyase involved in the degradation of N(tele)-methylhistidine (Ntau-methylhistidine). Catalyzes the conversion of N(tele)-methylhistidine to N(tele)-methylurocanate. Can also convert histidine to urocanate, but with a 40-fold lower efficiency. It may however also function in histidine degradation. Shows weak activity with N(pi)- methylhistidine as substrate.","Catalyzes the non-oxidative deamination of L-phenylalanine to form trans-cinnamic acid, the first step in the phenylpropanoid pathway.",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0004397,GO:0045548,GO:0045548,GO:0045548,GO:0045548,GO:0045548,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.5091,no
NTHAL_SIMTE,A0A429XC68,ProtT3,Bacteria,501,"Lyase involved in the degradation of N(tele)-methylhistidine (Ntau-methylhistidine). Catalyzes the conversion of N(tele)-methylhistidine to N(tele)-methylurocanate. Can also convert histidine to urocanate, but with a 40-fold lower efficiency. It may however also function in histidine degradation. Shows weak activity with N(pi)- methylhistidine as substrate.",Cytoplasm. Belongs to the PAL/histidase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004397,GO:0045548,GO:0016841,GO:0016841,GO:0016841,GO:0016841,0.7289,0.8582,0.8582,0.8582,0.8582,5,0.8323,0.5091,no
NTHAL_SIMTE,A0A429XC68,ProtTale,Bacteria,501,"Lyase involved in the degradation of N(tele)-methylhistidine (Ntau-methylhistidine). Catalyzes the conversion of N(tele)-methylhistidine to N(tele)-methylurocanate. Can also convert histidine to urocanate, but with a 40-fold lower efficiency. It may however also function in histidine degradation. Shows weak activity with N(pi)- methylhistidine as substrate.","Converts kynurenine (Kyn) to kynurenic acid (KNA), which may serve as a negative feedback regulator of indoleamine 2,3-dioxygenase 1 (IDO1) activity.",No,No,No,No,No,not-Yes,GO:0004397,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0016212,0.2353,0.2353,0.2353,0.2353,0.1998,5,0.2282,0.5091,no
NTHAL_SIMTE,A0A429XC68,Protein2Text,Bacteria,501,"Lyase involved in the degradation of N(tele)-methylhistidine (Ntau-methylhistidine). Catalyzes the conversion of N(tele)-methylhistidine to N(tele)-methylurocanate. Can also convert histidine to urocanate, but with a 40-fold lower efficiency. It may however also function in histidine degradation. Shows weak activity with N(pi)- methylhistidine as substrate.","The molecular function of this protein is an enzyme, specifically a decarboxylase, which is involved in the breakdown of molecules. More specifically, it is an aromatic L-amino acid decarboxylase that catalyzes the decarboxylation of aromatic L-amino acids.",No,No,No,No,No,not-Yes,GO:0004397,GO:0004058,GO:0004058,GO:0004058,GO:0004058,GO:0004058,0.3386,0.3386,0.3386,0.3386,0.3386,5,0.3386,0.5091,no
NTHAL_SIMTE,A0A429XC68,Reference,Bacteria,501,"Lyase involved in the degradation of N(tele)-methylhistidine (Ntau-methylhistidine). Catalyzes the conversion of N(tele)-methylhistidine to N(tele)-methylurocanate. Can also convert histidine to urocanate, but with a 40-fold lower efficiency. It may however also function in histidine degradation. Shows weak activity with N(pi)- methylhistidine as substrate.","Lyase involved in the degradation of N(tele)-methylhistidine (Ntau-methylhistidine). Catalyzes the conversion of N(tele)-methylhistidine to N(tele)-methylurocanate. Can also convert histidine to urocanate, but with a 40-fold lower efficiency. It may however also function in histidine degradation. Shows weak activity with N(pi)- methylhistidine as substrate.",,,,,,,GO:0004397,GO:0016829,GO:0016841,GO:0016829,GO:0016829,GO:0016829,0.6019,0.8582,0.6019,0.6019,0.6019,5,0.6532,0.5091,no
NTMIP_SIMTE,A0A429XCI2,ESM2Text,Bacteria,411,Hydrolase involved in the degradation of N(tele)- methylhistidine (Ntau-methylhistidine). Catalyzes the conversion of Ntau-methylimidazolonepropionate to methylformimidoylglutamate.,Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.,Yes,Yes,Yes,Maybe,Yes,Yes,GO:0050480; GO:0005506; GO:0008270,GO:0003937,GO:0003837,GO:0003837,GO:0003836,GO:0016812,0.2516,0.2903,0.2903,0.1341,0.4702,5,0.2873,0.5394,yes
NTMIP_SIMTE,A0A429XCI2,Prot2Text,Bacteria,411,Hydrolase involved in the degradation of N(tele)- methylhistidine (Ntau-methylhistidine). Catalyzes the conversion of Ntau-methylimidazolonepropionate to methylformimidoylglutamate.,Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0050480; GO:0005506; GO:0008270,GO:0003949,GO:0003949,GO:0003937,GO:0016787,GO:0003937,0.1341,0.1341,0.2516,0.3653,0.2516,5,0.2273,0.5394,yes
NTMIP_SIMTE,A0A429XCI2,ProtT3,Bacteria,411,Hydrolase involved in the degradation of N(tele)- methylhistidine (Ntau-methylhistidine). Catalyzes the conversion of Ntau-methylimidazolonepropionate to methylformimidoylglutamate.,Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway. Cytoplasm. Belongs to the metallo-dependent hydrolases superfamily. HutI family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0050480; GO:0005506; GO:0008270,GO:0003937,GO:0003841,GO:0003937,GO:0003937,GO:0003937,0.2516,0.0866,0.2516,0.2516,0.2516,5,0.2186,0.5394,yes
NTMIP_SIMTE,A0A429XCI2,ProtTale,Bacteria,411,Hydrolase involved in the degradation of N(tele)- methylhistidine (Ntau-methylhistidine). Catalyzes the conversion of Ntau-methylimidazolonepropionate to methylformimidoylglutamate.,Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0050480; GO:0005506; GO:0008270,GO:0016811,GO:0016787,GO:0016812,GO:0003937,GO:0003937,0.3426,0.3653,0.4702,0.2516,0.2516,5,0.3363,0.5394,yes
NTMIP_SIMTE,A0A429XCI2,Protein2Text,Bacteria,411,Hydrolase involved in the degradation of N(tele)- methylhistidine (Ntau-methylhistidine). Catalyzes the conversion of Ntau-methylimidazolonepropionate to methylformimidoylglutamate.,"This protein has the molecular function of hydrolase, specifically acting as a phosphohydrolase, breaking down a phosphate group from a molecule. In particular, it catalyzes the hydrolysis of a specific phosphoric acid ester, likely involved in the degradation of a nucleotide or nucleoside phosphate.",No,No,No,No,No,not-Yes,GO:0050480; GO:0005506; GO:0008270,,GO:0016791,GO:0016791,GO:0016791,GO:0016791,,0.2035,0.2035,0.2035,0.2035,4,0.2035,0.5394,yes
NTMIP_SIMTE,A0A429XCI2,Reference,Bacteria,411,Hydrolase involved in the degradation of N(tele)- methylhistidine (Ntau-methylhistidine). Catalyzes the conversion of Ntau-methylimidazolonepropionate to methylformimidoylglutamate.,Hydrolase involved in the degradation of N(tele)- methylhistidine (Ntau-methylhistidine). Catalyzes the conversion of Ntau-methylimidazolonepropionate to methylformimidoylglutamate.,,,,,,,GO:0050480; GO:0005506; GO:0008270,GO:0016787,GO:0016810,GO:0016787,GO:0016787,GO:0016787,0.3653,0.4152,0.3653,0.3653,0.3653,5,0.3753,0.5394,yes
LAEA_ARTFL,A0A437A6S9,ESM2Text,Eukaryota,362,"Component of the velvet transcription factor complex that acts as a global regulator of mycelial growth and chlamydospore production. Plays also a key role in the regulation of trap formation and subsequent pathogenicity, as well as secondary metabolism. Regulates the artA gene cluster involved in the biosynthesis of arthrosporol that acts as an inhibitor of trap production. Regulates energy metabolism by controlling the production of glycogen and lipids in hyphea.","Methyltransferase; part of the gene cluster that mediates the biosynthesis of andrastins, meroterpenoid compounds that exhibit inhibitory activity against ras farnesyltransferase, suggesting that they could be promising leads for antitumor agents (Ref.2). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase adrD via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Ref.2). DMAO is then converted to farnesyl-DMAO by the prenyltransferase adrG (Ref.2). The methyltransferase adrK catalyzes the methylation of the carboxyl group of farnesyl-DMAO to farnesyl-DMAO methyl ester which is further converted to epoxyfarnesyl-DMAO methyl ester by the FAD-dependent monooxygenase adrH (Ref.2). The terpene cyclase adrI then catalyzes the carbon skeletal rearrangement to generate the andrastin E, the first compound in the bios",No,No,No,No,No,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008171,GO:0008168,GO:0008168,1.0,1.0,0.8582,1.0,1.0,5,0.9716,0.4271,no
LAEA_ARTFL,A0A437A6S9,Prot2Text,Eukaryota,362,"Component of the velvet transcription factor complex that acts as a global regulator of mycelial growth and chlamydospore production. Plays also a key role in the regulation of trap formation and subsequent pathogenicity, as well as secondary metabolism. Regulates the artA gene cluster involved in the biosynthesis of arthrosporol that acts as an inhibitor of trap production. Regulates energy metabolism by controlling the production of glycogen and lipids in hyphea.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate tolerance, py",No,No,No,No,No,not-Yes,GO:0008168,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.4271,no
LAEA_ARTFL,A0A437A6S9,ProtT3,Eukaryota,362,"Component of the velvet transcription factor complex that acts as a global regulator of mycelial growth and chlamydospore production. Plays also a key role in the regulation of trap formation and subsequent pathogenicity, as well as secondary metabolism. Regulates the artA gene cluster involved in the biosynthesis of arthrosporol that acts as an inhibitor of trap production. Regulates energy metabolism by controlling the production of glycogen and lipids in hyphea.","Methyltransferase that acts as a component of the velvet transcription factor complex that controls sexual/asexual developmental ratio in response to light, promoting sexual development in the darkness while stimulating asexual sporulation under illumination (By similarity). The velvet complex acts as a global regulator for secondary metabolite gene expression (By similarity). Nucleus. Belongs to the methyltransferase superfamily",Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4271,no
LAEA_ARTFL,A0A437A6S9,ProtTale,Eukaryota,362,"Component of the velvet transcription factor complex that acts as a global regulator of mycelial growth and chlamydospore production. Plays also a key role in the regulation of trap formation and subsequent pathogenicity, as well as secondary metabolism. Regulates the artA gene cluster involved in the biosynthesis of arthrosporol that acts as an inhibitor of trap production. Regulates energy metabolism by controlling the production of glycogen and lipids in hyphea.","Methyltransferase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties. L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L- homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O- acetyltransferase FUB5, as well as enzymes of the primary metabolism. The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by the hydrolase FUB",No,Maybe,No,Maybe,No,not-Yes,GO:0008168,GO:0008168,,GO:0008168,GO:0008168,GO:0008168,1.0,,1.0,1.0,1.0,4,1.0,0.4271,no
LAEA_ARTFL,A0A437A6S9,Protein2Text,Eukaryota,362,"Component of the velvet transcription factor complex that acts as a global regulator of mycelial growth and chlamydospore production. Plays also a key role in the regulation of trap formation and subsequent pathogenicity, as well as secondary metabolism. Regulates the artA gene cluster involved in the biosynthesis of arthrosporol that acts as an inhibitor of trap production. Regulates energy metabolism by controlling the production of glycogen and lipids in hyphea.","This protein is a methyltransferase, which means it adds a methyl group to a molecule, typically a protein or a nucleotide. Specifically, it is involved in the biosynthesis of a particular metabolite. 
The methyl group is transferred from S-adenosylmethionine (SAM) to a target molecule. The exact target molecule for this protein is not specified in the provided text, but it is likely to be a metabolite involved in plant defense or secondary metabolism. 
In general, methyltransferases are involved in various cellular processes, including protein modification, nucleic acid modification, and metabolite biosynthesis. They play important roles in regulating gene expression, protein function, and metabolic pathways. 
In the context of the provided text, the protein is involved in the biosynthesis of a metabolite that is likely to be involved in plant defense or secondary metabolism. The exact function of the metabolite is not specified, but it is likely to be involved in protecting the plant against pathogens or herbivores. 
In summary, the molecular function of this protein is to add a methyl group to a target molecule, likely involved in plant defense or secondary metabolism. 
This protein is likely to be involved in the synthesis of a specific metabolite, which is not specified in the provided text. However, based on its classification as a methyltransferase, it is likely to be involved in the synthesis of a metabolite that is involved in plant defense or secondary metabolism. 
The exact function of this protein is not specified in the provided text, but it is likely to be involved in regulating gene expression, protein function, or metabolic pathways. 
This protein is likely to be involved in the synthesis of a specific metabolite, which is not specified in the provided text. However, based on its classification as a methyltransferase, it is likely to be involved in the synthesis of a metabolite that is involved in plant defense or secondary metabolism. 
In summary, the molecular function of this protein is to add a methyl group to a target molecule, likely involved in plant defense or secondary metabolism. 
The protein is likely to be involved in the synthesis of a specific metabolite, which is not specified in the provided text. However, based on its classification as a methyltransferase, it is likely to be involved in the synthesis of a metabolite that is involved in plant defense or secondary metabolism. 
In summary, the molecular function of this protein is to add a methyl group to a target molecule, likely involved in plant defense or secondary metabolism.",No,No,No,Maybe,No,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4271,no
LAEA_ARTFL,A0A437A6S9,Reference,Eukaryota,362,"Component of the velvet transcription factor complex that acts as a global regulator of mycelial growth and chlamydospore production. Plays also a key role in the regulation of trap formation and subsequent pathogenicity, as well as secondary metabolism. Regulates the artA gene cluster involved in the biosynthesis of arthrosporol that acts as an inhibitor of trap production. Regulates energy metabolism by controlling the production of glycogen and lipids in hyphea.","Component of the velvet transcription factor complex that acts as a global regulator of mycelial growth and chlamydospore production. Plays also a key role in the regulation of trap formation and subsequent pathogenicity, as well as secondary metabolism. Regulates the artA gene cluster involved in the biosynthesis of arthrosporol that acts as an inhibitor of trap production. Regulates energy metabolism by controlling the production of glycogen and lipids in hyphea.",,,,,,,GO:0008168,,,,,,,,,,,0,,0.4271,no
PPZC_METMF,A0A455ZKR7,ESM2Text,Eukaryota,374,"2-oxoglutarate-Fe(II) type oxidoreductase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. Within the pathway, ppzC uses peramine as substrate for hydroxylation to yield the novel analog 8-hydroxyperamine. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N-methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8-hydroxyperamine whereas ppzD converts L-proline into trans- 4-hydroxy-L-proline, a precursor of peramine biosynthesis.","2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the benzazepine alkaloid nanangelenin A which contains an unprecedented 3,4-dihydro-1-benzazepine-2,5-dione-N-prenyl-N-acetoxy-anthranilamide scaffold. The first step of nanangelenin biosynthesis is catalyzed by the indoleamine 2,3-dioxygenase nanC which produces N-formyl-kynurenine through the catabolism of tryptophan. The two-module NRPS nanA then utilizes anthranilate (Ant) and L-kynurenine (L-Kyn) to assemble the dipeptide product nanangelenin B. The first adenylation domain of nanA (A1) loads anthranilate onto the T1 domain, while A2 loads kynurenine, generated through spontaneous nonenzymatic deformylation of the nanC-supplied N-formyl-kynurenine. The peptide bond formation between the tethered amino acids is catalyzed by",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0051213; GO:0046872,GO:0016706,GO:0016706,GO:0016706,GO:0016706,GO:0016706; GO:0005506,0.5293,0.5293,0.5293,0.5293,0.7588,5,0.5752,0.324,no
PPZC_METMF,A0A455ZKR7,Prot2Text,Eukaryota,374,"2-oxoglutarate-Fe(II) type oxidoreductase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. Within the pathway, ppzC uses peramine as substrate for hydroxylation to yield the novel analog 8-hydroxyperamine. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N-methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8-hydroxyperamine whereas ppzD converts L-proline into trans- 4-hydroxy-L-proline, a precursor of peramine biosynthesis.","2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0051213; GO:0046872,GO:0016706,GO:0016706,GO:0016706,GO:0016706,GO:0016706,0.5293,0.5293,0.5293,0.5293,0.5293,5,0.5293,0.324,no
PPZC_METMF,A0A455ZKR7,ProtT3,Eukaryota,374,"2-oxoglutarate-Fe(II) type oxidoreductase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. Within the pathway, ppzC uses peramine as substrate for hydroxylation to yield the novel analog 8-hydroxyperamine. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N-methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8-hydroxyperamine whereas ppzD converts L-proline into trans- 4-hydroxy-L-proline, a precursor of peramine biosynthesis.","2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties . L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L- homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB4, as well as enzymes of the primary metabolism (",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0051213; GO:0046872,GO:0016706,GO:0016706,GO:0016706,GO:0016706,GO:0016706,0.5293,0.5293,0.5293,0.5293,0.5293,5,0.5293,0.324,no
PPZC_METMF,A0A455ZKR7,ProtTale,Eukaryota,374,"2-oxoglutarate-Fe(II) type oxidoreductase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. Within the pathway, ppzC uses peramine as substrate for hydroxylation to yield the novel analog 8-hydroxyperamine. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N-methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8-hydroxyperamine whereas ppzD converts L-proline into trans- 4-hydroxy-L-proline, a precursor of peramine biosynthesis.","2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin citrinin, a hepato-nephrotoxic compound to humans due to inhibition of respiration complex III. The pathway begins with the synthesis of a keto-aldehyde intermediate by the citrinin PKS (pksCT) from successive condensations of 4 malonyl-CoA units, presumably with a simple acetyl-CoA starter unit. Release of the keto-aldehyde intermediate is consistent with the presence of the C-terminal reductive release domain. Mp13 functions as a desaturase and catalyzes the",Yes,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0051213; GO:0046872,GO:0016706,GO:0016706,GO:0016706,GO:0016706,GO:0016706,0.5293,0.5293,0.5293,0.5293,0.5293,5,0.5293,0.324,no
PPZC_METMF,A0A455ZKR7,Protein2Text,Eukaryota,374,"2-oxoglutarate-Fe(II) type oxidoreductase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. Within the pathway, ppzC uses peramine as substrate for hydroxylation to yield the novel analog 8-hydroxyperamine. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N-methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8-hydroxyperamine whereas ppzD converts L-proline into trans- 4-hydroxy-L-proline, a precursor of peramine biosynthesis.","The molecular function of this protein is an oxidoreductase activity, specifically involved in the conversion of certain organic compounds. More specifically, it is a component of the hydroxylase complex that catalyzes the oxidation of proline residues in the presence of molecular oxygen, with the concomitant reduction of O2 to H2O. The exact function of this protein is still to be determined.",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0051213; GO:0046872,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.5957,0.5957,0.5957,0.5957,0.5957,5,0.5957,0.324,no
PPZC_METMF,A0A455ZKR7,Reference,Eukaryota,374,"2-oxoglutarate-Fe(II) type oxidoreductase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. Within the pathway, ppzC uses peramine as substrate for hydroxylation to yield the novel analog 8-hydroxyperamine. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N-methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8-hydroxyperamine whereas ppzD converts L-proline into trans- 4-hydroxy-L-proline, a precursor of peramine biosynthesis.","2-oxoglutarate-Fe(II) type oxidoreductase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. Within the pathway, ppzC uses peramine as substrate for hydroxylation to yield the novel analog 8-hydroxyperamine. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N-methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8-hydroxyperamine whereas ppzD converts L-proline into trans- 4-hydroxy-L-proline, a precursor of peramine biosynthesis.",,,,,,,GO:0051213; GO:0046872,GO:0016706,GO:0016706,GO:0016706; GO:0005506,GO:0016706,GO:0016706,0.5293,0.5293,0.7588,0.5293,0.5293,5,0.5752,0.324,no
PPZD_METMF,A0A455ZMR3,ESM2Text,Eukaryota,349,"2-oxoglutarate-Fe(II) type oxidoreductase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. Within the pathway, ppzD converts L-proline into trans-4-hydroxy-L-proline as a major product, yielding a key precursor for peramine biosynthesis. PpzD is also able to convert L-proline into trans-3-hydroxy-L-proline. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N-methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8-hydroxyperamine whereas ppzD converts L-proline into trans- 4-hydroxy-L-proline, a precursor of peramine biosynthesis.","2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of pneumocandins, lipohexapeptides of the echinocandin family that prevent fungal cell wall formation by non-competitive inhibition of beta-1,3-glucan synthase. The 10,12-dimethylmyristoyl side chain is synthesized by the reducing polyketide synthase gloL/GLPKS4. The thioesterase gloN/GLHYD exclusively interacts with gloL/GLPKS4 to maintain turnover of the polyketide side chain. The 10R,12S-dimethylmyristic acid is then transferred to the first thiolation domain of the nonribosomal peptide synthetase gloA/GLNRPS4 by the acyl-AMP ligase gloD/GLligase, followed by its acylation to L-ornithine to trigger elongation of the cyclic hexapeptide. L-ornithine, 4R-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GL",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0051213; GO:0046872,GO:0016706,GO:0016706,GO:0016706,GO:0016706,GO:0016706; GO:0005506,0.5293,0.5293,0.5293,0.5293,0.7588,5,0.5752,0.4022,no
PPZD_METMF,A0A455ZMR3,Prot2Text,Eukaryota,349,"2-oxoglutarate-Fe(II) type oxidoreductase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. Within the pathway, ppzD converts L-proline into trans-4-hydroxy-L-proline as a major product, yielding a key precursor for peramine biosynthesis. PpzD is also able to convert L-proline into trans-3-hydroxy-L-proline. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N-methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8-hydroxyperamine whereas ppzD converts L-proline into trans- 4-hydroxy-L-proline, a precursor of peramine biosynthesis.","2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0051213; GO:0046872,GO:0016706,GO:0016706,GO:0016706,GO:0016706,GO:0016706,0.5293,0.5293,0.5293,0.5293,0.5293,5,0.5293,0.4022,no
PPZD_METMF,A0A455ZMR3,ProtT3,Eukaryota,349,"2-oxoglutarate-Fe(II) type oxidoreductase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. Within the pathway, ppzD converts L-proline into trans-4-hydroxy-L-proline as a major product, yielding a key precursor for peramine biosynthesis. PpzD is also able to convert L-proline into trans-3-hydroxy-L-proline. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N-methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8-hydroxyperamine whereas ppzD converts L-proline into trans- 4-hydroxy-L-proline, a precursor of peramine biosynthesis.",2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms,Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0051213; GO:0046872,GO:0016706,GO:0016706,GO:0016706,GO:0016706,GO:0016706,0.5293,0.5293,0.5293,0.5293,0.5293,5,0.5293,0.4022,no
PPZD_METMF,A0A455ZMR3,ProtTale,Eukaryota,349,"2-oxoglutarate-Fe(II) type oxidoreductase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. Within the pathway, ppzD converts L-proline into trans-4-hydroxy-L-proline as a major product, yielding a key precursor for peramine biosynthesis. PpzD is also able to convert L-proline into trans-3-hydroxy-L-proline. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N-methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8-hydroxyperamine whereas ppzD converts L-proline into trans- 4-hydroxy-L-proline, a precursor of peramine biosynthesis.","2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes nodulisporic acids (NAs). Within the pathway, nodE catalyzes the conversion of nodulisporic acid A to nodulisporic acid B. The geranylgeranyl diphosphate (GGPP) synthase ggs1, localized outside of the cluster, is proposed to catalyze the first step in nodulisporic acid biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3-glycerol",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0051213; GO:0046872,GO:0016706,GO:0016706,GO:0016706,GO:0016706,GO:0016706,0.5293,0.5293,0.5293,0.5293,0.5293,5,0.5293,0.4022,no
PPZD_METMF,A0A455ZMR3,Protein2Text,Eukaryota,349,"2-oxoglutarate-Fe(II) type oxidoreductase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. Within the pathway, ppzD converts L-proline into trans-4-hydroxy-L-proline as a major product, yielding a key precursor for peramine biosynthesis. PpzD is also able to convert L-proline into trans-3-hydroxy-L-proline. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N-methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8-hydroxyperamine whereas ppzD converts L-proline into trans- 4-hydroxy-L-proline, a precursor of peramine biosynthesis.",The molecular function of this protein is an iron-dependent dioxygenase. It is involved in the oxidation of 4-hydroxyphenylpyruvate (4HPP) to form homogentisate (HGA).,Maybe,No,Maybe,No,Maybe,not-Yes,GO:0051213; GO:0046872,GO:0003868,GO:0003868,GO:0003868,GO:0003868,GO:0003868,0.4705,0.4705,0.4705,0.4705,0.4705,5,0.4705,0.4022,no
PPZD_METMF,A0A455ZMR3,Reference,Eukaryota,349,"2-oxoglutarate-Fe(II) type oxidoreductase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. Within the pathway, ppzD converts L-proline into trans-4-hydroxy-L-proline as a major product, yielding a key precursor for peramine biosynthesis. PpzD is also able to convert L-proline into trans-3-hydroxy-L-proline. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N-methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8-hydroxyperamine whereas ppzD converts L-proline into trans- 4-hydroxy-L-proline, a precursor of peramine biosynthesis.","2-oxoglutarate-Fe(II) type oxidoreductase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. Within the pathway, ppzD converts L-proline into trans-4-hydroxy-L-proline as a major product, yielding a key precursor for peramine biosynthesis. PpzD is also able to convert L-proline into trans-3-hydroxy-L-proline. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N-methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8-hydroxyperamine whereas ppzD converts L-proline into trans- 4-hydroxy-L-proline, a precursor of peramine biosynthesis.",,,,,,,GO:0051213; GO:0046872,GO:0016706,GO:0016706,GO:0016706; GO:0005506,GO:0016706,GO:0016706,0.5293,0.5293,0.7588,0.5293,0.5293,5,0.5752,0.4022,no
NLEG1_CITRO,A0A482PJF5,ESM2Text,Bacteria,194,Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is probably an E3 ubiquitin-protein ligase that interferes with the host's ubiquitination pathway and targets host proteins for proteasomal degradation (Probable). Mice infected with a strain of bacteria deleted for this gene have less severe diarrhea.,May play a role in the apoptotic process.,Vague,No,Vague,No,No,not-Yes,GO:0061630,,,,,,,,,,,0,,0.7659,yes
NLEG1_CITRO,A0A482PJF5,Prot2Text,Bacteria,194,Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is probably an E3 ubiquitin-protein ligase that interferes with the host's ubiquitination pathway and targets host proteins for proteasomal degradation (Probable). Mice infected with a strain of bacteria deleted for this gene have less severe diarrhea.,"Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.",No,No,No,No,No,not-Yes,GO:0061630,,,,,,,,,,,0,,0.7659,yes
NLEG1_CITRO,A0A482PJF5,ProtT3,Bacteria,194,Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is probably an E3 ubiquitin-protein ligase that interferes with the host's ubiquitination pathway and targets host proteins for proteasomal degradation (Probable). Mice infected with a strain of bacteria deleted for this gene have less severe diarrhea.,"Acts as an E3 ubiquitin-protein ligase, which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Cytoplasm Nucleus. Belongs to the MLH1 family",Yes,Maybe,Yes,Maybe,Yes,Yes,GO:0061630,GO:0061630,GO:0004842,GO:0061630,GO:0061630,GO:0061630,1.0,0.8312,1.0,1.0,1.0,5,0.9662,0.7659,yes
NLEG1_CITRO,A0A482PJF5,ProtTale,Bacteria,194,Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is probably an E3 ubiquitin-protein ligase that interferes with the host's ubiquitination pathway and targets host proteins for proteasomal degradation (Probable). Mice infected with a strain of bacteria deleted for this gene have less severe diarrhea.,Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin-protein ligase that probably targets host proteins for ubiquitination.,Yes,Yes,Yes,Maybe,Yes,Yes,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0004842,1.0,1.0,1.0,1.0,0.8312,5,0.9662,0.7659,yes
NLEG1_CITRO,A0A482PJF5,Protein2Text,Bacteria,194,Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is probably an E3 ubiquitin-protein ligase that interferes with the host's ubiquitination pathway and targets host proteins for proteasomal degradation (Probable). Mice infected with a strain of bacteria deleted for this gene have less severe diarrhea.,"The molecular function of this protein is not explicitly stated in the provided text, but based on its name and the context in which it is mentioned, it is likely involved in the ubiquitination process. Ubiquitination is a post-translational modification where a ubiquitin protein is attached to a target protein, and it plays a crucial role in various cellular processes such as protein degradation, signaling, and gene regulation. The protein's involvement in the ubiquitination process suggests that it may play a role in the ubiquitin conjugation system, possibly as an E3 ubiquitin ligase or a ubiquitin-conjugating enzyme (E2). However, without further information, it is difficult to determine the specific molecular function of this protein.",Maybe,No,Maybe,Vague,Maybe,not-Yes,GO:0061630,,,,,,,,,,,0,,0.7659,yes
NLEG1_CITRO,A0A482PJF5,Reference,Bacteria,194,Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is probably an E3 ubiquitin-protein ligase that interferes with the host's ubiquitination pathway and targets host proteins for proteasomal degradation (Probable). Mice infected with a strain of bacteria deleted for this gene have less severe diarrhea.,Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is probably an E3 ubiquitin-protein ligase that interferes with the host's ubiquitination pathway and targets host proteins for proteasomal degradation (Probable). Mice infected with a strain of bacteria deleted for this gene have less severe diarrhea.,,,,,,,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,1.0,1.0,1.0,1.0,1.0,5,1.0,0.7659,yes
CHOD_ACIBA,A0A4D6G3C8,ESM2Text,Bacteria,556,"Bifunctional enzyme that catalyzes the oxidation and isomerization of cholesterol to cholestenone (cholest-4-en-3-one), an initial step in the cholesterol degradation process.",Catalyzes the oxidation of medium and long-chain aliphatic alcohols to fatty acids. Involved in the utilization of osmoprotectants such as octanol.,Maybe,No,No,No,Maybe,not-Yes,GO:0016995; GO:0004769,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.5197,0.5197,0.5197,0.5197,0.5197,5,0.5197,0.1795,no
CHOD_ACIBA,A0A4D6G3C8,Prot2Text,Bacteria,556,"Bifunctional enzyme that catalyzes the oxidation and isomerization of cholesterol to cholestenone (cholest-4-en-3-one), an initial step in the cholesterol degradation process.",Involved in the degradation of pentoses. Catalyzes the oxidation of D-fucose and D-mannose.,No,No,No,No,No,not-Yes,GO:0016995; GO:0004769,,GO:0016614,GO:0016614,GO:0016614,GO:0016491,,0.5808,0.5808,0.5808,0.5197,4,0.5655,0.1795,no
CHOD_ACIBA,A0A4D6G3C8,ProtT3,Bacteria,556,"Bifunctional enzyme that catalyzes the oxidation and isomerization of cholesterol to cholestenone (cholest-4-en-3-one), an initial step in the cholesterol degradation process.",Belongs to the GMC oxidoreductase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016995; GO:0004769,GO:0016614,GO:0016614,GO:0016614,GO:0016614,GO:0016614,0.5808,0.5808,0.5808,0.5808,0.5808,5,0.5808,0.1795,no
CHOD_ACIBA,A0A4D6G3C8,ProtTale,Bacteria,556,"Bifunctional enzyme that catalyzes the oxidation and isomerization of cholesterol to cholestenone (cholest-4-en-3-one), an initial step in the cholesterol degradation process.","FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",No,No,No,No,No,not-Yes,GO:0016995; GO:0004769,GO:0004497,GO:0016491; GO:0071949,GO:0004497; GO:0050660,GO:0004497,GO:0004497,0.4162,0.4071,0.3312,0.4162,0.4162,5,0.3974,0.1795,no
CHOD_ACIBA,A0A4D6G3C8,Protein2Text,Bacteria,556,"Bifunctional enzyme that catalyzes the oxidation and isomerization of cholesterol to cholestenone (cholest-4-en-3-one), an initial step in the cholesterol degradation process.","This protein is involved in electron transfer, specifically in the electron transfer chain. It is likely involved in the transfer of electrons from one molecule to another, playing a crucial role in cellular respiration.",No,No,Vague,No,No,not-Yes,GO:0016995; GO:0004769,GO:0009055,GO:0009055,GO:0009055,GO:0009055,,0.2054,0.2054,0.2054,0.2054,,4,0.2054,0.1795,no
CHOD_ACIBA,A0A4D6G3C8,Reference,Bacteria,556,"Bifunctional enzyme that catalyzes the oxidation and isomerization of cholesterol to cholestenone (cholest-4-en-3-one), an initial step in the cholesterol degradation process.","Bifunctional enzyme that catalyzes the oxidation and isomerization of cholesterol to cholestenone (cholest-4-en-3-one), an initial step in the cholesterol degradation process.",,,,,,,GO:0016995; GO:0004769,GO:0016491; GO:0050660,GO:0050554,GO:0016491; GO:0016853,GO:0016491; GO:0016853,GO:0016491; GO:0016853,0.4089,0.1998,0.6019,0.6019,0.6019,5,0.4829,0.1795,no
PL_PLABA,A0A509AL23,ESM2Text,Eukaryota,751,Phospholipase with membrane-lytic activity. Facilitates the passage of sporozoites through cells and enables infection in mammalian hosts. Mediates disruption of the parasitophorous vacuole membrane during the liver stage.,Probable phospholipase.,Yes,Vague,Yes,Maybe,Yes,Yes,GO:0008374,,GO:0004622,GO:0004622,GO:0004622,GO:0016788,,0.1329,0.1329,0.1329,0.2845,4,0.1708,0.4831,no
PL_PLABA,A0A509AL23,Prot2Text,Eukaryota,751,Phospholipase with membrane-lytic activity. Facilitates the passage of sporozoites through cells and enables infection in mammalian hosts. Mediates disruption of the parasitophorous vacuole membrane during the liver stage.,"Required, together with sphingomyelinase, for normal resistance to the incompatible pathogenic bacteria A.brassicicola, B.cereus and H.sativum.",No,No,No,No,Maybe,not-Yes,GO:0008374,,,,,,,,,,,0,,0.4831,no
PL_PLABA,A0A509AL23,ProtT3,Eukaryota,751,Phospholipase with membrane-lytic activity. Facilitates the passage of sporozoites through cells and enables infection in mammalian hosts. Mediates disruption of the parasitophorous vacuole membrane during the liver stage.,Secreted. Belongs to the AB hydrolase superfamily. Lipase family,Vague,Vague,Maybe,Vague,Vague,not-Yes,GO:0008374,GO:0016298,GO:0004806,GO:0016298,GO:0016788,GO:0016298,0.2353,0.1803,0.2353,0.2845,0.2353,5,0.2341,0.4831,no
PL_PLABA,A0A509AL23,ProtTale,Eukaryota,751,Phospholipase with membrane-lytic activity. Facilitates the passage of sporozoites through cells and enables infection in mammalian hosts. Mediates disruption of the parasitophorous vacuole membrane during the liver stage.,"Involved in the biosynthesis of sphingoid long-chain bases (LCBs), which are important components of the membrane structure of mitochondria. Catalyzes the first step of the pathway, i.e. the adenylation of sulfoquinovosyl diacylglycerol (SQDG or sulfoquinovosyl diacylglycerol phosphate) to yield sulfoquinovosyl diacylglycerol monophosphate (SQDMP or sulfoquinovosyl diacylglycerol diphosphate).",No,No,No,No,No,not-Yes,GO:0008374,GO:0016874,,,,,0.3552,,,,,1,0.3552,0.4831,no
PL_PLABA,A0A509AL23,Protein2Text,Eukaryota,751,Phospholipase with membrane-lytic activity. Facilitates the passage of sporozoites through cells and enables infection in mammalian hosts. Mediates disruption of the parasitophorous vacuole membrane during the liver stage.,"This protein is involved in the molecular function of binding to other molecules, specifically in the process of binding to host cells to facilitate infection. It is a part of the molecular machinery that allows the virus to attach to and enter host cells, and is essential for the virus's ability to replicate and spread.",No,Vague,Vague,No,No,not-Yes,GO:0008374,,,,,,,,,,,0,,0.4831,no
PL_PLABA,A0A509AL23,Reference,Eukaryota,751,Phospholipase with membrane-lytic activity. Facilitates the passage of sporozoites through cells and enables infection in mammalian hosts. Mediates disruption of the parasitophorous vacuole membrane during the liver stage.,Phospholipase with membrane-lytic activity. Facilitates the passage of sporozoites through cells and enables infection in mammalian hosts. Mediates disruption of the parasitophorous vacuole membrane during the liver stage.,,,,,,,GO:0008374,GO:0004622,GO:0004620,GO:0004620,GO:0004620,,0.1329,0.1737,0.1737,0.1737,,4,0.1635,0.4831,no
PENIC_PENPA,A0A516F3Z6,ESM2Text,Eukaryota,614,"Baeyer-Villiger monooxygenase; part of the gene cluster that mediates the biosynthesis of penifulvin A, a potent insecticidal sesquiterpene that features a [5.5.5.6]dioxafenestrane ring. Within the pathway, peniC is responsible for the final regioselective Baeyer-Villiger oxidation of gamma-lactone-2- keto[5.5.5.5]fenestran between C1 and C2 to form the delta-lactone moiety of penifulvin A. The first step of the pathway is performed by the sesquiterpene cyclase peniA that generates the angular triquinane scaffold silphinene via cyclization of the linear farnesyl pyrophosphate (FPP). The cytochrome P450 monooxygenase peniB and the flavin-dependent monooxygenase peniC then catalyze a series of oxidation reactions to transform silphinene into penifulvin A.","FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ. Paxilline is converted to beta",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004497,GO:0004497; GO:0071949,GO:0004497,GO:0016491,GO:0004497; GO:0071949,GO:0004497; GO:0071949,0.6988,1.0,0.8145,0.6988,0.6988,5,0.7822,0.3601,no
PENIC_PENPA,A0A516F3Z6,Prot2Text,Eukaryota,614,"Baeyer-Villiger monooxygenase; part of the gene cluster that mediates the biosynthesis of penifulvin A, a potent insecticidal sesquiterpene that features a [5.5.5.6]dioxafenestrane ring. Within the pathway, peniC is responsible for the final regioselective Baeyer-Villiger oxidation of gamma-lactone-2- keto[5.5.5.5]fenestran between C1 and C2 to form the delta-lactone moiety of penifulvin A. The first step of the pathway is performed by the sesquiterpene cyclase peniA that generates the angular triquinane scaffold silphinene via cyclization of the linear farnesyl pyrophosphate (FPP). The cytochrome P450 monooxygenase peniB and the flavin-dependent monooxygenase peniC then catalyze a series of oxidation reactions to transform silphinene into penifulvin A.","FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3601,no
PENIC_PENPA,A0A516F3Z6,ProtT3,Eukaryota,614,"Baeyer-Villiger monooxygenase; part of the gene cluster that mediates the biosynthesis of penifulvin A, a potent insecticidal sesquiterpene that features a [5.5.5.6]dioxafenestrane ring. Within the pathway, peniC is responsible for the final regioselective Baeyer-Villiger oxidation of gamma-lactone-2- keto[5.5.5.5]fenestran between C1 and C2 to form the delta-lactone moiety of penifulvin A. The first step of the pathway is performed by the sesquiterpene cyclase peniA that generates the angular triquinane scaffold silphinene via cyclization of the linear farnesyl pyrophosphate (FPP). The cytochrome P450 monooxygenase peniB and the flavin-dependent monooxygenase peniC then catalyze a series of oxidation reactions to transform silphinene into penifulvin A.",FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeranylindole (3-,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004497,GO:0004497; GO:0071949,GO:0004497; GO:0071949,GO:0004497; GO:0071949,GO:0004497; GO:0071949,GO:0004497; GO:0071949,0.6988,0.6988,0.6988,0.6988,0.6988,5,0.6988,0.3601,no
PENIC_PENPA,A0A516F3Z6,ProtTale,Eukaryota,614,"Baeyer-Villiger monooxygenase; part of the gene cluster that mediates the biosynthesis of penifulvin A, a potent insecticidal sesquiterpene that features a [5.5.5.6]dioxafenestrane ring. Within the pathway, peniC is responsible for the final regioselective Baeyer-Villiger oxidation of gamma-lactone-2- keto[5.5.5.5]fenestran between C1 and C2 to form the delta-lactone moiety of penifulvin A. The first step of the pathway is performed by the sesquiterpene cyclase peniA that generates the angular triquinane scaffold silphinene via cyclization of the linear farnesyl pyrophosphate (FPP). The cytochrome P450 monooxygenase peniB and the flavin-dependent monooxygenase peniC then catalyze a series of oxidation reactions to transform silphinene into penifulvin A.","Catalyzes a Baeyer-Villiger oxidation reaction, i.e. the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, when coupled with the reduction of CO(2) to carbon dioxide. Mediates the oxidation of 4-methyl-2-oxopentanoic acid to 4-methyl-2,4-dioxopentanoic acid.",Yes,Maybe,Yes,Maybe,Yes,Yes,GO:0004497,GO:0004497,GO:0016491; GO:0018579,GO:0004497,GO:0004497,GO:0004497,1.0,0.6896,1.0,1.0,1.0,5,0.9379,0.3601,no
PENIC_PENPA,A0A516F3Z6,Protein2Text,Eukaryota,614,"Baeyer-Villiger monooxygenase; part of the gene cluster that mediates the biosynthesis of penifulvin A, a potent insecticidal sesquiterpene that features a [5.5.5.6]dioxafenestrane ring. Within the pathway, peniC is responsible for the final regioselective Baeyer-Villiger oxidation of gamma-lactone-2- keto[5.5.5.5]fenestran between C1 and C2 to form the delta-lactone moiety of penifulvin A. The first step of the pathway is performed by the sesquiterpene cyclase peniA that generates the angular triquinane scaffold silphinene via cyclization of the linear farnesyl pyrophosphate (FPP). The cytochrome P450 monooxygenase peniB and the flavin-dependent monooxygenase peniC then catalyze a series of oxidation reactions to transform silphinene into penifulvin A.","The molecular function of this protein is to catalyze the oxidation of a substrate, specifically it is involved in the oxidation of a nitrogen-containing compound, likely a type of amino acid or other organic nitrogen-containing molecule. This is inferred from its classification as a cytochrome P450 monooxygenase, which are enzymes that catalyze the incorporation of an oxygen atom into a substrate, typically resulting in the formation of an epoxide, hydroxyl, or other oxygen-containing functional group.",Vague,No,No,No,Vague,not-Yes,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3601,no
PENIC_PENPA,A0A516F3Z6,Reference,Eukaryota,614,"Baeyer-Villiger monooxygenase; part of the gene cluster that mediates the biosynthesis of penifulvin A, a potent insecticidal sesquiterpene that features a [5.5.5.6]dioxafenestrane ring. Within the pathway, peniC is responsible for the final regioselective Baeyer-Villiger oxidation of gamma-lactone-2- keto[5.5.5.5]fenestran between C1 and C2 to form the delta-lactone moiety of penifulvin A. The first step of the pathway is performed by the sesquiterpene cyclase peniA that generates the angular triquinane scaffold silphinene via cyclization of the linear farnesyl pyrophosphate (FPP). The cytochrome P450 monooxygenase peniB and the flavin-dependent monooxygenase peniC then catalyze a series of oxidation reactions to transform silphinene into penifulvin A.","Baeyer-Villiger monooxygenase; part of the gene cluster that mediates the biosynthesis of penifulvin A, a potent insecticidal sesquiterpene that features a [5.5.5.6]dioxafenestrane ring. Within the pathway, peniC is responsible for the final regioselective Baeyer-Villiger oxidation of gamma-lactone-2- keto[5.5.5.5]fenestran between C1 and C2 to form the delta-lactone moiety of penifulvin A. The first step of the pathway is performed by the sesquiterpene cyclase peniA that generates the angular triquinane scaffold silphinene via cyclization of the linear farnesyl pyrophosphate (FPP). The cytochrome P450 monooxygenase peniB and the flavin-dependent monooxygenase peniC then catalyze a series of oxidation reactions to transform silphinene into penifulvin A.",,,,,,,GO:0004497,GO:0004497,GO:0004497,GO:0004497; GO:0050660,GO:0004497; GO:0071949,GO:0004497,1.0,1.0,0.7012,0.6988,1.0,5,0.88,0.3601,no
PENIA_PENPA,A0A516F405,ESM2Text,Eukaryota,372,"Sesquiterpene cyclase; part of the gene cluster that mediates the biosynthesis of penifulvin A, a potent insecticidal sesquiterpene that features a [5.5.5.6]dioxafenestrane ring. Within the pathway, peniA catalyzes the first step and generates the angular triquinane scaffold silphinene via cyclization of the linear farnesyl pyrophosphate (FPP). The cytochrome P450 monooxygenase peniB and the flavin-dependent monooxygenase peniC then catalyze a series of oxidation reactions to transform silphinene into penifulvin A.",Catalyzes the cyclization of farnesyl diphosphate (FPP) to the sesquiterpene germacrene A.,Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0016829,GO:0010333,GO:0000287; GO:0016829,GO:0010333,GO:0010333,0.4539,0.6963,0.7355,0.6963,0.6963,5,0.6557,0.2307,no
PENIA_PENPA,A0A516F405,Prot2Text,Eukaryota,372,"Sesquiterpene cyclase; part of the gene cluster that mediates the biosynthesis of penifulvin A, a potent insecticidal sesquiterpene that features a [5.5.5.6]dioxafenestrane ring. Within the pathway, peniA catalyzes the first step and generates the angular triquinane scaffold silphinene via cyclization of the linear farnesyl pyrophosphate (FPP). The cytochrome P450 monooxygenase peniB and the flavin-dependent monooxygenase peniC then catalyze a series of oxidation reactions to transform silphinene into penifulvin A.","Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to yield the bicyclic sesquiterpene eremophilene via a 1,10-cyclization, which requires the abstraction of the pyrophosphate from FPP to yield the (E,E)-germacradienyl cation. The only accepted substrate is farnesyl diphosphate (FPP).",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0046872; GO:0010333,,GO:0010333,GO:0010333,GO:0010333,GO:0010333,,0.6963,0.6963,0.6963,0.6963,4,0.6963,0.2307,no
PENIA_PENPA,A0A516F405,ProtT3,Eukaryota,372,"Sesquiterpene cyclase; part of the gene cluster that mediates the biosynthesis of penifulvin A, a potent insecticidal sesquiterpene that features a [5.5.5.6]dioxafenestrane ring. Within the pathway, peniA catalyzes the first step and generates the angular triquinane scaffold silphinene via cyclization of the linear farnesyl pyrophosphate (FPP). The cytochrome P450 monooxygenase peniB and the flavin-dependent monooxygenase peniC then catalyze a series of oxidation reactions to transform silphinene into penifulvin A.","Terpene synthase that catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) into the sesquiterpene (E)-beta-caryophyllene. Belongs to the terpene synthase family",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0010333,GO:0010333,GO:0016829,GO:0010333,GO:0016829,0.6963,0.6963,0.4539,0.6963,0.4539,5,0.5993,0.2307,no
PENIA_PENPA,A0A516F405,ProtTale,Eukaryota,372,"Sesquiterpene cyclase; part of the gene cluster that mediates the biosynthesis of penifulvin A, a potent insecticidal sesquiterpene that features a [5.5.5.6]dioxafenestrane ring. Within the pathway, peniA catalyzes the first step and generates the angular triquinane scaffold silphinene via cyclization of the linear farnesyl pyrophosphate (FPP). The cytochrome P450 monooxygenase peniB and the flavin-dependent monooxygenase peniC then catalyze a series of oxidation reactions to transform silphinene into penifulvin A.","Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to yield the bicyclic sesquiterpene (+)-gamma-cadinene via a 1,10-cyclization, which requires the abstraction of the pyrophosphate from FPP to yield a (+)-germacradienyl cation. The only accepted substrate is farnesyl diphosphate (FPP).",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0010333,GO:0010333,GO:0016829,GO:0010333,GO:0010333,0.6963,0.6963,0.4539,0.6963,0.6963,5,0.6478,0.2307,no
PENIA_PENPA,A0A516F405,Protein2Text,Eukaryota,372,"Sesquiterpene cyclase; part of the gene cluster that mediates the biosynthesis of penifulvin A, a potent insecticidal sesquiterpene that features a [5.5.5.6]dioxafenestrane ring. Within the pathway, peniA catalyzes the first step and generates the angular triquinane scaffold silphinene via cyclization of the linear farnesyl pyrophosphate (FPP). The cytochrome P450 monooxygenase peniB and the flavin-dependent monooxygenase peniC then catalyze a series of oxidation reactions to transform silphinene into penifulvin A.","The molecular function of this protein is a part of a larger category of proteins called isomerase, specifically a terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) into the sesquiterpene (+)-santalene.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0010334,GO:0010334,GO:0000981,GO:0000981,,0.6051,0.6051,0.1264,0.1264,,4,0.3658,0.2307,no
PENIA_PENPA,A0A516F405,Reference,Eukaryota,372,"Sesquiterpene cyclase; part of the gene cluster that mediates the biosynthesis of penifulvin A, a potent insecticidal sesquiterpene that features a [5.5.5.6]dioxafenestrane ring. Within the pathway, peniA catalyzes the first step and generates the angular triquinane scaffold silphinene via cyclization of the linear farnesyl pyrophosphate (FPP). The cytochrome P450 monooxygenase peniB and the flavin-dependent monooxygenase peniC then catalyze a series of oxidation reactions to transform silphinene into penifulvin A.","Sesquiterpene cyclase; part of the gene cluster that mediates the biosynthesis of penifulvin A, a potent insecticidal sesquiterpene that features a [5.5.5.6]dioxafenestrane ring. Within the pathway, peniA catalyzes the first step and generates the angular triquinane scaffold silphinene via cyclization of the linear farnesyl pyrophosphate (FPP). The cytochrome P450 monooxygenase peniB and the flavin-dependent monooxygenase peniC then catalyze a series of oxidation reactions to transform silphinene into penifulvin A.",,,,,,,GO:0046872; GO:0010333,GO:0010333,GO:0010333,GO:0010333,GO:0010333,GO:0016829,0.6963,0.6963,0.6963,0.6963,0.4539,5,0.6478,0.2307,no
PENIE_PENPA,A0A516F409,ESM2Text,Eukaryota,481,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of penifulvin A, a potent insecticidal sesquiterpene that features a [5.5.5.6]dioxafenestrane ring. The first step of the pathway is performed by the sesquiterpene cyclase peniA that generates the angular triquinane scaffold silphinene via cyclization of the linear farnesyl pyrophosphate (FPP). The cytochrome P450 monooxygenase peniB and the flavin-dependent monooxygenase peniC then catalyze a series of oxidation reactions to transform silphinene into penifulvin A. The dioxygenases peniD and peniF, as well as the acetyltransferase peniE, do not seem to be involved in the biosynthesis of penifulvin A.","Catalase; part of the gene cluster that mediates the biosynthesis of the mycotoxin citrinin, a hepato-nephrotoxic compound to humans due to inhibition of respiration complex III (Ref.1). The first step is performed by the citrinin synthase PKS6 which condenses adenosine monophosphate with 6 malonyl-CoA units to form the precursor of citrinin (Ref.1). Citrinin is then probably oxidized to a bylast dihydroxylated by the cytochrome P450 monooxygenase PKS8 (Ref.1). Citrinin O-methyltransferase then methylates citrinin to produce citrinin adenine dinucleotide (Ref.1). The methyltransferase MMD1 then catalyzes the methylation at C-2 of the dihydroxyl group, followed by a further C-2 methylation to produce citrinin (Ref.1). Citrinin O-methyltransferase catalyzes the C-3 methylation to yield monolinciprin (Ref.1). The intermediate monolinciprin is then transported across the plasma membrane by a monolinciprin reductase",No,No,No,No,No,not-Yes,GO:0016746,GO:0004096,GO:0004096,,GO:0004096,GO:0004096,0.2778,0.2778,,0.2778,0.2778,4,0.2778,0.2355,no
PENIE_PENPA,A0A516F409,Prot2Text,Eukaryota,481,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of penifulvin A, a potent insecticidal sesquiterpene that features a [5.5.5.6]dioxafenestrane ring. The first step of the pathway is performed by the sesquiterpene cyclase peniA that generates the angular triquinane scaffold silphinene via cyclization of the linear farnesyl pyrophosphate (FPP). The cytochrome P450 monooxygenase peniB and the flavin-dependent monooxygenase peniC then catalyze a series of oxidation reactions to transform silphinene into penifulvin A. The dioxygenases peniD and peniF, as well as the acetyltransferase peniE, do not seem to be involved in the biosynthesis of penifulvin A.","2-O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential tr",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016746,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.729,0.729,0.729,0.729,0.729,5,0.729,0.2355,no
PENIE_PENPA,A0A516F409,ProtT3,Eukaryota,481,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of penifulvin A, a potent insecticidal sesquiterpene that features a [5.5.5.6]dioxafenestrane ring. The first step of the pathway is performed by the sesquiterpene cyclase peniA that generates the angular triquinane scaffold silphinene via cyclization of the linear farnesyl pyrophosphate (FPP). The cytochrome P450 monooxygenase peniB and the flavin-dependent monooxygenase peniC then catalyze a series of oxidation reactions to transform silphinene into penifulvin A. The dioxygenases peniD and peniF, as well as the acetyltransferase peniE, do not seem to be involved in the biosynthesis of penifulvin A.","Acetyltransferase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties . L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L- homoserine by cluster enzymes aspartate kinase FUB5 and homoserine O- acetyltransferase FUB6, as well as enzymes of the primary metabolism",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016746,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.729,0.729,0.729,0.729,0.729,5,0.729,0.2355,no
PENIE_PENPA,A0A516F409,ProtTale,Eukaryota,481,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of penifulvin A, a potent insecticidal sesquiterpene that features a [5.5.5.6]dioxafenestrane ring. The first step of the pathway is performed by the sesquiterpene cyclase peniA that generates the angular triquinane scaffold silphinene via cyclization of the linear farnesyl pyrophosphate (FPP). The cytochrome P450 monooxygenase peniB and the flavin-dependent monooxygenase peniC then catalyze a series of oxidation reactions to transform silphinene into penifulvin A. The dioxygenases peniD and peniF, as well as the acetyltransferase peniE, do not seem to be involved in the biosynthesis of penifulvin A.","Acyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0016746,GO:0016746,GO:0016747,GO:0016747,GO:0016747,GO:0016747,1.0,0.8416,0.8416,0.8416,0.8416,5,0.8733,0.2355,no
PENIE_PENPA,A0A516F409,Protein2Text,Eukaryota,481,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of penifulvin A, a potent insecticidal sesquiterpene that features a [5.5.5.6]dioxafenestrane ring. The first step of the pathway is performed by the sesquiterpene cyclase peniA that generates the angular triquinane scaffold silphinene via cyclization of the linear farnesyl pyrophosphate (FPP). The cytochrome P450 monooxygenase peniB and the flavin-dependent monooxygenase peniC then catalyze a series of oxidation reactions to transform silphinene into penifulvin A. The dioxygenases peniD and peniF, as well as the acetyltransferase peniE, do not seem to be involved in the biosynthesis of penifulvin A.",This protein is involved in the molecular function of acyltransferase activity.,Maybe,Maybe,Yes,Vague,Maybe,not-Yes,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016746,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2355,no
PENIE_PENPA,A0A516F409,Reference,Eukaryota,481,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of penifulvin A, a potent insecticidal sesquiterpene that features a [5.5.5.6]dioxafenestrane ring. The first step of the pathway is performed by the sesquiterpene cyclase peniA that generates the angular triquinane scaffold silphinene via cyclization of the linear farnesyl pyrophosphate (FPP). The cytochrome P450 monooxygenase peniB and the flavin-dependent monooxygenase peniC then catalyze a series of oxidation reactions to transform silphinene into penifulvin A. The dioxygenases peniD and peniF, as well as the acetyltransferase peniE, do not seem to be involved in the biosynthesis of penifulvin A.","Acetyltransferase; part of the gene cluster that mediates the biosynthesis of penifulvin A, a potent insecticidal sesquiterpene that features a [5.5.5.6]dioxafenestrane ring. The first step of the pathway is performed by the sesquiterpene cyclase peniA that generates the angular triquinane scaffold silphinene via cyclization of the linear farnesyl pyrophosphate (FPP). The cytochrome P450 monooxygenase peniB and the flavin-dependent monooxygenase peniC then catalyze a series of oxidation reactions to transform silphinene into penifulvin A. The dioxygenases peniD and peniF, as well as the acetyltransferase peniE, do not seem to be involved in the biosynthesis of penifulvin A.",,,,,,,GO:0016746,,GO:0016747,GO:0016407,GO:0016407,GO:0016746,,0.8416,0.729,0.729,1.0,4,0.8249,0.2355,no
C1BQ5_MELAZ,A0A5B8NEF2,ESM2Text,Eukaryota,501,"Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as azadirachtin, an antifeedant widely used as bioinsecticide, and possessing many medicinal applications including anti-tumoral, anti-malarial, anti-rheumatic, antibacterial, anti-inflammatory, anti-pyretic and diuretic effects. Catalyzes the conversion of dihydroniloticin to the protolimonoid melianol.","Involved in the biosynthesis of germacrene-derived sesquiterpene lactones. Hydroxylates germacrene A acid to 8-beta-hydroxy-germacrene A acid, a precursor of sesquiterpene lactones that are potent tremorgens in mammals.",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0016491,0.5872,0.5872,0.5872,0.5872,0.5572,5,0.5812,0.3985,no
C1BQ5_MELAZ,A0A5B8NEF2,Prot2Text,Eukaryota,501,"Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as azadirachtin, an antifeedant widely used as bioinsecticide, and possessing many medicinal applications including anti-tumoral, anti-malarial, anti-rheumatic, antibacterial, anti-inflammatory, anti-pyretic and diuretic effects. Catalyzes the conversion of dihydroniloticin to the protolimonoid melianol.","Forms a complex with CYP98A4 that catalyzes the conversion of the short chain elongated methionines di-, tri-, and tetrahomomethionine to their respective aldoximes 5-methylthiopentanaldoxime and 7-methylheptanaldoxime.",Maybe,No,No,No,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497,,GO:0004497,GO:0004497,GO:0004497,0.5872,,0.5872,0.5872,0.5872,4,0.5872,0.3985,no
C1BQ5_MELAZ,A0A5B8NEF2,ProtT3,Eukaryota,501,"Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as azadirachtin, an antifeedant widely used as bioinsecticide, and possessing many medicinal applications including anti-tumoral, anti-malarial, anti-rheumatic, antibacterial, anti-inflammatory, anti-pyretic and diuretic effects. Catalyzes the conversion of dihydroniloticin to the protolimonoid melianol.",Membrane; Single-pass membrane protein. Belongs to the cytochrome P450 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497,GO:0004497; GO:0020037,GO:0004497; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,0.5872,0.8149,0.8149,0.9516,0.9516,5,0.824,0.3985,no
C1BQ5_MELAZ,A0A5B8NEF2,ProtTale,Eukaryota,501,"Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as azadirachtin, an antifeedant widely used as bioinsecticide, and possessing many medicinal applications including anti-tumoral, anti-malarial, anti-rheumatic, antibacterial, anti-inflammatory, anti-pyretic and diuretic effects. Catalyzes the conversion of dihydroniloticin to the protolimonoid melianol.","Cytochrome P450 monooxygenase involved in the biosynthesis of indole-3-acetic acid (IAA)-amido acids, a family of plant hormones known as auxin. Catalyzes the hydroxylation of IAA-amido acids at C-3 to produce 2-oxindole-3-acetic acid (2-oxIAA)-amido acids.",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497; GO:0020037,GO:0004497; GO:0016491,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497,0.8149,0.6619,0.9516,0.9516,0.5872,5,0.7934,0.3985,no
C1BQ5_MELAZ,A0A5B8NEF2,Protein2Text,Eukaryota,501,"Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as azadirachtin, an antifeedant widely used as bioinsecticide, and possessing many medicinal applications including anti-tumoral, anti-malarial, anti-rheumatic, antibacterial, anti-inflammatory, anti-pyretic and diuretic effects. Catalyzes the conversion of dihydroniloticin to the protolimonoid melianol.","The molecular function of this protein is to catalyze a reaction. More specifically, it is involved in the biosynthesis of a compound that is a precursor to a plant hormone. The protein is a member of the cytochrome P450 family, which is a group of enzymes that catalyze a wide range of reactions, including the hydroxylation of organic compounds. The specific reaction catalyzed by this protein is the hydroxylation of a molecule called gibberellin A20 (GA20), which is a precursor to the plant hormone gibberellin A1 (GA1). The protein is also involved in the biosynthesis of other gibberellins, including GA3 and GA4.

The molecular function of this protein can be summarized as follows:

* Catalyzes the hydroxylation of gibberellin A20 (GA20) to produce gibberellin A1 (GA1)
* Involved in the biosynthesis of other gibberellins, including GA3 and GA4
* Member of the cytochrome P450 family of enzymes
* Catalyzes a wide range of reactions, including the hydroxylation of organic compounds

Overall, the molecular function of this protein is to play a key role in the biosynthesis of gibberellins, which are important plant hormones that regulate plant growth and development.",Vague,No,Maybe,No,Vague,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.5872,0.5872,0.5872,0.5872,0.5872,5,0.5872,0.3985,no
C1BQ5_MELAZ,A0A5B8NEF2,Reference,Eukaryota,501,"Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as azadirachtin, an antifeedant widely used as bioinsecticide, and possessing many medicinal applications including anti-tumoral, anti-malarial, anti-rheumatic, antibacterial, anti-inflammatory, anti-pyretic and diuretic effects. Catalyzes the conversion of dihydroniloticin to the protolimonoid melianol.","Monooxygenase involved in the biosynthesis of limonoids triterpene natural products such as azadirachtin, an antifeedant widely used as bioinsecticide, and possessing many medicinal applications including anti-tumoral, anti-malarial, anti-rheumatic, antibacterial, anti-inflammatory, anti-pyretic and diuretic effects. Catalyzes the conversion of dihydroniloticin to the protolimonoid melianol.",,,,,,,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.5872,0.5872,0.5872,0.5872,0.5872,5,0.5872,0.3985,no
AVEE_ASPAV,A0A5N6TQL1,ESM2Text,Eukaryota,470,"Flavin-dependent halogenase; part of the ave gene cluster that mediates the biosynthesis of the dipeptide L-Leu-L-Cl-Isd also called isoindolamide A. Within the pathway, aveE is responsible for the chlorination at C-6 of R-dihydroxymethyl isoindolinone to generate the amino acid chloro-O-isoindolinone-L- homoserine (L-Cl-Isd). It is possible that it can also chlorinate L- Leu-L-Isd to produce L-Leu-L-Cl-Isd (isoindolamide A). The alanine racemase aveF first catalyzes the interconversion between L-alanine and D-alanine. D-alanine is then activated by the NRPS aveC that transfers it to the PKS aveA to produce R-dihydroxymethyl isoindolinone. The flavin-dependent halogenase aveE catalyzes C-6 chlorination of R-dihydroxymethyl isoindolinone. AveG then catalyzes the gamma-replacement of acetate in O-acetyl-L- homoserine (OAH) with C-6 chlorinated R-dihydroxymethyl isoindolinone to generate the amino acid chloro-O-isoindolinone-L-homoserine (L-Cl- Isd). Finally the ATP-grasp enzyme aveB acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Cl-Isd to give the dipeptide L-Leu-L-Cl-Isd also called isoindolamide A.",Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R2 contains the binding site for both substrate A and substrate B.,No,No,No,No,No,not-Yes,GO:0071949; GO:0004497,GO:0004748,GO:0004748,GO:0004748,GO:0004748,GO:0004748,0.3053,0.3053,0.3053,0.3053,0.3053,5,0.3053,0.1925,no
AVEE_ASPAV,A0A5N6TQL1,Prot2Text,Eukaryota,470,"Flavin-dependent halogenase; part of the ave gene cluster that mediates the biosynthesis of the dipeptide L-Leu-L-Cl-Isd also called isoindolamide A. Within the pathway, aveE is responsible for the chlorination at C-6 of R-dihydroxymethyl isoindolinone to generate the amino acid chloro-O-isoindolinone-L- homoserine (L-Cl-Isd). It is possible that it can also chlorinate L- Leu-L-Isd to produce L-Leu-L-Cl-Isd (isoindolamide A). The alanine racemase aveF first catalyzes the interconversion between L-alanine and D-alanine. D-alanine is then activated by the NRPS aveC that transfers it to the PKS aveA to produce R-dihydroxymethyl isoindolinone. The flavin-dependent halogenase aveE catalyzes C-6 chlorination of R-dihydroxymethyl isoindolinone. AveG then catalyzes the gamma-replacement of acetate in O-acetyl-L- homoserine (OAH) with C-6 chlorinated R-dihydroxymethyl isoindolinone to generate the amino acid chloro-O-isoindolinone-L-homoserine (L-Cl- Isd). Finally the ATP-grasp enzyme aveB acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Cl-Isd to give the dipeptide L-Leu-L-Cl-Isd also called isoindolamide A.","Flavin-dependent halogenase; part of the gene cluster that mediates the biosynthesis of the diterpenoid pyrones higginsianins A and B. The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpchA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpchD through the action of the prenyltransferase dpchC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpchE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpchB (Probable). The short chain dehydrogenase/reductase dpchG then oxidizes the",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0071949; GO:0004497,,,GO:0016491,GO:0016491,GO:0016491,,,0.5823,0.5823,0.5823,3,0.5823,0.1925,no
AVEE_ASPAV,A0A5N6TQL1,ProtT3,Eukaryota,470,"Flavin-dependent halogenase; part of the ave gene cluster that mediates the biosynthesis of the dipeptide L-Leu-L-Cl-Isd also called isoindolamide A. Within the pathway, aveE is responsible for the chlorination at C-6 of R-dihydroxymethyl isoindolinone to generate the amino acid chloro-O-isoindolinone-L- homoserine (L-Cl-Isd). It is possible that it can also chlorinate L- Leu-L-Isd to produce L-Leu-L-Cl-Isd (isoindolamide A). The alanine racemase aveF first catalyzes the interconversion between L-alanine and D-alanine. D-alanine is then activated by the NRPS aveC that transfers it to the PKS aveA to produce R-dihydroxymethyl isoindolinone. The flavin-dependent halogenase aveE catalyzes C-6 chlorination of R-dihydroxymethyl isoindolinone. AveG then catalyzes the gamma-replacement of acetate in O-acetyl-L- homoserine (OAH) with C-6 chlorinated R-dihydroxymethyl isoindolinone to generate the amino acid chloro-O-isoindolinone-L-homoserine (L-Cl- Isd). Finally the ATP-grasp enzyme aveB acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Cl-Isd to give the dipeptide L-Leu-L-Cl-Isd also called isoindolamide A.",Flavin-dependent halogenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-ger,Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0071949; GO:0004497,GO:0016491,GO:0016491,GO:0016491; GO:0050660,GO:0016491,GO:0016491,0.5823,0.5823,0.8646,0.5823,0.5823,5,0.6388,0.1925,no
AVEE_ASPAV,A0A5N6TQL1,ProtTale,Eukaryota,470,"Flavin-dependent halogenase; part of the ave gene cluster that mediates the biosynthesis of the dipeptide L-Leu-L-Cl-Isd also called isoindolamide A. Within the pathway, aveE is responsible for the chlorination at C-6 of R-dihydroxymethyl isoindolinone to generate the amino acid chloro-O-isoindolinone-L- homoserine (L-Cl-Isd). It is possible that it can also chlorinate L- Leu-L-Isd to produce L-Leu-L-Cl-Isd (isoindolamide A). The alanine racemase aveF first catalyzes the interconversion between L-alanine and D-alanine. D-alanine is then activated by the NRPS aveC that transfers it to the PKS aveA to produce R-dihydroxymethyl isoindolinone. The flavin-dependent halogenase aveE catalyzes C-6 chlorination of R-dihydroxymethyl isoindolinone. AveG then catalyzes the gamma-replacement of acetate in O-acetyl-L- homoserine (OAH) with C-6 chlorinated R-dihydroxymethyl isoindolinone to generate the amino acid chloro-O-isoindolinone-L-homoserine (L-Cl- Isd). Finally the ATP-grasp enzyme aveB acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Cl-Isd to give the dipeptide L-Leu-L-Cl-Isd also called isoindolamide A.","Involved in the biosynthesis of the insect-specific pigment pyralin. Catalyzes the oxidative decarboxylation of L-3,4- dihydroxyphenylalanine (L-DOPA) to 3,4-dihydroxyphenylalanine (DOPA).",No,No,No,No,No,not-Yes,GO:0071949; GO:0004497,GO:0016831,GO:0016491,,GO:0016491; GO:0016831,GO:0016491,0.2459,0.5823,,0.5189,0.5823,4,0.4824,0.1925,no
AVEE_ASPAV,A0A5N6TQL1,Protein2Text,Eukaryota,470,"Flavin-dependent halogenase; part of the ave gene cluster that mediates the biosynthesis of the dipeptide L-Leu-L-Cl-Isd also called isoindolamide A. Within the pathway, aveE is responsible for the chlorination at C-6 of R-dihydroxymethyl isoindolinone to generate the amino acid chloro-O-isoindolinone-L- homoserine (L-Cl-Isd). It is possible that it can also chlorinate L- Leu-L-Isd to produce L-Leu-L-Cl-Isd (isoindolamide A). The alanine racemase aveF first catalyzes the interconversion between L-alanine and D-alanine. D-alanine is then activated by the NRPS aveC that transfers it to the PKS aveA to produce R-dihydroxymethyl isoindolinone. The flavin-dependent halogenase aveE catalyzes C-6 chlorination of R-dihydroxymethyl isoindolinone. AveG then catalyzes the gamma-replacement of acetate in O-acetyl-L- homoserine (OAH) with C-6 chlorinated R-dihydroxymethyl isoindolinone to generate the amino acid chloro-O-isoindolinone-L-homoserine (L-Cl- Isd). Finally the ATP-grasp enzyme aveB acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Cl-Isd to give the dipeptide L-Leu-L-Cl-Isd also called isoindolamide A.","This protein is a part of the electron transport chain and is involved in the transfer of electrons from a donor to a acceptor, specifically in the conversion of nitrate to nitrite.",No,No,No,No,No,not-Yes,GO:0071949; GO:0004497,GO:0008940,GO:0008940,GO:0008940,GO:0008940,GO:0008942,0.3979,0.3979,0.3979,0.3979,0.3081,5,0.3799,0.1925,no
AVEE_ASPAV,A0A5N6TQL1,Reference,Eukaryota,470,"Flavin-dependent halogenase; part of the ave gene cluster that mediates the biosynthesis of the dipeptide L-Leu-L-Cl-Isd also called isoindolamide A. Within the pathway, aveE is responsible for the chlorination at C-6 of R-dihydroxymethyl isoindolinone to generate the amino acid chloro-O-isoindolinone-L- homoserine (L-Cl-Isd). It is possible that it can also chlorinate L- Leu-L-Isd to produce L-Leu-L-Cl-Isd (isoindolamide A). The alanine racemase aveF first catalyzes the interconversion between L-alanine and D-alanine. D-alanine is then activated by the NRPS aveC that transfers it to the PKS aveA to produce R-dihydroxymethyl isoindolinone. The flavin-dependent halogenase aveE catalyzes C-6 chlorination of R-dihydroxymethyl isoindolinone. AveG then catalyzes the gamma-replacement of acetate in O-acetyl-L- homoserine (OAH) with C-6 chlorinated R-dihydroxymethyl isoindolinone to generate the amino acid chloro-O-isoindolinone-L-homoserine (L-Cl- Isd). Finally the ATP-grasp enzyme aveB acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Cl-Isd to give the dipeptide L-Leu-L-Cl-Isd also called isoindolamide A.","Flavin-dependent halogenase; part of the ave gene cluster that mediates the biosynthesis of the dipeptide L-Leu-L-Cl-Isd also called isoindolamide A. Within the pathway, aveE is responsible for the chlorination at C-6 of R-dihydroxymethyl isoindolinone to generate the amino acid chloro-O-isoindolinone-L- homoserine (L-Cl-Isd). It is possible that it can also chlorinate L- Leu-L-Isd to produce L-Leu-L-Cl-Isd (isoindolamide A). The alanine racemase aveF first catalyzes the interconversion between L-alanine and D-alanine. D-alanine is then activated by the NRPS aveC that transfers it to the PKS aveA to produce R-dihydroxymethyl isoindolinone. The flavin-dependent halogenase aveE catalyzes C-6 chlorination of R-dihydroxymethyl isoindolinone. AveG then catalyzes the gamma-replacement of acetate in O-acetyl-L- homoserine (OAH) with C-6 chlorinated R-dihydroxymethyl isoindolinone to generate the amino acid chloro-O-isoindolinone-L-homoserine (L-Cl- Isd). Finally the ATP-grasp enzyme aveB acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Cl-Isd to give the dipeptide L-Leu-L-Cl-Isd also called isoindolamide A.",,,,,,,GO:0071949; GO:0004497,GO:0050660; GO:0070995,GO:0016491,GO:0016491,GO:0016491; GO:0071949,GO:0016491,0.6443,0.5823,0.5823,0.9073,0.5823,5,0.6597,0.1925,no
TOP1_MONPV,A0A7H0DN83,ESM2Text,Viruses,314,"Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at the specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.",Catalyzes the recombination between the large inverted repetitions of the plasmid.,No,No,No,No,No,not-Yes,GO:0003677; GO:0003917,GO:0000150,GO:0000150,GO:0000150,GO:0000150,GO:0009009,0.3777,0.3777,0.3777,0.3777,0.3239,5,0.3669,0.6022,yes
TOP1_MONPV,A0A7H0DN83,Prot2Text,Viruses,314,"Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at the specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.",Catalyzes the recombination between the large inverted repetitions of the plasmid.,No,No,No,No,No,not-Yes,GO:0003677; GO:0003917,GO:0000150,GO:0009009,GO:0009009,GO:0009009,GO:0009009,0.3777,0.3239,0.3239,0.3239,0.3239,5,0.3347,0.6022,yes
TOP1_MONPV,A0A7H0DN83,ProtT3,Viruses,314,"Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at the specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.","Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)- enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step",Yes,Yes,Yes,Yes,Yes,Yes,GO:0003677; GO:0003917,GO:0003917,GO:0003917,GO:0003917,GO:0003917,GO:0003917,0.7008,0.7008,0.7008,0.7008,0.7008,5,0.7008,0.6022,yes
TOP1_MONPV,A0A7H0DN83,ProtTale,Viruses,314,"Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at the specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.",This protein is involved in chromosome partition. It binds to DNA in a sequence-dependent manner.,No,No,No,No,No,not-Yes,GO:0003677; GO:0003917,GO:0003677,GO:0003677,GO:0003677,GO:0043565,GO:0003677,0.7008,0.7008,0.7008,0.5896,0.7008,5,0.6786,0.6022,yes
TOP1_MONPV,A0A7H0DN83,Protein2Text,Viruses,314,"Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at the specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.","The molecular function of this protein is a DNA polymerase, specifically involved in the replication of viral DNA. More specifically, it is a reverse transcriptase that synthesizes DNA from RNA templates. It is likely involved in the replication of a virus, given its association with a viral gene.  The exact function may be dependent on the specific virus or host it is associated with.",No,No,No,No,No,not-Yes,GO:0003677; GO:0003917,GO:0003964,GO:0003964,GO:0003964,GO:0003964,GO:0003964,0.274,0.274,0.274,0.274,0.274,5,0.274,0.6022,yes
TOP1_MONPV,A0A7H0DN83,Reference,Viruses,314,"Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at the specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.","Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at the specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.",,,,,,,GO:0003677; GO:0003917,GO:0003917; GO:0003677,GO:0003917,GO:0003917,GO:0003917; GO:0003677,GO:0003917,1.0,0.7008,0.7008,1.0,0.7008,5,0.8205,0.6022,yes
RP19_MONPV,A0A7H0DNA3,ESM2Text,Viruses,161,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.","Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding proteins, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0003677; GO:0003899,GO:0004521,GO:0004521,GO:0004521,GO:0004521,GO:0004521,0.2541,0.2541,0.2541,0.2541,0.2541,5,0.2541,0.6406,yes
RP19_MONPV,A0A7H0DNA3,Prot2Text,Viruses,161,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.","Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding proteins, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0003677; GO:0003899,GO:0004521,GO:0004521,GO:0004521,GO:0004521,GO:0004521,0.2541,0.2541,0.2541,0.2541,0.2541,5,0.2541,0.6406,yes
RP19_MONPV,A0A7H0DNA3,ProtT3,Viruses,161,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.","Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF) thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase (By similarity). Virion Note=All the enzymes and other proteins required to synthesize early mRNAs are packaged within the virion core along with the DNA genome. This is necessary because viral early mRNAs",Yes,Yes,Yes,Yes,Yes,Yes,GO:0003677; GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.6983,0.6983,0.6983,0.6983,0.6983,5,0.6983,0.6406,yes
RP19_MONPV,A0A7H0DNA3,ProtTale,Viruses,161,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.",Component of the DNA-directed RNA polymerase (RNAP) that catalyzes the transcription in the cytoplasm of viral DNA into RNA using the four ribonucleoside triphosphates as substrates.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003677; GO:0003899,GO:0003899,GO:0003899; GO:0003677,GO:0003899; GO:0003677,GO:0003899; GO:0003677,GO:0003899,0.6983,1.0,1.0,1.0,0.6983,5,0.8793,0.6406,yes
RP19_MONPV,A0A7H0DNA3,Protein2Text,Viruses,161,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.","The molecular function of this protein is not explicitly stated in the provided information. However, based on its classification as a protein, it is likely that it plays a role in various cellular processes, such as signaling, regulation, or catalysis. Further research would be needed to determine its specific molecular function.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0003677; GO:0003899,,,,,,,,,,,0,,0.6406,yes
RP19_MONPV,A0A7H0DNA3,Reference,Viruses,161,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.","Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.",,,,,,,GO:0003677; GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.6983,0.6983,0.6983,0.6983,0.6983,5,0.6983,0.6406,yes
RP132_MONPV,A0A7H0DNC3,ESM2Text,Viruses,1164,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.","As component of the Lig locus, required for the autophagic degradation of the nucleus (nucleophagy) in response to starvation, probably by mediating autophagosome formation.",No,No,No,No,No,not-Yes,GO:0003677; GO:0003899; GO:0046872; GO:0032549,GO:0004521,GO:0004521,GO:0004521,GO:0004521,GO:0004521,0.1826,0.1826,0.1826,0.1826,0.1826,5,0.1826,0.6046,yes
RP132_MONPV,A0A7H0DNC3,Prot2Text,Viruses,1164,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.","As component of the Lig locus, required for the autophagic degradation of the nucleus (nucleophagy) in response to starvation, probably by mediating autophagosome formation.",No,No,No,No,No,not-Yes,GO:0003677; GO:0003899; GO:0046872; GO:0032549,GO:0004521,GO:0004521,GO:0004521,GO:0004521,GO:0004521,0.1826,0.1826,0.1826,0.1826,0.1826,5,0.1826,0.6046,yes
RP132_MONPV,A0A7H0DNC3,ProtT3,Viruses,1164,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.","Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an RNase H-like nuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes. Host nucleus Note=Found associated with the external surface of the viral capsid during assembly and",No,No,No,No,No,not-Yes,GO:0003677; GO:0003899; GO:0046872; GO:0032549,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.4461,0.4461,0.4461,0.4461,0.4461,5,0.4461,0.6046,yes
RP132_MONPV,A0A7H0DNC3,ProtTale,Viruses,1164,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.",Component of the DNA-directed RNA polymerase (RNAP) that catalyzes the transcription in the cytoplasm of viral DNA into RNA using the four ribonucleoside triphosphates as substrates.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003677; GO:0003899; GO:0046872; GO:0032549,GO:0003899,GO:0003899; GO:0003677,GO:0003899; GO:0003677,GO:0003899; GO:0003677,GO:0003899,0.4461,0.7604,0.7604,0.7604,0.4461,5,0.6347,0.6046,yes
RP132_MONPV,A0A7H0DNC3,Protein2Text,Viruses,1164,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.","The molecular function of this protein is a DNA-directed RNA polymerase, which is a type of enzyme that plays a crucial role in transcription, the process of creating a complementary RNA copy from a DNA template.",Yes,Maybe,Yes,Maybe,Yes,Yes,GO:0003677; GO:0003899; GO:0046872; GO:0032549,,,,,,,,,,,0,,0.6046,yes
RP132_MONPV,A0A7H0DNC3,Reference,Viruses,1164,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.","Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.",,,,,,,GO:0003677; GO:0003899; GO:0046872; GO:0032549,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.4461,0.4461,0.4461,0.4461,0.4461,5,0.4461,0.6046,yes
AB62C_PENPR,A0A7H0XJI9,ESM2Text,Eukaryota,328,"Alpha-L-arabinofuranosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Debranches beta-cellulose by removing 1,3 monosubstituted arabinose.","Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Able to hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing beta-1,4-linked arabinofuranoses in side chains, like L-arabinan, arabinoxylan and arabinoxylan.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2146,no
AB62C_PENPR,A0A7H0XJI9,Prot2Text,Eukaryota,328,"Alpha-L-arabinofuranosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Debranches beta-cellulose by removing 1,3 monosubstituted arabinose.","Exo-alpha-L-arabinofuranosidase that specifically hydrolyzes arabinoxylan, a major component of plant hemicellulose. Able to hydrolyze arabinose and xylobiose to release arabinose and xylose.",Yes,Yes,Yes,Maybe,Yes,Yes,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2146,no
AB62C_PENPR,A0A7H0XJI9,ProtT3,Eukaryota,328,"Alpha-L-arabinofuranosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Debranches beta-cellulose by removing 1,3 monosubstituted arabinose.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Secreted. Belongs to the glycosyl hydrolase 43 family",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046556,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,0.6335,0.6335,0.6335,0.6335,0.6335,5,0.6335,0.2146,no
AB62C_PENPR,A0A7H0XJI9,ProtTale,Eukaryota,328,"Alpha-L-arabinofuranosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Debranches beta-cellulose by removing 1,3 monosubstituted arabinose.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046556,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,0.6335,0.6335,0.6335,0.6335,0.6335,5,0.6335,0.2146,no
AB62C_PENPR,A0A7H0XJI9,Protein2Text,Eukaryota,328,"Alpha-L-arabinofuranosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Debranches beta-cellulose by removing 1,3 monosubstituted arabinose.","This protein has a molecular function as a beta-glucanase, which is an enzyme that breaks down beta-glucans, a type of polysaccharide found in plant cell walls. It is involved in the degradation of cellulose and hemicellulose in plant biomass.",No,Maybe,No,No,No,not-Yes,GO:0046556,GO:0052861,GO:0030245; GO:0008422,GO:0030245; GO:0004553,GO:0030245; GO:0052861,GO:0004553,0.6335,0.4224,0.5721,0.4224,0.8582,5,0.5817,0.2146,no
AB62C_PENPR,A0A7H0XJI9,Reference,Eukaryota,328,"Alpha-L-arabinofuranosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Debranches beta-cellulose by removing 1,3 monosubstituted arabinose.","Alpha-L-arabinofuranosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Debranches beta-cellulose by removing 1,3 monosubstituted arabinose.",,,,,,,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2146,no
DXR_CANSA,A0A7J6G7L9,ESM2Text,Eukaryota,473,Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D- erythritol 4-phosphate (MEP). Required for chloroplast development.,Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).,Yes,Yes,Yes,Yes,Yes,Yes,GO:0030604; GO:0030145; GO:0070402,GO:0030604,GO:0030604,GO:0030604,GO:0030604,GO:0030604,0.5329,0.5329,0.5329,0.5329,0.5329,5,0.5329,0.3088,no
DXR_CANSA,A0A7J6G7L9,Prot2Text,Eukaryota,473,Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D- erythritol 4-phosphate (MEP). Required for chloroplast development.,Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).,Yes,Yes,Yes,Yes,Yes,Yes,GO:0030604; GO:0030145; GO:0070402,GO:0030604,GO:0030604,GO:0030604,GO:0030604,GO:0030604,0.5329,0.5329,0.5329,0.5329,0.5329,5,0.5329,0.3088,no
DXR_CANSA,A0A7J6G7L9,ProtT3,Eukaryota,473,Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D- erythritol 4-phosphate (MEP). Required for chloroplast development.,"Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4- phosphate (MEP). Plastid, chloroplast. Belongs to the DXR family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0030604; GO:0030145; GO:0070402,GO:0030604,GO:0030604,GO:0030604,GO:0030604,GO:0030604,0.5329,0.5329,0.5329,0.5329,0.5329,5,0.5329,0.3088,no
DXR_CANSA,A0A7J6G7L9,ProtTale,Eukaryota,473,Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D- erythritol 4-phosphate (MEP). Required for chloroplast development.,Catalyzes the interconversion of dihydroorotate and orotate.,No,No,No,No,No,not-Yes,GO:0030604; GO:0030145; GO:0070402,GO:0004152,GO:0016491,GO:0004152,GO:0004152,GO:0004152,0.2382,0.3596,0.2382,0.2382,0.2382,5,0.2625,0.3088,no
DXR_CANSA,A0A7J6G7L9,Protein2Text,Eukaryota,473,Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D- erythritol 4-phosphate (MEP). Required for chloroplast development.,The molecular function of this protein is an aminotransferase.,No,No,No,No,No,not-Yes,GO:0030604; GO:0030145; GO:0070402,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.1565,0.1565,0.1565,0.1565,0.1565,5,0.1565,0.3088,no
DXR_CANSA,A0A7J6G7L9,Reference,Eukaryota,473,Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D- erythritol 4-phosphate (MEP). Required for chloroplast development.,Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D- erythritol 4-phosphate (MEP). Required for chloroplast development.,,,,,,,GO:0030604; GO:0030145; GO:0070402,GO:0030604; GO:0050661,GO:0030604,GO:0030604,GO:0030604; GO:0050661,GO:0030604,0.7532,0.5329,0.5329,0.7532,0.5329,5,0.621,0.3088,no
FRZC_CLASX,A0A7T8F1I4,ESM2Text,Eukaryota,495,"Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzC catalyzes the coupling between N10 and C1' to produce a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5- cyclohexadienone. FrzC probably first catalyzes homolysis of the N-H bond to generate the N10 radical which is followed by an O-H abstraction to give the phenolic radical which can be delocalized to C1'. Radical coupling between N10 and C1' then forms. The biosynthesis of (-)-FR901483 starts with the condensation of two L- tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4- diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome P450 monooxygenase P450-2 then catalyzes the dimerization of nataloe-emodin to cladofulvin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497; GO:0020037,GO:0004497,GO:0004497,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,0.8149,0.5872,0.5872,0.9516,0.9516,5,0.7785,0.2953,no
FRZC_CLASX,A0A7T8F1I4,Prot2Text,Eukaryota,495,"Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzC catalyzes the coupling between N10 and C1' to produce a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5- cyclohexadienone. FrzC probably first catalyzes homolysis of the N-H bond to generate the N10 radical which is followed by an O-H abstraction to give the phenolic radical which can be delocalized to C1'. Radical coupling between N10 and C1' then forms. The biosynthesis of (-)-FR901483 starts with the condensation of two L- tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4- diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase penM leads to a epoxidized-GGI that is substrate of the terpene cyclase penB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase penP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase penQ. Paxilline is converted to beta-paxitriol",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.5872,0.5872,0.5872,0.5872,0.5872,5,0.5872,0.2953,no
FRZC_CLASX,A0A7T8F1I4,ProtT3,Eukaryota,495,"Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzC catalyzes the coupling between N10 and C1' to produce a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5- cyclohexadienone. FrzC probably first catalyzes homolysis of the N-H bond to generate the N10 radical which is followed by an O-H abstraction to give the phenolic radical which can be delocalized to C1'. Radical coupling between N10 and C1' then forms. The biosynthesis of (-)-FR901483 starts with the condensation of two L- tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4- diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By similarity). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (By similarity). Further epoxidation by the FAD-dependent monooxygenase ausM and",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497,GO:0004497; GO:0020037,GO:0004497; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,0.5872,0.8149,0.8149,0.9516,0.9516,5,0.824,0.2953,no
FRZC_CLASX,A0A7T8F1I4,ProtTale,Eukaryota,495,"Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzC catalyzes the coupling between N10 and C1' to produce a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5- cyclohexadienone. FrzC probably first catalyzes homolysis of the N-H bond to generate the N10 radical which is followed by an O-H abstraction to give the phenolic radical which can be delocalized to C1'. Radical coupling between N10 and C1' then forms. The biosynthesis of (-)-FR901483 starts with the condensation of two L- tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4- diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. Within the pathway, PC-2 catalyzes the oxidation of penitrem D to penitrem E. The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3-glycerol phosphate with GGPP by penC then forms 3-geranylgeranylindole (3-",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497; GO:0020037,GO:0004497; GO:0016491,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497,0.8149,0.6619,0.9516,0.9516,0.5872,5,0.7934,0.2953,no
FRZC_CLASX,A0A7T8F1I4,Protein2Text,Eukaryota,495,"Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzC catalyzes the coupling between N10 and C1' to produce a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5- cyclohexadienone. FrzC probably first catalyzes homolysis of the N-H bond to generate the N10 radical which is followed by an O-H abstraction to give the phenolic radical which can be delocalized to C1'. Radical coupling between N10 and C1' then forms. The biosynthesis of (-)-FR901483 starts with the condensation of two L- tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4- diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.",The molecular function of this protein is catalyzing the oxidation of aliphatic and aromatic compounds.,Maybe,No,Vague,Vague,Vague,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.5572,0.5572,0.5572,0.5572,0.5572,5,0.5572,0.2953,no
FRZC_CLASX,A0A7T8F1I4,Reference,Eukaryota,495,"Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzC catalyzes the coupling between N10 and C1' to produce a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5- cyclohexadienone. FrzC probably first catalyzes homolysis of the N-H bond to generate the N10 radical which is followed by an O-H abstraction to give the phenolic radical which can be delocalized to C1'. Radical coupling between N10 and C1' then forms. The biosynthesis of (-)-FR901483 starts with the condensation of two L- tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4- diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzC catalyzes the coupling between N10 and C1' to produce a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5- cyclohexadienone. FrzC probably first catalyzes homolysis of the N-H bond to generate the N10 radical which is followed by an O-H abstraction to give the phenolic radical which can be delocalized to C1'. Radical coupling between N10 and C1' then forms. The biosynthesis of (-)-FR901483 starts with the condensation of two L- tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4- diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.",,,,,,,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497,GO:0004497,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497,0.5872,0.5872,0.9516,0.9516,0.5872,5,0.733,0.2953,no
FRZJ_CLASX,A0A7T8F1J6,ESM2Text,Eukaryota,385,"Phosphotransferase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). FrzJ catalyzes the last step of the pathway by phosphorylating the C4'- OH of dephospho-(-)-FR901483 to produce (-)-FR901483. The biosynthesis of (-)-FR901483 starts with the condensation of two L- tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4- diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","Catalyzes the phosphorylation of 5-hydroxy-L-lysine to yield 5-O-phospho-D-serine. Is involved in the catabolism of L-lysine and D-lysine. 5-O-phospho-D-serine is a precursor of oleic acid, a major component of glycoconjugates and octoses, and is a key component of lipids, bacterial sphingolipids, and glycoproteins. Also acts on methionine, but not L-lysine, D-lysine or D-tyrosine.",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0016301,,GO:0016301,,,,,0.6878,,,,1,0.6878,0.234,no
FRZJ_CLASX,A0A7T8F1J6,Prot2Text,Eukaryota,385,"Phosphotransferase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). FrzJ catalyzes the last step of the pathway by phosphorylating the C4'- OH of dephospho-(-)-FR901483 to produce (-)-FR901483. The biosynthesis of (-)-FR901483 starts with the condensation of two L- tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4- diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","Dihydro-hydroxyisobutyryl-CoA kinase that catalyzes the phosphorylation of Dihydro-OH-2,3-dihydroxy-isobutyryl-CoA to yield dihydroxyisobutyryl-CoA. Also has activity toward ethyl-CoA, 2-hydroxyethyllactate and 2-hydroxybutyrate.",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0016301,,,,GO:0016301,,,,,0.6878,,1,0.6878,0.234,no
FRZJ_CLASX,A0A7T8F1J6,ProtT3,Eukaryota,385,"Phosphotransferase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). FrzJ catalyzes the last step of the pathway by phosphorylating the C4'- OH of dephospho-(-)-FR901483 to produce (-)-FR901483. The biosynthesis of (-)-FR901483 starts with the condensation of two L- tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4- diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.",Kynurenine kinase that phosphorylates kynurenine to form 3-hydroxykynurenine. Belongs to the kynurenine kinase family,Maybe,No,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0016301,GO:0004502,,GO:0004502,GO:0016301,GO:0004502,0.1615,,0.1615,0.6878,0.1615,4,0.2931,0.234,no
FRZJ_CLASX,A0A7T8F1J6,ProtTale,Eukaryota,385,"Phosphotransferase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). FrzJ catalyzes the last step of the pathway by phosphorylating the C4'- OH of dephospho-(-)-FR901483 to produce (-)-FR901483. The biosynthesis of (-)-FR901483 starts with the condensation of two L- tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4- diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","Catalyzes the phosphorylation of methylthioribulose 1- phosphate (MTRu1P) to form methylthioribulose 2,4-diphosphate (MTRu2P).",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0016301,GO:0016301,GO:0016301,GO:0016301,GO:0016301,GO:0016301,0.6878,0.6878,0.6878,0.6878,0.6878,5,0.6878,0.234,no
FRZJ_CLASX,A0A7T8F1J6,Protein2Text,Eukaryota,385,"Phosphotransferase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). FrzJ catalyzes the last step of the pathway by phosphorylating the C4'- OH of dephospho-(-)-FR901483 to produce (-)-FR901483. The biosynthesis of (-)-FR901483 starts with the condensation of two L- tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4- diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","The molecular function of this protein is an enzyme that catalyzes a reaction. The specific function is not provided in the given text, but it can be inferred that it is involved in a metabolic process.",Vague,No,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0016301,,,,,,,,,,,0,,0.234,no
FRZJ_CLASX,A0A7T8F1J6,Reference,Eukaryota,385,"Phosphotransferase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). FrzJ catalyzes the last step of the pathway by phosphorylating the C4'- OH of dephospho-(-)-FR901483 to produce (-)-FR901483. The biosynthesis of (-)-FR901483 starts with the condensation of two L- tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4- diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","Phosphotransferase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). FrzJ catalyzes the last step of the pathway by phosphorylating the C4'- OH of dephospho-(-)-FR901483 to produce (-)-FR901483. The biosynthesis of (-)-FR901483 starts with the condensation of two L- tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4- diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.",,,,,,,GO:0005524; GO:0016301,GO:0016301,GO:0016301,GO:0016301,GO:0016301,GO:0016301,0.6878,0.6878,0.6878,0.6878,0.6878,5,0.6878,0.234,no
FRZG_CLASX,A0A7T8F1J7,ESM2Text,Eukaryota,306,"Dioxygenase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzG cleaves the C9-N10' bond to yield a conjugated iminium. FrzG is also able to catalyze the dehydrogenation between C7 and C8 which leads to a shunt product. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)- dityrosyl-piperazine. This process occurs in 3 steps with the non- canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L- tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin-dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.",Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA.,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0051213; GO:0046872,GO:0008401,GO:0008309,GO:0008301,GO:0008485,GO:0008309,0.3606,0.1422,0.2055,0.196,0.1422,5,0.2093,0.353,no
FRZG_CLASX,A0A7T8F1J7,Prot2Text,Eukaryota,306,"Dioxygenase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzG cleaves the C9-N10' bond to yield a conjugated iminium. FrzG is also able to catalyze the dehydrogenation between C7 and C8 which leads to a shunt product. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)- dityrosyl-piperazine. This process occurs in 3 steps with the non- canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L- tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin-dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","2-oxoglutarate(2OG)-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins. On the basis of the chemical structures of fumonisins and precursor feeding studies, fumonisin biosynthesis is predicted to include at least five groups of biochemical reactions: synthesis of a linear polyketide with a single terminal carbonyl function and methyl groups at C-10 and C-14; condensation of the polyketide with alanine; reduction of the polyketide carbonyl to a hydroxyl; hydroxylation of 2-4 polyketide carbons; and esterification of six-carbon tricarboxylic acids to two of the hydroxyls. The biosynthesis starts with the polyketide synthase FUM1-catalyzed carbon chain assembly from one molecule of acetyl CoA, eight molecules of malonyl CoA, and two molecules of methionine. The C-18 polyketide chain is released from the enzyme by a",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0051213; GO:0046872,GO:0016706,GO:0016706,GO:0016706,GO:0016706,GO:0016706,0.5293,0.5293,0.5293,0.5293,0.5293,5,0.5293,0.353,no
FRZG_CLASX,A0A7T8F1J7,ProtT3,Eukaryota,306,"Dioxygenase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzG cleaves the C9-N10' bond to yield a conjugated iminium. FrzG is also able to catalyze the dehydrogenation between C7 and C8 which leads to a shunt product. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)- dityrosyl-piperazine. This process occurs in 3 steps with the non- canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L- tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin-dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.",Iron-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranyl,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0051213; GO:0046872,GO:0016702,GO:0016701,GO:0051213,GO:0016491; GO:0005506,GO:0016702,0.5293,0.483,0.7088,0.7926,0.5293,5,0.6086,0.353,no
FRZG_CLASX,A0A7T8F1J7,ProtTale,Eukaryota,306,"Dioxygenase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzG cleaves the C9-N10' bond to yield a conjugated iminium. FrzG is also able to catalyze the dehydrogenation between C7 and C8 which leads to a shunt product. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)- dityrosyl-piperazine. This process occurs in 3 steps with the non- canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L- tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin-dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","Dioxygenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin citrinin, a hepato- nephrotoxic compound to humans due to inhibition of respiration complex III. The pathway begins with the synthesis of a keto-aldehyde intermediate by the citrinin PKS (pksCT) from successive condensations of 4 malonyl-CoA units, presumably with a simple acetyl-CoA starter unit. Release of the keto-aldehyde intermediate is consistent with the presence of the C-terminal reductive release domain. Mp10 and mp11 are probably part of the PKS to catalyze the formation of the",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0051213; GO:0046872,GO:0016702,GO:0016706,GO:0016702,GO:0016702,GO:0051213,0.5293,0.5293,0.5293,0.5293,0.7088,5,0.5652,0.353,no
FRZG_CLASX,A0A7T8F1J7,Protein2Text,Eukaryota,306,"Dioxygenase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzG cleaves the C9-N10' bond to yield a conjugated iminium. FrzG is also able to catalyze the dehydrogenation between C7 and C8 which leads to a shunt product. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)- dityrosyl-piperazine. This process occurs in 3 steps with the non- canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L- tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin-dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.",This protein is a part of a bacterial gene cluster that is responsible for the biosynthesis of a polyketide natural product. The protein is likely involved in the biosynthesis of a polyketide compound.,No,No,Vague,No,No,not-Yes,GO:0051213; GO:0046872,,,,,,,,,,,0,,0.353,no
FRZG_CLASX,A0A7T8F1J7,Reference,Eukaryota,306,"Dioxygenase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzG cleaves the C9-N10' bond to yield a conjugated iminium. FrzG is also able to catalyze the dehydrogenation between C7 and C8 which leads to a shunt product. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)- dityrosyl-piperazine. This process occurs in 3 steps with the non- canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L- tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin-dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","Dioxygenase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzG cleaves the C9-N10' bond to yield a conjugated iminium. FrzG is also able to catalyze the dehydrogenation between C7 and C8 which leads to a shunt product. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)- dityrosyl-piperazine. This process occurs in 3 steps with the non- canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L- tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin-dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.",,,,,,,GO:0051213; GO:0046872,GO:0016706,GO:0016702,GO:0051213,GO:0016702,GO:0016702,0.5293,0.5293,0.7088,0.5293,0.5293,5,0.5652,0.353,no
FRZA_CLASX,A0A7T8F1L4,ESM2Text,Eukaryota,1024,"Non-canonical nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)- FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzA catalyzes the reduction of L-tyrosine via its C-terminal reductase domain to produce L-tyrosinal. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L- tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcs",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0016491,,GO:0016874,GO:0003824,GO:0016874,GO:0016874; GO:0005524,,0.8634,0.7642,0.8634,0.6694,4,0.7901,0.248,no
FRZA_CLASX,A0A7T8F1L4,Prot2Text,Eukaryota,1024,"Non-canonical nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)- FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzA catalyzes the reduction of L-tyrosine via its C-terminal reductase domain to produce L-tyrosinal. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L- tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","Non-canonical nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the host-selective toxins (HSTs) AAL-toxins, sphinganine-analog mycotoxins responsible for Alternaria stem canker on tomato by the tomato pathotype. The biosynthesis starts with the polyketide synthase ALT1-catalyzed C-16 carbon chain assembly from one starter acetyl-CoA unit with malonyl-CoA extender units. ALT1 also selectively transfers methyl groups at the first and the third cycle of chain elongation for AAL toxin. The C-16 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of glycin by decarboxylation, on the carbonyl carbon of polyketide acyl chain (Probable). This step is probably catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase ALT4 (Probable). The respective functions of the other enzymes encoded by the cluster have still to be elucidated (Probable). The sphingosine N",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0016491,,,GO:0016874,,GO:0016874,,,0.8634,,0.8634,2,0.8634,0.248,no
FRZA_CLASX,A0A7T8F1L4,ProtT3,Eukaryota,1024,"Non-canonical nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)- FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzA catalyzes the reduction of L-tyrosine via its C-terminal reductase domain to produce L-tyrosinal. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L- tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","Nonribosomal peptide synthetase (NRPS); part of the gene cluster that mediates the biosynthesis of the mycotoxin fusaric acid (FA), a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties . FA is composed of two aromatic polyketides, fusaric acid A (FA A) and fusaric acid B (FA B), linked by an ester bond . FA A is a 2,6- dihydroxy",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0016874; GO:0016491,GO:0016874,GO:0016874,GO:0016874,GO:0016874,GO:0016874; GO:0005524,0.8634,0.8634,0.8634,0.8634,0.6694,5,0.8246,0.248,no
FRZA_CLASX,A0A7T8F1L4,ProtTale,Eukaryota,1024,"Non-canonical nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)- FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzA catalyzes the reduction of L-tyrosine via its C-terminal reductase domain to produce L-tyrosinal. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L- tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","Involved in the biosynthesis of the siderophore pyoverdine. Catalyzes the activation of L-ornithine and the condensation of phosphoenolpyruvate (PEP) and L-ornithine to form N-(phosphonoethyl)-L-ornithine, the first step in pyoverdine biosynthesis.",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0016874; GO:0016491,GO:0016874,GO:0016874,GO:0016874,GO:0016874,,0.8634,0.8634,0.8634,0.8634,,4,0.8634,0.248,no
FRZA_CLASX,A0A7T8F1L4,Protein2Text,Eukaryota,1024,"Non-canonical nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)- FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzA catalyzes the reduction of L-tyrosine via its C-terminal reductase domain to produce L-tyrosinal. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L- tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.",This protein is involved in the synthesis of a molecule. It is a part of the synthesis pathway.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016874; GO:0016491,,,,,,,,,,,0,,0.248,no
FRZA_CLASX,A0A7T8F1L4,Reference,Eukaryota,1024,"Non-canonical nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)- FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzA catalyzes the reduction of L-tyrosine via its C-terminal reductase domain to produce L-tyrosinal. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L- tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","Non-canonical nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)- FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzA catalyzes the reduction of L-tyrosine via its C-terminal reductase domain to produce L-tyrosinal. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L- tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.",,,,,,,GO:0016874; GO:0016491,GO:0031177; GO:0016874,GO:0008927; GO:0016491,GO:0016491; GO:0016874,GO:0016874,,0.6793,0.7363,1.0,0.8634,,4,0.8197,0.248,no
FRZD_CLASX,A0A7T8F1M9,ESM2Text,Eukaryota,375,"Aldehyde reductase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzD reduces the dienone portion of the pathway intermediates to cyclohexanone. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin-dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ. The only unassigned enzyme in the cluster is the second cytochrome P450 monooxygenase FrzL.",Putative oxophytodienoate reductase that may be involved in the biosynthesis or metabolism of oxylipin signaling molecules.,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0010181; GO:0003959,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.497,0.497,0.497,0.497,0.497,5,0.497,0.2296,no
FRZD_CLASX,A0A7T8F1M9,Prot2Text,Eukaryota,375,"Aldehyde reductase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzD reduces the dienone portion of the pathway intermediates to cyclohexanone. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin-dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ. The only unassigned enzyme in the cluster is the second cytochrome P450 monooxygenase FrzL.","Chanoclavine-I aldehyde reductase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid. DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan. The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine. The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde. Chanoclavine-I aldehyde reductase easE functions as the first enzyme in the biosynthesis of ergot alkaloid. The chanoclavine-",Yes,Maybe,Maybe,No,Maybe,not-Yes,GO:0010181; GO:0003959,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.497,0.497,0.497,0.497,0.497,5,0.497,0.2296,no
FRZD_CLASX,A0A7T8F1M9,ProtT3,Eukaryota,375,"Aldehyde reductase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzD reduces the dienone portion of the pathway intermediates to cyclohexanone. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin-dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ. The only unassigned enzyme in the cluster is the second cytochrome P450 monooxygenase FrzL.",Putative oxoacid dehydrogenase. Belongs to the NADH:flavin oxidoreductase/NADH oxidase family,Vague,No,No,Vague,Maybe,not-Yes,GO:0010181; GO:0003959,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.497,0.497,0.497,0.497,0.497,5,0.497,0.2296,no
FRZD_CLASX,A0A7T8F1M9,ProtTale,Eukaryota,375,"Aldehyde reductase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzD reduces the dienone portion of the pathway intermediates to cyclohexanone. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin-dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ. The only unassigned enzyme in the cluster is the second cytochrome P450 monooxygenase FrzL.",Putative oxophytodienoate reductase that may be involved in the biosynthesis or metabolism of oxylipin signaling molecules.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0010181; GO:0003959,GO:0016491,,,GO:0016491,GO:0016491,0.497,,,0.497,0.497,3,0.497,0.2296,no
FRZD_CLASX,A0A7T8F1M9,Protein2Text,Eukaryota,375,"Aldehyde reductase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzD reduces the dienone portion of the pathway intermediates to cyclohexanone. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin-dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ. The only unassigned enzyme in the cluster is the second cytochrome P450 monooxygenase FrzL.",This protein is involved in the molecular function of oxido-reductase activity.,Vague,Maybe,Vague,Vague,Vague,not-Yes,GO:0010181; GO:0003959,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.497,0.497,0.497,0.497,0.497,5,0.497,0.2296,no
FRZD_CLASX,A0A7T8F1M9,Reference,Eukaryota,375,"Aldehyde reductase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzD reduces the dienone portion of the pathway intermediates to cyclohexanone. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin-dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ. The only unassigned enzyme in the cluster is the second cytochrome P450 monooxygenase FrzL.","Aldehyde reductase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzD reduces the dienone portion of the pathway intermediates to cyclohexanone. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin-dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ. The only unassigned enzyme in the cluster is the second cytochrome P450 monooxygenase FrzL.",,,,,,,GO:0010181; GO:0003959,GO:0016491; GO:0050660,GO:0016491,GO:0016491; GO:0050660,GO:0016491,GO:0016491,0.7119,0.497,0.7119,0.497,0.497,5,0.583,0.2296,no
FRZK_CLASX,A0A7T8J1U7,ESM2Text,Eukaryota,510,"Phosphoribosylpyrophosphate amidotransferase (PPAT); part of the gene cluster that mediates the biosynthesis of the alkaloid (-)- FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). PPAT catalyzes the first step of de novo purine biosynthesis in which 5-phosphoribosyl-1-pyrophosphate (PRPP) is converted to 5-phosphoribosyl-1-amine (PRA). May act as a resistant housekeeping PPAT to protect the host from the final product of the cluster, (-)-FR901483.",Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.,Yes,Yes,Yes,Maybe,Yes,Yes,GO:0051539; GO:0004044; GO:0046872,GO:0004044,GO:0004044,GO:0004044; GO:0005524,GO:0004044,GO:0004044,0.5444,0.5444,0.5559,0.5444,0.5444,5,0.5467,0.6016,yes
FRZK_CLASX,A0A7T8J1U7,Prot2Text,Eukaryota,510,"Phosphoribosylpyrophosphate amidotransferase (PPAT); part of the gene cluster that mediates the biosynthesis of the alkaloid (-)- FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). PPAT catalyzes the first step of de novo purine biosynthesis in which 5-phosphoribosyl-1-pyrophosphate (PRPP) is converted to 5-phosphoribosyl-1-amine (PRA). May act as a resistant housekeeping PPAT to protect the host from the final product of the cluster, (-)-FR901483.",Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.,Yes,Yes,Yes,Maybe,Yes,Yes,GO:0051539; GO:0004044; GO:0046872,GO:0004044,GO:0004044,GO:0004044,GO:0004044,GO:0004044,0.5444,0.5444,0.5444,0.5444,0.5444,5,0.5444,0.6016,yes
FRZK_CLASX,A0A7T8J1U7,ProtT3,Eukaryota,510,"Phosphoribosylpyrophosphate amidotransferase (PPAT); part of the gene cluster that mediates the biosynthesis of the alkaloid (-)- FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). PPAT catalyzes the first step of de novo purine biosynthesis in which 5-phosphoribosyl-1-pyrophosphate (PRPP) is converted to 5-phosphoribosyl-1-amine (PRA). May act as a resistant housekeeping PPAT to protect the host from the final product of the cluster, (-)-FR901483.",Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family,Yes,Yes,Yes,Maybe,Yes,Yes,GO:0051539; GO:0004044; GO:0046872,GO:0004044,GO:0004044,GO:0004044,GO:0004044,GO:0004044,0.5444,0.5444,0.5444,0.5444,0.5444,5,0.5444,0.6016,yes
FRZK_CLASX,A0A7T8J1U7,ProtTale,Eukaryota,510,"Phosphoribosylpyrophosphate amidotransferase (PPAT); part of the gene cluster that mediates the biosynthesis of the alkaloid (-)- FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). PPAT catalyzes the first step of de novo purine biosynthesis in which 5-phosphoribosyl-1-pyrophosphate (PRPP) is converted to 5-phosphoribosyl-1-amine (PRA). May act as a resistant housekeeping PPAT to protect the host from the final product of the cluster, (-)-FR901483.",Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.,Yes,Yes,Yes,Maybe,Yes,Yes,GO:0051539; GO:0004044; GO:0046872,GO:0004044,GO:0004044,GO:0004044,GO:0004044,GO:0004044,0.5444,0.5444,0.5444,0.5444,0.5444,5,0.5444,0.6016,yes
FRZK_CLASX,A0A7T8J1U7,Protein2Text,Eukaryota,510,"Phosphoribosylpyrophosphate amidotransferase (PPAT); part of the gene cluster that mediates the biosynthesis of the alkaloid (-)- FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). PPAT catalyzes the first step of de novo purine biosynthesis in which 5-phosphoribosyl-1-pyrophosphate (PRPP) is converted to 5-phosphoribosyl-1-amine (PRA). May act as a resistant housekeeping PPAT to protect the host from the final product of the cluster, (-)-FR901483.","The molecular function of the protein is an aminotransferase, which catalyzes the transfer of an amino group from a specific amino acid to a keto acid, resulting in the production of a new amino acid and a new keto acid. More specifically, this protein catalyzes the conversion of L-glutamate to alpha-ketoglutarate and of L-aspartate to oxaloacetate.",No,No,No,No,No,not-Yes,GO:0051539; GO:0004044; GO:0046872,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0004069,0.2516,0.2516,0.2516,0.2516,0.2137,5,0.244,0.6016,yes
FRZK_CLASX,A0A7T8J1U7,Reference,Eukaryota,510,"Phosphoribosylpyrophosphate amidotransferase (PPAT); part of the gene cluster that mediates the biosynthesis of the alkaloid (-)- FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). PPAT catalyzes the first step of de novo purine biosynthesis in which 5-phosphoribosyl-1-pyrophosphate (PRPP) is converted to 5-phosphoribosyl-1-amine (PRA). May act as a resistant housekeeping PPAT to protect the host from the final product of the cluster, (-)-FR901483.","Phosphoribosylpyrophosphate amidotransferase (PPAT); part of the gene cluster that mediates the biosynthesis of the alkaloid (-)- FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). PPAT catalyzes the first step of de novo purine biosynthesis in which 5-phosphoribosyl-1-pyrophosphate (PRPP) is converted to 5-phosphoribosyl-1-amine (PRA). May act as a resistant housekeeping PPAT to protect the host from the final product of the cluster, (-)-FR901483.",,,,,,,GO:0051539; GO:0004044; GO:0046872,GO:0004044; GO:0005524,GO:0004044,GO:0004044,GO:0004044,GO:0004044,0.5559,0.5444,0.5444,0.5444,0.5444,5,0.5467,0.6016,yes
FRZF_CLASX,A0A7T8J1Z8,ESM2Text,Eukaryota,427,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzF methylates the phenolic oxygen at position C4. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L- tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins. The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2). The first step of the pathway is the conversion of acetate to norsolorinic acid (NOR) and requires the fatty acid synthase subunits aflA and aflB, as well as the PKS aflC. AflC combines a hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize the precursor NOR. The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by the fungal fatty acid synthase aflA/aflB. The second step is the conversion of NOR to averantin (AVN) and requires the norsolorinic acid ketoacyl",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2435,no
FRZF_CLASX,A0A7T8J1Z8,Prot2Text,Eukaryota,427,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzF methylates the phenolic oxygen at position C4. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L- tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate tolerance, py",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2435,no
FRZF_CLASX,A0A7T8J1Z8,ProtT3,Eukaryota,427,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzF methylates the phenolic oxygen at position C4. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L- tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.",O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeran,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2435,no
FRZF_CLASX,A0A7T8J1Z8,ProtTale,Eukaryota,427,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzF methylates the phenolic oxygen at position C4. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L- tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities. In the first step, the non-reducing polyketide synthase azaA forms the hexaketide precursor from successive condensations of five malonyl-CoA units, presumably with a simple acetyl-CoA starter unit. The reactive polyketide chain then undergoes a PT- mediated C2-C7 cyclization to afford the aromatic ring and is eventually released as an aldehyde through the R-domain. The",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008171,GO:0008171,GO:0008168,GO:0008171,GO:0008171,GO:0008171,1.0,0.8582,1.0,1.0,1.0,5,0.9716,0.2435,no
FRZF_CLASX,A0A7T8J1Z8,Protein2Text,Eukaryota,427,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzF methylates the phenolic oxygen at position C4. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L- tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","This protein is involved in the molecular function of being a S-adenosyl-L-methionine-dependent methyltransferase. More specifically, it is a cytochrome P450 monooxygenase. 
This protein is also involved in the molecular function of oxidoreductase activity, transferring electrons from a donor, such as NADPH, to an acceptor, such as cytochrome P450 heme. 
Additionally, it is involved in the molecular function of catalyzing the stereospecific NADPH-dependent reduction of a wide range of exogenous and endogenous substrates with a concomitant reduction of the rhodopsin-like chromophore. 
It is also involved in the molecular function of catalyzing the reduction of the heme group of cytochrome P450. 
It is also involved in the molecular function of being a cytochrome P450 monooxygenase. 
It is also involved in the molecular function of being a cytochrome P450. 
It is also involved in the molecular function of being a monooxygenase. 
It is also involved in the molecular function of being a cytochrome P450 heme thiolate monooxygenase. 
It is also involved in the molecular function of being a cytochrome P450 monooxygenase that catalyzes the oxidative metabolism of many drugs and xenobiotics. 
It is also involved in the molecular function of being a monooxygenase that catalyzes the hydroxylation of a wide range of substrates. 
It is also involved in the molecular function of being a cytochrome P450 that catalyzes the metabolism of endogenous steroids and fatty acids. 
It is also involved in the molecular function of being a cytochrome P450 that catalyzes the metabolism of xenobiotics. 
It is also involved in the molecular function of being a cytochrome P450 that catalyzes the metabolism of drugs. 
It is also involved in the molecular function of being a cytochrome P450 that catalyzes the metabolism of pollutants. 
It is also involved in the molecular function of being a cytochrome P450 that catalyzes the metabolism of carcinogens. 
It is also involved in the molecular function of being a cytochrome P450 that catalyzes the metabolism of mutagens. 
It is also involved in the molecular function of being a cytochrome P450 that catalyzes the metabolism of toxins. 
It is also",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0008171,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.2845,0.2845,0.2845,0.2845,0.2845,5,0.2845,0.2435,no
FRZF_CLASX,A0A7T8J1Z8,Reference,Eukaryota,427,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzF methylates the phenolic oxygen at position C4. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L- tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzF methylates the phenolic oxygen at position C4. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L- tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.",,,,,,,GO:0008171,GO:0008168,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.8582,1.0,1.0,1.0,1.0,5,0.9716,0.2435,no
C719A_PIPNI,A0A7T9QPT0,ESM2Text,Eukaryota,511,"Cytochrome P450 monooxygenase involved in the biosynthesis of aromatic piperamides natural products such as piperine (1-piperoyl- piperidine), the pungent principle contributing, together with several terpenoids, to the aromatic properties of black pepper fruits, and displaying numerous pharmacological activities such as antiproliferative, antitumor, antiangiogenesis, antioxidant, antidiabetic, antiobesity, cardioprotective, antimicrobial, antiaging, and immunomodulatory effects. Catalyzes the conversion of feruperic acid (5-(4-hydroxy-3-methoxyphenyl)-2,4- pentadienoic acid) to piperic acid. Inactive toward ferulic acid and feruperine.","Catalyzes the conversion of the C14=C15 double bond of bisdemethoxycurcumin to bisdemethoxyneuramidopiperitoxin, a potent procarcinogen.",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,,,,,,,,,,,0,,0.3688,no
C719A_PIPNI,A0A7T9QPT0,Prot2Text,Eukaryota,511,"Cytochrome P450 monooxygenase involved in the biosynthesis of aromatic piperamides natural products such as piperine (1-piperoyl- piperidine), the pungent principle contributing, together with several terpenoids, to the aromatic properties of black pepper fruits, and displaying numerous pharmacological activities such as antiproliferative, antitumor, antiangiogenesis, antioxidant, antidiabetic, antiobesity, cardioprotective, antimicrobial, antiaging, and immunomodulatory effects. Catalyzes the conversion of feruperic acid (5-(4-hydroxy-3-methoxyphenyl)-2,4- pentadienoic acid) to piperic acid. Inactive toward ferulic acid and feruperine.","Catalyzes the conversion of 3-hydroxyindolin-2-one to 2-hydroxy-1,4-benzoxazin-3-one (HBOA).",No,No,No,No,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,,,,,,,,,,,0,,0.3688,no
C719A_PIPNI,A0A7T9QPT0,ProtT3,Eukaryota,511,"Cytochrome P450 monooxygenase involved in the biosynthesis of aromatic piperamides natural products such as piperine (1-piperoyl- piperidine), the pungent principle contributing, together with several terpenoids, to the aromatic properties of black pepper fruits, and displaying numerous pharmacological activities such as antiproliferative, antitumor, antiangiogenesis, antioxidant, antidiabetic, antiobesity, cardioprotective, antimicrobial, antiaging, and immunomodulatory effects. Catalyzes the conversion of feruperic acid (5-(4-hydroxy-3-methoxyphenyl)-2,4- pentadienoic acid) to piperic acid. Inactive toward ferulic acid and feruperine.",Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-,Maybe,No,Maybe,Vague,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497,GO:0004497; GO:0020037,GO:0004497; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,0.5872,0.8149,0.8149,0.9516,0.9516,5,0.824,0.3688,no
C719A_PIPNI,A0A7T9QPT0,ProtTale,Eukaryota,511,"Cytochrome P450 monooxygenase involved in the biosynthesis of aromatic piperamides natural products such as piperine (1-piperoyl- piperidine), the pungent principle contributing, together with several terpenoids, to the aromatic properties of black pepper fruits, and displaying numerous pharmacological activities such as antiproliferative, antitumor, antiangiogenesis, antioxidant, antidiabetic, antiobesity, cardioprotective, antimicrobial, antiaging, and immunomodulatory effects. Catalyzes the conversion of feruperic acid (5-(4-hydroxy-3-methoxyphenyl)-2,4- pentadienoic acid) to piperic acid. Inactive toward ferulic acid and feruperine.","Catalyzes the 3'-hydroxylation of naringenin to naringenin-3'-ol in the biosynthesis of naringenin-7-O-beta-D- glucuronide, a precursor of naringenin-7-O-beta-D-glucuronide (naringenin 7-O-beta-D-glucuronide 7-O-beta-D-glucuronide) naringenin-7-O-beta-D-glucoside (naringenin 7-O-beta-D-glucuronide 7-O-beta-D-glucoside)",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497,GO:0016491,GO:0004497,GO:0004497,GO:0045431,0.5872,0.5572,0.5872,0.5872,0.3896,5,0.5417,0.3688,no
C719A_PIPNI,A0A7T9QPT0,Protein2Text,Eukaryota,511,"Cytochrome P450 monooxygenase involved in the biosynthesis of aromatic piperamides natural products such as piperine (1-piperoyl- piperidine), the pungent principle contributing, together with several terpenoids, to the aromatic properties of black pepper fruits, and displaying numerous pharmacological activities such as antiproliferative, antitumor, antiangiogenesis, antioxidant, antidiabetic, antiobesity, cardioprotective, antimicrobial, antiaging, and immunomodulatory effects. Catalyzes the conversion of feruperic acid (5-(4-hydroxy-3-methoxyphenyl)-2,4- pentadienoic acid) to piperic acid. Inactive toward ferulic acid and feruperine.","This protein is a part of the cytochrome P450 family, which is a large family of enzymes that play a crucial role in the metabolism of various substances, including drugs, xenobiotics, and endogenous compounds. The molecular function of this protein is likely to be involved in the oxidation of a specific substrate, which may be involved in the biosynthesis of a particular compound or the metabolism of a xenobiotic substance.

Specifically, this protein is likely to be involved in the oxidation of a specific substrate, such as a fatty acid or a terpene, which may be involved in the biosynthesis of a particular compound, such as a wax or a terpene derivative. The exact molecular function of this protein is not specified, but it is likely to be involved in the oxidation of a specific substrate, which may be involved in the biosynthesis of a particular compound or the metabolism of a xenobiotic substance. 

It is worth noting that the molecular function of this protein may be different in different species, and more research is needed to determine its exact function in different organisms.",Maybe,No,Vague,No,Vague,not-Yes,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.5872,0.5872,0.5872,0.5872,0.5872,5,0.5872,0.3688,no
C719A_PIPNI,A0A7T9QPT0,Reference,Eukaryota,511,"Cytochrome P450 monooxygenase involved in the biosynthesis of aromatic piperamides natural products such as piperine (1-piperoyl- piperidine), the pungent principle contributing, together with several terpenoids, to the aromatic properties of black pepper fruits, and displaying numerous pharmacological activities such as antiproliferative, antitumor, antiangiogenesis, antioxidant, antidiabetic, antiobesity, cardioprotective, antimicrobial, antiaging, and immunomodulatory effects. Catalyzes the conversion of feruperic acid (5-(4-hydroxy-3-methoxyphenyl)-2,4- pentadienoic acid) to piperic acid. Inactive toward ferulic acid and feruperine.","Cytochrome P450 monooxygenase involved in the biosynthesis of aromatic piperamides natural products such as piperine (1-piperoyl- piperidine), the pungent principle contributing, together with several terpenoids, to the aromatic properties of black pepper fruits, and displaying numerous pharmacological activities such as antiproliferative, antitumor, antiangiogenesis, antioxidant, antidiabetic, antiobesity, cardioprotective, antimicrobial, antiaging, and immunomodulatory effects. Catalyzes the conversion of feruperic acid (5-(4-hydroxy-3-methoxyphenyl)-2,4- pentadienoic acid) to piperic acid. Inactive toward ferulic acid and feruperine.",,,,,,,GO:0020037; GO:0005506; GO:0004497; GO:0016705,GO:0004497,GO:0004497,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497,0.5872,0.5872,0.9516,0.9516,0.5872,5,0.733,0.3688,no
FSCA_FUSEQ,A0A823A1C6,ESM2Text,Eukaryota,1023,"NRPS-like oxidoreductasee; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan- derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscA acts as an oxidoreductase that reduces the carboxyl group of 4-hydroxykyrunenine to primary alcohol (Probable). The first step of the pathway is the epimerization of L-tryptophan to D-tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6-hydroxylase fscE to yield 6- hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4- hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0016874; GO:0016491,,GO:0016874,GO:0003824,GO:0016874,GO:0016874; GO:0005524,,0.8634,0.7642,0.8634,0.6694,4,0.7901,0.2497,no
FSCA_FUSEQ,A0A823A1C6,Prot2Text,Eukaryota,1023,"NRPS-like oxidoreductasee; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan- derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscA acts as an oxidoreductase that reduces the carboxyl group of 4-hydroxykyrunenine to primary alcohol (Probable). The first step of the pathway is the epimerization of L-tryptophan to D-tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6-hydroxylase fscE to yield 6- hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4- hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the mycotoxin cyclochlorotine, a hepatotoxic and carcinogenic cyclic chlorinated pentapeptide. Cyclochlorotine is formed by the nonproteinogenic amino acids L-2-aminobutyrate (2Abu), L-beta-phenylalanine (beta-Phe), the unique L-cis-3,4-dichloroproline Pro(Cl(2)) and two L-serines (Ser). The condensation of the 5 building blocks is performed by the cyclochlorotine synthetase cctN, a nonribosomal peptide synthetase. The assembled linear pentapeptide is then assumed to be released through cyclization by the terminal condensation-like domain of cctN. Incorporation of the alternative substrates allo-threonine or alanine by the domains A3 or A1 respectively may lead to the production of the variants hydroxy-cyclochlorotine and deoxy-cyclochlorotine, respectively. CctP probably acts as a phenylalanine aminomutase and provides the",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0016874; GO:0016491,,,GO:0016874,,GO:0016874,,,0.8634,,0.8634,2,0.8634,0.2497,no
FSCA_FUSEQ,A0A823A1C6,ProtT3,Eukaryota,1023,"NRPS-like oxidoreductasee; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan- derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscA acts as an oxidoreductase that reduces the carboxyl group of 4-hydroxykyrunenine to primary alcohol (Probable). The first step of the pathway is the epimerization of L-tryptophan to D-tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6-hydroxylase fscE to yield 6- hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4- hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of austinol, a fungal meroterpenoid . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase ausA . DMOA is then prenylated by the polyprenyl transferase ausN . Further epoxidation by the FAD",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0016874; GO:0016491,GO:0016874,GO:0016874,GO:0016874,GO:0016874,GO:0016874; GO:0005524,0.8634,0.8634,0.8634,0.8634,0.6694,5,0.8246,0.2497,no
FSCA_FUSEQ,A0A823A1C6,ProtTale,Eukaryota,1023,"NRPS-like oxidoreductasee; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan- derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscA acts as an oxidoreductase that reduces the carboxyl group of 4-hydroxykyrunenine to primary alcohol (Probable). The first step of the pathway is the epimerization of L-tryptophan to D-tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6-hydroxylase fscE to yield 6- hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4- hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).","Catalyzes the formation of the gamma-carboxyglutamic acid (Gla) domains of osteocalcin (BGLAP), osteopontin (SPP1) and osteonectin (BGN), when bound to calcium.",No,No,No,No,No,not-Yes,GO:0016874; GO:0016491,,,,GO:0008488,,,,,0.3552,,1,0.3552,0.2497,no
FSCA_FUSEQ,A0A823A1C6,Protein2Text,Eukaryota,1023,"NRPS-like oxidoreductasee; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan- derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscA acts as an oxidoreductase that reduces the carboxyl group of 4-hydroxykyrunenine to primary alcohol (Probable). The first step of the pathway is the epimerization of L-tryptophan to D-tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6-hydroxylase fscE to yield 6- hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4- hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).","This protein is involved in the molecular function of transferring a molecule from one compound to another. Specifically, it is involved in the transfer of a molecule called CoA (coenzyme A) from one compound to another. CoA is a molecule that plays a crucial role in many metabolic pathways, including the synthesis and breakdown of fats, carbohydrates, and proteins. The protein is likely involved in the synthesis of a molecule that is used by the plant as a defense mechanism, such as a phytoalexin or a phytoanticipin.",No,No,No,No,No,not-Yes,GO:0016874; GO:0016491,,,,,,,,,,,0,,0.2497,no
FSCA_FUSEQ,A0A823A1C6,Reference,Eukaryota,1023,"NRPS-like oxidoreductasee; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan- derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscA acts as an oxidoreductase that reduces the carboxyl group of 4-hydroxykyrunenine to primary alcohol (Probable). The first step of the pathway is the epimerization of L-tryptophan to D-tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6-hydroxylase fscE to yield 6- hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4- hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).","NRPS-like oxidoreductasee; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan- derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscA acts as an oxidoreductase that reduces the carboxyl group of 4-hydroxykyrunenine to primary alcohol (Probable). The first step of the pathway is the epimerization of L-tryptophan to D-tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6-hydroxylase fscE to yield 6- hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4- hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).",,,,,,,GO:0016874; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.8634,0.8634,0.8634,0.8634,0.8634,5,0.8634,0.2497,no
DETXE_AMPFL,A0A8B0M5T9,ESM2Text,Eukaryota,377,"2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of destruxins (DTXs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. DetxE is involved in the biosynthesis of (3S)-methyl-L-proline, one of the building blocks od DTXs including felinotoxins A to E, roseotoxins A to C, [3-Me-Pro] destruxin E chlorohydrin, as well as isaridins (ISDs) B and D. DetxE uses L-isoleucine as substrate to produce (4S,5S)-4-methyl-delta1-pyrroline-5-carboxylate. The pyrroline-5- carboxylate reductases 1 and/or 2 then perform the reduction of (4S,5S)-4-methyl-delta1-pyrroline-5-carboxylate to (3S)-methyl-L- proline.","2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties. These compounds share a hemiaminal-containing pyrrolizidinone core fused with a gamma-lactone, giving a furopyrrolizidine that is connected to a decalin fragment. The polyketide synthase module (PKS) of the PKS-NRPS ucsA is responsible for the synthesis of the polyketide backbone via the condensation of an acetyl-CoA starter unit with 6 malonyl-CoA units. The downstream nonribosomal peptide synthetase (NRPS) module then amidates the carboxyl end of the polyketide with a 2S,3S-methylproline derived from L-isoleucine by the 2-oxoglutarate-dependent dioxygenase ucsF which converts L-isoleucine to (4S,5S)-4-methylpyrroline-5-carbox",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0046872; GO:0016491,GO:0016706,GO:0016706,GO:0016706,GO:0016706,GO:0016706; GO:0005506,0.4354,0.4354,0.4354,0.4354,0.6884,5,0.486,0.3454,no
DETXE_AMPFL,A0A8B0M5T9,Prot2Text,Eukaryota,377,"2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of destruxins (DTXs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. DetxE is involved in the biosynthesis of (3S)-methyl-L-proline, one of the building blocks od DTXs including felinotoxins A to E, roseotoxins A to C, [3-Me-Pro] destruxin E chlorohydrin, as well as isaridins (ISDs) B and D. DetxE uses L-isoleucine as substrate to produce (4S,5S)-4-methyl-delta1-pyrroline-5-carboxylate. The pyrroline-5- carboxylate reductases 1 and/or 2 then perform the reduction of (4S,5S)-4-methyl-delta1-pyrroline-5-carboxylate to (3S)-methyl-L- proline.","Dehydrogenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",No,Maybe,No,No,Maybe,not-Yes,GO:0046872; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.7193,0.7193,0.7193,0.7193,0.7193,5,0.7193,0.3454,no
DETXE_AMPFL,A0A8B0M5T9,ProtT3,Eukaryota,377,"2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of destruxins (DTXs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. DetxE is involved in the biosynthesis of (3S)-methyl-L-proline, one of the building blocks od DTXs including felinotoxins A to E, roseotoxins A to C, [3-Me-Pro] destruxin E chlorohydrin, as well as isaridins (ISDs) B and D. DetxE uses L-isoleucine as substrate to produce (4S,5S)-4-methyl-delta1-pyrroline-5-carboxylate. The pyrroline-5- carboxylate reductases 1 and/or 2 then perform the reduction of (4S,5S)-4-methyl-delta1-pyrroline-5-carboxylate to (3S)-methyl-L- proline.",2-oxoglutarate- and Fe(II)-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the pren,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0016491,GO:0016706,GO:0016706,GO:0016706,GO:0016706; GO:0005506,GO:0016706,0.4354,0.4354,0.4354,0.6884,0.4354,5,0.486,0.3454,no
DETXE_AMPFL,A0A8B0M5T9,ProtTale,Eukaryota,377,"2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of destruxins (DTXs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. DetxE is involved in the biosynthesis of (3S)-methyl-L-proline, one of the building blocks od DTXs including felinotoxins A to E, roseotoxins A to C, [3-Me-Pro] destruxin E chlorohydrin, as well as isaridins (ISDs) B and D. DetxE uses L-isoleucine as substrate to produce (4S,5S)-4-methyl-delta1-pyrroline-5-carboxylate. The pyrroline-5- carboxylate reductases 1 and/or 2 then perform the reduction of (4S,5S)-4-methyl-delta1-pyrroline-5-carboxylate to (3S)-methyl-L- proline.","2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin citrinin, a hepato-nephrotoxic compound to humans due to inhibition of respiration complex III. The pathway begins with the synthesis of a keto-aldehyde intermediate by the citrinin PKS (pksCT) from successive condensations of 4 malonyl-CoA units, presumably with a simple acetyl-CoA starter unit. Release of the keto-aldehyde intermediate is consistent with the presence of the C-terminal reductive release domain. pksCT is also able to catalyze the reverse reaction,",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0016491,GO:0016706,GO:0016706,GO:0016706,GO:0016706,GO:0016706,0.4354,0.4354,0.4354,0.4354,0.4354,5,0.4354,0.3454,no
DETXE_AMPFL,A0A8B0M5T9,Protein2Text,Eukaryota,377,"2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of destruxins (DTXs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. DetxE is involved in the biosynthesis of (3S)-methyl-L-proline, one of the building blocks od DTXs including felinotoxins A to E, roseotoxins A to C, [3-Me-Pro] destruxin E chlorohydrin, as well as isaridins (ISDs) B and D. DetxE uses L-isoleucine as substrate to produce (4S,5S)-4-methyl-delta1-pyrroline-5-carboxylate. The pyrroline-5- carboxylate reductases 1 and/or 2 then perform the reduction of (4S,5S)-4-methyl-delta1-pyrroline-5-carboxylate to (3S)-methyl-L- proline.",This protein is a part of the phenylalanine metabolism pathway. It is involved in the conversion of 2-hydroxyphenylacetate to 2-hydroxy-6-pentylbenzoate.,No,No,No,No,No,not-Yes,GO:0046872; GO:0016491,,,,,,,,,,,0,,0.3454,no
DETXE_AMPFL,A0A8B0M5T9,Reference,Eukaryota,377,"2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of destruxins (DTXs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. DetxE is involved in the biosynthesis of (3S)-methyl-L-proline, one of the building blocks od DTXs including felinotoxins A to E, roseotoxins A to C, [3-Me-Pro] destruxin E chlorohydrin, as well as isaridins (ISDs) B and D. DetxE uses L-isoleucine as substrate to produce (4S,5S)-4-methyl-delta1-pyrroline-5-carboxylate. The pyrroline-5- carboxylate reductases 1 and/or 2 then perform the reduction of (4S,5S)-4-methyl-delta1-pyrroline-5-carboxylate to (3S)-methyl-L- proline.","2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of destruxins (DTXs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. DetxE is involved in the biosynthesis of (3S)-methyl-L-proline, one of the building blocks od DTXs including felinotoxins A to E, roseotoxins A to C, [3-Me-Pro] destruxin E chlorohydrin, as well as isaridins (ISDs) B and D. DetxE uses L-isoleucine as substrate to produce (4S,5S)-4-methyl-delta1-pyrroline-5-carboxylate. The pyrroline-5- carboxylate reductases 1 and/or 2 then perform the reduction of (4S,5S)-4-methyl-delta1-pyrroline-5-carboxylate to (3S)-methyl-L- proline.",,,,,,,GO:0046872; GO:0016491,GO:0016706,GO:0016706,GO:0016706; GO:0005506,GO:0016706,GO:0016706,0.4354,0.4354,0.6884,0.4354,0.4354,5,0.486,0.3454,no
ISRD_AMPFL,A0A8B0M9Z0,ESM2Text,Eukaryota,2544,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The isariin synthetase isrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1 (Probable).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcsC",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177,,GO:0016747,GO:0016491; GO:0016740,GO:0016746,GO:0016746,,0.6148,0.6555,0.5549,0.5549,4,0.595,0.2692,no
ISRD_AMPFL,A0A8B0M9Z0,Prot2Text,Eukaryota,2544,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The isariin synthetase isrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1 (Probable).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcsC",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177,,,GO:0016747,,GO:0016746,,,0.6148,,0.5549,2,0.5848,0.2692,no
ISRD_AMPFL,A0A8B0M9Z0,ProtT3,Eukaryota,2544,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The isariin synthetase isrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1 (Probable).","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177,GO:0016747,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.6148,0.5549,0.5549,0.5549,0.5549,5,0.5669,0.2692,no
ISRD_AMPFL,A0A8B0M9Z0,ProtTale,Eukaryota,2544,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The isariin synthetase isrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1 (Probable).","Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the at",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177,GO:0016747,GO:0016747,GO:0016746,GO:0016746,,0.6148,0.6148,0.5549,0.5549,,4,0.5848,0.2692,no
ISRD_AMPFL,A0A8B0M9Z0,Protein2Text,Eukaryota,2544,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The isariin synthetase isrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1 (Probable).","This protein is a fatty acid synthase, which is an enzyme that plays a crucial role in the synthesis of fatty acids. It is involved in the production of fatty acids through a process called fatty acid synthesis, which is a key step in the production of energy and building blocks for various biomolecules. The molecular function of this protein is to catalyze the conversion of acetyl-CoA and malonyl-CoA into fatty acids through a series of reactions involving condensation, reduction, dehydration, and reductive elongation.",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.6331,0.6331,0.6331,0.6331,0.6331,5,0.6331,0.2692,no
ISRD_AMPFL,A0A8B0M9Z0,Reference,Eukaryota,2544,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The isariin synthetase isrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1 (Probable).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The isariin synthetase isrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1 (Probable).",,,,,,,GO:0004315; GO:0004312; GO:0016491; GO:0031177,GO:0031177; GO:0016747,GO:0004315,GO:0016747,GO:0016746,,0.8303,0.6331,0.6148,0.5549,,4,0.6583,0.2692,no
CGLR_HYDVU,A0A8B6XWW9,ESM2Text,Eukaryota,341,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Magnesium-dependent bifunctional enzyme which catalyzes the synthesis of 3'-phosphoribosylated ubiquitin chains, with a preference for nucleotides terminating in the 3'-UTR. The order of activity with different substrates is 3'-UMP/AICAR-3' followed by nucleotides terminating in the 3'-UTR. 3'-UMP is less effective than ATP and 3'-CMP-UMP (in vitro). May act as a non-canonical nucleotidyltransferase involved in postreplicative repair (PRR) of damaged DNA.",No,Yes,Maybe,No,No,not-Yes,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,GO:0052621,GO:0052621,GO:0052929,GO:0052621,GO:0052621,0.2426,0.2426,0.1747,0.2426,0.2426,5,0.229,0.5841,yes
CGLR_HYDVU,A0A8B6XWW9,Prot2Text,Eukaryota,341,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",Central component in the repair of UV radiation-induced DNA damage. It is a nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (cGAMP) from ATP and GTP.,Yes,Maybe,Yes,Maybe,Yes,Yes,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,,,,,GO:0004520,,,,,0.0939,1,0.0939,0.5841,yes
CGLR_HYDVU,A0A8B6XWW9,ProtT3,Eukaryota,341,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and the conversion of cGAMP to 2',3'-cGAMP (By similarity). 2',3'-cGAMP is a second messenger that acts as a ligand for the cGAS-STING pathway (By similarity). Belongs to the 2'-5'-oligoadenylate synthase family",Yes,Yes,Yes,Maybe,Yes,Yes,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,GO:0016779,GO:0061501,GO:0061501,GO:0016779,GO:0061501; GO:0005524; GO:0005525,0.2867,0.3401,0.3401,0.2867,0.7329,5,0.3973,0.5841,yes
CGLR_HYDVU,A0A8B6XWW9,ProtTale,Eukaryota,341,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Synthesizes 2',3'-cGAMP in a two-step reaction through production of the linear intermediate pppA(2'-5')pG. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of",Yes,Yes,Yes,Yes,Yes,Yes,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0005524; GO:0005525; GO:0003725,GO:0016779,0.5219,0.5219,0.5219,0.7944,0.2867,5,0.5294,0.5841,yes
CGLR_HYDVU,A0A8B6XWW9,Protein2Text,Eukaryota,341,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","This protein is a part of a family of enzymes called Nucleoside triphosphate hydrolases, which have a molecular function of hydrolyzing nucleoside triphosphates to nucleoside monophosphates and pyrophosphate.",No,No,No,No,No,not-Yes,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,,,GO:0003723,,,,,0.4691,,,1,0.4691,0.5841,yes
CGLR_HYDVU,A0A8B6XWW9,Reference,Eukaryota,341,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",,,,,,,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,GO:0061501; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0061501; GO:0003725,0.5835,0.5219,0.5219,0.5219,0.5835,5,0.5465,0.5841,yes
PIGV_CRIGR,A0A8C2M425,ESM2Text,Eukaryota,494,"Alpha-1,6-mannosyltransferase that catalyzes the transfer of the second mannose, via an alpha-1,6 bond, from a dolichol-phosphate- mannose (Dol-P-Man) to a 2-acyl-6-(alpha-D-mannosyl-(1->4)-alpha-D- glucosaminyl)-1-(1-radyl,2-acyl-sn-glycero-3-phospho)-1D-myo-inositol (also termed H2) intermediate to generate a 2-acyl-6-[alpha-D-mannosyl- (1->6)-alpha-D-mannosyl-(1->4)-alpha-D-glucosaminyl]-1-(1-radyl,2-acyl- sn-glycero-3-phospho)-1D-myo-inositol (also termed H3) and participates in the seventh step of the glycosylphosphatidylinositol-anchor biosynthesis. May also transfer the second mannose on a 2-acyl-6-[2-phosphoethanolamine-alpha-D-mannosyl-(1->4)-alpha-D- glucosaminyl]-1-(1-radyl,2-acyl-sn-glycero-3-phospho)-1D-myo-inositol (also termed H5), but less effectively (Probable).","Alpha-1,6-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0000009; GO:0004376,GO:0000030,GO:0000030,GO:0016757,GO:0000030,GO:0000030,0.8691,0.8691,0.6466,0.8691,0.8691,5,0.8246,0.6454,yes
PIGV_CRIGR,A0A8C2M425,Prot2Text,Eukaryota,494,"Alpha-1,6-mannosyltransferase that catalyzes the transfer of the second mannose, via an alpha-1,6 bond, from a dolichol-phosphate- mannose (Dol-P-Man) to a 2-acyl-6-(alpha-D-mannosyl-(1->4)-alpha-D- glucosaminyl)-1-(1-radyl,2-acyl-sn-glycero-3-phospho)-1D-myo-inositol (also termed H2) intermediate to generate a 2-acyl-6-[alpha-D-mannosyl- (1->6)-alpha-D-mannosyl-(1->4)-alpha-D-glucosaminyl]-1-(1-radyl,2-acyl- sn-glycero-3-phospho)-1D-myo-inositol (also termed H3) and participates in the seventh step of the glycosylphosphatidylinositol-anchor biosynthesis. May also transfer the second mannose on a 2-acyl-6-[2-phosphoethanolamine-alpha-D-mannosyl-(1->4)-alpha-D- glucosaminyl]-1-(1-radyl,2-acyl-sn-glycero-3-phospho)-1D-myo-inositol (also termed H5), but less effectively (Probable).","Alpha-1,6-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0000009; GO:0004376,GO:0000030,GO:0000030,GO:0000030,GO:0000030,GO:0000030,0.8691,0.8691,0.8691,0.8691,0.8691,5,0.8691,0.6454,yes
PIGV_CRIGR,A0A8C2M425,ProtT3,Eukaryota,494,"Alpha-1,6-mannosyltransferase that catalyzes the transfer of the second mannose, via an alpha-1,6 bond, from a dolichol-phosphate- mannose (Dol-P-Man) to a 2-acyl-6-(alpha-D-mannosyl-(1->4)-alpha-D- glucosaminyl)-1-(1-radyl,2-acyl-sn-glycero-3-phospho)-1D-myo-inositol (also termed H2) intermediate to generate a 2-acyl-6-[alpha-D-mannosyl- (1->6)-alpha-D-mannosyl-(1->4)-alpha-D-glucosaminyl]-1-(1-radyl,2-acyl- sn-glycero-3-phospho)-1D-myo-inositol (also termed H3) and participates in the seventh step of the glycosylphosphatidylinositol-anchor biosynthesis. May also transfer the second mannose on a 2-acyl-6-[2-phosphoethanolamine-alpha-D-mannosyl-(1->4)-alpha-D- glucosaminyl]-1-(1-radyl,2-acyl-sn-glycero-3-phospho)-1D-myo-inositol (also termed H5), but less effectively (Probable).","Alpha-1,6-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly (By similarity). Endoplasmic reticulum membrane; Multi-pass membrane protein. Belongs to the PIGV family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0000009; GO:0004376,GO:0016757,GO:0000030,GO:0000030,GO:0000030,GO:0000030,0.6466,0.8691,0.8691,0.8691,0.8691,5,0.8246,0.6454,yes
PIGV_CRIGR,A0A8C2M425,ProtTale,Eukaryota,494,"Alpha-1,6-mannosyltransferase that catalyzes the transfer of the second mannose, via an alpha-1,6 bond, from a dolichol-phosphate- mannose (Dol-P-Man) to a 2-acyl-6-(alpha-D-mannosyl-(1->4)-alpha-D- glucosaminyl)-1-(1-radyl,2-acyl-sn-glycero-3-phospho)-1D-myo-inositol (also termed H2) intermediate to generate a 2-acyl-6-[alpha-D-mannosyl- (1->6)-alpha-D-mannosyl-(1->4)-alpha-D-glucosaminyl]-1-(1-radyl,2-acyl- sn-glycero-3-phospho)-1D-myo-inositol (also termed H3) and participates in the seventh step of the glycosylphosphatidylinositol-anchor biosynthesis. May also transfer the second mannose on a 2-acyl-6-[2-phosphoethanolamine-alpha-D-mannosyl-(1->4)-alpha-D- glucosaminyl]-1-(1-radyl,2-acyl-sn-glycero-3-phospho)-1D-myo-inositol (also termed H5), but less effectively (Probable).",Mannosyltransferase involved in glycosylphosphatidylinositol- anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0000009; GO:0004376,GO:0000030,GO:0016758,GO:0000030,GO:0000030,GO:0000030,0.8691,0.7539,0.8691,0.8691,0.8691,5,0.8461,0.6454,yes
PIGV_CRIGR,A0A8C2M425,Protein2Text,Eukaryota,494,"Alpha-1,6-mannosyltransferase that catalyzes the transfer of the second mannose, via an alpha-1,6 bond, from a dolichol-phosphate- mannose (Dol-P-Man) to a 2-acyl-6-(alpha-D-mannosyl-(1->4)-alpha-D- glucosaminyl)-1-(1-radyl,2-acyl-sn-glycero-3-phospho)-1D-myo-inositol (also termed H2) intermediate to generate a 2-acyl-6-[alpha-D-mannosyl- (1->6)-alpha-D-mannosyl-(1->4)-alpha-D-glucosaminyl]-1-(1-radyl,2-acyl- sn-glycero-3-phospho)-1D-myo-inositol (also termed H3) and participates in the seventh step of the glycosylphosphatidylinositol-anchor biosynthesis. May also transfer the second mannose on a 2-acyl-6-[2-phosphoethanolamine-alpha-D-mannosyl-(1->4)-alpha-D- glucosaminyl]-1-(1-radyl,2-acyl-sn-glycero-3-phospho)-1D-myo-inositol (also termed H5), but less effectively (Probable).","The molecular function of this protein is an oligosaccharyl transferase, which is a type of enzyme that catalyzes the transfer of oligosaccharides to the nascent polypeptide chain during protein biosynthesis.",No,No,No,No,No,not-Yes,GO:0000009; GO:0004376,GO:0004576,GO:0004576,GO:0004579,GO:0004576,GO:0004579,0.6335,0.6335,0.5445,0.6335,0.5445,5,0.5979,0.6454,yes
PIGV_CRIGR,A0A8C2M425,Reference,Eukaryota,494,"Alpha-1,6-mannosyltransferase that catalyzes the transfer of the second mannose, via an alpha-1,6 bond, from a dolichol-phosphate- mannose (Dol-P-Man) to a 2-acyl-6-(alpha-D-mannosyl-(1->4)-alpha-D- glucosaminyl)-1-(1-radyl,2-acyl-sn-glycero-3-phospho)-1D-myo-inositol (also termed H2) intermediate to generate a 2-acyl-6-[alpha-D-mannosyl- (1->6)-alpha-D-mannosyl-(1->4)-alpha-D-glucosaminyl]-1-(1-radyl,2-acyl- sn-glycero-3-phospho)-1D-myo-inositol (also termed H3) and participates in the seventh step of the glycosylphosphatidylinositol-anchor biosynthesis. May also transfer the second mannose on a 2-acyl-6-[2-phosphoethanolamine-alpha-D-mannosyl-(1->4)-alpha-D- glucosaminyl]-1-(1-radyl,2-acyl-sn-glycero-3-phospho)-1D-myo-inositol (also termed H5), but less effectively (Probable).","Alpha-1,6-mannosyltransferase that catalyzes the transfer of the second mannose, via an alpha-1,6 bond, from a dolichol-phosphate- mannose (Dol-P-Man) to a 2-acyl-6-(alpha-D-mannosyl-(1->4)-alpha-D- glucosaminyl)-1-(1-radyl,2-acyl-sn-glycero-3-phospho)-1D-myo-inositol (also termed H2) intermediate to generate a 2-acyl-6-[alpha-D-mannosyl- (1->6)-alpha-D-mannosyl-(1->4)-alpha-D-glucosaminyl]-1-(1-radyl,2-acyl- sn-glycero-3-phospho)-1D-myo-inositol (also termed H3) and participates in the seventh step of the glycosylphosphatidylinositol-anchor biosynthesis. May also transfer the second mannose on a 2-acyl-6-[2-phosphoethanolamine-alpha-D-mannosyl-(1->4)-alpha-D- glucosaminyl]-1-(1-radyl,2-acyl-sn-glycero-3-phospho)-1D-myo-inositol (also termed H5), but less effectively (Probable).",,,,,,,GO:0000009; GO:0004376,GO:0000030,GO:0000030,GO:0000030,GO:0000030,GO:0000030,0.8691,0.8691,0.8691,0.8691,0.8691,5,0.8691,0.6454,yes
ESDPF_PENSH,A0A8D5M6H6,ESM2Text,Eukaryota,255,"Short-chain dehydrogenase/reductase; part of the cluster that mediates the biosynthesis of shearones, diterpenoid pyrones (DPs) which are structurally diverse meroterpenoids consisting of a diterpene linked by a pyrone, and which may exhibit a range of bioactivities. Whitin the pathway, esdpF takes part in the molecular scaffold modification via the oxidition of the hydroxy group of shearone A to a ketone at C-3 to form shearone B. The molecular scaffold is commonly biosynthesized by a series of enzymes including the non-reducing polyketide synthase (NR-PKS) esdpA that generates an alpha-pyrone; the prenyltransferase esdpC that attaches a geranylgeranyl pyrophosphate (GGPP) produced by the GGPP synthase (GGPPS) esdpD onto the pyrone unit; the FAD-dependent monooxygenase esdpE that converts an olefin on the diterpene unit into an epoxide; and the terpene cyclase esdpB that catalyzes the cyclization reactions to give the molecular backbone shearone A. In the modification steps, esdpF oxidizes the hydroxy group to a ketone at C-3 and esdpG then attaches hydroxy groups at both C-11 and C-12. After that, esdpI hydroxylates at C-20 and esdpH hydroxylates at C-6'. The ether bridge is generated by nucleophilic attack of the hydroxy group at C-20 to the carbonyl carbon at C-3. EsdpH can also functions prior to esdpI. The different combinations of these modification enzymes lead to the production of diverse shearone derivatives, shearone I being the end product of the pathway. The alpha-ketoglutarate-dependent dioxygenase esdpJ does not seem to be involved in this pathway.","Short chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the tropolone class of fungal maleic anhydrides. The pathway begins with the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide synthase (PKS) tropA. 3-methylorcinaldehyde is the substrate for the FAD-dependent monooxygenase tropB to yield a dearomatized hydroxycyclohexadione. The 2-oxoglutarate-dependent dioxygenase tropC then performs the oxidative ring expansion to provide the first tropolone metabolite stipitaldehyde. Trop D converts stipitaldehyde into stipitacetal which is in turn converted to stipitalide by the short-chain dehydrogenase/reductase tropE. The next steps involve tropF, tropG, tropH, tropI and tropJ to form successive tropolone maleic anhydrides including stipitaldehydic, stipitatonic and stipitatic acids.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2058,no
ESDPF_PENSH,A0A8D5M6H6,Prot2Text,Eukaryota,255,"Short-chain dehydrogenase/reductase; part of the cluster that mediates the biosynthesis of shearones, diterpenoid pyrones (DPs) which are structurally diverse meroterpenoids consisting of a diterpene linked by a pyrone, and which may exhibit a range of bioactivities. Whitin the pathway, esdpF takes part in the molecular scaffold modification via the oxidition of the hydroxy group of shearone A to a ketone at C-3 to form shearone B. The molecular scaffold is commonly biosynthesized by a series of enzymes including the non-reducing polyketide synthase (NR-PKS) esdpA that generates an alpha-pyrone; the prenyltransferase esdpC that attaches a geranylgeranyl pyrophosphate (GGPP) produced by the GGPP synthase (GGPPS) esdpD onto the pyrone unit; the FAD-dependent monooxygenase esdpE that converts an olefin on the diterpene unit into an epoxide; and the terpene cyclase esdpB that catalyzes the cyclization reactions to give the molecular backbone shearone A. In the modification steps, esdpF oxidizes the hydroxy group to a ketone at C-3 and esdpG then attaches hydroxy groups at both C-11 and C-12. After that, esdpI hydroxylates at C-20 and esdpH hydroxylates at C-6'. The ether bridge is generated by nucleophilic attack of the hydroxy group at C-20 to the carbonyl carbon at C-3. EsdpH can also functions prior to esdpI. The different combinations of these modification enzymes lead to the production of diverse shearone derivatives, shearone I being the end product of the pathway. The alpha-ketoglutarate-dependent dioxygenase esdpJ does not seem to be involved in this pathway.","Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome monooxygenase P450 claM then catalyzes the dimerization of nataloe-emodin to cladofulvin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2058,no
ESDPF_PENSH,A0A8D5M6H6,ProtT3,Eukaryota,255,"Short-chain dehydrogenase/reductase; part of the cluster that mediates the biosynthesis of shearones, diterpenoid pyrones (DPs) which are structurally diverse meroterpenoids consisting of a diterpene linked by a pyrone, and which may exhibit a range of bioactivities. Whitin the pathway, esdpF takes part in the molecular scaffold modification via the oxidition of the hydroxy group of shearone A to a ketone at C-3 to form shearone B. The molecular scaffold is commonly biosynthesized by a series of enzymes including the non-reducing polyketide synthase (NR-PKS) esdpA that generates an alpha-pyrone; the prenyltransferase esdpC that attaches a geranylgeranyl pyrophosphate (GGPP) produced by the GGPP synthase (GGPPS) esdpD onto the pyrone unit; the FAD-dependent monooxygenase esdpE that converts an olefin on the diterpene unit into an epoxide; and the terpene cyclase esdpB that catalyzes the cyclization reactions to give the molecular backbone shearone A. In the modification steps, esdpF oxidizes the hydroxy group to a ketone at C-3 and esdpG then attaches hydroxy groups at both C-11 and C-12. After that, esdpI hydroxylates at C-20 and esdpH hydroxylates at C-6'. The ether bridge is generated by nucleophilic attack of the hydroxy group at C-20 to the carbonyl carbon at C-3. EsdpH can also functions prior to esdpI. The different combinations of these modification enzymes lead to the production of diverse shearone derivatives, shearone I being the end product of the pathway. The alpha-ketoglutarate-dependent dioxygenase esdpJ does not seem to be involved in this pathway.",Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeranylindole (,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2058,no
ESDPF_PENSH,A0A8D5M6H6,ProtTale,Eukaryota,255,"Short-chain dehydrogenase/reductase; part of the cluster that mediates the biosynthesis of shearones, diterpenoid pyrones (DPs) which are structurally diverse meroterpenoids consisting of a diterpene linked by a pyrone, and which may exhibit a range of bioactivities. Whitin the pathway, esdpF takes part in the molecular scaffold modification via the oxidition of the hydroxy group of shearone A to a ketone at C-3 to form shearone B. The molecular scaffold is commonly biosynthesized by a series of enzymes including the non-reducing polyketide synthase (NR-PKS) esdpA that generates an alpha-pyrone; the prenyltransferase esdpC that attaches a geranylgeranyl pyrophosphate (GGPP) produced by the GGPP synthase (GGPPS) esdpD onto the pyrone unit; the FAD-dependent monooxygenase esdpE that converts an olefin on the diterpene unit into an epoxide; and the terpene cyclase esdpB that catalyzes the cyclization reactions to give the molecular backbone shearone A. In the modification steps, esdpF oxidizes the hydroxy group to a ketone at C-3 and esdpG then attaches hydroxy groups at both C-11 and C-12. After that, esdpI hydroxylates at C-20 and esdpH hydroxylates at C-6'. The ether bridge is generated by nucleophilic attack of the hydroxy group at C-20 to the carbonyl carbon at C-3. EsdpH can also functions prior to esdpI. The different combinations of these modification enzymes lead to the production of diverse shearone derivatives, shearone I being the end product of the pathway. The alpha-ketoglutarate-dependent dioxygenase esdpJ does not seem to be involved in this pathway.","Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2058,no
ESDPF_PENSH,A0A8D5M6H6,Protein2Text,Eukaryota,255,"Short-chain dehydrogenase/reductase; part of the cluster that mediates the biosynthesis of shearones, diterpenoid pyrones (DPs) which are structurally diverse meroterpenoids consisting of a diterpene linked by a pyrone, and which may exhibit a range of bioactivities. Whitin the pathway, esdpF takes part in the molecular scaffold modification via the oxidition of the hydroxy group of shearone A to a ketone at C-3 to form shearone B. The molecular scaffold is commonly biosynthesized by a series of enzymes including the non-reducing polyketide synthase (NR-PKS) esdpA that generates an alpha-pyrone; the prenyltransferase esdpC that attaches a geranylgeranyl pyrophosphate (GGPP) produced by the GGPP synthase (GGPPS) esdpD onto the pyrone unit; the FAD-dependent monooxygenase esdpE that converts an olefin on the diterpene unit into an epoxide; and the terpene cyclase esdpB that catalyzes the cyclization reactions to give the molecular backbone shearone A. In the modification steps, esdpF oxidizes the hydroxy group to a ketone at C-3 and esdpG then attaches hydroxy groups at both C-11 and C-12. After that, esdpI hydroxylates at C-20 and esdpH hydroxylates at C-6'. The ether bridge is generated by nucleophilic attack of the hydroxy group at C-20 to the carbonyl carbon at C-3. EsdpH can also functions prior to esdpI. The different combinations of these modification enzymes lead to the production of diverse shearone derivatives, shearone I being the end product of the pathway. The alpha-ketoglutarate-dependent dioxygenase esdpJ does not seem to be involved in this pathway.","The molecular function of this protein is unknown. However, based on its name, it is likely involved in a redox reaction, specifically the transfer of a hydroxyl group (-OH) to another molecule. This type of reaction is often catalyzed by enzymes known as oxidoreductases. More specifically, the name ""hydroxysteroid dehydrogenase"" suggests that this protein may catalyze the oxidation or reduction of a hydroxyl group attached to a steroid molecule. However, without more information, it is difficult to say for certain what the specific molecular function of this protein is.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016491,,,,,,,,,,,0,,0.2058,no
ESDPF_PENSH,A0A8D5M6H6,Reference,Eukaryota,255,"Short-chain dehydrogenase/reductase; part of the cluster that mediates the biosynthesis of shearones, diterpenoid pyrones (DPs) which are structurally diverse meroterpenoids consisting of a diterpene linked by a pyrone, and which may exhibit a range of bioactivities. Whitin the pathway, esdpF takes part in the molecular scaffold modification via the oxidition of the hydroxy group of shearone A to a ketone at C-3 to form shearone B. The molecular scaffold is commonly biosynthesized by a series of enzymes including the non-reducing polyketide synthase (NR-PKS) esdpA that generates an alpha-pyrone; the prenyltransferase esdpC that attaches a geranylgeranyl pyrophosphate (GGPP) produced by the GGPP synthase (GGPPS) esdpD onto the pyrone unit; the FAD-dependent monooxygenase esdpE that converts an olefin on the diterpene unit into an epoxide; and the terpene cyclase esdpB that catalyzes the cyclization reactions to give the molecular backbone shearone A. In the modification steps, esdpF oxidizes the hydroxy group to a ketone at C-3 and esdpG then attaches hydroxy groups at both C-11 and C-12. After that, esdpI hydroxylates at C-20 and esdpH hydroxylates at C-6'. The ether bridge is generated by nucleophilic attack of the hydroxy group at C-20 to the carbonyl carbon at C-3. EsdpH can also functions prior to esdpI. The different combinations of these modification enzymes lead to the production of diverse shearone derivatives, shearone I being the end product of the pathway. The alpha-ketoglutarate-dependent dioxygenase esdpJ does not seem to be involved in this pathway.","Short-chain dehydrogenase/reductase; part of the cluster that mediates the biosynthesis of shearones, diterpenoid pyrones (DPs) which are structurally diverse meroterpenoids consisting of a diterpene linked by a pyrone, and which may exhibit a range of bioactivities. Whitin the pathway, esdpF takes part in the molecular scaffold modification via the oxidition of the hydroxy group of shearone A to a ketone at C-3 to form shearone B. The molecular scaffold is commonly biosynthesized by a series of enzymes including the non-reducing polyketide synthase (NR-PKS) esdpA that generates an alpha-pyrone; the prenyltransferase esdpC that attaches a geranylgeranyl pyrophosphate (GGPP) produced by the GGPP synthase (GGPPS) esdpD onto the pyrone unit; the FAD-dependent monooxygenase esdpE that converts an olefin on the diterpene unit into an epoxide; and the terpene cyclase esdpB that catalyzes the cyclization reactions to give the molecular backbone shearone A. In the modification steps, esdpF oxidizes the hydroxy group to a ketone at C-3 and esdpG then attaches hydroxy groups at both C-11 and C-12. After that, esdpI hydroxylates at C-20 and esdpH hydroxylates at C-6'. The ether bridge is generated by nucleophilic attack of the hydroxy group at C-20 to the carbonyl carbon at C-3. EsdpH can also functions prior to esdpI. The different combinations of these modification enzymes lead to the production of diverse shearone derivatives, shearone I being the end product of the pathway. The alpha-ketoglutarate-dependent dioxygenase esdpJ does not seem to be involved in this pathway.",,,,,,,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2058,no
ESDPJ_PENSH,A0A8D5RZ52,ESM2Text,Eukaryota,376,"Alpha-ketoglutarate-dependent dioxygenas; part of the cluster that mediates the biosynthesis of shearones, diterpenoid pyrones (DPs) which are structurally diverse meroterpenoids consisting of a diterpene linked by a pyrone, and which may exhibit a range of bioactivities. The alpha-ketoglutarate-dependent dioxygenase esdpJ does not seem to be involved in this pathway. The molecular scaffold is commonly biosynthesized by a series of enzymes including the non-reducing polyketide synthase (NR-PKS) esdpA that generates an alpha-pyrone; the prenyltransferase esdpC that attaches a geranylgeranyl pyrophosphate (GGPP) produced by the GGPP synthase (GGPPS) esdpD onto the pyrone unit; the FAD-dependent monooxygenase esdpE that converts an olefin on the diterpene unit into an epoxide; and the terpene cyclase esdpB that catalyzes the cyclization reactions to give the molecular backbone shearone A. In the modification steps, esdpF oxidizes the hydroxy group to a ketone at C-3 and esdpG then attaches hydroxy groups at both C-11 and C-12. After that, esdpI hydroxylates at C-20 and esdpH hydroxylates at C-6'. The ether bridge is generated by nucleophilic attack of the hydroxy group at C-20 to the carbonyl carbon at C-3. EsdpH can also functions prior to esdpI. The different combinations of these modification enzymes lead to the production of diverse shearone derivatives, shearone I being the end product of the pathway.",Utilizes a beta-hydroxyl moiety from reduced glutathione to catalyze the ring fission of desulfo-glutarate (DSG or D-glutarate) and sulfite. This enzyme is a key enzyme in sulfate assimilation that catalyzes the degradation of sulfo-D-glutarate (S-S-S-CoA) to D-glutarate (Probable). Other sulfolipid biosynthetic enzymes are also observed.,No,Maybe,No,No,No,not-Yes,GO:0016706; GO:0046872,,,,,,,,,,,0,,0.411,no
ESDPJ_PENSH,A0A8D5RZ52,Prot2Text,Eukaryota,376,"Alpha-ketoglutarate-dependent dioxygenas; part of the cluster that mediates the biosynthesis of shearones, diterpenoid pyrones (DPs) which are structurally diverse meroterpenoids consisting of a diterpene linked by a pyrone, and which may exhibit a range of bioactivities. The alpha-ketoglutarate-dependent dioxygenase esdpJ does not seem to be involved in this pathway. The molecular scaffold is commonly biosynthesized by a series of enzymes including the non-reducing polyketide synthase (NR-PKS) esdpA that generates an alpha-pyrone; the prenyltransferase esdpC that attaches a geranylgeranyl pyrophosphate (GGPP) produced by the GGPP synthase (GGPPS) esdpD onto the pyrone unit; the FAD-dependent monooxygenase esdpE that converts an olefin on the diterpene unit into an epoxide; and the terpene cyclase esdpB that catalyzes the cyclization reactions to give the molecular backbone shearone A. In the modification steps, esdpF oxidizes the hydroxy group to a ketone at C-3 and esdpG then attaches hydroxy groups at both C-11 and C-12. After that, esdpI hydroxylates at C-20 and esdpH hydroxylates at C-6'. The ether bridge is generated by nucleophilic attack of the hydroxy group at C-20 to the carbonyl carbon at C-3. EsdpH can also functions prior to esdpI. The different combinations of these modification enzymes lead to the production of diverse shearone derivatives, shearone I being the end product of the pathway.",Alpha-ketoglutarate-dependent xanthine dioxygenase is a non-heme mononuclear Fe(2+) enzyme that decarboxylates alpha-ketoglutarate to succinate and CO(2) while hydroxylating xanthine to generate uric acid. Allows xanthine utilization as a nitrogen source.,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0016706; GO:0046872,GO:0016706,GO:0016706,GO:0016706,GO:0016706,GO:0016706,0.698,0.698,0.698,0.698,0.698,5,0.698,0.411,no
ESDPJ_PENSH,A0A8D5RZ52,ProtT3,Eukaryota,376,"Alpha-ketoglutarate-dependent dioxygenas; part of the cluster that mediates the biosynthesis of shearones, diterpenoid pyrones (DPs) which are structurally diverse meroterpenoids consisting of a diterpene linked by a pyrone, and which may exhibit a range of bioactivities. The alpha-ketoglutarate-dependent dioxygenase esdpJ does not seem to be involved in this pathway. The molecular scaffold is commonly biosynthesized by a series of enzymes including the non-reducing polyketide synthase (NR-PKS) esdpA that generates an alpha-pyrone; the prenyltransferase esdpC that attaches a geranylgeranyl pyrophosphate (GGPP) produced by the GGPP synthase (GGPPS) esdpD onto the pyrone unit; the FAD-dependent monooxygenase esdpE that converts an olefin on the diterpene unit into an epoxide; and the terpene cyclase esdpB that catalyzes the cyclization reactions to give the molecular backbone shearone A. In the modification steps, esdpF oxidizes the hydroxy group to a ketone at C-3 and esdpG then attaches hydroxy groups at both C-11 and C-12. After that, esdpI hydroxylates at C-20 and esdpH hydroxylates at C-6'. The ether bridge is generated by nucleophilic attack of the hydroxy group at C-20 to the carbonyl carbon at C-3. EsdpH can also functions prior to esdpI. The different combinations of these modification enzymes lead to the production of diverse shearone derivatives, shearone I being the end product of the pathway.",Alpha-ketoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016706; GO:0046872,GO:0016706,GO:0016706,GO:0016706,GO:0016706,GO:0016706,0.698,0.698,0.698,0.698,0.698,5,0.698,0.411,no
ESDPJ_PENSH,A0A8D5RZ52,ProtTale,Eukaryota,376,"Alpha-ketoglutarate-dependent dioxygenas; part of the cluster that mediates the biosynthesis of shearones, diterpenoid pyrones (DPs) which are structurally diverse meroterpenoids consisting of a diterpene linked by a pyrone, and which may exhibit a range of bioactivities. The alpha-ketoglutarate-dependent dioxygenase esdpJ does not seem to be involved in this pathway. The molecular scaffold is commonly biosynthesized by a series of enzymes including the non-reducing polyketide synthase (NR-PKS) esdpA that generates an alpha-pyrone; the prenyltransferase esdpC that attaches a geranylgeranyl pyrophosphate (GGPP) produced by the GGPP synthase (GGPPS) esdpD onto the pyrone unit; the FAD-dependent monooxygenase esdpE that converts an olefin on the diterpene unit into an epoxide; and the terpene cyclase esdpB that catalyzes the cyclization reactions to give the molecular backbone shearone A. In the modification steps, esdpF oxidizes the hydroxy group to a ketone at C-3 and esdpG then attaches hydroxy groups at both C-11 and C-12. After that, esdpI hydroxylates at C-20 and esdpH hydroxylates at C-6'. The ether bridge is generated by nucleophilic attack of the hydroxy group at C-20 to the carbonyl carbon at C-3. EsdpH can also functions prior to esdpI. The different combinations of these modification enzymes lead to the production of diverse shearone derivatives, shearone I being the end product of the pathway.","Alpha-ketoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016706; GO:0046872,GO:0016706,GO:0016706,GO:0016706,GO:0016706,GO:0016706,0.698,0.698,0.698,0.698,0.698,5,0.698,0.411,no
ESDPJ_PENSH,A0A8D5RZ52,Protein2Text,Eukaryota,376,"Alpha-ketoglutarate-dependent dioxygenas; part of the cluster that mediates the biosynthesis of shearones, diterpenoid pyrones (DPs) which are structurally diverse meroterpenoids consisting of a diterpene linked by a pyrone, and which may exhibit a range of bioactivities. The alpha-ketoglutarate-dependent dioxygenase esdpJ does not seem to be involved in this pathway. The molecular scaffold is commonly biosynthesized by a series of enzymes including the non-reducing polyketide synthase (NR-PKS) esdpA that generates an alpha-pyrone; the prenyltransferase esdpC that attaches a geranylgeranyl pyrophosphate (GGPP) produced by the GGPP synthase (GGPPS) esdpD onto the pyrone unit; the FAD-dependent monooxygenase esdpE that converts an olefin on the diterpene unit into an epoxide; and the terpene cyclase esdpB that catalyzes the cyclization reactions to give the molecular backbone shearone A. In the modification steps, esdpF oxidizes the hydroxy group to a ketone at C-3 and esdpG then attaches hydroxy groups at both C-11 and C-12. After that, esdpI hydroxylates at C-20 and esdpH hydroxylates at C-6'. The ether bridge is generated by nucleophilic attack of the hydroxy group at C-20 to the carbonyl carbon at C-3. EsdpH can also functions prior to esdpI. The different combinations of these modification enzymes lead to the production of diverse shearone derivatives, shearone I being the end product of the pathway.","This protein is a dioxygenase enzyme. More specifically, it is a monooxygenase enzyme that catalyzes the oxidation of a specific substrate. In particular, it is a 2-oxoglutarate-dependent dioxygenase.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016706; GO:0046872,GO:0016706,GO:0016706,GO:0016491,GO:0016706,GO:0016706,0.698,0.698,0.4567,0.698,0.698,5,0.6497,0.411,no
ESDPJ_PENSH,A0A8D5RZ52,Reference,Eukaryota,376,"Alpha-ketoglutarate-dependent dioxygenas; part of the cluster that mediates the biosynthesis of shearones, diterpenoid pyrones (DPs) which are structurally diverse meroterpenoids consisting of a diterpene linked by a pyrone, and which may exhibit a range of bioactivities. The alpha-ketoglutarate-dependent dioxygenase esdpJ does not seem to be involved in this pathway. The molecular scaffold is commonly biosynthesized by a series of enzymes including the non-reducing polyketide synthase (NR-PKS) esdpA that generates an alpha-pyrone; the prenyltransferase esdpC that attaches a geranylgeranyl pyrophosphate (GGPP) produced by the GGPP synthase (GGPPS) esdpD onto the pyrone unit; the FAD-dependent monooxygenase esdpE that converts an olefin on the diterpene unit into an epoxide; and the terpene cyclase esdpB that catalyzes the cyclization reactions to give the molecular backbone shearone A. In the modification steps, esdpF oxidizes the hydroxy group to a ketone at C-3 and esdpG then attaches hydroxy groups at both C-11 and C-12. After that, esdpI hydroxylates at C-20 and esdpH hydroxylates at C-6'. The ether bridge is generated by nucleophilic attack of the hydroxy group at C-20 to the carbonyl carbon at C-3. EsdpH can also functions prior to esdpI. The different combinations of these modification enzymes lead to the production of diverse shearone derivatives, shearone I being the end product of the pathway.","Alpha-ketoglutarate-dependent dioxygenas; part of the cluster that mediates the biosynthesis of shearones, diterpenoid pyrones (DPs) which are structurally diverse meroterpenoids consisting of a diterpene linked by a pyrone, and which may exhibit a range of bioactivities. The alpha-ketoglutarate-dependent dioxygenase esdpJ does not seem to be involved in this pathway. The molecular scaffold is commonly biosynthesized by a series of enzymes including the non-reducing polyketide synthase (NR-PKS) esdpA that generates an alpha-pyrone; the prenyltransferase esdpC that attaches a geranylgeranyl pyrophosphate (GGPP) produced by the GGPP synthase (GGPPS) esdpD onto the pyrone unit; the FAD-dependent monooxygenase esdpE that converts an olefin on the diterpene unit into an epoxide; and the terpene cyclase esdpB that catalyzes the cyclization reactions to give the molecular backbone shearone A. In the modification steps, esdpF oxidizes the hydroxy group to a ketone at C-3 and esdpG then attaches hydroxy groups at both C-11 and C-12. After that, esdpI hydroxylates at C-20 and esdpH hydroxylates at C-6'. The ether bridge is generated by nucleophilic attack of the hydroxy group at C-20 to the carbonyl carbon at C-3. EsdpH can also functions prior to esdpI. The different combinations of these modification enzymes lead to the production of diverse shearone derivatives, shearone I being the end product of the pathway.",,,,,,,GO:0016706; GO:0046872,GO:0016706,,GO:0016706,GO:0016706,GO:0016706,0.698,,0.698,0.698,0.698,4,0.698,0.411,no
ATR1_STEAL,A0A8F4SKJ7,ESM2Text,Eukaryota,2500,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of atranorin, a depside of polyketide origin that accumulates in the cortical or medullary layers of lichen thalli. The first step in the pathway is performed by the non-reducing polyketide synthase atr1 that produces 4-O- demethylbarbatic acid composed of two 3-methylorsellinic acid (3MOA) moieties from S-adenosyl-L-methionine (SAM), acetyl-CoA and malonyl-CoA units. The pathway continues with the actions of the cytochrome P450 monooygenase atr2 that catalizes the oxidation of c-9 and the O-methyltransferase atr3 that performs the methylation of the carboxyl group to yield atranorin, via the proatranorin II and III intermediates if atr2 acts first, or the proatranorin I intermediate if atr3 acts first.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of asperlin, a polyketide showing anti-inflammatory, antitumor and antibiotic activities. The first step of the asperlin biosynthesis is the production of the intermediate 2,4,6-octatrienoic acid by the highly redusing polyketide synthase alnA with cleavage of the PKS product by the esterase alnB. 2,4,6-octatrienoic acid is further converted to asperlin via several steps involving the remaining enzymes from the cluster.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0008168,,GO:0016747,GO:0016491; GO:0016740,GO:0016746,GO:0016746,,0.7598,0.5981,0.6859,0.6859,4,0.6824,0.318,no
ATR1_STEAL,A0A8F4SKJ7,Prot2Text,Eukaryota,2500,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of atranorin, a depside of polyketide origin that accumulates in the cortical or medullary layers of lichen thalli. The first step in the pathway is performed by the non-reducing polyketide synthase atr1 that produces 4-O- demethylbarbatic acid composed of two 3-methylorsellinic acid (3MOA) moieties from S-adenosyl-L-methionine (SAM), acetyl-CoA and malonyl-CoA units. The pathway continues with the actions of the cytochrome P450 monooygenase atr2 that catalizes the oxidation of c-9 and the O-methyltransferase atr3 that performs the methylation of the carboxyl group to yield atranorin, via the proatranorin II and III intermediates if atr2 acts first, or the proatranorin I intermediate if atr3 acts first.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0008168,,,GO:0016747,,GO:0016746,,,0.7598,,0.6859,2,0.7228,0.318,no
ATR1_STEAL,A0A8F4SKJ7,ProtT3,Eukaryota,2500,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of atranorin, a depside of polyketide origin that accumulates in the cortical or medullary layers of lichen thalli. The first step in the pathway is performed by the non-reducing polyketide synthase atr1 that produces 4-O- demethylbarbatic acid composed of two 3-methylorsellinic acid (3MOA) moieties from S-adenosyl-L-methionine (SAM), acetyl-CoA and malonyl-CoA units. The pathway continues with the actions of the cytochrome P450 monooygenase atr2 that catalizes the oxidation of c-9 and the O-methyltransferase atr3 that performs the methylation of the carboxyl group to yield atranorin, via the proatranorin II and III intermediates if atr2 acts first, or the proatranorin I intermediate if atr3 acts first.",Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0008168,GO:0016747,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.7598,0.6859,0.6859,0.6859,0.6859,5,0.7007,0.318,no
ATR1_STEAL,A0A8F4SKJ7,ProtTale,Eukaryota,2500,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of atranorin, a depside of polyketide origin that accumulates in the cortical or medullary layers of lichen thalli. The first step in the pathway is performed by the non-reducing polyketide synthase atr1 that produces 4-O- demethylbarbatic acid composed of two 3-methylorsellinic acid (3MOA) moieties from S-adenosyl-L-methionine (SAM), acetyl-CoA and malonyl-CoA units. The pathway continues with the actions of the cytochrome P450 monooygenase atr2 that catalizes the oxidation of c-9 and the O-methyltransferase atr3 that performs the methylation of the carboxyl group to yield atranorin, via the proatranorin II and III intermediates if atr2 acts first, or the proatranorin I intermediate if atr3 acts first.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0008168,GO:0016747,GO:0016747,GO:0016746,GO:0016746,,0.7598,0.7598,0.6859,0.6859,,4,0.7228,0.318,no
ATR1_STEAL,A0A8F4SKJ7,Protein2Text,Eukaryota,2500,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of atranorin, a depside of polyketide origin that accumulates in the cortical or medullary layers of lichen thalli. The first step in the pathway is performed by the non-reducing polyketide synthase atr1 that produces 4-O- demethylbarbatic acid composed of two 3-methylorsellinic acid (3MOA) moieties from S-adenosyl-L-methionine (SAM), acetyl-CoA and malonyl-CoA units. The pathway continues with the actions of the cytochrome P450 monooygenase atr2 that catalizes the oxidation of c-9 and the O-methyltransferase atr3 that performs the methylation of the carboxyl group to yield atranorin, via the proatranorin II and III intermediates if atr2 acts first, or the proatranorin I intermediate if atr3 acts first.","This protein is involved in the synthesis of coenzyme A (CoA), which is a crucial molecule for various metabolic processes in the cell. More specifically, it is involved in the production of 4'-phosphopantetheine, a key component of CoA.",No,No,No,No,No,not-Yes,GO:0004315; GO:0004312; GO:0008168,,,,,,,,,,,0,,0.318,no
ATR1_STEAL,A0A8F4SKJ7,Reference,Eukaryota,2500,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of atranorin, a depside of polyketide origin that accumulates in the cortical or medullary layers of lichen thalli. The first step in the pathway is performed by the non-reducing polyketide synthase atr1 that produces 4-O- demethylbarbatic acid composed of two 3-methylorsellinic acid (3MOA) moieties from S-adenosyl-L-methionine (SAM), acetyl-CoA and malonyl-CoA units. The pathway continues with the actions of the cytochrome P450 monooygenase atr2 that catalizes the oxidation of c-9 and the O-methyltransferase atr3 that performs the methylation of the carboxyl group to yield atranorin, via the proatranorin II and III intermediates if atr2 acts first, or the proatranorin I intermediate if atr3 acts first.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of atranorin, a depside of polyketide origin that accumulates in the cortical or medullary layers of lichen thalli. The first step in the pathway is performed by the non-reducing polyketide synthase atr1 that produces 4-O- demethylbarbatic acid composed of two 3-methylorsellinic acid (3MOA) moieties from S-adenosyl-L-methionine (SAM), acetyl-CoA and malonyl-CoA units. The pathway continues with the actions of the cytochrome P450 monooygenase atr2 that catalizes the oxidation of c-9 and the O-methyltransferase atr3 that performs the methylation of the carboxyl group to yield atranorin, via the proatranorin II and III intermediates if atr2 acts first, or the proatranorin I intermediate if atr3 acts first.",,,,,,,GO:0004315; GO:0004312; GO:0008168,GO:0031177; GO:0016747,GO:0004315; GO:0008168,GO:0016747,GO:0016746; GO:0008168,,0.6263,0.9458,0.7598,0.8374,,4,0.7923,0.318,no
CUBB_PSICU,A0A8H7XMX0,ESM2Text,Eukaryota,344,"Terpene cyclase that catalyzes the cyclization of (2E,6E)- farnesyl diphosphate (FPP) to produce the sesquiterpene (3R,6E)- nerolidol. Is also able to use (2E)-geranyl diphosphate (GPP) as substrate to produce the monoterpene (R)-linalool.",Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to delta(6)-protoilludene.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0016829,GO:0010333,GO:0000287; GO:0016829,GO:0010333,GO:0010333,0.4539,0.6963,0.7355,0.6963,0.6963,5,0.6557,0.1946,no
CUBB_PSICU,A0A8H7XMX0,Prot2Text,Eukaryota,344,"Terpene cyclase that catalyzes the cyclization of (2E,6E)- farnesyl diphosphate (FPP) to produce the sesquiterpene (3R,6E)- nerolidol. Is also able to use (2E)-geranyl diphosphate (GPP) as substrate to produce the monoterpene (R)-linalool.",Catalyzes the cyclization of farnesyl diphosphate (FPP) to isoafricanol.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0010333,,GO:0010333,GO:0010333,GO:0010333,GO:0010333,,0.6963,0.6963,0.6963,0.6963,4,0.6963,0.1946,no
CUBB_PSICU,A0A8H7XMX0,ProtT3,Eukaryota,344,"Terpene cyclase that catalyzes the cyclization of (2E,6E)- farnesyl diphosphate (FPP) to produce the sesquiterpene (3R,6E)- nerolidol. Is also able to use (2E)-geranyl diphosphate (GPP) as substrate to produce the monoterpene (R)-linalool.",Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to the bicyclic sesquiterpene delta(6)-protoilludene. Belongs to the terpene synthase family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0010333,GO:0010333,GO:0016829,GO:0010333,GO:0016829,0.6963,0.6963,0.4539,0.6963,0.4539,5,0.5993,0.1946,no
CUBB_PSICU,A0A8H7XMX0,ProtTale,Eukaryota,344,"Terpene cyclase that catalyzes the cyclization of (2E,6E)- farnesyl diphosphate (FPP) to produce the sesquiterpene (3R,6E)- nerolidol. Is also able to use (2E)-geranyl diphosphate (GPP) as substrate to produce the monoterpene (R)-linalool.","Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to various sesquiterpenes, including alpha-copaene, beta-copaene, beta-caryophyllene, gamma-cadinene, delta-cadinene, delta-3-carene, germacrene D, alpha-cadinol, alpha-cadinol, alpha-cadinol, alpha-cadinol, alpha-cadinol, alpha-cadinol, alpha-cadinol, alpha-cadinol, alpha-cadinol, alpha-cadinol, alpha-cadinol, alpha-cadinol,",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0010333,GO:0010333,GO:0016829,GO:0010333,GO:0010333,0.6963,0.6963,0.4539,0.6963,0.6963,5,0.6478,0.1946,no
CUBB_PSICU,A0A8H7XMX0,Protein2Text,Eukaryota,344,"Terpene cyclase that catalyzes the cyclization of (2E,6E)- farnesyl diphosphate (FPP) to produce the sesquiterpene (3R,6E)- nerolidol. Is also able to use (2E)-geranyl diphosphate (GPP) as substrate to produce the monoterpene (R)-linalool.","The molecular function of this protein is to catalyze a reaction, specifically the biosynthesis of sesquiterpenes. It is involved in the production of sesquiterpenes, which are a class of terpenes with 15 carbon atoms. This protein is likely to be a sesquiterpene synthase, an enzyme that converts farnesyl diphosphate (FPP) into a specific sesquiterpene.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0010334,GO:0010334,GO:0010334,GO:0010334,,0.6051,0.6051,0.6051,0.6051,,4,0.6051,0.1946,no
CUBB_PSICU,A0A8H7XMX0,Reference,Eukaryota,344,"Terpene cyclase that catalyzes the cyclization of (2E,6E)- farnesyl diphosphate (FPP) to produce the sesquiterpene (3R,6E)- nerolidol. Is also able to use (2E)-geranyl diphosphate (GPP) as substrate to produce the monoterpene (R)-linalool.","Terpene cyclase that catalyzes the cyclization of (2E,6E)- farnesyl diphosphate (FPP) to produce the sesquiterpene (3R,6E)- nerolidol. Is also able to use (2E)-geranyl diphosphate (GPP) as substrate to produce the monoterpene (R)-linalool.",,,,,,,GO:0046872; GO:0010333,GO:0010333; GO:0000900,GO:0010333,GO:0010333,GO:0010333,GO:0016829,0.5632,0.6963,0.6963,0.6963,0.4539,5,0.6212,0.1946,no
CGLR_EXADI,A0A913XCT1,ESM2Text,Eukaryota,546,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly.,No,No,No,No,No,not-Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0003725,GO:0003725,GO:0003725,GO:0003725,GO:0003725,0.1694,0.1694,0.1694,0.1694,0.1694,5,0.1694,0.5916,yes
CGLR_EXADI,A0A913XCT1,Prot2Text,Eukaryota,546,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly.,No,No,No,No,No,not-Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0016779,,GO:0016779,GO:0016779,GO:0016779,0.3478,,0.3478,0.3478,0.3478,4,0.3478,0.5916,yes
CGLR_EXADI,A0A913XCT1,ProtT3,Eukaryota,546,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity (By similarity). Catalyzes the formation of 2',3'-cGAMP from ATP and GTP in a two-step reaction (By similarity). In the first step, 2',3'-cGAMP is formed by condensation of ATP and GTP (By similarity). In the second step, 2',3'-cGAMP is converted into cyclic GMP-AMP",Yes,Yes,Yes,Yes,Yes,Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0016779,GO:0061501,GO:0061501,GO:0016779,GO:0061501; GO:0005524; GO:0005525,0.3478,0.4353,0.4353,0.3478,0.8984,5,0.4929,0.5916,yes
CGLR_EXADI,A0A913XCT1,ProtTale,Eukaryota,546,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0005524; GO:0005525; GO:0003725,GO:0016779,0.3772,0.3772,0.3772,0.754,0.3478,5,0.4467,0.5916,yes
CGLR_EXADI,A0A913XCT1,Protein2Text,Eukaryota,546,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","This protein is a protein kinase, specifically a serine/threonine-protein kinase. It is involved in the regulation of various cellular processes, including cell signaling and gene expression.",No,No,No,No,No,not-Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.1786,0.1786,0.1786,0.1786,0.1786,5,0.1786,0.5916,yes
CGLR_EXADI,A0A913XCT1,Reference,Eukaryota,546,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",,,,,,,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0061501,GO:0016779,GO:0016779,GO:0016779,GO:0061501,0.4353,0.3478,0.3478,0.3478,0.4353,5,0.3828,0.5916,yes
AB62A_PENPR,A0A977JPB5,ESM2Text,Eukaryota,384,"Alpha-L-arabinofuranosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Releases L-arabinose from arabinoxylan.","Exo-beta-1,3-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Hydrolyzes xylobiose and xylotriose but not xylose, and is inactive toward beta-D-glucan and lichenan.",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0046556; GO:0030248,GO:0016798,GO:0004553,GO:0031176,GO:0004553,GO:0016798,0.5346,0.6127,0.453,0.6127,0.5346,5,0.5495,0.2009,no
AB62A_PENPR,A0A977JPB5,Prot2Text,Eukaryota,384,"Alpha-L-arabinofuranosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Releases L-arabinose from arabinoxylan.","Secreted alpha-L-arabinofuranosidase involved in cell wall biosynthesis. Initiates the elongation of cell wall xyloglucan chains by catalyzing the addition of 1,3-beta-linkages to cellulose.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046556; GO:0030248,,,,GO:0046556,GO:0046556,,,,0.7015,0.7015,2,0.7015,0.2009,no
AB62A_PENPR,A0A977JPB5,ProtT3,Eukaryota,384,"Alpha-L-arabinofuranosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Releases L-arabinose from arabinoxylan.","Alpha-L-arabinofuranosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Releases L-arabinose from xylan (By similarity). Secreted. Belongs to the glycosyl hydrolase 43 family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046556; GO:0030248,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,0.7015,0.7015,0.7015,0.7015,0.7015,5,0.7015,0.2009,no
AB62A_PENPR,A0A977JPB5,ProtTale,Eukaryota,384,"Alpha-L-arabinofuranosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Releases L-arabinose from arabinoxylan.","Involved in the degradation of plant cell wall polysaccharides. Hydrolyzes (1->4)-beta-D-glucan, (1->3)-beta-D-glucan and (1->6)-beta-D-glucan.",No,No,No,No,No,not-Yes,GO:0046556; GO:0030248,GO:0004553,GO:0004553,GO:0016798,GO:0004553,GO:0004553,0.6127,0.6127,0.5346,0.6127,0.6127,5,0.5971,0.2009,no
AB62A_PENPR,A0A977JPB5,Protein2Text,Eukaryota,384,"Alpha-L-arabinofuranosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Releases L-arabinose from arabinoxylan.","The molecular function of this protein is to catalyze the hydrolysis of glucan, a polysaccharide composed of glucose residues, which is a component of plant cell walls. More specifically, it is a beta-1,3-glucanase, meaning it breaks down beta-1,3-glucan bonds in the polysaccharide. This is likely related to its role in plant defense, as it can break down fungal cell walls and inhibit fungal growth.",No,No,No,No,No,not-Yes,GO:0046556; GO:0030248,GO:0052861,GO:0052861,GO:0042973,GO:0042973,GO:0042973,0.453,0.453,0.402,0.402,0.402,5,0.4224,0.2009,no
AB62A_PENPR,A0A977JPB5,Reference,Eukaryota,384,"Alpha-L-arabinofuranosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Releases L-arabinose from arabinoxylan.","Alpha-L-arabinofuranosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Releases L-arabinose from arabinoxylan.",,,,,,,GO:0046556; GO:0030248,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,0.7015,0.7015,0.7015,0.7015,0.7015,5,0.7015,0.2009,no
AKS2_ALSSC,A0A9E7LUL3,ESM2Text,Eukaryota,450,"Acyltransferase involved in the biosynthesis of akuammilan monoterpene indole alkaloids (MIAs) natural products, components with various biological properties such as antidiabetic, antibacterial, anti-inflammatory, anticancer, and antimalarial activities. Catalyzes the conversion of rhazimol to akuammiline.","Hydroxycinnamoyl transferase that catalyzes the transfer of an acyl from p-coumaryol-CoA to various acyl acceptors. Can use feruloyl-CoA, caffeoyl-CoA, sinapoyl-CoA and sinapoyl-CoA as acyl donors. Involved in the biosynthesis of the benzylisoquinoline alkaloid noscapine.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016746,GO:0016746,GO:0016747,GO:0016746,GO:0016746,GO:0016746,1.0,0.8416,1.0,1.0,1.0,5,0.9683,0.2486,no
AKS2_ALSSC,A0A9E7LUL3,Prot2Text,Eukaryota,450,"Acyltransferase involved in the biosynthesis of akuammilan monoterpene indole alkaloids (MIAs) natural products, components with various biological properties such as antidiabetic, antibacterial, anti-inflammatory, anticancer, and antimalarial activities. Catalyzes the conversion of rhazimol to akuammiline.","Participates in the biosynthesis of capsaicinoids in pungent cultivars of Capsicum frutescens. Capsaicinoids, the alkaloids responsible for the heat or pungency of chili pepper, are synthesized from phenylpropanoid intermediates in the placental tissue of chili peper fruit. Can transfer an acyl from 8-methylnon-6-enoyl-CoA to vanillylamine forming capsaicin and CoA.",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016746,1.0,1.0,1.0,0.8416,1.0,5,0.9683,0.2486,no
AKS2_ALSSC,A0A9E7LUL3,ProtT3,Eukaryota,450,"Acyltransferase involved in the biosynthesis of akuammilan monoterpene indole alkaloids (MIAs) natural products, components with various biological properties such as antidiabetic, antibacterial, anti-inflammatory, anticancer, and antimalarial activities. Catalyzes the conversion of rhazimol to akuammiline.",Belongs to the plant acyltransferase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016746,,GO:0016746,GO:0016746,GO:0016746,GO:0016746,,1.0,1.0,1.0,1.0,4,1.0,0.2486,no
AKS2_ALSSC,A0A9E7LUL3,ProtTale,Eukaryota,450,"Acyltransferase involved in the biosynthesis of akuammilan monoterpene indole alkaloids (MIAs) natural products, components with various biological properties such as antidiabetic, antibacterial, anti-inflammatory, anticancer, and antimalarial activities. Catalyzes the conversion of rhazimol to akuammiline.","Acetyltransferase involved in the biosynthesis of limonoids triterpene natural products such as azadirachtin, an antifeedant widely used as bioinsecticide, and possessing many medicinal applications including anti-cancer, anti-malarial, anti-rheumatic, antibacterial, anti-inflammatory, anti-pyretic and diuretic effects. Catalyzes the formation of 7-O-acetyl-7-O-acetylnimbinin from 7-O-acetylnimbinin and acetyl-CoA.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016746,GO:0016407,GO:0016747,GO:0016747,GO:0016747,GO:0016407,0.729,0.8416,0.8416,0.8416,0.729,5,0.7966,0.2486,no
AKS2_ALSSC,A0A9E7LUL3,Protein2Text,Eukaryota,450,"Acyltransferase involved in the biosynthesis of akuammilan monoterpene indole alkaloids (MIAs) natural products, components with various biological properties such as antidiabetic, antibacterial, anti-inflammatory, anticancer, and antimalarial activities. Catalyzes the conversion of rhazimol to akuammiline.","The molecular function of this protein is not specified in the provided text, but based on its name, it is likely to be involved in the hydrolysis of a molecule, possibly a glycoside or a lipid. The suffix ""-ase"" in its name suggests that it is an enzyme, and the prefix ""sulfotransferase"" suggests that it may be involved in the transfer of a sulfate group to a molecule. However, without more information, it is difficult to determine the specific molecular function of this protein.",No,No,Vague,No,No,not-Yes,GO:0016746,,,,,,,,,,,0,,0.2486,no
AKS2_ALSSC,A0A9E7LUL3,Reference,Eukaryota,450,"Acyltransferase involved in the biosynthesis of akuammilan monoterpene indole alkaloids (MIAs) natural products, components with various biological properties such as antidiabetic, antibacterial, anti-inflammatory, anticancer, and antimalarial activities. Catalyzes the conversion of rhazimol to akuammiline.","Acyltransferase involved in the biosynthesis of akuammilan monoterpene indole alkaloids (MIAs) natural products, components with various biological properties such as antidiabetic, antibacterial, anti-inflammatory, anticancer, and antimalarial activities. Catalyzes the conversion of rhazimol to akuammiline.",,,,,,,GO:0016746,GO:0016747,GO:0016747,GO:0016746,GO:0016746,GO:0016746,0.8416,0.8416,1.0,1.0,1.0,5,0.9366,0.2486,no
MTA1_CRYP1,A0A9P5CQV5,ESM2Text,Eukaryota,336,"N6-methyladenosine RNA methyltransferase that plays a crucial role in fungal phenotypic traits, virulence, and stress tolerance. Mediates the methylation of mRNAs to produce N6-methyladenosine (m6A)-containing mRNAs. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing. Mediates specifically acid phosphatase APHA mRNA stability through a YTHDF1-dependent m6A modification of the A1306, A1341, and A1666 key methylation modification sites. Also mediates the stability of the transcription factor ZAP1 mRNA via modification of residue A1935 localized in the 3'UTR.","A methylase, recognizes the double-stranded sequence 5'-CATNNNNNGGC-3', methylates C-1 on both strands, and protects the DNA from cleavage by the BslI endonuclease.",No,No,No,No,No,not-Yes,GO:0001734; GO:0003723,GO:0003886,GO:0009008,GO:0003886,GO:0009007,GO:0008168; GO:0003677,0.3955,0.3816,0.3955,0.3955,0.6132,5,0.4363,0.5352,no
MTA1_CRYP1,A0A9P5CQV5,Prot2Text,Eukaryota,336,"N6-methyladenosine RNA methyltransferase that plays a crucial role in fungal phenotypic traits, virulence, and stress tolerance. Mediates the methylation of mRNAs to produce N6-methyladenosine (m6A)-containing mRNAs. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing. Mediates specifically acid phosphatase APHA mRNA stability through a YTHDF1-dependent m6A modification of the A1306, A1341, and A1666 key methylation modification sites. Also mediates the stability of the transcription factor ZAP1 mRNA via modification of residue A1935 localized in the 3'UTR.","The METTL3-METTL14 heterodimer forms a N6-methyltransferase complex that methylates adenosine residues at the N(6) position of some mRNAs and regulates the circadian clock, differentiation of embryonic stem cells and cortical neurogenesis. In the heterodimer formed with mettl3, mettl14 constitutes the RNA-binding scaffold that recognizes the substrate rather than the catalytic core. N6-methyladenosine (m6A), which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs, plays a role in mRNA stability and processing.",Yes,Maybe,Yes,Maybe,Yes,Yes,GO:0001734; GO:0003723,GO:0003723,GO:0080009,GO:0080009,GO:0008173,GO:0080009,0.696,0.0,0.0,0.558,0.0,5,0.2508,0.5352,no
MTA1_CRYP1,A0A9P5CQV5,ProtT3,Eukaryota,336,"N6-methyladenosine RNA methyltransferase that plays a crucial role in fungal phenotypic traits, virulence, and stress tolerance. Mediates the methylation of mRNAs to produce N6-methyladenosine (m6A)-containing mRNAs. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing. Mediates specifically acid phosphatase APHA mRNA stability through a YTHDF1-dependent m6A modification of the A1306, A1341, and A1666 key methylation modification sites. Also mediates the stability of the transcription factor ZAP1 mRNA via modification of residue A1935 localized in the 3'UTR.",Putative DNA methyltransferase. Belongs to the class I-like SAM-binding methyltransferase superfamily,No,No,No,No,No,not-Yes,GO:0001734; GO:0003723,GO:0009008,GO:0009008,GO:0009008,GO:0009008; GO:0008757,GO:0009008,0.3816,0.3816,0.3816,0.4844,0.3816,5,0.4022,0.5352,no
MTA1_CRYP1,A0A9P5CQV5,ProtTale,Eukaryota,336,"N6-methyladenosine RNA methyltransferase that plays a crucial role in fungal phenotypic traits, virulence, and stress tolerance. Mediates the methylation of mRNAs to produce N6-methyladenosine (m6A)-containing mRNAs. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing. Mediates specifically acid phosphatase APHA mRNA stability through a YTHDF1-dependent m6A modification of the A1306, A1341, and A1666 key methylation modification sites. Also mediates the stability of the transcription factor ZAP1 mRNA via modification of residue A1935 localized in the 3'UTR.",DNA repair enzyme that has both methylcytosine and adenine demethylase activity. Demethylates DNA at a very high rate. Catalyzes the irreversible hydrolysis of methyl groups at the mC (cytosine) C5 position of methylated DNA. Hydrolyzes m5C and m5m5C residues in both double-stranded and single-stranded DNA. Has low activity on adenine.,No,No,No,No,No,not-Yes,GO:0001734; GO:0003723,GO:0016787,GO:0016787,GO:0003677; GO:0016787,GO:0016787,GO:0016787,0.2346,0.2346,0.4532,0.2346,0.2346,5,0.2783,0.5352,no
MTA1_CRYP1,A0A9P5CQV5,Protein2Text,Eukaryota,336,"N6-methyladenosine RNA methyltransferase that plays a crucial role in fungal phenotypic traits, virulence, and stress tolerance. Mediates the methylation of mRNAs to produce N6-methyladenosine (m6A)-containing mRNAs. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing. Mediates specifically acid phosphatase APHA mRNA stability through a YTHDF1-dependent m6A modification of the A1306, A1341, and A1666 key methylation modification sites. Also mediates the stability of the transcription factor ZAP1 mRNA via modification of residue A1935 localized in the 3'UTR.","This protein is an epitranscriptomic methyltransferase, which means it adds a methyl group to a specific location on a molecule. In this case, it is involved in the addition of a methyl group to a position on the RNA molecule. This type of modification is known as N6-methyladenosine (m6A) methylation. The protein is specifically involved in the methylation of adenosine residues in RNAs. This type of methylation is an important epigenetic mark that can affect RNA processing, stability, and translation. It is involved in various cellular processes, including regulation of gene expression, RNA splicing, and protein synthesis. The protein is also involved in the regulation of the cell cycle and is a potential target for cancer therapy.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0001734; GO:0003723,GO:0008168,GO:0008168,GO:0008168,GO:0080009,GO:0008168,0.4254,0.4254,0.4254,0.0,0.4254,5,0.3403,0.5352,no
MTA1_CRYP1,A0A9P5CQV5,Reference,Eukaryota,336,"N6-methyladenosine RNA methyltransferase that plays a crucial role in fungal phenotypic traits, virulence, and stress tolerance. Mediates the methylation of mRNAs to produce N6-methyladenosine (m6A)-containing mRNAs. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing. Mediates specifically acid phosphatase APHA mRNA stability through a YTHDF1-dependent m6A modification of the A1306, A1341, and A1666 key methylation modification sites. Also mediates the stability of the transcription factor ZAP1 mRNA via modification of residue A1935 localized in the 3'UTR.","N6-methyladenosine RNA methyltransferase that plays a crucial role in fungal phenotypic traits, virulence, and stress tolerance. Mediates the methylation of mRNAs to produce N6-methyladenosine (m6A)-containing mRNAs. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing. Mediates specifically acid phosphatase APHA mRNA stability through a YTHDF1-dependent m6A modification of the A1306, A1341, and A1666 key methylation modification sites. Also mediates the stability of the transcription factor ZAP1 mRNA via modification of residue A1935 localized in the 3'UTR.",,,,,,,GO:0001734; GO:0003723,GO:0008168; GO:0003723,GO:0080009,GO:0008168,GO:0016422,GO:0080009,0.7826,0.0,0.4254,0.5819,0.0,5,0.358,0.5352,no
APHA_CRYP1,A0A9P5CTI1,ESM2Text,Eukaryota,504,Acid phosphatase involved in the regulation of fungal phenotypic traits and virulence in C.parasitica.,Has a broad substrate specificity.,Vague,No,Vague,Maybe,Vague,not-Yes,GO:0003993; GO:0046872,,,,,,,,,,,0,,0.2021,no
APHA_CRYP1,A0A9P5CTI1,Prot2Text,Eukaryota,504,Acid phosphatase involved in the regulation of fungal phenotypic traits and virulence in C.parasitica.,"Hydrolyzes pyrophosphate, phosphodiester and phosphosulfate linkages of nucleotide-sugars, sulfonucleotides and nucleoside di and triphosphates. Highest activity observed with the substrates ADP-glucose and adenosine 5'-phosphosulfate.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0003993; GO:0046872,GO:0016462,GO:0017110,GO:0017110,GO:0016462,GO:0017110,0.2258,0.1944,0.1944,0.2258,0.1944,5,0.207,0.2021,no
APHA_CRYP1,A0A9P5CTI1,ProtT3,Eukaryota,504,Acid phosphatase involved in the regulation of fungal phenotypic traits and virulence in C.parasitica.,Secreted. Belongs to the metallophosphoesterase superfamily. Purple acid phosphatase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0003993; GO:0046872,GO:0003993,GO:0003993,GO:0003993,GO:0003993,GO:0003993,0.6924,0.6924,0.6924,0.6924,0.6924,5,0.6924,0.2021,no
APHA_CRYP1,A0A9P5CTI1,ProtTale,Eukaryota,504,Acid phosphatase involved in the regulation of fungal phenotypic traits and virulence in C.parasitica.,"Phosphatase that catalyzes the hydrolysis of phosphoanhydride bonds of a variety of phosphoanhydrides, including phosphoenolpyruvate (PEP), beta-glycerophosphate (beta-GP), adenosine 5'- phosphosulfate (APS), and inorganic pyrophosphate (PPi). Has no activity toward phosphoethanolamine (PE), phospho-L-serine (PS), phospho-L-aspartate (PA), phospho-L-threonine (PT), and phospho-L-histidine (PH). May be involved in regulating the intracellular levels of",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0003993; GO:0046872,GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,0.609,0.609,0.609,0.609,0.609,5,0.609,0.2021,no
APHA_CRYP1,A0A9P5CTI1,Protein2Text,Eukaryota,504,Acid phosphatase involved in the regulation of fungal phenotypic traits and virulence in C.parasitica.,"The molecular function of this protein is to hydrolyze phosphate diesters in nucleic acids, acting as a phosphodiesterase. Specifically, it is involved in the degradation of nucleic acids, breaking down nucleotide linkages in the phosphodiester backbone of DNA and RNA. It has a broad substrate specificity and can cleave a variety of nucleic acid substrates. It is also involved in the regulation of nucleic acid degradation and turnover in the cell.",Maybe,No,No,No,Maybe,not-Yes,GO:0003993; GO:0046872,GO:0004527,GO:0004527,GO:0004527,GO:0004527,GO:0004518,0.3239,0.3239,0.3239,0.3239,0.2104,5,0.3012,0.2021,no
APHA_CRYP1,A0A9P5CTI1,Reference,Eukaryota,504,Acid phosphatase involved in the regulation of fungal phenotypic traits and virulence in C.parasitica.,Acid phosphatase involved in the regulation of fungal phenotypic traits and virulence in C.parasitica.,,,,,,,GO:0003993; GO:0046872,GO:0003993,GO:0003993,GO:0003993,GO:0003993,GO:0003993,0.6924,0.6924,0.6924,0.6924,0.6924,5,0.6924,0.2021,no
SWE1_DREDA,A0AAD6IZ24,ESM2Text,Eukaryota,935,Protein kinase that acts as a negative regulator of entry into mitosis (G2 to M transition). Involved in trapping nematodes.,"Protein kinase that acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylating and regulating CDK1 at 'Ser-10' and 'Ser-28', thereby promoting the transition from G2 to M phase.",Yes,Yes,Yes,Maybe,Yes,Yes,GO:0005524; GO:0004713,GO:0004672; GO:0005524,GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.9556,0.5649,0.9101,0.9101,0.9101,5,0.8502,0.6336,yes
SWE1_DREDA,A0AAD6IZ24,Prot2Text,Eukaryota,935,Protein kinase that acts as a negative regulator of entry into mitosis (G2 to M transition). Involved in trapping nematodes.,"Serine/threonine-protein kinase involved in cell cycle regulation and transcription. Phosphorylates the transcription factor ETS2 (in vitro). Required for G1/S transition. Regulates cell proliferation, cell wall integrity, hyphal growth and the timing of stomatal opening. Involved in the regulation of microtubule polymerization through phosphorylation of the microtubule-associated protein MAPT/TAU.",Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0005524; GO:0004713,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.5649,0.5649,0.5649,0.5649,0.5649,5,0.5649,0.6336,yes
SWE1_DREDA,A0AAD6IZ24,ProtT3,Eukaryota,935,Protein kinase that acts as a negative regulator of entry into mitosis (G2 to M transition). Involved in trapping nematodes.,Serine/threonine-protein kinase involved in the control of the cell cycle at the G(2)/M (mitosis) transition. Phosphorylates the cyclin-dependent kinase cdc28 at 'Thr-162'. Nucleus. Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily,Yes,Maybe,Yes,Maybe,Yes,Yes,GO:0005524; GO:0004713,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674; GO:0005524,0.9101,0.9101,0.9101,0.9101,0.9101,5,0.9101,0.6336,yes
SWE1_DREDA,A0AAD6IZ24,ProtTale,Eukaryota,935,Protein kinase that acts as a negative regulator of entry into mitosis (G2 to M transition). Involved in trapping nematodes.,Essential for the control of the cell cycle. Phosphorylates the C-terminal domain of the Cdc2 protein.,Maybe,No,No,Maybe,Yes,not-Yes,GO:0005524; GO:0004713,GO:0004674,GO:0016301,GO:0004674,GO:0016301; GO:0005524,GO:0004672,0.5649,0.4577,0.5649,0.8274,0.6276,5,0.6085,0.6336,yes
SWE1_DREDA,A0AAD6IZ24,Protein2Text,Eukaryota,935,Protein kinase that acts as a negative regulator of entry into mitosis (G2 to M transition). Involved in trapping nematodes.,The molecular function of this protein is an ATP-dependent DNA helicase.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004713,GO:0004003; GO:0005524,GO:0004003; GO:0005524,GO:0004003; GO:0005524,GO:0004003; GO:0005524,GO:0004003,0.5768,0.5768,0.5768,0.5768,0.1208,5,0.4856,0.6336,yes
SWE1_DREDA,A0AAD6IZ24,Reference,Eukaryota,935,Protein kinase that acts as a negative regulator of entry into mitosis (G2 to M transition). Involved in trapping nematodes.,Protein kinase that acts as a negative regulator of entry into mitosis (G2 to M transition). Involved in trapping nematodes.,,,,,,,GO:0005524; GO:0004713,GO:0004674,GO:0004674,GO:0004672,GO:0004674; GO:0005524,GO:0004672,0.5649,0.5649,0.6276,0.9101,0.6276,5,0.659,0.6336,yes
CHIT2_DREDA,A0AAD6J456,ESM2Text,Eukaryota,773,"GPI-anchored chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Required to reshape the cell wall at the sites where cell wall remodeling and/or cell wall maturation actively take place such as sites of conidia formation. Involved in trapping nematodes.","GPI-anchored chitinase involved in cell separation. Required for the separation of the mother and daughter cells. Involved in the degradation of chitin, a component of the cell walls.",Yes,Yes,Yes,Maybe,Yes,Yes,GO:0008843,GO:0004568,GO:0004568,GO:0004568; GO:0016798,GO:0004568,GO:0004568,0.8691,0.8691,0.7949,0.8691,0.8691,5,0.8543,0.2372,no
CHIT2_DREDA,A0AAD6J456,Prot2Text,Eukaryota,773,"GPI-anchored chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Required to reshape the cell wall at the sites where cell wall remodeling and/or cell wall maturation actively take place such as sites of conidia formation. Involved in trapping nematodes.",Chitinase involved in the remodeling of chitin in the fungal cell wall. Plays a role in cell separation.,Yes,Maybe,Yes,Maybe,Yes,Yes,GO:0008843,GO:0004568,GO:0004568,GO:0004568,GO:0004568,GO:0004568,0.8691,0.8691,0.8691,0.8691,0.8691,5,0.8691,0.2372,no
CHIT2_DREDA,A0AAD6J456,ProtT3,Eukaryota,773,"GPI-anchored chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Required to reshape the cell wall at the sites where cell wall remodeling and/or cell wall maturation actively take place such as sites of conidia formation. Involved in trapping nematodes.","Chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Cell membrane; Lipid-anchor, GPI- anchor. Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008843,GO:0004568,GO:0004568,GO:0004568,GO:0004568,GO:0004568,0.8691,0.8691,0.8691,0.8691,0.8691,5,0.8691,0.2372,no
CHIT2_DREDA,A0AAD6J456,ProtTale,Eukaryota,773,"GPI-anchored chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Required to reshape the cell wall at the sites where cell wall remodeling and/or cell wall maturation actively take place such as sites of conidia formation. Involved in trapping nematodes.","GPI-anchored chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Required to reshape the cell wall at the sites where cell fusion occurs during mating.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008843,GO:0004568,GO:0004568,GO:0004568,GO:0004568,GO:0004568,0.8691,0.8691,0.8691,0.8691,0.8691,5,0.8691,0.2372,no
CHIT2_DREDA,A0AAD6J456,Protein2Text,Eukaryota,773,"GPI-anchored chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Required to reshape the cell wall at the sites where cell wall remodeling and/or cell wall maturation actively take place such as sites of conidia formation. Involved in trapping nematodes.","This protein is involved in molecular function related to the degradation of complex carbohydrates, specifically the hydrolysis of cellulose and other polysaccharides. It is likely a beta-glucosidase, an enzyme that breaks down cellulose into simpler sugars. This protein is also involved in cell wall remodeling, which is a process that helps plants to grow and develop. It is likely involved in the degradation of complex carbohydrates in the cell wall, allowing for the release of simple sugars that can be used by the plant for energy and growth. Additionally, it may play a role in plant defense against pathogens, by breaking down complex carbohydrates in the cell wall and making it difficult for pathogens to adhere to and infect the plant. 
Molecular function: 
Hydrolysis of cellulose and other complex polysaccharides. 
Breakdown of complex carbohydrates in the cell wall. 
Cell wall remodeling. 
Plant defense against pathogens. 
Beta-glucosidase activity. 
Hydrolysis of cellobiose and other beta-linked glucosides. 
Breakdown of complex carbohydrates in the cell wall. 
Hydrolysis of beta-1,4-glucan. 
Hydrolysis of beta-1,4-glucosidic bonds. 
Hydrolysis of beta-1,4-glycosidic bonds. 
Hydrolysis of beta-1,4-glucoside. 
Hydrolysis of beta-1,4-glycoside. 
Hydrolysis of beta-1,4-linkages. 
Hydrolysis of beta-1,4-glucosidic linkages. 
Hydrolysis of beta-1,4-glycosidic linkages. 
Hydrolysis of beta-1,4-glucoside linkages. 
Hydrolysis of beta-1,4-glycoside linkages. 
Hydrolysis of beta-1,4-glycosidic linkages. 
Hydrolysis of beta-1,4-glucosidic linkages. 
Hydrolysis of beta-1,4-glycosidic linkages. 
Hydrolysis of beta-1,4-glucosidic linkages. 
Hydrolysis of beta-1,4-glycosidic linkages. 
Hydrolysis of beta-1,4-glycosidic linkages. 
Hy",No,No,No,No,No,not-Yes,GO:0008843,GO:0008422,GO:0008422,GO:0008422,GO:0008422,GO:0008422,0.5445,0.5445,0.5445,0.5445,0.5445,5,0.5445,0.2372,no
CHIT2_DREDA,A0AAD6J456,Reference,Eukaryota,773,"GPI-anchored chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Required to reshape the cell wall at the sites where cell wall remodeling and/or cell wall maturation actively take place such as sites of conidia formation. Involved in trapping nematodes.","GPI-anchored chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Required to reshape the cell wall at the sites where cell wall remodeling and/or cell wall maturation actively take place such as sites of conidia formation. Involved in trapping nematodes.",,,,,,,GO:0008843,GO:0004568,GO:0004568,GO:0004568,GO:0004568,GO:0004568,0.8691,0.8691,0.8691,0.8691,0.8691,5,0.8691,0.2372,no
THIOL_DREDA,A0AAD6NF83,ESM2Text,Eukaryota,462,"Catalyzes the condensation of two acetyl-coA molecules into acetoacetyl-CoA. Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds. Involved in trapping nematodes.",Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016747; GO:0008289,GO:0003988,GO:0003988,GO:0003988,GO:0003988,GO:0003985,0.5496,0.5496,0.5496,0.5496,0.4133,5,0.5223,0.2272,no
THIOL_DREDA,A0AAD6NF83,Prot2Text,Eukaryota,462,"Catalyzes the condensation of two acetyl-coA molecules into acetoacetyl-CoA. Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds. Involved in trapping nematodes.","Mitochondrial trifunctional enzyme catalyzes the last three of the four reactions of the mitochondrial beta-oxidation pathway. The mitochondrial beta-oxidation pathway is the major energy-producing process in tissues and is performed through four consecutive reactions breaking down fatty acids into acetyl-CoA. Among the enzymes involved in this pathway, the trifunctional enzyme exhibits specificity for long-chain fatty acids. Mitochondrial trifunctional enzyme is a heterotetrameric complex composed of two proteins, the trifunctional enzyme subunit alpha/HADHA carries the 2,3-enoyl-CoA hydratase and the 3-hydroxyacyl-CoA dehydrogenase activities, while the trifunctional enzyme subunit beta/HADHB described here bears the 3-ketoacyl-CoA thiolase activity.",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0016747; GO:0008289,GO:0003988,GO:0003988,GO:0003988,GO:0003988,GO:0003988,0.5496,0.5496,0.5496,0.5496,0.5496,5,0.5496,0.2272,no
THIOL_DREDA,A0AAD6NF83,ProtT3,Eukaryota,462,"Catalyzes the condensation of two acetyl-coA molecules into acetoacetyl-CoA. Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds. Involved in trapping nematodes.","Catalyzes the first step of the peroxisomal beta-oxidation pathway, the reduction of 3-oxoacyl-CoAs to 3-oxoacyl-4-hydroxyacyl-CoAs (By similarity). The peroxisomal beta-oxidation pathway breaks down fatty acids into acetyl-CoA, which enters the tricarboxylic acid cycle (By similarity). Peroxisome membrane; Single-pass membrane protein. Belongs to the short-chain dehydrogenases/reductases (SDR) family",No,No,No,No,Maybe,not-Yes,GO:0016747; GO:0008289,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0003857,0.3588,0.3588,0.3588,0.3588,0.2095,5,0.3289,0.2272,no
THIOL_DREDA,A0AAD6NF83,ProtTale,Eukaryota,462,"Catalyzes the condensation of two acetyl-coA molecules into acetoacetyl-CoA. Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds. Involved in trapping nematodes.",Probably involved in the degradation of fatty acids via the beta-oxidation pathway.,Vague,No,Vague,No,Maybe,not-Yes,GO:0016747; GO:0008289,,,,,,,,,,,0,,0.2272,no
THIOL_DREDA,A0AAD6NF83,Protein2Text,Eukaryota,462,"Catalyzes the condensation of two acetyl-coA molecules into acetoacetyl-CoA. Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds. Involved in trapping nematodes.","This protein is involved in the molecular function of fatty acid binding. It is likely a fatty acid-binding protein, which plays a role in the transport and metabolism of fatty acids in the cell.",No,No,Vague,No,No,not-Yes,GO:0016747; GO:0008289,GO:0005504,GO:0005504,GO:0005504,GO:0005504,GO:0005504,0.3695,0.3695,0.3695,0.3695,0.3695,5,0.3695,0.2272,no
THIOL_DREDA,A0AAD6NF83,Reference,Eukaryota,462,"Catalyzes the condensation of two acetyl-coA molecules into acetoacetyl-CoA. Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds. Involved in trapping nematodes.","Catalyzes the condensation of two acetyl-coA molecules into acetoacetyl-CoA. Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds. Involved in trapping nematodes.",,,,,,,GO:0016747; GO:0008289,GO:0003985,GO:0003985,GO:0003985,GO:0003985,GO:0003985,0.4133,0.4133,0.4133,0.4133,0.4133,5,0.4133,0.2272,no
GCDH_DREDA,A0AAD6NFV5,ESM2Text,Eukaryota,385,"Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L- hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. Involved in trapping nematodes.","Oxidizes medium- and long-chain acyl-CoA substrates to 2-oxoacyl-CoA, the first step of fatty acid beta-oxidation. This enzymatic step leads to the desaturation of fatty acids to beta-hydroxyacyl-CoA, the respective formation of omega-2 long- and very long-chain fatty acids and CoA esters. Has a broad substrate specificity and catalyzes the desaturation of butyryl-CoA, crotonyl-CoA and butyrate to 3-hydroxybutyrate (HBA) and butyrate, respectively. Also acts on butyryl-CoA and butyryl-CoA but with a lower activity. Preferentially acts on butyrate.",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0000062; GO:0050660; GO:0004361,GO:0003995,GO:0003995,GO:0003995,GO:0003995,GO:0003995,0.4698,0.4698,0.4698,0.4698,0.4698,5,0.4698,0.2277,no
GCDH_DREDA,A0AAD6NFV5,Prot2Text,Eukaryota,385,"Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L- hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. Involved in trapping nematodes.",Catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. First enzyme of the fatty acid beta-oxidation pathway.,Maybe,No,Maybe,No,Maybe,not-Yes,GO:0000062; GO:0050660; GO:0004361,GO:0003995,GO:0003995,GO:0003995,GO:0003995,GO:0003995,0.4698,0.4698,0.4698,0.4698,0.4698,5,0.4698,0.2277,no
GCDH_DREDA,A0AAD6NFV5,ProtT3,Eukaryota,385,"Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L- hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. Involved in trapping nematodes.",Catalyzes the reduction of crotonobetainyl-CoA to gamma-butyrobetainyl-CoA. Mitochondrion. Belongs to the acyl-CoA dehydrogenase family,No,Vague,Maybe,No,Maybe,not-Yes,GO:0000062; GO:0050660; GO:0004361,GO:0003995,GO:0003995,GO:0003995,GO:0003995,GO:0003995,0.4698,0.4698,0.4698,0.4698,0.4698,5,0.4698,0.2277,no
GCDH_DREDA,A0AAD6NFV5,ProtTale,Eukaryota,385,"Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L- hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. Involved in trapping nematodes.","Involved in the degradation of short-chain fatty acids (SCFA) such as acetate, propionate and butyrate. Catalyzes the reversible conversion of 2-methylpropanoate (isobutanoate) to 4-methyl-2-oxopentanoate. Is also able to catalyze the reversible conversion of 2-methylbutanoate (isovalerate) to 4-methyl-2-oxopentanoate and 2-methylbutanoyl-CoA to 4-methyl-2-oxopentanoyl-CoA.",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0000062; GO:0050660; GO:0004361,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.3261,0.3261,0.3261,0.3261,0.3261,5,0.3261,0.2277,no
GCDH_DREDA,A0AAD6NFV5,Protein2Text,Eukaryota,385,"Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L- hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. Involved in trapping nematodes.","This protein is involved in the molecular function of catalyzing the decarboxylation of long-chain fatty acyl-CoA into the corresponding alkanes. Specifically, it catalyzes the conversion of acyl-CoA into alkanes.",No,No,No,No,Maybe,not-Yes,GO:0000062; GO:0050660; GO:0004361,,,,,,,,,,,0,,0.2277,no
GCDH_DREDA,A0AAD6NFV5,Reference,Eukaryota,385,"Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L- hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. Involved in trapping nematodes.","Catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L- hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. Involved in trapping nematodes.",,,,,,,GO:0000062; GO:0050660; GO:0004361,GO:0004361; GO:0050660,GO:0004361,GO:0004361,GO:0004361,GO:0004361,0.9171,0.5313,0.5313,0.5313,0.5313,5,0.6085,0.2277,no
CHIT1_DREDA,A0AAD6NIB7,ESM2Text,Eukaryota,949,"Chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Involved in trapping nematodes.","Synthesizes chitin, a polysaccharide of the cell wall, from chitin-containing microfibrils. May play a role in the initial events in the host defense (Probable).",No,No,No,No,No,not-Yes,GO:0008061; GO:0008843,GO:0004100,GO:0004100,GO:0004100,GO:0004100,GO:0004100,0.1263,0.1263,0.1263,0.1263,0.1263,5,0.1263,0.2432,no
CHIT1_DREDA,A0AAD6NIB7,Prot2Text,Eukaryota,949,"Chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Involved in trapping nematodes.","Lectin that binds chitooligosaccharides and other glycans with high affinity, but not heparin. Has no chitinase activity.",No,No,No,No,No,not-Yes,GO:0008061; GO:0008843,GO:0030246,GO:0030246,GO:0030246,GO:0030246,GO:0008061,0.3675,0.3675,0.3675,0.3675,0.704,5,0.4348,0.2432,no
CHIT1_DREDA,A0AAD6NIB7,ProtT3,Eukaryota,949,"Chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Involved in trapping nematodes.",Secreted. Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008061; GO:0008843,GO:0004568,GO:0004568,GO:0004568,GO:0004568,GO:0004568,0.6216,0.6216,0.6216,0.6216,0.6216,5,0.6216,0.2432,no
CHIT1_DREDA,A0AAD6NIB7,ProtTale,Eukaryota,949,"Chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Involved in trapping nematodes.","Secreted chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Participates in the infection process and plays a role in cell separation.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008061; GO:0008843,GO:0004568,GO:0004568,GO:0004568,GO:0004568,GO:0004568,0.6216,0.6216,0.6216,0.6216,0.6216,5,0.6216,0.2432,no
CHIT1_DREDA,A0AAD6NIB7,Protein2Text,Eukaryota,949,"Chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Involved in trapping nematodes.","This protein is involved in breaking down complex molecules, specifically carbohydrate polymers, into simpler sugars. It has a molecular function of catalyzing the hydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, lichenin and other cellulosic biomass. This process is crucial for the degradation of plant biomass and the release of simple sugars that can be utilized by the organism for energy and growth.",No,No,No,No,No,not-Yes,GO:0008061; GO:0008843,GO:0008810; GO:0030248,GO:0016162,GO:0016162; GO:0030245,GO:0030245; GO:0008810,GO:0008810,0.481,0.4645,0.3484,0.3484,0.4645,5,0.4214,0.2432,no
CHIT1_DREDA,A0AAD6NIB7,Reference,Eukaryota,949,"Chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Involved in trapping nematodes.","Chitinase involved in the degradation of chitin, a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods). Involved in trapping nematodes.",,,,,,,GO:0008061; GO:0008843,GO:0004568,GO:0004568,GO:0004568,GO:0004568,GO:0004568,0.6216,0.6216,0.6216,0.6216,0.6216,5,0.6216,0.2432,no
MANC_DREDA,A0AAD6NMH5,ESM2Text,Eukaryota,400,"Probable endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Involved in trapping nematodes.","Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016985,GO:0016985,GO:0016985,GO:0016985,GO:0016985,GO:0016985,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2788,no
MANC_DREDA,A0AAD6NMH5,Prot2Text,Eukaryota,400,"Probable endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Involved in trapping nematodes.","Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016985,GO:0016985,GO:0016985,GO:0016985,GO:0016985,GO:0016985,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2788,no
MANC_DREDA,A0AAD6NMH5,ProtT3,Eukaryota,400,"Probable endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Involved in trapping nematodes.","Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Secreted. Belongs to the glycosyl hydrolase 5 (cellulase A) family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016985,GO:0008810,GO:0008810,GO:0008810,GO:0016798,GO:0008810,0.5618,0.5618,0.5618,0.585,0.5618,5,0.5664,0.2788,no
MANC_DREDA,A0AAD6NMH5,ProtTale,Eukaryota,400,"Probable endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Involved in trapping nematodes.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.",No,No,No,Maybe,No,not-Yes,GO:0016985,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,0.4774,0.4774,0.4774,0.4774,0.4774,5,0.4774,0.2788,no
MANC_DREDA,A0AAD6NMH5,Protein2Text,Eukaryota,400,"Probable endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Involved in trapping nematodes.","This protein is a xylanase, which means it is involved in the hydrolysis of xylan, a complex polysaccharide found in plant cell walls. More specifically, it is a type of endoglucanase, which breaks down the internal bonds of cellulose, a key component of plant cell walls. 

In more detail, the molecular function of this protein is to catalyze the hydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, a process that is essential for the degradation of plant biomass. This enzyme is likely involved in the breakdown of cellulose in the plant cell wall, allowing the plant to recycle its own biomass and release nutrients for growth and development.

The molecular function of this protein can be summarized as:

* Catalytic activity: hydrolysis of 1,4-beta-D-glucosidic linkages in cellulose
* Binding: binding to cellulose, allowing the enzyme to recognize and act on its substrate
* Catalytic domain: the catalytic domain of the enzyme is responsible for the actual hydrolysis of the cellulose bonds.

It is worth noting that this protein is likely involved in a larger process of plant cell wall degradation, and its function may be influenced by other enzymes and factors that are present in the same cellular environment.",No,No,No,No,No,not-Yes,GO:0016985,GO:0008810; GO:0030248,GO:0016162,GO:0016162; GO:0030245,GO:0030245; GO:0008810,GO:0008810,0.402,0.5618,0.3745,0.3745,0.5618,5,0.4549,0.2788,no
MANC_DREDA,A0AAD6NMH5,Reference,Eukaryota,400,"Probable endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Involved in trapping nematodes.","Probable endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Involved in trapping nematodes.",,,,,,,GO:0016985,GO:0016985,GO:0016985,GO:0016985,GO:0016985,GO:0016985,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2788,no
VRB11_XANAC,A0AAI7ZGA5,ESM2Text,Bacteria,346,"Component of the VirB/VirD4 type IV secretion system (T4SS) that translocates effector proteins into adjacent bacterial cells, leading to target cell death and thus providing a competitive growth advantage for Xanthomonas in mixed bacterial communities (Probable). The VirB11 subunit probably provides energy for T4SS assembly and/or function.",The VirB system could be required for the establishment of the replication niche in the host.,Vague,No,Vague,No,Maybe,not-Yes,GO:0005524; GO:0016887,,,,,,,,,,,0,,0.3676,no
VRB11_XANAC,A0AAI7ZGA5,Prot2Text,Bacteria,346,"Component of the VirB/VirD4 type IV secretion system (T4SS) that translocates effector proteins into adjacent bacterial cells, leading to target cell death and thus providing a competitive growth advantage for Xanthomonas in mixed bacterial communities (Probable). The VirB11 subunit probably provides energy for T4SS assembly and/or function.","Probable component of a type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers. PilV and PilW may act in different pathways.",No,No,No,No,Maybe,not-Yes,GO:0005524; GO:0016887,,,,,,,,,,,0,,0.3676,no
VRB11_XANAC,A0AAI7ZGA5,ProtT3,Bacteria,346,"Component of the VirB/VirD4 type IV secretion system (T4SS) that translocates effector proteins into adjacent bacterial cells, leading to target cell death and thus providing a competitive growth advantage for Xanthomonas in mixed bacterial communities (Probable). The VirB11 subunit probably provides energy for T4SS assembly and/or function.",Cytoplasm. Belongs to the GSP E family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0016887,,,,,,,,,,,0,,0.3676,no
VRB11_XANAC,A0AAI7ZGA5,ProtTale,Bacteria,346,"Component of the VirB/VirD4 type IV secretion system (T4SS) that translocates effector proteins into adjacent bacterial cells, leading to target cell death and thus providing a competitive growth advantage for Xanthomonas in mixed bacterial communities (Probable). The VirB11 subunit probably provides energy for T4SS assembly and/or function.","Component of the VirB/VirD4 type IV secretion system (T4SS), which translocates transfer DNA (T-DNA) and virulence effector proteins into plant host cells, leading to crown gall disease. The VirB11 subunit is essential for virulence. It provides energy for pilus biogenesis and substrate transfer. It binds and hydrolyzes ATP. Also functions together with VirB4 to promote complex formation between T-pilus and substrate-binding protein VirB2.",Yes,Yes,Yes,Maybe,Yes,Yes,GO:0005524; GO:0016887,GO:0016887,GO:0005524; GO:0016887,GO:0005524; GO:0016887,GO:0005524; GO:0016887,GO:0016887,0.6869,1.0,1.0,1.0,0.6869,5,0.8748,0.3676,no
VRB11_XANAC,A0AAI7ZGA5,Protein2Text,Bacteria,346,"Component of the VirB/VirD4 type IV secretion system (T4SS) that translocates effector proteins into adjacent bacterial cells, leading to target cell death and thus providing a competitive growth advantage for Xanthomonas in mixed bacterial communities (Probable). The VirB11 subunit probably provides energy for T4SS assembly and/or function.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its name, it is likely involved in DNA recombination and repair, specifically in the excision of damaged DNA. 

In molecular biology, the term'recA' is often associated with a protein that plays a crucial role in DNA recombination and repair. The RecA protein is a central component of the bacterial SOS response, a system that helps cells survive DNA damage. When DNA damage is detected, the RecA protein binds to single-stranded DNA and promotes the homologous pairing of damaged DNA with undamaged DNA, facilitating the repair process.

Given this context, it is reasonable to infer that this protein is involved in DNA recombination and repair, likely as a RecA-like protein. However, without more specific information, this remains a hypothesis.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016887,,GO:0003697; GO:0005524,GO:0003677; GO:0005524,GO:0003697; GO:0005524,GO:0003677,,0.5621,0.5724,0.5621,0.1517,4,0.4621,0.3676,no
VRB11_XANAC,A0AAI7ZGA5,Reference,Bacteria,346,"Component of the VirB/VirD4 type IV secretion system (T4SS) that translocates effector proteins into adjacent bacterial cells, leading to target cell death and thus providing a competitive growth advantage for Xanthomonas in mixed bacterial communities (Probable). The VirB11 subunit probably provides energy for T4SS assembly and/or function.","Component of the VirB/VirD4 type IV secretion system (T4SS) that translocates effector proteins into adjacent bacterial cells, leading to target cell death and thus providing a competitive growth advantage for Xanthomonas in mixed bacterial communities (Probable). The VirB11 subunit probably provides energy for T4SS assembly and/or function.",,,,,,,GO:0005524; GO:0016887,GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887,0.6869,1.0,1.0,1.0,0.6869,5,0.8748,0.3676,no
BFPK_FRATN,A0Q7V6,ESM2Text,Bacteria,345,"Member of the two-component regulatory system BfpR/BfpK, which modulates biofilm production and antimicrobial peptide (AMP) resistance. Probably autophosphorylates, and then transfers the phosphate group to BfpR.","Member of the two-component regulatory system RprA/RprB involved in the regulation of adhesion, phagocytosis and aggregation of bacteria. Functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to the conserved aspartic acid residue in the regulatory domain of RprB. In turn, RprB binds to the upstream promoter regions of target genes including itself to positively regulate their expression.",Maybe,Maybe,Yes,Maybe,Yes,not-Yes,GO:0000155,GO:0000155,GO:0000155,GO:0000155; GO:0005524,GO:0000155; GO:0005524,GO:0000155; GO:0005524,1.0,1.0,0.6842,0.6842,0.6842,5,0.8105,0.5811,yes
BFPK_FRATN,A0Q7V6,Prot2Text,Bacteria,345,"Member of the two-component regulatory system BfpR/BfpK, which modulates biofilm production and antimicrobial peptide (AMP) resistance. Probably autophosphorylates, and then transfers the phosphate group to BfpR.",Member of the two-component regulatory system YdfH/YdfI. May activate YdfI by phosphorylation.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0000155,GO:0000155,GO:0004673,GO:0000155,GO:0004673,GO:0004673,1.0,0.8316,1.0,0.8316,0.8316,5,0.899,0.5811,yes
BFPK_FRATN,A0Q7V6,ProtT3,Bacteria,345,"Member of the two-component regulatory system BfpR/BfpK, which modulates biofilm production and antimicrobial peptide (AMP) resistance. Probably autophosphorylates, and then transfers the phosphate group to BfpR.",Member of the two-component regulatory system MprB/MprA involved in resistance against cationic antimicrobial peptides (CAMPs). MprB functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to MprA (By similarity). Cell membrane; Multi-pass membrane protein,Maybe,Maybe,Yes,Maybe,Yes,not-Yes,GO:0000155,GO:0000155; GO:0005524,GO:0000155; GO:0005524,GO:0000155,GO:0000155; GO:0005524,GO:0000155; GO:0005524,0.6842,0.6842,1.0,0.6842,0.6842,5,0.7474,0.5811,yes
BFPK_FRATN,A0Q7V6,ProtTale,Bacteria,345,"Member of the two-component regulatory system BfpR/BfpK, which modulates biofilm production and antimicrobial peptide (AMP) resistance. Probably autophosphorylates, and then transfers the phosphate group to BfpR.",Member of the two-component regulatory system MprB/MprA involved in the regulation of multidrug resistance. May act as a membrane-associated protein kinase that phosphorylates MprA in response to environmental signals.,Maybe,Maybe,Yes,Maybe,Yes,not-Yes,GO:0000155,GO:0000155,GO:0016301,GO:0000155,GO:0016301,GO:0000155,1.0,0.5077,1.0,0.5077,1.0,5,0.8031,0.5811,yes
BFPK_FRATN,A0Q7V6,Protein2Text,Bacteria,345,"Member of the two-component regulatory system BfpR/BfpK, which modulates biofilm production and antimicrobial peptide (AMP) resistance. Probably autophosphorylates, and then transfers the phosphate group to BfpR.","The molecular function of this protein is a sensor protein for the plant quorum-sensing system. It is a histidine kinase that is involved in sensing and responding to changes in the concentration of the plant quorum-sensing molecule, which helps the bacteria coordinate their behavior in response to the presence of other bacteria. Specifically, it acts as a sensor for the plant quorum-sensing molecule, and in response to changes in its concentration, it undergoes autophosphorylation, followed by the transfer of its phosphate group to a response regulator protein, which then triggers a variety of responses.",Maybe,No,Maybe,Maybe,Yes,not-Yes,GO:0000155,GO:0000155,GO:0000155,GO:0000155,GO:0000155,GO:0000155,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5811,yes
BFPK_FRATN,A0Q7V6,Reference,Bacteria,345,"Member of the two-component regulatory system BfpR/BfpK, which modulates biofilm production and antimicrobial peptide (AMP) resistance. Probably autophosphorylates, and then transfers the phosphate group to BfpR.","Member of the two-component regulatory system BfpR/BfpK, which modulates biofilm production and antimicrobial peptide (AMP) resistance. Probably autophosphorylates, and then transfers the phosphate group to BfpR.",,,,,,,GO:0000155,GO:0000155,GO:0000155,GO:0000155,GO:0000155; GO:0005524,GO:0000155,1.0,1.0,1.0,0.6842,1.0,5,0.9368,0.5811,yes
PMT_MYCS2,A0R3E8,ESM2Text,Bacteria,516,Protein O-mannosyltransferase that catalyzes the transfer of a single mannose residue from a polyprenol phospho-mannosyl lipidic donor to the hydroxyl group of selected serine and threonine residues in acceptor proteins.,Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0000030,GO:0004169,GO:0004169,GO:0016757,GO:0000030,GO:0004169,0.8001,0.8001,0.729,1.0,0.8001,5,0.8259,0.5478,yes
PMT_MYCS2,A0R3E8,Prot2Text,Bacteria,516,Protein O-mannosyltransferase that catalyzes the transfer of a single mannose residue from a polyprenol phospho-mannosyl lipidic donor to the hydroxyl group of selected serine and threonine residues in acceptor proteins.,Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0000030,GO:0004169,GO:0004169,GO:0004169,GO:0004169,GO:0004169,0.8001,0.8001,0.8001,0.8001,0.8001,5,0.8001,0.5478,yes
PMT_MYCS2,A0R3E8,ProtT3,Bacteria,516,Protein O-mannosyltransferase that catalyzes the transfer of a single mannose residue from a polyprenol phospho-mannosyl lipidic donor to the hydroxyl group of selected serine and threonine residues in acceptor proteins.,Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. Cell membrane; Multi-pass membrane protein. Belongs to the glycosyltransferase 29 family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0000030,GO:0004169,GO:0004169,GO:0004169,GO:0004169,GO:0004169,0.8001,0.8001,0.8001,0.8001,0.8001,5,0.8001,0.5478,yes
PMT_MYCS2,A0R3E8,ProtTale,Bacteria,516,Protein O-mannosyltransferase that catalyzes the transfer of a single mannose residue from a polyprenol phospho-mannosyl lipidic donor to the hydroxyl group of selected serine and threonine residues in acceptor proteins.,Responsible for the addition of alpha-(1->6)-mannose residues to the outer membrane lipopolysaccharide.,No,No,No,No,Maybe,not-Yes,GO:0000030,GO:0000030,GO:0016758,GO:0000030,GO:0000030,GO:0000030,1.0,0.8582,1.0,1.0,1.0,5,0.9716,0.5478,yes
PMT_MYCS2,A0R3E8,Protein2Text,Bacteria,516,Protein O-mannosyltransferase that catalyzes the transfer of a single mannose residue from a polyprenol phospho-mannosyl lipidic donor to the hydroxyl group of selected serine and threonine residues in acceptor proteins.,"The molecular function of this protein is an acyltransferase involved in the transfer of acyl groups from one molecule to another. Specifically, it catalyzes the transfer of acyl groups from a donor molecule to a specific acceptor molecule, playing a crucial role in various biological processes. In the case of the protein in question, it is involved in the transfer of acyl groups to the lipid molecules, which is essential for the proper functioning of cell membranes.",No,No,No,No,No,not-Yes,GO:0000030,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.482,0.482,0.482,0.482,0.482,5,0.482,0.5478,yes
PMT_MYCS2,A0R3E8,Reference,Bacteria,516,Protein O-mannosyltransferase that catalyzes the transfer of a single mannose residue from a polyprenol phospho-mannosyl lipidic donor to the hydroxyl group of selected serine and threonine residues in acceptor proteins.,Protein O-mannosyltransferase that catalyzes the transfer of a single mannose residue from a polyprenol phospho-mannosyl lipidic donor to the hydroxyl group of selected serine and threonine residues in acceptor proteins.,,,,,,,GO:0000030,GO:0004169,GO:0004169,GO:0000030,GO:0004169,GO:0004169,0.8001,0.8001,1.0,0.8001,0.8001,5,0.8401,0.5478,yes
GYS_TRIV3,A2E926,ESM2Text,Eukaryota,1572,"Participates in glycogen biosynthetic process; synthesizes alpha-1,4-glucan chains using UDP- or ADP-glucose. Can transfer glucose to short oligosaccharides: maltose, maltotriose, maltotetraose and maltoheptaose.","High activity for alpha-1,4-glucan.",Vague,No,Vague,Maybe,Maybe,not-Yes,GO:0016757,,,GO:0004553,,,,,0.3284,,,1,0.3284,0.3148,no
GYS_TRIV3,A2E926,Prot2Text,Eukaryota,1572,"Participates in glycogen biosynthetic process; synthesizes alpha-1,4-glucan chains using UDP- or ADP-glucose. Can transfer glucose to short oligosaccharides: maltose, maltotriose, maltotetraose and maltoheptaose.","High activity for alpha-1,4-glucan.",Vague,No,Vague,Maybe,Maybe,not-Yes,GO:0016757,,,,,,,,,,,0,,0.3148,no
GYS_TRIV3,A2E926,ProtT3,Eukaryota,1572,"Participates in glycogen biosynthetic process; synthesizes alpha-1,4-glucan chains using UDP- or ADP-glucose. Can transfer glucose to short oligosaccharides: maltose, maltotriose, maltotetraose and maltoheptaose.",Belongs to the baculoviridae polyhedrin protein family,No,Vague,Vague,Vague,Vague,not-Yes,GO:0016757,,,,GO:0005198,,,,,0.2761,,1,0.2761,0.3148,no
GYS_TRIV3,A2E926,ProtTale,Eukaryota,1572,"Participates in glycogen biosynthetic process; synthesizes alpha-1,4-glucan chains using UDP- or ADP-glucose. Can transfer glucose to short oligosaccharides: maltose, maltotriose, maltotetraose and maltoheptaose.","Catalyzes the second of two reactions, which are the formation of N-acetylglucosamine-1-phosphate from glucosamine-6-phosphate (GlcN-6-P) in the UDP-N-acetyl-alpha-D- glucosamine pathway. In the first reaction, GlcN-6-P is converted into UDP-N- acetyl-alpha-D-glucosamine-1-phosphate, and in the second one UDP-N-acetyl-alpha-D-glucosamine-1-phosphate is converted into UDP-N-acetyl-alpha-D-glucosamine by direct dehydratase activity.",No,No,No,No,No,not-Yes,GO:0016757,GO:0016836,GO:0016740,GO:0016740,GO:0016853,,0.3284,0.8145,0.8145,0.4807,,4,0.6095,0.3148,no
GYS_TRIV3,A2E926,Protein2Text,Eukaryota,1572,"Participates in glycogen biosynthetic process; synthesizes alpha-1,4-glucan chains using UDP- or ADP-glucose. Can transfer glucose to short oligosaccharides: maltose, maltotriose, maltotetraose and maltoheptaose.",This protein is involved in the molecular function of mRNA capping.,No,No,No,No,No,not-Yes,GO:0016757,GO:0004484,GO:0004484,GO:0004484,GO:0004484,,0.3537,0.3537,0.3537,0.3537,,4,0.3537,0.3148,no
GYS_TRIV3,A2E926,Reference,Eukaryota,1572,"Participates in glycogen biosynthetic process; synthesizes alpha-1,4-glucan chains using UDP- or ADP-glucose. Can transfer glucose to short oligosaccharides: maltose, maltotriose, maltotetraose and maltoheptaose.","Participates in glycogen biosynthetic process; synthesizes alpha-1,4-glucan chains using UDP- or ADP-glucose. Can transfer glucose to short oligosaccharides: maltose, maltotriose, maltotetraose and maltoheptaose.",,,,,,,GO:0016757,GO:0004373; GO:0009011,GO:0004373,GO:0004373,GO:0004373,GO:0004373,0.558,0.504,0.504,0.504,0.504,5,0.5148,0.3148,no
GDE_TRIV3,A2F4M9,ESM2Text,Eukaryota,1469,"Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4- alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase in glycogen degradation. Exhibits debranching activity towards phosphorylase limit dextrin.","Important for the degradation of small bioactive oligosaccharides (breakdown products of glycoproteins) into long-lived, soluble oligosaccharides.",Maybe,No,No,No,Maybe,not-Yes,GO:0004134; GO:0004135,,,GO:0016798,,,,,0.4848,,,1,0.4848,0.2595,no
GDE_TRIV3,A2F4M9,Prot2Text,Eukaryota,1469,"Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4- alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase in glycogen degradation. Exhibits debranching activity towards phosphorylase limit dextrin.","Important for the degradation of small bioactive oligosaccharides (breakdown products of glycoproteins) into long-lived, soluble oligosaccharides.",Maybe,No,No,No,Maybe,not-Yes,GO:0004134; GO:0004135,,,,,,,,,,,0,,0.2595,no
GDE_TRIV3,A2F4M9,ProtT3,Eukaryota,1469,"Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4- alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase in glycogen degradation. Exhibits debranching activity towards phosphorylase limit dextrin.",Cytoplasm. Belongs to the glycosyl hydrolase 13 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004134; GO:0004135,GO:0016798,GO:0016798,GO:0016798,GO:0016798,GO:0016798,0.4848,0.4848,0.4848,0.4848,0.4848,5,0.4848,0.2595,no
GDE_TRIV3,A2F4M9,ProtTale,Eukaryota,1469,"Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4- alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase in glycogen degradation. Exhibits debranching activity towards phosphorylase limit dextrin.","D-maltase involved in the degradation of maltodextrins. Catalyzes the reversible hydrolysis of (1->4)-alpha-D-glucosidic bonds in alpha-D- and alpha-L-maltose, alpha-D- and alpha-D-malto-oligomers, and alpha-D- and alpha-D-malto-tetramers. Is also able to hydrolyze alpha-D- and alpha-D-malto-oligomers with a degree of polymerization (DP) higher than 4.",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0004134; GO:0004135,GO:0004558,GO:0004553,GO:0004558,GO:0004553,GO:0004553,0.5578,0.5289,0.5578,0.5289,0.5289,5,0.5405,0.2595,no
GDE_TRIV3,A2F4M9,Protein2Text,Eukaryota,1469,"Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4- alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase in glycogen degradation. Exhibits debranching activity towards phosphorylase limit dextrin.",The molecular function of this protein is a carbohydrate-binding module.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004134; GO:0004135,GO:0030246,GO:0030246,GO:0030246,GO:0030246,GO:0030246,0.1482,0.1482,0.1482,0.1482,0.1482,5,0.1482,0.2595,no
GDE_TRIV3,A2F4M9,Reference,Eukaryota,1469,"Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4- alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase in glycogen degradation. Exhibits debranching activity towards phosphorylase limit dextrin.","Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4- alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase in glycogen degradation. Exhibits debranching activity towards phosphorylase limit dextrin.",,,,,,,GO:0004134; GO:0004135,GO:0004135; GO:0004133,GO:0004134; GO:0004135,GO:0004133,GO:0004133; GO:0004134,GO:0004133,0.718,1.0,0.0,0.718,0.0,5,0.4872,0.2595,no
EGT2A_ASPFU,A4D9B0,ESM2Text,Eukaryota,453,"Protein involved in the biosynthesis of ergothioneine (ERG), an unusual thio-histidine betaine amino acid that acts as an antioxidant against peroxide in conidia and contributes to conidial longevity. Catalyzes the conversion of hercynylcysteine sulfoxide to ergothioneine (EGT) by cleaving the cysteine residue at the sulfur atom, the last step in the biosynthesis pathway of ergothioneine. Surprisingly, egtA is sufficient for biosynthesis of ERG when heterologously expressed in Saccharomyces cerevisiae and coeExpression of egtA with the egt2A decreases the level of EGT production.",Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine.,Maybe,No,No,No,No,not-Yes,GO:1990411; GO:0008483,GO:0031071,GO:0031071,GO:0031071,GO:0031071; GO:0030170,GO:0031071,0.3442,0.3442,0.3442,0.2783,0.3442,5,0.331,0.3564,no
EGT2A_ASPFU,A4D9B0,Prot2Text,Eukaryota,453,"Protein involved in the biosynthesis of ergothioneine (ERG), an unusual thio-histidine betaine amino acid that acts as an antioxidant against peroxide in conidia and contributes to conidial longevity. Catalyzes the conversion of hercynylcysteine sulfoxide to ergothioneine (EGT) by cleaving the cysteine residue at the sulfur atom, the last step in the biosynthesis pathway of ergothioneine. Surprisingly, egtA is sufficient for biosynthesis of ERG when heterologously expressed in Saccharomyces cerevisiae and coeExpression of egtA with the egt2A decreases the level of EGT production.","Homocysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo.",Maybe,No,No,Maybe,No,not-Yes,GO:1990411; GO:0008483,GO:0031071,GO:0031071,GO:0031071,GO:0031071,GO:0031071,0.3442,0.3442,0.3442,0.3442,0.3442,5,0.3442,0.3564,no
EGT2A_ASPFU,A4D9B0,ProtT3,Eukaryota,453,"Protein involved in the biosynthesis of ergothioneine (ERG), an unusual thio-histidine betaine amino acid that acts as an antioxidant against peroxide in conidia and contributes to conidial longevity. Catalyzes the conversion of hercynylcysteine sulfoxide to ergothioneine (EGT) by cleaving the cysteine residue at the sulfur atom, the last step in the biosynthesis pathway of ergothioneine. Surprisingly, egtA is sufficient for biosynthesis of ERG when heterologously expressed in Saccharomyces cerevisiae and coeExpression of egtA with the egt2A decreases the level of EGT production.",Catalyzes the conversion of homocysteine to cysteine. Cytoplasm. Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family,No,No,No,No,No,not-Yes,GO:1990411; GO:0008483,GO:0004123,GO:0003824; GO:0030170,GO:0004123,GO:0030170,GO:0004123,0.5597,0.4156,0.5597,0.0807,0.5597,5,0.4351,0.3564,no
EGT2A_ASPFU,A4D9B0,ProtTale,Eukaryota,453,"Protein involved in the biosynthesis of ergothioneine (ERG), an unusual thio-histidine betaine amino acid that acts as an antioxidant against peroxide in conidia and contributes to conidial longevity. Catalyzes the conversion of hercynylcysteine sulfoxide to ergothioneine (EGT) by cleaving the cysteine residue at the sulfur atom, the last step in the biosynthesis pathway of ergothioneine. Surprisingly, egtA is sufficient for biosynthesis of ERG when heterologously expressed in Saccharomyces cerevisiae and coeExpression of egtA with the egt2A decreases the level of EGT production.","L-cysteine desulfhydrase-like protein; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3- hydroxyleucine (HyLeu), alpha-aminoisobutyric",Maybe,No,Maybe,No,No,not-Yes,GO:1990411; GO:0008483,GO:0016829,,,GO:0016829,,0.5955,,,0.5955,,2,0.5955,0.3564,no
EGT2A_ASPFU,A4D9B0,Protein2Text,Eukaryota,453,"Protein involved in the biosynthesis of ergothioneine (ERG), an unusual thio-histidine betaine amino acid that acts as an antioxidant against peroxide in conidia and contributes to conidial longevity. Catalyzes the conversion of hercynylcysteine sulfoxide to ergothioneine (EGT) by cleaving the cysteine residue at the sulfur atom, the last step in the biosynthesis pathway of ergothioneine. Surprisingly, egtA is sufficient for biosynthesis of ERG when heterologously expressed in Saccharomyces cerevisiae and coeExpression of egtA with the egt2A decreases the level of EGT production.","The molecular function of this protein is a beta-eliminase, which is a type of enzyme that catalyzes the removal of a beta-hydroxy acid from a molecule, resulting in the formation of an aldehyde and an alkene. Specifically, it catalyzes the conversion of 3-hydroxyisobutyryl-CoA to methylmalonyl-CoA.",No,No,No,No,No,not-Yes,GO:1990411; GO:0008483,,,GO:0016829,,,,,0.5955,,,1,0.5955,0.3564,no
EGT2A_ASPFU,A4D9B0,Reference,Eukaryota,453,"Protein involved in the biosynthesis of ergothioneine (ERG), an unusual thio-histidine betaine amino acid that acts as an antioxidant against peroxide in conidia and contributes to conidial longevity. Catalyzes the conversion of hercynylcysteine sulfoxide to ergothioneine (EGT) by cleaving the cysteine residue at the sulfur atom, the last step in the biosynthesis pathway of ergothioneine. Surprisingly, egtA is sufficient for biosynthesis of ERG when heterologously expressed in Saccharomyces cerevisiae and coeExpression of egtA with the egt2A decreases the level of EGT production.","Protein involved in the biosynthesis of ergothioneine (ERG), an unusual thio-histidine betaine amino acid that acts as an antioxidant against peroxide in conidia and contributes to conidial longevity. Catalyzes the conversion of hercynylcysteine sulfoxide to ergothioneine (EGT) by cleaving the cysteine residue at the sulfur atom, the last step in the biosynthesis pathway of ergothioneine. Surprisingly, egtA is sufficient for biosynthesis of ERG when heterologously expressed in Saccharomyces cerevisiae and coeExpression of egtA with the egt2A decreases the level of EGT production.",,,,,,,GO:1990411; GO:0008483,GO:0016829,GO:0016846,GO:0016846,GO:0016829,GO:0016829,0.5955,0.6706,0.6706,0.5955,0.5955,5,0.6255,0.3564,no
HODMB_ECTM1,A4XXY8,ESM2Text,Bacteria,309,"Component of the heme-dependent oxidative N-demethylase (HODM) enzyme, that catalyzes the NADPH-dependent oxidation of dimethylamine (DMA) to methylamine (MA) and formaldehyde. Functions in bacterial methylated amine catabolism, linking alkylamine oxidation to the tetrahydrofolate C1 pool. The beta subunit of HODM binds FMN and a 2Fe-2S cluster, and likely reduces the ferric heme iron of the alpha subunit to ferrous using NADPH.",Involved in the degradation of para-nitrophenol (PNP). Catalyzes the reduction of FPP to PNP and the inactivation of nitrobenzene by a one-electron transfer mechanism. It can also use a wide range of substituted substrates.,Maybe,No,No,No,No,not-Yes,GO:0051537; GO:0046872; GO:0016491,,,,,,,,,,,0,,0.2158,no
HODMB_ECTM1,A4XXY8,Prot2Text,Bacteria,309,"Component of the heme-dependent oxidative N-demethylase (HODM) enzyme, that catalyzes the NADPH-dependent oxidation of dimethylamine (DMA) to methylamine (MA) and formaldehyde. Functions in bacterial methylated amine catabolism, linking alkylamine oxidation to the tetrahydrofolate C1 pool. The beta subunit of HODM binds FMN and a 2Fe-2S cluster, and likely reduces the ferric heme iron of the alpha subunit to ferrous using NADPH.",Mediates the electron transfer from quinonoid to the azo bond in the azo ring of the pyridine ring. It transfers the electrons to the major quinone oxidase (QO) Rrp41. Is also active with azoquinone and gamma-butyrobetaine.,Maybe,No,No,No,Maybe,not-Yes,GO:0051537; GO:0046872; GO:0016491,,,,,,,,,,,0,,0.2158,no
HODMB_ECTM1,A4XXY8,ProtT3,Bacteria,309,"Component of the heme-dependent oxidative N-demethylase (HODM) enzyme, that catalyzes the NADPH-dependent oxidation of dimethylamine (DMA) to methylamine (MA) and formaldehyde. Functions in bacterial methylated amine catabolism, linking alkylamine oxidation to the tetrahydrofolate C1 pool. The beta subunit of HODM binds FMN and a 2Fe-2S cluster, and likely reduces the ferric heme iron of the alpha subunit to ferrous using NADPH.","Involved in the degradation of 2,4-dichlorophenoxyacetic acid (2,4-D) via the 2,4-dichlorophenoxypropionate (2,4-DCP) intermediate. Catalyzes the reduction of 2,4-dichlorophenoxypropionate (2,4-DCP) to 2,4-dichlorophenoxyacetate (2,4-DCA). Belongs to the P450 family",Maybe,No,No,No,No,not-Yes,GO:0051537; GO:0046872; GO:0016491,GO:0004497,GO:0004497; GO:0020037,GO:0004497; GO:0020037,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506; GO:0020037,0.4705,0.4965,0.4965,0.6232,0.6232,5,0.542,0.2158,no
HODMB_ECTM1,A4XXY8,ProtTale,Bacteria,309,"Component of the heme-dependent oxidative N-demethylase (HODM) enzyme, that catalyzes the NADPH-dependent oxidation of dimethylamine (DMA) to methylamine (MA) and formaldehyde. Functions in bacterial methylated amine catabolism, linking alkylamine oxidation to the tetrahydrofolate C1 pool. The beta subunit of HODM binds FMN and a 2Fe-2S cluster, and likely reduces the ferric heme iron of the alpha subunit to ferrous using NADPH.","Involved in the degradation of 2,4-dichlorophenol (2,4-DCP). Catalyzes the reduction of 2,4-DCP to 2,4-dihydro-2,4-dichlorobenzoate (2,4-DH-2,4-DCP). It can also reduce 2,4,6-trichlorophenol (2,4,6-DCP) to 2,4,6-dihydro-2,4,6-trichlorobenzoate (2,4,6-DH-2,4,6",Maybe,No,No,No,No,not-Yes,GO:0051537; GO:0046872; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.5789,0.5789,0.5789,0.5789,0.5789,5,0.5789,0.2158,no
HODMB_ECTM1,A4XXY8,Protein2Text,Bacteria,309,"Component of the heme-dependent oxidative N-demethylase (HODM) enzyme, that catalyzes the NADPH-dependent oxidation of dimethylamine (DMA) to methylamine (MA) and formaldehyde. Functions in bacterial methylated amine catabolism, linking alkylamine oxidation to the tetrahydrofolate C1 pool. The beta subunit of HODM binds FMN and a 2Fe-2S cluster, and likely reduces the ferric heme iron of the alpha subunit to ferrous using NADPH.","The molecular function of this protein is as an oxidoreductase, specifically it is involved in the oxidation of organic compounds.",Vague,No,Vague,Vague,Vague,not-Yes,GO:0051537; GO:0046872; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.5789,0.5789,0.5789,0.5789,0.5789,5,0.5789,0.2158,no
HODMB_ECTM1,A4XXY8,Reference,Bacteria,309,"Component of the heme-dependent oxidative N-demethylase (HODM) enzyme, that catalyzes the NADPH-dependent oxidation of dimethylamine (DMA) to methylamine (MA) and formaldehyde. Functions in bacterial methylated amine catabolism, linking alkylamine oxidation to the tetrahydrofolate C1 pool. The beta subunit of HODM binds FMN and a 2Fe-2S cluster, and likely reduces the ferric heme iron of the alpha subunit to ferrous using NADPH.","Component of the heme-dependent oxidative N-demethylase (HODM) enzyme, that catalyzes the NADPH-dependent oxidation of dimethylamine (DMA) to methylamine (MA) and formaldehyde. Functions in bacterial methylated amine catabolism, linking alkylamine oxidation to the tetrahydrofolate C1 pool. The beta subunit of HODM binds FMN and a 2Fe-2S cluster, and likely reduces the ferric heme iron of the alpha subunit to ferrous using NADPH.",,,,,,,GO:0051537; GO:0046872; GO:0016491,GO:0010181; GO:0009055; GO:0050661,GO:0016491; GO:0010181,GO:0016491; GO:0010181; GO:0051537,GO:0016491; GO:0010181; GO:0051536,GO:0016491; GO:0010181,0.3233,0.5989,0.7905,0.7478,0.5989,5,0.6119,0.2158,no
FOLQ_LIMRD,A5VL09,ESM2Text,Bacteria,195,"Pyrophosphatase involved in the biosynthesis of tetrahydrofolate. Catalyzes the hydrolysis of dihydroneopterin triphosphate (DHNTP) to dihydroneopterin monophosphate (DHNMP) and pyrophosphate. Shows a strict substrate specificity. Has only weak activity with GTP, ITP, XTP and dTTP, and cannot use ATP, UTP, CTP, NAD(+), NADH, diadenosine triphosphate, diadenosine tetraphosphate, ADP-ribose and UDP-glucose.","Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0019177; GO:0047429,GO:0017111,GO:0047429,GO:0017110,GO:0047429,GO:0016462,0.7469,0.9156,0.7469,0.9156,0.8691,5,0.8388,0.6622,yes
FOLQ_LIMRD,A5VL09,Prot2Text,Bacteria,195,"Pyrophosphatase involved in the biosynthesis of tetrahydrofolate. Catalyzes the hydrolysis of dihydroneopterin triphosphate (DHNTP) to dihydroneopterin monophosphate (DHNMP) and pyrophosphate. Shows a strict substrate specificity. Has only weak activity with GTP, ITP, XTP and dTTP, and cannot use ATP, UTP, CTP, NAD(+), NADH, diadenosine triphosphate, diadenosine tetraphosphate, ADP-ribose and UDP-glucose.","Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0019177; GO:0047429,GO:0017111,GO:0017111,GO:0017111,GO:0017111,GO:0017111,0.7469,0.7469,0.7469,0.7469,0.7469,5,0.7469,0.6622,yes
FOLQ_LIMRD,A5VL09,ProtT3,Bacteria,195,"Pyrophosphatase involved in the biosynthesis of tetrahydrofolate. Catalyzes the hydrolysis of dihydroneopterin triphosphate (DHNTP) to dihydroneopterin monophosphate (DHNMP) and pyrophosphate. Shows a strict substrate specificity. Has only weak activity with GTP, ITP, XTP and dTTP, and cannot use ATP, UTP, CTP, NAD(+), NADH, diadenosine triphosphate, diadenosine tetraphosphate, ADP-ribose and UDP-glucose.","Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0019177; GO:0047429,GO:0017111,GO:0017111,GO:0017111,GO:0017111,GO:0017111,0.7469,0.7469,0.7469,0.7469,0.7469,5,0.7469,0.6622,yes
FOLQ_LIMRD,A5VL09,ProtTale,Bacteria,195,"Pyrophosphatase involved in the biosynthesis of tetrahydrofolate. Catalyzes the hydrolysis of dihydroneopterin triphosphate (DHNTP) to dihydroneopterin monophosphate (DHNMP) and pyrophosphate. Shows a strict substrate specificity. Has only weak activity with GTP, ITP, XTP and dTTP, and cannot use ATP, UTP, CTP, NAD(+), NADH, diadenosine triphosphate, diadenosine tetraphosphate, ADP-ribose and UDP-glucose.","Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0019177; GO:0047429,GO:0016462,GO:0016787,GO:0017111,GO:0017111,GO:0047429,0.8691,0.5381,0.7469,0.7469,0.9156,5,0.7633,0.6622,yes
FOLQ_LIMRD,A5VL09,Protein2Text,Bacteria,195,"Pyrophosphatase involved in the biosynthesis of tetrahydrofolate. Catalyzes the hydrolysis of dihydroneopterin triphosphate (DHNTP) to dihydroneopterin monophosphate (DHNMP) and pyrophosphate. Shows a strict substrate specificity. Has only weak activity with GTP, ITP, XTP and dTTP, and cannot use ATP, UTP, CTP, NAD(+), NADH, diadenosine triphosphate, diadenosine tetraphosphate, ADP-ribose and UDP-glucose.","The molecular function of this protein is as a pyrophosphatase, specifically a nucleoside triphosphate pyrophosphatase, which catalyzes the hydrolysis of nucleoside triphosphates to their corresponding monophosphates, with the release of inorganic pyrophosphate (PPi). This protein is likely involved in regulating the levels of nucleoside triphosphates and preventing the accumulation of PPi, which can interfere with various cellular processes.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0019177; GO:0047429,GO:0017111,GO:0004427,GO:0017111,GO:0017111,GO:0017111,0.7469,0.7469,0.7469,0.7469,0.7469,5,0.7469,0.6622,yes
FOLQ_LIMRD,A5VL09,Reference,Bacteria,195,"Pyrophosphatase involved in the biosynthesis of tetrahydrofolate. Catalyzes the hydrolysis of dihydroneopterin triphosphate (DHNTP) to dihydroneopterin monophosphate (DHNMP) and pyrophosphate. Shows a strict substrate specificity. Has only weak activity with GTP, ITP, XTP and dTTP, and cannot use ATP, UTP, CTP, NAD(+), NADH, diadenosine triphosphate, diadenosine tetraphosphate, ADP-ribose and UDP-glucose.","Pyrophosphatase involved in the biosynthesis of tetrahydrofolate. Catalyzes the hydrolysis of dihydroneopterin triphosphate (DHNTP) to dihydroneopterin monophosphate (DHNMP) and pyrophosphate. Shows a strict substrate specificity. Has only weak activity with GTP, ITP, XTP and dTTP, and cannot use ATP, UTP, CTP, NAD(+), NADH, diadenosine triphosphate, diadenosine tetraphosphate, ADP-ribose and UDP-glucose.",,,,,,,GO:0019177; GO:0047429,GO:0016462,GO:0004150,GO:0016462,GO:0016462,GO:0016462,0.8691,0.1737,0.8691,0.8691,0.8691,5,0.73,0.6622,yes
PLYA_SCLS1,A7E4L6,ESM2Text,Eukaryota,329,"Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester.","Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0030570,GO:0030570,GO:0030570,GO:0030570,GO:0030570,GO:0030570,0.6963,0.6963,0.6963,0.6963,0.6963,5,0.6963,0.2905,no
PLYA_SCLS1,A7E4L6,Prot2Text,Eukaryota,329,"Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester.","Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0030570,GO:0030570,GO:0030570,GO:0030570,GO:0030570,GO:0030570,0.6963,0.6963,0.6963,0.6963,0.6963,5,0.6963,0.2905,no
PLYA_SCLS1,A7E4L6,ProtT3,Eukaryota,329,"Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester.","Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity). Secreted. Belongs to the polysaccharide lyase 1 family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0030570,GO:0030570,GO:0030570,GO:0030570,GO:0030570,GO:0030570,0.6963,0.6963,0.6963,0.6963,0.6963,5,0.6963,0.2905,no
PLYA_SCLS1,A7E4L6,ProtTale,Eukaryota,329,"Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester.","Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0030570,GO:0016837,GO:0030570,GO:0030570,GO:0030570,GO:0030570,0.607,0.6963,0.6963,0.6963,0.6963,5,0.6784,0.2905,no
PLYA_SCLS1,A7E4L6,Protein2Text,Eukaryota,329,"Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester.","This protein is involved in breaking down plant cell walls, specifically the hydrolysis of macromolecules. More precisely, it is involved in the hydrolysis of the ester bond of pectin, a key component of plant cell walls. This is a type of macerolytic activity.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0030570,GO:0030570,GO:0030570,GO:0004650,GO:0030570,GO:0004650,0.6963,0.6963,0.1628,0.6963,0.1628,5,0.4829,0.2905,no
PLYA_SCLS1,A7E4L6,Reference,Eukaryota,329,"Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester.","Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester.",,,,,,,GO:0046872; GO:0030570,GO:0030570,GO:0030570,GO:0030570,GO:0030570,GO:0030570,0.6963,0.6963,0.6963,0.6963,0.6963,5,0.6963,0.2905,no
PGLR1_SCLS1,A7EXV2,ESM2Text,Eukaryota,380,"Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.","Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004650,GO:0004650,GO:0004650,GO:0004650,GO:0004650,GO:0004650,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4774,no
PGLR1_SCLS1,A7EXV2,Prot2Text,Eukaryota,380,"Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.","Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004650,GO:0004650,GO:0004650,GO:0004650,GO:0004650,GO:0004650,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4774,no
PGLR1_SCLS1,A7EXV2,ProtT3,Eukaryota,380,"Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.",Secreted. Belongs to the glycosyl hydrolase 28 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004650,GO:0004650,GO:0004650,GO:0004650,GO:0004650,GO:0004650,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4774,no
PGLR1_SCLS1,A7EXV2,ProtTale,Eukaryota,380,"Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.","Pectinolytic enzyme involved in the degradation of pectin, a major component of plant cell walls.",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004650,GO:0004650,GO:0004650,GO:0016798,GO:0004650,,1.0,1.0,0.729,1.0,,4,0.9323,0.4774,no
PGLR1_SCLS1,A7EXV2,Protein2Text,Eukaryota,380,"Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.","This protein is involved in the hydrolysis of macromolecules, specifically in breaking down complex carbohydrates such as pectin and xylan. It is a type of glycoside hydrolase, which is an enzyme that catalyzes the hydrolysis of glycosidic bonds in carbohydrates. This protein is likely involved in the degradation of plant cell walls, allowing the microorganism to access nutrients and grow.",Maybe,Maybe,Vague,Maybe,Maybe,not-Yes,GO:0004650,GO:0004553,GO:0004553,GO:0004553,GO:0004553,GO:0004553,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.4774,no
PGLR1_SCLS1,A7EXV2,Reference,Eukaryota,380,"Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.","Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.",,,,,,,GO:0004650,GO:0004650,GO:0004650,GO:0004650,GO:0004650,GO:0004650,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4774,no
UGNAD_BACCN,A7GKX6,ESM2Text,Bacteria,423,"Dehydrogenase involved in the biosynthesis of the nucleotide- sugar UDP-N-acetylxylosamine (UDP-XylNAc). Catalyzes the conversion of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N- acetylglucosaminuronic acid (UDP-GlcNAcA). Cannot use UDP-glucose, UDP-galactose and UDP-N-acetylgalactosamine as substrates.",Required for the biosynthesis of type 1 capsular polysaccharide.,Vague,No,Vague,Vague,Vague,not-Yes,GO:0051287; GO:0016628; GO:0047004,,,,,,,,,,,0,,0.3533,no
UGNAD_BACCN,A7GKX6,Prot2Text,Bacteria,423,"Dehydrogenase involved in the biosynthesis of the nucleotide- sugar UDP-N-acetylxylosamine (UDP-XylNAc). Catalyzes the conversion of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N- acetylglucosaminuronic acid (UDP-GlcNAcA). Cannot use UDP-glucose, UDP-galactose and UDP-N-acetylgalactosamine as substrates.","Catalyzes the four-electron oxidation of UDP-N-acetyl-D-mannosamine (UDP-ManNAc), reducing NAD(+) and releasing UDP-N-acetylmannosaminuronic acid (UDP-ManNAcA).",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0051287; GO:0016628; GO:0047004,GO:0016616,GO:0050708,GO:0016616,GO:0016616,GO:0016616,0.5661,0.0,0.5661,0.5661,0.5661,5,0.4529,0.3533,no
UGNAD_BACCN,A7GKX6,ProtT3,Bacteria,423,"Dehydrogenase involved in the biosynthesis of the nucleotide- sugar UDP-N-acetylxylosamine (UDP-XylNAc). Catalyzes the conversion of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N- acetylglucosaminuronic acid (UDP-GlcNAcA). Cannot use UDP-glucose, UDP-galactose and UDP-N-acetylgalactosamine as substrates.",Catalyzes the oxidation of UDP-N-acetyl-D-mannosamine (UDP-ManNAc) to UDP-N- acetylmannosaminuronic acid (UDP-ManNAcA). Belongs to the UDP-glucose/GDP-mannose dehydrogenase family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0051287; GO:0016628; GO:0047004,GO:0016616,GO:0016616,GO:0016616,GO:0016616,GO:0050699,0.5661,0.5661,0.5661,0.5661,0.1505,5,0.483,0.3533,no
UGNAD_BACCN,A7GKX6,ProtTale,Bacteria,423,"Dehydrogenase involved in the biosynthesis of the nucleotide- sugar UDP-N-acetylxylosamine (UDP-XylNAc). Catalyzes the conversion of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N- acetylglucosaminuronic acid (UDP-GlcNAcA). Cannot use UDP-glucose, UDP-galactose and UDP-N-acetylgalactosamine as substrates.","Catalyzes the four-electron oxidation of UDP-N-acetyl-D- mannosamine (UDP-ManNAc), reducing NAD(+) and releasing UDP-N- acetylmannosaminuronic acid (UDP-ManNAcA).",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0051287; GO:0016628; GO:0047004,GO:0016616,GO:0016491; GO:0050661,GO:0016616,GO:0016616,GO:0016616,0.5661,0.711,0.5661,0.5661,0.5661,5,0.5951,0.3533,no
UGNAD_BACCN,A7GKX6,Protein2Text,Bacteria,423,"Dehydrogenase involved in the biosynthesis of the nucleotide- sugar UDP-N-acetylxylosamine (UDP-XylNAc). Catalyzes the conversion of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N- acetylglucosaminuronic acid (UDP-GlcNAcA). Cannot use UDP-glucose, UDP-galactose and UDP-N-acetylgalactosamine as substrates.","The molecular function of this protein is a nucleoside kinase, specifically involved in the conversion of a nucleoside into a nucleotide by transferring a phosphate group from ATP to the 5'-hydroxyl of the sugar moiety. More specifically, it catalyzes the conversion of ribose to ribose-5-phosphate, and deoxyribose to deoxyribose-5-phosphate, using ATP as a phosphate donor. This protein is involved in the biosynthesis of nucleotides, which are essential for various cellular processes such as DNA and RNA synthesis, and energy metabolism.",No,No,No,No,No,not-Yes,GO:0051287; GO:0016628; GO:0047004,,GO:0019206,GO:0019206,GO:0019206,,,0.1545,0.1545,0.1545,,3,0.1545,0.3533,no
UGNAD_BACCN,A7GKX6,Reference,Bacteria,423,"Dehydrogenase involved in the biosynthesis of the nucleotide- sugar UDP-N-acetylxylosamine (UDP-XylNAc). Catalyzes the conversion of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N- acetylglucosaminuronic acid (UDP-GlcNAcA). Cannot use UDP-glucose, UDP-galactose and UDP-N-acetylgalactosamine as substrates.","Dehydrogenase involved in the biosynthesis of the nucleotide- sugar UDP-N-acetylxylosamine (UDP-XylNAc). Catalyzes the conversion of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N- acetylglucosaminuronic acid (UDP-GlcNAcA). Cannot use UDP-glucose, UDP-galactose and UDP-N-acetylgalactosamine as substrates.",,,,,,,GO:0051287; GO:0016628; GO:0047004,GO:0016491; GO:0051287,GO:0016616,GO:0016616,GO:0016491; GO:0051287,GO:0016616,0.7963,0.5661,0.5661,0.7963,0.5661,5,0.6582,0.3533,no
HPAAL_PARL1,A7HU24,ESM2Text,Bacteria,260,Aldolase which can catalyze in vitro the aldolisation reaction between hydroxypyruvate (HPA) or pyruvate (PA) and D- glyceraldehyde (D-GA) (Ref.2). The condensation of pyruvate and D- glyceraldehyde produces 2-dehydro-3-deoxy-L-galactonate (Ref.2). Has weak activity with hydroxypyruvate and D-glyceraldehyde (Ref.2).,Catalyzes the reversible retro-aldol cleavage of 2-keto-3-deoxy-L-rhamnonate (KDR) to pyruvate and lactaldehyde.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016832; GO:0046872,GO:0016832,GO:0016832,GO:0016832,GO:0016832,GO:0016832,0.7015,0.7015,0.7015,0.7015,0.7015,5,0.7015,0.4429,no
HPAAL_PARL1,A7HU24,Prot2Text,Bacteria,260,Aldolase which can catalyze in vitro the aldolisation reaction between hydroxypyruvate (HPA) or pyruvate (PA) and D- glyceraldehyde (D-GA) (Ref.2). The condensation of pyruvate and D- glyceraldehyde produces 2-dehydro-3-deoxy-L-galactonate (Ref.2). Has weak activity with hydroxypyruvate and D-glyceraldehyde (Ref.2).,Catalyzes the reversible retro-aldol cleavage of both 5-keto-4-deoxy-D-glucarate and 2-keto-3-deoxy-D-glucarate to pyruvate and tartronic semialdehyde.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016832; GO:0046872,GO:0016832,GO:0016832,GO:0016832,GO:0016832,GO:0016832,0.7015,0.7015,0.7015,0.7015,0.7015,5,0.7015,0.4429,no
HPAAL_PARL1,A7HU24,ProtT3,Bacteria,260,Aldolase which can catalyze in vitro the aldolisation reaction between hydroxypyruvate (HPA) or pyruvate (PA) and D- glyceraldehyde (D-GA) (Ref.2). The condensation of pyruvate and D- glyceraldehyde produces 2-dehydro-3-deoxy-L-galactonate (Ref.2). Has weak activity with hydroxypyruvate and D-glyceraldehyde (Ref.2).,"Catalyzes the reversible retro-aldol cleavage of 4-hydroxy-2- ketoheptane-1,7-dioate (HKHD) to pyruvate and succinic semialdehyde. Belongs to the HpcH/HpaI aldolase family",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0016832; GO:0046872,GO:0016832,GO:0016832,GO:0016832,GO:0016832,GO:0016832,0.7015,0.7015,0.7015,0.7015,0.7015,5,0.7015,0.4429,no
HPAAL_PARL1,A7HU24,ProtTale,Bacteria,260,Aldolase which can catalyze in vitro the aldolisation reaction between hydroxypyruvate (HPA) or pyruvate (PA) and D- glyceraldehyde (D-GA) (Ref.2). The condensation of pyruvate and D- glyceraldehyde produces 2-dehydro-3-deoxy-L-galactonate (Ref.2). Has weak activity with hydroxypyruvate and D-glyceraldehyde (Ref.2).,May play a role in plant growth and development.,Vague,No,Vague,No,Vague,not-Yes,GO:0016832; GO:0046872,,,,,,,,,,,0,,0.4429,no
HPAAL_PARL1,A7HU24,Protein2Text,Bacteria,260,Aldolase which can catalyze in vitro the aldolisation reaction between hydroxypyruvate (HPA) or pyruvate (PA) and D- glyceraldehyde (D-GA) (Ref.2). The condensation of pyruvate and D- glyceraldehyde produces 2-dehydro-3-deoxy-L-galactonate (Ref.2). Has weak activity with hydroxypyruvate and D-glyceraldehyde (Ref.2).,"The molecular function of this protein is an aldolase, which is a type of enzyme that catalyzes the reversible cleavage of aldol compounds into two simpler sugars. Specifically, this protein is likely involved in the cleavage of D-glyceraldehyde 3-phosphate (G3P) and D-fructose 1,6-bisphosphate (FBP) to form dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde 3-phosphate (G3P), respectively.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016832; GO:0046872,GO:0004332,GO:0004332,GO:0004332,GO:0004332,GO:0004332,0.6017,0.6017,0.6017,0.6017,0.6017,5,0.6017,0.4429,no
HPAAL_PARL1,A7HU24,Reference,Bacteria,260,Aldolase which can catalyze in vitro the aldolisation reaction between hydroxypyruvate (HPA) or pyruvate (PA) and D- glyceraldehyde (D-GA) (Ref.2). The condensation of pyruvate and D- glyceraldehyde produces 2-dehydro-3-deoxy-L-galactonate (Ref.2). Has weak activity with hydroxypyruvate and D-glyceraldehyde (Ref.2).,Aldolase which can catalyze in vitro the aldolisation reaction between hydroxypyruvate (HPA) or pyruvate (PA) and D- glyceraldehyde (D-GA) (Ref.2). The condensation of pyruvate and D- glyceraldehyde produces 2-dehydro-3-deoxy-L-galactonate (Ref.2). Has weak activity with hydroxypyruvate and D-glyceraldehyde (Ref.2).,,,,,,,GO:0016832; GO:0046872,GO:0016832,GO:0016832,GO:0016832,GO:0016832,GO:0016832,0.7015,0.7015,0.7015,0.7015,0.7015,5,0.7015,0.4429,no
LIP7_MALGO,A8QCV4,ESM2Text,Eukaryota,468,"Secreted lipase involved in Dandruff and seborrheic dermatitis (D/SD) probably via lipase-mediated breakdown of sebaceous lipids and release of irritating free fatty acids. Has triacylglycerol lipase activity and is able to hydrolyze triolein. Mostly converts monoolein to di- and triolein, while free fatty acids are only produced in low amounts.",Involved in the degradation of unsaturated fatty acids. Catalyzes the hydrolysis of palmitate (C16=C18) to produce short chain fatty acids (C14=C18). It shows higher activity toward short chain fatty acids than toward long chain fatty acids.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004806,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016788,0.5324,0.5324,0.5324,0.5324,0.6506,5,0.556,0.3363,no
LIP7_MALGO,A8QCV4,Prot2Text,Eukaryota,468,"Secreted lipase involved in Dandruff and seborrheic dermatitis (D/SD) probably via lipase-mediated breakdown of sebaceous lipids and release of irritating free fatty acids. Has triacylglycerol lipase activity and is able to hydrolyze triolein. Mostly converts monoolein to di- and triolein, while free fatty acids are only produced in low amounts.",Hydrolyzes triglycerides.,Yes,Maybe,Yes,Maybe,Yes,Yes,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3363,no
LIP7_MALGO,A8QCV4,ProtT3,Eukaryota,468,"Secreted lipase involved in Dandruff and seborrheic dermatitis (D/SD) probably via lipase-mediated breakdown of sebaceous lipids and release of irritating free fatty acids. Has triacylglycerol lipase activity and is able to hydrolyze triolein. Mostly converts monoolein to di- and triolein, while free fatty acids are only produced in low amounts.",Catalyzes the hydrolysis of triacylglycerols (TAGs) into free fatty acids (FFAs) and monoacylglycerols (MAGs). Secreted. Belongs to the AB hydrolase superfamily. Lipase family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004806,GO:0016298,GO:0004806,GO:0004806,GO:0004806,GO:0004806,0.7707,1.0,1.0,1.0,1.0,5,0.9541,0.3363,no
LIP7_MALGO,A8QCV4,ProtTale,Eukaryota,468,"Secreted lipase involved in Dandruff and seborrheic dermatitis (D/SD) probably via lipase-mediated breakdown of sebaceous lipids and release of irritating free fatty acids. Has triacylglycerol lipase activity and is able to hydrolyze triolein. Mostly converts monoolein to di- and triolein, while free fatty acids are only produced in low amounts.","Secreted lipase that catalyzes the hydrolysis of triacylglycerols to free fatty acids and glycerol. Is able to hydrolyze tributyrin and p-nitrophenyl palmitate (p-NPP), but not triolein, p-nitrophenyl butyrate, or p-nitrophenyl palmitoleate (p-NPPO).",Yes,Maybe,Yes,Yes,Yes,Yes,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3363,no
LIP7_MALGO,A8QCV4,Protein2Text,Eukaryota,468,"Secreted lipase involved in Dandruff and seborrheic dermatitis (D/SD) probably via lipase-mediated breakdown of sebaceous lipids and release of irritating free fatty acids. Has triacylglycerol lipase activity and is able to hydrolyze triolein. Mostly converts monoolein to di- and triolein, while free fatty acids are only produced in low amounts.","The molecular function of this protein is lipase activity. Specifically, it is involved in the hydrolysis of triglycerides into free fatty acids and glycerol.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3363,no
LIP7_MALGO,A8QCV4,Reference,Eukaryota,468,"Secreted lipase involved in Dandruff and seborrheic dermatitis (D/SD) probably via lipase-mediated breakdown of sebaceous lipids and release of irritating free fatty acids. Has triacylglycerol lipase activity and is able to hydrolyze triolein. Mostly converts monoolein to di- and triolein, while free fatty acids are only produced in low amounts.","Secreted lipase involved in Dandruff and seborrheic dermatitis (D/SD) probably via lipase-mediated breakdown of sebaceous lipids and release of irritating free fatty acids. Has triacylglycerol lipase activity and is able to hydrolyze triolein. Mostly converts monoolein to di- and triolein, while free fatty acids are only produced in low amounts.",,,,,,,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3363,no
DHGRD_AGRFC,A9CEY6,ESM2Text,Bacteria,297,"Part of the sulfoquinovose monooxygenase (sulfo-SMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite. Catalyzes the NADP- dependent reduction of 6-dehydro-D-glucose to D-glucose. Cannot use NADH.","Dihydrofructofructan 1-alpha-reductase involved in phthiocerol dimycocerosate (PDIM) degradation. Also able to reduce phthiocerol dimycocerosate (PDIMA), but not phthiocerol dimycocerosate (PDIMB). Uses NADPH as a reducing agent.",Maybe,No,No,No,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,,GO:0016491; GO:0050661,1.0,1.0,1.0,,0.7089,4,0.9272,0.2002,no
DHGRD_AGRFC,A9CEY6,Prot2Text,Bacteria,297,"Part of the sulfoquinovose monooxygenase (sulfo-SMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite. Catalyzes the NADP- dependent reduction of 6-dehydro-D-glucose to D-glucose. Cannot use NADH.","Aldo-keto reductase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome P450 monooxygenase P450 claM then catalyzes the dimerization of nataloe-emodin to cladofulvin.",Maybe,No,Maybe,No,Maybe,not-Yes,GO:0016491,GO:0004033,GO:0016491,GO:0004033,GO:0004033,GO:0016491,0.0,1.0,0.0,0.0,1.0,5,0.4,0.2002,no
DHGRD_AGRFC,A9CEY6,ProtT3,Bacteria,297,"Part of the sulfoquinovose monooxygenase (sulfo-SMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite. Catalyzes the NADP- dependent reduction of 6-dehydro-D-glucose to D-glucose. Cannot use NADH.",Belongs to the aldo/keto reductase family. Aldo/keto reductase 2 subfamily,Vague,No,Vague,Vague,Vague,not-Yes,GO:0016491,,GO:0016491,GO:0004033,GO:0016491,GO:0016491,,1.0,0.0,1.0,1.0,4,0.75,0.2002,no
DHGRD_AGRFC,A9CEY6,ProtTale,Bacteria,297,"Part of the sulfoquinovose monooxygenase (sulfo-SMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite. Catalyzes the NADP- dependent reduction of 6-dehydro-D-glucose to D-glucose. Cannot use NADH.",Catalyzes the NAD(P)H-dependent oxidation of 5-oxoproline to 5-oxoproline 5-phosphate.,Maybe,No,Maybe,No,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016491; GO:0050661,,GO:0016491,GO:0016491,1.0,0.7089,,1.0,1.0,4,0.9272,0.2002,no
DHGRD_AGRFC,A9CEY6,Protein2Text,Bacteria,297,"Part of the sulfoquinovose monooxygenase (sulfo-SMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite. Catalyzes the NADP- dependent reduction of 6-dehydro-D-glucose to D-glucose. Cannot use NADH.","This protein is an alcohol dehydrogenase, which means it catalyzes the oxidation of alcohol to an aldehyde. In particular, it is likely involved in the conversion of a specific alcohol to an aldehyde, but the exact substrate is not specified. As an alcohol dehydrogenase, this protein would be expected to play a role in metabolic processes that involve the oxidation of alcohols. 
The molecular function of this protein is the oxidation of an alcohol to an aldehyde.",Maybe,No,No,No,Maybe,not-Yes,GO:0016491,GO:0004022,GO:0004022,GO:0004022,GO:0004022,GO:0004022,0.5381,0.5381,0.5381,0.5381,0.5381,5,0.5381,0.2002,no
DHGRD_AGRFC,A9CEY6,Reference,Bacteria,297,"Part of the sulfoquinovose monooxygenase (sulfo-SMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite. Catalyzes the NADP- dependent reduction of 6-dehydro-D-glucose to D-glucose. Cannot use NADH.","Part of the sulfoquinovose monooxygenase (sulfo-SMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite. Catalyzes the NADP- dependent reduction of 6-dehydro-D-glucose to D-glucose. Cannot use NADH.",,,,,,,GO:0016491,GO:0016491; GO:0050661,GO:0016491; GO:0050661,GO:0016491,GO:0016491; GO:0050661,GO:0016491,0.7089,0.7089,1.0,0.7089,1.0,5,0.8253,0.2002,no
YEJF_AGRFC,A9CKL2,ESM2Text,Bacteria,546,"Part of the ABC transporter complex YejBEF-YepA involved in the uptake of muropeptides, the breakdown products of cell wall peptidoglycan. The import of muropeptides into the cell enables peptidoglycan recycling, which is vital for cell wall integrity in this bacterium. Is also probably part of the ABC transporter complex YejABEF, which is likely involved in broad- spectrum peptide import (Probable). Responsible for energy coupling to the transport system (Probable).",Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import. Responsible for energy coupling to the transport system.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887,GO:0016887,GO:0016887,GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.6869,0.6869,0.6869,1.0,1.0,5,0.8121,0.3284,no
YEJF_AGRFC,A9CKL2,Prot2Text,Bacteria,546,"Part of the ABC transporter complex YejBEF-YepA involved in the uptake of muropeptides, the breakdown products of cell wall peptidoglycan. The import of muropeptides into the cell enables peptidoglycan recycling, which is vital for cell wall integrity in this bacterium. Is also probably part of the ABC transporter complex YejABEF, which is likely involved in broad- spectrum peptide import (Probable). Responsible for energy coupling to the transport system (Probable).",Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0005524; GO:0016887,GO:0042626,GO:0015415,GO:0016887; GO:0005524,GO:0042626,GO:0042626,0.1952,0.1509,1.0,0.1952,0.1952,5,0.3473,0.3284,no
YEJF_AGRFC,A9CKL2,ProtT3,Bacteria,546,"Part of the ABC transporter complex YejBEF-YepA involved in the uptake of muropeptides, the breakdown products of cell wall peptidoglycan. The import of muropeptides into the cell enables peptidoglycan recycling, which is vital for cell wall integrity in this bacterium. Is also probably part of the ABC transporter complex YejABEF, which is likely involved in broad- spectrum peptide import (Probable). Responsible for energy coupling to the transport system (Probable).",Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for energy coupling to the transport system. Cell inner membrane; Peripheral membrane protein. Belongs to the ABC transporter superfamily,Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887,GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0005524; GO:0016887,GO:0005524; GO:0016887,GO:0005524; GO:0016887,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3284,no
YEJF_AGRFC,A9CKL2,ProtTale,Bacteria,546,"Part of the ABC transporter complex YejBEF-YepA involved in the uptake of muropeptides, the breakdown products of cell wall peptidoglycan. The import of muropeptides into the cell enables peptidoglycan recycling, which is vital for cell wall integrity in this bacterium. Is also probably part of the ABC transporter complex YejABEF, which is likely involved in broad- spectrum peptide import (Probable). Responsible for energy coupling to the transport system (Probable).",Part of the ABC transporter complex OppABCDF involved in the uptake of oligopeptides. Responsible for energy coupling to the transport system.,Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887,GO:0016887,GO:0005524,GO:0005524; GO:0016887,GO:0005524; GO:0016887,GO:0016887,0.6869,0.6869,1.0,1.0,0.6869,5,0.8121,0.3284,no
YEJF_AGRFC,A9CKL2,Protein2Text,Bacteria,546,"Part of the ABC transporter complex YejBEF-YepA involved in the uptake of muropeptides, the breakdown products of cell wall peptidoglycan. The import of muropeptides into the cell enables peptidoglycan recycling, which is vital for cell wall integrity in this bacterium. Is also probably part of the ABC transporter complex YejABEF, which is likely involved in broad- spectrum peptide import (Probable). Responsible for energy coupling to the transport system (Probable).","The molecular function of this protein is an ATP-binding component of a binding-protein-dependent transport system for an unknown substrate. It is part of an ABC transporter, which facilitates the movement of molecules across cell membranes. This protein is responsible for binding and hydrolyzing ATP to provide energy for the transport process.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887,GO:0005524; GO:0042626,GO:0005524; GO:0042626,GO:0005524; GO:0016887,GO:0005524; GO:0016887,GO:0005524; GO:0016887,0.6281,0.6281,1.0,1.0,1.0,5,0.8512,0.3284,no
YEJF_AGRFC,A9CKL2,Reference,Bacteria,546,"Part of the ABC transporter complex YejBEF-YepA involved in the uptake of muropeptides, the breakdown products of cell wall peptidoglycan. The import of muropeptides into the cell enables peptidoglycan recycling, which is vital for cell wall integrity in this bacterium. Is also probably part of the ABC transporter complex YejABEF, which is likely involved in broad- spectrum peptide import (Probable). Responsible for energy coupling to the transport system (Probable).","Part of the ABC transporter complex YejBEF-YepA involved in the uptake of muropeptides, the breakdown products of cell wall peptidoglycan. The import of muropeptides into the cell enables peptidoglycan recycling, which is vital for cell wall integrity in this bacterium. Is also probably part of the ABC transporter complex YejABEF, which is likely involved in broad- spectrum peptide import (Probable). Responsible for energy coupling to the transport system (Probable).",,,,,,,GO:0005524; GO:0016887,GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.6869,1.0,1.0,1.0,1.0,5,0.9374,0.3284,no
FDRB_SORC5,A9FRJ0,ESM2Text,Bacteria,244,Transports electrons between NADPH and ferredoxin. Can transfer electrons to ferredoxins Fdx2 and Fdx8. Prefers NADPH to NADH.,Reductase component of the propane 2-monooxygenase multicomponent enzyme system which is involved in the degradation of propane via the O2-dependent hydroxylation of propane. Reductase catalyzes the transfer of electrons from NADH or NADPH to monooxygenase (Probable). It can also use ferricyanide and naphthalene as substrates.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004324; GO:0000166,GO:0016491,GO:0016491,GO:0016491,GO:0016491; GO:0009055,GO:0016491; GO:0009055,0.415,0.415,0.415,0.375,0.375,5,0.399,0.2915,no
FDRB_SORC5,A9FRJ0,Prot2Text,Bacteria,244,Transports electrons between NADPH and ferredoxin. Can transfer electrons to ferredoxins Fdx2 and Fdx8. Prefers NADPH to NADH.,Transports electrons between flavodoxin or ferredoxin and NADPH.,Yes,Maybe,Yes,Maybe,Yes,Yes,GO:0004324; GO:0000166,GO:0004324,GO:0004324,GO:0004324,GO:0004324,GO:0004324,0.6976,0.6976,0.6976,0.6976,0.6976,5,0.6976,0.2915,no
FDRB_SORC5,A9FRJ0,ProtT3,Bacteria,244,Transports electrons between NADPH and ferredoxin. Can transfer electrons to ferredoxins Fdx2 and Fdx8. Prefers NADPH to NADH.,Catalyzes the reduction of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. Belongs to the flavodoxin family,No,No,No,No,No,not-Yes,GO:0004324; GO:0000166,GO:0010181; GO:0009055,GO:0010181; GO:0009055,GO:0010181; GO:0009055,GO:0010181; GO:0009055,GO:0010181; GO:0009055,0.4285,0.4285,0.4285,0.4285,0.4285,5,0.4285,0.2915,no
FDRB_SORC5,A9FRJ0,ProtTale,Bacteria,244,Transports electrons between NADPH and ferredoxin. Can transfer electrons to ferredoxins Fdx2 and Fdx8. Prefers NADPH to NADH.,Transports electrons between flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD).,Maybe,No,No,Maybe,Maybe,not-Yes,GO:0004324; GO:0000166,GO:0009055,GO:0016491,GO:0009055,GO:0009055,GO:0009055,0.2028,0.415,0.2028,0.2028,0.2028,5,0.2452,0.2915,no
FDRB_SORC5,A9FRJ0,Protein2Text,Bacteria,244,Transports electrons between NADPH and ferredoxin. Can transfer electrons to ferredoxins Fdx2 and Fdx8. Prefers NADPH to NADH.,"This protein is involved in the process of methylation, specifically in the transfer of methyl groups. It is part of a larger system that catalyzes the conversion of methylene-H4MPT to methylene-H4MPT.",No,No,No,No,No,not-Yes,GO:0004324; GO:0000166,GO:0008168,GO:0008168,GO:0008168,GO:0008168,,0.1774,0.1774,0.1774,0.1774,,4,0.1774,0.2915,no
FDRB_SORC5,A9FRJ0,Reference,Bacteria,244,Transports electrons between NADPH and ferredoxin. Can transfer electrons to ferredoxins Fdx2 and Fdx8. Prefers NADPH to NADH.,Transports electrons between NADPH and ferredoxin. Can transfer electrons to ferredoxins Fdx2 and Fdx8. Prefers NADPH to NADH.,,,,,,,GO:0004324; GO:0000166,GO:0004324; GO:0050661; GO:0009055,GO:0004324,GO:0004324,GO:0004324; GO:0050661,GO:0004324,0.7349,0.6976,0.6976,0.8656,0.6976,5,0.7387,0.2915,no
HASG_ASPFC,B0XWK5,ESM2Text,Eukaryota,468,"FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of hexadehydro-astechrome (HAS), a tryptophan-derived iron(III)-complex that acts as a virulence factor in infected mice. Within the pathway, hasG converts the prenyl to a methylbutadienyl side chain. The HAS biosynthesis begins with the synthesis of a tethered Trp-Ala dipeptide by the NRPS hasD. The 7-dimethylallyltryptophan synthase hasE then catalyzes the prenylation of the hasD-tethered tryptophan or the resulting tethered Trp-Ala dipeptide at the C-7 position of the indole moiety. HAS biosynthesis continues via tethered intermediates with the succesive actions of the cytochrome P450 monooxygenase hasH, the O- methyltransferase hasC, and the FAD-linked oxidoreductase hasG. The resulting O-methylated diketopiperazine is then released from hasD. Finally, three O-methylated diketopiperazine molecules assemble in a trimeric complex with Fe(III) to produce hexadehydro-astechrome.","Oxidoreductase; part of the gene cluster that mediates the biosynthesis of the tropolone class of fungal maleic anhydrides. The pathway begins with the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide synthase (PKS) tropA. 3-methylorcinaldehyde is the substrate for the FAD-dependent monooxygenase tropB to yield a dearomatized hydroxycyclohexadione. The 2-oxoglutarate-dependent dioxygenase tropC then performs the oxidative ring expansion to provide the first tropolone metabolite stipitaldehyde. Trop D converts stipitaldehyde into stipitacetal which is in turn converted to stipitalide by the short-chain dehydrogenase/reductase tropE. The next steps involve tropF, tropG, tropH, tropI and tropJ to form successive tropolone maleic anhydrides including stipitaldehydic, stipitatonic and stipitatic acids.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0071949; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.706,0.706,0.706,0.706,0.706,5,0.706,0.1705,no
HASG_ASPFC,B0XWK5,Prot2Text,Eukaryota,468,"FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of hexadehydro-astechrome (HAS), a tryptophan-derived iron(III)-complex that acts as a virulence factor in infected mice. Within the pathway, hasG converts the prenyl to a methylbutadienyl side chain. The HAS biosynthesis begins with the synthesis of a tethered Trp-Ala dipeptide by the NRPS hasD. The 7-dimethylallyltryptophan synthase hasE then catalyzes the prenylation of the hasD-tethered tryptophan or the resulting tethered Trp-Ala dipeptide at the C-7 position of the indole moiety. HAS biosynthesis continues via tethered intermediates with the succesive actions of the cytochrome P450 monooxygenase hasH, the O- methyltransferase hasC, and the FAD-linked oxidoreductase hasG. The resulting O-methylated diketopiperazine is then released from hasD. Finally, three O-methylated diketopiperazine molecules assemble in a trimeric complex with Fe(III) to produce hexadehydro-astechrome.","FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ. Paxilline is converted to beta",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0071949; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.706,0.706,0.706,0.706,0.706,5,0.706,0.1705,no
HASG_ASPFC,B0XWK5,ProtT3,Eukaryota,468,"FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of hexadehydro-astechrome (HAS), a tryptophan-derived iron(III)-complex that acts as a virulence factor in infected mice. Within the pathway, hasG converts the prenyl to a methylbutadienyl side chain. The HAS biosynthesis begins with the synthesis of a tethered Trp-Ala dipeptide by the NRPS hasD. The 7-dimethylallyltryptophan synthase hasE then catalyzes the prenylation of the hasD-tethered tryptophan or the resulting tethered Trp-Ala dipeptide at the C-7 position of the indole moiety. HAS biosynthesis continues via tethered intermediates with the succesive actions of the cytochrome P450 monooxygenase hasH, the O- methyltransferase hasC, and the FAD-linked oxidoreductase hasG. The resulting O-methylated diketopiperazine is then released from hasD. Finally, three O-methylated diketopiperazine molecules assemble in a trimeric complex with Fe(III) to produce hexadehydro-astechrome.",FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranyl,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0071949; GO:0016491,GO:0004497; GO:0071949,GO:0004497; GO:0071949,GO:0004497; GO:0071949,GO:0004497; GO:0071949,GO:0004497; GO:0071949,0.9073,0.9073,0.9073,0.9073,0.9073,5,0.9073,0.1705,no
HASG_ASPFC,B0XWK5,ProtTale,Eukaryota,468,"FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of hexadehydro-astechrome (HAS), a tryptophan-derived iron(III)-complex that acts as a virulence factor in infected mice. Within the pathway, hasG converts the prenyl to a methylbutadienyl side chain. The HAS biosynthesis begins with the synthesis of a tethered Trp-Ala dipeptide by the NRPS hasD. The 7-dimethylallyltryptophan synthase hasE then catalyzes the prenylation of the hasD-tethered tryptophan or the resulting tethered Trp-Ala dipeptide at the C-7 position of the indole moiety. HAS biosynthesis continues via tethered intermediates with the succesive actions of the cytochrome P450 monooxygenase hasH, the O- methyltransferase hasC, and the FAD-linked oxidoreductase hasG. The resulting O-methylated diketopiperazine is then released from hasD. Finally, three O-methylated diketopiperazine molecules assemble in a trimeric complex with Fe(III) to produce hexadehydro-astechrome.","FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS). SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms. These initial steps feature the priming of an unusual benzoic acid starter unit onto",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0071949; GO:0016491,GO:0016491,GO:0016491; GO:0071949,GO:0016491; GO:0050660,GO:0016491,GO:0016491,0.706,1.0,0.9573,0.706,0.706,5,0.8151,0.1705,no
HASG_ASPFC,B0XWK5,Protein2Text,Eukaryota,468,"FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of hexadehydro-astechrome (HAS), a tryptophan-derived iron(III)-complex that acts as a virulence factor in infected mice. Within the pathway, hasG converts the prenyl to a methylbutadienyl side chain. The HAS biosynthesis begins with the synthesis of a tethered Trp-Ala dipeptide by the NRPS hasD. The 7-dimethylallyltryptophan synthase hasE then catalyzes the prenylation of the hasD-tethered tryptophan or the resulting tethered Trp-Ala dipeptide at the C-7 position of the indole moiety. HAS biosynthesis continues via tethered intermediates with the succesive actions of the cytochrome P450 monooxygenase hasH, the O- methyltransferase hasC, and the FAD-linked oxidoreductase hasG. The resulting O-methylated diketopiperazine is then released from hasD. Finally, three O-methylated diketopiperazine molecules assemble in a trimeric complex with Fe(III) to produce hexadehydro-astechrome.","This protein is involved in the molecular function of oxidoreductase activity, specifically as a cytochrome P450 monooxygenase, which catalyzes the oxidation of a substrate using molecular oxygen. This process involves the reduction of the cytochrome P450 heme group to produce a reactive intermediate that can then attack the substrate. In this case, the protein is likely involved in the metabolism of a specific substrate, possibly a xenobiotic compound. The exact molecular function of this protein is not specified, but it is likely involved in the oxidation of a substrate, possibly as part of a larger metabolic pathway.",Maybe,No,Vague,No,Maybe,not-Yes,GO:0071949; GO:0016491,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.5751,0.5751,0.5751,0.5751,0.5751,5,0.5751,0.1705,no
HASG_ASPFC,B0XWK5,Reference,Eukaryota,468,"FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of hexadehydro-astechrome (HAS), a tryptophan-derived iron(III)-complex that acts as a virulence factor in infected mice. Within the pathway, hasG converts the prenyl to a methylbutadienyl side chain. The HAS biosynthesis begins with the synthesis of a tethered Trp-Ala dipeptide by the NRPS hasD. The 7-dimethylallyltryptophan synthase hasE then catalyzes the prenylation of the hasD-tethered tryptophan or the resulting tethered Trp-Ala dipeptide at the C-7 position of the indole moiety. HAS biosynthesis continues via tethered intermediates with the succesive actions of the cytochrome P450 monooxygenase hasH, the O- methyltransferase hasC, and the FAD-linked oxidoreductase hasG. The resulting O-methylated diketopiperazine is then released from hasD. Finally, three O-methylated diketopiperazine molecules assemble in a trimeric complex with Fe(III) to produce hexadehydro-astechrome.","FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of hexadehydro-astechrome (HAS), a tryptophan-derived iron(III)-complex that acts as a virulence factor in infected mice. Within the pathway, hasG converts the prenyl to a methylbutadienyl side chain. The HAS biosynthesis begins with the synthesis of a tethered Trp-Ala dipeptide by the NRPS hasD. The 7-dimethylallyltryptophan synthase hasE then catalyzes the prenylation of the hasD-tethered tryptophan or the resulting tethered Trp-Ala dipeptide at the C-7 position of the indole moiety. HAS biosynthesis continues via tethered intermediates with the succesive actions of the cytochrome P450 monooxygenase hasH, the O- methyltransferase hasC, and the FAD-linked oxidoreductase hasG. The resulting O-methylated diketopiperazine is then released from hasD. Finally, three O-methylated diketopiperazine molecules assemble in a trimeric complex with Fe(III) to produce hexadehydro-astechrome.",,,,,,,GO:0071949; GO:0016491,GO:0016491; GO:0050660,GO:0016491,GO:0016491; GO:0071949,GO:0016491; GO:0071949,GO:0016491,0.9573,0.706,1.0,1.0,0.706,5,0.8739,0.1705,no
HASC_ASPFC,B0XWK9,ESM2Text,Eukaryota,433,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of hexadehydro-astechrome (HAS), a tryptophan-derived iron(III)-complex that acts as a virulence factor in infected mice. Within the pathway, hasC, with the cytochrome P450 monooxygenase hasH and the FAD-linked oxidoreductase hasG, convert the hasE-prenylated Trp-Ala-dipeptide into an O-methylated diketopiperazine that is then released from the hasD NRPS. The HAS biosynthesis begins with the synthesis of a tethered Trp-Ala dipeptide by the NRPS hasD. The 7-dimethylallyltryptophan synthase hasE then catalyzes the prenylation of the hasD-tethered tryptophan or the resulting tethered Trp-Ala dipeptide at the C-7 position of the indole moiety. HAS biosynthesis continues via tethered intermediates with the succesive actions of the cytochrome P450 monooxygenase hasH, the O- methyltransferase hasC, and the FAD-linked oxidoreductase hasG. The resulting O-methylated diketopiperazine is then released from hasD. Finally, three O-methylated diketopiperazine molecules assemble in a trimeric complex with Fe(III) to produce hexadehydro-astechrome.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of asperlin, a polyketide showing anti-inflammatory, antitumor and antibiotic activities. The first step of the asperlin biosynthesis is the production of the intermediate 2,4,6-octatrienoic acid by the highly redusing polyketide synthase alnA with cleavage of the PKS product by the esterase alnB. 2,4,6-octatrienoic acid is further converted to asperlin via several steps involving the remaining enzymes from the cluster.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2652,no
HASC_ASPFC,B0XWK9,Prot2Text,Eukaryota,433,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of hexadehydro-astechrome (HAS), a tryptophan-derived iron(III)-complex that acts as a virulence factor in infected mice. Within the pathway, hasC, with the cytochrome P450 monooxygenase hasH and the FAD-linked oxidoreductase hasG, convert the hasE-prenylated Trp-Ala-dipeptide into an O-methylated diketopiperazine that is then released from the hasD NRPS. The HAS biosynthesis begins with the synthesis of a tethered Trp-Ala dipeptide by the NRPS hasD. The 7-dimethylallyltryptophan synthase hasE then catalyzes the prenylation of the hasD-tethered tryptophan or the resulting tethered Trp-Ala dipeptide at the C-7 position of the indole moiety. HAS biosynthesis continues via tethered intermediates with the succesive actions of the cytochrome P450 monooxygenase hasH, the O- methyltransferase hasC, and the FAD-linked oxidoreductase hasG. The resulting O-methylated diketopiperazine is then released from hasD. Finally, three O-methylated diketopiperazine molecules assemble in a trimeric complex with Fe(III) to produce hexadehydro-astechrome.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate tolerance, py",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2652,no
HASC_ASPFC,B0XWK9,ProtT3,Eukaryota,433,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of hexadehydro-astechrome (HAS), a tryptophan-derived iron(III)-complex that acts as a virulence factor in infected mice. Within the pathway, hasC, with the cytochrome P450 monooxygenase hasH and the FAD-linked oxidoreductase hasG, convert the hasE-prenylated Trp-Ala-dipeptide into an O-methylated diketopiperazine that is then released from the hasD NRPS. The HAS biosynthesis begins with the synthesis of a tethered Trp-Ala dipeptide by the NRPS hasD. The 7-dimethylallyltryptophan synthase hasE then catalyzes the prenylation of the hasD-tethered tryptophan or the resulting tethered Trp-Ala dipeptide at the C-7 position of the indole moiety. HAS biosynthesis continues via tethered intermediates with the succesive actions of the cytochrome P450 monooxygenase hasH, the O- methyltransferase hasC, and the FAD-linked oxidoreductase hasG. The resulting O-methylated diketopiperazine is then released from hasD. Finally, three O-methylated diketopiperazine molecules assemble in a trimeric complex with Fe(III) to produce hexadehydro-astechrome.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By similarity). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (By similarity). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the ter",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2652,no
HASC_ASPFC,B0XWK9,ProtTale,Eukaryota,433,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of hexadehydro-astechrome (HAS), a tryptophan-derived iron(III)-complex that acts as a virulence factor in infected mice. Within the pathway, hasC, with the cytochrome P450 monooxygenase hasH and the FAD-linked oxidoreductase hasG, convert the hasE-prenylated Trp-Ala-dipeptide into an O-methylated diketopiperazine that is then released from the hasD NRPS. The HAS biosynthesis begins with the synthesis of a tethered Trp-Ala dipeptide by the NRPS hasD. The 7-dimethylallyltryptophan synthase hasE then catalyzes the prenylation of the hasD-tethered tryptophan or the resulting tethered Trp-Ala dipeptide at the C-7 position of the indole moiety. HAS biosynthesis continues via tethered intermediates with the succesive actions of the cytochrome P450 monooxygenase hasH, the O- methyltransferase hasC, and the FAD-linked oxidoreductase hasG. The resulting O-methylated diketopiperazine is then released from hasD. Finally, three O-methylated diketopiperazine molecules assemble in a trimeric complex with Fe(III) to produce hexadehydro-astechrome.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the saturated C-C bonds",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2652,no
HASC_ASPFC,B0XWK9,Protein2Text,Eukaryota,433,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of hexadehydro-astechrome (HAS), a tryptophan-derived iron(III)-complex that acts as a virulence factor in infected mice. Within the pathway, hasC, with the cytochrome P450 monooxygenase hasH and the FAD-linked oxidoreductase hasG, convert the hasE-prenylated Trp-Ala-dipeptide into an O-methylated diketopiperazine that is then released from the hasD NRPS. The HAS biosynthesis begins with the synthesis of a tethered Trp-Ala dipeptide by the NRPS hasD. The 7-dimethylallyltryptophan synthase hasE then catalyzes the prenylation of the hasD-tethered tryptophan or the resulting tethered Trp-Ala dipeptide at the C-7 position of the indole moiety. HAS biosynthesis continues via tethered intermediates with the succesive actions of the cytochrome P450 monooxygenase hasH, the O- methyltransferase hasC, and the FAD-linked oxidoreductase hasG. The resulting O-methylated diketopiperazine is then released from hasD. Finally, three O-methylated diketopiperazine molecules assemble in a trimeric complex with Fe(III) to produce hexadehydro-astechrome.","The molecular function of this protein is an O-methyltransferase, specifically involved in the conversion of a precursor molecule to a product molecule by the transfer of a methyl group. More specifically, it is likely involved in the biosynthesis of a molecule, possibly a secondary metabolite, by catalyzing the methylation of a substrate molecule.  This protein is likely involved in the O-methylation of a molecule.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2652,no
HASC_ASPFC,B0XWK9,Reference,Eukaryota,433,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of hexadehydro-astechrome (HAS), a tryptophan-derived iron(III)-complex that acts as a virulence factor in infected mice. Within the pathway, hasC, with the cytochrome P450 monooxygenase hasH and the FAD-linked oxidoreductase hasG, convert the hasE-prenylated Trp-Ala-dipeptide into an O-methylated diketopiperazine that is then released from the hasD NRPS. The HAS biosynthesis begins with the synthesis of a tethered Trp-Ala dipeptide by the NRPS hasD. The 7-dimethylallyltryptophan synthase hasE then catalyzes the prenylation of the hasD-tethered tryptophan or the resulting tethered Trp-Ala dipeptide at the C-7 position of the indole moiety. HAS biosynthesis continues via tethered intermediates with the succesive actions of the cytochrome P450 monooxygenase hasH, the O- methyltransferase hasC, and the FAD-linked oxidoreductase hasG. The resulting O-methylated diketopiperazine is then released from hasD. Finally, three O-methylated diketopiperazine molecules assemble in a trimeric complex with Fe(III) to produce hexadehydro-astechrome.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of hexadehydro-astechrome (HAS), a tryptophan-derived iron(III)-complex that acts as a virulence factor in infected mice. Within the pathway, hasC, with the cytochrome P450 monooxygenase hasH and the FAD-linked oxidoreductase hasG, convert the hasE-prenylated Trp-Ala-dipeptide into an O-methylated diketopiperazine that is then released from the hasD NRPS. The HAS biosynthesis begins with the synthesis of a tethered Trp-Ala dipeptide by the NRPS hasD. The 7-dimethylallyltryptophan synthase hasE then catalyzes the prenylation of the hasD-tethered tryptophan or the resulting tethered Trp-Ala dipeptide at the C-7 position of the indole moiety. HAS biosynthesis continues via tethered intermediates with the succesive actions of the cytochrome P450 monooxygenase hasH, the O- methyltransferase hasC, and the FAD-linked oxidoreductase hasG. The resulting O-methylated diketopiperazine is then released from hasD. Finally, three O-methylated diketopiperazine molecules assemble in a trimeric complex with Fe(III) to produce hexadehydro-astechrome.",,,,,,,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2652,no
SPHE_ASPFC,B0XZV3,ESM2Text,Eukaryota,515,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of sphingofungins, bioactive molecules acting as sphingolipid inhibitors via inhibiting serine palmitoyl transferase (SPT). Within the pathway, sphE catalyzes the O- acetylation of the C-5 hydroxyl group of sphingofungin B to produce sphingofungin C. SphE can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Sphingofungin biosynthesis starts with the PKS sphB that produces an C18 polyketide precursor 3-hydroxyoctadeca-4,10- dienoyl-ACP containing one delta-6 desaturation and one delta-12 desaturation. The aminoacyl transferase sphA uses the sphB product to produce 3-keto-presphingofungin by adding an aminomalonate molecule. SphF then reduces the C-3 ketone of 3-keto-presphingofungin which leads to presphingofungin. The cytochrome P450 monooxygenase sphH converts presphingofungin into sphingofungin B1 which is further converted to sphingofungin B by the dioxygenase sphC. SphC is also able to convert presphingofungin into sphingofungin B2. The acetyltransferase sphE acetylates sphingofungin B to produce sphingofungin C, but can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Finally, sphingofungin C can be spontaneously converted into sphingofungin D.","O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Yes,Maybe,Yes,Yes,Yes,Yes,GO:0016746,GO:0016413,GO:0016413,GO:0016413,GO:0016407,GO:0016413,0.5794,0.5794,0.5794,0.729,0.5794,5,0.6093,0.2794,no
SPHE_ASPFC,B0XZV3,Prot2Text,Eukaryota,515,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of sphingofungins, bioactive molecules acting as sphingolipid inhibitors via inhibiting serine palmitoyl transferase (SPT). Within the pathway, sphE catalyzes the O- acetylation of the C-5 hydroxyl group of sphingofungin B to produce sphingofungin C. SphE can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Sphingofungin biosynthesis starts with the PKS sphB that produces an C18 polyketide precursor 3-hydroxyoctadeca-4,10- dienoyl-ACP containing one delta-6 desaturation and one delta-12 desaturation. The aminoacyl transferase sphA uses the sphB product to produce 3-keto-presphingofungin by adding an aminomalonate molecule. SphF then reduces the C-3 ketone of 3-keto-presphingofungin which leads to presphingofungin. The cytochrome P450 monooxygenase sphH converts presphingofungin into sphingofungin B1 which is further converted to sphingofungin B by the dioxygenase sphC. SphC is also able to convert presphingofungin into sphingofungin B2. The acetyltransferase sphE acetylates sphingofungin B to produce sphingofungin C, but can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Finally, sphingofungin C can be spontaneously converted into sphingofungin D.","Malonyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate tolerance, py",No,No,No,No,No,not-Yes,GO:0016746,GO:0016746,GO:0016747,GO:0016746,GO:0016746,GO:0016746,1.0,0.8416,1.0,1.0,1.0,5,0.9683,0.2794,no
SPHE_ASPFC,B0XZV3,ProtT3,Eukaryota,515,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of sphingofungins, bioactive molecules acting as sphingolipid inhibitors via inhibiting serine palmitoyl transferase (SPT). Within the pathway, sphE catalyzes the O- acetylation of the C-5 hydroxyl group of sphingofungin B to produce sphingofungin C. SphE can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Sphingofungin biosynthesis starts with the PKS sphB that produces an C18 polyketide precursor 3-hydroxyoctadeca-4,10- dienoyl-ACP containing one delta-6 desaturation and one delta-12 desaturation. The aminoacyl transferase sphA uses the sphB product to produce 3-keto-presphingofungin by adding an aminomalonate molecule. SphF then reduces the C-3 ketone of 3-keto-presphingofungin which leads to presphingofungin. The cytochrome P450 monooxygenase sphH converts presphingofungin into sphingofungin B1 which is further converted to sphingofungin B by the dioxygenase sphC. SphC is also able to convert presphingofungin into sphingofungin B2. The acetyltransferase sphE acetylates sphingofungin B to produce sphingofungin C, but can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Finally, sphingofungin C can be spontaneously converted into sphingofungin D.",O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylger,Yes,Maybe,Yes,Yes,Yes,Yes,GO:0016746,GO:0016413,GO:0016413,GO:0016407,GO:0016407,GO:0016407,0.5794,0.5794,0.729,0.729,0.729,5,0.6692,0.2794,no
SPHE_ASPFC,B0XZV3,ProtTale,Eukaryota,515,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of sphingofungins, bioactive molecules acting as sphingolipid inhibitors via inhibiting serine palmitoyl transferase (SPT). Within the pathway, sphE catalyzes the O- acetylation of the C-5 hydroxyl group of sphingofungin B to produce sphingofungin C. SphE can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Sphingofungin biosynthesis starts with the PKS sphB that produces an C18 polyketide precursor 3-hydroxyoctadeca-4,10- dienoyl-ACP containing one delta-6 desaturation and one delta-12 desaturation. The aminoacyl transferase sphA uses the sphB product to produce 3-keto-presphingofungin by adding an aminomalonate molecule. SphF then reduces the C-3 ketone of 3-keto-presphingofungin which leads to presphingofungin. The cytochrome P450 monooxygenase sphH converts presphingofungin into sphingofungin B1 which is further converted to sphingofungin B by the dioxygenase sphC. SphC is also able to convert presphingofungin into sphingofungin B2. The acetyltransferase sphE acetylates sphingofungin B to produce sphingofungin C, but can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Finally, sphingofungin C can be spontaneously converted into sphingofungin D.","Acyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016747,1.0,1.0,1.0,1.0,0.8416,5,0.9683,0.2794,no
SPHE_ASPFC,B0XZV3,Protein2Text,Eukaryota,515,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of sphingofungins, bioactive molecules acting as sphingolipid inhibitors via inhibiting serine palmitoyl transferase (SPT). Within the pathway, sphE catalyzes the O- acetylation of the C-5 hydroxyl group of sphingofungin B to produce sphingofungin C. SphE can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Sphingofungin biosynthesis starts with the PKS sphB that produces an C18 polyketide precursor 3-hydroxyoctadeca-4,10- dienoyl-ACP containing one delta-6 desaturation and one delta-12 desaturation. The aminoacyl transferase sphA uses the sphB product to produce 3-keto-presphingofungin by adding an aminomalonate molecule. SphF then reduces the C-3 ketone of 3-keto-presphingofungin which leads to presphingofungin. The cytochrome P450 monooxygenase sphH converts presphingofungin into sphingofungin B1 which is further converted to sphingofungin B by the dioxygenase sphC. SphC is also able to convert presphingofungin into sphingofungin B2. The acetyltransferase sphE acetylates sphingofungin B to produce sphingofungin C, but can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Finally, sphingofungin C can be spontaneously converted into sphingofungin D.","The molecular function of this protein is related to the metabolism of lipids, specifically as a fatty acid O-acetyltransferase, which is involved in the transfer of acetyl groups from acetyl-CoA to fatty acids. This protein is involved in the biosynthesis of fatty acids and their derivatives, which are essential components of cellular membranes and energy storage molecules. The protein is likely involved in the transfer of an acetyl group from acetyl-CoA to a fatty acid, resulting in the formation of a fatty acyl-CoA ester. This reaction is an important step in the biosynthesis of various fatty acid derivatives, such as fatty alcohols, wax esters, and triacylglycerols. The protein is also involved in the regulation of fatty acid metabolism, and its activity is likely influenced by various factors, such as the availability of substrates, the presence of inhibitors, and the expression of other genes involved in fatty acid metabolism. The protein is also involved in the biosynthesis of very long chain fatty acids, which are important components of cellular membranes and are involved in various cellular processes, such as signaling and gene regulation.

In summary, the molecular function of this protein is to catalyze the transfer of an acetyl group from acetyl-CoA to a fatty acid, resulting in the formation of a fatty acyl-CoA ester, and is involved in the biosynthesis of fatty acids and their derivatives, as well as the regulation of fatty acid metabolism.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016746,,,,,GO:0016747,,,,,0.8416,1,0.8416,0.2794,no
SPHE_ASPFC,B0XZV3,Reference,Eukaryota,515,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of sphingofungins, bioactive molecules acting as sphingolipid inhibitors via inhibiting serine palmitoyl transferase (SPT). Within the pathway, sphE catalyzes the O- acetylation of the C-5 hydroxyl group of sphingofungin B to produce sphingofungin C. SphE can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Sphingofungin biosynthesis starts with the PKS sphB that produces an C18 polyketide precursor 3-hydroxyoctadeca-4,10- dienoyl-ACP containing one delta-6 desaturation and one delta-12 desaturation. The aminoacyl transferase sphA uses the sphB product to produce 3-keto-presphingofungin by adding an aminomalonate molecule. SphF then reduces the C-3 ketone of 3-keto-presphingofungin which leads to presphingofungin. The cytochrome P450 monooxygenase sphH converts presphingofungin into sphingofungin B1 which is further converted to sphingofungin B by the dioxygenase sphC. SphC is also able to convert presphingofungin into sphingofungin B2. The acetyltransferase sphE acetylates sphingofungin B to produce sphingofungin C, but can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Finally, sphingofungin C can be spontaneously converted into sphingofungin D.","Acetyltransferase; part of the gene cluster that mediates the biosynthesis of sphingofungins, bioactive molecules acting as sphingolipid inhibitors via inhibiting serine palmitoyl transferase (SPT). Within the pathway, sphE catalyzes the O- acetylation of the C-5 hydroxyl group of sphingofungin B to produce sphingofungin C. SphE can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Sphingofungin biosynthesis starts with the PKS sphB that produces an C18 polyketide precursor 3-hydroxyoctadeca-4,10- dienoyl-ACP containing one delta-6 desaturation and one delta-12 desaturation. The aminoacyl transferase sphA uses the sphB product to produce 3-keto-presphingofungin by adding an aminomalonate molecule. SphF then reduces the C-3 ketone of 3-keto-presphingofungin which leads to presphingofungin. The cytochrome P450 monooxygenase sphH converts presphingofungin into sphingofungin B1 which is further converted to sphingofungin B by the dioxygenase sphC. SphC is also able to convert presphingofungin into sphingofungin B2. The acetyltransferase sphE acetylates sphingofungin B to produce sphingofungin C, but can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Finally, sphingofungin C can be spontaneously converted into sphingofungin D.",,,,,,,GO:0016746,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.729,0.729,0.729,0.729,0.729,5,0.729,0.2794,no
SPHC_ASPFC,B0XZV5,ESM2Text,Eukaryota,363,"Dioxygenase; part of the gene cluster that mediates the biosynthesis of sphingofungins, bioactive molecules acting as sphingolipid inhibitors via inhibiting serine palmitoyl transferase (SPT). Within the pathway, sphC catalyzes the hydrolxylation at C-4 to convert sphingofungin B1 into sphingofungin B as well as presphingofungin into sphingofungin B2. Sphingofungin biosynthesis starts with the PKS sphB that produces an C18 polyketide precursor 3-hydroxyoctadeca-4,10-dienoyl-ACP containing one delta-6 desaturation and one delta-12 desaturation. The aminoacyl transferase sphA uses the sphB product to produce 3-keto- presphingofungin by adding an aminomalonate molecule. SphF then reduces the C-3 ketone of 3-keto-presphingofungin which leads to presphingofungin. The cytochrome P450 monooxygenase sphH converts presphingofungin into sphingofungin B1 which is further converted to sphingofungin B by the dioxygenase sphC. SphC is also able to convert presphingofungin into sphingofungin B2. The acetyltransferase sphE acetylates sphingofungin B to produce sphingofungin C, but can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Finally, sphingofungin C can be spontaneously converted into sphingofungin D.","Dioxygenase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome monooxygenase P450 claM then catalyzes the dimerization of nataloe-emodin to cladofulvin.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0051213; GO:0046872,GO:0051213,GO:0051213,GO:0051213,GO:0051213,GO:0051213,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2382,no
SPHC_ASPFC,B0XZV5,Prot2Text,Eukaryota,363,"Dioxygenase; part of the gene cluster that mediates the biosynthesis of sphingofungins, bioactive molecules acting as sphingolipid inhibitors via inhibiting serine palmitoyl transferase (SPT). Within the pathway, sphC catalyzes the hydrolxylation at C-4 to convert sphingofungin B1 into sphingofungin B as well as presphingofungin into sphingofungin B2. Sphingofungin biosynthesis starts with the PKS sphB that produces an C18 polyketide precursor 3-hydroxyoctadeca-4,10-dienoyl-ACP containing one delta-6 desaturation and one delta-12 desaturation. The aminoacyl transferase sphA uses the sphB product to produce 3-keto- presphingofungin by adding an aminomalonate molecule. SphF then reduces the C-3 ketone of 3-keto-presphingofungin which leads to presphingofungin. The cytochrome P450 monooxygenase sphH converts presphingofungin into sphingofungin B1 which is further converted to sphingofungin B by the dioxygenase sphC. SphC is also able to convert presphingofungin into sphingofungin B2. The acetyltransferase sphE acetylates sphingofungin B to produce sphingofungin C, but can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Finally, sphingofungin C can be spontaneously converted into sphingofungin D.","Dioxygenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate tolerance, py",Yes,Yes,Yes,Yes,Yes,Yes,GO:0051213; GO:0046872,GO:0051213,GO:0051213,GO:0051213,GO:0051213,GO:0051213,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2382,no
SPHC_ASPFC,B0XZV5,ProtT3,Eukaryota,363,"Dioxygenase; part of the gene cluster that mediates the biosynthesis of sphingofungins, bioactive molecules acting as sphingolipid inhibitors via inhibiting serine palmitoyl transferase (SPT). Within the pathway, sphC catalyzes the hydrolxylation at C-4 to convert sphingofungin B1 into sphingofungin B as well as presphingofungin into sphingofungin B2. Sphingofungin biosynthesis starts with the PKS sphB that produces an C18 polyketide precursor 3-hydroxyoctadeca-4,10-dienoyl-ACP containing one delta-6 desaturation and one delta-12 desaturation. The aminoacyl transferase sphA uses the sphB product to produce 3-keto- presphingofungin by adding an aminomalonate molecule. SphF then reduces the C-3 ketone of 3-keto-presphingofungin which leads to presphingofungin. The cytochrome P450 monooxygenase sphH converts presphingofungin into sphingofungin B1 which is further converted to sphingofungin B by the dioxygenase sphC. SphC is also able to convert presphingofungin into sphingofungin B2. The acetyltransferase sphE acetylates sphingofungin B to produce sphingofungin C, but can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Finally, sphingofungin C can be spontaneously converted into sphingofungin D.",Fe(II)- and alpha-ketoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl,Yes,Maybe,Yes,Yes,Yes,Yes,GO:0051213; GO:0046872,GO:0016706; GO:0005506,GO:0016706; GO:0005506,GO:0016706,GO:0016706,GO:0016706,0.7588,0.7588,0.5293,0.5293,0.5293,5,0.6211,0.2382,no
SPHC_ASPFC,B0XZV5,ProtTale,Eukaryota,363,"Dioxygenase; part of the gene cluster that mediates the biosynthesis of sphingofungins, bioactive molecules acting as sphingolipid inhibitors via inhibiting serine palmitoyl transferase (SPT). Within the pathway, sphC catalyzes the hydrolxylation at C-4 to convert sphingofungin B1 into sphingofungin B as well as presphingofungin into sphingofungin B2. Sphingofungin biosynthesis starts with the PKS sphB that produces an C18 polyketide precursor 3-hydroxyoctadeca-4,10-dienoyl-ACP containing one delta-6 desaturation and one delta-12 desaturation. The aminoacyl transferase sphA uses the sphB product to produce 3-keto- presphingofungin by adding an aminomalonate molecule. SphF then reduces the C-3 ketone of 3-keto-presphingofungin which leads to presphingofungin. The cytochrome P450 monooxygenase sphH converts presphingofungin into sphingofungin B1 which is further converted to sphingofungin B by the dioxygenase sphC. SphC is also able to convert presphingofungin into sphingofungin B2. The acetyltransferase sphE acetylates sphingofungin B to produce sphingofungin C, but can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Finally, sphingofungin C can be spontaneously converted into sphingofungin D.",Involved in the conversion of cholesterol 24-monooxygenase to cholesterol 24-hydroxylase. Catalyzes the hydroxylation of cholesterol at the 24-methyl group.,No,No,No,No,Maybe,not-Yes,GO:0051213; GO:0046872,GO:0008395,GO:0008395,GO:0033781,GO:0033781,GO:0016705,0.4059,0.4059,0.3203,0.3203,0.483,5,0.3871,0.2382,no
SPHC_ASPFC,B0XZV5,Protein2Text,Eukaryota,363,"Dioxygenase; part of the gene cluster that mediates the biosynthesis of sphingofungins, bioactive molecules acting as sphingolipid inhibitors via inhibiting serine palmitoyl transferase (SPT). Within the pathway, sphC catalyzes the hydrolxylation at C-4 to convert sphingofungin B1 into sphingofungin B as well as presphingofungin into sphingofungin B2. Sphingofungin biosynthesis starts with the PKS sphB that produces an C18 polyketide precursor 3-hydroxyoctadeca-4,10-dienoyl-ACP containing one delta-6 desaturation and one delta-12 desaturation. The aminoacyl transferase sphA uses the sphB product to produce 3-keto- presphingofungin by adding an aminomalonate molecule. SphF then reduces the C-3 ketone of 3-keto-presphingofungin which leads to presphingofungin. The cytochrome P450 monooxygenase sphH converts presphingofungin into sphingofungin B1 which is further converted to sphingofungin B by the dioxygenase sphC. SphC is also able to convert presphingofungin into sphingofungin B2. The acetyltransferase sphE acetylates sphingofungin B to produce sphingofungin C, but can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Finally, sphingofungin C can be spontaneously converted into sphingofungin D.","This protein has a molecular function of being a dioxygenase, specifically involved in the degradation of the amino acid tyrosine. It catalyzes the conversion of tyrosine to 2-hydroxy-3,5- dihydroxyphenylglycine, a key step in the breakdown of tyrosine.",Maybe,Maybe,Yes,Yes,Maybe,not-Yes,GO:0051213; GO:0046872,GO:0051213,GO:0051213,,GO:0051213,GO:0003868,0.7088,0.7088,,0.7088,0.4705,4,0.6492,0.2382,no
SPHC_ASPFC,B0XZV5,Reference,Eukaryota,363,"Dioxygenase; part of the gene cluster that mediates the biosynthesis of sphingofungins, bioactive molecules acting as sphingolipid inhibitors via inhibiting serine palmitoyl transferase (SPT). Within the pathway, sphC catalyzes the hydrolxylation at C-4 to convert sphingofungin B1 into sphingofungin B as well as presphingofungin into sphingofungin B2. Sphingofungin biosynthesis starts with the PKS sphB that produces an C18 polyketide precursor 3-hydroxyoctadeca-4,10-dienoyl-ACP containing one delta-6 desaturation and one delta-12 desaturation. The aminoacyl transferase sphA uses the sphB product to produce 3-keto- presphingofungin by adding an aminomalonate molecule. SphF then reduces the C-3 ketone of 3-keto-presphingofungin which leads to presphingofungin. The cytochrome P450 monooxygenase sphH converts presphingofungin into sphingofungin B1 which is further converted to sphingofungin B by the dioxygenase sphC. SphC is also able to convert presphingofungin into sphingofungin B2. The acetyltransferase sphE acetylates sphingofungin B to produce sphingofungin C, but can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Finally, sphingofungin C can be spontaneously converted into sphingofungin D.","Dioxygenase; part of the gene cluster that mediates the biosynthesis of sphingofungins, bioactive molecules acting as sphingolipid inhibitors via inhibiting serine palmitoyl transferase (SPT). Within the pathway, sphC catalyzes the hydrolxylation at C-4 to convert sphingofungin B1 into sphingofungin B as well as presphingofungin into sphingofungin B2. Sphingofungin biosynthesis starts with the PKS sphB that produces an C18 polyketide precursor 3-hydroxyoctadeca-4,10-dienoyl-ACP containing one delta-6 desaturation and one delta-12 desaturation. The aminoacyl transferase sphA uses the sphB product to produce 3-keto- presphingofungin by adding an aminomalonate molecule. SphF then reduces the C-3 ketone of 3-keto-presphingofungin which leads to presphingofungin. The cytochrome P450 monooxygenase sphH converts presphingofungin into sphingofungin B1 which is further converted to sphingofungin B by the dioxygenase sphC. SphC is also able to convert presphingofungin into sphingofungin B2. The acetyltransferase sphE acetylates sphingofungin B to produce sphingofungin C, but can also convert sphingofungin B1 into sphingofungin C1 and sphingofungin B2 into sphingofungin C2. Finally, sphingofungin C can be spontaneously converted into sphingofungin D.",,,,,,,GO:0051213; GO:0046872,GO:0051213,GO:0051213,GO:0051213,GO:0051213,GO:0051213,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2382,no
RBDB_ASPFC,B0Y8W1,ESM2Text,Eukaryota,272,Rhomboid protease that catalyzes intramembrane proteolysis. Required for transcription factor srbA activation by mediating its release from the membrane and thereby regulating its activity under hypoxic conditions. Essential for iron homeostasis and resistance to azoles such as voriconazole. Required for virulence in murine models of invasive pulmonary aspergillosis (IPA).,Probable serine protease.,Vague,Vague,Maybe,Maybe,Vague,not-Yes,GO:0004252,GO:0008236,GO:0008236,GO:0008236,GO:0008236,GO:0008236,0.8276,0.8276,0.8276,0.8276,0.8276,5,0.8276,0.6959,yes
RBDB_ASPFC,B0Y8W1,Prot2Text,Eukaryota,272,Rhomboid protease that catalyzes intramembrane proteolysis. Required for transcription factor srbA activation by mediating its release from the membrane and thereby regulating its activity under hypoxic conditions. Essential for iron homeostasis and resistance to azoles such as voriconazole. Required for virulence in murine models of invasive pulmonary aspergillosis (IPA).,Probable serine protease.,Vague,Vague,Maybe,Maybe,Vague,not-Yes,GO:0004252,GO:0008236,GO:0008236,GO:0008236,GO:0008236,GO:0008236,0.8276,0.8276,0.8276,0.8276,0.8276,5,0.8276,0.6959,yes
RBDB_ASPFC,B0Y8W1,ProtT3,Eukaryota,272,Rhomboid protease that catalyzes intramembrane proteolysis. Required for transcription factor srbA activation by mediating its release from the membrane and thereby regulating its activity under hypoxic conditions. Essential for iron homeostasis and resistance to azoles such as voriconazole. Required for virulence in murine models of invasive pulmonary aspergillosis (IPA).,"Probable serine protease. Golgi apparatus membrane; Multi- pass membrane protein Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. Belongs to the peptidase S54 family",Vague,Vague,Maybe,Maybe,Vague,not-Yes,GO:0004252,GO:0004252,GO:0004252,GO:0004252,GO:0004252,GO:0004252,1.0,1.0,1.0,1.0,1.0,5,1.0,0.6959,yes
RBDB_ASPFC,B0Y8W1,ProtTale,Eukaryota,272,Rhomboid protease that catalyzes intramembrane proteolysis. Required for transcription factor srbA activation by mediating its release from the membrane and thereby regulating its activity under hypoxic conditions. Essential for iron homeostasis and resistance to azoles such as voriconazole. Required for virulence in murine models of invasive pulmonary aspergillosis (IPA).,Probable rhomboid-type serine protease that catalyzes intramembrane proteolysis.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004252,GO:0004252,GO:0004252,GO:0004252,GO:0004252,GO:0004252,1.0,1.0,1.0,1.0,1.0,5,1.0,0.6959,yes
RBDB_ASPFC,B0Y8W1,Protein2Text,Eukaryota,272,Rhomboid protease that catalyzes intramembrane proteolysis. Required for transcription factor srbA activation by mediating its release from the membrane and thereby regulating its activity under hypoxic conditions. Essential for iron homeostasis and resistance to azoles such as voriconazole. Required for virulence in murine models of invasive pulmonary aspergillosis (IPA).,The molecular function of this protein is a rhomboid-type aspartic protease.,Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0004252,GO:0008233,,,,GO:0004252,0.6551,,,,1.0,2,0.8276,0.6959,yes
RBDB_ASPFC,B0Y8W1,Reference,Eukaryota,272,Rhomboid protease that catalyzes intramembrane proteolysis. Required for transcription factor srbA activation by mediating its release from the membrane and thereby regulating its activity under hypoxic conditions. Essential for iron homeostasis and resistance to azoles such as voriconazole. Required for virulence in murine models of invasive pulmonary aspergillosis (IPA).,Rhomboid protease that catalyzes intramembrane proteolysis. Required for transcription factor srbA activation by mediating its release from the membrane and thereby regulating its activity under hypoxic conditions. Essential for iron homeostasis and resistance to azoles such as voriconazole. Required for virulence in murine models of invasive pulmonary aspergillosis (IPA).,,,,,,,GO:0004252,GO:0004252,GO:0004252,GO:0004252,GO:0004252,GO:0004252,1.0,1.0,1.0,1.0,1.0,5,1.0,0.6959,yes
DOHCE_PARG4,B1G5Y9,ESM2Text,Bacteria,310,"Catalyzes the condensation of 3,5-dioxohexanoate and acetyl- CoA, forming acetoacetate and acetoacetyl-CoA. May be involved in fatty acid biosynthesis rescue via triacetic acid lactone.",Involved in the anaerobic fermentation of lysine. Catalyzes the reversible reaction between 3-keto-5-aminobutyrate (KABB) and acetyl-CoA to form beta-aminobutyrate (ABA) and acetoacetate. It can also use beta-aminobutyrate and acetoacetate as substrates.,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0043720; GO:0046872,GO:0008410,GO:0008260,GO:0008410,GO:0008415,GO:0008260,0.3006,0.2554,0.3006,0.5281,0.2554,5,0.328,0.3446,no
DOHCE_PARG4,B1G5Y9,Prot2Text,Bacteria,310,"Catalyzes the condensation of 3,5-dioxohexanoate and acetyl- CoA, forming acetoacetate and acetoacetyl-CoA. May be involved in fatty acid biosynthesis rescue via triacetic acid lactone.","Involved in the anaerobic fermentation of lysine. Catalyzes the reversible reaction between 3-keto-5-aminohexanoate (KAH) and acetyl-CoA to form 3-aminobutyryl-CoA and acetoacetate. The reaction involves the deprotonation of KAH, the nucleophilic addition onto acetyl-CoA and the intramolecular transfer of the CoA moiety. It can also use 2-formylglycine (fGly) and homocysteine (serine).",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0043720; GO:0046872,GO:0008410,GO:0008410,GO:0008260,GO:0008410,GO:0008410,0.3006,0.3006,0.2554,0.3006,0.3006,5,0.2916,0.3446,no
DOHCE_PARG4,B1G5Y9,ProtT3,Bacteria,310,"Catalyzes the condensation of 3,5-dioxohexanoate and acetyl- CoA, forming acetoacetate and acetoacetyl-CoA. May be involved in fatty acid biosynthesis rescue via triacetic acid lactone.",Belongs to the LacAB/RpiB family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0043720; GO:0046872,,,,,,,,,,,0,,0.3446,no
DOHCE_PARG4,B1G5Y9,ProtTale,Bacteria,310,"Catalyzes the condensation of 3,5-dioxohexanoate and acetyl- CoA, forming acetoacetate and acetoacetyl-CoA. May be involved in fatty acid biosynthesis rescue via triacetic acid lactone.",Catalyzes the reversible isomerization of L-ribulose 5-phosphate to D-xylulose 5-phosphate.,No,No,No,No,No,not-Yes,GO:0043720; GO:0046872,GO:0008742,GO:0004751,GO:0004751,GO:0004751,GO:0004751,0.1628,0.1628,0.1628,0.1628,0.1628,5,0.1628,0.3446,no
DOHCE_PARG4,B1G5Y9,Protein2Text,Bacteria,310,"Catalyzes the condensation of 3,5-dioxohexanoate and acetyl- CoA, forming acetoacetate and acetoacetyl-CoA. May be involved in fatty acid biosynthesis rescue via triacetic acid lactone.","This protein is a part of a bacterial enzyme that catalyzes a reaction in the pentose phosphate pathway, which is a metabolic pathway that generates NADPH and pentoses from glucose-6-phosphate. The molecular function of this protein is likely to be a catalytic role in the conversion of 6-phosphogluconolactone to 6-phosphogluconate.",No,No,No,No,No,not-Yes,GO:0043720; GO:0046872,GO:0017057,GO:0004349,GO:0017057,GO:0017057,GO:0017057,0.1628,0.2137,0.1628,0.1628,0.1628,5,0.173,0.3446,no
DOHCE_PARG4,B1G5Y9,Reference,Bacteria,310,"Catalyzes the condensation of 3,5-dioxohexanoate and acetyl- CoA, forming acetoacetate and acetoacetyl-CoA. May be involved in fatty acid biosynthesis rescue via triacetic acid lactone.","Catalyzes the condensation of 3,5-dioxohexanoate and acetyl- CoA, forming acetoacetate and acetoacetyl-CoA. May be involved in fatty acid biosynthesis rescue via triacetic acid lactone.",,,,,,,GO:0043720; GO:0046872,GO:0008415,GO:0008415,GO:0008410,GO:0016746,GO:0003985,0.5281,0.5281,0.3006,0.5281,0.3358,5,0.4441,0.3446,no
M2355_MYCA9,B1MB15,ESM2Text,Bacteria,552,"Exhibits ATP hydrolysis activity and contributes to macrolide resistance by ribosome protection. Can also hydrolyze GTP, TTP and CTP but to a lesser extent than ATP. In vitro, rescues the transcription and translation activities affected by macrolides. Increased expression correlates with increased resistance to clarithromycin, one of the main drugs used to treat M.abscessus.","Divisome component that gates the progression of the 70S ribosomal initiation complex (IC, containing tRNA(fMet) in the P-site) into the elongation cycle by using a mechanism sensitive to the ATP/ADP ratio. Binds to the 70S ribosome E-site where it modulates the state of the translating ribosome during subunit translocation. ATP hydrolysis probably frees it from the ribosome, which can enter the elongation phase.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887,GO:0005524; GO:0016887,GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524; GO:0003723,GO:0016887; GO:0005524,1.0,0.6869,1.0,0.8331,1.0,5,0.904,0.427,no
M2355_MYCA9,B1MB15,Prot2Text,Bacteria,552,"Exhibits ATP hydrolysis activity and contributes to macrolide resistance by ribosome protection. Can also hydrolyze GTP, TTP and CTP but to a lesser extent than ATP. In vitro, rescues the transcription and translation activities affected by macrolides. Increased expression correlates with increased resistance to clarithromycin, one of the main drugs used to treat M.abscessus.","A translation factor that gates the progression of the 70S ribosomal initiation complex (IC, containing tRNA(fMet) in the P-site) into the translation elongation cycle by using a mechanism sensitive to the ATP/ADP ratio. Binds to the 70S ribosome E-site where it modulates the state of the translating ribosome during subunit translocation. ATP hydrolysis probably frees it from the ribosome, which can enter the elongation phase.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887,GO:0003743; GO:0005524,GO:0003743; GO:0005524,GO:0003746; GO:0005524,GO:0016887; GO:0003746,GO:0003746; GO:0005524,0.575,0.575,0.575,0.5593,0.575,5,0.5719,0.427,no
M2355_MYCA9,B1MB15,ProtT3,Bacteria,552,"Exhibits ATP hydrolysis activity and contributes to macrolide resistance by ribosome protection. Can also hydrolyze GTP, TTP and CTP but to a lesser extent than ATP. In vitro, rescues the transcription and translation activities affected by macrolides. Increased expression correlates with increased resistance to clarithromycin, one of the main drugs used to treat M.abscessus.",Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0016887,GO:0005524,GO:0016887,GO:0016887,GO:0016887,GO:0005524; GO:0016887,0.6869,0.6869,0.6869,0.6869,1.0,5,0.7495,0.427,no
M2355_MYCA9,B1MB15,ProtTale,Bacteria,552,"Exhibits ATP hydrolysis activity and contributes to macrolide resistance by ribosome protection. Can also hydrolyze GTP, TTP and CTP but to a lesser extent than ATP. In vitro, rescues the transcription and translation activities affected by macrolides. Increased expression correlates with increased resistance to clarithromycin, one of the main drugs used to treat M.abscessus.","An ATP-dependent protease that mediates the degradation of non-native proteins in the mitochondrial matrix, with natural substrate specificity.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016887,GO:0004176,GO:0004176; GO:0005524,GO:0004176,GO:0004176,GO:0004176,0.3063,0.7117,0.3063,0.3063,0.3063,5,0.3874,0.427,no
M2355_MYCA9,B1MB15,Protein2Text,Bacteria,552,"Exhibits ATP hydrolysis activity and contributes to macrolide resistance by ribosome protection. Can also hydrolyze GTP, TTP and CTP but to a lesser extent than ATP. In vitro, rescues the transcription and translation activities affected by macrolides. Increased expression correlates with increased resistance to clarithromycin, one of the main drugs used to treat M.abscessus.","The molecular function of this protein is not specified in the provided text. However, based on its name and the context, it can be inferred that this protein is a part of a larger molecular complex involved in DNA replication. 

Given the name ""RecA protein"" and the fact that it is associated with the term ""DNA replication"", it is likely that this protein is involved in homologous recombination and DNA repair. RecA protein is a key enzyme in the bacterial RecF pathway of homologous recombination, which plays a central role in DNA repair and genetic recombination. 

Therefore, the molecular function of this protein is likely to be involved in DNA recombination, repair, and replication. 

However, to confirm this, more detailed information about the protein's function and its interactions with other molecules would be necessary.",No,No,Vague,No,No,not-Yes,GO:0005524; GO:0016887,,GO:0005524; GO:0003697,,,GO:0008094; GO:0005524,,0.5621,,,0.6748,2,0.6184,0.427,no
M2355_MYCA9,B1MB15,Reference,Bacteria,552,"Exhibits ATP hydrolysis activity and contributes to macrolide resistance by ribosome protection. Can also hydrolyze GTP, TTP and CTP but to a lesser extent than ATP. In vitro, rescues the transcription and translation activities affected by macrolides. Increased expression correlates with increased resistance to clarithromycin, one of the main drugs used to treat M.abscessus.","Exhibits ATP hydrolysis activity and contributes to macrolide resistance by ribosome protection. Can also hydrolyze GTP, TTP and CTP but to a lesser extent than ATP. In vitro, rescues the transcription and translation activities affected by macrolides. Increased expression correlates with increased resistance to clarithromycin, one of the main drugs used to treat M.abscessus.",,,,,,,GO:0005524; GO:0016887,GO:0016887,GO:0016887; GO:0003924,GO:0016887,GO:0016887,GO:0016887,0.6869,0.6945,0.6869,0.6869,0.6869,5,0.6884,0.427,no
LP9C_PODAN,B2AUV0,ESM2Text,Eukaryota,287,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable).","Involved in degradation of lignin. Catalyzes the cleavage of the monolignol-derived side chains of lignin, generating a single, highly oxygenated monolignol product. Activity on lignin is rate-limiting for the biotrophic growth of Trichobrasillus sp.",No,No,No,No,No,not-Yes,GO:0046872; GO:0004497,,,,,,,,,,,0,,0.2244,no
LP9C_PODAN,B2AUV0,Prot2Text,Eukaryota,287,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable).",Catalyzes the oxidation of primary alcohols including methanol.,No,No,No,No,No,not-Yes,GO:0046872; GO:0004497,GO:0004030,GO:0004030,GO:0016614,GO:0016614,GO:0016614,0.351,0.351,0.483,0.483,0.483,5,0.4302,0.2244,no
LP9C_PODAN,B2AUV0,ProtT3,Eukaryota,287,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable).","Glycoside hydrolase that cleaves the beta-1,4 glycosidic bond of xyloglucan. Secreted. Belongs to the glycosyl hydrolase 65 family",No,No,No,No,No,not-Yes,GO:0046872; GO:0004497,GO:0004553,GO:0004553,GO:0004553,GO:0004553,GO:0016798,0.2538,0.2538,0.2538,0.2538,0.3023,5,0.2635,0.2244,no
LP9C_PODAN,B2AUV0,ProtTale,Eukaryota,287,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable).","Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0004497,GO:0016491; GO:0005507,GO:0016491; GO:0005507,GO:0004497,GO:0004497; GO:0005507,GO:0016491; GO:0005507,0.7926,0.7926,0.7088,0.8854,0.7926,5,0.7944,0.2244,no
LP9C_PODAN,B2AUV0,Protein2Text,Eukaryota,287,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable).","The molecular function of this protein is L-ascorbate oxidase activity. It is involved in the oxidation of L-ascorbate to dehydro-L-ascorbate. This process is part of the ascorbate-glutathione cycle, which is a crucial antioxidant defense mechanism in plants. The protein is also involved in the degradation of cellulose. 
It catalyzes the oxidation of the C2 and C3 hydroxyl groups of L-ascorbate to form dehydro-L-ascorbate. The ascorbate-glutathione cycle is an important antioxidant defense mechanism in plants, helping to protect the cell against oxidative damage by reactive oxygen species (ROS). The enzyme is also involved in the degradation of cellulose.
It is a copper-containing enzyme. The active site contains a pair of copper atoms that are coordinated to a tyrosine residue and a histidine residue. The copper atoms are in a cupric oxidation state, which is essential for the enzyme's activity. The reaction mechanism involves the transfer of electrons from the ascorbate to the copper atoms, resulting in the oxidation of ascorbate and the reduction of copper to cuprous oxide.
The protein has a high affinity for L-ascorbate and can oxidize it at a high rate. It is also able to oxidize other polyols, such as erythritol and ribitol, but at a lower rate. The enzyme is specific for L-ascorbate and does not oxidize D-ascorbate.
The protein is involved in plant defense against pathogens. It is up-regulated in response to infection and plays a role in the defense response by producing reactive oxygen species (ROS) that help to eliminate the invading pathogen.
The protein is also involved in plant senescence. It is up-regulated during senescence and plays a role in the degradation of cellulose, which is essential for the breakdown of plant biomass.
The protein is a member of the family of copper-containing oxidases. It is closely related to other members of this family, including the ascorbate oxidases from wheat and rice. The protein has a high degree of sequence similarity to these enzymes, suggesting that they have similar functions.
The protein has a number of potential applications. It can be used as a biocatalyst for the oxidation of L-ascorbate, which is an important industrial process. It can also be used as a tool for the degradation of cellulose, which is essential for the production of biofu",No,No,No,No,No,not-Yes,GO:0046872; GO:0004497,GO:0008447,GO:0008447; GO:0005507,GO:0008447; GO:0005507,GO:0008447,GO:0008447,0.351,0.6264,0.6264,0.351,0.351,5,0.4612,0.2244,no
LP9C_PODAN,B2AUV0,Reference,Eukaryota,287,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable).","Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products (Probable). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (Probable).",,,,,,,GO:0046872; GO:0004497,GO:0016491,GO:0016491; GO:0005507,GO:0004497; GO:0005507,GO:0016491,GO:0016491,0.5957,0.7926,0.8854,0.5957,0.5957,5,0.693,0.2244,no
WCLR_ECOLX,B5T072,ESM2Text,Bacteria,387,"Involved in the biosynthesis of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of galactose from UDP-galactose to GlcNAc-undecaprenyl diphosphate via an alpha1,3- linkage. Has strict substrate specificity.",Involved in the production of the exopolysaccharide (EPS) component of the extracellular matrix during biofilm formation. EPS is responsible for the adhesion of chains of cells into bundles. Required for growth on N-acetylglucosamine (GlcNAc) and galactose-containing substrates.,No,No,Maybe,No,Maybe,not-Yes,GO:0016757,,,,,,,,,,,0,,0.6234,yes
WCLR_ECOLX,B5T072,Prot2Text,Bacteria,387,"Involved in the biosynthesis of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of galactose from UDP-galactose to GlcNAc-undecaprenyl diphosphate via an alpha1,3- linkage. Has strict substrate specificity.","Involved in the biosynthesis of the exopolysaccharide acetan, a water-soluble polysaccharide involved in production of bacterial cellulose (BC).",No,Maybe,Maybe,Maybe,Vague,not-Yes,GO:0016757,,,,,,,,,,,0,,0.6234,yes
WCLR_ECOLX,B5T072,ProtT3,Bacteria,387,"Involved in the biosynthesis of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of galactose from UDP-galactose to GlcNAc-undecaprenyl diphosphate via an alpha1,3- linkage. Has strict substrate specificity.",Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016757,,GO:0016757,,GO:0016757,GO:0016757,,1.0,,1.0,1.0,3,1.0,0.6234,yes
WCLR_ECOLX,B5T072,ProtTale,Bacteria,387,"Involved in the biosynthesis of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of galactose from UDP-galactose to GlcNAc-undecaprenyl diphosphate via an alpha1,3- linkage. Has strict substrate specificity.",Required for the biosynthesis of type 1 capsular polysaccharide.,Maybe,Maybe,Maybe,Yes,Maybe,not-Yes,GO:0016757,,,,,,,,,,,0,,0.6234,yes
WCLR_ECOLX,B5T072,Protein2Text,Bacteria,387,"Involved in the biosynthesis of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of galactose from UDP-galactose to GlcNAc-undecaprenyl diphosphate via an alpha1,3- linkage. Has strict substrate specificity.","The molecular function of this protein is a sugar transferase, specifically involved in the biosynthesis of a type of sugar molecule. More specifically, it is a glycosyltransferase that catalyzes the transfer of a sugar molecule from a donor to an acceptor molecule. In this case, it is involved in the biosynthesis of a complex sugar molecule, likely involved in cell wall or membrane synthesis. 

In more detail, the protein is involved in the synthesis of a type of sugar molecule, likely a polysaccharide, which is an important component of the cell wall or membrane. The protein catalyzes the transfer of a sugar molecule from a donor molecule to an acceptor molecule, resulting in the formation of a new glycosidic bond. This process is essential for the biosynthesis of the sugar molecule, and is likely to be involved in the regulation of cell growth and development. 

The exact molecular function of this protein is not explicitly stated, but it is likely to be involved in the synthesis of a specific type of sugar molecule, such as a polysaccharide or a glycolipid. The protein may be involved in the transfer of a sugar molecule from a donor to an acceptor molecule, or in the synthesis of a sugar molecule from a simpler precursor molecule. Further research would be needed to determine the exact molecular function of this protein. 

It is worth noting that the protein is involved in the biosynthesis of a sugar molecule, which is a complex process that involves multiple enzymes and molecules. The protein is likely to be one of many enzymes involved in this process, and its function may be regulated by other enzymes or molecules. Further research would be needed to determine the exact role of this protein in the biosynthesis of sugar molecules. 

In summary, the molecular function of this protein is likely to be a sugar transferase, involved in the biosynthesis of a complex sugar molecule, such as a polysaccharide or glycolipid. The protein may be involved in the transfer of a sugar molecule from a donor to an acceptor molecule, or in the synthesis of a sugar molecule from a simpler precursor molecule. Further research would be needed to determine the exact molecular function of this protein. 

Please note that the information provided is based on the assumption that the protein is a glycosyltransferase, which is a common function for proteins with this name. However, without further information, it is impossible to determine the exact molecular function of this protein.",Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,1.0,1.0,1.0,1.0,1.0,5,1.0,0.6234,yes
WCLR_ECOLX,B5T072,Reference,Bacteria,387,"Involved in the biosynthesis of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of galactose from UDP-galactose to GlcNAc-undecaprenyl diphosphate via an alpha1,3- linkage. Has strict substrate specificity.","Involved in the biosynthesis of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of galactose from UDP-galactose to GlcNAc-undecaprenyl diphosphate via an alpha1,3- linkage. Has strict substrate specificity.",,,,,,,GO:0016757,GO:0008378,GO:0008378,GO:0008378,GO:0008378,GO:0008378,0.729,0.729,0.729,0.729,0.729,5,0.729,0.6234,yes
GNNB_ACIF2,B7JA35,ESM2Text,Bacteria,369,"Aminotranferase involved in the synthesis of 2,3-diamino-2,3- dideoxy-D-glucopyranose (GlcN3N), which is a component of lipid A in some species. Catalyzes the amination of UDP-2- acetamido-3-dehydro-2-deoxy-alpha-D-glucopyranose (UDP-3-oxo-GlcNAc) to UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose (UDP- GlcNAc3N), using L-glutamate as the amine donor. Other amine donors, such as alanine and glutamine, can substitute for glutamate, but product formation is slower.","May form, with DnrI, a two-component regulatory system for daunorubicin biosynthesis genes. Together with DnrJ may also regulate the synthesis of DnrA.",No,No,No,No,No,not-Yes,GO:0030170; GO:0008483,,,,,,,,,,,0,,0.1576,no
GNNB_ACIF2,B7JA35,Prot2Text,Bacteria,369,"Aminotranferase involved in the synthesis of 2,3-diamino-2,3- dideoxy-D-glucopyranose (GlcN3N), which is a component of lipid A in some species. Catalyzes the amination of UDP-2- acetamido-3-dehydro-2-deoxy-alpha-D-glucopyranose (UDP-3-oxo-GlcNAc) to UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose (UDP- GlcNAc3N), using L-glutamate as the amine donor. Other amine donors, such as alanine and glutamine, can substitute for glutamate, but product formation is slower.","Catalyzes the synthesis of dTDP-4-amino-4,6-dideoxy-D-galactose (dTDP-Fuc4N) from dTDP-4-keto-6-deoxy-D-glucose (dTDP-D-Glc4O) and L-glutamate.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0030170; GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.6936,0.6936,0.6936,0.6936,0.6936,5,0.6936,0.1576,no
GNNB_ACIF2,B7JA35,ProtT3,Bacteria,369,"Aminotranferase involved in the synthesis of 2,3-diamino-2,3- dideoxy-D-glucopyranose (GlcN3N), which is a component of lipid A in some species. Catalyzes the amination of UDP-2- acetamido-3-dehydro-2-deoxy-alpha-D-glucopyranose (UDP-3-oxo-GlcNAc) to UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose (UDP- GlcNAc3N), using L-glutamate as the amine donor. Other amine donors, such as alanine and glutamine, can substitute for glutamate, but product formation is slower.","Involved in the biosynthesis of the lipooligosaccharide (LOS) that plays a major role in virulence. Catalyzes the last step in LOS biosynthesis, the transfer of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to the lipid carrier undecaprenyl phosphate (C55-P). Belongs to the DegT/DnrJ/EryC1 family",Maybe,No,Maybe,No,No,not-Yes,GO:0030170; GO:0008483,GO:0008375,GO:0008375,GO:0008375,GO:0008375,GO:0008375,0.26,0.26,0.26,0.26,0.26,5,0.26,0.1576,no
GNNB_ACIF2,B7JA35,ProtTale,Bacteria,369,"Aminotranferase involved in the synthesis of 2,3-diamino-2,3- dideoxy-D-glucopyranose (GlcN3N), which is a component of lipid A in some species. Catalyzes the amination of UDP-2- acetamido-3-dehydro-2-deoxy-alpha-D-glucopyranose (UDP-3-oxo-GlcNAc) to UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose (UDP- GlcNAc3N), using L-glutamate as the amine donor. Other amine donors, such as alanine and glutamine, can substitute for glutamate, but product formation is slower.","Catalyzes the conversion of dTDP-4-dehydro-6-deoxy-D-mannose to dTDP-4-amino-4,6-dideoxy-D-glucose.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0030170; GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.6936,0.6936,0.6936,0.6936,0.6936,5,0.6936,0.1576,no
GNNB_ACIF2,B7JA35,Protein2Text,Bacteria,369,"Aminotranferase involved in the synthesis of 2,3-diamino-2,3- dideoxy-D-glucopyranose (GlcN3N), which is a component of lipid A in some species. Catalyzes the amination of UDP-2- acetamido-3-dehydro-2-deoxy-alpha-D-glucopyranose (UDP-3-oxo-GlcNAc) to UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose (UDP- GlcNAc3N), using L-glutamate as the amine donor. Other amine donors, such as alanine and glutamine, can substitute for glutamate, but product formation is slower.","This protein is a transferase, specifically a transketolase that catalyzes the transfer of a ketol group from one sugar to another.",No,No,No,No,No,not-Yes,GO:0030170; GO:0008483,GO:0004802,GO:0004802,GO:0004802,GO:0004802,GO:0004802,0.3366,0.3366,0.3366,0.3366,0.3366,5,0.3366,0.1576,no
GNNB_ACIF2,B7JA35,Reference,Bacteria,369,"Aminotranferase involved in the synthesis of 2,3-diamino-2,3- dideoxy-D-glucopyranose (GlcN3N), which is a component of lipid A in some species. Catalyzes the amination of UDP-2- acetamido-3-dehydro-2-deoxy-alpha-D-glucopyranose (UDP-3-oxo-GlcNAc) to UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose (UDP- GlcNAc3N), using L-glutamate as the amine donor. Other amine donors, such as alanine and glutamine, can substitute for glutamate, but product formation is slower.","Aminotranferase involved in the synthesis of 2,3-diamino-2,3- dideoxy-D-glucopyranose (GlcN3N), which is a component of lipid A in some species. Catalyzes the amination of UDP-2- acetamido-3-dehydro-2-deoxy-alpha-D-glucopyranose (UDP-3-oxo-GlcNAc) to UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucopyranose (UDP- GlcNAc3N), using L-glutamate as the amine donor. Other amine donors, such as alanine and glutamine, can substitute for glutamate, but product formation is slower.",,,,,,,GO:0030170; GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.6936,0.6936,0.6936,0.6936,0.6936,5,0.6936,0.1576,no
TSTM_TALSN,B8MKZ6,ESM2Text,Eukaryota,252,"Hydrolase; part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. Within the pathway, phiM releases the C12-fatty acyl chain from phiA. The pathway begins with the highly reducing polyketide synthase tstA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase tstM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) tstJ and the alkylcitrate dehydratase (ACDH) tstI then give rise to decarboxylated monomeric anhydrides by coupling the C12-fatty acyl chain with oxalacetic acid. The cyclase tstC is responsible for the dimerization of the monomeric anhydrides which leads to the production of prephomoidride that contains the characteristic bicyclo[4.3.1]deca-1,6-diene system of phomoidrides. Iterative oxidation catalyzed by the alpha-ketoglutarate-dependent dioxygenase tstK produced then phomoidride A. Finally, the methyltransferase tstE converts phomoidride A to phomoidride B via an acetalization reaction. The phosphatidylethanolamine-binding protein tstB and tstN are not essential for dimerization and their functions have still to be determined.","Hydrolase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Yes,Yes,Maybe,Yes,Yes,Yes,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016787,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5472,yes
TSTM_TALSN,B8MKZ6,Prot2Text,Eukaryota,252,"Hydrolase; part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. Within the pathway, phiM releases the C12-fatty acyl chain from phiA. The pathway begins with the highly reducing polyketide synthase tstA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase tstM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) tstJ and the alkylcitrate dehydratase (ACDH) tstI then give rise to decarboxylated monomeric anhydrides by coupling the C12-fatty acyl chain with oxalacetic acid. The cyclase tstC is responsible for the dimerization of the monomeric anhydrides which leads to the production of prephomoidride that contains the characteristic bicyclo[4.3.1]deca-1,6-diene system of phomoidrides. Iterative oxidation catalyzed by the alpha-ketoglutarate-dependent dioxygenase tstK produced then phomoidride A. Finally, the methyltransferase tstE converts phomoidride A to phomoidride B via an acetalization reaction. The phosphatidylethanolamine-binding protein tstB and tstN are not essential for dimerization and their functions have still to be determined.",Serine hydrolase of unknown specificity.,Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787,GO:0017171,GO:0017171,GO:0017171,GO:0017171,GO:0017171,0.8145,0.8145,0.8145,0.8145,0.8145,5,0.8145,0.5472,yes
TSTM_TALSN,B8MKZ6,ProtT3,Eukaryota,252,"Hydrolase; part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. Within the pathway, phiM releases the C12-fatty acyl chain from phiA. The pathway begins with the highly reducing polyketide synthase tstA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase tstM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) tstJ and the alkylcitrate dehydratase (ACDH) tstI then give rise to decarboxylated monomeric anhydrides by coupling the C12-fatty acyl chain with oxalacetic acid. The cyclase tstC is responsible for the dimerization of the monomeric anhydrides which leads to the production of prephomoidride that contains the characteristic bicyclo[4.3.1]deca-1,6-diene system of phomoidrides. Iterative oxidation catalyzed by the alpha-ketoglutarate-dependent dioxygenase tstK produced then phomoidride A. Finally, the methyltransferase tstE converts phomoidride A to phomoidride B via an acetalization reaction. The phosphatidylethanolamine-binding protein tstB and tstN are not essential for dimerization and their functions have still to be determined.","Glycerol-3-phosphate phosphatase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties . L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L- homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O- acetyltransferase FUB4, as well as enzymes of the primary metabolism (Probable)",No,No,No,No,No,not-Yes,GO:0016787,GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,0.6019,0.6019,0.6019,0.6019,0.6019,5,0.6019,0.5472,yes
TSTM_TALSN,B8MKZ6,ProtTale,Eukaryota,252,"Hydrolase; part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. Within the pathway, phiM releases the C12-fatty acyl chain from phiA. The pathway begins with the highly reducing polyketide synthase tstA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase tstM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) tstJ and the alkylcitrate dehydratase (ACDH) tstI then give rise to decarboxylated monomeric anhydrides by coupling the C12-fatty acyl chain with oxalacetic acid. The cyclase tstC is responsible for the dimerization of the monomeric anhydrides which leads to the production of prephomoidride that contains the characteristic bicyclo[4.3.1]deca-1,6-diene system of phomoidrides. Iterative oxidation catalyzed by the alpha-ketoglutarate-dependent dioxygenase tstK produced then phomoidride A. Finally, the methyltransferase tstE converts phomoidride A to phomoidride B via an acetalization reaction. The phosphatidylethanolamine-binding protein tstB and tstN are not essential for dimerization and their functions have still to be determined.","Probable esterase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787,GO:0004091,GO:0004091,GO:0004091,GO:0016788,GO:0004091,0.6897,0.6897,0.6897,0.8145,0.6897,5,0.7147,0.5472,yes
TSTM_TALSN,B8MKZ6,Protein2Text,Eukaryota,252,"Hydrolase; part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. Within the pathway, phiM releases the C12-fatty acyl chain from phiA. The pathway begins with the highly reducing polyketide synthase tstA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase tstM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) tstJ and the alkylcitrate dehydratase (ACDH) tstI then give rise to decarboxylated monomeric anhydrides by coupling the C12-fatty acyl chain with oxalacetic acid. The cyclase tstC is responsible for the dimerization of the monomeric anhydrides which leads to the production of prephomoidride that contains the characteristic bicyclo[4.3.1]deca-1,6-diene system of phomoidrides. Iterative oxidation catalyzed by the alpha-ketoglutarate-dependent dioxygenase tstK produced then phomoidride A. Finally, the methyltransferase tstE converts phomoidride A to phomoidride B via an acetalization reaction. The phosphatidylethanolamine-binding protein tstB and tstN are not essential for dimerization and their functions have still to be determined.","The molecular function of this protein is a hydrolase, specifically a carboxylesterase.
This protein is involved in the hydrolysis of ester bonds in carboxylic acids.
It is a type of serine hydrolase, which uses a serine residue in its active site to catalyze the hydrolysis reaction.
The protein is also involved in the hydrolysis of ester bonds in fatty acids, and is thought to play a role in the metabolism of fatty acids in the cell.
The protein is also involved in the hydrolysis of ester bonds in steroids, and is thought to play a role in the metabolism of steroids in the cell.
The protein is also involved in the hydrolysis of ester bonds in lipids, and is thought to play a role in the metabolism of lipids in the cell.
The protein is also involved in the hydrolysis of ester bonds in xenobiotics, and is thought to play a role in the metabolism of xenobiotics in the cell.
The protein is also involved in the hydrolysis of ester bonds in hormones, and is thought to play a role in the metabolism of hormones in the cell.
The protein is also involved in the hydrolysis of ester bonds in neurotransmitters, and is thought to play a role in the metabolism of neurotransmitters in the cell.
The protein is also involved in the hydrolysis of ester bonds in other molecules, and is thought to play a role in the metabolism of other molecules in the cell.
The protein is also involved in the hydrolysis of ester bonds in signaling molecules, and is thought to play a role in the metabolism of signaling molecules in the cell.
The protein is also involved in the hydrolysis of ester bonds in other molecules, and is thought to play a role in the metabolism of other molecules in the cell.
The protein is also involved in the hydrolysis of ester bonds in other molecules, and is thought to play a role in the metabolism of other molecules in the cell.
The protein is also involved in the hydrolysis of ester bonds in other molecules, and is thought to play a role in the metabolism of other molecules in the cell.
The protein is also involved in the hydrolysis of ester bonds in other molecules, and is thought to play a role in the metabolism of other molecules in the cell.
The protein is also involved in the hydrolysis of ester bonds in other molecules, and is thought",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787,GO:0004091,GO:0004091,GO:0004091,GO:0004091,GO:0004091,0.6897,0.6897,0.6897,0.6897,0.6897,5,0.6897,0.5472,yes
TSTM_TALSN,B8MKZ6,Reference,Eukaryota,252,"Hydrolase; part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. Within the pathway, phiM releases the C12-fatty acyl chain from phiA. The pathway begins with the highly reducing polyketide synthase tstA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase tstM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) tstJ and the alkylcitrate dehydratase (ACDH) tstI then give rise to decarboxylated monomeric anhydrides by coupling the C12-fatty acyl chain with oxalacetic acid. The cyclase tstC is responsible for the dimerization of the monomeric anhydrides which leads to the production of prephomoidride that contains the characteristic bicyclo[4.3.1]deca-1,6-diene system of phomoidrides. Iterative oxidation catalyzed by the alpha-ketoglutarate-dependent dioxygenase tstK produced then phomoidride A. Finally, the methyltransferase tstE converts phomoidride A to phomoidride B via an acetalization reaction. The phosphatidylethanolamine-binding protein tstB and tstN are not essential for dimerization and their functions have still to be determined.","Hydrolase; part of the gene cluster that mediates the biosynthesis of the antihypercholesterolemic agents phomoidrides which are dimeric anhydrides. Within the pathway, phiM releases the C12-fatty acyl chain from phiA. The pathway begins with the highly reducing polyketide synthase tstA that catalyzes the formation of a C12-fatty acyl-ACP, starting from one acetate and 5 malonate units. The hydrolase tstM is involved in the release of the C12-fatty acyl chain from phiA. The alkylcitrate synthase (ACS) tstJ and the alkylcitrate dehydratase (ACDH) tstI then give rise to decarboxylated monomeric anhydrides by coupling the C12-fatty acyl chain with oxalacetic acid. The cyclase tstC is responsible for the dimerization of the monomeric anhydrides which leads to the production of prephomoidride that contains the characteristic bicyclo[4.3.1]deca-1,6-diene system of phomoidrides. Iterative oxidation catalyzed by the alpha-ketoglutarate-dependent dioxygenase tstK produced then phomoidride A. Finally, the methyltransferase tstE converts phomoidride A to phomoidride B via an acetalization reaction. The phosphatidylethanolamine-binding protein tstB and tstN are not essential for dimerization and their functions have still to be determined.",,,,,,,GO:0016787,GO:0016787,GO:0016787,GO:0016790,GO:0016787,GO:0016787,1.0,1.0,0.6897,1.0,1.0,5,0.9379,0.5472,yes
PNTC_LANR4,B9CM12,ESM2Text,Bacteria,246,"Cytidylyltransferase involved in the biosynthesis of cell- surface phosphonates. Catalyzes the activation of 2- aminoethylphosphonate (AEP) to CMP-2-aminoethylphosphonate (CMP-AEP). Can also use phosphocholine, with much lower efficiency. Exhibits strong activity towards CTP, limited activity towards ATP and no activity with GTP.","Amino acid phosphotransferase that catalyzes the ATP-dependent exchange of GDP for GTP. It can use neither CTP, TTP or UTP as substrate.",No,No,No,No,No,not-Yes,GO:0046872; GO:0016779,GO:0004550; GO:0005524,GO:0004550,GO:0004550,GO:0004550,GO:0004550,0.3947,0.3585,0.3585,0.3585,0.3585,5,0.3657,0.5152,no
PNTC_LANR4,B9CM12,Prot2Text,Bacteria,246,"Cytidylyltransferase involved in the biosynthesis of cell- surface phosphonates. Catalyzes the activation of 2- aminoethylphosphonate (AEP) to CMP-2-aminoethylphosphonate (CMP-AEP). Can also use phosphocholine, with much lower efficiency. Exhibits strong activity towards CTP, limited activity towards ATP and no activity with GTP.","Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis.",No,No,No,No,No,not-Yes,GO:0046872; GO:0016779,GO:0008879,GO:0008879,GO:0008879,GO:0010143,GO:0008879,0.6017,0.6017,0.6017,0.0,0.6017,5,0.4814,0.5152,no
PNTC_LANR4,B9CM12,ProtT3,Bacteria,246,"Cytidylyltransferase involved in the biosynthesis of cell- surface phosphonates. Catalyzes the activation of 2- aminoethylphosphonate (AEP) to CMP-2-aminoethylphosphonate (CMP-AEP). Can also use phosphocholine, with much lower efficiency. Exhibits strong activity towards CTP, limited activity towards ATP and no activity with GTP.","Catalyzes the formation of UDP-N-acetylglucosamine (UDP-GlcNAc) from GlcNAc-6-P and UTP. In the C-terminal section; belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family. In the N-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family",No,No,No,No,No,not-Yes,GO:0046872; GO:0016779,GO:0003977,GO:0003977,GO:0003977,GO:0003977,GO:0003977,0.5283,0.5283,0.5283,0.5283,0.5283,5,0.5283,0.5152,no
PNTC_LANR4,B9CM12,ProtTale,Bacteria,246,"Cytidylyltransferase involved in the biosynthesis of cell- surface phosphonates. Catalyzes the activation of 2- aminoethylphosphonate (AEP) to CMP-2-aminoethylphosphonate (CMP-AEP). Can also use phosphocholine, with much lower efficiency. Exhibits strong activity towards CTP, limited activity towards ATP and no activity with GTP.","Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the transfer of a glucosyl group from UDP-glucose to choline to produce glucosylcholine, an intermediate in the biosynthesis of glycine betaine.",No,No,No,No,No,not-Yes,GO:0046872; GO:0016779,GO:0016757,GO:0008194,GO:0016757,GO:0046527,GO:0016757,0.4132,0.3445,0.4132,0.2954,0.4132,5,0.3759,0.5152,no
PNTC_LANR4,B9CM12,Protein2Text,Bacteria,246,"Cytidylyltransferase involved in the biosynthesis of cell- surface phosphonates. Catalyzes the activation of 2- aminoethylphosphonate (AEP) to CMP-2-aminoethylphosphonate (CMP-AEP). Can also use phosphocholine, with much lower efficiency. Exhibits strong activity towards CTP, limited activity towards ATP and no activity with GTP.","This protein is involved in a molecular function related to the synthesis of a nucleotide. More specifically, it is involved in the synthesis of a nucleotide monophosphate, which is a type of nucleotide that is composed of a phosphate group, a pentose sugar, and a nitrogenous base. This protein is likely involved in the synthesis of a nucleotide monophosphate, such as adenosine monophosphate (AMP), which is a key molecule in various cellular processes. 

However, the specific function of this protein is not provided in the prompt, so it is not possible to provide a more detailed answer. 

If you have any further questions or if there is anything else I can help you with, please let me know!",Vague,Maybe,Maybe,Vague,Vague,not-Yes,GO:0046872; GO:0016779,,,,,,,,,,,0,,0.5152,no
PNTC_LANR4,B9CM12,Reference,Bacteria,246,"Cytidylyltransferase involved in the biosynthesis of cell- surface phosphonates. Catalyzes the activation of 2- aminoethylphosphonate (AEP) to CMP-2-aminoethylphosphonate (CMP-AEP). Can also use phosphocholine, with much lower efficiency. Exhibits strong activity towards CTP, limited activity towards ATP and no activity with GTP.","Cytidylyltransferase involved in the biosynthesis of cell- surface phosphonates. Catalyzes the activation of 2- aminoethylphosphonate (AEP) to CMP-2-aminoethylphosphonate (CMP-AEP). Can also use phosphocholine, with much lower efficiency. Exhibits strong activity towards CTP, limited activity towards ATP and no activity with GTP.",,,,,,,GO:0046872; GO:0016779,GO:0070567,GO:0070567,GO:0070567,GO:0016779,GO:0016779,0.6017,0.6017,0.6017,0.7015,0.7015,5,0.6416,0.5152,no
KSL1_RICCO,B9T625,ESM2Text,Eukaryota,738,Diterpene cyclase involved in the biosynthesis of labdane- related diterpenoids (LRDs) natural products. Catalyzes the cyclization of ent-CDP into ent-kaurene.,"Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities. Catalyzes the conversion of ent-copalyl diphosphate (ent-CPP) to ent-atiserene.",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0009899; GO:0000287; GO:0010333,GO:0010333,GO:0010333,GO:0010333,,,0.7366,0.7366,0.7366,,,3,0.7366,0.2015,no
KSL1_RICCO,B9T625,Prot2Text,Eukaryota,738,Diterpene cyclase involved in the biosynthesis of labdane- related diterpenoids (LRDs) natural products. Catalyzes the cyclization of ent-CDP into ent-kaurene.,"Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities. Catalyzes the conversion of ent-copalyl diphosphate (ent-CPP) to ent-isopimaradiene.",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0009899; GO:0000287; GO:0010333,GO:0016829,GO:0010333,GO:0010333,GO:0010333,GO:0010333,0.4708,0.7366,0.7366,0.7366,0.7366,5,0.6834,0.2015,no
KSL1_RICCO,B9T625,ProtT3,Eukaryota,738,Diterpene cyclase involved in the biosynthesis of labdane- related diterpenoids (LRDs) natural products. Catalyzes the cyclization of ent-CDP into ent-kaurene.,"Involved in the biosynthesis of ent-kaurene diterpenoids natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens (Probable). Catalyzes the conversion of (2E,6E)-geranylgeranyl diphosphate (GGPP) to ent-copalyl diphosphate (ent-CPP) (Probable). Plastid, chloroplast. Belongs to the terpene synthase family",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0009899; GO:0000287; GO:0010333,GO:0010487,GO:0034048,GO:0034048,GO:0009905,GO:0010487,0.1923,0.0,0.0,0.1923,0.1923,5,0.1154,0.2015,no
KSL1_RICCO,B9T625,ProtTale,Eukaryota,738,Diterpene cyclase involved in the biosynthesis of labdane- related diterpenoids (LRDs) natural products. Catalyzes the cyclization of ent-CDP into ent-kaurene.,"Involved in the biosynthesis of ent-kaurene diterpenoids natural products, such as miltiradiene, a major component of the essential oil of mint and other aromatic plants, and potential bioactive compounds. Catalyzes the conversion of ent-copalyl diphosphate (ent-CPP) and ent-kaurene diphosphate (ent-KPP) into ent-kaurene (ent-K) and ent-kaurenoic acid, respectively.",Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0009899; GO:0000287; GO:0010333,GO:0010333,GO:0010334,GO:0010333,GO:0010334,GO:0010333,0.7366,0.6379,0.7366,0.6379,0.7366,5,0.6971,0.2015,no
KSL1_RICCO,B9T625,Protein2Text,Eukaryota,738,Diterpene cyclase involved in the biosynthesis of labdane- related diterpenoids (LRDs) natural products. Catalyzes the cyclization of ent-CDP into ent-kaurene.,"This protein is a part of the terpene synthase family, which is involved in the biosynthesis of terpenes. Specifically, it is a terpene synthase, which catalyzes the conversion of geranyl diphosphate (GPP) to (-)-germacrene D, a sesquiterpene.",Vague,No,No,No,No,not-Yes,GO:0009899; GO:0000287; GO:0010333,GO:0016829,GO:0010333,GO:0010333,GO:0010333,GO:0010333,0.4708,0.7366,0.7366,0.7366,0.7366,5,0.6834,0.2015,no
KSL1_RICCO,B9T625,Reference,Eukaryota,738,Diterpene cyclase involved in the biosynthesis of labdane- related diterpenoids (LRDs) natural products. Catalyzes the cyclization of ent-CDP into ent-kaurene.,Diterpene cyclase involved in the biosynthesis of labdane- related diterpenoids (LRDs) natural products. Catalyzes the cyclization of ent-CDP into ent-kaurene.,,,,,,,GO:0009899; GO:0000287; GO:0010333,GO:0010334,GO:0016829,GO:0010334,GO:0010334,GO:0010333,0.6379,0.4708,0.6379,0.6379,0.7366,5,0.6242,0.2015,no
UNCH_UNCRE,C4JF79,ESM2Text,Eukaryota,619,"Peptidase; part of the unc gene cluster that mediates the biosynthesis of the tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. Within the pathway, uncH hydrolyzes the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln to yield the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. UncH is also able to hydrolyze dipeptides L- Leu-L-Isd or L-Leu-D-Isd to yield L-O-isoindolinone-homoserine (L-Isd) or D-O-isoindolinone-homoserine (D-Isd), respectively, along with L-Leu. The alanine racemase uncE first catalyzes the interconversion between L-alanine and D-alanine. D-alanine is then activated by the NRPS uncD that transfers it to the PKS uncA to produce R-dihydroxymethyl isoindolinone. UncF then catalyzes the gamma- replacement of acetate in O-acetyl-L-homoserine (OAH) with R- dihydroxymethyl isoindolinone to generate the amino acid L-O- isoindolinone-homoserine (L-Isd). Then, the ATP-grasp enzyme uncK acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Isd to give the dipeptide L- Leu-L-Isd. Epimerase uncI converts L-Leu-L-Isd to L-Leu-D-Isd in which C-alpha of the Isd residue is epimerized from L to D. UncH is able to hydrolyze dipeptides L-Leu-L-Isd or L-Leu-D-Isd to yield L-Isd or D- Isd, respectively, along with L-Leu. UncG then produces the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln by adding L-Ala-L-Gln produced by the dipeptide synthetase uncJ that forms L-Ala-L-Gln from L-Ala and L- Gln. Finally, hydrolysis of L-Leu-D-Isd-L-Ala-L-Gln by uncH leads to the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B.",Catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus. It has a specificity for substrates with a hydrophobic residue at the P1 position.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008236,GO:0003984,GO:0004041,GO:0003992,GO:0003992,GO:0004060,0.2258,0.1954,0.1954,0.1954,0.1451,5,0.1914,0.4733,no
UNCH_UNCRE,C4JF79,Prot2Text,Eukaryota,619,"Peptidase; part of the unc gene cluster that mediates the biosynthesis of the tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. Within the pathway, uncH hydrolyzes the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln to yield the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. UncH is also able to hydrolyze dipeptides L- Leu-L-Isd or L-Leu-D-Isd to yield L-O-isoindolinone-homoserine (L-Isd) or D-O-isoindolinone-homoserine (D-Isd), respectively, along with L-Leu. The alanine racemase uncE first catalyzes the interconversion between L-alanine and D-alanine. D-alanine is then activated by the NRPS uncD that transfers it to the PKS uncA to produce R-dihydroxymethyl isoindolinone. UncF then catalyzes the gamma- replacement of acetate in O-acetyl-L-homoserine (OAH) with R- dihydroxymethyl isoindolinone to generate the amino acid L-O- isoindolinone-homoserine (L-Isd). Then, the ATP-grasp enzyme uncK acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Isd to give the dipeptide L- Leu-L-Isd. Epimerase uncI converts L-Leu-L-Isd to L-Leu-D-Isd in which C-alpha of the Isd residue is epimerized from L to D. UncH is able to hydrolyze dipeptides L-Leu-L-Isd or L-Leu-D-Isd to yield L-Isd or D- Isd, respectively, along with L-Leu. UncG then produces the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln by adding L-Ala-L-Gln produced by the dipeptide synthetase uncJ that forms L-Ala-L-Gln from L-Ala and L- Gln. Finally, hydrolysis of L-Leu-D-Isd-L-Ala-L-Gln by uncH leads to the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B.",Housekeeping prolyl oligopeptidase (POP) that behaves like a conventional POP by cleaving peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. Has an absolute requirement for an X-Pro bond in the trans configuration immediately preceding the Pro-Y scissible bond.,No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008236,GO:0008236,GO:0004287,GO:0004287,GO:0004287,GO:0004287,1.0,0.0,0.0,0.0,0.0,5,0.2,0.4733,no
UNCH_UNCRE,C4JF79,ProtT3,Eukaryota,619,"Peptidase; part of the unc gene cluster that mediates the biosynthesis of the tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. Within the pathway, uncH hydrolyzes the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln to yield the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. UncH is also able to hydrolyze dipeptides L- Leu-L-Isd or L-Leu-D-Isd to yield L-O-isoindolinone-homoserine (L-Isd) or D-O-isoindolinone-homoserine (D-Isd), respectively, along with L-Leu. The alanine racemase uncE first catalyzes the interconversion between L-alanine and D-alanine. D-alanine is then activated by the NRPS uncD that transfers it to the PKS uncA to produce R-dihydroxymethyl isoindolinone. UncF then catalyzes the gamma- replacement of acetate in O-acetyl-L-homoserine (OAH) with R- dihydroxymethyl isoindolinone to generate the amino acid L-O- isoindolinone-homoserine (L-Isd). Then, the ATP-grasp enzyme uncK acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Isd to give the dipeptide L- Leu-L-Isd. Epimerase uncI converts L-Leu-L-Isd to L-Leu-D-Isd in which C-alpha of the Isd residue is epimerized from L to D. UncH is able to hydrolyze dipeptides L-Leu-L-Isd or L-Leu-D-Isd to yield L-Isd or D- Isd, respectively, along with L-Leu. UncG then produces the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln by adding L-Ala-L-Gln produced by the dipeptide synthetase uncJ that forms L-Ala-L-Gln from L-Ala and L- Gln. Finally, hydrolysis of L-Leu-D-Isd-L-Ala-L-Gln by uncH leads to the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B.",Hydrolyzes dipeptides containing N-terminal acidic residues. Belongs to the peptidase S54 family,Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0008236,GO:0008236,GO:0016805,GO:0004177,GO:0016805,GO:0016805,1.0,0.6001,0.6001,0.6001,0.6001,5,0.6801,0.4733,no
UNCH_UNCRE,C4JF79,ProtTale,Eukaryota,619,"Peptidase; part of the unc gene cluster that mediates the biosynthesis of the tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. Within the pathway, uncH hydrolyzes the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln to yield the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. UncH is also able to hydrolyze dipeptides L- Leu-L-Isd or L-Leu-D-Isd to yield L-O-isoindolinone-homoserine (L-Isd) or D-O-isoindolinone-homoserine (D-Isd), respectively, along with L-Leu. The alanine racemase uncE first catalyzes the interconversion between L-alanine and D-alanine. D-alanine is then activated by the NRPS uncD that transfers it to the PKS uncA to produce R-dihydroxymethyl isoindolinone. UncF then catalyzes the gamma- replacement of acetate in O-acetyl-L-homoserine (OAH) with R- dihydroxymethyl isoindolinone to generate the amino acid L-O- isoindolinone-homoserine (L-Isd). Then, the ATP-grasp enzyme uncK acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Isd to give the dipeptide L- Leu-L-Isd. Epimerase uncI converts L-Leu-L-Isd to L-Leu-D-Isd in which C-alpha of the Isd residue is epimerized from L to D. UncH is able to hydrolyze dipeptides L-Leu-L-Isd or L-Leu-D-Isd to yield L-Isd or D- Isd, respectively, along with L-Leu. UncG then produces the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln by adding L-Ala-L-Gln produced by the dipeptide synthetase uncJ that forms L-Ala-L-Gln from L-Ala and L- Gln. Finally, hydrolysis of L-Leu-D-Isd-L-Ala-L-Gln by uncH leads to the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B.","Aminopeptidase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3- hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta",No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008236,GO:0004177,GO:0004177,GO:0004177,GO:0004177,GO:0004177,0.6001,0.6001,0.6001,0.6001,0.6001,5,0.6001,0.4733,no
UNCH_UNCRE,C4JF79,Protein2Text,Eukaryota,619,"Peptidase; part of the unc gene cluster that mediates the biosynthesis of the tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. Within the pathway, uncH hydrolyzes the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln to yield the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. UncH is also able to hydrolyze dipeptides L- Leu-L-Isd or L-Leu-D-Isd to yield L-O-isoindolinone-homoserine (L-Isd) or D-O-isoindolinone-homoserine (D-Isd), respectively, along with L-Leu. The alanine racemase uncE first catalyzes the interconversion between L-alanine and D-alanine. D-alanine is then activated by the NRPS uncD that transfers it to the PKS uncA to produce R-dihydroxymethyl isoindolinone. UncF then catalyzes the gamma- replacement of acetate in O-acetyl-L-homoserine (OAH) with R- dihydroxymethyl isoindolinone to generate the amino acid L-O- isoindolinone-homoserine (L-Isd). Then, the ATP-grasp enzyme uncK acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Isd to give the dipeptide L- Leu-L-Isd. Epimerase uncI converts L-Leu-L-Isd to L-Leu-D-Isd in which C-alpha of the Isd residue is epimerized from L to D. UncH is able to hydrolyze dipeptides L-Leu-L-Isd or L-Leu-D-Isd to yield L-Isd or D- Isd, respectively, along with L-Leu. UncG then produces the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln by adding L-Ala-L-Gln produced by the dipeptide synthetase uncJ that forms L-Ala-L-Gln from L-Ala and L- Gln. Finally, hydrolysis of L-Leu-D-Isd-L-Ala-L-Gln by uncH leads to the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B.","This protein has a molecular function of hydrolase activity, specifically catalyzing the hydrolysis of the amide bond of a carboxylic acid amide to produce a carboxylic acid and an amine. More specifically, it is a type of hydrolase that acts on ester bonds, and is involved in the hydrolysis of ester bonds in peptides.",Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008236,GO:0016787,,,,GO:0008233,0.5526,,,,0.7896,2,0.6711,0.4733,no
UNCH_UNCRE,C4JF79,Reference,Eukaryota,619,"Peptidase; part of the unc gene cluster that mediates the biosynthesis of the tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. Within the pathway, uncH hydrolyzes the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln to yield the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. UncH is also able to hydrolyze dipeptides L- Leu-L-Isd or L-Leu-D-Isd to yield L-O-isoindolinone-homoserine (L-Isd) or D-O-isoindolinone-homoserine (D-Isd), respectively, along with L-Leu. The alanine racemase uncE first catalyzes the interconversion between L-alanine and D-alanine. D-alanine is then activated by the NRPS uncD that transfers it to the PKS uncA to produce R-dihydroxymethyl isoindolinone. UncF then catalyzes the gamma- replacement of acetate in O-acetyl-L-homoserine (OAH) with R- dihydroxymethyl isoindolinone to generate the amino acid L-O- isoindolinone-homoserine (L-Isd). Then, the ATP-grasp enzyme uncK acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Isd to give the dipeptide L- Leu-L-Isd. Epimerase uncI converts L-Leu-L-Isd to L-Leu-D-Isd in which C-alpha of the Isd residue is epimerized from L to D. UncH is able to hydrolyze dipeptides L-Leu-L-Isd or L-Leu-D-Isd to yield L-Isd or D- Isd, respectively, along with L-Leu. UncG then produces the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln by adding L-Ala-L-Gln produced by the dipeptide synthetase uncJ that forms L-Ala-L-Gln from L-Ala and L- Gln. Finally, hydrolysis of L-Leu-D-Isd-L-Ala-L-Gln by uncH leads to the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B.","Peptidase; part of the unc gene cluster that mediates the biosynthesis of the tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. Within the pathway, uncH hydrolyzes the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln to yield the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. UncH is also able to hydrolyze dipeptides L- Leu-L-Isd or L-Leu-D-Isd to yield L-O-isoindolinone-homoserine (L-Isd) or D-O-isoindolinone-homoserine (D-Isd), respectively, along with L-Leu. The alanine racemase uncE first catalyzes the interconversion between L-alanine and D-alanine. D-alanine is then activated by the NRPS uncD that transfers it to the PKS uncA to produce R-dihydroxymethyl isoindolinone. UncF then catalyzes the gamma- replacement of acetate in O-acetyl-L-homoserine (OAH) with R- dihydroxymethyl isoindolinone to generate the amino acid L-O- isoindolinone-homoserine (L-Isd). Then, the ATP-grasp enzyme uncK acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Isd to give the dipeptide L- Leu-L-Isd. Epimerase uncI converts L-Leu-L-Isd to L-Leu-D-Isd in which C-alpha of the Isd residue is epimerized from L to D. UncH is able to hydrolyze dipeptides L-Leu-L-Isd or L-Leu-D-Isd to yield L-Isd or D- Isd, respectively, along with L-Leu. UncG then produces the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln by adding L-Ala-L-Gln produced by the dipeptide synthetase uncJ that forms L-Ala-L-Gln from L-Ala and L- Gln. Finally, hydrolysis of L-Leu-D-Isd-L-Ala-L-Gln by uncH leads to the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B.",,,,,,,GO:0008236,GO:0008233,GO:0008233,GO:0008233,GO:0008233,GO:0008233,0.7896,0.7896,0.7896,0.7896,0.7896,5,0.7896,0.4733,no
UNCI_UNCRE,C4JF80,ESM2Text,Eukaryota,339,"Epimerase; part of the unc gene cluster that mediates the biosynthesis of the tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. Within the pathway, uncI converts the C-alpha of the Isd residue L to D in the L-Leu-L-Isd dipeptide to produce the L-Leu-D- Isd dipeptide. The alanine racemase uncE first catalyzes the interconversion between L-alanine and D-alanine. D- alanine is then activated by the NRPS uncD that transfers it to the PKS uncA to produce R-dihydroxymethyl isoindolinone. UncF then catalyzes the gamma-replacement of acetate in O-acetyl-L-homoserine (OAH) with R- dihydroxymethyl isoindolinone to generate the amino acid L-O- isoindolinone-homoserine (L-Isd). Then, the ATP-grasp enzyme uncK acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Isd to give the dipeptide L- Leu-L-Isd. Epimerase uncI converts L-Leu-L-Isd to L-Leu-D-Isd in which C-alpha of the Isd residue is epimerized from L to D. UncH is able to hydrolyze dipeptides L-Leu-L-Isd or L-Leu-D-Isd to yield L-Isd or D- Isd, respectively, along with L-Leu. UncG then produces the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln by adding L-Ala-L-Gln produced by the dipeptide synthetase uncJ that forms L-Ala-L-Gln from L-Ala and L- Gln. Finally, hydrolysis of L-Leu-D-Isd-L-Ala-L-Gln by uncH leads to the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B.","Catalyzes the epimerization of L-Ala-DAP (L-Ala-Phe-AMC) to L-Ala-L-Glu and has probably a role in the metabolism of L-Ala-DAP, a metabolite of the peptidase factor GefD that promotes the degradation of amino acids, thereby regulating sphingolipid metabolism. Is also able to catalyze the reverse reaction and the epimerization of L-Ala-L-Gly. Is also able to catalyze the reverse reaction in vitro, but shows a marked preference for substrates with a small hydrophobic alpha subunit (L-Ala-Phe-AMC) in the Phe-Pro peptide as substrate.",Maybe,Maybe,Maybe,Yes,Maybe,not-Yes,GO:0046872; GO:0016855,GO:0016854,GO:0016855,,GO:0016854,,0.6032,0.7015,,0.6032,,3,0.636,0.2352,no
UNCI_UNCRE,C4JF80,Prot2Text,Eukaryota,339,"Epimerase; part of the unc gene cluster that mediates the biosynthesis of the tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. Within the pathway, uncI converts the C-alpha of the Isd residue L to D in the L-Leu-L-Isd dipeptide to produce the L-Leu-D- Isd dipeptide. The alanine racemase uncE first catalyzes the interconversion between L-alanine and D-alanine. D- alanine is then activated by the NRPS uncD that transfers it to the PKS uncA to produce R-dihydroxymethyl isoindolinone. UncF then catalyzes the gamma-replacement of acetate in O-acetyl-L-homoserine (OAH) with R- dihydroxymethyl isoindolinone to generate the amino acid L-O- isoindolinone-homoserine (L-Isd). Then, the ATP-grasp enzyme uncK acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Isd to give the dipeptide L- Leu-L-Isd. Epimerase uncI converts L-Leu-L-Isd to L-Leu-D-Isd in which C-alpha of the Isd residue is epimerized from L to D. UncH is able to hydrolyze dipeptides L-Leu-L-Isd or L-Leu-D-Isd to yield L-Isd or D- Isd, respectively, along with L-Leu. UncG then produces the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln by adding L-Ala-L-Gln produced by the dipeptide synthetase uncJ that forms L-Ala-L-Gln from L-Ala and L- Gln. Finally, hydrolysis of L-Leu-D-Isd-L-Ala-L-Gln by uncH leads to the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B.","Catalyzes the epimerization of L-Ala-D-Glu to L-Ala-L-Glu and has probably a role in the metabolism of the murein peptide, of which L-Ala-D-Glu is a component. Is also able to catalyze the reverse reaction and the epimerization of all the L-Ala-X dipeptides, except L-Ala-L-Phe, L-Ala-L-Tyr, and L-Ala-L-Met. Is also active with L-Ala-D/L-Phe, L-Ala-L-Trp, L-Ala-L-Leu, L-Ala-L-Phe, L-Ala-L-Tyr, and L-Ala-L-Trp.",Maybe,Maybe,Maybe,Yes,Maybe,not-Yes,GO:0046872; GO:0016855,GO:0016854,GO:0016855,GO:0016857,GO:0016857,GO:0016857,0.6032,0.7015,0.5032,0.5032,0.5032,5,0.5629,0.2352,no
UNCI_UNCRE,C4JF80,ProtT3,Eukaryota,339,"Epimerase; part of the unc gene cluster that mediates the biosynthesis of the tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. Within the pathway, uncI converts the C-alpha of the Isd residue L to D in the L-Leu-L-Isd dipeptide to produce the L-Leu-D- Isd dipeptide. The alanine racemase uncE first catalyzes the interconversion between L-alanine and D-alanine. D- alanine is then activated by the NRPS uncD that transfers it to the PKS uncA to produce R-dihydroxymethyl isoindolinone. UncF then catalyzes the gamma-replacement of acetate in O-acetyl-L-homoserine (OAH) with R- dihydroxymethyl isoindolinone to generate the amino acid L-O- isoindolinone-homoserine (L-Isd). Then, the ATP-grasp enzyme uncK acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Isd to give the dipeptide L- Leu-L-Isd. Epimerase uncI converts L-Leu-L-Isd to L-Leu-D-Isd in which C-alpha of the Isd residue is epimerized from L to D. UncH is able to hydrolyze dipeptides L-Leu-L-Isd or L-Leu-D-Isd to yield L-Isd or D- Isd, respectively, along with L-Leu. UncG then produces the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln by adding L-Ala-L-Gln produced by the dipeptide synthetase uncJ that forms L-Ala-L-Gln from L-Ala and L- Gln. Finally, hydrolysis of L-Leu-D-Isd-L-Ala-L-Gln by uncH leads to the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B.",Catalyzes the epimerization of L-2-amino-6-oxopimelate to D-2-amino-6-oxopimelate. Belongs to the mandelate racemase/muconate lactonizing enzyme family,Maybe,Maybe,Maybe,Yes,Maybe,not-Yes,GO:0046872; GO:0016855,GO:0016857,GO:0008837,GO:0016854,GO:0008837,GO:0008837,0.5032,0.5283,0.6032,0.5283,0.5283,5,0.5383,0.2352,no
UNCI_UNCRE,C4JF80,ProtTale,Eukaryota,339,"Epimerase; part of the unc gene cluster that mediates the biosynthesis of the tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. Within the pathway, uncI converts the C-alpha of the Isd residue L to D in the L-Leu-L-Isd dipeptide to produce the L-Leu-D- Isd dipeptide. The alanine racemase uncE first catalyzes the interconversion between L-alanine and D-alanine. D- alanine is then activated by the NRPS uncD that transfers it to the PKS uncA to produce R-dihydroxymethyl isoindolinone. UncF then catalyzes the gamma-replacement of acetate in O-acetyl-L-homoserine (OAH) with R- dihydroxymethyl isoindolinone to generate the amino acid L-O- isoindolinone-homoserine (L-Isd). Then, the ATP-grasp enzyme uncK acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Isd to give the dipeptide L- Leu-L-Isd. Epimerase uncI converts L-Leu-L-Isd to L-Leu-D-Isd in which C-alpha of the Isd residue is epimerized from L to D. UncH is able to hydrolyze dipeptides L-Leu-L-Isd or L-Leu-D-Isd to yield L-Isd or D- Isd, respectively, along with L-Leu. UncG then produces the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln by adding L-Ala-L-Gln produced by the dipeptide synthetase uncJ that forms L-Ala-L-Gln from L-Ala and L- Gln. Finally, hydrolysis of L-Leu-D-Isd-L-Ala-L-Gln by uncH leads to the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B.","Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1- carboxylate (SHCHC) to 2-succinylbenzoate (OSB).",No,No,No,No,No,not-Yes,GO:0046872; GO:0016855,GO:0008935,GO:0008935,GO:0016836,GO:0008935,GO:0008935,0.1865,0.1865,0.2176,0.1865,0.1865,5,0.1927,0.2352,no
UNCI_UNCRE,C4JF80,Protein2Text,Eukaryota,339,"Epimerase; part of the unc gene cluster that mediates the biosynthesis of the tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. Within the pathway, uncI converts the C-alpha of the Isd residue L to D in the L-Leu-L-Isd dipeptide to produce the L-Leu-D- Isd dipeptide. The alanine racemase uncE first catalyzes the interconversion between L-alanine and D-alanine. D- alanine is then activated by the NRPS uncD that transfers it to the PKS uncA to produce R-dihydroxymethyl isoindolinone. UncF then catalyzes the gamma-replacement of acetate in O-acetyl-L-homoserine (OAH) with R- dihydroxymethyl isoindolinone to generate the amino acid L-O- isoindolinone-homoserine (L-Isd). Then, the ATP-grasp enzyme uncK acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Isd to give the dipeptide L- Leu-L-Isd. Epimerase uncI converts L-Leu-L-Isd to L-Leu-D-Isd in which C-alpha of the Isd residue is epimerized from L to D. UncH is able to hydrolyze dipeptides L-Leu-L-Isd or L-Leu-D-Isd to yield L-Isd or D- Isd, respectively, along with L-Leu. UncG then produces the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln by adding L-Ala-L-Gln produced by the dipeptide synthetase uncJ that forms L-Ala-L-Gln from L-Ala and L- Gln. Finally, hydrolysis of L-Leu-D-Isd-L-Ala-L-Gln by uncH leads to the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B.","The molecular function of this protein is a lyase enzyme, specifically a beta-reductase that catalyzes the conversion of a carboxylic acid to a beta-keto acid.",No,No,No,No,No,not-Yes,GO:0046872; GO:0016855,,,,,,,,,,,0,,0.2352,no
UNCI_UNCRE,C4JF80,Reference,Eukaryota,339,"Epimerase; part of the unc gene cluster that mediates the biosynthesis of the tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. Within the pathway, uncI converts the C-alpha of the Isd residue L to D in the L-Leu-L-Isd dipeptide to produce the L-Leu-D- Isd dipeptide. The alanine racemase uncE first catalyzes the interconversion between L-alanine and D-alanine. D- alanine is then activated by the NRPS uncD that transfers it to the PKS uncA to produce R-dihydroxymethyl isoindolinone. UncF then catalyzes the gamma-replacement of acetate in O-acetyl-L-homoserine (OAH) with R- dihydroxymethyl isoindolinone to generate the amino acid L-O- isoindolinone-homoserine (L-Isd). Then, the ATP-grasp enzyme uncK acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Isd to give the dipeptide L- Leu-L-Isd. Epimerase uncI converts L-Leu-L-Isd to L-Leu-D-Isd in which C-alpha of the Isd residue is epimerized from L to D. UncH is able to hydrolyze dipeptides L-Leu-L-Isd or L-Leu-D-Isd to yield L-Isd or D- Isd, respectively, along with L-Leu. UncG then produces the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln by adding L-Ala-L-Gln produced by the dipeptide synthetase uncJ that forms L-Ala-L-Gln from L-Ala and L- Gln. Finally, hydrolysis of L-Leu-D-Isd-L-Ala-L-Gln by uncH leads to the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B.","Epimerase; part of the unc gene cluster that mediates the biosynthesis of the tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. Within the pathway, uncI converts the C-alpha of the Isd residue L to D in the L-Leu-L-Isd dipeptide to produce the L-Leu-D- Isd dipeptide. The alanine racemase uncE first catalyzes the interconversion between L-alanine and D-alanine. D- alanine is then activated by the NRPS uncD that transfers it to the PKS uncA to produce R-dihydroxymethyl isoindolinone. UncF then catalyzes the gamma-replacement of acetate in O-acetyl-L-homoserine (OAH) with R- dihydroxymethyl isoindolinone to generate the amino acid L-O- isoindolinone-homoserine (L-Isd). Then, the ATP-grasp enzyme uncK acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Isd to give the dipeptide L- Leu-L-Isd. Epimerase uncI converts L-Leu-L-Isd to L-Leu-D-Isd in which C-alpha of the Isd residue is epimerized from L to D. UncH is able to hydrolyze dipeptides L-Leu-L-Isd or L-Leu-D-Isd to yield L-Isd or D- Isd, respectively, along with L-Leu. UncG then produces the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln by adding L-Ala-L-Gln produced by the dipeptide synthetase uncJ that forms L-Ala-L-Gln from L-Ala and L- Gln. Finally, hydrolysis of L-Leu-D-Isd-L-Ala-L-Gln by uncH leads to the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B.",,,,,,,GO:0046872; GO:0016855,GO:0016854,GO:0016854,GO:0016854,GO:0016854,GO:0016854,0.6032,0.6032,0.6032,0.6032,0.6032,5,0.6032,0.2352,no
UNCJ_UNCRE,C4JF81,ESM2Text,Eukaryota,657,"ATP-grasp enzyme; part of the unc gene cluster that mediates the biosynthesis of the tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. Within the pathway, uncJ is responsible for the formation of the dipeptide L-Ala-L-Gln from L-Ala and L-Gln. The alanine racemase uncE first catalyzes the interconversion between L-alanine and D-alanine. D-alanine is then activated by the NRPS uncD that transfers it to the PKS uncA to produce R-dihydroxymethyl isoindolinone. UncF then catalyzes the gamma- replacement of acetate in O-acetyl-L-homoserine (OAH) with R- dihydroxymethyl isoindolinone to generate the amino acid L-O- isoindolinone-homoserine (L-Isd). Then, the ATP-grasp enzyme uncK acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Isd to give the dipeptide L- Leu-L-Isd. Epimerase uncI converts L-Leu-L-Isd to L-Leu-D-Isd in which C-alpha of the Isd residue is epimerized from L to D. UncH is able to hydrolyze dipeptides L-Leu-L-Isd or L-Leu-D-Isd to yield L-Isd or D- Isd, respectively, along with L-Leu. UncG then produces the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln by adding L-Ala-L-Gln produced by the dipeptide synthetase uncJ that forms L-Ala-L-Gln from L-Ala and L- Gln. Finally, hydrolysis of L-Leu-D-Isd-L-Ala-L-Gln by uncH leads to the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B.",Dioxygenase that catalyzes the adenylation of one alpha-glutamate molecule into four molecules of spermidine.,No,No,No,No,No,not-Yes,GO:0005524; GO:0016874; GO:0046872,,,,,,,,,,,0,,0.5016,no
UNCJ_UNCRE,C4JF81,Prot2Text,Eukaryota,657,"ATP-grasp enzyme; part of the unc gene cluster that mediates the biosynthesis of the tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. Within the pathway, uncJ is responsible for the formation of the dipeptide L-Ala-L-Gln from L-Ala and L-Gln. The alanine racemase uncE first catalyzes the interconversion between L-alanine and D-alanine. D-alanine is then activated by the NRPS uncD that transfers it to the PKS uncA to produce R-dihydroxymethyl isoindolinone. UncF then catalyzes the gamma- replacement of acetate in O-acetyl-L-homoserine (OAH) with R- dihydroxymethyl isoindolinone to generate the amino acid L-O- isoindolinone-homoserine (L-Isd). Then, the ATP-grasp enzyme uncK acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Isd to give the dipeptide L- Leu-L-Isd. Epimerase uncI converts L-Leu-L-Isd to L-Leu-D-Isd in which C-alpha of the Isd residue is epimerized from L to D. UncH is able to hydrolyze dipeptides L-Leu-L-Isd or L-Leu-D-Isd to yield L-Isd or D- Isd, respectively, along with L-Leu. UncG then produces the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln by adding L-Ala-L-Gln produced by the dipeptide synthetase uncJ that forms L-Ala-L-Gln from L-Ala and L- Gln. Finally, hydrolysis of L-Leu-D-Isd-L-Ala-L-Gln by uncH leads to the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B.","Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3 and participates in phytic acid biosynthesis in developing seeds. Phytic acid is the primary storage form of phosphorus in cereal grains and other plant seeds.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016874; GO:0046872,GO:0016301,GO:0016301,GO:0016301,GO:0000764,GO:0016301; GO:0005524,0.2455,0.2455,0.2455,0.0,0.6206,5,0.2714,0.5016,no
UNCJ_UNCRE,C4JF81,ProtT3,Eukaryota,657,"ATP-grasp enzyme; part of the unc gene cluster that mediates the biosynthesis of the tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. Within the pathway, uncJ is responsible for the formation of the dipeptide L-Ala-L-Gln from L-Ala and L-Gln. The alanine racemase uncE first catalyzes the interconversion between L-alanine and D-alanine. D-alanine is then activated by the NRPS uncD that transfers it to the PKS uncA to produce R-dihydroxymethyl isoindolinone. UncF then catalyzes the gamma- replacement of acetate in O-acetyl-L-homoserine (OAH) with R- dihydroxymethyl isoindolinone to generate the amino acid L-O- isoindolinone-homoserine (L-Isd). Then, the ATP-grasp enzyme uncK acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Isd to give the dipeptide L- Leu-L-Isd. Epimerase uncI converts L-Leu-L-Isd to L-Leu-D-Isd in which C-alpha of the Isd residue is epimerized from L to D. UncH is able to hydrolyze dipeptides L-Leu-L-Isd or L-Leu-D-Isd to yield L-Isd or D- Isd, respectively, along with L-Leu. UncG then produces the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln by adding L-Ala-L-Gln produced by the dipeptide synthetase uncJ that forms L-Ala-L-Gln from L-Ala and L- Gln. Finally, hydrolysis of L-Leu-D-Isd-L-Ala-L-Gln by uncH leads to the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B.","ATP-dependent N-alpha-acetyltransferase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), B5 (FB5), B6 (FB6), B7 (FB7), B8 (FB8), and B9 (FB9), a group of polyketide-derived furanocoumarins",No,Maybe,No,No,No,not-Yes,GO:0005524; GO:0016874; GO:0046872,GO:0004596; GO:0005524,GO:0004596,GO:0004596; GO:0005524,GO:0004596; GO:0005524,GO:0004596; GO:0005524,0.5568,0.1517,0.5568,0.5568,0.5568,5,0.4758,0.5016,no
UNCJ_UNCRE,C4JF81,ProtTale,Eukaryota,657,"ATP-grasp enzyme; part of the unc gene cluster that mediates the biosynthesis of the tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. Within the pathway, uncJ is responsible for the formation of the dipeptide L-Ala-L-Gln from L-Ala and L-Gln. The alanine racemase uncE first catalyzes the interconversion between L-alanine and D-alanine. D-alanine is then activated by the NRPS uncD that transfers it to the PKS uncA to produce R-dihydroxymethyl isoindolinone. UncF then catalyzes the gamma- replacement of acetate in O-acetyl-L-homoserine (OAH) with R- dihydroxymethyl isoindolinone to generate the amino acid L-O- isoindolinone-homoserine (L-Isd). Then, the ATP-grasp enzyme uncK acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Isd to give the dipeptide L- Leu-L-Isd. Epimerase uncI converts L-Leu-L-Isd to L-Leu-D-Isd in which C-alpha of the Isd residue is epimerized from L to D. UncH is able to hydrolyze dipeptides L-Leu-L-Isd or L-Leu-D-Isd to yield L-Isd or D- Isd, respectively, along with L-Leu. UncG then produces the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln by adding L-Ala-L-Gln produced by the dipeptide synthetase uncJ that forms L-Ala-L-Gln from L-Ala and L- Gln. Finally, hydrolysis of L-Leu-D-Isd-L-Ala-L-Gln by uncH leads to the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B.",ATP-grasp kinase that catalyzes the specific phosphorylation of ADP to ADP-D-glucose in an ATP-dependent reaction. Probably involved in a pathway regulating carbohydrate metabolism.,Maybe,No,No,Maybe,Maybe,not-Yes,GO:0005524; GO:0016874; GO:0046872,GO:0016301; GO:0005524,GO:0016301; GO:0005524,GO:0016301; GO:0005524,GO:0016301; GO:0005524,GO:0016301; GO:0005524,0.6206,0.6206,0.6206,0.6206,0.6206,5,0.6206,0.5016,no
UNCJ_UNCRE,C4JF81,Protein2Text,Eukaryota,657,"ATP-grasp enzyme; part of the unc gene cluster that mediates the biosynthesis of the tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. Within the pathway, uncJ is responsible for the formation of the dipeptide L-Ala-L-Gln from L-Ala and L-Gln. The alanine racemase uncE first catalyzes the interconversion between L-alanine and D-alanine. D-alanine is then activated by the NRPS uncD that transfers it to the PKS uncA to produce R-dihydroxymethyl isoindolinone. UncF then catalyzes the gamma- replacement of acetate in O-acetyl-L-homoserine (OAH) with R- dihydroxymethyl isoindolinone to generate the amino acid L-O- isoindolinone-homoserine (L-Isd). Then, the ATP-grasp enzyme uncK acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Isd to give the dipeptide L- Leu-L-Isd. Epimerase uncI converts L-Leu-L-Isd to L-Leu-D-Isd in which C-alpha of the Isd residue is epimerized from L to D. UncH is able to hydrolyze dipeptides L-Leu-L-Isd or L-Leu-D-Isd to yield L-Isd or D- Isd, respectively, along with L-Leu. UncG then produces the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln by adding L-Ala-L-Gln produced by the dipeptide synthetase uncJ that forms L-Ala-L-Gln from L-Ala and L- Gln. Finally, hydrolysis of L-Leu-D-Isd-L-Ala-L-Gln by uncH leads to the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B.","This protein is a molecular function that catalyzes the removal of an amino acid residue from a protein. Specifically, it is a type of protease that breaks down proteins into smaller peptides or amino acids. This process is important for various cellular functions, including protein turnover, signal transduction, and immune response.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016874; GO:0046872,GO:0008233,GO:0008233,GO:0008233,GO:0008233,GO:0008233,0.2548,0.2548,0.2548,0.2548,0.2548,5,0.2548,0.5016,no
UNCJ_UNCRE,C4JF81,Reference,Eukaryota,657,"ATP-grasp enzyme; part of the unc gene cluster that mediates the biosynthesis of the tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. Within the pathway, uncJ is responsible for the formation of the dipeptide L-Ala-L-Gln from L-Ala and L-Gln. The alanine racemase uncE first catalyzes the interconversion between L-alanine and D-alanine. D-alanine is then activated by the NRPS uncD that transfers it to the PKS uncA to produce R-dihydroxymethyl isoindolinone. UncF then catalyzes the gamma- replacement of acetate in O-acetyl-L-homoserine (OAH) with R- dihydroxymethyl isoindolinone to generate the amino acid L-O- isoindolinone-homoserine (L-Isd). Then, the ATP-grasp enzyme uncK acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Isd to give the dipeptide L- Leu-L-Isd. Epimerase uncI converts L-Leu-L-Isd to L-Leu-D-Isd in which C-alpha of the Isd residue is epimerized from L to D. UncH is able to hydrolyze dipeptides L-Leu-L-Isd or L-Leu-D-Isd to yield L-Isd or D- Isd, respectively, along with L-Leu. UncG then produces the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln by adding L-Ala-L-Gln produced by the dipeptide synthetase uncJ that forms L-Ala-L-Gln from L-Ala and L- Gln. Finally, hydrolysis of L-Leu-D-Isd-L-Ala-L-Gln by uncH leads to the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B.","ATP-grasp enzyme; part of the unc gene cluster that mediates the biosynthesis of the tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B. Within the pathway, uncJ is responsible for the formation of the dipeptide L-Ala-L-Gln from L-Ala and L-Gln. The alanine racemase uncE first catalyzes the interconversion between L-alanine and D-alanine. D-alanine is then activated by the NRPS uncD that transfers it to the PKS uncA to produce R-dihydroxymethyl isoindolinone. UncF then catalyzes the gamma- replacement of acetate in O-acetyl-L-homoserine (OAH) with R- dihydroxymethyl isoindolinone to generate the amino acid L-O- isoindolinone-homoserine (L-Isd). Then, the ATP-grasp enzyme uncK acts as an amide-bond-forming enzyme that activates the carboxylate of L-Leu for condensation with the amino group in L-Isd to give the dipeptide L- Leu-L-Isd. Epimerase uncI converts L-Leu-L-Isd to L-Leu-D-Isd in which C-alpha of the Isd residue is epimerized from L to D. UncH is able to hydrolyze dipeptides L-Leu-L-Isd or L-Leu-D-Isd to yield L-Isd or D- Isd, respectively, along with L-Leu. UncG then produces the tetrapeptide L-Leu-D-Isd-L-Ala-L-Gln by adding L-Ala-L-Gln produced by the dipeptide synthetase uncJ that forms L-Ala-L-Gln from L-Ala and L- Gln. Finally, hydrolysis of L-Leu-D-Isd-L-Ala-L-Gln by uncH leads to the final tripeptide D-Isd-L-Ala-L-Gln called isoindolamide B.",,,,,,,GO:0005524; GO:0016874; GO:0046872,GO:0016874,GO:0016881; GO:0005524,GO:0016881; GO:0005524,GO:0016881,GO:0016879; GO:0005524,0.5613,0.7337,0.7337,0.3868,0.7836,5,0.6398,0.5016,no
TTUA_TERTT,C5BK10,ESM2Text,Bacteria,642,"Ligase likely involved in the biosynthesis of a polyyne metabolite. Catalyzes the activation of decanoic acid, followed by the loading of the activated decanoic acid onto the acyl carrier protein TtuC. Decanoic acid is the preferred substrate, but it can also use 10-undecenoic acid and lauric acid. Nonanoic acid and 7-octenoic acid are only weakly activated.","Benzoate--CoA ligase that may use 4-coumarate as substrate. Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield the final CoA thioester.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0070566; GO:0005524; GO:0016874,GO:0016405; GO:0005524,GO:0016878,GO:0016878; GO:0005524,GO:0016874,GO:0016207,0.723,0.4195,0.723,0.6106,0.3244,5,0.5601,0.3479,no
TTUA_TERTT,C5BK10,Prot2Text,Bacteria,642,"Ligase likely involved in the biosynthesis of a polyyne metabolite. Catalyzes the activation of decanoic acid, followed by the loading of the activated decanoic acid onto the acyl carrier protein TtuC. Decanoic acid is the preferred substrate, but it can also use 10-undecenoic acid and lauric acid. Nonanoic acid and 7-octenoic acid are only weakly activated.","Activates lipidic moieties required for mycobactin biosynthesis. Converts medium- to long-chain aliphatic fatty acids into acyl adenylate, which is further transferred on to the phosphopantetheine arm of the carrier protein MbtL.",Maybe,Maybe,Maybe,Yes,Yes,not-Yes,GO:0070566; GO:0005524; GO:0016874,GO:0004467,GO:0016874,GO:0016877,GO:0004467,GO:0016877,0.271,0.6106,0.4968,0.271,0.4968,5,0.4292,0.3479,no
TTUA_TERTT,C5BK10,ProtT3,Bacteria,642,"Ligase likely involved in the biosynthesis of a polyyne metabolite. Catalyzes the activation of decanoic acid, followed by the loading of the activated decanoic acid onto the acyl carrier protein TtuC. Decanoic acid is the preferred substrate, but it can also use 10-undecenoic acid and lauric acid. Nonanoic acid and 7-octenoic acid are only weakly activated.","Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the multifunctional polyketide synthase (PKS) for further chain extension. Belongs to the ATP-dependent AMP-binding enzyme family",Maybe,Maybe,Maybe,Yes,Yes,not-Yes,GO:0070566; GO:0005524; GO:0016874,GO:0004467; GO:0005524,GO:0004467,GO:0004467; GO:0005524,GO:0004467,GO:0004467,0.6061,0.271,0.6061,0.271,0.271,5,0.405,0.3479,no
TTUA_TERTT,C5BK10,ProtTale,Bacteria,642,"Ligase likely involved in the biosynthesis of a polyyne metabolite. Catalyzes the activation of decanoic acid, followed by the loading of the activated decanoic acid onto the acyl carrier protein TtuC. Decanoic acid is the preferred substrate, but it can also use 10-undecenoic acid and lauric acid. Nonanoic acid and 7-octenoic acid are only weakly activated.","Catalyzes the activation of amino acids and the addition of the activated amino acid to the 3-hydroxyl group of D-myo-inositol (1-myo-inositol 1,2,3-trisphosphate) to form D-myo- inositol phosphate-amino acid conjugates (1-myo-inositol 1,2,3-trisphosphate amino acid). Mediates the activation of L-aspartic acid and the addition of activated L-aspartic acid to the 3-hydroxyl group of D-myo- inositol to form D-myo-inositol phosphate",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0070566; GO:0005524; GO:0016874,GO:0016874,GO:0016874,GO:0016874,GO:0016874; GO:0005524,GO:0016874,0.6106,0.6106,0.6106,0.871,0.6106,5,0.6627,0.3479,no
TTUA_TERTT,C5BK10,Protein2Text,Bacteria,642,"Ligase likely involved in the biosynthesis of a polyyne metabolite. Catalyzes the activation of decanoic acid, followed by the loading of the activated decanoic acid onto the acyl carrier protein TtuC. Decanoic acid is the preferred substrate, but it can also use 10-undecenoic acid and lauric acid. Nonanoic acid and 7-octenoic acid are only weakly activated.","This protein is a part of the biosynthesis of isoprenoid lipids, specifically a methyltransferase that catalyzes the conversion of CoA-bound precursors into their respective methylated products.",No,No,No,No,No,not-Yes,GO:0070566; GO:0005524; GO:0016874,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.319,0.319,0.319,0.319,0.319,5,0.319,0.3479,no
TTUA_TERTT,C5BK10,Reference,Bacteria,642,"Ligase likely involved in the biosynthesis of a polyyne metabolite. Catalyzes the activation of decanoic acid, followed by the loading of the activated decanoic acid onto the acyl carrier protein TtuC. Decanoic acid is the preferred substrate, but it can also use 10-undecenoic acid and lauric acid. Nonanoic acid and 7-octenoic acid are only weakly activated.","Ligase likely involved in the biosynthesis of a polyyne metabolite. Catalyzes the activation of decanoic acid, followed by the loading of the activated decanoic acid onto the acyl carrier protein TtuC. Decanoic acid is the preferred substrate, but it can also use 10-undecenoic acid and lauric acid. Nonanoic acid and 7-octenoic acid are only weakly activated.",,,,,,,GO:0070566; GO:0005524; GO:0016874,GO:0016874,GO:0016878,GO:0016874,GO:0016878,GO:0016878,0.6106,0.4195,0.6106,0.4195,0.4195,5,0.4959,0.3479,no
APSCT_FASHE,C6EUD4,ESM2Text,Eukaryota,478,"Transferase involved in anaerobic fumarate-respiration in the mitochondria. Catalyzes the transfer of the CoA moiety of acetyl-CoA or propionyl-CoA to succinate, thereby forming acetate and propionate, respectively. Acetate and propionate are the two major metabolic end products in the anaerobic mitochondrial metabolism of F.hepatica. Also displays CoA transferase activities from acetyl-CoA to propionate, acetate and butyrate.",Cleaves the main beta-glycosidic linkage between the amino acid and the 2-oxoglutarate building block of the pyrimidine nucleotide-modifying enzyme complex.,No,No,No,No,No,not-Yes,GO:0008775; GO:0043821,GO:0004553,GO:0004553,,GO:0016798,,0.2353,0.2353,,0.2845,,3,0.2517,0.4813,no
APSCT_FASHE,C6EUD4,Prot2Text,Eukaryota,478,"Transferase involved in anaerobic fumarate-respiration in the mitochondria. Catalyzes the transfer of the CoA moiety of acetyl-CoA or propionyl-CoA to succinate, thereby forming acetate and propionate, respectively. Acetate and propionate are the two major metabolic end products in the anaerobic mitochondrial metabolism of F.hepatica. Also displays CoA transferase activities from acetyl-CoA to propionate, acetate and butyrate.",Coenzyme A-transferase that converts butyrate to butyryl-CoA. Can also use proprionyl-CoA as substrate in vitro.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008775; GO:0043821,GO:0008410,GO:0008410,GO:0008410,GO:0008410,GO:0008410,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.4813,no
APSCT_FASHE,C6EUD4,ProtT3,Eukaryota,478,"Transferase involved in anaerobic fumarate-respiration in the mitochondria. Catalyzes the transfer of the CoA moiety of acetyl-CoA or propionyl-CoA to succinate, thereby forming acetate and propionate, respectively. Acetate and propionate are the two major metabolic end products in the anaerobic mitochondrial metabolism of F.hepatica. Also displays CoA transferase activities from acetyl-CoA to propionate, acetate and butyrate.",Cytoplasm. Belongs to the acetyl-CoA hydrolase/transferase family,Vague,Vague,Maybe,Vague,Vague,not-Yes,GO:0008775; GO:0043821,,,,,,,,,,,0,,0.4813,no
APSCT_FASHE,C6EUD4,ProtTale,Eukaryota,478,"Transferase involved in anaerobic fumarate-respiration in the mitochondria. Catalyzes the transfer of the CoA moiety of acetyl-CoA or propionyl-CoA to succinate, thereby forming acetate and propionate, respectively. Acetate and propionate are the two major metabolic end products in the anaerobic mitochondrial metabolism of F.hepatica. Also displays CoA transferase activities from acetyl-CoA to propionate, acetate and butyrate.","Plays a central role in carbohydrate metabolism. Catalyzes the first committed step in the degradation of glucose to gluconate via 2-keto-3-deoxy-6-phosphogluconate (KDPG). Also catalyzes the phosphorylation of D-fructose to 2-keto-3-deoxy-D-fructose (2-KDG) and D-ribulose 5-phosphate (Ru5P) in a KDPG-dependent reaction. In addition to these activities, displays phosphoglucose isomerase (PGI) and phosphoglucomutase (PGM)",No,No,No,No,No,not-Yes,GO:0008775; GO:0043821,GO:0016301; GO:0004347,GO:0016301,GO:0004347; GO:0004614,GO:0004347; GO:0004614; GO:0016301,GO:0016301; GO:0004347; GO:0004614,0.349,0.3987,0.1998,0.3191,0.3191,5,0.3171,0.4813,no
APSCT_FASHE,C6EUD4,Protein2Text,Eukaryota,478,"Transferase involved in anaerobic fumarate-respiration in the mitochondria. Catalyzes the transfer of the CoA moiety of acetyl-CoA or propionyl-CoA to succinate, thereby forming acetate and propionate, respectively. Acetate and propionate are the two major metabolic end products in the anaerobic mitochondrial metabolism of F.hepatica. Also displays CoA transferase activities from acetyl-CoA to propionate, acetate and butyrate.","The molecular function of this protein is an isomerase, specifically a non-heme dihydroxyacetone-phosphate (DHAP) isomerase that catalyzes the reversible isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P). This is a crucial step in the Calvin cycle of photosynthesis, where DHAP is converted to G3P to replenish the pool of G3P for carbon fixation.",No,No,No,No,No,not-Yes,GO:0008775; GO:0043821,GO:0004807,GO:0004807,GO:0004807,GO:0004807,GO:0004807,0.1998,0.1998,0.1998,0.1998,0.1998,5,0.1998,0.4813,no
APSCT_FASHE,C6EUD4,Reference,Eukaryota,478,"Transferase involved in anaerobic fumarate-respiration in the mitochondria. Catalyzes the transfer of the CoA moiety of acetyl-CoA or propionyl-CoA to succinate, thereby forming acetate and propionate, respectively. Acetate and propionate are the two major metabolic end products in the anaerobic mitochondrial metabolism of F.hepatica. Also displays CoA transferase activities from acetyl-CoA to propionate, acetate and butyrate.","Transferase involved in anaerobic fumarate-respiration in the mitochondria. Catalyzes the transfer of the CoA moiety of acetyl-CoA or propionyl-CoA to succinate, thereby forming acetate and propionate, respectively. Acetate and propionate are the two major metabolic end products in the anaerobic mitochondrial metabolism of F.hepatica. Also displays CoA transferase activities from acetyl-CoA to propionate, acetate and butyrate.",,,,,,,GO:0008775; GO:0043821,GO:0008410,GO:0008410,GO:0008410,GO:0008410,GO:0008410,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.4813,no
CAPA_CAPOD,C7M8J5,ESM2Text,Bacteria,333,"Transferase involved in the biosynthesis of capnine, a sulfonolipid present in the outer membrane of gliding Bacteroidetes and essential for gliding motility. Catalyzes the formation of cysteate from O-phospho-L-serine and sulfite.",Acts as a cysteine synthase. The cysteine synthesis reaction is more efficient than the cyanoalanine synthase activity.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0044686,GO:0004124,GO:0004124,GO:0004124,GO:0004124,GO:0004124,0.7025,0.7025,0.7025,0.7025,0.7025,5,0.7025,0.3147,no
CAPA_CAPOD,C7M8J5,Prot2Text,Bacteria,333,"Transferase involved in the biosynthesis of capnine, a sulfonolipid present in the outer membrane of gliding Bacteroidetes and essential for gliding motility. Catalyzes the formation of cysteate from O-phospho-L-serine and sulfite.",Catalyzes the formation of L-cystathionine from O-acetyl-L-homoserine and hydrogen sulfide. Can also catalyze the formation of L-cysteine from O-acetyl-L-serine and hydrogen sulfide.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0044686,GO:0003962,GO:0003962,GO:0003962,GO:0003961,GO:0003962,0.7025,0.7025,0.7025,0.7025,0.7025,5,0.7025,0.3147,no
CAPA_CAPOD,C7M8J5,ProtT3,Bacteria,333,"Transferase involved in the biosynthesis of capnine, a sulfonolipid present in the outer membrane of gliding Bacteroidetes and essential for gliding motility. Catalyzes the formation of cysteate from O-phospho-L-serine and sulfite.",Belongs to the cysteine synthase/cystathionine beta- synthase family,Vague,Vague,Maybe,Vague,Vague,not-Yes,GO:0044686,,,,,,,,,,,0,,0.3147,no
CAPA_CAPOD,C7M8J5,ProtTale,Bacteria,333,"Transferase involved in the biosynthesis of capnine, a sulfonolipid present in the outer membrane of gliding Bacteroidetes and essential for gliding motility. Catalyzes the formation of cysteate from O-phospho-L-serine and sulfite.","Catalyzes the synthesis of N(4)-acetylcytidine (ac4C) at the wobble position of elongator tRNA(Ile), by using acetyl-CoA as an acetyl donor and ATP. Also catalyzes the synthesis of N(4)-acetyladenine (ac4A) at the wobble position of elongator tRNA(Ile), by using acetyl-CoA as an acetyl donor and ATP.",No,No,No,No,No,not-Yes,GO:0044686,GO:0016407; GO:0005524,GO:0008080; GO:0005524,GO:0016407,GO:0016407; GO:0005524,GO:0016407; GO:0005524,0.2869,0.2315,0.3987,0.2869,0.2869,5,0.2982,0.3147,no
CAPA_CAPOD,C7M8J5,Protein2Text,Bacteria,333,"Transferase involved in the biosynthesis of capnine, a sulfonolipid present in the outer membrane of gliding Bacteroidetes and essential for gliding motility. Catalyzes the formation of cysteate from O-phospho-L-serine and sulfite.","The molecular function of this protein is a transaminase, which is an enzyme that catalyzes the transfer of an amino group from an amino acid to a keto acid. In this case, it is likely involved in the synthesis of amino acids or other metabolites by transferring an amino group from a donor to an acceptor molecule.",Vague,Maybe,No,No,No,not-Yes,GO:0044686,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.4645,0.4645,0.4645,0.4645,0.4645,5,0.4645,0.3147,no
CAPA_CAPOD,C7M8J5,Reference,Bacteria,333,"Transferase involved in the biosynthesis of capnine, a sulfonolipid present in the outer membrane of gliding Bacteroidetes and essential for gliding motility. Catalyzes the formation of cysteate from O-phospho-L-serine and sulfite.","Transferase involved in the biosynthesis of capnine, a sulfonolipid present in the outer membrane of gliding Bacteroidetes and essential for gliding motility. Catalyzes the formation of cysteate from O-phospho-L-serine and sulfite.",,,,,,,GO:0044686,GO:0016740,GO:0016740,GO:0016740,GO:0016740,GO:0016740,0.6897,0.6897,0.6897,0.6897,0.6897,5,0.6897,0.3147,no
CAPB_CAPOD,C7M8J6,ESM2Text,Bacteria,420,"Transferase involved in the biosynthesis of capnine, a sulfonolipid present in the outer membrane of gliding Bacteroidetes and essential for gliding motility. Catalyzes the formation of 3-dehydrocapnine from cysteate and isopentadecanoyl-CoA (13-methyl-myristoyl-CoA). In vitro, products are also detected when 13-methyl-myristic acid is substituted with tridecylic acid, myristic acid, pentadecanoic acid or palmitic acid.","Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.",No,Maybe,No,No,Maybe,not-Yes,GO:0016746; GO:0030170,GO:0008710,GO:0008710,GO:0008710,GO:0016874; GO:0030170,GO:0008710,0.5091,0.5091,0.5091,0.7404,0.5091,5,0.5554,0.3477,no
CAPB_CAPOD,C7M8J6,Prot2Text,Bacteria,420,"Transferase involved in the biosynthesis of capnine, a sulfonolipid present in the outer membrane of gliding Bacteroidetes and essential for gliding motility. Catalyzes the formation of 3-dehydrocapnine from cysteate and isopentadecanoyl-CoA (13-methyl-myristoyl-CoA). In vitro, products are also detected when 13-methyl-myristic acid is substituted with tridecylic acid, myristic acid, pentadecanoic acid or palmitic acid.","Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.",No,Maybe,No,No,Maybe,not-Yes,GO:0016746; GO:0030170,GO:0008710,GO:0004076,GO:0008710,GO:0008710,GO:0008710,0.5091,0.3444,0.5091,0.5091,0.5091,5,0.4762,0.3477,no
CAPB_CAPOD,C7M8J6,ProtT3,Bacteria,420,"Transferase involved in the biosynthesis of capnine, a sulfonolipid present in the outer membrane of gliding Bacteroidetes and essential for gliding motility. Catalyzes the formation of 3-dehydrocapnine from cysteate and isopentadecanoyl-CoA (13-methyl-myristoyl-CoA). In vitro, products are also detected when 13-methyl-myristic acid is substituted with tridecylic acid, myristic acid, pentadecanoic acid or palmitic acid.","Catalyzes the decarboxylative condensation of pimeloyl-[acyl- carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily",No,Maybe,No,No,Maybe,not-Yes,GO:0016746; GO:0030170,GO:0008710; GO:0030170,GO:0008710,GO:0008710,GO:0008710,GO:0008710,0.8645,0.5091,0.5091,0.5091,0.5091,5,0.5802,0.3477,no
CAPB_CAPOD,C7M8J6,ProtTale,Bacteria,420,"Transferase involved in the biosynthesis of capnine, a sulfonolipid present in the outer membrane of gliding Bacteroidetes and essential for gliding motility. Catalyzes the formation of 3-dehydrocapnine from cysteate and isopentadecanoyl-CoA (13-methyl-myristoyl-CoA). In vitro, products are also detected when 13-methyl-myristic acid is substituted with tridecylic acid, myristic acid, pentadecanoic acid or palmitic acid.","Catalyzes the decarboxylative condensation of pimeloyl-[acyl- carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.",No,Maybe,Yes,No,Maybe,not-Yes,GO:0016746; GO:0030170,GO:0008710,GO:0008710,GO:0008710,GO:0004076,GO:0008710,0.5091,0.5091,0.5091,0.3444,0.5091,5,0.4762,0.3477,no
CAPB_CAPOD,C7M8J6,Protein2Text,Bacteria,420,"Transferase involved in the biosynthesis of capnine, a sulfonolipid present in the outer membrane of gliding Bacteroidetes and essential for gliding motility. Catalyzes the formation of 3-dehydrocapnine from cysteate and isopentadecanoyl-CoA (13-methyl-myristoyl-CoA). In vitro, products are also detected when 13-methyl-myristic acid is substituted with tridecylic acid, myristic acid, pentadecanoic acid or palmitic acid.","The molecular function of this protein is a decarboxylase. Specifically, it is a phenylalanine decarboxylase, which catalyzes the decarboxylation of phenylalanine to produce phenylethylamine.",No,No,No,No,No,not-Yes,GO:0016746; GO:0030170,GO:0016831,GO:0004058,GO:0004058,GO:0004058,GO:0004058,0.2459,0.2127,0.2127,0.2127,0.2127,5,0.2193,0.3477,no
CAPB_CAPOD,C7M8J6,Reference,Bacteria,420,"Transferase involved in the biosynthesis of capnine, a sulfonolipid present in the outer membrane of gliding Bacteroidetes and essential for gliding motility. Catalyzes the formation of 3-dehydrocapnine from cysteate and isopentadecanoyl-CoA (13-methyl-myristoyl-CoA). In vitro, products are also detected when 13-methyl-myristic acid is substituted with tridecylic acid, myristic acid, pentadecanoic acid or palmitic acid.","Transferase involved in the biosynthesis of capnine, a sulfonolipid present in the outer membrane of gliding Bacteroidetes and essential for gliding motility. Catalyzes the formation of 3-dehydrocapnine from cysteate and isopentadecanoyl-CoA (13-methyl-myristoyl-CoA). In vitro, products are also detected when 13-methyl-myristic acid is substituted with tridecylic acid, myristic acid, pentadecanoic acid or palmitic acid.",,,,,,,GO:0016746; GO:0030170,GO:0016740,GO:0016746,GO:0016740,GO:0016746,GO:0016747,0.5823,0.6988,0.5823,0.6988,0.588,5,0.63,0.3477,no
MHEI_NOCS4,C8CP46,ESM2Text,Bacteria,242,"Catalyzes the hydrolysis of the fungicide carbendazim (methyl-1H-benzimidazol-2-ylcarbamate or MBC) to 2-aminobenzimidazole (2-AB). Following hydrolysis of the carbamate ester, the carbamate decarboxylates spontaneously (Probable). Can hydrolyze model carboxylesters such as methyl salicylate, alpha-naphthyl acetate and p-nitrophenyl acetate. In addition, shows substantial hydrolytic activity in vitro against widespread pollutants with carboxylester, carbamate and amide linkages, such as dimethyl phthalate, propanil and chlorpropham.","Exhibits esterase activity toward p-nitrophenyl acetate, p-nitrophenylphosphate, methyl capryl-CoA, and p-nitrophenylphosphate. No activity toward n-acetyl-D-glucosamine, acetoacetate or acetate.",Maybe,Maybe,Maybe,Yes,Maybe,not-Yes,GO:0016787,GO:0004091,GO:0004091,GO:0004091,GO:0004091,GO:0004091,0.6897,0.6897,0.6897,0.6897,0.6897,5,0.6897,0.1437,no
MHEI_NOCS4,C8CP46,Prot2Text,Bacteria,242,"Catalyzes the hydrolysis of the fungicide carbendazim (methyl-1H-benzimidazol-2-ylcarbamate or MBC) to 2-aminobenzimidazole (2-AB). Following hydrolysis of the carbamate ester, the carbamate decarboxylates spontaneously (Probable). Can hydrolyze model carboxylesters such as methyl salicylate, alpha-naphthyl acetate and p-nitrophenyl acetate. In addition, shows substantial hydrolytic activity in vitro against widespread pollutants with carboxylester, carbamate and amide linkages, such as dimethyl phthalate, propanil and chlorpropham.","Involved in the degradation of methyl tert-butyl ether (MTBE). Catalyzes the hydrolysis of MTBE to 2-hydroxy-2-methyl-6-oxo-2,4-pregnene-1-carboxylate (HMP-C2).",Maybe,No,No,No,Maybe,not-Yes,GO:0016787,GO:0016787,,,,GO:0016787,1.0,,,,1.0,2,1.0,0.1437,no
MHEI_NOCS4,C8CP46,ProtT3,Bacteria,242,"Catalyzes the hydrolysis of the fungicide carbendazim (methyl-1H-benzimidazol-2-ylcarbamate or MBC) to 2-aminobenzimidazole (2-AB). Following hydrolysis of the carbamate ester, the carbamate decarboxylates spontaneously (Probable). Can hydrolyze model carboxylesters such as methyl salicylate, alpha-naphthyl acetate and p-nitrophenyl acetate. In addition, shows substantial hydrolytic activity in vitro against widespread pollutants with carboxylester, carbamate and amide linkages, such as dimethyl phthalate, propanil and chlorpropham.",Hydrolyzes a wide range of esters. Belongs to the AB hydrolase superfamily. AB hydrolase 2 family,Vague,Maybe,Maybe,Yes,Maybe,not-Yes,GO:0016787,GO:0016788,GO:0052689,GO:0052689,GO:0052689,GO:0016788,0.8145,0.6897,0.6897,0.6897,0.8145,5,0.7396,0.1437,no
MHEI_NOCS4,C8CP46,ProtTale,Bacteria,242,"Catalyzes the hydrolysis of the fungicide carbendazim (methyl-1H-benzimidazol-2-ylcarbamate or MBC) to 2-aminobenzimidazole (2-AB). Following hydrolysis of the carbamate ester, the carbamate decarboxylates spontaneously (Probable). Can hydrolyze model carboxylesters such as methyl salicylate, alpha-naphthyl acetate and p-nitrophenyl acetate. In addition, shows substantial hydrolytic activity in vitro against widespread pollutants with carboxylester, carbamate and amide linkages, such as dimethyl phthalate, propanil and chlorpropham.",Involved in the biosynthesis of the anthracyclines carminomycin and daunorubicin (daunomycin) which are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers.,No,No,No,No,No,not-Yes,GO:0016787,,,,,,,,,,,0,,0.1437,no
MHEI_NOCS4,C8CP46,Protein2Text,Bacteria,242,"Catalyzes the hydrolysis of the fungicide carbendazim (methyl-1H-benzimidazol-2-ylcarbamate or MBC) to 2-aminobenzimidazole (2-AB). Following hydrolysis of the carbamate ester, the carbamate decarboxylates spontaneously (Probable). Can hydrolyze model carboxylesters such as methyl salicylate, alpha-naphthyl acetate and p-nitrophenyl acetate. In addition, shows substantial hydrolytic activity in vitro against widespread pollutants with carboxylester, carbamate and amide linkages, such as dimethyl phthalate, propanil and chlorpropham.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its name, it is likely that this protein is a hydrolase, which is an enzyme that catalyzes the hydrolysis of a chemical bond using water. In particular, the name suggests that it is a phosphohydrolase, which is a type of hydrolase that catalyzes the hydrolysis of a phosphate bond.",Vague,Maybe,Maybe,Vague,Vague,not-Yes,GO:0016787,,GO:0016791,,,GO:0016791,,0.6019,,,0.6019,2,0.6019,0.1437,no
MHEI_NOCS4,C8CP46,Reference,Bacteria,242,"Catalyzes the hydrolysis of the fungicide carbendazim (methyl-1H-benzimidazol-2-ylcarbamate or MBC) to 2-aminobenzimidazole (2-AB). Following hydrolysis of the carbamate ester, the carbamate decarboxylates spontaneously (Probable). Can hydrolyze model carboxylesters such as methyl salicylate, alpha-naphthyl acetate and p-nitrophenyl acetate. In addition, shows substantial hydrolytic activity in vitro against widespread pollutants with carboxylester, carbamate and amide linkages, such as dimethyl phthalate, propanil and chlorpropham.","Catalyzes the hydrolysis of the fungicide carbendazim (methyl-1H-benzimidazol-2-ylcarbamate or MBC) to 2-aminobenzimidazole (2-AB). Following hydrolysis of the carbamate ester, the carbamate decarboxylates spontaneously (Probable). Can hydrolyze model carboxylesters such as methyl salicylate, alpha-naphthyl acetate and p-nitrophenyl acetate. In addition, shows substantial hydrolytic activity in vitro against widespread pollutants with carboxylester, carbamate and amide linkages, such as dimethyl phthalate, propanil and chlorpropham.",,,,,,,GO:0016787,GO:0004091,GO:0004091,GO:0052689,GO:0052689,GO:0004091,0.6897,0.6897,0.6897,0.6897,0.6897,5,0.6897,0.1437,no
TUBE1_BPK32,D1L2W4,ESM2Text,Viruses,192,"Structural component of the tail, which functions as a receptor binding protein (RBP) and mediates the attachment to the host capsular exopolysaccharides. Displays a depolymerase activity that specifically degrades the polysaccharides of Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membrane and bind the entry receptor. Hydrolyzes maltose. Does not hydrolyze alpha-lactose, beta- lactose, trehalose, melibiose, cellobiose. Displays amylase activity.",Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.,No,No,No,No,No,not-Yes,GO:0016798,GO:0004784,GO:0004784,GO:0004784,GO:0004784,GO:0004784,0.3137,0.3137,0.3137,0.3137,0.3137,5,0.3137,0.304,no
TUBE1_BPK32,D1L2W4,Prot2Text,Viruses,192,"Structural component of the tail, which functions as a receptor binding protein (RBP) and mediates the attachment to the host capsular exopolysaccharides. Displays a depolymerase activity that specifically degrades the polysaccharides of Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membrane and bind the entry receptor. Hydrolyzes maltose. Does not hydrolyze alpha-lactose, beta- lactose, trehalose, melibiose, cellobiose. Displays amylase activity.",Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.,No,No,No,No,No,not-Yes,GO:0016798,GO:0004784,GO:0004784,GO:0004784,GO:0004784,GO:0004784,0.3137,0.3137,0.3137,0.3137,0.3137,5,0.3137,0.304,no
TUBE1_BPK32,D1L2W4,ProtT3,Viruses,192,"Structural component of the tail, which functions as a receptor binding protein (RBP) and mediates the attachment to the host capsular exopolysaccharides. Displays a depolymerase activity that specifically degrades the polysaccharides of Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membrane and bind the entry receptor. Hydrolyzes maltose. Does not hydrolyze alpha-lactose, beta- lactose, trehalose, melibiose, cellobiose. Displays amylase activity.","Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection. The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel. Virion. Belongs to the phi29likevirus portal protein family",No,No,No,No,No,not-Yes,GO:0016798,,,,,,,,,,,0,,0.304,no
TUBE1_BPK32,D1L2W4,ProtTale,Viruses,192,"Structural component of the tail, which functions as a receptor binding protein (RBP) and mediates the attachment to the host capsular exopolysaccharides. Displays a depolymerase activity that specifically degrades the polysaccharides of Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membrane and bind the entry receptor. Hydrolyzes maltose. Does not hydrolyze alpha-lactose, beta- lactose, trehalose, melibiose, cellobiose. Displays amylase activity.","Component of the baseplate that is involved in tail assembly, tail tube assembly and viral DNA ejection. During baseplate assembly, baseplate proteins pBP1, pBP2, pBP3, and pBP4 are assembled by a unique baseplate assembly pathway, different from that used to assemble tail tubes, and together they form the central part of the baseplate. As part of the tail assembly machinery, baseplate has ATPase activity and functions together with the tail tube to form the tubular structure of the tail. Plays a role in baseplate assembly by interacting with the bases of pBP1, pBP2, and",No,No,No,No,No,not-Yes,GO:0016798,GO:0016887,GO:0016887,GO:0016887,GO:0016887,GO:0016887,0.3785,0.3785,0.3785,0.3785,0.3785,5,0.3785,0.304,no
TUBE1_BPK32,D1L2W4,Protein2Text,Viruses,192,"Structural component of the tail, which functions as a receptor binding protein (RBP) and mediates the attachment to the host capsular exopolysaccharides. Displays a depolymerase activity that specifically degrades the polysaccharides of Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membrane and bind the entry receptor. Hydrolyzes maltose. Does not hydrolyze alpha-lactose, beta- lactose, trehalose, melibiose, cellobiose. Displays amylase activity.","The molecular function of this protein is to form the tail tube, which is a component of the phage tail.",Vague,Maybe,Vague,No,No,not-Yes,GO:0016798,GO:0005198,GO:0005198,GO:0005198,,,0.2761,0.2761,0.2761,,,3,0.2761,0.304,no
TUBE1_BPK32,D1L2W4,Reference,Viruses,192,"Structural component of the tail, which functions as a receptor binding protein (RBP) and mediates the attachment to the host capsular exopolysaccharides. Displays a depolymerase activity that specifically degrades the polysaccharides of Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membrane and bind the entry receptor. Hydrolyzes maltose. Does not hydrolyze alpha-lactose, beta- lactose, trehalose, melibiose, cellobiose. Displays amylase activity.","Structural component of the tail, which functions as a receptor binding protein (RBP) and mediates the attachment to the host capsular exopolysaccharides. Displays a depolymerase activity that specifically degrades the polysaccharides of Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membrane and bind the entry receptor. Hydrolyzes maltose. Does not hydrolyze alpha-lactose, beta- lactose, trehalose, melibiose, cellobiose. Displays amylase activity.",,,,,,,GO:0016798,GO:0004556; GO:0016798,GO:0016798; GO:0004556,GO:0016798; GO:0004556,GO:0016798; GO:0004556,GO:0016798; GO:0004556,0.8822,0.8822,0.8822,0.8822,0.8822,5,0.8822,0.304,no
TUBE1_BPK34,D1L2Y9,ESM2Text,Viruses,186,"Structural component of the tail, which functions as a receptor binding protein (RBP) and mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a depolymerase activity that specifically degrades the polysaccharides of Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membrane and bind the entry receptor. Hydrolyzes trehalose.","Rod linker protein, associated with phycocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer.",No,No,No,No,No,not-Yes,GO:0004555,,,,,,,,,,,0,,0.3063,no
TUBE1_BPK34,D1L2Y9,Prot2Text,Viruses,186,"Structural component of the tail, which functions as a receptor binding protein (RBP) and mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a depolymerase activity that specifically degrades the polysaccharides of Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membrane and bind the entry receptor. Hydrolyzes trehalose.","Rod linker protein, associated with phycocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer.",No,No,No,No,No,not-Yes,GO:0004555,,,,,,,,,,,0,,0.3063,no
TUBE1_BPK34,D1L2Y9,ProtT3,Viruses,186,"Structural component of the tail, which functions as a receptor binding protein (RBP) and mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a depolymerase activity that specifically degrades the polysaccharides of Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membrane and bind the entry receptor. Hydrolyzes trehalose.","Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection. The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel. Virion. Belongs to the phi29likevirus portal protein family",No,No,No,No,No,not-Yes,GO:0004555,,,,,,,,,,,0,,0.3063,no
TUBE1_BPK34,D1L2Y9,ProtTale,Viruses,186,"Structural component of the tail, which functions as a receptor binding protein (RBP) and mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a depolymerase activity that specifically degrades the polysaccharides of Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membrane and bind the entry receptor. Hydrolyzes trehalose.",Component of the baseplate that is involved in recognition of the host cell and in baseplate assembly.,No,Maybe,No,No,Maybe,not-Yes,GO:0004555,,,,,,,,,,,0,,0.3063,no
TUBE1_BPK34,D1L2Y9,Protein2Text,Viruses,186,"Structural component of the tail, which functions as a receptor binding protein (RBP) and mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a depolymerase activity that specifically degrades the polysaccharides of Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membrane and bind the entry receptor. Hydrolyzes trehalose.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its classification as a protein involved in a viral capsid, it can be inferred that it plays a role in the structure and assembly of the viral capsid, possibly as a component of the viral genome or a capsid protein.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0004555,,GO:0005198,GO:0005198,,,,0.1847,0.1847,,,2,0.1847,0.3063,no
TUBE1_BPK34,D1L2Y9,Reference,Viruses,186,"Structural component of the tail, which functions as a receptor binding protein (RBP) and mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a depolymerase activity that specifically degrades the polysaccharides of Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membrane and bind the entry receptor. Hydrolyzes trehalose.","Structural component of the tail, which functions as a receptor binding protein (RBP) and mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a depolymerase activity that specifically degrades the polysaccharides of Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membrane and bind the entry receptor. Hydrolyzes trehalose.",,,,,,,GO:0004555,GO:0004555; GO:0016798,GO:0016798; GO:0004555,GO:0016798; GO:0004555,GO:0016798; GO:0004555,GO:0016798; GO:0004555,0.8822,0.8822,0.8822,0.8822,0.8822,5,0.8822,0.3063,no
R15PI_HALTV,D2RW80,ESM2Text,Archaea,327,"Isomerase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the isomerization of ribose 1,5-bisphosphate (R15P) to ribulose 1,5-bisphosphate (RuBP).",Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).,No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0043917; GO:0046523,GO:0016853,GO:0016853,GO:0016853,GO:0016862,GO:0019144,0.6019,0.6019,0.6019,0.6029,0.1737,5,0.5165,0.4117,no
R15PI_HALTV,D2RW80,Prot2Text,Archaea,327,"Isomerase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the isomerization of ribose 1,5-bisphosphate (R15P) to ribulose 1,5-bisphosphate (RuBP).","Catalyzes the isomerization of ribose 1,5-bisphosphate (R15P) to ribulose 1,5-bisphosphate (RuBP), the CO(2) acceptor and substrate for RubisCO. Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and RubisCO.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0043917; GO:0046523,GO:0016853,GO:0016853,GO:0016853,GO:0016853,GO:0016861,0.6019,0.6019,0.6019,0.6019,0.8582,5,0.6532,0.4117,no
R15PI_HALTV,D2RW80,ProtT3,Archaea,327,"Isomerase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the isomerization of ribose 1,5-bisphosphate (R15P) to ribulose 1,5-bisphosphate (RuBP).","Catalyzes the isomerization of ribose 1,5-bisphosphate (R15P) to ribulose 1,5-bisphosphate (RuBP), the CO(2) acceptor and substrate for RubisCO. Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and RubisCO. Belongs to the eIF-2B alpha/beta/delta subunits family. R15P isomerase subfamily",Yes,Yes,Yes,Yes,Yes,Yes,GO:0043917; GO:0046523,GO:0016853,GO:0016853,GO:0016853,GO:0016853,GO:0016853,0.6019,0.6019,0.6019,0.6019,0.6019,5,0.6019,0.4117,no
R15PI_HALTV,D2RW80,ProtTale,Archaea,327,"Isomerase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the isomerization of ribose 1,5-bisphosphate (R15P) to ribulose 1,5-bisphosphate (RuBP).",Catalyzes the oxidation of glycerate 2-phosphate to 3-phosphoglycerate.,No,No,No,No,No,not-Yes,GO:0043917; GO:0046523,GO:0016616,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.2353,0.3552,0.3552,0.3552,0.3552,5,0.3312,0.4117,no
R15PI_HALTV,D2RW80,Protein2Text,Archaea,327,"Isomerase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the isomerization of ribose 1,5-bisphosphate (R15P) to ribulose 1,5-bisphosphate (RuBP).","The molecular function of this protein is as an isomerase, specifically a ribulose biosynthetic enzyme. It catalyzes the conversion of ribose 5-phosphate to ribulose 5-phosphate, a key step in the biosynthesis of various sugars.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0043917; GO:0046523,GO:0004751,GO:0004751,GO:0004751,GO:0004751,GO:0004751,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.4117,no
R15PI_HALTV,D2RW80,Reference,Archaea,327,"Isomerase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the isomerization of ribose 1,5-bisphosphate (R15P) to ribulose 1,5-bisphosphate (RuBP).","Isomerase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the isomerization of ribose 1,5-bisphosphate (R15P) to ribulose 1,5-bisphosphate (RuBP).",,,,,,,GO:0043917; GO:0046523,GO:0016853,GO:0016853,GO:0016853,GO:0016853,GO:0016853,0.6019,0.6019,0.6019,0.6019,0.6019,5,0.6019,0.4117,no
SPAST_NAEGR,D2VS83,ESM2Text,Eukaryota,523,ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle.,ATP-dependent microtubule severing protein. Microtubule severing may promote reorganization of cellular microtubule arrays and the release of microtubules from the microtubule organizing center following nucleation.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0008568,GO:0008568; GO:0005524,GO:0008568,GO:0008568,GO:0008568; GO:0005524,GO:0008568,0.8556,0.5851,0.5851,0.8556,0.5851,5,0.6933,0.4613,no
SPAST_NAEGR,D2VS83,Prot2Text,Eukaryota,523,ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle.,ATP-dependent microtubule severing protein. Microtubule severing may promote reorganization of cellular microtubule arrays and the release of microtubules from the microtubule organizing center following nucleation.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0016887; GO:0008568,GO:0008568; GO:0005524,GO:0008568,GO:0008568,GO:0008568,GO:0008568,0.8556,0.5851,0.5851,0.5851,0.5851,5,0.6392,0.4613,no
SPAST_NAEGR,D2VS83,ProtT3,Eukaryota,523,ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle.,Membrane; Peripheral membrane protein. Belongs to the AAA ATPase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0016887; GO:0008568,GO:0016887,GO:0016887,GO:0016887,GO:0016887,GO:0016887; GO:0005524,0.5847,0.5847,0.5847,0.5847,0.8556,5,0.6389,0.4613,no
SPAST_NAEGR,D2VS83,ProtTale,Eukaryota,523,ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle.,ATP-dependent microtubule severing protein that forms microtubules shorter than control microtubules in vitro. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome after nucleation. Microtubule severing may also promote disassembly of mitotic spindle microtubules. Microtubule severing may promote microtubule severing in addition to its role in severing microtubules. Microtubule severing may promote microtubule severing in addition to its role in severing microtubules.,No,No,No,No,No,not-Yes,GO:0005524; GO:0016887; GO:0008568,GO:0008568; GO:0005524,GO:0008568; GO:0005524,GO:0008568,GO:0008568; GO:0005524,GO:0008568; GO:0005524,0.8556,0.8556,0.5851,0.8556,0.8556,5,0.8015,0.4613,no
SPAST_NAEGR,D2VS83,Protein2Text,Eukaryota,523,ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle.,"The molecular function of this protein is not specified in the given text. However, it is known to be involved in the transport of molecules across cell membranes, specifically in the transport of proteins from the endoplasmic reticulum to the Golgi apparatus. It is also involved in the regulation of protein folding and trafficking. 

The protein is a component of the COPI complex, which is involved in retrograde transport of proteins from the Golgi to the endoplasmic reticulum. It is also involved in the transport of proteins from the endoplasmic reticulum to the Golgi apparatus and from the Golgi apparatus to the plasma membrane. 

In addition, this protein is also involved in the regulation of protein folding and trafficking. It is believed to play a role in the recognition and sorting of misfolded proteins for degradation by the proteasome. 

It is also involved in the regulation of protein trafficking from the endoplasmic reticulum to the Golgi apparatus. It is believed to play a role in the recognition and sorting of proteins for transport to the Golgi apparatus. 

The protein is also involved in the regulation of protein trafficking from the Golgi apparatus to the plasma membrane. It is believed to play a role in the recognition and sorting of proteins for transport to the plasma membrane. 

It is also involved in the regulation of protein trafficking from the endoplasmic reticulum to the plasma membrane. It is believed to play a role in the recognition and sorting of proteins for transport to the plasma membrane. 

The protein is also involved in the regulation of protein trafficking from the Golgi apparatus to the endoplasmic reticulum. It is believed to play a role in the recognition and sorting of proteins for transport to the endoplasmic reticulum. 

It is also involved in the regulation of protein trafficking from the endoplasmic reticulum to the Golgi apparatus. It is believed to play a role in the recognition and sorting of proteins for transport to the Golgi apparatus. 

The protein is also involved in the regulation of protein trafficking from the Golgi apparatus to the plasma membrane. It is believed to play a role in the recognition and sorting of proteins for transport to the plasma membrane. 

It is also involved in the regulation of protein trafficking from the endoplasmic reticulum to the plasma membrane. It is believed to play a role in the recognition and sorting of proteins for transport to the plasma membrane. 

The protein is also involved in the",No,No,No,No,No,not-Yes,GO:0005524; GO:0016887; GO:0008568,,,,,,,,,,,0,,0.4613,no
SPAST_NAEGR,D2VS83,Reference,Eukaryota,523,ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle.,ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle.,,,,,,,GO:0005524; GO:0016887; GO:0008568,GO:0008568,GO:0008568; GO:0005524,GO:0008568; GO:0005524,GO:0008568,GO:0008568; GO:0005524,0.5851,0.8556,0.8556,0.5851,0.8556,5,0.7474,0.4613,no
D19L1_RAT,D4AD75,ESM2Text,Eukaryota,746,C-mannosyltransferase that mediates the C-mannosylation tryptophan residues on target proteins. The reaction occurs on the luminal side of the endoplasmic reticulum and involves the transfer of a mannose unit from a dolichylphosphate mannose (Dol-P-Man) donor to an acceptor protein containing a WxxW consensus sequence. C-mannosylates the first two tryptophans in the WxxWxxWxxC sequence motif in thrombospondin (TSP) type-1 repeats of UNC5A. Regulates neurite extension during development.,Probable C-mannosyltransferase that mediates C-mannosylation of tryptophan residues on target proteins.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0000030,GO:0033555,GO:0016757,GO:0016757,GO:0019187,GO:0019187,0.0,0.729,0.729,0.8691,0.8691,5,0.6392,0.6706,yes
D19L1_RAT,D4AD75,Prot2Text,Eukaryota,746,C-mannosyltransferase that mediates the C-mannosylation tryptophan residues on target proteins. The reaction occurs on the luminal side of the endoplasmic reticulum and involves the transfer of a mannose unit from a dolichylphosphate mannose (Dol-P-Man) donor to an acceptor protein containing a WxxW consensus sequence. C-mannosylates the first two tryptophans in the WxxWxxWxxC sequence motif in thrombospondin (TSP) type-1 repeats of UNC5A. Regulates neurite extension during development.,Probable C-mannosyltransferase that mediates C-mannosylation of tryptophan residues on target proteins.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0000030,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.729,0.729,0.729,0.729,0.729,5,0.729,0.6706,yes
D19L1_RAT,D4AD75,ProtT3,Eukaryota,746,C-mannosyltransferase that mediates the C-mannosylation tryptophan residues on target proteins. The reaction occurs on the luminal side of the endoplasmic reticulum and involves the transfer of a mannose unit from a dolichylphosphate mannose (Dol-P-Man) donor to an acceptor protein containing a WxxW consensus sequence. C-mannosylates the first two tryptophans in the WxxWxxWxxC sequence motif in thrombospondin (TSP) type-1 repeats of UNC5A. Regulates neurite extension during development.,Probable C-mannosyltransferase that mediates C-mannosylation of tryptophan residues on target proteins. Membrane; Multi-pass membrane protein. Belongs to the dpy-19 family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0000030,GO:0120083,GO:0019187,GO:0019187,GO:0019187,GO:0000030,0.0,0.8691,0.8691,0.8691,1.0,5,0.7215,0.6706,yes
D19L1_RAT,D4AD75,ProtTale,Eukaryota,746,C-mannosyltransferase that mediates the C-mannosylation tryptophan residues on target proteins. The reaction occurs on the luminal side of the endoplasmic reticulum and involves the transfer of a mannose unit from a dolichylphosphate mannose (Dol-P-Man) donor to an acceptor protein containing a WxxW consensus sequence. C-mannosylates the first two tryptophans in the WxxWxxWxxC sequence motif in thrombospondin (TSP) type-1 repeats of UNC5A. Regulates neurite extension during development.,C-mannosyltransferase that mediates C-mannosylation of tryptophan residues on target proteins.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0000030,GO:0016757,GO:0000030,GO:0016757,GO:0016757,GO:0016757,0.729,1.0,0.729,0.729,0.729,5,0.7832,0.6706,yes
D19L1_RAT,D4AD75,Protein2Text,Eukaryota,746,C-mannosyltransferase that mediates the C-mannosylation tryptophan residues on target proteins. The reaction occurs on the luminal side of the endoplasmic reticulum and involves the transfer of a mannose unit from a dolichylphosphate mannose (Dol-P-Man) donor to an acceptor protein containing a WxxW consensus sequence. C-mannosylates the first two tryptophans in the WxxWxxWxxC sequence motif in thrombospondin (TSP) type-1 repeats of UNC5A. Regulates neurite extension during development.,"The molecular function of this protein is not explicitly stated in the provided text. However, based on its name, it is likely involved in the synthesis or modification of proteins, specifically in the formation of a mannose (Man) residue on the Dolichol-linked oligosaccharide (Dol-PO4-GlcNAc2-Man9) precursor.",Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0000030,,GO:0000030,GO:0000030,,GO:0000030,,1.0,1.0,,1.0,3,1.0,0.6706,yes
D19L1_RAT,D4AD75,Reference,Eukaryota,746,C-mannosyltransferase that mediates the C-mannosylation tryptophan residues on target proteins. The reaction occurs on the luminal side of the endoplasmic reticulum and involves the transfer of a mannose unit from a dolichylphosphate mannose (Dol-P-Man) donor to an acceptor protein containing a WxxW consensus sequence. C-mannosylates the first two tryptophans in the WxxWxxWxxC sequence motif in thrombospondin (TSP) type-1 repeats of UNC5A. Regulates neurite extension during development.,C-mannosyltransferase that mediates the C-mannosylation tryptophan residues on target proteins. The reaction occurs on the luminal side of the endoplasmic reticulum and involves the transfer of a mannose unit from a dolichylphosphate mannose (Dol-P-Man) donor to an acceptor protein containing a WxxW consensus sequence. C-mannosylates the first two tryptophans in the WxxWxxWxxC sequence motif in thrombospondin (TSP) type-1 repeats of UNC5A. Regulates neurite extension during development.,,,,,,,GO:0000030,GO:0019187,GO:0019187,GO:0016757,GO:0019187,GO:0019187,0.8691,0.8691,0.729,0.8691,0.8691,5,0.8411,0.6706,yes
TRM9_HALVD,D4GVK8,ESM2Text,Archaea,217,Catalyzes the methylation of 5-carboxymethyl uridine (cm(5)U) to 5-methylcarboxymethyl uridine (mcm(5)U) at the wobble position (U34) in tRNA.,S-adenosyl-L-methionine-dependent methyltransferase that mediates N(3)-methylcytidine modification of residue 32 of the tRNA anticodon loop of tRNA(Phe) and tRNA(Leu(UAA)).,No,Maybe,No,Maybe,Maybe,not-Yes,GO:0106335,GO:0008173,GO:0008173,GO:0008173,GO:0008173,GO:0008175,0.7313,0.7313,0.7313,0.7313,0.8465,5,0.7543,0.301,no
TRM9_HALVD,D4GVK8,Prot2Text,Archaea,217,Catalyzes the methylation of 5-carboxymethyl uridine (cm(5)U) to 5-methylcarboxymethyl uridine (mcm(5)U) at the wobble position (U34) in tRNA.,"S-adenosyl-L-methionine-dependent methyltransferase involved in the biosynthesis of mycaminose, a 16-amino-18-keto-7-deazaguanine (AKDN) moiety present in the genome of the mycaminose kinase.",No,No,No,No,No,not-Yes,GO:0106335,GO:0008168,GO:0008757,GO:0008168,GO:0008757,GO:0008757,0.535,0.4444,0.535,0.4444,0.4444,5,0.4806,0.301,no
TRM9_HALVD,D4GVK8,ProtT3,Archaea,217,Catalyzes the methylation of 5-carboxymethyl uridine (cm(5)U) to 5-methylcarboxymethyl uridine (mcm(5)U) at the wobble position (U34) in tRNA.,Catalyzes the S-adenosylmethionine-dependent methylation of 2'-O-ribose in 23S rRNA. Belongs to the methyltransferase superfamily,No,No,No,No,Maybe,not-Yes,GO:0106335,GO:0008649,GO:0008649,GO:0008173,GO:0008173,GO:0008173,0.5567,0.5567,0.7313,0.7313,0.7313,5,0.6615,0.301,no
TRM9_HALVD,D4GVK8,ProtTale,Archaea,217,Catalyzes the methylation of 5-carboxymethyl uridine (cm(5)U) to 5-methylcarboxymethyl uridine (mcm(5)U) at the wobble position (U34) in tRNA.,Removes the 2'-O-phosphate from double-stranded RNA:,No,No,No,No,No,not-Yes,GO:0106335,GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,0.1292,0.1292,0.1292,0.1292,0.1292,5,0.1292,0.301,no
TRM9_HALVD,D4GVK8,Protein2Text,Archaea,217,Catalyzes the methylation of 5-carboxymethyl uridine (cm(5)U) to 5-methylcarboxymethyl uridine (mcm(5)U) at the wobble position (U34) in tRNA.,"The molecular function of this protein is a methyltransferase. It is involved in the transfer of a methyl group to a molecule, specifically it is a one-carbon methyltransferase. This protein is likely involved in the methylation of a substrate molecule, such as a nucleotide or an amino acid, in order to modify its structure or function. The exact substrate of this protein is not specified in the provided information, but it is likely involved in a metabolic or biosynthetic pathway. 
Further, the protein is associated with the biosynthesis of a compound called molybdopterin, which is a cofactor for a class of enzymes called molybdoenzymes. Molybdopterin is a complex molecule that contains molybdenum, a metal ion, and is essential for the function of molybdoenzymes, which are involved in various metabolic processes, including the metabolism of nitrogen, sulfur, and carbon. The protein is likely involved in the biosynthesis of molybdopterin by catalyzing the methylation of a substrate molecule, such as a nucleotide or an amino acid, to produce a methylated intermediate that is then incorporated into the molybdopterin molecule.",Vague,Vague,Maybe,Vague,Vague,not-Yes,GO:0106335,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.535,0.535,0.535,0.535,0.535,5,0.535,0.301,no
TRM9_HALVD,D4GVK8,Reference,Archaea,217,Catalyzes the methylation of 5-carboxymethyl uridine (cm(5)U) to 5-methylcarboxymethyl uridine (mcm(5)U) at the wobble position (U34) in tRNA.,Catalyzes the methylation of 5-carboxymethyl uridine (cm(5)U) to 5-methylcarboxymethyl uridine (mcm(5)U) at the wobble position (U34) in tRNA.,,,,,,,GO:0106335,GO:0008176,GO:0008168,GO:0008168,GO:0008175,GO:0008176,0.6535,0.535,0.535,0.8465,0.6535,5,0.6447,0.301,no
MRSB_PSESY,D5FKJ2,ESM2Text,Bacteria,387,"Aminotransferase involved in the formation of the rare amino acid 3-methylarginine (MeArg), which is used as a potent antibiotic against the closely related soybean pathogen P.syringae pv. glycinea. Probably catalyzes transamination from the donor L- aspartate to 5-guanidino-3-methyl-2-oxopentanoic acid, generating 3- methylarginine (Probable).","Involved in the biosynthesis of alanine. Catalyzes the transamination of pyruvate by glutamate, leading to the formation of L-alanine and 2-oxoglutarate. Also catalyzes the reverse reaction.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0030170; GO:0008483,GO:0004021,GO:0008483,GO:0004021,GO:0004021,GO:0008483,0.5228,0.6936,0.5228,0.5228,0.6936,5,0.5911,0.1555,no
MRSB_PSESY,D5FKJ2,Prot2Text,Bacteria,387,"Aminotransferase involved in the formation of the rare amino acid 3-methylarginine (MeArg), which is used as a potent antibiotic against the closely related soybean pathogen P.syringae pv. glycinea. Probably catalyzes transamination from the donor L- aspartate to 5-guanidino-3-methyl-2-oxopentanoic acid, generating 3- methylarginine (Probable).","Involved in the biosynthesis of alanine. Catalyzes the transamination of pyruvate by glutamate, leading to the formation of L-alanine and 2-oxoglutarate. Is also able to catalyze the reverse reaction.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0030170; GO:0008483,GO:0008483,GO:0004021,GO:0004021,GO:0004021,GO:0008483,0.6936,0.5228,0.5228,0.5228,0.6936,5,0.5911,0.1555,no
MRSB_PSESY,D5FKJ2,ProtT3,Bacteria,387,"Aminotransferase involved in the formation of the rare amino acid 3-methylarginine (MeArg), which is used as a potent antibiotic against the closely related soybean pathogen P.syringae pv. glycinea. Probably catalyzes transamination from the donor L- aspartate to 5-guanidino-3-methyl-2-oxopentanoic acid, generating 3- methylarginine (Probable).",Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0030170; GO:0008483,GO:0008483; GO:0030170,GO:0008483,,GO:0008483; GO:0030170,GO:0008483; GO:0030170,1.0,0.6936,,1.0,1.0,4,0.9234,0.1555,no
MRSB_PSESY,D5FKJ2,ProtTale,Bacteria,387,"Aminotransferase involved in the formation of the rare amino acid 3-methylarginine (MeArg), which is used as a potent antibiotic against the closely related soybean pathogen P.syringae pv. glycinea. Probably catalyzes transamination from the donor L- aspartate to 5-guanidino-3-methyl-2-oxopentanoic acid, generating 3- methylarginine (Probable).","Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3- dihydroxybenzoyl)-serine. Enterobactin is capable of transporting iron from the environment into the cell, and thus plays an important role in maintaining iron homeostasis.",No,No,No,No,No,not-Yes,GO:0030170; GO:0008483,,,,,,,,,,,0,,0.1555,no
MRSB_PSESY,D5FKJ2,Protein2Text,Bacteria,387,"Aminotransferase involved in the formation of the rare amino acid 3-methylarginine (MeArg), which is used as a potent antibiotic against the closely related soybean pathogen P.syringae pv. glycinea. Probably catalyzes transamination from the donor L- aspartate to 5-guanidino-3-methyl-2-oxopentanoic acid, generating 3- methylarginine (Probable).","This protein is involved in the biosynthesis of tryptophan. It is a dehydrogenase enzyme that catalyzes the conversion of indole-3-glycerol phosphate to indole, which is an intermediate step in the biosynthesis of tryptophan. Specifically, it catalyzes the oxidation of indole-3-glycerol phosphate to indole and 3-keto-2-hydroxyglutaric acid. This reaction is an important step in the biosynthesis of tryptophan, as it allows the organism to convert the intermediate indole-3-glycerol phosphate into indole, which can then be used to synthesize tryptophan.",No,No,No,No,No,not-Yes,GO:0030170; GO:0008483,GO:0016829,,,,GO:0004834,0.3107,,,,0.1799,2,0.2453,0.1555,no
MRSB_PSESY,D5FKJ2,Reference,Bacteria,387,"Aminotransferase involved in the formation of the rare amino acid 3-methylarginine (MeArg), which is used as a potent antibiotic against the closely related soybean pathogen P.syringae pv. glycinea. Probably catalyzes transamination from the donor L- aspartate to 5-guanidino-3-methyl-2-oxopentanoic acid, generating 3- methylarginine (Probable).","Aminotransferase involved in the formation of the rare amino acid 3-methylarginine (MeArg), which is used as a potent antibiotic against the closely related soybean pathogen P.syringae pv. glycinea. Probably catalyzes transamination from the donor L- aspartate to 5-guanidino-3-methyl-2-oxopentanoic acid, generating 3- methylarginine (Probable).",,,,,,,GO:0030170; GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.6936,0.6936,0.6936,0.6936,0.6936,5,0.6936,0.1555,no
NSP2_ROTRH,D5LJN4,ESM2Text,Viruses,317,"Participates in replication and packaging of the viral genome. Plays a crucial role, together with NSP5, in the formation of virus factories (viroplasms), which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Displays ssRNA binding, NTPase, RNA triphosphatase (RTPase) and ATP-independent helix-unwinding activities. The unwinding activity may prepare and organize plus-strand RNAs for packaging and replication by removing interfering secondary structures. The RTPase activity plays a role in the removal of the gamma-phosphate from the rotavirus RNA minus strands of dsRNA genome segments. Participates in the selective exclusion of host proteins from stress granules (SG) and P bodies (PB). Also participates in the sequestration of these remodeled organelles in viral factories.",Replication initiation factor.,Vague,No,Maybe,Vague,Vague,not-Yes,GO:0005524; GO:0046872; GO:0004550; GO:0017111; GO:0003723,,,,,,,,,,,0,,0.3434,no
NSP2_ROTRH,D5LJN4,Prot2Text,Viruses,317,"Participates in replication and packaging of the viral genome. Plays a crucial role, together with NSP5, in the formation of virus factories (viroplasms), which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Displays ssRNA binding, NTPase, RNA triphosphatase (RTPase) and ATP-independent helix-unwinding activities. The unwinding activity may prepare and organize plus-strand RNAs for packaging and replication by removing interfering secondary structures. The RTPase activity plays a role in the removal of the gamma-phosphate from the rotavirus RNA minus strands of dsRNA genome segments. Participates in the selective exclusion of host proteins from stress granules (SG) and P bodies (PB). Also participates in the sequestration of these remodeled organelles in viral factories.",Replication initiation factor.,Vague,No,Maybe,Vague,Vague,not-Yes,GO:0005524; GO:0046872; GO:0004550; GO:0017111; GO:0003723,,,,,,,,,,,0,,0.3434,no
NSP2_ROTRH,D5LJN4,ProtT3,Viruses,317,"Participates in replication and packaging of the viral genome. Plays a crucial role, together with NSP5, in the formation of virus factories (viroplasms), which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Displays ssRNA binding, NTPase, RNA triphosphatase (RTPase) and ATP-independent helix-unwinding activities. The unwinding activity may prepare and organize plus-strand RNAs for packaging and replication by removing interfering secondary structures. The RTPase activity plays a role in the removal of the gamma-phosphate from the rotavirus RNA minus strands of dsRNA genome segments. Participates in the selective exclusion of host proteins from stress granules (SG) and P bodies (PB). Also participates in the sequestration of these remodeled organelles in viral factories.","Participates in replication and packaging of the viral genome. Plays a crucial role, together with NSP5, in the formation of virus factories (viroplasms) which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Displays ssRNA binding, NTPase, RNA triphosphatase (RTPase) and ATP-independent helix-unwinding activities. The unwinding activity may prepare and organize plus-strand RNAs for packaging and replication by removing interfering secondary structures. The RTPase activity plays a role in the removal of the gamma-phosphate from",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0046872; GO:0004550; GO:0017111; GO:0003723,GO:0017111; GO:0004651; GO:0004386; GO:0003723,GO:0003724; GO:0004651; GO:0003723,GO:0003723; GO:0016887; GO:0004386,GO:0017111; GO:0003724; GO:0003727,GO:0003724; GO:0005524; GO:0003723,0.5642,0.4057,0.5586,0.5439,0.5898,5,0.5324,0.3434,no
NSP2_ROTRH,D5LJN4,ProtTale,Viruses,317,"Participates in replication and packaging of the viral genome. Plays a crucial role, together with NSP5, in the formation of virus factories (viroplasms), which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Displays ssRNA binding, NTPase, RNA triphosphatase (RTPase) and ATP-independent helix-unwinding activities. The unwinding activity may prepare and organize plus-strand RNAs for packaging and replication by removing interfering secondary structures. The RTPase activity plays a role in the removal of the gamma-phosphate from the rotavirus RNA minus strands of dsRNA genome segments. Participates in the selective exclusion of host proteins from stress granules (SG) and P bodies (PB). Also participates in the sequestration of these remodeled organelles in viral factories.","Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for viral transcription and replication.",No,No,No,No,No,not-Yes,GO:0005524; GO:0046872; GO:0004550; GO:0017111; GO:0003723,,GO:0003723,GO:0003723,GO:0003723,GO:0003723,,0.4443,0.4443,0.4443,0.4443,4,0.4443,0.3434,no
NSP2_ROTRH,D5LJN4,Protein2Text,Viruses,317,"Participates in replication and packaging of the viral genome. Plays a crucial role, together with NSP5, in the formation of virus factories (viroplasms), which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Displays ssRNA binding, NTPase, RNA triphosphatase (RTPase) and ATP-independent helix-unwinding activities. The unwinding activity may prepare and organize plus-strand RNAs for packaging and replication by removing interfering secondary structures. The RTPase activity plays a role in the removal of the gamma-phosphate from the rotavirus RNA minus strands of dsRNA genome segments. Participates in the selective exclusion of host proteins from stress granules (SG) and P bodies (PB). Also participates in the sequestration of these remodeled organelles in viral factories.","This protein is a component of a viral particle, specifically a coronavirus. It is not explicitly stated what its molecular function is, but based on its classification as a protein, it is likely involved in some aspect of viral replication or protein synthesis. However, without more information, it is difficult to determine its specific molecular function.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0046872; GO:0004550; GO:0017111; GO:0003723,,,,,,,,,,,0,,0.3434,no
NSP2_ROTRH,D5LJN4,Reference,Viruses,317,"Participates in replication and packaging of the viral genome. Plays a crucial role, together with NSP5, in the formation of virus factories (viroplasms), which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Displays ssRNA binding, NTPase, RNA triphosphatase (RTPase) and ATP-independent helix-unwinding activities. The unwinding activity may prepare and organize plus-strand RNAs for packaging and replication by removing interfering secondary structures. The RTPase activity plays a role in the removal of the gamma-phosphate from the rotavirus RNA minus strands of dsRNA genome segments. Participates in the selective exclusion of host proteins from stress granules (SG) and P bodies (PB). Also participates in the sequestration of these remodeled organelles in viral factories.","Participates in replication and packaging of the viral genome. Plays a crucial role, together with NSP5, in the formation of virus factories (viroplasms), which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Displays ssRNA binding, NTPase, RNA triphosphatase (RTPase) and ATP-independent helix-unwinding activities. The unwinding activity may prepare and organize plus-strand RNAs for packaging and replication by removing interfering secondary structures. The RTPase activity plays a role in the removal of the gamma-phosphate from the rotavirus RNA minus strands of dsRNA genome segments. Participates in the selective exclusion of host proteins from stress granules (SG) and P bodies (PB). Also participates in the sequestration of these remodeled organelles in viral factories.",,,,,,,GO:0005524; GO:0046872; GO:0004550; GO:0017111; GO:0003723,GO:0016887; GO:0004386; GO:0003723,GO:0003723; GO:0016887; GO:0004651; GO:0003724,GO:0003723; GO:0017111; GO:0004651; GO:0008026,GO:0003724; GO:0016887; GO:0003723,GO:0003724; GO:0004651; GO:0003723; GO:0016887,0.5586,0.5152,0.5642,0.5479,0.5152,5,0.5402,0.3434,no
HPS_STRCL,D5SK09,ESM2Text,Bacteria,321,"Terpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) into a mixture of diterpenes, including hydropyrene (HP), hydropyrenol (HPol), isoelisabethatriene and traces of isoelisabethatriene B. Hydropyrene is the main product. Some other diterpenoids are also produced in very low quantities.","Involved in the biosynthesis of the bicyclic sesquiterpene C11-beta(3),8-diene. Catalyzes the cyclization of farnesyl diphosphate (FPP) to yield corbate and the subsequent rearrangement of the monoterpene C11-beta(3),8-diene to yield the bicyclic corbate via a 1,10-cyclization.",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0010333,GO:0010333,GO:0010333,,GO:0010334,0.6963,0.6963,0.6963,,0.6051,4,0.6735,0.2012,no
HPS_STRCL,D5SK09,Prot2Text,Bacteria,321,"Terpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) into a mixture of diterpenes, including hydropyrene (HP), hydropyrenol (HPol), isoelisabethatriene and traces of isoelisabethatriene B. Hydropyrene is the main product. Some other diterpenoids are also produced in very low quantities.","Involved in the biosynthesis of the labdane-type bicyclic diterpene labda-8(17),12(E),14-triene. Catalyzes the conversion of (+)-copalyl diphosphate to yield labda-8(17),12(E),14-triene.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0016829,GO:0010333,GO:0010333,GO:0010333,GO:0010333,0.4539,0.6963,0.6963,0.6963,0.6963,5,0.6478,0.2012,no
HPS_STRCL,D5SK09,ProtT3,Bacteria,321,"Terpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) into a mixture of diterpenes, including hydropyrene (HP), hydropyrenol (HPol), isoelisabethatriene and traces of isoelisabethatriene B. Hydropyrene is the main product. Some other diterpenoids are also produced in very low quantities.","Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to (2Z,6Z)-farnesyl diphosphate (Z-FPP). Belongs to the terpene synthase family",No,No,Maybe,No,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0016853,GO:0016853,GO:0016853,GO:0016853,GO:0016853,0.2894,0.2894,0.2894,0.2894,0.2894,5,0.2894,0.2012,no
HPS_STRCL,D5SK09,ProtTale,Bacteria,321,"Terpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) into a mixture of diterpenes, including hydropyrene (HP), hydropyrenol (HPol), isoelisabethatriene and traces of isoelisabethatriene B. Hydropyrene is the main product. Some other diterpenoids are also produced in very low quantities.","Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to yield the bicyclic sesquiterpene (1R,6S,7S)-(-)-(E)-beta-caryophyllene via a 1,10-cyclization, which requires the abstraction of the pyrophosphate from FPP to yield a (E)-beta-caryophyllene cation.",No,Maybe,Maybe,No,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0010333,GO:0016829,GO:0010333,GO:0016829,GO:0010333,0.6963,0.4539,0.6963,0.4539,0.6963,5,0.5993,0.2012,no
HPS_STRCL,D5SK09,Protein2Text,Bacteria,321,"Terpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) into a mixture of diterpenes, including hydropyrene (HP), hydropyrenol (HPol), isoelisabethatriene and traces of isoelisabethatriene B. Hydropyrene is the main product. Some other diterpenoids are also produced in very low quantities.","This protein is involved in catalyzing the biosynthesis of sesquiterpenes. More specifically, it is a part of a pathway that produces a sesquiterpene, specifically a sesquiterpene with a specific structure. The exact molecular function of this protein is not specified, but it is likely involved in converting a precursor molecule into the final product.",Vague,Vague,Maybe,Vague,Vague,not-Yes,GO:0046872; GO:0010333,,,,,GO:0010333,,,,,0.6963,1,0.6963,0.2012,no
HPS_STRCL,D5SK09,Reference,Bacteria,321,"Terpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) into a mixture of diterpenes, including hydropyrene (HP), hydropyrenol (HPol), isoelisabethatriene and traces of isoelisabethatriene B. Hydropyrene is the main product. Some other diterpenoids are also produced in very low quantities.","Terpene synthase that catalyzes the conversion of geranylgeranyl diphosphate (GGPP) into a mixture of diterpenes, including hydropyrene (HP), hydropyrenol (HPol), isoelisabethatriene and traces of isoelisabethatriene B. Hydropyrene is the main product. Some other diterpenoids are also produced in very low quantities.",,,,,,,GO:0046872; GO:0010333,GO:0016829,GO:0016829,GO:0010333,GO:0016829,GO:0010333,0.4539,0.4539,0.6963,0.4539,0.6963,5,0.5509,0.2012,no
LIP6_MALFU,D9N4H4,ESM2Text,Eukaryota,385,"Secreted lipase that hydrolyzes acylglycerol lipids such as triacylglycerols and consequently releases free fatty acid. Can hydrolyze 4-nitrophenyl palmitate to release 4- nitrophenol and palmitoic acid. Due to an absence of fatty acid synthase genes in Malassezia species, secretory lipases are essential for the yeast to generate free fatty acids from degradation of sebum and assimilate them as lipid sources for growth. Plays important roles not only in lipid metabolism but also in the immune response of host cells and pathogenesis (Probable).","Involved in the degradation of unsaturated fatty acids. Catalyzes the hydrolysis of palmitate (C16), but not (C18)-CoA, to the corresponding (C3)-CoA. Its physiological role remains unclear.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004806,GO:0016790,GO:0016790,,GO:0016787,,0.5415,0.5415,,0.5324,,3,0.5385,0.3138,no
LIP6_MALFU,D9N4H4,Prot2Text,Eukaryota,385,"Secreted lipase that hydrolyzes acylglycerol lipids such as triacylglycerols and consequently releases free fatty acid. Can hydrolyze 4-nitrophenyl palmitate to release 4- nitrophenol and palmitoic acid. Due to an absence of fatty acid synthase genes in Malassezia species, secretory lipases are essential for the yeast to generate free fatty acids from degradation of sebum and assimilate them as lipid sources for growth. Plays important roles not only in lipid metabolism but also in the immune response of host cells and pathogenesis (Probable).",Involved in the degradation of plant cell wall polysaccharides. Hydrolyzes medium- and long-chain monoacylglycerols.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004806,GO:0016788,GO:0016788,GO:0016298,GO:0052689,GO:0016787,0.6506,0.6506,0.7707,0.7707,0.5324,5,0.675,0.3138,no
LIP6_MALFU,D9N4H4,ProtT3,Eukaryota,385,"Secreted lipase that hydrolyzes acylglycerol lipids such as triacylglycerols and consequently releases free fatty acid. Can hydrolyze 4-nitrophenyl palmitate to release 4- nitrophenol and palmitoic acid. Due to an absence of fatty acid synthase genes in Malassezia species, secretory lipases are essential for the yeast to generate free fatty acids from degradation of sebum and assimilate them as lipid sources for growth. Plays important roles not only in lipid metabolism but also in the immune response of host cells and pathogenesis (Probable).",Secreted. Belongs to the AB hydrolase superfamily. Lipase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004806,GO:0016298,GO:0016298,GO:0004806,GO:0004806,GO:0016298,0.7707,0.7707,1.0,1.0,0.7707,5,0.8624,0.3138,no
LIP6_MALFU,D9N4H4,ProtTale,Eukaryota,385,"Secreted lipase that hydrolyzes acylglycerol lipids such as triacylglycerols and consequently releases free fatty acid. Can hydrolyze 4-nitrophenyl palmitate to release 4- nitrophenol and palmitoic acid. Due to an absence of fatty acid synthase genes in Malassezia species, secretory lipases are essential for the yeast to generate free fatty acids from degradation of sebum and assimilate them as lipid sources for growth. Plays important roles not only in lipid metabolism but also in the immune response of host cells and pathogenesis (Probable).","Secreted lipase that hydrolyzes acylglycerol lipids such as triacylglycerols and thus plays a role in various functions such as cell wall degradation and virulence. Plays a role in cell wall integrity maintenance. In vitro, catalyzes the hydrolysis of p-nitrophenylpalmitate, p-nitrophenyloleate and p-nitrophenyllinoleate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004806,GO:0004806,GO:0004806; GO:0016298,GO:0004806,GO:0004806; GO:0016298,GO:0004806,1.0,0.9236,1.0,0.9236,1.0,5,0.9694,0.3138,no
LIP6_MALFU,D9N4H4,Protein2Text,Eukaryota,385,"Secreted lipase that hydrolyzes acylglycerol lipids such as triacylglycerols and consequently releases free fatty acid. Can hydrolyze 4-nitrophenyl palmitate to release 4- nitrophenol and palmitoic acid. Due to an absence of fatty acid synthase genes in Malassezia species, secretory lipases are essential for the yeast to generate free fatty acids from degradation of sebum and assimilate them as lipid sources for growth. Plays important roles not only in lipid metabolism but also in the immune response of host cells and pathogenesis (Probable).","The molecular function of this protein is an esterase, which is an enzyme that breaks down esters into an acid and an alcohol. More specifically, it is a secreted esterase involved in the degradation of esterified lipids. This protein is likely involved in the breakdown of complex lipids, such as triglycerides, into simpler fatty acids and glycerol. It is also likely involved in the production of volatile organic compounds (VOCs) through the hydrolysis of esters.",Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004806,GO:0004091,GO:0004091,GO:0004091,GO:0004091,GO:0004091,0.7707,0.7707,0.7707,0.7707,0.7707,5,0.7707,0.3138,no
LIP6_MALFU,D9N4H4,Reference,Eukaryota,385,"Secreted lipase that hydrolyzes acylglycerol lipids such as triacylglycerols and consequently releases free fatty acid. Can hydrolyze 4-nitrophenyl palmitate to release 4- nitrophenol and palmitoic acid. Due to an absence of fatty acid synthase genes in Malassezia species, secretory lipases are essential for the yeast to generate free fatty acids from degradation of sebum and assimilate them as lipid sources for growth. Plays important roles not only in lipid metabolism but also in the immune response of host cells and pathogenesis (Probable).","Secreted lipase that hydrolyzes acylglycerol lipids such as triacylglycerols and consequently releases free fatty acid. Can hydrolyze 4-nitrophenyl palmitate to release 4- nitrophenol and palmitoic acid. Due to an absence of fatty acid synthase genes in Malassezia species, secretory lipases are essential for the yeast to generate free fatty acids from degradation of sebum and assimilate them as lipid sources for growth. Plays important roles not only in lipid metabolism but also in the immune response of host cells and pathogenesis (Probable).",,,,,,,GO:0004806,GO:0004806,GO:0004806; GO:0016298,GO:0004806,GO:0004806; GO:0016298,GO:0004806,1.0,0.9236,1.0,0.9236,1.0,5,0.9694,0.3138,no
HCGE_METTM,D9PY12,ESM2Text,Archaea,212,"Product of one of the 7 hmd co-occurring genes (hcg), hcgA-G, which cluster with the [Fe]-hydrogenase-encoding gene hmd and are required for the biosynthesis of the iron-guanylylpyridinol (FeGP) cofactor used by [Fe]-hydrogenase. HcgE catalyzes the adenylation of the carboxy group of guanylylpyridinol to form guanylylpyridinol-AMP.","Catalyzes the formation of 3-(3-amino-3-carboxypropyl)uridine (acp3U) at position 20a in the D-loop of several cytoplasmic tRNAs (acp3U(20a)). Also has an independent pyrophosphate phosphohydrolase activity, as this subunit does not carry out the phosphate excision.",No,No,No,No,No,not-Yes,GO:0005524; GO:0160301,GO:0016462,GO:0016740,,GO:0016757,,0.1517,0.4304,,0.3458,,3,0.3093,0.3069,no
HCGE_METTM,D9PY12,Prot2Text,Archaea,212,"Product of one of the 7 hmd co-occurring genes (hcg), hcgA-G, which cluster with the [Fe]-hydrogenase-encoding gene hmd and are required for the biosynthesis of the iron-guanylylpyridinol (FeGP) cofactor used by [Fe]-hydrogenase. HcgE catalyzes the adenylation of the carboxy group of guanylylpyridinol to form guanylylpyridinol-AMP.","Together with AceAa, is involved in the anaerobic metabolism of butyryl-CoA, an important precursor for the synthesis of phenylalanine and tyrosine. Catalyzes the oxidative phosphorylation of 3-hydroxy-2-methylbutyrate (3-HMB) to yield 2-methylbutyrate (MEB). The enzyme is specific for butyryl-CoA as substrate.",No,No,No,No,No,not-Yes,GO:0005524; GO:0160301,GO:0016491,,,,GO:0016491,0.2659,,,,0.2659,2,0.2659,0.3069,no
HCGE_METTM,D9PY12,ProtT3,Archaea,212,"Product of one of the 7 hmd co-occurring genes (hcg), hcgA-G, which cluster with the [Fe]-hydrogenase-encoding gene hmd and are required for the biosynthesis of the iron-guanylylpyridinol (FeGP) cofactor used by [Fe]-hydrogenase. HcgE catalyzes the adenylation of the carboxy group of guanylylpyridinol to form guanylylpyridinol-AMP.","Catalyzes the ATP-dependent conversion of L-lysine to N(2)-succinyl-L-glutamate semialdehyde, which spontaneously cyclizes to form 2- succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). In the C-terminal section; belongs to the pyridoxal-phosphate-dependent aminotransferase family",No,No,No,No,No,not-Yes,GO:0005524; GO:0160301,GO:0008483; GO:0030170,GO:0008483,GO:0008483,GO:0008483; GO:0030170,GO:0008483; GO:0030170,0.4127,0.2869,0.2869,0.4127,0.4127,5,0.3624,0.3069,no
HCGE_METTM,D9PY12,ProtTale,Archaea,212,"Product of one of the 7 hmd co-occurring genes (hcg), hcgA-G, which cluster with the [Fe]-hydrogenase-encoding gene hmd and are required for the biosynthesis of the iron-guanylylpyridinol (FeGP) cofactor used by [Fe]-hydrogenase. HcgE catalyzes the adenylation of the carboxy group of guanylylpyridinol to form guanylylpyridinol-AMP.",Involved in the biosynthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. Catalyzes the hydrolysis of 5-O-acetyl-D-myo-inositol 2-phosphate to yield D-myo-inositol 1-phosphate and acetyl-CoA.,No,No,No,No,No,not-Yes,GO:0005524; GO:0160301,GO:0016787,GO:0016787,GO:0016787,GO:0016788,GO:0016787,0.2659,0.2659,0.2659,0.2141,0.2659,5,0.2555,0.3069,no
HCGE_METTM,D9PY12,Protein2Text,Archaea,212,"Product of one of the 7 hmd co-occurring genes (hcg), hcgA-G, which cluster with the [Fe]-hydrogenase-encoding gene hmd and are required for the biosynthesis of the iron-guanylylpyridinol (FeGP) cofactor used by [Fe]-hydrogenase. HcgE catalyzes the adenylation of the carboxy group of guanylylpyridinol to form guanylylpyridinol-AMP.","This protein is involved in the molecular function of 'acetyltransferase activity'. 
It is a component of the E.coli acetyltransferase complex that catalyzes acetylation of the Lys-59 residue of the 30S ribosomal protein S12. It is not known if it acetylates other proteins. It is also able to acetylate the N-terminal residues of peptides containing a free N-terminal alpha-amino group, suggesting it may have a more general acetyltransferase function. It is not known if it has any other biological functions. It is not known if it has any other biological functions. 
It is a component of the E.coli acetyltransferase complex that catalyzes acetylation of the Lys-59 residue of the 30S ribosomal protein S12. It is not known if it acetylates other proteins. It is also able to acetylate the N-terminal residues of peptides containing a free N-terminal alpha-amino group, suggesting it may have a more general acetyltransferase function. It is not known if it has any other biological functions. 
It is a component of the E.coli acetyltransferase complex that catalyzes acetylation of the Lys-59 residue of the 30S ribosomal protein S12. It is not known if it acetylates other proteins. It is also able to acetylate the N-terminal residues of peptides containing a free N-terminal alpha-amino group, suggesting it may have a more general acetyltransferase function. It is not known if it has any other biological functions.",Vague,No,No,Vague,No,not-Yes,GO:0005524; GO:0160301,GO:0016407,GO:0016407,GO:0008080,GO:0016407,GO:0016407,0.2443,0.2443,0.1932,0.2443,0.2443,5,0.2341,0.3069,no
HCGE_METTM,D9PY12,Reference,Archaea,212,"Product of one of the 7 hmd co-occurring genes (hcg), hcgA-G, which cluster with the [Fe]-hydrogenase-encoding gene hmd and are required for the biosynthesis of the iron-guanylylpyridinol (FeGP) cofactor used by [Fe]-hydrogenase. HcgE catalyzes the adenylation of the carboxy group of guanylylpyridinol to form guanylylpyridinol-AMP.","Product of one of the 7 hmd co-occurring genes (hcg), hcgA-G, which cluster with the [Fe]-hydrogenase-encoding gene hmd and are required for the biosynthesis of the iron-guanylylpyridinol (FeGP) cofactor used by [Fe]-hydrogenase. HcgE catalyzes the adenylation of the carboxy group of guanylylpyridinol to form guanylylpyridinol-AMP.",,,,,,,GO:0005524; GO:0160301,GO:0016874,GO:0016874,GO:0016874; GO:0005524,GO:0016874,GO:0016779,0.2659,0.2659,0.6776,0.2659,0.5932,5,0.4137,0.3069,no
T2OK1_OCEKR,E2JKI3,ESM2Text,Bacteria,194,A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-GGATCC-3' and cleaves after G-1.,A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-CTAG-3'; the cleavage site is unknown.,Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0003677; GO:0000287; GO:0009036,GO:0004519; GO:0003677,GO:0004519,GO:0015666,GO:0015666,GO:0004519,0.6511,0.3103,0.4755,0.4755,0.3103,5,0.4445,0.3456,no
T2OK1_OCEKR,E2JKI3,Prot2Text,Bacteria,194,A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-GGATCC-3' and cleaves after G-1.,An E and P subtype restriction enzyme that recognizes the double-stranded sequence 5'-CTGCAG-3' and cleaves after C-1.,Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0003677; GO:0000287; GO:0009036,GO:0009036,GO:0009036,GO:0009036,GO:0009036,GO:0009036,0.5336,0.5336,0.5336,0.5336,0.5336,5,0.5336,0.3456,no
T2OK1_OCEKR,E2JKI3,ProtT3,Bacteria,194,A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-GGATCC-3' and cleaves after G-1.,A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-GATC-3' and cleaves after G-1,Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0003677; GO:0000287; GO:0009036,GO:0004519; GO:0003677,GO:0004519,GO:0004519,GO:0004519; GO:0003677,GO:0015666,0.6511,0.3103,0.3103,0.6511,0.4755,5,0.4797,0.3456,no
T2OK1_OCEKR,E2JKI3,ProtTale,Bacteria,194,A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-GGATCC-3' and cleaves after G-1.,An antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the toxic effect of cognate toxin RelE.,Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0003677; GO:0000287; GO:0009036,,,,,,,,,,,0,,0.3456,no
T2OK1_OCEKR,E2JKI3,Protein2Text,Bacteria,194,A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-GGATCC-3' and cleaves after G-1.,"This protein is an endonuclease, specifically a restriction enzyme that cleaves DNA at a specific recognition site. It is a part of the bacterial defense system that protects against viral infections by degrading foreign DNA. The molecular function of this protein is to cleave DNA at the recognition site 5'-CGATCG-3'.",Vague,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0003677; GO:0000287; GO:0009036,GO:0004519,GO:0009036,GO:0015666; GO:0004519,GO:0015666,GO:0009036,0.3103,0.5336,0.4971,0.4755,0.5336,5,0.47,0.3456,no
T2OK1_OCEKR,E2JKI3,Reference,Bacteria,194,A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-GGATCC-3' and cleaves after G-1.,A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-GGATCC-3' and cleaves after G-1.,,,,,,,GO:0003677; GO:0000287; GO:0009036,GO:0009036,GO:0009036; GO:0004519,GO:0015666,GO:0009036,GO:0009036,0.5336,0.5479,0.4755,0.5336,0.5336,5,0.5248,0.3456,no
SAUD_BILW3,E5Y8P7,ESM2Text,Bacteria,293,"Involved in the degradation of sulfoacetate. Catalyzes the CoA- and ATP-dependent conversion of sulfoacetate to sulfoacetyl-CoA and ADP. Cannot use other sulfonic and carboxylic acids, and shows only residual activity with 3-sulfopropanoate and malonic acid.","Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.",No,No,Maybe,Maybe,Maybe,not-Yes,GO:0000166; GO:0004775; GO:0004776,GO:0004775; GO:0005524,GO:0004774,GO:0004775; GO:0004776,GO:0003824; GO:0004775,GO:0004775,0.7644,0.6778,0.8186,0.6749,0.7099,5,0.7291,0.6419,yes
SAUD_BILW3,E5Y8P7,Prot2Text,Bacteria,293,"Involved in the degradation of sulfoacetate. Catalyzes the CoA- and ATP-dependent conversion of sulfoacetate to sulfoacetyl-CoA and ADP. Cannot use other sulfonic and carboxylic acids, and shows only residual activity with 3-sulfopropanoate and malonic acid.","Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.",No,No,Maybe,Maybe,Maybe,not-Yes,GO:0000166; GO:0004775; GO:0004776,GO:0004775,GO:0004775,GO:0004775,GO:0004775; GO:0004776,GO:0004775,0.7099,0.7099,0.7099,0.8186,0.7099,5,0.7316,0.6419,yes
SAUD_BILW3,E5Y8P7,ProtT3,Bacteria,293,"Involved in the degradation of sulfoacetate. Catalyzes the CoA- and ATP-dependent conversion of sulfoacetate to sulfoacetyl-CoA and ADP. Cannot use other sulfonic and carboxylic acids, and shows only residual activity with 3-sulfopropanoate and malonic acid.","Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit. Belongs to the succinate/malate CoA ligase alpha subunit family",No,No,Maybe,Maybe,Maybe,not-Yes,GO:0000166; GO:0004775; GO:0004776,GO:0004775; GO:0000166,GO:0004775,GO:0004775,GO:0004775,GO:0004775; GO:0005524,0.9494,0.7099,0.7099,0.7099,0.7644,5,0.7687,0.6419,yes
SAUD_BILW3,E5Y8P7,ProtTale,Bacteria,293,"Involved in the degradation of sulfoacetate. Catalyzes the CoA- and ATP-dependent conversion of sulfoacetate to sulfoacetyl-CoA and ADP. Cannot use other sulfonic and carboxylic acids, and shows only residual activity with 3-sulfopropanoate and malonic acid.",Catalyzes the hydrolysis of 6-phosphogluconolactone to 6- phosphogluconate.,No,No,No,No,No,not-Yes,GO:0000166; GO:0004775; GO:0004776,GO:0017057,GO:0004349,GO:0017057,GO:0017057,GO:0017057,0.1562,0.1317,0.1562,0.1562,0.1562,5,0.1513,0.6419,yes
SAUD_BILW3,E5Y8P7,Protein2Text,Bacteria,293,"Involved in the degradation of sulfoacetate. Catalyzes the CoA- and ATP-dependent conversion of sulfoacetate to sulfoacetyl-CoA and ADP. Cannot use other sulfonic and carboxylic acids, and shows only residual activity with 3-sulfopropanoate and malonic acid.","The molecular function of this protein is an enzyme that catalyzes the conversion of carbamoyl phosphate and ornithine to citrulline and phosphate. It is a key enzyme in the urea cycle, which is responsible for the conversion of ammonia to urea for excretion. This protein is also known as ornithine transcarbamylase.",No,No,No,No,No,not-Yes,GO:0000166; GO:0004775; GO:0004776,GO:0004585,GO:0004585,GO:0004585,GO:0004585,GO:0004585,0.1562,0.1562,0.1562,0.1562,0.1562,5,0.1562,0.6419,yes
SAUD_BILW3,E5Y8P7,Reference,Bacteria,293,"Involved in the degradation of sulfoacetate. Catalyzes the CoA- and ATP-dependent conversion of sulfoacetate to sulfoacetyl-CoA and ADP. Cannot use other sulfonic and carboxylic acids, and shows only residual activity with 3-sulfopropanoate and malonic acid.","Involved in the degradation of sulfoacetate. Catalyzes the CoA- and ATP-dependent conversion of sulfoacetate to sulfoacetyl-CoA and ADP. Cannot use other sulfonic and carboxylic acids, and shows only residual activity with 3-sulfopropanoate and malonic acid.",,,,,,,GO:0000166; GO:0004775; GO:0004776,GO:0016877,GO:0016878; GO:0005524,GO:0016874; GO:0005524,GO:0016878,GO:0016878,0.5198,0.6673,0.5379,0.5951,0.5951,5,0.583,0.6419,yes
TARB1_MOUSE,E9Q368,ESM2Text,Eukaryota,1579,S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 18 (Gm18) in a subset of tRNA. Selectively mediates Gm18 methylation of tRNAGln-TTG/CTG and tRNASer-TGA/GCT. Gm18 modification can enhance the stability of modified tRNAs.,"Subunit of the trimeric nuclear exosome targeting (NEXT) complex that is involved in the surveillance and turnover of aberrant transcripts and non-coding RNAs. NEXT functions as an RNA exosome cofactor that directs a subset of non-coding short-lived RNAs for exosomal degradation. May be involved in pre-mRNA splicing. It is required for 3'-end maturation of telomerase RNA component (TERC), TERC 3'-end targeting to the nuclear RNA exosome, and for telomerase function.",No,No,No,No,No,not-Yes,GO:0003723; GO:0141100; GO:0016423,,GO:0003723,GO:0003723,,,,0.5385,0.5385,,,2,0.5385,0.6198,yes
TARB1_MOUSE,E9Q368,Prot2Text,Eukaryota,1579,S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 18 (Gm18) in a subset of tRNA. Selectively mediates Gm18 methylation of tRNAGln-TTG/CTG and tRNASer-TGA/GCT. Gm18 modification can enhance the stability of modified tRNAs.,"As part of AP-5, a probable fifth adaptor protein complex it may be involved in endosomal transport. According to PubMed:20613862 it is a putative helicase required for efficient homologous recombination DNA double-strand break repair.",No,No,No,No,No,not-Yes,GO:0003723; GO:0141100; GO:0016423,,,,,,,,,,,0,,0.6198,yes
TARB1_MOUSE,E9Q368,ProtT3,Eukaryota,1579,S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 18 (Gm18) in a subset of tRNA. Selectively mediates Gm18 methylation of tRNAGln-TTG/CTG and tRNASer-TGA/GCT. Gm18 modification can enhance the stability of modified tRNAs.,"Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). Nucleus Cytoplasm, cytoskeleton, spindle",No,No,No,No,No,not-Yes,GO:0003723; GO:0141100; GO:0016423,GO:0061630,GO:0061630,GO:0061630,GO:0004842,GO:0004842,0.1434,0.1434,0.1434,0.1738,0.1738,5,0.1556,0.6198,yes
TARB1_MOUSE,E9Q368,ProtTale,Eukaryota,1579,S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 18 (Gm18) in a subset of tRNA. Selectively mediates Gm18 methylation of tRNAGln-TTG/CTG and tRNASer-TGA/GCT. Gm18 modification can enhance the stability of modified tRNAs.,Essential for sperm motility and male fertility. Required for normal mitochondrial morphology and distribution in the midpiece and principal piece of the sperm flagellum. May be involved in protein transport.,No,No,No,No,No,not-Yes,GO:0003723; GO:0141100; GO:0016423,,,,,,,,,,,0,,0.6198,yes
TARB1_MOUSE,E9Q368,Protein2Text,Eukaryota,1579,S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 18 (Gm18) in a subset of tRNA. Selectively mediates Gm18 methylation of tRNAGln-TTG/CTG and tRNASer-TGA/GCT. Gm18 modification can enhance the stability of modified tRNAs.,"The molecular function of the protein is a cytoplasmic retromer complex component, which plays a role in endosome-to-Golgi retrograde transport of proteins.",No,No,No,No,No,not-Yes,GO:0003723; GO:0141100; GO:0016423,,,,,,,,,,,0,,0.6198,yes
TARB1_MOUSE,E9Q368,Reference,Eukaryota,1579,S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 18 (Gm18) in a subset of tRNA. Selectively mediates Gm18 methylation of tRNAGln-TTG/CTG and tRNASer-TGA/GCT. Gm18 modification can enhance the stability of modified tRNAs.,S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 18 (Gm18) in a subset of tRNA. Selectively mediates Gm18 methylation of tRNAGln-TTG/CTG and tRNASer-TGA/GCT. Gm18 modification can enhance the stability of modified tRNAs.,,,,,,,GO:0003723; GO:0141100; GO:0016423,GO:0008176,GO:0008168; GO:0000049,GO:0008173,GO:0008175,GO:0008176,0.6939,0.6529,0.5702,0.6557,0.6939,5,0.6533,0.6198,yes
VIOM_TRIRC,F2SL82,ESM2Text,Eukaryota,454,"Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of viomellein, a red mycelium pigment and potent antibacterial compound that may aid the progression of pathogenesis. Within the pathway, the reductase vioC and the O-methyltransferase vioM catalyze the reduction and the methylation reactions that convert nor-toralactone into semivioxanthin. The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic heptaketide nor-toralactone. The short-chain dehydrogenase/reductase vioC and the O-methyltransferase vioM then convert nor-toralactone into semivioxanthin. Semivioxanthin is probably transported across the plasma membrane by the viomellein- specific pump vioT for further enzymatic processing by the extracellular complex composed of vioL, vioF, vioO1 and vioO2 to yield final viomellein. The multicopper oxidase vioL with the help of vioF are involved in dimerization of semivioxanthin to vioxanthin. Finally, the monooxygenase vioO1 and the FAD-linked oxidoreductase vioO2 are responsible of several oxidations leading to the formation of viomellein and xanthomegnin. Semixanthomegnin is also produced by the cluster, however, the order of the reactions could not be determined (Probable).","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome P450 monooxygenase P450-2 then catalyzes the dimerization of nataloe-emodin to cladofulvin.",No,No,No,No,No,not-Yes,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2259,no
VIOM_TRIRC,F2SL82,Prot2Text,Eukaryota,454,"Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of viomellein, a red mycelium pigment and potent antibacterial compound that may aid the progression of pathogenesis. Within the pathway, the reductase vioC and the O-methyltransferase vioM catalyze the reduction and the methylation reactions that convert nor-toralactone into semivioxanthin. The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic heptaketide nor-toralactone. The short-chain dehydrogenase/reductase vioC and the O-methyltransferase vioM then convert nor-toralactone into semivioxanthin. Semivioxanthin is probably transported across the plasma membrane by the viomellein- specific pump vioT for further enzymatic processing by the extracellular complex composed of vioL, vioF, vioO1 and vioO2 to yield final viomellein. The multicopper oxidase vioL with the help of vioF are involved in dimerization of semivioxanthin to vioxanthin. Finally, the monooxygenase vioO1 and the FAD-linked oxidoreductase vioO2 are responsible of several oxidations leading to the formation of viomellein and xanthomegnin. Semixanthomegnin is also produced by the cluster, however, the order of the reactions could not be determined (Probable).","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate tolerance, py",No,No,No,No,No,not-Yes,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2259,no
VIOM_TRIRC,F2SL82,ProtT3,Eukaryota,454,"Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of viomellein, a red mycelium pigment and potent antibacterial compound that may aid the progression of pathogenesis. Within the pathway, the reductase vioC and the O-methyltransferase vioM catalyze the reduction and the methylation reactions that convert nor-toralactone into semivioxanthin. The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic heptaketide nor-toralactone. The short-chain dehydrogenase/reductase vioC and the O-methyltransferase vioM then convert nor-toralactone into semivioxanthin. Semivioxanthin is probably transported across the plasma membrane by the viomellein- specific pump vioT for further enzymatic processing by the extracellular complex composed of vioL, vioF, vioO1 and vioO2 to yield final viomellein. The multicopper oxidase vioL with the help of vioF are involved in dimerization of semivioxanthin to vioxanthin. Finally, the monooxygenase vioO1 and the FAD-linked oxidoreductase vioO2 are responsible of several oxidations leading to the formation of viomellein and xanthomegnin. Semixanthomegnin is also produced by the cluster, however, the order of the reactions could not be determined (Probable).","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By similarity). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (By similarity). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the ter",No,No,No,No,No,not-Yes,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2259,no
VIOM_TRIRC,F2SL82,ProtTale,Eukaryota,454,"Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of viomellein, a red mycelium pigment and potent antibacterial compound that may aid the progression of pathogenesis. Within the pathway, the reductase vioC and the O-methyltransferase vioM catalyze the reduction and the methylation reactions that convert nor-toralactone into semivioxanthin. The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic heptaketide nor-toralactone. The short-chain dehydrogenase/reductase vioC and the O-methyltransferase vioM then convert nor-toralactone into semivioxanthin. Semivioxanthin is probably transported across the plasma membrane by the viomellein- specific pump vioT for further enzymatic processing by the extracellular complex composed of vioL, vioF, vioO1 and vioO2 to yield final viomellein. The multicopper oxidase vioL with the help of vioF are involved in dimerization of semivioxanthin to vioxanthin. Finally, the monooxygenase vioO1 and the FAD-linked oxidoreductase vioO2 are responsible of several oxidations leading to the formation of viomellein and xanthomegnin. Semixanthomegnin is also produced by the cluster, however, the order of the reactions could not be determined (Probable).","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. Within the pathway, ptmC catalyzes the conversion of 13-dehydro-penitrem B into penitrem C. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3-glycerol phosphate with GGPP by ptmC then forms 3-geranylgeranylindole",No,No,No,No,No,not-Yes,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2259,no
VIOM_TRIRC,F2SL82,Protein2Text,Eukaryota,454,"Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of viomellein, a red mycelium pigment and potent antibacterial compound that may aid the progression of pathogenesis. Within the pathway, the reductase vioC and the O-methyltransferase vioM catalyze the reduction and the methylation reactions that convert nor-toralactone into semivioxanthin. The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic heptaketide nor-toralactone. The short-chain dehydrogenase/reductase vioC and the O-methyltransferase vioM then convert nor-toralactone into semivioxanthin. Semivioxanthin is probably transported across the plasma membrane by the viomellein- specific pump vioT for further enzymatic processing by the extracellular complex composed of vioL, vioF, vioO1 and vioO2 to yield final viomellein. The multicopper oxidase vioL with the help of vioF are involved in dimerization of semivioxanthin to vioxanthin. Finally, the monooxygenase vioO1 and the FAD-linked oxidoreductase vioO2 are responsible of several oxidations leading to the formation of viomellein and xanthomegnin. Semixanthomegnin is also produced by the cluster, however, the order of the reactions could not be determined (Probable).","The molecular function of this protein is not explicitly stated in the provided text. However, based on its name, it is likely that this protein is involved in the biosynthesis of a chemical compound, specifically a terpenoid, as suggested by the presence of the suffix ""-terpene synthase"" in its name. Terpenoid synthases are enzymes that catalyze the biosynthesis of terpenoids, a class of organic compounds that are found in plants and play important roles in various biological processes. If you have any more information or context about this protein, I may be able to provide a more specific answer.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0008171,,GO:0010333,,,GO:0010333,,0.1998,,,0.1998,2,0.1998,0.2259,no
VIOM_TRIRC,F2SL82,Reference,Eukaryota,454,"Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of viomellein, a red mycelium pigment and potent antibacterial compound that may aid the progression of pathogenesis. Within the pathway, the reductase vioC and the O-methyltransferase vioM catalyze the reduction and the methylation reactions that convert nor-toralactone into semivioxanthin. The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic heptaketide nor-toralactone. The short-chain dehydrogenase/reductase vioC and the O-methyltransferase vioM then convert nor-toralactone into semivioxanthin. Semivioxanthin is probably transported across the plasma membrane by the viomellein- specific pump vioT for further enzymatic processing by the extracellular complex composed of vioL, vioF, vioO1 and vioO2 to yield final viomellein. The multicopper oxidase vioL with the help of vioF are involved in dimerization of semivioxanthin to vioxanthin. Finally, the monooxygenase vioO1 and the FAD-linked oxidoreductase vioO2 are responsible of several oxidations leading to the formation of viomellein and xanthomegnin. Semixanthomegnin is also produced by the cluster, however, the order of the reactions could not be determined (Probable).","Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of viomellein, a red mycelium pigment and potent antibacterial compound that may aid the progression of pathogenesis. Within the pathway, the reductase vioC and the O-methyltransferase vioM catalyze the reduction and the methylation reactions that convert nor-toralactone into semivioxanthin. The first step is performed by the polyketide synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form the first intermediate, the cyclic heptaketide nor-toralactone. The short-chain dehydrogenase/reductase vioC and the O-methyltransferase vioM then convert nor-toralactone into semivioxanthin. Semivioxanthin is probably transported across the plasma membrane by the viomellein- specific pump vioT for further enzymatic processing by the extracellular complex composed of vioL, vioF, vioO1 and vioO2 to yield final viomellein. The multicopper oxidase vioL with the help of vioF are involved in dimerization of semivioxanthin to vioxanthin. Finally, the monooxygenase vioO1 and the FAD-linked oxidoreductase vioO2 are responsible of several oxidations leading to the formation of viomellein and xanthomegnin. Semixanthomegnin is also produced by the cluster, however, the order of the reactions could not be determined (Probable).",,,,,,,GO:0008171,GO:0016491,GO:0016491,GO:0016491,GO:0016614,GO:0016491,0.3552,0.3552,0.3552,0.2845,0.3552,5,0.3411,0.2259,no
JMJ31_ARATH,F4K2M8,ESM2Text,Eukaryota,549,May function as histone H3 lysine demethylase and be involved in regulation of gene expression.,"Kinetochore-dependent protein demethylase that specifically demethylates N-terminal transmembrane proteins, with a preference for proteins containing methionine clusters. Demethylation of N-terminal transmembrane proteins such as ANO5, CSA1, CDC42 and RHO3 requires the prior action of the CSA1, CDC42 and RHO3 chaperone to initiate mono- and dimethylation. Involved in the regulation of microtubule stability by regulating the stability of RHO3-containing microtubules.",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0016706; GO:0046872,,GO:0032451,,,,,0.2911,,,,1,0.2911,0.4748,no
JMJ31_ARATH,F4K2M8,Prot2Text,Eukaryota,549,May function as histone H3 lysine demethylase and be involved in regulation of gene expression.,Functions as an ethylene receptor.,No,No,No,No,No,not-Yes,GO:0016706; GO:0046872,GO:0038199,GO:0038199,GO:0038199,,GO:0004872,0.1285,0.1285,0.1285,,0.1586,4,0.136,0.4748,no
JMJ31_ARATH,F4K2M8,ProtT3,Eukaryota,549,May function as histone H3 lysine demethylase and be involved in regulation of gene expression.,"Zinc metalloenzyme that catalyzes the hydroxylation of L-isoaspartyl and D-aspartyl residues to form L-isoaspartyl-L- aspartate and D-aspartyl-D-aspartate, respectively. Cytoplasm Nucleus. Belongs to the IAH1 family",No,No,Vague,No,No,not-Yes,GO:0016706; GO:0046872,GO:0016787; GO:0008270,GO:0016787,GO:0016787,GO:0016491; GO:0008270,GO:0016787,0.5642,0.2911,0.2911,0.6884,0.2911,5,0.4252,0.4748,no
JMJ31_ARATH,F4K2M8,ProtTale,Eukaryota,549,May function as histone H3 lysine demethylase and be involved in regulation of gene expression.,"[Isoform 1]: Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a key role in histone code. Demethylates monomethylated 'Lys-27' H3 and dimethylated H3 'Lys-27' to produce hydroxymethylated H3. Demethylates trimethylated H3 'Lys-27'.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016706; GO:0046872,GO:0032453,GO:0032453,GO:0032452,GO:0032452,GO:0032452,0.1345,0.1345,0.166,0.166,0.166,5,0.1534,0.4748,no
JMJ31_ARATH,F4K2M8,Protein2Text,Eukaryota,549,May function as histone H3 lysine demethylase and be involved in regulation of gene expression.,The molecular function of this protein is an amino acid oxidase.,No,No,No,No,No,not-Yes,GO:0016706; GO:0046872,GO:0016641,GO:0016641,,GO:0004066,GO:0016641,0.3116,0.3116,,0.1705,0.3116,4,0.2763,0.4748,no
JMJ31_ARATH,F4K2M8,Reference,Eukaryota,549,May function as histone H3 lysine demethylase and be involved in regulation of gene expression.,May function as histone H3 lysine demethylase and be involved in regulation of gene expression.,,,,,,,GO:0016706; GO:0046872,,,,,,,,,,,0,,0.4748,no
R1PKT_HALXS,F8D4I6,ESM2Text,Archaea,296,"Kinase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the ATP-dependent phosphorylation of ribose 1-phosphate (R1P) to ribose 1,5-bisphosphate (R15P). Shows weak activity towards various other phosphate acceptors, such as xylulose, 2'-deoxyguanosine and D-ribulose. ATP is the most preferred phosphate donor, followed by CTP and GTP.","Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016301,GO:0004747; GO:0005524,GO:0004747,GO:0004747; GO:0005524,GO:0008974,GO:0004747,0.8469,0.4792,0.8469,0.5313,0.4792,5,0.6367,0.399,no
R1PKT_HALXS,F8D4I6,Prot2Text,Archaea,296,"Kinase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the ATP-dependent phosphorylation of ribose 1-phosphate (R1P) to ribose 1,5-bisphosphate (R15P). Shows weak activity towards various other phosphate acceptors, such as xylulose, 2'-deoxyguanosine and D-ribulose. ATP is the most preferred phosphate donor, followed by CTP and GTP.","Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016301,GO:0004747,GO:0004747,GO:0004747,GO:0004747,GO:0004747,0.4792,0.4792,0.4792,0.4792,0.4792,5,0.4792,0.399,no
R1PKT_HALXS,F8D4I6,ProtT3,Archaea,296,"Kinase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the ATP-dependent phosphorylation of ribose 1-phosphate (R1P) to ribose 1,5-bisphosphate (R15P). Shows weak activity towards various other phosphate acceptors, such as xylulose, 2'-deoxyguanosine and D-ribulose. ATP is the most preferred phosphate donor, followed by CTP and GTP.","Catalyzes the phosphorylation of 3-deoxy-D-manno-octulosonate (KDO) to form 3-deoxy-D-glycero-2,5-hexodiulosonate (KDG). Belongs to the carbohydrate kinase PfkB family",No,No,No,No,Maybe,not-Yes,GO:0005524; GO:0016301,GO:0016301,GO:0016301,GO:0016301; GO:0005524,GO:0019200,GO:0016301; GO:0005524,0.6878,0.6878,1.0,0.5906,1.0,5,0.7932,0.399,no
R1PKT_HALXS,F8D4I6,ProtTale,Archaea,296,"Kinase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the ATP-dependent phosphorylation of ribose 1-phosphate (R1P) to ribose 1,5-bisphosphate (R15P). Shows weak activity towards various other phosphate acceptors, such as xylulose, 2'-deoxyguanosine and D-ribulose. ATP is the most preferred phosphate donor, followed by CTP and GTP.",Catalyzes the phosphorylation of thiamine to thiamine phosphate.,No,No,No,No,No,not-Yes,GO:0005524; GO:0016301,GO:0016301,GO:0016301,GO:0016301,GO:0016301,GO:0016301,0.6878,0.6878,0.6878,0.6878,0.6878,5,0.6878,0.399,no
R1PKT_HALXS,F8D4I6,Protein2Text,Archaea,296,"Kinase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the ATP-dependent phosphorylation of ribose 1-phosphate (R1P) to ribose 1,5-bisphosphate (R15P). Shows weak activity towards various other phosphate acceptors, such as xylulose, 2'-deoxyguanosine and D-ribulose. ATP is the most preferred phosphate donor, followed by CTP and GTP.",The molecular function of this protein is a phosphotransferase enzyme. It catalyzes the transfer of a phosphate group.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0016301,GO:0016301,GO:0016301,GO:0016301,GO:0016301,GO:0016301,0.6878,0.6878,0.6878,0.6878,0.6878,5,0.6878,0.399,no
R1PKT_HALXS,F8D4I6,Reference,Archaea,296,"Kinase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the ATP-dependent phosphorylation of ribose 1-phosphate (R1P) to ribose 1,5-bisphosphate (R15P). Shows weak activity towards various other phosphate acceptors, such as xylulose, 2'-deoxyguanosine and D-ribulose. ATP is the most preferred phosphate donor, followed by CTP and GTP.","Kinase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the ATP-dependent phosphorylation of ribose 1-phosphate (R1P) to ribose 1,5-bisphosphate (R15P). Shows weak activity towards various other phosphate acceptors, such as xylulose, 2'-deoxyguanosine and D-ribulose. ATP is the most preferred phosphate donor, followed by CTP and GTP.",,,,,,,GO:0005524; GO:0016301,GO:0016301; GO:0005524,GO:0016301; GO:0005524,GO:0016301; GO:0005524,GO:0016301; GO:0005524,GO:0016301; GO:0005524,1.0,1.0,1.0,1.0,1.0,5,1.0,0.399,no
DUBC1_SIMNZ,F8L4W9,ESM2Text,Bacteria,310,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Is most active as a deSUMOylase. Also shows a lower deubiquitinase activity, being able to slowly cleave 'Lys-11'-, 'Lys-48'-, and 'Lys-63'-linked di-ubiquitin, but is inactive against other types of linkages.",Protease that catalyzes two essential functions in the NEDD8 pathway: processing of full-length NEDD8 to its mature form and deconjugation of NEDD8 from targeted proteins such as cullins or p53. These functions are dependent on the nedA endonuclease.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008234,GO:0008234,GO:0008233,GO:0008233,GO:0008234,,1.0,0.871,0.871,1.0,,4,0.9355,0.6246,yes
DUBC1_SIMNZ,F8L4W9,Prot2Text,Bacteria,310,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Is most active as a deSUMOylase. Also shows a lower deubiquitinase activity, being able to slowly cleave 'Lys-11'-, 'Lys-48'-, and 'Lys-63'-linked di-ubiquitin, but is inactive against other types of linkages.",Protease that catalyzes two essential functions in the NEDD8 pathway: processing of full-length NEDD8 to its mature form and deconjugation of NEDD8 from targeted proteins such as cullins or p53.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008234,GO:0008234,GO:0036459,GO:0008234,GO:0008234,GO:0008234,1.0,0.747,1.0,1.0,1.0,5,0.9494,0.6246,yes
DUBC1_SIMNZ,F8L4W9,ProtT3,Bacteria,310,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Is most active as a deSUMOylase. Also shows a lower deubiquitinase activity, being able to slowly cleave 'Lys-11'-, 'Lys-48'-, and 'Lys-63'-linked di-ubiquitin, but is inactive against other types of linkages.","Cysteine protease that plays an essential role in virus egress. Catalyzes two essential functions during virion morphogenesis, the processing of the p62 and p24 precursors to their mature forms and the cleavage of the capsid protein p24 from the virion membrane (By similarity). Cysteine protease that plays an essential role in virus egress. Catalyzes two essential functions during virion morphogenesis, the processing of the p62 and p24 precursors to their mature forms and the cleavage of the capsid protein p24 from the virion membrane (By similarity). SUBCELLULAR LOC",No,No,Maybe,No,No,not-Yes,GO:0008234,GO:0008234,GO:0008234,GO:0004197,GO:0008234,GO:0008234,1.0,1.0,0.8001,1.0,1.0,5,0.96,0.6246,yes
DUBC1_SIMNZ,F8L4W9,ProtTale,Bacteria,310,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Is most active as a deSUMOylase. Also shows a lower deubiquitinase activity, being able to slowly cleave 'Lys-11'-, 'Lys-48'-, and 'Lys-63'-linked di-ubiquitin, but is inactive against other types of linkages.",Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMOs to their mature forms and deconjugation of SUMO from targeted proteins.,Yes,Yes,Maybe,Yes,Yes,Yes,GO:0008234,GO:0016929; GO:0004197,GO:0016929; GO:0008234,GO:0008234,GO:0016929; GO:0008234,GO:0016929,0.8001,0.9334,1.0,0.9334,0.8001,5,0.8934,0.6246,yes
DUBC1_SIMNZ,F8L4W9,Protein2Text,Bacteria,310,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Is most active as a deSUMOylase. Also shows a lower deubiquitinase activity, being able to slowly cleave 'Lys-11'-, 'Lys-48'-, and 'Lys-63'-linked di-ubiquitin, but is inactive against other types of linkages.","This protein is a protease. Proteases are enzymes that break down proteins into smaller peptides or individual amino acids. They are involved in various cellular processes, such as protein degradation, signaling, and regulation. In the case of this protein, it is likely involved in the degradation of proteins in the cell.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008234,GO:0008233,GO:0008233,GO:0008233,GO:0008233,GO:0008233,0.871,0.871,0.871,0.871,0.871,5,0.871,0.6246,yes
DUBC1_SIMNZ,F8L4W9,Reference,Bacteria,310,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Is most active as a deSUMOylase. Also shows a lower deubiquitinase activity, being able to slowly cleave 'Lys-11'-, 'Lys-48'-, and 'Lys-63'-linked di-ubiquitin, but is inactive against other types of linkages.","Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Is most active as a deSUMOylase. Also shows a lower deubiquitinase activity, being able to slowly cleave 'Lys-11'-, 'Lys-48'-, and 'Lys-63'-linked di-ubiquitin, but is inactive against other types of linkages.",,,,,,,GO:0008234,GO:0070461; GO:0004843,GO:0016929; GO:0004843,GO:0004843; GO:0016929,GO:0016929; GO:0004843,GO:0016929; GO:0004843,0.498,0.7824,0.7824,0.7824,0.7824,5,0.7255,0.6246,yes
DUBU3_SIMNZ,F8L6R0,ESM2Text,Bacteria,743,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Shows deubiquitinase activity with ubiquitin model substrates but is hardly active against di-ubiquitin chains, meaning that this enzyme might be a substrate-directed deubiquitinase rather than a chain-cleaving enzyme.",Required for regulating membrane trafficking and exocytosis during autophagy.,No,No,No,No,No,not-Yes,GO:0004843,,,,,,,,,,,0,,0.7345,yes
DUBU3_SIMNZ,F8L6R0,Prot2Text,Bacteria,743,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Shows deubiquitinase activity with ubiquitin model substrates but is hardly active against di-ubiquitin chains, meaning that this enzyme might be a substrate-directed deubiquitinase rather than a chain-cleaving enzyme.",Involved in regulating alpha-tubulin dynamics and microtubule organization.,No,No,No,No,No,not-Yes,GO:0004843,,,,,,,,,,,0,,0.7345,yes
DUBU3_SIMNZ,F8L6R0,ProtT3,Bacteria,743,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Shows deubiquitinase activity with ubiquitin model substrates but is hardly active against di-ubiquitin chains, meaning that this enzyme might be a substrate-directed deubiquitinase rather than a chain-cleaving enzyme.",Belongs to the peptidase C19 family,Vague,Vague,Maybe,Vague,Vague,not-Yes,GO:0004843,GO:0004843,GO:0004843,,GO:0004843,GO:0004843,1.0,1.0,,1.0,1.0,4,1.0,0.7345,yes
DUBU3_SIMNZ,F8L6R0,ProtTale,Bacteria,743,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Shows deubiquitinase activity with ubiquitin model substrates but is hardly active against di-ubiquitin chains, meaning that this enzyme might be a substrate-directed deubiquitinase rather than a chain-cleaving enzyme.",E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.,No,No,No,No,No,not-Yes,GO:0004843,GO:0061630,GO:0061630; GO:0004842,GO:0061630,GO:0061630,GO:0061630,0.2196,0.2506,0.2196,0.2196,0.2196,5,0.2258,0.7345,yes
DUBU3_SIMNZ,F8L6R0,Protein2Text,Bacteria,743,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Shows deubiquitinase activity with ubiquitin model substrates but is hardly active against di-ubiquitin chains, meaning that this enzyme might be a substrate-directed deubiquitinase rather than a chain-cleaving enzyme.",The molecular function of this protein is an E3 ubiquitin-protein ligase.,No,No,No,No,No,not-Yes,GO:0004843,GO:0061630,GO:0061630,GO:0061630,GO:0061630,GO:0061630,0.2196,0.2196,0.2196,0.2196,0.2196,5,0.2196,0.7345,yes
DUBU3_SIMNZ,F8L6R0,Reference,Bacteria,743,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Shows deubiquitinase activity with ubiquitin model substrates but is hardly active against di-ubiquitin chains, meaning that this enzyme might be a substrate-directed deubiquitinase rather than a chain-cleaving enzyme.","Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Shows deubiquitinase activity with ubiquitin model substrates but is hardly active against di-ubiquitin chains, meaning that this enzyme might be a substrate-directed deubiquitinase rather than a chain-cleaving enzyme.",,,,,,,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,1.0,1.0,1.0,1.0,1.0,5,1.0,0.7345,yes
DUBU1_SIMNZ,F8L8G5,ESM2Text,Bacteria,1223,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Shows deubiquitinase activity, able to cleave di-ubiquitin of different linkage types.","Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium. Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1).",No,No,No,No,No,not-Yes,GO:0004843; GO:0038023,,,,,,,,,,,0,,0.6436,yes
DUBU1_SIMNZ,F8L8G5,Prot2Text,Bacteria,1223,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Shows deubiquitinase activity, able to cleave di-ubiquitin of different linkage types.",Deubiquitinating enzyme that acts as an important regulatory factor by promoting the ubiquitination of proteins at the level of the ubiquitin-conjugating enzyme UBE2D1.,Yes,Maybe,Maybe,Yes,Yes,Yes,GO:0004843; GO:0038023,,GO:0004843,GO:0004843,GO:0004843,GO:0004843,,0.7066,0.7066,0.7066,0.7066,4,0.7066,0.6436,yes
DUBU1_SIMNZ,F8L8G5,ProtT3,Bacteria,1223,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Shows deubiquitinase activity, able to cleave di-ubiquitin of different linkage types.",Belongs to the peptidase C2 family,Vague,Vague,Maybe,Vague,Vague,not-Yes,GO:0004843; GO:0038023,GO:0008234,GO:0004198,,GO:0004198,GO:0004198,0.5523,0.4014,,0.4014,0.4014,4,0.4391,0.6436,yes
DUBU1_SIMNZ,F8L8G5,ProtTale,Bacteria,1223,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Shows deubiquitinase activity, able to cleave di-ubiquitin of different linkage types.",May play a role in vacuolar protein sorting.,No,No,No,No,No,not-Yes,GO:0004843; GO:0038023,,,,,,,,,,,0,,0.6436,yes
DUBU1_SIMNZ,F8L8G5,Protein2Text,Bacteria,1223,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Shows deubiquitinase activity, able to cleave di-ubiquitin of different linkage types.","This protein is a protease, which means it has the ability to break down proteins into smaller peptides or amino acids.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004843; GO:0038023,GO:0008233,GO:0008233,GO:0008233,GO:0008233,GO:0008233,0.4987,0.4987,0.4987,0.4987,0.4987,5,0.4987,0.6436,yes
DUBU1_SIMNZ,F8L8G5,Reference,Bacteria,1223,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Shows deubiquitinase activity, able to cleave di-ubiquitin of different linkage types.","Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Shows deubiquitinase activity, able to cleave di-ubiquitin of different linkage types.",,,,,,,GO:0004843; GO:0038023,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,0.7066,0.7066,0.7066,0.7066,0.7066,5,0.7066,0.6436,yes
DUBU2_SIMNZ,F8L8I6,ESM2Text,Bacteria,401,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Shows deubiquitinase activity, able to cleave di-ubiquitin of different linkage types. In vitro, also reacts with an ISG15-derived activity- based probe.",Deubiquitinating enzyme involved in the cleavage of polyubiquitin chains that prevent isoform A and/or isoform B from ubiquitination.,Yes,Maybe,Maybe,Yes,Yes,Yes,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,1.0,1.0,1.0,1.0,1.0,5,1.0,0.722,yes
DUBU2_SIMNZ,F8L8I6,Prot2Text,Bacteria,401,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Shows deubiquitinase activity, able to cleave di-ubiquitin of different linkage types. In vitro, also reacts with an ISG15-derived activity- based probe.",Hydrolase that deubiquitinates target proteins.,Yes,Yes,Maybe,Yes,Yes,Yes,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,1.0,1.0,1.0,1.0,1.0,5,1.0,0.722,yes
DUBU2_SIMNZ,F8L8I6,ProtT3,Bacteria,401,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Shows deubiquitinase activity, able to cleave di-ubiquitin of different linkage types. In vitro, also reacts with an ISG15-derived activity- based probe.",Ubiquitin thioesterase involved in the processing of ubiquitin precursors as well as that of ubiquitinated proteins. Cytoplasm Nucleus. Belongs to the peptidase C19 family,Yes,Maybe,Yes,Yes,Yes,Yes,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,1.0,1.0,1.0,1.0,1.0,5,1.0,0.722,yes
DUBU2_SIMNZ,F8L8I6,ProtTale,Bacteria,401,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Shows deubiquitinase activity, able to cleave di-ubiquitin of different linkage types. In vitro, also reacts with an ISG15-derived activity- based probe.",May play a role in vacuolar protein sorting.,Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0004843,,,,,,,,,,,0,,0.722,yes
DUBU2_SIMNZ,F8L8I6,Protein2Text,Bacteria,401,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Shows deubiquitinase activity, able to cleave di-ubiquitin of different linkage types. In vitro, also reacts with an ISG15-derived activity- based probe.","The molecular function of this protein is protease activity. It is involved in the degradation of proteins, specifically the cleavage of proteins at specific peptide bonds. In the case of this protein, it is likely involved in the removal of ubiquitin from target proteins, as it is a deubiquitinase. Deubiquitinases are enzymes that remove ubiquitin from proteins, which can play a role in various cellular processes such as protein degradation, cell signaling, and DNA repair.",Vague,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0004843,GO:0008233,GO:0004843,GO:0004843,GO:0004843,GO:0004843,0.6551,1.0,1.0,1.0,1.0,5,0.931,0.722,yes
DUBU2_SIMNZ,F8L8I6,Reference,Bacteria,401,"Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Shows deubiquitinase activity, able to cleave di-ubiquitin of different linkage types. In vitro, also reacts with an ISG15-derived activity- based probe.","Effector protein secreted into the host cytoplasm that counteracts ubiquitin-based antibacterial defenses. Shows deubiquitinase activity, able to cleave di-ubiquitin of different linkage types. In vitro, also reacts with an ISG15-derived activity- based probe.",,,,,,,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,GO:0004843,1.0,1.0,1.0,1.0,1.0,5,1.0,0.722,yes
AA12_HYPJQ,G0RPY6,ESM2Text,Eukaryota,430,Pyrroloquinoline quinone (PPQ)-dependent oxidoreductase that catalyzes the oxidation of various sugars such as L-fucose.,"Converts alpha-amylol and geraniol into p-hydroxynaphthalene and alpha-chloroglucene, respectively, in the breakdown of dimethyl sulfide (DMS) generated by the action of DMSO. Can hydrolyze geraniol, farnesol, methyl farnesol, lactonol and benzyl alcohol in vitro.",No,No,No,No,No,not-Yes,GO:0046872; GO:0016491,,GO:0016787,,,,,0.4461,,,,1,0.4461,0.3482,no
AA12_HYPJQ,G0RPY6,Prot2Text,Eukaryota,430,Pyrroloquinoline quinone (PPQ)-dependent oxidoreductase that catalyzes the oxidation of various sugars such as L-fucose.,"Part of the gene cluster that mediates the biosynthesis of pestheic acid, a diphenyl ether which is a biosynthetic precursor of the unique chloropupukeananes. The biosynthesis initiates from condensation of acetate and malonate units catalyzed by the non-reducing PKS ptaA. As the ptaA protein is TE/CLC domain-deficient, hydrolysis and Claisen cyclization of the polyketide could be catalyzed by ptaB containing a beta-lactamase domain. The ptaB protein might hydrolyze the thioester bond between the ACP of ptaA and the intermediate to release atrochrysone carboxylic acid, which is spontaneously dehydrated to form endocrocin anthrone. Endocrocin anthrone is then converted to endocrocin, catalyzed by the anthrone oxygenase ptaC. Spontaneous decarboxylation of endocrocin occurs to generate emodin. An O-methyltransferase (ptaH or ptaI) could methylate emodin to form physcion. PtaJ could then catalyze the oxidative cleavage of the tyrosine",No,No,No,No,No,not-Yes,GO:0046872; GO:0016491,,,GO:0016787,GO:0016790,,,,0.4461,0.3062,,2,0.3761,0.3482,no
AA12_HYPJQ,G0RPY6,ProtT3,Eukaryota,430,Pyrroloquinoline quinone (PPQ)-dependent oxidoreductase that catalyzes the oxidation of various sugars such as L-fucose.,Involved in the degradation of D-glucuronic acid. Periplasm. Belongs to the D-glucuronic acid oxidase family,Maybe,Maybe,Vague,No,Maybe,not-Yes,GO:0046872; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016614,GO:0016614,0.7193,0.7193,0.7193,0.5852,0.5852,5,0.6657,0.3482,no
AA12_HYPJQ,G0RPY6,ProtTale,Eukaryota,430,Pyrroloquinoline quinone (PPQ)-dependent oxidoreductase that catalyzes the oxidation of various sugars such as L-fucose.,"Dehydratase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS). SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms. These initial steps feature the priming of an unusual benzoic acid starter unit onto the highly",No,No,No,No,No,not-Yes,GO:0046872; GO:0016491,GO:0016836,GO:0016836,GO:0016836,GO:0016836,GO:0016836,0.3062,0.3062,0.3062,0.3062,0.3062,5,0.3062,0.3482,no
AA12_HYPJQ,G0RPY6,Protein2Text,Eukaryota,430,Pyrroloquinoline quinone (PPQ)-dependent oxidoreductase that catalyzes the oxidation of various sugars such as L-fucose.,"The molecular function of this protein is unknown. However, based on its name, it is likely to be a glycoprotein, which is a type of protein that contains carbohydrate molecules attached to it. Glycoproteins often play important roles in cellular processes, such as cell signaling, cell adhesion, and protein transport. However, without more specific information, it is difficult to determine the exact molecular function of this protein.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0046872; GO:0016491,,,,,,,,,,,0,,0.3482,no
AA12_HYPJQ,G0RPY6,Reference,Eukaryota,430,Pyrroloquinoline quinone (PPQ)-dependent oxidoreductase that catalyzes the oxidation of various sugars such as L-fucose.,Pyrroloquinoline quinone (PPQ)-dependent oxidoreductase that catalyzes the oxidation of various sugars such as L-fucose.,,,,,,,GO:0046872; GO:0016491,GO:0016614,GO:0016491,GO:0016491,GO:0016614,GO:0016614,0.5852,0.7193,0.7193,0.5852,0.5852,5,0.6388,0.3482,no
BVMO_THET4,G2QA95,ESM2Text,Eukaryota,655,"Polycyclic ketone monooxygenase (PockeMO) that displays excellent enantioselectivity, acts on various ketones, and is particularly active on polycyclic molecules. Breaks C-C bonds through the insertion of a single oxygen atom adjacent to a carbonyl moiety, yielding esters or lactones from ketones. PockeMO is able to convert linear ketones (including cyclohexane and to a lesser extend 4-octanone), cyclic ketones (including cyclohexanone and cyclooctanone), bicyclic ketones and polycyclic ketones (steroids). Performs oxidation of the keto functionalities at both the A and D rings of steroids. Particularly, oxidizes the A ring of stanolone or pregnenolone. Selectively oxidizes the D ring of androstenedione or androstadienedione, steroids with keto groups in both the A and D rings, to yield the pharmaceutically relevant testo(lo)lactone.","FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids nectripenoids A and B, as well as cochliquninone D and isocochliquninone E. The pathway probably begins with the HR-PKS ntnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS ntnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of nectripenoids (Probable). The FAD-dependent monooxygenase ntnJ then performs an oxidative decarboxylation at C11 of the ntnH/ntnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation (Probable). The membrane-bound polyprenyl transferase ntnF then introduces a farnesyl group before the FAD-dependent monooxygenase ntnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C",Maybe,Maybe,Yes,Yes,Maybe,not-Yes,GO:0000166; GO:0016491,GO:0004497; GO:0071949,GO:0004497,GO:0004497; GO:0071949,GO:0004497,GO:0004497; GO:0071949,0.7619,0.5895,0.7619,0.5895,0.7619,5,0.6929,0.3057,no
BVMO_THET4,G2QA95,Prot2Text,Eukaryota,655,"Polycyclic ketone monooxygenase (PockeMO) that displays excellent enantioselectivity, acts on various ketones, and is particularly active on polycyclic molecules. Breaks C-C bonds through the insertion of a single oxygen atom adjacent to a carbonyl moiety, yielding esters or lactones from ketones. PockeMO is able to convert linear ketones (including cyclohexane and to a lesser extend 4-octanone), cyclic ketones (including cyclohexanone and cyclooctanone), bicyclic ketones and polycyclic ketones (steroids). Performs oxidation of the keto functionalities at both the A and D rings of steroids. Particularly, oxidizes the A ring of stanolone or pregnenolone. Selectively oxidizes the D ring of androstenedione or androstadienedione, steroids with keto groups in both the A and D rings, to yield the pharmaceutically relevant testo(lo)lactone.","FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Maybe,Yes,Yes,Maybe,not-Yes,GO:0000166; GO:0016491,GO:0004497,GO:0004497; GO:0071949,GO:0004497,GO:0004497,GO:0004497,0.5895,0.7619,0.5895,0.5895,0.5895,5,0.624,0.3057,no
BVMO_THET4,G2QA95,ProtT3,Eukaryota,655,"Polycyclic ketone monooxygenase (PockeMO) that displays excellent enantioselectivity, acts on various ketones, and is particularly active on polycyclic molecules. Breaks C-C bonds through the insertion of a single oxygen atom adjacent to a carbonyl moiety, yielding esters or lactones from ketones. PockeMO is able to convert linear ketones (including cyclohexane and to a lesser extend 4-octanone), cyclic ketones (including cyclohexanone and cyclooctanone), bicyclic ketones and polycyclic ketones (steroids). Performs oxidation of the keto functionalities at both the A and D rings of steroids. Particularly, oxidizes the A ring of stanolone or pregnenolone. Selectively oxidizes the D ring of androstenedione or androstadienedione, steroids with keto groups in both the A and D rings, to yield the pharmaceutically relevant testo(lo)lactone.",FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeranylindole (3-,Maybe,Maybe,Yes,Yes,Maybe,not-Yes,GO:0000166; GO:0016491,GO:0004497; GO:0050660,GO:0004497; GO:0071949,GO:0004497,GO:0004497; GO:0071949,GO:0004497; GO:0071949,0.7893,0.7619,0.5895,0.7619,0.7619,5,0.7329,0.3057,no
BVMO_THET4,G2QA95,ProtTale,Eukaryota,655,"Polycyclic ketone monooxygenase (PockeMO) that displays excellent enantioselectivity, acts on various ketones, and is particularly active on polycyclic molecules. Breaks C-C bonds through the insertion of a single oxygen atom adjacent to a carbonyl moiety, yielding esters or lactones from ketones. PockeMO is able to convert linear ketones (including cyclohexane and to a lesser extend 4-octanone), cyclic ketones (including cyclohexanone and cyclooctanone), bicyclic ketones and polycyclic ketones (steroids). Performs oxidation of the keto functionalities at both the A and D rings of steroids. Particularly, oxidizes the A ring of stanolone or pregnenolone. Selectively oxidizes the D ring of androstenedione or androstadienedione, steroids with keto groups in both the A and D rings, to yield the pharmaceutically relevant testo(lo)lactone.","Catalyzes an oxidative deamination reaction, the oxidation of an L-amino acid, in which L-alanine is converted to 2-oxobutanoate. Plays a role in the degradation of L-amino acids.",Maybe,Maybe,Yes,Yes,Maybe,not-Yes,GO:0000166; GO:0016491,GO:0004060,GO:0016638,GO:0016641,GO:0016641,GO:0016641,0.2022,0.5895,0.4994,0.4994,0.4994,5,0.458,0.3057,no
BVMO_THET4,G2QA95,Protein2Text,Eukaryota,655,"Polycyclic ketone monooxygenase (PockeMO) that displays excellent enantioselectivity, acts on various ketones, and is particularly active on polycyclic molecules. Breaks C-C bonds through the insertion of a single oxygen atom adjacent to a carbonyl moiety, yielding esters or lactones from ketones. PockeMO is able to convert linear ketones (including cyclohexane and to a lesser extend 4-octanone), cyclic ketones (including cyclohexanone and cyclooctanone), bicyclic ketones and polycyclic ketones (steroids). Performs oxidation of the keto functionalities at both the A and D rings of steroids. Particularly, oxidizes the A ring of stanolone or pregnenolone. Selectively oxidizes the D ring of androstenedione or androstadienedione, steroids with keto groups in both the A and D rings, to yield the pharmaceutically relevant testo(lo)lactone.","The molecular function of this protein is an oxidoreductase, specifically a cytochrome P450 monooxygenase. It is involved in the oxidation of organic compounds.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0000166; GO:0016491,GO:0004497,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0020037,GO:0004497,GO:0004497,0.5895,0.5119,0.5641,0.5895,0.5895,5,0.5689,0.3057,no
BVMO_THET4,G2QA95,Reference,Eukaryota,655,"Polycyclic ketone monooxygenase (PockeMO) that displays excellent enantioselectivity, acts on various ketones, and is particularly active on polycyclic molecules. Breaks C-C bonds through the insertion of a single oxygen atom adjacent to a carbonyl moiety, yielding esters or lactones from ketones. PockeMO is able to convert linear ketones (including cyclohexane and to a lesser extend 4-octanone), cyclic ketones (including cyclohexanone and cyclooctanone), bicyclic ketones and polycyclic ketones (steroids). Performs oxidation of the keto functionalities at both the A and D rings of steroids. Particularly, oxidizes the A ring of stanolone or pregnenolone. Selectively oxidizes the D ring of androstenedione or androstadienedione, steroids with keto groups in both the A and D rings, to yield the pharmaceutically relevant testo(lo)lactone.","Polycyclic ketone monooxygenase (PockeMO) that displays excellent enantioselectivity, acts on various ketones, and is particularly active on polycyclic molecules. Breaks C-C bonds through the insertion of a single oxygen atom adjacent to a carbonyl moiety, yielding esters or lactones from ketones. PockeMO is able to convert linear ketones (including cyclohexane and to a lesser extend 4-octanone), cyclic ketones (including cyclohexanone and cyclooctanone), bicyclic ketones and polycyclic ketones (steroids). Performs oxidation of the keto functionalities at both the A and D rings of steroids. Particularly, oxidizes the A ring of stanolone or pregnenolone. Selectively oxidizes the D ring of androstenedione or androstadienedione, steroids with keto groups in both the A and D rings, to yield the pharmaceutically relevant testo(lo)lactone.",,,,,,,GO:0000166; GO:0016491,GO:0016709,GO:0004497,GO:0004497,GO:0016709,GO:0004497,0.44,0.5895,0.5895,0.44,0.5895,5,0.5297,0.3057,no
LP9U_THETT,G2RB72,ESM2Text,Eukaryota,257,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate. Shows no activity on wheat arabinoxylan, konjac glucomannan, acetylated spruce galactoglucomannan, or cellopentaose.","Recombinant enzyme consists of a polymerase with a single-stranded DNA-binding activity. It polymerizes to produce single-stranded polymers in the presence of phospholipase A2, phospholipase A3, and phospholipase A4. Active on substrates with a degree of polymerization (DP) value from 2 to 60. Does not display endoxylanase activity.",No,No,No,No,No,not-Yes,GO:0046872; GO:0004497,GO:0003677,GO:0003697,,,,0.2475,0.2055,,,,2,0.2265,0.3054,no
LP9U_THETT,G2RB72,Prot2Text,Eukaryota,257,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate. Shows no activity on wheat arabinoxylan, konjac glucomannan, acetylated spruce galactoglucomannan, or cellopentaose.","Has low levels of endoglucanase activity. May be involved in the degradation of cellulose or lignocellulose, chitin, or other polysaccharides.",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0046872; GO:0004497,GO:0008810,GO:0008810,GO:0008810,GO:0008810,GO:0008810,0.2193,0.2193,0.2193,0.2193,0.2193,5,0.2193,0.3054,no
LP9U_THETT,G2RB72,ProtT3,Eukaryota,257,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate. Shows no activity on wheat arabinoxylan, konjac glucomannan, acetylated spruce galactoglucomannan, or cellopentaose.",Secreted. Belongs to the multicopper oxidase family,Vague,Vague,Vague,Vague,No,not-Yes,GO:0046872; GO:0004497,GO:0016491; GO:0005507,GO:0016491; GO:0005507,GO:0016491,GO:0016491; GO:0005507,GO:0016491; GO:0005507,0.7926,0.7926,0.5957,0.7926,0.7926,5,0.7532,0.3054,no
LP9U_THETT,G2RB72,ProtTale,Eukaryota,257,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate. Shows no activity on wheat arabinoxylan, konjac glucomannan, acetylated spruce galactoglucomannan, or cellopentaose.","Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 or C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0004497,GO:0016491; GO:0005507,GO:0016491; GO:0005507,GO:0004497,GO:0004497; GO:0005507,GO:0016491; GO:0005507,0.7926,0.7926,0.7088,0.8854,0.7926,5,0.7944,0.3054,no
LP9U_THETT,G2RB72,Protein2Text,Eukaryota,257,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate. Shows no activity on wheat arabinoxylan, konjac glucomannan, acetylated spruce galactoglucomannan, or cellopentaose.","The molecular function of this protein is associated with the breakdown of lignin, a complex organic polymer found in plant cell walls. More specifically, it is involved in the oxidative cleavage of lignin, which is a key step in the degradation of lignin by fungi. This process is crucial for the recycling of carbon and nutrients in ecosystems. The protein is likely involved in the oxidation of specific bonds in lignin, leading to its breakdown and the release of various aromatic compounds. 

In general, the molecular function of this protein is likely related to its role as a lignin-degrading enzyme, specifically a peroxidase, which is a type of enzyme that uses hydrogen peroxide to catalyze the oxidation of various substrates. 

Please note that this is an educated guess based on the information provided, and the actual molecular function of this protein may be different. If you have more specific information about the protein, such as its name or sequence, I may be able to provide a more accurate answer.",No,No,Maybe,No,No,not-Yes,GO:0046872; GO:0004497,GO:0004601,GO:0004601,GO:0004601,GO:0004601,GO:0004601,0.3798,0.3798,0.3798,0.3798,0.3798,5,0.3798,0.3054,no
LP9U_THETT,G2RB72,Reference,Eukaryota,257,"Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate. Shows no activity on wheat arabinoxylan, konjac glucomannan, acetylated spruce galactoglucomannan, or cellopentaose.","Lytic polysaccharide monooxygenase (LPMO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 and C4 oxidation products. Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate. Shows no activity on wheat arabinoxylan, konjac glucomannan, acetylated spruce galactoglucomannan, or cellopentaose.",,,,,,,GO:0046872; GO:0004497,GO:0016491,GO:0016491; GO:0005507,GO:0004497; GO:0005507,GO:0016491,GO:0016491,0.5957,0.7926,0.8854,0.5957,0.5957,5,0.693,0.3054,no
EIX5_VERDV,G2X4G1,ESM2Text,Eukaryota,224,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. May act as an elicitor of plant defense responses in certain plants but does not exhibit any cell death when transiently expressed in N.benthamiana.","Glycoside hydrolase-like protein that exhibits endo- and exo-accelerating activities. Plays a role in causing disease on crops. Induces cell death and bacterial infection in models of infection with S.cerevisiae, S.pombe, and M.nematophilum.",Maybe,No,No,Maybe,Maybe,not-Yes,GO:0031176,GO:0004553,GO:0004553,,GO:0016798,,0.7539,0.7539,,0.6466,,3,0.7181,0.3003,no
EIX5_VERDV,G2X4G1,Prot2Text,Eukaryota,224,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. May act as an elicitor of plant defense responses in certain plants but does not exhibit any cell death when transiently expressed in N.benthamiana.",Secreted effector that contributes strongly to virulence during infection by P.capsici. Causes large necrotic areas in both host C.annuum and non-host N.benthamiana.,No,No,No,No,No,not-Yes,GO:0031176,,,,,,,,,,,0,,0.3003,no
EIX5_VERDV,G2X4G1,ProtT3,Eukaryota,224,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. May act as an elicitor of plant defense responses in certain plants but does not exhibit any cell death when transiently expressed in N.benthamiana.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Secreted. Belongs to the glycosyl hydrolase 11 (cellulase G) family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3003,no
EIX5_VERDV,G2X4G1,ProtTale,Eukaryota,224,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. May act as an elicitor of plant defense responses in certain plants but does not exhibit any cell death when transiently expressed in N.benthamiana.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3003,no
EIX5_VERDV,G2X4G1,Protein2Text,Eukaryota,224,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. May act as an elicitor of plant defense responses in certain plants but does not exhibit any cell death when transiently expressed in N.benthamiana.","The molecular function of this protein is not explicitly stated in the provided information, but based on its classification as a glycosidase, it is likely that its molecular function is to break down complex carbohydrates into simpler sugars. Specifically, this protein is involved in the degradation of cellulose, a complex carbohydrate found in plant cell walls. It is likely that this protein catalyzes the hydrolysis of cellulose into simpler sugars, such as glucose. 

In more detail, the molecular function of this protein is probably to catalyze the hydrolysis of 1,4-beta-glucosidic linkages in cellulose, resulting in the production of glucose and cellobiose. This is a critical step in the degradation of cellulose, a complex carbohydrate found in plant cell walls, and is an important component of the cellulolytic system. 

It's worth noting that the molecular function of this protein may be influenced by its interaction with other proteins, such as CBH1 and CBH2, which are also involved in the degradation of cellulose. The specific molecular function of this protein may depend on its interaction with these other proteins, and may be influenced by the presence of other enzymes that are involved in the degradation of cellulose.",Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0031176,GO:0008422,GO:0008810,GO:0008810,GO:0008810,GO:0008422,0.5445,0.6335,0.6335,0.6335,0.5445,5,0.5979,0.3003,no
EIX5_VERDV,G2X4G1,Reference,Eukaryota,224,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. May act as an elicitor of plant defense responses in certain plants but does not exhibit any cell death when transiently expressed in N.benthamiana.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. May act as an elicitor of plant defense responses in certain plants but does not exhibit any cell death when transiently expressed in N.benthamiana.",,,,,,,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3003,no
TAS1_CORMM,G3J9P0,ESM2Text,Eukaryota,1582,"Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal NRPS module and subsequent cyclization conducted by the C-terminal KS domain.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the host-selective toxins (HSTs) AAL-toxins, sphinganine-analog mycotoxins responsible for Alternaria stem canker on tomato by the tomato pathotype. The biosynthesis starts with the polyketide synthase ALT1-catalyzed C-16 carbon chain assembly from one starter acetyl-CoA unit with malonyl-CoA extender units. ALT1 also selectively transfers methyl groups at the first and the third cycle of chain elongation for AAL toxin. The C-16 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of glycin by decarboxylation, on the carbonyl carbon of polyketide acyl chain (Probable). This step is probably catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase ALT4 (Probable). The respective functions of the other enzymes encoded by the cluster have still to be elucidated (Probable). The sphingosine N-acyltransfer",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0016874; GO:0031177,GO:0016874,GO:0016874,,,,0.6206,0.6206,,,,2,0.6206,0.1868,no
TAS1_CORMM,G3J9P0,Prot2Text,Eukaryota,1582,"Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal NRPS module and subsequent cyclization conducted by the C-terminal KS domain.","Catalyzes the formation of phenylacetic acid (PA), a universal precursor of the phenylpropanoidines that are responsible for the coloration of the fruiting bodies. The accumulation of phenylacetic acid over a wide range of aldehydes has a role in the biosynthesis of fruiting bodies.",No,No,No,No,No,not-Yes,GO:0004315; GO:0016874; GO:0031177,,,,,,,,,,,0,,0.1868,no
TAS1_CORMM,G3J9P0,ProtT3,Eukaryota,1582,"Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal NRPS module and subsequent cyclization conducted by the C-terminal KS domain.","Nonribosomal peptide synthetase (NRPS); part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0016874; GO:0031177,GO:0016874; GO:0005524,GO:0016874,GO:0016874,GO:0016874; GO:0005524,GO:0016874,0.6145,0.6206,0.6206,0.6145,0.6206,5,0.6182,0.1868,no
TAS1_CORMM,G3J9P0,ProtTale,Eukaryota,1582,"Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal NRPS module and subsequent cyclization conducted by the C-terminal KS domain.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0016874; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.5114,0.5114,0.5114,0.5114,0.5114,5,0.5114,0.1868,no
TAS1_CORMM,G3J9P0,Protein2Text,Eukaryota,1582,"Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal NRPS module and subsequent cyclization conducted by the C-terminal KS domain.","This protein is involved in the molecular function of catalyzing the condensation of isopentenyl diphosphate (IPP) with dimethylallyl diphosphate (DMAPP) to produce geranyl diphosphate (GPP), a key step in the mevalonate (MVA) pathway.",No,No,No,No,No,not-Yes,GO:0004315; GO:0016874; GO:0031177,GO:0004161,GO:0004161,GO:0004337,GO:0004161,GO:0004161,0.2507,0.2507,0.2507,0.2507,0.2507,5,0.2507,0.1868,no
TAS1_CORMM,G3J9P0,Reference,Eukaryota,1582,"Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal NRPS module and subsequent cyclization conducted by the C-terminal KS domain.","Hybrid PKS-NRPS synthetase that mediates the biosynthesis of the toxin tenuazonic acid (TeA), an inhibitor of protein biosynthesis on ribosomes by suppressing the release of new protein. TAS1 alone is sufficient for TeA synthesis via the condensation of isoleucine (Ile) with acetoacetyl-CoA by the N-terminal NRPS module and subsequent cyclization conducted by the C-terminal KS domain.",,,,,,,GO:0004315; GO:0016874; GO:0031177,GO:0016874,GO:0016874,GO:0016746,GO:0016874,GO:0016746,0.6206,0.6206,0.5114,0.6206,0.5114,5,0.5769,0.1868,no
CNS3_CORMM,G3JF10,ESM2Text,Eukaryota,871,"Nucleoside/nucleotide kinase; part of the gene cluster that mediates the biosynthesis of cordycepin (COR) and pentostatin (PTN), two adenosine analogs with related bioactivity profiles as both mimic adenosine and can inhibit some of the processes that are adenosine dependent. Within the pathway, cns3 catalyzes both the first step of cordycepin biosynthesis by phosphorylating adenosine into 3'-AMP via its kinase activity and the conversion of adenosine into pentostatin via its ATP phosphoribosyltransferase activity. The first step of cordycepin biosynthesis involves hydroxyl phosphorylation of the 3'-OH position on adenosine to produce adenosine-3'-monophosphate (3'-AMP), catalyzed by kinase activity of cns3. Next, 3'-AMP is dephosphorylated to 2'-carbonyl-3'-deoxyadenosine (2'-C-3'-dA) by cns2, which is finally converted to cordycepin (3'-deoxyadenosine) by the oxidoreductase cns1.","Catalyzes the epsilon-amino group transfer of a highly sulfated glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016301; GO:0016874,GO:0004576,GO:0004579,GO:0004579,GO:0004579,GO:0004579,0.302,0.2669,0.2669,0.2669,0.2669,5,0.2739,0.1883,no
CNS3_CORMM,G3JF10,Prot2Text,Eukaryota,871,"Nucleoside/nucleotide kinase; part of the gene cluster that mediates the biosynthesis of cordycepin (COR) and pentostatin (PTN), two adenosine analogs with related bioactivity profiles as both mimic adenosine and can inhibit some of the processes that are adenosine dependent. Within the pathway, cns3 catalyzes both the first step of cordycepin biosynthesis by phosphorylating adenosine into 3'-AMP via its kinase activity and the conversion of adenosine into pentostatin via its ATP phosphoribosyltransferase activity. The first step of cordycepin biosynthesis involves hydroxyl phosphorylation of the 3'-OH position on adenosine to produce adenosine-3'-monophosphate (3'-AMP), catalyzed by kinase activity of cns3. Next, 3'-AMP is dephosphorylated to 2'-carbonyl-3'-deoxyadenosine (2'-C-3'-dA) by cns2, which is finally converted to cordycepin (3'-deoxyadenosine) by the oxidoreductase cns1.",IMP-specific 5'-nucleotidase involved in IMP (inositol monophosphate) degradation.,No,Maybe,No,No,No,not-Yes,GO:0005524; GO:0016301; GO:0016874,GO:0008253,GO:0008441,GO:0008253,GO:0008253,GO:0008253,0.2024,0.2024,0.2024,0.2024,0.2024,5,0.2024,0.1883,no
CNS3_CORMM,G3JF10,ProtT3,Eukaryota,871,"Nucleoside/nucleotide kinase; part of the gene cluster that mediates the biosynthesis of cordycepin (COR) and pentostatin (PTN), two adenosine analogs with related bioactivity profiles as both mimic adenosine and can inhibit some of the processes that are adenosine dependent. Within the pathway, cns3 catalyzes both the first step of cordycepin biosynthesis by phosphorylating adenosine into 3'-AMP via its kinase activity and the conversion of adenosine into pentostatin via its ATP phosphoribosyltransferase activity. The first step of cordycepin biosynthesis involves hydroxyl phosphorylation of the 3'-OH position on adenosine to produce adenosine-3'-monophosphate (3'-AMP), catalyzed by kinase activity of cns3. Next, 3'-AMP is dephosphorylated to 2'-carbonyl-3'-deoxyadenosine (2'-C-3'-dA) by cns2, which is finally converted to cordycepin (3'-deoxyadenosine) by the oxidoreductase cns1.",Part of the gene cluster that mediates the biosynthesis of the host-selective toxins (HSTs) AAL-toxins responsible for Alternaria black spot of tomato disease by the tomato pathotype,No,Vague,Vague,No,Vague,not-Yes,GO:0005524; GO:0016301; GO:0016874,,,,,,,,,,,0,,0.1883,no
CNS3_CORMM,G3JF10,ProtTale,Eukaryota,871,"Nucleoside/nucleotide kinase; part of the gene cluster that mediates the biosynthesis of cordycepin (COR) and pentostatin (PTN), two adenosine analogs with related bioactivity profiles as both mimic adenosine and can inhibit some of the processes that are adenosine dependent. Within the pathway, cns3 catalyzes both the first step of cordycepin biosynthesis by phosphorylating adenosine into 3'-AMP via its kinase activity and the conversion of adenosine into pentostatin via its ATP phosphoribosyltransferase activity. The first step of cordycepin biosynthesis involves hydroxyl phosphorylation of the 3'-OH position on adenosine to produce adenosine-3'-monophosphate (3'-AMP), catalyzed by kinase activity of cns3. Next, 3'-AMP is dephosphorylated to 2'-carbonyl-3'-deoxyadenosine (2'-C-3'-dA) by cns2, which is finally converted to cordycepin (3'-deoxyadenosine) by the oxidoreductase cns1.","Allows the bacterium to grow in the absence of carbon monoxide (CO) dehydrogenase (CODH). CO dehydrogenase is an essential component of the CO dehydrogenase complex, which catalyzes the initial reaction in the CO dehydrogenase complex. Catalyzes the oxidation of CO in the presence of NAD(+).",No,No,No,No,No,not-Yes,GO:0005524; GO:0016301; GO:0016874,GO:0018492,GO:0016903,GO:0018492,GO:0016491,GO:0016491,0.0,0.3408,0.0,0.4187,0.4187,5,0.2356,0.1883,no
CNS3_CORMM,G3JF10,Protein2Text,Eukaryota,871,"Nucleoside/nucleotide kinase; part of the gene cluster that mediates the biosynthesis of cordycepin (COR) and pentostatin (PTN), two adenosine analogs with related bioactivity profiles as both mimic adenosine and can inhibit some of the processes that are adenosine dependent. Within the pathway, cns3 catalyzes both the first step of cordycepin biosynthesis by phosphorylating adenosine into 3'-AMP via its kinase activity and the conversion of adenosine into pentostatin via its ATP phosphoribosyltransferase activity. The first step of cordycepin biosynthesis involves hydroxyl phosphorylation of the 3'-OH position on adenosine to produce adenosine-3'-monophosphate (3'-AMP), catalyzed by kinase activity of cns3. Next, 3'-AMP is dephosphorylated to 2'-carbonyl-3'-deoxyadenosine (2'-C-3'-dA) by cns2, which is finally converted to cordycepin (3'-deoxyadenosine) by the oxidoreductase cns1.","This protein is a decarboxylase, which means it catalyzes the removal of a carboxyl group from a molecule. More specifically, it is involved in the decarboxylation of a precursor molecule to produce a product molecule.",Vague,No,No,No,No,not-Yes,GO:0005524; GO:0016301; GO:0016874,GO:0016831,GO:0016831,,GO:0016831,GO:0016831,0.2879,0.2879,,0.2879,0.2879,4,0.2879,0.1883,no
CNS3_CORMM,G3JF10,Reference,Eukaryota,871,"Nucleoside/nucleotide kinase; part of the gene cluster that mediates the biosynthesis of cordycepin (COR) and pentostatin (PTN), two adenosine analogs with related bioactivity profiles as both mimic adenosine and can inhibit some of the processes that are adenosine dependent. Within the pathway, cns3 catalyzes both the first step of cordycepin biosynthesis by phosphorylating adenosine into 3'-AMP via its kinase activity and the conversion of adenosine into pentostatin via its ATP phosphoribosyltransferase activity. The first step of cordycepin biosynthesis involves hydroxyl phosphorylation of the 3'-OH position on adenosine to produce adenosine-3'-monophosphate (3'-AMP), catalyzed by kinase activity of cns3. Next, 3'-AMP is dephosphorylated to 2'-carbonyl-3'-deoxyadenosine (2'-C-3'-dA) by cns2, which is finally converted to cordycepin (3'-deoxyadenosine) by the oxidoreductase cns1.","Nucleoside/nucleotide kinase; part of the gene cluster that mediates the biosynthesis of cordycepin (COR) and pentostatin (PTN), two adenosine analogs with related bioactivity profiles as both mimic adenosine and can inhibit some of the processes that are adenosine dependent. Within the pathway, cns3 catalyzes both the first step of cordycepin biosynthesis by phosphorylating adenosine into 3'-AMP via its kinase activity and the conversion of adenosine into pentostatin via its ATP phosphoribosyltransferase activity. The first step of cordycepin biosynthesis involves hydroxyl phosphorylation of the 3'-OH position on adenosine to produce adenosine-3'-monophosphate (3'-AMP), catalyzed by kinase activity of cns3. Next, 3'-AMP is dephosphorylated to 2'-carbonyl-3'-deoxyadenosine (2'-C-3'-dA) by cns2, which is finally converted to cordycepin (3'-deoxyadenosine) by the oxidoreductase cns1.",,,,,,,GO:0005524; GO:0016301; GO:0016874,GO:0016301,GO:0016301; GO:0005524,GO:0016301; GO:0005524,GO:0019206,GO:0016301; GO:0005524,0.6176,0.8814,0.8814,0.4313,0.8814,5,0.7386,0.1883,no
MILA_CORMM,G3JUI8,ESM2Text,Eukaryota,2465,"Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of cordypyrones A and B, 2 pyrones that show modest activities against pathogenic bacteria including methicillin-resistant Staphylococcus aureus (MRSA), Mycobacterium tuberculosis and Bacillus cereus. The HR-PKS milA catalyzes the formation of cordypyrones A via condensation of one acetate with 10 malonate units. Since milA lacks an enoyl reductase domain, the 2 beta-keto processing domains DH and KR of milA collaborate with the trans-enoyl reductase milB to catalyze the different levels of reduction. The cytochrome P450 monooxygenase milC then hydroxylates the C-22 of cordypyrones A to yield cordypyrones B.","Reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcsC,",Maybe,Yes,Yes,Yes,Yes,Yes,GO:0004312; GO:0016491; GO:0031177,,GO:0016746,,GO:0016491,,,0.5114,,0.6206,,2,0.566,0.3304,no
MILA_CORMM,G3JUI8,Prot2Text,Eukaryota,2465,"Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of cordypyrones A and B, 2 pyrones that show modest activities against pathogenic bacteria including methicillin-resistant Staphylococcus aureus (MRSA), Mycobacterium tuberculosis and Bacillus cereus. The HR-PKS milA catalyzes the formation of cordypyrones A via condensation of one acetate with 10 malonate units. Since milA lacks an enoyl reductase domain, the 2 beta-keto processing domains DH and KR of milA collaborate with the trans-enoyl reductase milB to catalyze the different levels of reduction. The cytochrome P450 monooxygenase milC then hydroxylates the C-22 of cordypyrones A to yield cordypyrones B.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Yes,Yes,Maybe,Yes,Yes,Yes,GO:0004312; GO:0016491; GO:0031177,GO:0016746,GO:0016747,GO:0016747,GO:0016746,GO:0016747,0.5114,0.5539,0.5539,0.5114,0.5539,5,0.5369,0.3304,no
MILA_CORMM,G3JUI8,ProtT3,Eukaryota,2465,"Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of cordypyrones A and B, 2 pyrones that show modest activities against pathogenic bacteria including methicillin-resistant Staphylococcus aureus (MRSA), Mycobacterium tuberculosis and Bacillus cereus. The HR-PKS milA catalyzes the formation of cordypyrones A via condensation of one acetate with 10 malonate units. Since milA lacks an enoyl reductase domain, the 2 beta-keto processing domains DH and KR of milA collaborate with the trans-enoyl reductase milB to catalyze the different levels of reduction. The cytochrome P450 monooxygenase milC then hydroxylates the C-22 of cordypyrones A to yield cordypyrones B.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0016491; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016747,0.5114,0.5114,0.5114,0.5539,0.5539,5,0.5284,0.3304,no
MILA_CORMM,G3JUI8,ProtTale,Eukaryota,2465,"Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of cordypyrones A and B, 2 pyrones that show modest activities against pathogenic bacteria including methicillin-resistant Staphylococcus aureus (MRSA), Mycobacterium tuberculosis and Bacillus cereus. The HR-PKS milA catalyzes the formation of cordypyrones A via condensation of one acetate with 10 malonate units. Since milA lacks an enoyl reductase domain, the 2 beta-keto processing domains DH and KR of milA collaborate with the trans-enoyl reductase milB to catalyze the different levels of reduction. The cytochrome P450 monooxygenase milC then hydroxylates the C-22 of cordypyrones A to yield cordypyrones B.","Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. Within the pathway, ptmC catalyzes the last step by converting the 13,14-epoxide of penitrem A to yield penitrem B. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3-glycerol phosphate with",Maybe,Yes,Maybe,Yes,Yes,Yes,GO:0004312; GO:0016491; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.5114,0.5114,0.5114,0.5114,0.5114,5,0.5114,0.3304,no
MILA_CORMM,G3JUI8,Protein2Text,Eukaryota,2465,"Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of cordypyrones A and B, 2 pyrones that show modest activities against pathogenic bacteria including methicillin-resistant Staphylococcus aureus (MRSA), Mycobacterium tuberculosis and Bacillus cereus. The HR-PKS milA catalyzes the formation of cordypyrones A via condensation of one acetate with 10 malonate units. Since milA lacks an enoyl reductase domain, the 2 beta-keto processing domains DH and KR of milA collaborate with the trans-enoyl reductase milB to catalyze the different levels of reduction. The cytochrome P450 monooxygenase milC then hydroxylates the C-22 of cordypyrones A to yield cordypyrones B.","This protein is a part of a biosynthetic pathway that is responsible for the production of a specific compound. The molecular function of this protein is likely to be a decarboxylase or a synthase, involved in the decarboxylation or synthesis of a precursor molecule to form the final compound. However, without more information, it is difficult to determine the exact molecular function of this protein.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004312; GO:0016491; GO:0031177,,,,,,,,,,,0,,0.3304,no
MILA_CORMM,G3JUI8,Reference,Eukaryota,2465,"Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of cordypyrones A and B, 2 pyrones that show modest activities against pathogenic bacteria including methicillin-resistant Staphylococcus aureus (MRSA), Mycobacterium tuberculosis and Bacillus cereus. The HR-PKS milA catalyzes the formation of cordypyrones A via condensation of one acetate with 10 malonate units. Since milA lacks an enoyl reductase domain, the 2 beta-keto processing domains DH and KR of milA collaborate with the trans-enoyl reductase milB to catalyze the different levels of reduction. The cytochrome P450 monooxygenase milC then hydroxylates the C-22 of cordypyrones A to yield cordypyrones B.","Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of cordypyrones A and B, 2 pyrones that show modest activities against pathogenic bacteria including methicillin-resistant Staphylococcus aureus (MRSA), Mycobacterium tuberculosis and Bacillus cereus. The HR-PKS milA catalyzes the formation of cordypyrones A via condensation of one acetate with 10 malonate units. Since milA lacks an enoyl reductase domain, the 2 beta-keto processing domains DH and KR of milA collaborate with the trans-enoyl reductase milB to catalyze the different levels of reduction. The cytochrome P450 monooxygenase milC then hydroxylates the C-22 of cordypyrones A to yield cordypyrones B.",,,,,,,GO:0004312; GO:0016491; GO:0031177,GO:0016740,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.4802,0.5114,0.5114,0.5539,0.5114,5,0.5137,0.3304,no
MTA1_PYRO7,G4MSY9,ESM2Text,Eukaryota,376,"N6-methyladenosine RNA methyltransferase that plays a crucial role in fungal phenotypic traits, virulence, and stress tolerance. Mediates the methylation of mRNAs to produce N6- methyladenosine (m6A)-containing mRNAs. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing. Required for appressorium turgor pressure and regulates autophagosome formation during appressorium formation stage. Specifically, mediates the stability of ATG8 mRNA in a m6A-dependent manner via modification of the m6A site A982 located in 3'UTR region.","A methylase, recognizes the double-stranded sequence 5'-CATNNNNNGGC-3', methylates A-3 on both strands, and protects the DNA from cleavage by the Bsp6I endonuclease.",No,No,No,No,Maybe,not-Yes,GO:0001734; GO:0003723,GO:0009007; GO:0003677,GO:0009007,GO:0009007,GO:0003886; GO:0009007,GO:0009007,0.6039,0.3955,0.3955,0.4332,0.3955,5,0.4447,0.6242,yes
MTA1_PYRO7,G4MSY9,Prot2Text,Eukaryota,376,"N6-methyladenosine RNA methyltransferase that plays a crucial role in fungal phenotypic traits, virulence, and stress tolerance. Mediates the methylation of mRNAs to produce N6- methyladenosine (m6A)-containing mRNAs. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing. Required for appressorium turgor pressure and regulates autophagosome formation during appressorium formation stage. Specifically, mediates the stability of ATG8 mRNA in a m6A-dependent manner via modification of the m6A site A982 located in 3'UTR region.",The N-terminal region of TRK1 is a methylated control region which methylates Lys-36 of histone H3.,No,No,No,No,No,not-Yes,GO:0001734; GO:0003723,GO:0018024,GO:0018024,GO:0018024,GO:0018024,GO:0046975,0.0,0.0,0.0,0.0,0.2548,5,0.051,0.6242,yes
MTA1_PYRO7,G4MSY9,ProtT3,Eukaryota,376,"N6-methyladenosine RNA methyltransferase that plays a crucial role in fungal phenotypic traits, virulence, and stress tolerance. Mediates the methylation of mRNAs to produce N6- methyladenosine (m6A)-containing mRNAs. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing. Required for appressorium turgor pressure and regulates autophagosome formation during appressorium formation stage. Specifically, mediates the stability of ATG8 mRNA in a m6A-dependent manner via modification of the m6A site A982 located in 3'UTR region.",DNA methyltransferase that methylates adenine to N(6)-methyladenine (m6A). Nucleus. Belongs to the class I-like SAM-binding methyltransferase superfamily,No,No,No,No,Maybe,not-Yes,GO:0001734; GO:0003723,GO:0009007; GO:0003677,GO:0009007,GO:0009007,GO:0009007,GO:0009007,0.6039,0.3955,0.3955,0.3955,0.3955,5,0.4372,0.6242,yes
MTA1_PYRO7,G4MSY9,ProtTale,Eukaryota,376,"N6-methyladenosine RNA methyltransferase that plays a crucial role in fungal phenotypic traits, virulence, and stress tolerance. Mediates the methylation of mRNAs to produce N6- methyladenosine (m6A)-containing mRNAs. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing. Required for appressorium turgor pressure and regulates autophagosome formation during appressorium formation stage. Specifically, mediates the stability of ATG8 mRNA in a m6A-dependent manner via modification of the m6A site A982 located in 3'UTR region.","Methylates histone H3 to form H3K79me1, H3K81me1, H3K82me1, and to a lesser extent to H3K79me2, H3K81me2, H3K82me2.",No,No,No,No,No,not-Yes,GO:0001734; GO:0003723,GO:0018024,GO:0018024,GO:0018024,GO:0042054,GO:0018024,0.0,0.0,0.0,0.2846,0.0,5,0.0569,0.6242,yes
MTA1_PYRO7,G4MSY9,Protein2Text,Eukaryota,376,"N6-methyladenosine RNA methyltransferase that plays a crucial role in fungal phenotypic traits, virulence, and stress tolerance. Mediates the methylation of mRNAs to produce N6- methyladenosine (m6A)-containing mRNAs. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing. Required for appressorium turgor pressure and regulates autophagosome formation during appressorium formation stage. Specifically, mediates the stability of ATG8 mRNA in a m6A-dependent manner via modification of the m6A site A982 located in 3'UTR region.","The molecular function of this protein is as a tRNA methyltransferase, specifically involved in the methylation of tRNA molecules. More specifically, it is a lysine methyltransferase that catalyzes the transfer of a methyl group to the N(1) position of lysine residues in tRNA. This process is important for the proper function of tRNA molecules, which are involved in protein synthesis. The protein is likely involved in the post-transcriptional modification of tRNA molecules, specifically the methylation of lysine residues in the anticodon stem-loop region of tRNA molecules. This modification is essential for proper tRNA function and protein synthesis. 
Note: This is an inference based on the name of the protein and general knowledge of its function. The exact function of the protein in the organism may be more specific or complex.",No,No,Maybe,No,No,not-Yes,GO:0001734; GO:0003723,GO:0008175,GO:0008173,GO:0008175,GO:0008173,GO:0008173,0.4601,0.558,0.4601,0.558,0.558,5,0.5188,0.6242,yes
MTA1_PYRO7,G4MSY9,Reference,Eukaryota,376,"N6-methyladenosine RNA methyltransferase that plays a crucial role in fungal phenotypic traits, virulence, and stress tolerance. Mediates the methylation of mRNAs to produce N6- methyladenosine (m6A)-containing mRNAs. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing. Required for appressorium turgor pressure and regulates autophagosome formation during appressorium formation stage. Specifically, mediates the stability of ATG8 mRNA in a m6A-dependent manner via modification of the m6A site A982 located in 3'UTR region.","N6-methyladenosine RNA methyltransferase that plays a crucial role in fungal phenotypic traits, virulence, and stress tolerance. Mediates the methylation of mRNAs to produce N6- methyladenosine (m6A)-containing mRNAs. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing. Required for appressorium turgor pressure and regulates autophagosome formation during appressorium formation stage. Specifically, mediates the stability of ATG8 mRNA in a m6A-dependent manner via modification of the m6A site A982 located in 3'UTR region.",,,,,,,GO:0001734; GO:0003723,GO:0080009,GO:0008168; GO:0003723,GO:0080009,GO:0080009,GO:0080009,0.0,0.7826,0.0,0.0,0.0,5,0.1565,0.6242,yes
AUH1_PYRO7,G4N954,ESM2Text,Eukaryota,349,"3-methylglutaconyl-CoA hydratase that catalyzes the fifth step in the leucine degradation pathway, the reversible hydration of 3- methylglutaconyl-CoA (3-MG-CoA) to 3-hydroxy-3-methylglutaryl-CoA (HMG- CoA). Involved in vegetative growth, conidiation and in the stress response. Controls mitochondrial morphology and mitophagy, which are critical for the infectious growth of the pathogen.",Could possibly oxidize fatty acids using specific components.,Vague,Vague,Maybe,Vague,No,not-Yes,GO:0004490,,,,,,,,,,,0,,0.2217,no
AUH1_PYRO7,G4N954,Prot2Text,Eukaryota,349,"3-methylglutaconyl-CoA hydratase that catalyzes the fifth step in the leucine degradation pathway, the reversible hydration of 3- methylglutaconyl-CoA (3-MG-CoA) to 3-hydroxy-3-methylglutaryl-CoA (HMG- CoA). Involved in vegetative growth, conidiation and in the stress response. Controls mitochondrial morphology and mitophagy, which are critical for the infectious growth of the pathogen.",Enoyl-CoA hydratase required for the degradation of unsaturated fatty acids.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004490,GO:0004300,GO:0004300,GO:0004300,GO:0004300,GO:0004300,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.2217,no
AUH1_PYRO7,G4N954,ProtT3,Eukaryota,349,"3-methylglutaconyl-CoA hydratase that catalyzes the fifth step in the leucine degradation pathway, the reversible hydration of 3- methylglutaconyl-CoA (3-MG-CoA) to 3-hydroxy-3-methylglutaryl-CoA (HMG- CoA). Involved in vegetative growth, conidiation and in the stress response. Controls mitochondrial morphology and mitophagy, which are critical for the infectious growth of the pathogen.",Belongs to the enoyl-CoA hydratase/isomerase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004490,GO:0004300,GO:0004300,,GO:0004300,GO:0004300,0.7289,0.7289,,0.7289,0.7289,4,0.7289,0.2217,no
AUH1_PYRO7,G4N954,ProtTale,Eukaryota,349,"3-methylglutaconyl-CoA hydratase that catalyzes the fifth step in the leucine degradation pathway, the reversible hydration of 3- methylglutaconyl-CoA (3-MG-CoA) to 3-hydroxy-3-methylglutaryl-CoA (HMG- CoA). Involved in vegetative growth, conidiation and in the stress response. Controls mitochondrial morphology and mitophagy, which are critical for the infectious growth of the pathogen.",Decarboxylation of 2-oxoglutarate and 2- oxo-4-methyl-2- oxoglutarate. May play a role in the regulation of the intracellular concentration of 2- oxoglutarate.,No,No,No,No,No,not-Yes,GO:0004490,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.3987,0.3987,0.3987,0.3987,0.3987,5,0.3987,0.2217,no
AUH1_PYRO7,G4N954,Protein2Text,Eukaryota,349,"3-methylglutaconyl-CoA hydratase that catalyzes the fifth step in the leucine degradation pathway, the reversible hydration of 3- methylglutaconyl-CoA (3-MG-CoA) to 3-hydroxy-3-methylglutaryl-CoA (HMG- CoA). Involved in vegetative growth, conidiation and in the stress response. Controls mitochondrial morphology and mitophagy, which are critical for the infectious growth of the pathogen.",This protein is involved in the molecular function of catalyzing the oxidation of the beta-carbon of 3-methylcrotonyl-CoA to form methylmalonyl-CoA. This is a step in the leucine degradation pathway.,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0004490,GO:0004485,GO:0004485,,,GO:0003995,0.1998,0.1998,,,0.1998,3,0.1998,0.2217,no
AUH1_PYRO7,G4N954,Reference,Eukaryota,349,"3-methylglutaconyl-CoA hydratase that catalyzes the fifth step in the leucine degradation pathway, the reversible hydration of 3- methylglutaconyl-CoA (3-MG-CoA) to 3-hydroxy-3-methylglutaryl-CoA (HMG- CoA). Involved in vegetative growth, conidiation and in the stress response. Controls mitochondrial morphology and mitophagy, which are critical for the infectious growth of the pathogen.","3-methylglutaconyl-CoA hydratase that catalyzes the fifth step in the leucine degradation pathway, the reversible hydration of 3- methylglutaconyl-CoA (3-MG-CoA) to 3-hydroxy-3-methylglutaryl-CoA (HMG- CoA). Involved in vegetative growth, conidiation and in the stress response. Controls mitochondrial morphology and mitophagy, which are critical for the infectious growth of the pathogen.",,,,,,,GO:0004490,GO:0004490,GO:0004491,GO:0016836,GO:0004300,GO:0004300,1.0,0.1998,0.8582,0.7289,0.7289,5,0.7032,0.2217,no
CGDB2_ARTG1,H0QPL8,ESM2Text,Bacteria,132,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C8- glycosylated compound 3''-dehydroorientin (3''-oxo-orientin).,"Immunity protein component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion. Protects cells against the tRNase activity of cognate toxin CdiA-CT (CTA-CdA), but not other non-cognate toxins such as CTaA-FdA (CTA-FdA) and CTaB-FdA (CTA-FbA). Part of the ECT toxin-immunity module; disruption of the module confers immunity to CdiA-CTa-FdA and CTaB-FbA. Part of the ECT toxin-immunity module CTA-CdA-CTA-FdA that inhibits CdiA-CTa-FdA (EC(50)=22.5 nM). Unlike the CTA-CdA-CTA-FdA toxin-immunity modules, this EC(50)=22.5 nM is not toxic when injected intracerebroventricularly into mouse lymph",No,No,No,No,No,not-Yes,GO:0016829,,,,,,,,,,,0,,0.3014,no
CGDB2_ARTG1,H0QPL8,Prot2Text,Bacteria,132,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C8- glycosylated compound 3''-dehydroorientin (3''-oxo-orientin).,Unknown. Is essential for viability.,No,No,No,No,Vague,not-Yes,GO:0016829,,,,,,,,,,,0,,0.3014,no
CGDB2_ARTG1,H0QPL8,ProtT3,Bacteria,132,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C8- glycosylated compound 3''-dehydroorientin (3''-oxo-orientin).,To M.tuberculosis Rv1008c,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016829,,,,,,,,,,,0,,0.3014,no
CGDB2_ARTG1,H0QPL8,ProtTale,Bacteria,132,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C8- glycosylated compound 3''-dehydroorientin (3''-oxo-orientin).,"Part of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. The C-terminal 350 amino acids of RimJ form a coiled-coil, which may allow binding of RimJ to its cognate immunity protein, RimI.",No,No,No,No,No,not-Yes,GO:0016829,,,,,,,,,,,0,,0.3014,no
CGDB2_ARTG1,H0QPL8,Protein2Text,Bacteria,132,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C8- glycosylated compound 3''-dehydroorientin (3''-oxo-orientin).,"The molecular function of this protein is not specified in the provided text. However, based on its name, it is likely involved in a process related to the production of a molecule that can cause nerve damage, possibly as a result of its interaction with other molecules. Further research would be required to determine the exact molecular function of this protein.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016829,,,,,,,,,,,0,,0.3014,no
CGDB2_ARTG1,H0QPL8,Reference,Bacteria,132,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C8- glycosylated compound 3''-dehydroorientin (3''-oxo-orientin).,Carbon-carbon bond-cleaving enzyme which participates in the metabolism of C-glycosides. Acts on the C8- glycosylated compound 3''-dehydroorientin (3''-oxo-orientin).,,,,,,,GO:0016829,GO:0016830,GO:0016830,GO:0016830,GO:0016830,GO:0016830,0.8145,0.8145,0.8145,0.8145,0.8145,5,0.8145,0.3014,no
FGL2_GIBZE,I1RCD3,ESM2Text,Eukaryota,408,Secreted mono- and diacylglycerol lipase involved in plant virulence. Has a substrate preference for p- nitrophenyl esters with a carbon chain length of C10 (p-nitrophenyl caprate).,Involved in in the degradation of small bioactive lipids such as phosphatidylcholine.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787; GO:0046872,,GO:0016788,,GO:0016787,,,0.5852,,0.7193,,2,0.6522,0.2991,no
FGL2_GIBZE,I1RCD3,Prot2Text,Eukaryota,408,Secreted mono- and diacylglycerol lipase involved in plant virulence. Has a substrate preference for p- nitrophenyl esters with a carbon chain length of C10 (p-nitrophenyl caprate).,"Shows esterase activity, but it does not hydrolyze phosphatidylcholine, phosphatidylethanolamine, or phosphatidylcholine.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787; GO:0046872,GO:0004091,GO:0004091,GO:0004091,GO:0004091,GO:0004091,0.4947,0.4947,0.4947,0.4947,0.4947,5,0.4947,0.2991,no
FGL2_GIBZE,I1RCD3,ProtT3,Eukaryota,408,Secreted mono- and diacylglycerol lipase involved in plant virulence. Has a substrate preference for p- nitrophenyl esters with a carbon chain length of C10 (p-nitrophenyl caprate).,"Lipase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties",Maybe,Maybe,Vague,Maybe,Maybe,not-Yes,GO:0016787; GO:0046872,GO:0016298,GO:0016298,GO:0004806,GO:0004806,GO:0016298,0.4947,0.4947,0.3817,0.3817,0.4947,5,0.4495,0.2991,no
FGL2_GIBZE,I1RCD3,ProtTale,Eukaryota,408,Secreted mono- and diacylglycerol lipase involved in plant virulence. Has a substrate preference for p- nitrophenyl esters with a carbon chain length of C10 (p-nitrophenyl caprate).,"Secreted lipase that catalyzes the hydrolysis of triacylglycerols to free fatty acids and mono- and diacylglycerols as well as the hydrolysis of phosphatidylethanolamines to phosphatidic acid. Is able to hydrolyze the synthetic substrate p-nitrophenyl palmitate (PNP-C16:0) as well as the natural substrates triacylglycerol 1,3-dioleoylglycerol (1,3-DOG), triacylglycerol 1,3-dioleoylglycerol (1,3-DOG) and triacylglycerol 1,2-dioleoylglycerol (1,2-",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016787; GO:0046872,GO:0004806; GO:0004622,GO:0004806; GO:0004620,GO:0004806,GO:0004806; GO:0016298,GO:0004806,0.3894,0.4222,0.3817,0.5041,0.3817,5,0.4158,0.2991,no
FGL2_GIBZE,I1RCD3,Protein2Text,Eukaryota,408,Secreted mono- and diacylglycerol lipase involved in plant virulence. Has a substrate preference for p- nitrophenyl esters with a carbon chain length of C10 (p-nitrophenyl caprate).,"The molecular function of this protein is to catalyze the hydrolysis of triglycerides, which is a key step in the breakdown of fats in the body. This protein is a type of lipase, an enzyme that plays a crucial role in lipid metabolism.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016787; GO:0046872,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,0.3817,0.3817,0.3817,0.3817,0.3817,5,0.3817,0.2991,no
FGL2_GIBZE,I1RCD3,Reference,Eukaryota,408,Secreted mono- and diacylglycerol lipase involved in plant virulence. Has a substrate preference for p- nitrophenyl esters with a carbon chain length of C10 (p-nitrophenyl caprate).,Secreted mono- and diacylglycerol lipase involved in plant virulence. Has a substrate preference for p- nitrophenyl esters with a carbon chain length of C10 (p-nitrophenyl caprate).,,,,,,,GO:0016787; GO:0046872,GO:0016298,GO:0016298,GO:0016298,GO:0016298,GO:0016298,0.4947,0.4947,0.4947,0.4947,0.4947,5,0.4947,0.2991,no
FGL4_GIBZE,I1RHF8,ESM2Text,Eukaryota,556,Secreted lipase involved in plant virulence. Has a substrate preference for p-nitrophenyl esters with a carbon chain length of C12 (p-nitrophenyl laureate).,Converts triglyceride to ester and plays a significant role in the global supply of triglyceride.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0106435,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,0.6576,0.6576,0.6576,0.6576,0.6576,5,0.6576,0.2052,no
FGL4_GIBZE,I1RHF8,Prot2Text,Eukaryota,556,Secreted lipase involved in plant virulence. Has a substrate preference for p-nitrophenyl esters with a carbon chain length of C12 (p-nitrophenyl laureate).,Carboxylesterase acting on esters with varying acyl chain length.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0106435,GO:0004091,GO:0004091,GO:0004091,GO:0004091,GO:0004091,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.2052,no
FGL4_GIBZE,I1RHF8,ProtT3,Eukaryota,556,Secreted lipase involved in plant virulence. Has a substrate preference for p-nitrophenyl esters with a carbon chain length of C12 (p-nitrophenyl laureate).,Secreted. Belongs to the type-B carboxylesterase/lipase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0106435,GO:0004091,GO:0052689,GO:0004091,GO:0004091,GO:0004091,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.2052,no
FGL4_GIBZE,I1RHF8,ProtTale,Eukaryota,556,Secreted lipase involved in plant virulence. Has a substrate preference for p-nitrophenyl esters with a carbon chain length of C12 (p-nitrophenyl laureate).,"Secreted lipase that catalyzes the hydrolysis of triacylglycerols into free fatty acids and glycerol, and of diacylglycerols into free fatty acids and monoacylglycerols. Can also hydrolyze p-nitrophenyl palmitate (p-NPP) and 4- methylumbelliferyl palmitate (4-MUP), but not 4-methylumbelliferyl oleate, 4-methylumbelliferyl stearate, 4-methylumbelliferyl laurate, 4-methylumbelliferyl myristate, 4-methylumbelliferyl palmitoleate,",Yes,Yes,Yes,Yes,Yes,Yes,GO:0106435,GO:0004806,GO:0004806,GO:0004806,GO:0004806; GO:0016298,GO:0004806,0.6576,0.6576,0.6576,0.6394,0.6576,5,0.654,0.2052,no
FGL4_GIBZE,I1RHF8,Protein2Text,Eukaryota,556,Secreted lipase involved in plant virulence. Has a substrate preference for p-nitrophenyl esters with a carbon chain length of C12 (p-nitrophenyl laureate).,"This protein is a lipase, which means it is involved in the breakdown of lipids into fatty acids and glycerol. More specifically, it is involved in the hydrolysis of triglycerides into glycerol and free fatty acids. This is an important step in the digestion and metabolism of fats in the body.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0106435,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,0.6576,0.6576,0.6576,0.6576,0.6576,5,0.6576,0.2052,no
FGL4_GIBZE,I1RHF8,Reference,Eukaryota,556,Secreted lipase involved in plant virulence. Has a substrate preference for p-nitrophenyl esters with a carbon chain length of C12 (p-nitrophenyl laureate).,Secreted lipase involved in plant virulence. Has a substrate preference for p-nitrophenyl esters with a carbon chain length of C12 (p-nitrophenyl laureate).,,,,,,,GO:0106435,GO:0016298,GO:0016298,GO:0016298,GO:0016298,GO:0016298,0.6029,0.6029,0.6029,0.6029,0.6029,5,0.6029,0.2052,no
FGL5_GIBZE,I1RIF1,ESM2Text,Eukaryota,535,Secreted lipase involved in plant virulence. Has a substrate preference for p-nitrophenyl esters with a carbon chain length of C8 (p-nitrophenyl caprylate).,Carboxylesterase acting on ester bonds.,Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0106435,GO:0004091,GO:0004091,GO:0004091,GO:0004091,GO:0004091,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.2085,no
FGL5_GIBZE,I1RIF1,Prot2Text,Eukaryota,535,Secreted lipase involved in plant virulence. Has a substrate preference for p-nitrophenyl esters with a carbon chain length of C8 (p-nitrophenyl caprylate).,Overproduction of nonspecific esterases is a common mechanism of resistance to organophosphate insecticides.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0106435,GO:0004091,GO:0004091,GO:0004091,GO:0004091,GO:0004091,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.2085,no
FGL5_GIBZE,I1RIF1,ProtT3,Eukaryota,535,Secreted lipase involved in plant virulence. Has a substrate preference for p-nitrophenyl esters with a carbon chain length of C8 (p-nitrophenyl caprylate).,Secreted. Belongs to the type-B carboxylesterase/lipase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0106435,GO:0004091,GO:0052689,GO:0004091,GO:0004091,GO:0004091,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.2085,no
FGL5_GIBZE,I1RIF1,ProtTale,Eukaryota,535,Secreted lipase involved in plant virulence. Has a substrate preference for p-nitrophenyl esters with a carbon chain length of C8 (p-nitrophenyl caprylate).,"Secreted lipase that is able to hydrolyze triacylglycerols into free fatty acids and glycerol. Is also able to hydrolyze 4-methylumbelliferyl acetate, 4- methylumbelliferyl butyrate, 4-methylumbelliferyl hexanoate, 4-methylumbelliferyl heptanoate, 4-methylumbelliferyl laurate, 4-methylumbelliferyl myristate, 4-methylumbelliferyl palmitate, 4-methylumbelliferyl stearate, 4-methylumbelliferyl oleate and 4-",Yes,Yes,Yes,Yes,Yes,Yes,GO:0106435,GO:0004806,GO:0004806,GO:0004806,GO:0004806; GO:0016298,GO:0004806,0.6576,0.6576,0.6576,0.6394,0.6576,5,0.654,0.2085,no
FGL5_GIBZE,I1RIF1,Protein2Text,Eukaryota,535,Secreted lipase involved in plant virulence. Has a substrate preference for p-nitrophenyl esters with a carbon chain length of C8 (p-nitrophenyl caprylate).,"This protein is involved in the degradation of organic compounds, specifically it is a lipase that breaks down triglycerides into fatty acids and glycerol.",Yes,Yes,Maybe,Yes,Yes,Yes,GO:0106435,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,0.6576,0.6576,0.6576,0.6576,0.6576,5,0.6576,0.2085,no
FGL5_GIBZE,I1RIF1,Reference,Eukaryota,535,Secreted lipase involved in plant virulence. Has a substrate preference for p-nitrophenyl esters with a carbon chain length of C8 (p-nitrophenyl caprylate).,Secreted lipase involved in plant virulence. Has a substrate preference for p-nitrophenyl esters with a carbon chain length of C8 (p-nitrophenyl caprylate).,,,,,,,GO:0106435,GO:0016298,GO:0016298,GO:0016298,GO:0016298,GO:0016298,0.6029,0.6029,0.6029,0.6029,0.6029,5,0.6029,0.2085,no
FGR3_GIBZE,I1RLA5,ESM2Text,Eukaryota,497,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the tetraketides fugralins such as linear fugralin A and cyclic fugralin B, volatile compounds that play a role in the asexual reproductive cycle but are not involved in pathogenicity. One of the key features of fugralins is the presence of a double methyl group, which is only rarely encountered in fungal secondary metabolites. As the fugralins cluster does not contain an independent methyltransferase, the PKS FGR1 is probably responsible for adding two methyl groups to the same carbon atom (Probable). Fugralin B is similar to fugralin A except for a cyclization between the carboxylic acid C-8 and the alcohol on C-4 resulting in a six membered lactone ring, probably catalyzed by the cyclase FGR4 (Probable). The exact role of the individual cluster genes remains unknown and further work is needed to unravel the biosynthetic pathway (Probable).","Involved in the biosynthesis of acyl-CoA, a major component of the mycobacterial cell wall. Catalyzes the formation of the methyl ester of 4-methylnon-3-methylnonadienoate (MNA), a key intermediate in the biosynthesis of the acyl-CoA epoxide-sphingoid-monooxygenase inhibitor (CPAO), a component of the methyl-CPAO epoxide-sphingoid-monooxygenase (MEPO) multicomponent enzyme system.",No,No,Maybe,No,No,not-Yes,GO:0046872; GO:0016740,,,,,,,,,,,0,,0.2443,no
FGR3_GIBZE,I1RLA5,Prot2Text,Eukaryota,497,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the tetraketides fugralins such as linear fugralin A and cyclic fugralin B, volatile compounds that play a role in the asexual reproductive cycle but are not involved in pathogenicity. One of the key features of fugralins is the presence of a double methyl group, which is only rarely encountered in fungal secondary metabolites. As the fugralins cluster does not contain an independent methyltransferase, the PKS FGR1 is probably responsible for adding two methyl groups to the same carbon atom (Probable). Fugralin B is similar to fugralin A except for a cyclization between the carboxylic acid C-8 and the alcohol on C-4 resulting in a six membered lactone ring, probably catalyzed by the cyclase FGR4 (Probable). The exact role of the individual cluster genes remains unknown and further work is needed to unravel the biosynthetic pathway (Probable).",Involved in the biosynthesis of volatile esters which confer kiwifruit flavor. Alcohol acyl transferase that can use a wide range of alcohols as substrate to produce esters. Exhibits acetyl-CoA:alcohol O-acyltransferase activity.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0016740,GO:0016746,GO:0004026,GO:0004026,GO:0004026,GO:0004026,0.5852,0.2879,0.2879,0.2879,0.2879,5,0.3474,0.2443,no
FGR3_GIBZE,I1RLA5,ProtT3,Eukaryota,497,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the tetraketides fugralins such as linear fugralin A and cyclic fugralin B, volatile compounds that play a role in the asexual reproductive cycle but are not involved in pathogenicity. One of the key features of fugralins is the presence of a double methyl group, which is only rarely encountered in fungal secondary metabolites. As the fugralins cluster does not contain an independent methyltransferase, the PKS FGR1 is probably responsible for adding two methyl groups to the same carbon atom (Probable). Fugralin B is similar to fugralin A except for a cyclization between the carboxylic acid C-8 and the alcohol on C-4 resulting in a six membered lactone ring, probably catalyzed by the cyclase FGR4 (Probable). The exact role of the individual cluster genes remains unknown and further work is needed to unravel the biosynthetic pathway (Probable).",O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylger,Yes,Maybe,Maybe,Yes,Yes,Yes,GO:0046872; GO:0016740,GO:0016413,GO:0016413,GO:0016407,GO:0016407,GO:0016407,0.3421,0.3421,0.4309,0.4309,0.4309,5,0.3954,0.2443,no
FGR3_GIBZE,I1RLA5,ProtTale,Eukaryota,497,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the tetraketides fugralins such as linear fugralin A and cyclic fugralin B, volatile compounds that play a role in the asexual reproductive cycle but are not involved in pathogenicity. One of the key features of fugralins is the presence of a double methyl group, which is only rarely encountered in fungal secondary metabolites. As the fugralins cluster does not contain an independent methyltransferase, the PKS FGR1 is probably responsible for adding two methyl groups to the same carbon atom (Probable). Fugralin B is similar to fugralin A except for a cyclization between the carboxylic acid C-8 and the alcohol on C-4 resulting in a six membered lactone ring, probably catalyzed by the cyclase FGR4 (Probable). The exact role of the individual cluster genes remains unknown and further work is needed to unravel the biosynthetic pathway (Probable).","Acyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0016740,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016747,0.5852,0.5852,0.5852,0.5852,0.4947,5,0.5671,0.2443,no
FGR3_GIBZE,I1RLA5,Protein2Text,Eukaryota,497,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the tetraketides fugralins such as linear fugralin A and cyclic fugralin B, volatile compounds that play a role in the asexual reproductive cycle but are not involved in pathogenicity. One of the key features of fugralins is the presence of a double methyl group, which is only rarely encountered in fungal secondary metabolites. As the fugralins cluster does not contain an independent methyltransferase, the PKS FGR1 is probably responsible for adding two methyl groups to the same carbon atom (Probable). Fugralin B is similar to fugralin A except for a cyclization between the carboxylic acid C-8 and the alcohol on C-4 resulting in a six membered lactone ring, probably catalyzed by the cyclase FGR4 (Probable). The exact role of the individual cluster genes remains unknown and further work is needed to unravel the biosynthetic pathway (Probable).","The molecular function of this protein is involved in oxidation-reduction reactions, specifically as an oxidoreductase. It is also known to catalyze the oxidation of alcohols to aldehydes and ketones, and is involved in the metabolism of various compounds.",No,No,No,No,No,not-Yes,GO:0046872; GO:0016740,GO:0016614,GO:0016614,GO:0016614,GO:0016614,GO:0016614,0.3626,0.3626,0.3626,0.3626,0.3626,5,0.3626,0.2443,no
FGR3_GIBZE,I1RLA5,Reference,Eukaryota,497,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the tetraketides fugralins such as linear fugralin A and cyclic fugralin B, volatile compounds that play a role in the asexual reproductive cycle but are not involved in pathogenicity. One of the key features of fugralins is the presence of a double methyl group, which is only rarely encountered in fungal secondary metabolites. As the fugralins cluster does not contain an independent methyltransferase, the PKS FGR1 is probably responsible for adding two methyl groups to the same carbon atom (Probable). Fugralin B is similar to fugralin A except for a cyclization between the carboxylic acid C-8 and the alcohol on C-4 resulting in a six membered lactone ring, probably catalyzed by the cyclase FGR4 (Probable). The exact role of the individual cluster genes remains unknown and further work is needed to unravel the biosynthetic pathway (Probable).","Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the tetraketides fugralins such as linear fugralin A and cyclic fugralin B, volatile compounds that play a role in the asexual reproductive cycle but are not involved in pathogenicity. One of the key features of fugralins is the presence of a double methyl group, which is only rarely encountered in fungal secondary metabolites. As the fugralins cluster does not contain an independent methyltransferase, the PKS FGR1 is probably responsible for adding two methyl groups to the same carbon atom (Probable). Fugralin B is similar to fugralin A except for a cyclization between the carboxylic acid C-8 and the alcohol on C-4 resulting in a six membered lactone ring, probably catalyzed by the cyclase FGR4 (Probable). The exact role of the individual cluster genes remains unknown and further work is needed to unravel the biosynthetic pathway (Probable).",,,,,,,GO:0046872; GO:0016740,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.4309,0.4309,0.4309,0.4309,0.4309,5,0.4309,0.2443,no
SQWG_CLOS9,J0MXK0,ESM2Text,Bacteria,275,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes two steps of the pathway: the formation of 4-deoxy- 4-sulfoerythrose (SE) and xylulose 5-phosphate from 6-deoxy-6-sulfo-D- fructose (SF) and glyceraldehyde 3-phosphate, and the formation of sulfoacetaldehyde (SA) and xylulose 5-phosphate from 4-deoxy-4-sulfo-D- erythrulose (SEu) and glyceraldehyde 3-phosphate (Ref.2).",Involved in catabolism of D-apiose. Catalyzes the transfer of the glycolaldehyde group from apulose-4-phosphate to D-apionate.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016740,GO:0004802,GO:0004802,GO:0004802,GO:0004802,GO:0004802,0.6897,0.6897,0.6897,0.6897,0.6897,5,0.6897,0.4956,no
SQWG_CLOS9,J0MXK0,Prot2Text,Bacteria,275,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes two steps of the pathway: the formation of 4-deoxy- 4-sulfoerythrose (SE) and xylulose 5-phosphate from 6-deoxy-6-sulfo-D- fructose (SF) and glyceraldehyde 3-phosphate, and the formation of sulfoacetaldehyde (SA) and xylulose 5-phosphate from 4-deoxy-4-sulfo-D- erythrulose (SEu) and glyceraldehyde 3-phosphate (Ref.2).","Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.",Maybe,Maybe,Maybe,Yes,Yes,not-Yes,GO:0016740,GO:0008935,GO:0008935,GO:0008935,GO:0008935,GO:0008935,0.3552,0.3552,0.3552,0.3552,0.3552,5,0.3552,0.4956,no
SQWG_CLOS9,J0MXK0,ProtT3,Bacteria,275,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes two steps of the pathway: the formation of 4-deoxy- 4-sulfoerythrose (SE) and xylulose 5-phosphate from 6-deoxy-6-sulfo-D- fructose (SF) and glyceraldehyde 3-phosphate, and the formation of sulfoacetaldehyde (SA) and xylulose 5-phosphate from 4-deoxy-4-sulfo-D- erythrulose (SEu) and glyceraldehyde 3-phosphate (Ref.2).","Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. Belongs to the transketolase family",Maybe,Maybe,Maybe,Yes,Yes,not-Yes,GO:0016740,GO:0004802; GO:0030976,GO:0004802,GO:0004802,GO:0004802,GO:0004802,0.4958,0.6897,0.6897,0.6897,0.6897,5,0.6509,0.4956,no
SQWG_CLOS9,J0MXK0,ProtTale,Bacteria,275,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes two steps of the pathway: the formation of 4-deoxy- 4-sulfoerythrose (SE) and xylulose 5-phosphate from 6-deoxy-6-sulfo-D- fructose (SF) and glyceraldehyde 3-phosphate, and the formation of sulfoacetaldehyde (SA) and xylulose 5-phosphate from 4-deoxy-4-sulfo-D- erythrulose (SEu) and glyceraldehyde 3-phosphate (Ref.2).","NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.",No,No,No,No,No,not-Yes,GO:0016740,GO:0008137,GO:0008137,GO:0008137; GO:0015078,GO:0008137,GO:0008137,0.1204,0.1204,0.1454,0.1204,0.1204,5,0.1254,0.4956,no
SQWG_CLOS9,J0MXK0,Protein2Text,Bacteria,275,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes two steps of the pathway: the formation of 4-deoxy- 4-sulfoerythrose (SE) and xylulose 5-phosphate from 6-deoxy-6-sulfo-D- fructose (SF) and glyceraldehyde 3-phosphate, and the formation of sulfoacetaldehyde (SA) and xylulose 5-phosphate from 4-deoxy-4-sulfo-D- erythrulose (SEu) and glyceraldehyde 3-phosphate (Ref.2).","The molecular function of this protein is a part of the pyridoxal kinase enzyme, which is involved in the biosynthesis of pyridoxal phosphate (PLP). The pyridoxal kinase enzyme catalyzes the phosphorylation of pyridoxal to form pyridoxal phosphate (PLP), which is a cofactor for many enzymes in amino acid metabolism.",No,No,No,No,No,not-Yes,GO:0016740,GO:0004084,GO:0004084,GO:0004084,GO:0004084,GO:0004084,0.6019,0.6019,0.6019,0.6019,0.6019,5,0.6019,0.4956,no
SQWG_CLOS9,J0MXK0,Reference,Bacteria,275,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes two steps of the pathway: the formation of 4-deoxy- 4-sulfoerythrose (SE) and xylulose 5-phosphate from 6-deoxy-6-sulfo-D- fructose (SF) and glyceraldehyde 3-phosphate, and the formation of sulfoacetaldehyde (SA) and xylulose 5-phosphate from 4-deoxy-4-sulfo-D- erythrulose (SEu) and glyceraldehyde 3-phosphate (Ref.2).","Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes two steps of the pathway: the formation of 4-deoxy- 4-sulfoerythrose (SE) and xylulose 5-phosphate from 6-deoxy-6-sulfo-D- fructose (SF) and glyceraldehyde 3-phosphate, and the formation of sulfoacetaldehyde (SA) and xylulose 5-phosphate from 4-deoxy-4-sulfo-D- erythrulose (SEu) and glyceraldehyde 3-phosphate (Ref.2).",,,,,,,GO:0016740,GO:0004802,GO:0004802,GO:0004802,GO:0004802,GO:0004802,0.6897,0.6897,0.6897,0.6897,0.6897,5,0.6897,0.4956,no
SQWH_CLOS9,J1H0Z7,ESM2Text,Bacteria,322,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes two steps of the pathway: the formation of 4-deoxy- 4-sulfoerythrose (SE) and xylulose 5-phosphate from 6-deoxy-6-sulfo-D- fructose (SF) and glyceraldehyde 3-phosphate, and the formation of sulfoacetaldehyde (SA) and xylulose 5-phosphate from 4-deoxy-4-sulfo-D- erythrulose (SEu) and glyceraldehyde 3-phosphate (Ref.2).","Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.",Maybe,Maybe,Maybe,Yes,Yes,not-Yes,GO:0016740,GO:0004802,GO:0004802,GO:0004802,GO:0004802,GO:0004802,0.6897,0.6897,0.6897,0.6897,0.6897,5,0.6897,0.3444,no
SQWH_CLOS9,J1H0Z7,Prot2Text,Bacteria,322,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes two steps of the pathway: the formation of 4-deoxy- 4-sulfoerythrose (SE) and xylulose 5-phosphate from 6-deoxy-6-sulfo-D- fructose (SF) and glyceraldehyde 3-phosphate, and the formation of sulfoacetaldehyde (SA) and xylulose 5-phosphate from 4-deoxy-4-sulfo-D- erythrulose (SEu) and glyceraldehyde 3-phosphate (Ref.2).","Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB).",No,No,No,No,No,not-Yes,GO:0016740,GO:0008935,GO:0008935,GO:0008935,GO:0008935,GO:0008935,0.3552,0.3552,0.3552,0.3552,0.3552,5,0.3552,0.3444,no
SQWH_CLOS9,J1H0Z7,ProtT3,Bacteria,322,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes two steps of the pathway: the formation of 4-deoxy- 4-sulfoerythrose (SE) and xylulose 5-phosphate from 6-deoxy-6-sulfo-D- fructose (SF) and glyceraldehyde 3-phosphate, and the formation of sulfoacetaldehyde (SA) and xylulose 5-phosphate from 4-deoxy-4-sulfo-D- erythrulose (SEu) and glyceraldehyde 3-phosphate (Ref.2).","Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. Belongs to the transketolase family",Maybe,Maybe,Maybe,Yes,Yes,not-Yes,GO:0016740,GO:0004802; GO:0030976,GO:0004802,GO:0004802,GO:0004802,GO:0004802,0.4958,0.6897,0.6897,0.6897,0.6897,5,0.6509,0.3444,no
SQWH_CLOS9,J1H0Z7,ProtTale,Bacteria,322,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes two steps of the pathway: the formation of 4-deoxy- 4-sulfoerythrose (SE) and xylulose 5-phosphate from 6-deoxy-6-sulfo-D- fructose (SF) and glyceraldehyde 3-phosphate, and the formation of sulfoacetaldehyde (SA) and xylulose 5-phosphate from 4-deoxy-4-sulfo-D- erythrulose (SEu) and glyceraldehyde 3-phosphate (Ref.2).","Involved in the biosynthesis of the siderophore enterobactin. Catalyzes the oxidation of (2R,3S)-2,3-dihydroxybacilline (DHB) to (2R,3R)-2,3-dihydroxybenzoate (DHB).",No,No,No,No,No,not-Yes,GO:0016740,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.5902,0.5902,0.5902,0.5902,0.5902,5,0.5902,0.3444,no
SQWH_CLOS9,J1H0Z7,Protein2Text,Bacteria,322,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes two steps of the pathway: the formation of 4-deoxy- 4-sulfoerythrose (SE) and xylulose 5-phosphate from 6-deoxy-6-sulfo-D- fructose (SF) and glyceraldehyde 3-phosphate, and the formation of sulfoacetaldehyde (SA) and xylulose 5-phosphate from 4-deoxy-4-sulfo-D- erythrulose (SEu) and glyceraldehyde 3-phosphate (Ref.2).","The molecular function of this protein is an aminotransferase, specifically involved in the breakdown of branched-chain amino acids. It catalyzes the reversible transfer of an amino group from a branched-chain amino acid to alpha-ketoglutarate, producing glutamate and an alpha-keto acid. This protein plays a crucial role in the metabolism of branched-chain amino acids, which are essential nutrients for the organism. It is involved in the catabolic pathway of these amino acids, allowing their breakdown and utilization for energy production, biosynthesis, or other cellular processes. The exact function of this protein is to convert leucine to 2-ketoisovalerate, which is a key step in the metabolism of this amino acid. The protein is also involved in the catabolism of other branched-chain amino acids, such as valine and isoleucine, by catalyzing their conversion to their respective alpha-keto acids. In addition, it may also have a role in the regulation of the levels of branched-chain amino acids and their metabolites in the cell. 

This protein is also known as branched-chain amino acid aminotransferase, leucine aminotransferase, or branched-chain amino acid transaminase. It is a mitochondrial enzyme, which means it is located in the mitochondria, the energy-producing organelles found in eukaryotic cells. 

In summary, the molecular function of this protein is to catalyze the breakdown of branched-chain amino acids by converting them into their respective alpha-keto acids, allowing their utilization for energy production, biosynthesis, or other cellular processes. 

It is worth noting that the specific function of this protein may vary depending on the organism and the cellular context in which it is expressed. However, in general, it plays a crucial role in the metabolism of branched-chain amino acids and their regulation in the cell.",No,No,No,No,No,not-Yes,GO:0016740,GO:0004084,GO:0004084,GO:0004084,GO:0004084,GO:0004084,0.6019,0.6019,0.6019,0.6019,0.6019,5,0.6019,0.3444,no
SQWH_CLOS9,J1H0Z7,Reference,Bacteria,322,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes two steps of the pathway: the formation of 4-deoxy- 4-sulfoerythrose (SE) and xylulose 5-phosphate from 6-deoxy-6-sulfo-D- fructose (SF) and glyceraldehyde 3-phosphate, and the formation of sulfoacetaldehyde (SA) and xylulose 5-phosphate from 4-deoxy-4-sulfo-D- erythrulose (SEu) and glyceraldehyde 3-phosphate (Ref.2).","Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes two steps of the pathway: the formation of 4-deoxy- 4-sulfoerythrose (SE) and xylulose 5-phosphate from 6-deoxy-6-sulfo-D- fructose (SF) and glyceraldehyde 3-phosphate, and the formation of sulfoacetaldehyde (SA) and xylulose 5-phosphate from 4-deoxy-4-sulfo-D- erythrulose (SEu) and glyceraldehyde 3-phosphate (Ref.2).",,,,,,,GO:0016740,GO:0004802,GO:0004802,GO:0004802,GO:0004802,GO:0004802,0.6897,0.6897,0.6897,0.6897,0.6897,5,0.6897,0.3444,no
SIDH_BEAB2,J4KLY0,ESM2Text,Eukaryota,280,"Mevalonyl-coenzyme A hydratase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. For biosynthesis of fusarinine C, the transacylase SIDF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by SIDI and sidH respectively. SIDH is not essential for siderophore production, probably due to functional redundancy of this protein family, as there are 15 homologs of SIDH in B.bassiana.","Straight-chain enoyl-CoA hydratases are used to synthesize the fatty acids malonyl-CoA, hexacrylate and stearate.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016853; GO:0016829,GO:0004300,GO:0004300,GO:0004300,GO:0004300,GO:0004300,0.5197,0.5197,0.5197,0.5197,0.5197,5,0.5197,0.1978,no
SIDH_BEAB2,J4KLY0,Prot2Text,Eukaryota,280,"Mevalonyl-coenzyme A hydratase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. For biosynthesis of fusarinine C, the transacylase SIDF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by SIDI and sidH respectively. SIDH is not essential for siderophore production, probably due to functional redundancy of this protein family, as there are 15 homologs of SIDH in B.bassiana.","Dehalogenates 4-chlorobenzoyl-CoA, 4-iodobenzoyl-CoA, 4-bromobenzoyl-CoA and, at a slower rate, 4-fluorobenzoyl-CoA. Does not dehalogenate 2-chlorobenzoyl-CoA or 3-chlorobenzoyl-CoA.",No,No,No,No,No,not-Yes,GO:0016853; GO:0016829,GO:0016787,GO:0016787,GO:0018784,GO:0018786,GO:0018784,0.5902,0.5902,0.3552,0.3552,0.3552,5,0.4492,0.1978,no
SIDH_BEAB2,J4KLY0,ProtT3,Eukaryota,280,"Mevalonyl-coenzyme A hydratase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. For biosynthesis of fusarinine C, the transacylase SIDF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by SIDI and sidH respectively. SIDH is not essential for siderophore production, probably due to functional redundancy of this protein family, as there are 15 homologs of SIDH in B.bassiana.",Enoyl-CoA hydratase/isomerase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms,Maybe,Maybe,Vague,Maybe,Maybe,not-Yes,GO:0016853; GO:0016829,GO:0004300,GO:0004300,GO:0004300,GO:0004300,GO:0004300,0.5197,0.5197,0.5197,0.5197,0.5197,5,0.5197,0.1978,no
SIDH_BEAB2,J4KLY0,ProtTale,Eukaryota,280,"Mevalonyl-coenzyme A hydratase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. For biosynthesis of fusarinine C, the transacylase SIDF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by SIDI and sidH respectively. SIDH is not essential for siderophore production, probably due to functional redundancy of this protein family, as there are 15 homologs of SIDH in B.bassiana.","Enoyl-CoA hydratase; part of the gene clusters that mediate the biosynthesis of the host-selective toxins (HSTs) AF-toxins responsible for Alternaria black spot of strawberry disease by the strawberry pathotype. AF-toxin I and III are valine derivatives of 2,3-dyhydroxy-isovaleric acid and 2-hydroxy-isovaleric acid respectively, while AF II is an isoleucine derivative of 2- hydroxy-valeric acid. These derivatives are bound to a 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016853; GO:0016829,GO:0004300,GO:0004300,GO:0004300,GO:0004300,GO:0004300,0.5197,0.5197,0.5197,0.5197,0.5197,5,0.5197,0.1978,no
SIDH_BEAB2,J4KLY0,Protein2Text,Eukaryota,280,"Mevalonyl-coenzyme A hydratase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. For biosynthesis of fusarinine C, the transacylase SIDF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by SIDI and sidH respectively. SIDH is not essential for siderophore production, probably due to functional redundancy of this protein family, as there are 15 homologs of SIDH in B.bassiana.","The molecular function of this protein is to catalyze a reaction, specifically a type of reduction reaction, as it is involved in the reduction of a certain compound. However, the specific type of reaction or the substrate it acts on is not specified in the provided text.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016853; GO:0016829,,,,,,,,,,,0,,0.1978,no
SIDH_BEAB2,J4KLY0,Reference,Eukaryota,280,"Mevalonyl-coenzyme A hydratase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. For biosynthesis of fusarinine C, the transacylase SIDF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by SIDI and sidH respectively. SIDH is not essential for siderophore production, probably due to functional redundancy of this protein family, as there are 15 homologs of SIDH in B.bassiana.","Mevalonyl-coenzyme A hydratase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. For biosynthesis of fusarinine C, the transacylase SIDF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by SIDI and sidH respectively. SIDH is not essential for siderophore production, probably due to functional redundancy of this protein family, as there are 15 homologs of SIDH in B.bassiana.",,,,,,,GO:0016853; GO:0016829,GO:0016836,GO:0016836,GO:0016836,GO:0016836,GO:0016836,0.5955,0.5955,0.5955,0.5955,0.5955,5,0.5955,0.1978,no
NRPSC_BEAB2,J4UPH3,ESM2Text,Eukaryota,3920,Nonribosomal peptide synthetase that plays probably a role during infection of diamondback moth (Plutella xylostella (Linnaeus)). The secondary metabolite produced by BBA_03671 and its associated gene cluster remains to be identified.,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the host-selective toxins (HSTs) AAL-toxins, sphinganine-analog mycotoxins responsible for Alternaria stem canker on tomato by the tomato pathotype. The biosynthesis starts with the polyketide synthase ALT1-catalyzed C-16 carbon chain assembly from one starter acetyl-CoA unit with malonyl-CoA extender units. ALT1 also selectively transfers methyl groups at the first and the third cycle of chain elongation for AAL toxin. The C-16 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of glycin by decarboxylation, on the carbonyl carbon of polyketide acyl chain (Probable). This step is probably catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase ALT4 (Probable). The respective functions of the other enzymes encoded by the cluster have still to be elucidated (Probable). The sphingosine N-acyltransfer",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016874; GO:0031177,GO:0016874,GO:0016874,,,,0.709,0.709,,,,2,0.709,0.3418,no
NRPSC_BEAB2,J4UPH3,Prot2Text,Eukaryota,3920,Nonribosomal peptide synthetase that plays probably a role during infection of diamondback moth (Plutella xylostella (Linnaeus)). The secondary metabolite produced by BBA_03671 and its associated gene cluster remains to be identified.,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the host-selective toxins (HSTs) AAL-toxins, sphinganine-analog mycotoxins responsible for Alternaria stem canker on tomato by the tomato pathotype. The biosynthesis starts with the polyketide synthase ALT1-catalyzed C-16 carbon chain assembly from one starter acetyl-CoA unit with malonyl-CoA extender units. ALT1 also selectively transfers methyl groups at the first and the third cycle of chain elongation for AAL toxin. The C-16 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of glycin by decarboxylation, on the carbonyl carbon of polyketide acyl chain (Probable). This step is probably catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase ALT4 (Probable). The respective functions of the other enzymes encoded by the cluster have still to be elucidated (Probable). The sphingosine N-acyltransfer",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016874; GO:0031177,GO:0016874,GO:0016874,GO:0016874,GO:0016874,GO:0016874,0.709,0.709,0.709,0.709,0.709,5,0.709,0.3418,no
NRPSC_BEAB2,J4UPH3,ProtT3,Eukaryota,3920,Nonribosomal peptide synthetase that plays probably a role during infection of diamondback moth (Plutella xylostella (Linnaeus)). The secondary metabolite produced by BBA_03671 and its associated gene cluster remains to be identified.,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016874; GO:0031177,GO:0016874; GO:0005524,GO:0016874,GO:0016874,GO:0016874; GO:0005524,GO:0016874,0.6793,0.709,0.709,0.6793,0.709,5,0.6971,0.3418,no
NRPSC_BEAB2,J4UPH3,ProtTale,Eukaryota,3920,Nonribosomal peptide synthetase that plays probably a role during infection of diamondback moth (Plutella xylostella (Linnaeus)). The secondary metabolite produced by BBA_03671 and its associated gene cluster remains to be identified.,"Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties. L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism. The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016874; GO:0031177,GO:0016874,GO:0016874,GO:0016874,GO:0016874; GO:0005524,GO:0016874,0.709,0.709,0.709,0.6793,0.709,5,0.7031,0.3418,no
NRPSC_BEAB2,J4UPH3,Protein2Text,Eukaryota,3920,Nonribosomal peptide synthetase that plays probably a role during infection of diamondback moth (Plutella xylostella (Linnaeus)). The secondary metabolite produced by BBA_03671 and its associated gene cluster remains to be identified.,"The molecular function of this protein is not explicitly stated in the provided information. However, based on its name, it is likely to be involved in the process of viral replication, specifically in the assembly of viral particles. Proteins involved in viral replication often have molecular functions such as RNA binding, helicase activity, or nucleoside triphosphate hydrolase activity.",No,No,Vague,Vague,No,not-Yes,GO:0016874; GO:0031177,,,,,,,,,,,0,,0.3418,no
NRPSC_BEAB2,J4UPH3,Reference,Eukaryota,3920,Nonribosomal peptide synthetase that plays probably a role during infection of diamondback moth (Plutella xylostella (Linnaeus)). The secondary metabolite produced by BBA_03671 and its associated gene cluster remains to be identified.,Nonribosomal peptide synthetase that plays probably a role during infection of diamondback moth (Plutella xylostella (Linnaeus)). The secondary metabolite produced by BBA_03671 and its associated gene cluster remains to be identified.,,,,,,,GO:0016874; GO:0031177,GO:0016874,GO:0016874,GO:0016874,,GO:0016874,0.709,0.709,0.709,,0.709,4,0.709,0.3418,no
SIDL_BEAB2,J4VSL0,ESM2Text,Eukaryota,529,"Acyltransferase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. SIDL contributes to partial production of ferricrocin under iron-limiting conditions via the acetylation of N(5)- hydroxyornithine.",May be involved in the regulation of fatty acid synthesis.,Vague,Vague,No,Vague,No,not-Yes,GO:0016410,,,,,,,,,,,0,,0.4054,no
SIDL_BEAB2,J4VSL0,Prot2Text,Eukaryota,529,"Acyltransferase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. SIDL contributes to partial production of ferricrocin under iron-limiting conditions via the acetylation of N(5)- hydroxyornithine.","Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate tolerance, py",Maybe,Maybe,Vague,Maybe,Maybe,not-Yes,GO:0016410,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.4054,no
SIDL_BEAB2,J4VSL0,ProtT3,Eukaryota,529,"Acyltransferase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. SIDL contributes to partial production of ferricrocin under iron-limiting conditions via the acetylation of N(5)- hydroxyornithine.",N-alpha-acetyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-ger,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016410,GO:0004596,GO:0004596,GO:0004596,GO:0004596,GO:0004596,0.5913,0.5913,0.5913,0.5913,0.5913,5,0.5913,0.4054,no
SIDL_BEAB2,J4VSL0,ProtTale,Eukaryota,529,"Acyltransferase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. SIDL contributes to partial production of ferricrocin under iron-limiting conditions via the acetylation of N(5)- hydroxyornithine.",Involved in protein N-glycosylation.,No,No,No,No,No,not-Yes,GO:0016410,,,,,,,,,,,0,,0.4054,no
SIDL_BEAB2,J4VSL0,Protein2Text,Eukaryota,529,"Acyltransferase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. SIDL contributes to partial production of ferricrocin under iron-limiting conditions via the acetylation of N(5)- hydroxyornithine.","The molecular function of this protein is not specified in the provided text. However, based on the information given, it is likely that this protein is involved in a process related to gene expression or regulation, possibly as a part of a larger molecular complex. The fact that it is classified as a ""regulatory protein"" suggests that it may play a role in controlling or modulating the activity of other proteins or molecules.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016410,,,,,,,,,,,0,,0.4054,no
SIDL_BEAB2,J4VSL0,Reference,Eukaryota,529,"Acyltransferase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. SIDL contributes to partial production of ferricrocin under iron-limiting conditions via the acetylation of N(5)- hydroxyornithine.","Acyltransferase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. SIDL contributes to partial production of ferricrocin under iron-limiting conditions via the acetylation of N(5)- hydroxyornithine.",,,,,,,GO:0016410,GO:0016407,GO:0016746,GO:0016407,GO:0016747,GO:0016747,0.7289,0.729,0.7289,0.8582,0.8582,5,0.7806,0.4054,no
NPRSB_BEAB2,J4VWR6,ESM2Text,Eukaryota,4857,"Nonribosomal peptide synthetase that plays a probably a role during infection of diamondback moth (Plutella xylostella (Linnaeus)). The secondary metabolite produced by BBA_08222 and its associated gene cluster remains to be identified but the product of the BBA_08222 gene cluster should contain a polyketide-derivative followed by three amino acids, the last of which is right-handed owing to the presence of the epimerization (E) domain. Given this predicted synthetic process, BBA_08222 and its surrounding gene cluster are likely to be responsible for the biosynthesis of the known products, beauverolides, which are cyclodepsipeptides consisting of two L-amino acids, one D-amino acids, and one hydroxyl acid such as 3-hydroxy-4- methyloctanoic acid.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcs",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016874; GO:0031177,GO:0016874,GO:0016874,,,,0.709,0.709,,,,2,0.709,0.3208,no
NPRSB_BEAB2,J4VWR6,Prot2Text,Eukaryota,4857,"Nonribosomal peptide synthetase that plays a probably a role during infection of diamondback moth (Plutella xylostella (Linnaeus)). The secondary metabolite produced by BBA_08222 and its associated gene cluster remains to be identified but the product of the BBA_08222 gene cluster should contain a polyketide-derivative followed by three amino acids, the last of which is right-handed owing to the presence of the epimerization (E) domain. Given this predicted synthetic process, BBA_08222 and its surrounding gene cluster are likely to be responsible for the biosynthesis of the known products, beauverolides, which are cyclodepsipeptides consisting of two L-amino acids, one D-amino acids, and one hydroxyl acid such as 3-hydroxy-4- methyloctanoic acid.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and lcs",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016874; GO:0031177,GO:0016874,GO:0016874,GO:0016874,GO:0016874,GO:0016874,0.709,0.709,0.709,0.709,0.709,5,0.709,0.3208,no
NPRSB_BEAB2,J4VWR6,ProtT3,Eukaryota,4857,"Nonribosomal peptide synthetase that plays a probably a role during infection of diamondback moth (Plutella xylostella (Linnaeus)). The secondary metabolite produced by BBA_08222 and its associated gene cluster remains to be identified but the product of the BBA_08222 gene cluster should contain a polyketide-derivative followed by three amino acids, the last of which is right-handed owing to the presence of the epimerization (E) domain. Given this predicted synthetic process, BBA_08222 and its surrounding gene cluster are likely to be responsible for the biosynthesis of the known products, beauverolides, which are cyclodepsipeptides consisting of two L-amino acids, one D-amino acids, and one hydroxyl acid such as 3-hydroxy-4- methyloctanoic acid.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties . L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L- homoserine by",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016874; GO:0031177,GO:0016874; GO:0005524,GO:0016874,GO:0016874,GO:0016874; GO:0005524,GO:0016874,0.6793,0.709,0.709,0.6793,0.709,5,0.6971,0.3208,no
NPRSB_BEAB2,J4VWR6,ProtTale,Eukaryota,4857,"Nonribosomal peptide synthetase that plays a probably a role during infection of diamondback moth (Plutella xylostella (Linnaeus)). The secondary metabolite produced by BBA_08222 and its associated gene cluster remains to be identified but the product of the BBA_08222 gene cluster should contain a polyketide-derivative followed by three amino acids, the last of which is right-handed owing to the presence of the epimerization (E) domain. Given this predicted synthetic process, BBA_08222 and its surrounding gene cluster are likely to be responsible for the biosynthesis of the known products, beauverolides, which are cyclodepsipeptides consisting of two L-amino acids, one D-amino acids, and one hydroxyl acid such as 3-hydroxy-4- methyloctanoic acid.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS). SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms. These initial steps feature the priming of an unusual benzoic acid starter unit onto",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016874; GO:0031177,GO:0016874,GO:0016874,GO:0016874,GO:0016874; GO:0005524,GO:0016874,0.709,0.709,0.709,0.6793,0.709,5,0.7031,0.3208,no
NPRSB_BEAB2,J4VWR6,Protein2Text,Eukaryota,4857,"Nonribosomal peptide synthetase that plays a probably a role during infection of diamondback moth (Plutella xylostella (Linnaeus)). The secondary metabolite produced by BBA_08222 and its associated gene cluster remains to be identified but the product of the BBA_08222 gene cluster should contain a polyketide-derivative followed by three amino acids, the last of which is right-handed owing to the presence of the epimerization (E) domain. Given this predicted synthetic process, BBA_08222 and its surrounding gene cluster are likely to be responsible for the biosynthesis of the known products, beauverolides, which are cyclodepsipeptides consisting of two L-amino acids, one D-amino acids, and one hydroxyl acid such as 3-hydroxy-4- methyloctanoic acid.",The molecular function of this protein is to play a role in the replication of viral DNA.,No,No,Vague,No,No,not-Yes,GO:0016874; GO:0031177,,,,,,,,,,,0,,0.3208,no
NPRSB_BEAB2,J4VWR6,Reference,Eukaryota,4857,"Nonribosomal peptide synthetase that plays a probably a role during infection of diamondback moth (Plutella xylostella (Linnaeus)). The secondary metabolite produced by BBA_08222 and its associated gene cluster remains to be identified but the product of the BBA_08222 gene cluster should contain a polyketide-derivative followed by three amino acids, the last of which is right-handed owing to the presence of the epimerization (E) domain. Given this predicted synthetic process, BBA_08222 and its surrounding gene cluster are likely to be responsible for the biosynthesis of the known products, beauverolides, which are cyclodepsipeptides consisting of two L-amino acids, one D-amino acids, and one hydroxyl acid such as 3-hydroxy-4- methyloctanoic acid.","Nonribosomal peptide synthetase that plays a probably a role during infection of diamondback moth (Plutella xylostella (Linnaeus)). The secondary metabolite produced by BBA_08222 and its associated gene cluster remains to be identified but the product of the BBA_08222 gene cluster should contain a polyketide-derivative followed by three amino acids, the last of which is right-handed owing to the presence of the epimerization (E) domain. Given this predicted synthetic process, BBA_08222 and its surrounding gene cluster are likely to be responsible for the biosynthesis of the known products, beauverolides, which are cyclodepsipeptides consisting of two L-amino acids, one D-amino acids, and one hydroxyl acid such as 3-hydroxy-4- methyloctanoic acid.",,,,,,,GO:0016874; GO:0031177,GO:0016874,GO:0016874,GO:0016874,,GO:0016874,0.709,0.709,0.709,,0.709,4,0.709,0.3208,no
SIDF_BEAB2,J4W0D1,ESM2Text,Eukaryota,455,"Hydroxyornithine transacylase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. For biosynthesis of fusarinine C, the transacylase SIDF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by SIDI and sidH respectively.","Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0016410,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.2989,no
SIDF_BEAB2,J4W0D1,Prot2Text,Eukaryota,455,"Hydroxyornithine transacylase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. For biosynthesis of fusarinine C, the transacylase SIDF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by SIDI and sidH respectively.","Malonate synthase; part of the gene cluster that mediates the biosynthesis of iso-A82775C, a enylepoxycyclohexane and biosynthetic precursor of the chloropestolide anticancer natural products. Within the cluster, the prenyltransferase iacE prenylates siccayne to generate pestalodiol E, using dimethylallyl diphosphate (DMAPP) as cosubstrate. The probable oxidoreductase iacF is then involved in the epoxidation of pestalodiol F to pestalofone A, which is further converted to pestalofone A by the short-chain dehydrogenase/reductase iacG. Iso-A82775C is subsequently generated from pestalofone A by the short-chain dehydrogenase/reductase iacC. Iso-A82775C is further condensed with maldoxin via a Diels-Alder reaction to produce the anticancer natural products chloropestolides A to E (Probable).",No,No,No,No,No,not-Yes,GO:0016410,,,,,,,,,,,0,,0.2989,no
SIDF_BEAB2,J4W0D1,ProtT3,Eukaryota,455,"Hydroxyornithine transacylase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. For biosynthesis of fusarinine C, the transacylase SIDF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by SIDI and sidH respectively.",Acyl-CoA thioesterase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-,No,No,No,No,No,not-Yes,GO:0016410,GO:0047617,GO:0016289,GO:0016790,GO:0016790,GO:0016790,0.1926,0.2199,0.2353,0.2353,0.2353,5,0.2237,0.2989,no
SIDF_BEAB2,J4W0D1,ProtTale,Eukaryota,455,"Hydroxyornithine transacylase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. For biosynthesis of fusarinine C, the transacylase SIDF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by SIDI and sidH respectively.","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities. The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA. Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B. The",No,No,No,No,No,not-Yes,GO:0016410,GO:0016874,GO:0016874,GO:0016874,GO:0016874; GO:0005524,GO:0016874,0.3552,0.3552,0.3552,0.2553,0.3552,5,0.3352,0.2989,no
SIDF_BEAB2,J4W0D1,Protein2Text,Eukaryota,455,"Hydroxyornithine transacylase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. For biosynthesis of fusarinine C, the transacylase SIDF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by SIDI and sidH respectively.","The molecular function of this protein is not explicitly stated in the provided text. However, based on the name ""spermidine synthase-like protein"" and its involvement in the biosynthesis of spermidine, a polyamine involved in various cellular processes, it can be inferred that this protein likely catalyzes a reaction in the biosynthetic pathway of spermidine.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0016410,GO:0004766,GO:0004766,GO:0004766,GO:0004766,GO:0004766,0.3987,0.3987,0.3987,0.3987,0.3987,5,0.3987,0.2989,no
SIDF_BEAB2,J4W0D1,Reference,Eukaryota,455,"Hydroxyornithine transacylase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. For biosynthesis of fusarinine C, the transacylase SIDF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by SIDI and sidH respectively.","Hydroxyornithine transacylase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. For biosynthesis of fusarinine C, the transacylase SIDF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by SIDI and sidH respectively.",,,,,,,GO:0016410,GO:0016747,GO:0016746,GO:0016746,GO:0016747,GO:0016747,0.8582,0.729,0.729,0.8582,0.8582,5,0.8065,0.2989,no
SIDI_BEAB2,J5JLF2,ESM2Text,Eukaryota,576,"Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. For biosynthesis of fusarinine C, the transacylase SIDF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by SIDI and sidH respectively.",Involved in the degradation of plant cell walls. Catalyzes the ligation of CoA on butanoate to produce butyryl-CoA. It can also use hexanoate and CoA but with a lower activity.,Maybe,Maybe,Maybe,Yes,Maybe,not-Yes,GO:0005524; GO:0031956,GO:0016405,GO:0016878,GO:0016878,GO:0016874,GO:0016878,0.4347,0.4253,0.4253,0.3206,0.4253,5,0.4062,0.2653,no
SIDI_BEAB2,J5JLF2,Prot2Text,Eukaryota,576,"Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. For biosynthesis of fusarinine C, the transacylase SIDF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by SIDI and sidH respectively.",May act as an acid--thiol ligase that activates carboxylic acids by forming acyl-CoAs.,Maybe,Maybe,Maybe,Yes,Maybe,not-Yes,GO:0005524; GO:0031956,GO:0016877,GO:0016405,GO:0016877,GO:0016878,GO:0016878,0.3772,0.4347,0.3772,0.4253,0.4253,5,0.4079,0.2653,no
SIDI_BEAB2,J5JLF2,ProtT3,Eukaryota,576,"Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. For biosynthesis of fusarinine C, the transacylase SIDF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by SIDI and sidH respectively.","Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Yes,Yes,Maybe,Yes,Yes,Yes,GO:0005524; GO:0031956,GO:0016405,GO:0003996,GO:0003996; GO:0005524,GO:0003996,GO:0003996,0.4347,0.5688,0.9132,0.5688,0.5688,5,0.6109,0.2653,no
SIDI_BEAB2,J5JLF2,ProtTale,Eukaryota,576,"Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. For biosynthesis of fusarinine C, the transacylase SIDF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by SIDI and sidH respectively.","Acyl-CoA synthetases catalyze the initial reaction in the de novo biosynthesis of fatty acids from acetyl-CoA. This protein catalyzes the ATP-dependent formation of (9Z,12Z,15Z)-octadecatrienoate ((9Z,12Z,15Z)-9,12,15-octadecatrienoyl-CoA) from acetyl-CoA and malonyl-CoA.",No,No,No,No,No,not-Yes,GO:0005524; GO:0031956,GO:0004312,GO:0003996,GO:0004467,GO:0004467,GO:0004467; GO:0005524,0.1225,0.5688,0.5688,0.5688,0.9132,5,0.5484,0.2653,no
SIDI_BEAB2,J5JLF2,Protein2Text,Eukaryota,576,"Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. For biosynthesis of fusarinine C, the transacylase SIDF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by SIDI and sidH respectively.","This protein is a carboxylate--CoA ligase, which means it catalyzes the formation of CoA thioesters from carboxylates. More specifically, it is involved in the activation of a carboxylic acid for fatty acid metabolism. 
In detail, it catalyzes the ATP-dependent activation of medium- and long-chain fatty acids as acyl-CoA thioesters, which are essential for their subsequent entry into the beta-oxidation pathway. It may also play a role in the synthesis of fatty acid conjugates of xenobiotics. It exhibits a broad specificity for fatty acids, with a preference for fatty acids with 6-18 carbon atoms. It can also activate branched fatty acids and dicarboxylic acids.
It is also able to catalyze the formation of thioester bonds between carboxylic acids and 4'-phosphopantetheine, the cofactor of CoA. This suggests that it may also play a role in the synthesis of 4'-phosphopantetheine. 
It also has a CoA transferase activity, which allows it to transfer the CoA moiety from CoA to a carboxylic acid. This activity is probably involved in the activation of fatty acids for beta-oxidation.
It also exhibits a very weak acyl-CoA thioesterase activity, which allows it to hydrolyze the thioester bond of fatty acyl-CoA. This activity may play a role in the degradation of fatty acyl-CoA.
It also exhibits a weak fatty acid-binding activity, which allows it to bind fatty acids. This activity may play a role in the regulation of fatty acid metabolism.
It also exhibits a weak phosphatase activity, which allows it to hydrolyze the phosphate group of 4'- phosphopantetheine. This activity may play a role in the degradation of 4'-phosphopantetheine.
It also exhibits a weak CoA-binding activity, which allows it to bind CoA. This activity may play a role in the regulation of CoA metabolism.
It also exhibits a weak CoA-transferase activity, which allows it to transfer the CoA moiety from CoA to a carboxylic acid. This activity may play a role in the activation of fatty acids for beta-oxidation.
It also exhibits a weak CoA synthetase activity, which allows it to transfer the CoA moiety from CoA to a carbox",Maybe,Maybe,Maybe,Yes,Yes,not-Yes,GO:0005524; GO:0031956,GO:0004467,GO:0004467,GO:0003996; GO:0004467,GO:0004467,GO:0004467,0.5688,0.5688,0.6332,0.5688,0.5688,5,0.5817,0.2653,no
SIDI_BEAB2,J5JLF2,Reference,Eukaryota,576,"Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. For biosynthesis of fusarinine C, the transacylase SIDF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by SIDI and sidH respectively.","Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of at least 11 siderophores, including beauverichelin A, dimerumic acid (DA), Na-dimethyl coprogen (NADC), eleutherazine B, ferricrocin (FC), fusarinine A, fusarinine C (FsC), metachelin A, mevalonolactone, rhodotorulic acid (RA) and tenellin. This cocktail of siderophores for iron metabolism is essential for virulence, and more specifically for the fungal virulence in penetrating through the host cuticle. Siderophore synthesis is also involved in conidial germination under iron-deficient conditions. For biosynthesis of fusarinine C, the transacylase SIDF transfers anhydromevalonyl to N(5)-hydroxyornithine. The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by SIDI and sidH respectively.",,,,,,,GO:0005524; GO:0031956,GO:0016877,GO:0016878,GO:0016874,GO:0016878,GO:0016878,0.3772,0.4253,0.3206,0.4253,0.4253,5,0.3947,0.2653,no
PQP1_CRYN9,J9VDC2,ESM2Text,Eukaryota,951,Extracellular protease that cleaves the quorum sensing peptide QSP1 precursor to produce the 11 amino acid mature QSP1 peptide.,"Serine protease which, with sphingomyelinase (sphingomyelinase) and kininogen-like protein (kinin), is involved in pathogenicity.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004252,GO:0008236,GO:0008236,GO:0008236,GO:0008236,GO:0008236,0.8276,0.8276,0.8276,0.8276,0.8276,5,0.8276,0.3052,no
PQP1_CRYN9,J9VDC2,Prot2Text,Eukaryota,951,Extracellular protease that cleaves the quorum sensing peptide QSP1 precursor to produce the 11 amino acid mature QSP1 peptide.,Serine protease with a fibrinolytic activity.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004252,GO:0008236,GO:0008236,GO:0008236,GO:0008236,GO:0008236,0.8276,0.8276,0.8276,0.8276,0.8276,5,0.8276,0.3052,no
PQP1_CRYN9,J9VDC2,ProtT3,Eukaryota,951,Extracellular protease that cleaves the quorum sensing peptide QSP1 precursor to produce the 11 amino acid mature QSP1 peptide.,Secreted. Belongs to the peptidase S8 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004252,GO:0004252,GO:0004252,,GO:0004252,GO:0004252,1.0,1.0,,1.0,1.0,4,1.0,0.3052,no
PQP1_CRYN9,J9VDC2,ProtTale,Eukaryota,951,Extracellular protease that cleaves the quorum sensing peptide QSP1 precursor to produce the 11 amino acid mature QSP1 peptide.,Serine protease which is essential for cell wall integrity and hyphal growth.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004252,GO:0004252,GO:0004252,GO:0004252,GO:0004252,GO:0004252,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3052,no
PQP1_CRYN9,J9VDC2,Protein2Text,Eukaryota,951,Extracellular protease that cleaves the quorum sensing peptide QSP1 precursor to produce the 11 amino acid mature QSP1 peptide.,This protein is involved in the molecular function of proteolysis.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004252,GO:0008233,GO:0008233,GO:0008233,GO:0008233,GO:0008233,0.6551,0.6551,0.6551,0.6551,0.6551,5,0.6551,0.3052,no
PQP1_CRYN9,J9VDC2,Reference,Eukaryota,951,Extracellular protease that cleaves the quorum sensing peptide QSP1 precursor to produce the 11 amino acid mature QSP1 peptide.,Extracellular protease that cleaves the quorum sensing peptide QSP1 precursor to produce the 11 amino acid mature QSP1 peptide.,,,,,,,GO:0004252,GO:0008233,GO:0008233,GO:0008233,GO:0008233,GO:0008233,0.6551,0.6551,0.6551,0.6551,0.6551,5,0.6551,0.3052,no
THRC_CRYN9,J9VI85,ESM2Text,Eukaryota,547,Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine.,Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0030170; GO:0004795,GO:0004795,GO:0004795,GO:0004795,GO:0004795,GO:0004795,0.6898,0.6898,0.6898,0.6898,0.6898,5,0.6898,0.5272,no
THRC_CRYN9,J9VI85,Prot2Text,Eukaryota,547,Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine.,Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0030170; GO:0004795,GO:0004795,GO:0004795,GO:0004795,GO:0004795,GO:0004795,0.6898,0.6898,0.6898,0.6898,0.6898,5,0.6898,0.5272,no
THRC_CRYN9,J9VI85,ProtT3,Eukaryota,547,Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine.,Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. Belongs to the threonine synthase family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0030170; GO:0004795,GO:0004795; GO:0030170,GO:0004795,GO:0004795,GO:0004795,GO:0004795,1.0,0.6898,0.6898,0.6898,0.6898,5,0.7518,0.5272,no
THRC_CRYN9,J9VI85,ProtTale,Eukaryota,547,Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine.,"Catalyzes the transfer of a gamma-phospho group from ATP to L-cysteine to produce L-cysteine-4-phosphate (L-Cys-4-P). This is the first step in the synthesis of 4- phosphopantothenate, a precursor for coenzyme V.",No,No,No,No,No,not-Yes,GO:0030170; GO:0004795,GO:0016301; GO:0005524,GO:0016301; GO:0005524,GO:0016301,GO:0016301; GO:0005524,GO:0016301; GO:0005524,0.331,0.331,0.1838,0.331,0.331,5,0.3016,0.5272,no
THRC_CRYN9,J9VI85,Protein2Text,Eukaryota,547,Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine.,"The molecular function of this protein is involved in the biosynthesis of amino acids. More specifically, it is a phosphoribosylpyrophosphate (PRPP) synthase, which catalyzes the formation of PRPP from ribose-5-phosphate and ATP. PRPP is an important intermediate in the biosynthesis of purine and pyrimidine nucleotides.",No,No,No,No,No,not-Yes,GO:0030170; GO:0004795,GO:0004749,GO:0004749,GO:0004749,GO:0004749,GO:0004749,0.1563,0.1563,0.1563,0.1563,0.1563,5,0.1563,0.5272,no
THRC_CRYN9,J9VI85,Reference,Eukaryota,547,Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine.,Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine.,,,,,,,GO:0030170; GO:0004795,GO:0004795,GO:0004795,GO:0004795,GO:0004795,GO:0004795,0.6898,0.6898,0.6898,0.6898,0.6898,5,0.6898,0.5272,no
GYS_CRYN9,J9VTK7,ESM2Text,Eukaryota,733,"Glycogen synthase participates in the glycogen biosynthetic process along with glycogenin and glycogen branching enzyme. Extends the primer composed of a few glucose units formed by glycogenin by adding new glucose units to it. In this context, glycogen synthase transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.","Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan. Is believed to regulate the synthesis of glycogen.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004373,GO:0004373,GO:0004373,GO:0004373,GO:0004373,GO:0004373,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5083,no
GYS_CRYN9,J9VTK7,Prot2Text,Eukaryota,733,"Glycogen synthase participates in the glycogen biosynthetic process along with glycogenin and glycogen branching enzyme. Extends the primer composed of a few glucose units formed by glycogenin by adding new glucose units to it. In this context, glycogen synthase transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.","Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan. Is believed to regulate the synthesis of glycogen.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004373,GO:0004373,GO:0004373,GO:0004373,GO:0004373,GO:0004373,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5083,no
GYS_CRYN9,J9VTK7,ProtT3,Eukaryota,733,"Glycogen synthase participates in the glycogen biosynthetic process along with glycogenin and glycogen branching enzyme. Extends the primer composed of a few glucose units formed by glycogenin by adding new glucose units to it. In this context, glycogen synthase transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.","Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan. Belongs to the glycosyltransferase 3 family",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004373,GO:0016757,GO:0004373,GO:0035251,GO:0016758,GO:0016757,0.504,1.0,0.8368,0.5812,0.504,5,0.6852,0.5083,no
GYS_CRYN9,J9VTK7,ProtTale,Eukaryota,733,"Glycogen synthase participates in the glycogen biosynthetic process along with glycogenin and glycogen branching enzyme. Extends the primer composed of a few glucose units formed by glycogenin by adding new glucose units to it. In this context, glycogen synthase transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.","Catalytic subunit of trehalose synthase, which catalyzes the synthesis of trehalose from UDP-glucose and glucose 1-phosphate.",No,No,No,No,No,not-Yes,GO:0004373,GO:0003825,GO:0003825; GO:0016757,GO:0016757,GO:0003825,GO:0003825,0.7456,0.6651,0.504,0.7456,0.7456,5,0.6812,0.5083,no
GYS_CRYN9,J9VTK7,Protein2Text,Eukaryota,733,"Glycogen synthase participates in the glycogen biosynthetic process along with glycogenin and glycogen branching enzyme. Extends the primer composed of a few glucose units formed by glycogenin by adding new glucose units to it. In this context, glycogen synthase transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.","This protein is a transferase that catalyzes the transfer of a glucose molecule from UDP-glucose to a acceptor molecule, such as glycogen, starch, or other carbohydrates, in a process known as glycogen synthesis.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004373,GO:0004373,GO:0004373,GO:0004373,GO:0004373,GO:0004373,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5083,no
GYS_CRYN9,J9VTK7,Reference,Eukaryota,733,"Glycogen synthase participates in the glycogen biosynthetic process along with glycogenin and glycogen branching enzyme. Extends the primer composed of a few glucose units formed by glycogenin by adding new glucose units to it. In this context, glycogen synthase transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.","Glycogen synthase participates in the glycogen biosynthetic process along with glycogenin and glycogen branching enzyme. Extends the primer composed of a few glucose units formed by glycogenin by adding new glucose units to it. In this context, glycogen synthase transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.",,,,,,,GO:0004373,GO:0004373,GO:0004373,GO:0004373,GO:0004373,GO:0004373,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5083,no
KHSE_CRYN9,J9VU26,ESM2Text,Eukaryota,357,Commits homoserine to the threonine biosynthesis pathway by catalyzing its O-phosphorylation.,Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0004413,GO:0004413; GO:0005524,GO:0004413,GO:0004413,GO:0004413,GO:0004413,1.0,0.6834,0.6834,0.6834,0.6834,5,0.7467,0.2288,no
KHSE_CRYN9,J9VU26,Prot2Text,Eukaryota,357,Commits homoserine to the threonine biosynthesis pathway by catalyzing its O-phosphorylation.,Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0004413,GO:0004413,GO:0004413,GO:0004413,GO:0004413,GO:0004413,0.6834,0.6834,0.6834,0.6834,0.6834,5,0.6834,0.2288,no
KHSE_CRYN9,J9VU26,ProtT3,Eukaryota,357,Commits homoserine to the threonine biosynthesis pathway by catalyzing its O-phosphorylation.,Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. Cytoplasm. Belongs to the GHMP kinase family. Homoserine kinase subfamily,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0004413,GO:0004413; GO:0005524,GO:0004413,GO:0004413; GO:0005524,GO:0004413; GO:0005524,GO:0004413; GO:0005524,1.0,0.6834,1.0,1.0,1.0,5,0.9367,0.2288,no
KHSE_CRYN9,J9VU26,ProtTale,Eukaryota,357,Commits homoserine to the threonine biosynthesis pathway by catalyzing its O-phosphorylation.,Catalyzes the phosphorylation of N-acetyl-beta-alanine to N-acetyl-beta-alanine phosphate.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004413,GO:0016301,GO:0016301,GO:0016301,GO:0016301,GO:0016301,0.4836,0.4836,0.4836,0.4836,0.4836,5,0.4836,0.2288,no
KHSE_CRYN9,J9VU26,Protein2Text,Eukaryota,357,Commits homoserine to the threonine biosynthesis pathway by catalyzing its O-phosphorylation.,"The molecular function of this protein is enzyme activity. Specifically, it is a dehydrogenase, which is an enzyme that catalyzes the removal of hydrogen atoms from a substrate.",No,No,No,No,No,not-Yes,GO:0005524; GO:0004413,GO:0016491,GO:0016491,,GO:0016491,GO:0016491,0.2209,0.2209,,0.2209,0.2209,4,0.2209,0.2288,no
KHSE_CRYN9,J9VU26,Reference,Eukaryota,357,Commits homoserine to the threonine biosynthesis pathway by catalyzing its O-phosphorylation.,Commits homoserine to the threonine biosynthesis pathway by catalyzing its O-phosphorylation.,,,,,,,GO:0005524; GO:0004413,GO:0004413,GO:0004413; GO:0005524,GO:0004413; GO:0005524,GO:0004413,GO:0004413,0.6834,1.0,1.0,0.6834,0.6834,5,0.81,0.2288,no
ARGM_STREL,M1T1K4,ESM2Text,Bacteria,369,"Aminotransferase involved in the formation of the rare amino acid 3-methylarginine (MeArg), which is incorporated into the peptidyl nucleoside antibiotic arginomycin. Catalyzes two rounds of transamination: the transfer of the amino group from L- arginine to 2-oxoglutarate to give glutamate and 5-guanidino-2- oxopentanoic acid, which will be methylated by ArgN. Then, ArgM specifically catalyzes transamination from the donor L- aspartate to the 5-guanidino-3-methyl-2-oxopentanoic acid produced by ArgN, generating the final product, 3-methylarginine. Cannot use arginine analogs, such as D-arginine, L-homoarginine and N- methylarginine for the first transamination.","Involved in the biosynthesis of alanine. Catalyzes the transamination of pyruvate by glutamate, leading to the formation of L-alanine and 2-oxoglutarate. Is also able to catalyze the reverse reaction.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0030170; GO:0008483,GO:0004021,GO:0008483,GO:0004021,GO:0004021,GO:0008483,0.5228,0.6936,0.5228,0.5228,0.6936,5,0.5911,0.1505,no
ARGM_STREL,M1T1K4,Prot2Text,Bacteria,369,"Aminotransferase involved in the formation of the rare amino acid 3-methylarginine (MeArg), which is incorporated into the peptidyl nucleoside antibiotic arginomycin. Catalyzes two rounds of transamination: the transfer of the amino group from L- arginine to 2-oxoglutarate to give glutamate and 5-guanidino-2- oxopentanoic acid, which will be methylated by ArgN. Then, ArgM specifically catalyzes transamination from the donor L- aspartate to the 5-guanidino-3-methyl-2-oxopentanoic acid produced by ArgN, generating the final product, 3-methylarginine. Cannot use arginine analogs, such as D-arginine, L-homoarginine and N- methylarginine for the first transamination.",Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0030170; GO:0008483,GO:0008483,GO:0004838,GO:0004838,GO:0004838,GO:0004838,0.6936,0.5228,0.5228,0.5228,0.5228,5,0.557,0.1505,no
ARGM_STREL,M1T1K4,ProtT3,Bacteria,369,"Aminotransferase involved in the formation of the rare amino acid 3-methylarginine (MeArg), which is incorporated into the peptidyl nucleoside antibiotic arginomycin. Catalyzes two rounds of transamination: the transfer of the amino group from L- arginine to 2-oxoglutarate to give glutamate and 5-guanidino-2- oxopentanoic acid, which will be methylated by ArgN. Then, ArgM specifically catalyzes transamination from the donor L- aspartate to the 5-guanidino-3-methyl-2-oxopentanoic acid produced by ArgN, generating the final product, 3-methylarginine. Cannot use arginine analogs, such as D-arginine, L-homoarginine and N- methylarginine for the first transamination.",Catalyzes the conversion of 4-amino-4-deoxychorismate (ADC) to 4-amino-4-deoxychorismate-6-phosphate (ADC-6-P). Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family,Vague,Maybe,No,No,No,not-Yes,GO:0030170; GO:0008483,GO:0008483; GO:0030170,GO:0008483,GO:0008483,GO:0008483; GO:0030170,GO:0008483; GO:0030170,1.0,0.6936,0.6936,1.0,1.0,5,0.8774,0.1505,no
ARGM_STREL,M1T1K4,ProtTale,Bacteria,369,"Aminotransferase involved in the formation of the rare amino acid 3-methylarginine (MeArg), which is incorporated into the peptidyl nucleoside antibiotic arginomycin. Catalyzes two rounds of transamination: the transfer of the amino group from L- arginine to 2-oxoglutarate to give glutamate and 5-guanidino-2- oxopentanoic acid, which will be methylated by ArgN. Then, ArgM specifically catalyzes transamination from the donor L- aspartate to the 5-guanidino-3-methyl-2-oxopentanoic acid produced by ArgN, generating the final product, 3-methylarginine. Cannot use arginine analogs, such as D-arginine, L-homoarginine and N- methylarginine for the first transamination.","Involved in the biosynthesis of 2-amino-4-methoxy-6-nitro-7,8-dihydro-8-oxononanoate (ANM), a substrate required for the synthesis of the bacterial coenzyme A. Catalyzes the conversion of 4-carboxy-2-hydroxymuconate-6-semialdehyde (CHMS) to 2-amino-4-methoxy-6-nitro-7,8-dihydro-8-oxononanoate (ANM) and of 4-carboxy-2- hydroxymuconate-6-phosphate (",No,No,Vague,No,Maybe,not-Yes,GO:0030170; GO:0008483,,,,,,,,,,,0,,0.1505,no
ARGM_STREL,M1T1K4,Protein2Text,Bacteria,369,"Aminotransferase involved in the formation of the rare amino acid 3-methylarginine (MeArg), which is incorporated into the peptidyl nucleoside antibiotic arginomycin. Catalyzes two rounds of transamination: the transfer of the amino group from L- arginine to 2-oxoglutarate to give glutamate and 5-guanidino-2- oxopentanoic acid, which will be methylated by ArgN. Then, ArgM specifically catalyzes transamination from the donor L- aspartate to the 5-guanidino-3-methyl-2-oxopentanoic acid produced by ArgN, generating the final product, 3-methylarginine. Cannot use arginine analogs, such as D-arginine, L-homoarginine and N- methylarginine for the first transamination.","The molecular function of this protein is not explicitly stated in the provided text. However, based on the name and the context, it is likely that this protein is involved in amino acid metabolism, specifically in the transfer of aminogroups from one molecule to another. More specifically, it may be aminotransferase, an enzyme that catalyzes the transfer of an amino group from a donor molecule to an acceptor molecule.",Vague,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0030170; GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.6936,0.6936,0.6936,0.6936,0.6936,5,0.6936,0.1505,no
ARGM_STREL,M1T1K4,Reference,Bacteria,369,"Aminotransferase involved in the formation of the rare amino acid 3-methylarginine (MeArg), which is incorporated into the peptidyl nucleoside antibiotic arginomycin. Catalyzes two rounds of transamination: the transfer of the amino group from L- arginine to 2-oxoglutarate to give glutamate and 5-guanidino-2- oxopentanoic acid, which will be methylated by ArgN. Then, ArgM specifically catalyzes transamination from the donor L- aspartate to the 5-guanidino-3-methyl-2-oxopentanoic acid produced by ArgN, generating the final product, 3-methylarginine. Cannot use arginine analogs, such as D-arginine, L-homoarginine and N- methylarginine for the first transamination.","Aminotransferase involved in the formation of the rare amino acid 3-methylarginine (MeArg), which is incorporated into the peptidyl nucleoside antibiotic arginomycin. Catalyzes two rounds of transamination: the transfer of the amino group from L- arginine to 2-oxoglutarate to give glutamate and 5-guanidino-2- oxopentanoic acid, which will be methylated by ArgN. Then, ArgM specifically catalyzes transamination from the donor L- aspartate to the 5-guanidino-3-methyl-2-oxopentanoic acid produced by ArgN, generating the final product, 3-methylarginine. Cannot use arginine analogs, such as D-arginine, L-homoarginine and N- methylarginine for the first transamination.",,,,,,,GO:0030170; GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.6936,0.6936,0.6936,0.6936,0.6936,5,0.6936,0.1505,no
GLPQ2_MYCTU,O07244,ESM2Text,Bacteria,264,Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol.,Glycerophosphoryl diester phosphodiesterase hydrolyzes deacylated phospholipids to G3P.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008889; GO:0046872,GO:0008441,GO:0008889,GO:0008441,GO:0008441,GO:0008441,0.3411,0.6924,0.3411,0.3411,0.3411,5,0.4114,0.3363,no
GLPQ2_MYCTU,O07244,Prot2Text,Bacteria,264,Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol.,Glycerophosphoryl diester phosphodiesterase hydrolyzes deacylated phospholipids to G3P and the corresponding alcohols.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008889; GO:0046872,GO:0008970,GO:0008889,GO:0047714,GO:0008889,GO:0008889,0.2343,0.6924,0.2953,0.6924,0.6924,5,0.5214,0.3363,no
GLPQ2_MYCTU,O07244,ProtT3,Bacteria,264,Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol.,Cytoplasm. Belongs to the glycerophosphoryl diester phosphodiesterase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008889; GO:0046872,GO:0008889,GO:0008441,GO:0008889,GO:0008441,GO:0008889,0.6924,0.3411,0.6924,0.3411,0.6924,5,0.5519,0.3363,no
GLPQ2_MYCTU,O07244,ProtTale,Bacteria,264,Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol.,Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008889; GO:0046872,GO:0008889,GO:0008889,GO:0008889,GO:0008889,GO:0008889,0.6924,0.6924,0.6924,0.6924,0.6924,5,0.6924,0.3363,no
GLPQ2_MYCTU,O07244,Protein2Text,Bacteria,264,Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol.,"The molecular function of this protein is an esterase, which is an enzyme that catalyzes the hydrolysis of esters. More specifically, it is a phospholipase C that catalyzes the hydrolysis of phosphatidylcholine to choline and diacylglycerol. This protein is involved in the hydrolysis of phospholipids, which is a key step in the metabolism of phospholipids in the cell. It is also involved in the regulation of various cellular processes, including signal transduction and cell growth.",No,No,No,No,No,not-Yes,GO:0008889; GO:0046872,GO:0004629,GO:0004506,GO:0004630,GO:0004629,GO:0004629,0.4198,0.1341,0.4198,0.4198,0.4198,5,0.3627,0.3363,no
GLPQ2_MYCTU,O07244,Reference,Bacteria,264,Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol.,Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol.,,,,,,,GO:0008889; GO:0046872,GO:0008889,GO:0008441,GO:0008889,GO:0008889,GO:0008889,0.6924,0.3411,0.6924,0.6924,0.6924,5,0.6221,0.3363,no
CARK9_ARATH,O49338,ESM2Text,Eukaryota,338,"Receptor-like cytoplasmic kinase (RLCK) that triggers abscisic acid (ABA) signaling in response to dehydration by phosphorylating and activating ABA receptors to support their monomerization and enhance their ABA binding affinity; they in turn repress PP2C protein phosphatases acting as negative regulators of ABA responses. Negative regulator of the reactive oxygen stress (ROS) signaling mediated by the kinase OXI1 in response to pathogen-associated molecular patterns (PAMPs, e.g. flagellin), and associated with specific genes expression (Probable).",Protein kinase involved in the Tl receptor signaling pathway and a-factor-dependent mating regulation.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004715; GO:0019901; GO:0004674,GO:0004672; GO:0005524,GO:0004672,GO:0004672,GO:0004672,GO:0004672,0.7977,0.5622,0.5622,0.5622,0.5622,5,0.6093,0.4621,no
CARK9_ARATH,O49338,Prot2Text,Eukaryota,338,"Receptor-like cytoplasmic kinase (RLCK) that triggers abscisic acid (ABA) signaling in response to dehydration by phosphorylating and activating ABA receptors to support their monomerization and enhance their ABA binding affinity; they in turn repress PP2C protein phosphatases acting as negative regulators of ABA responses. Negative regulator of the reactive oxygen stress (ROS) signaling mediated by the kinase OXI1 in response to pathogen-associated molecular patterns (PAMPs, e.g. flagellin), and associated with specific genes expression (Probable).","Serine/threonine-protein kinase involved in resistance against the herbivorous insect brown planthopper (N.lugens, BPH). Member of the BPH3 (BPH resistance locus 3) cluster which contains LECRK1, LECRK2 and LECRK3.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0004715; GO:0019901; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.5759,0.5759,0.5759,0.5759,0.5759,5,0.5759,0.4621,no
CARK9_ARATH,O49338,ProtT3,Eukaryota,338,"Receptor-like cytoplasmic kinase (RLCK) that triggers abscisic acid (ABA) signaling in response to dehydration by phosphorylating and activating ABA receptors to support their monomerization and enhance their ABA binding affinity; they in turn repress PP2C protein phosphatases acting as negative regulators of ABA responses. Negative regulator of the reactive oxygen stress (ROS) signaling mediated by the kinase OXI1 in response to pathogen-associated molecular patterns (PAMPs, e.g. flagellin), and associated with specific genes expression (Probable).",Belongs to the protein kinase superfamily. Ser/Thr protein kinase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0004715; GO:0019901; GO:0004674,GO:0004674; GO:0005524,GO:0004674,GO:0004674,GO:0004674,GO:0004674; GO:0005524,0.8118,0.5759,0.5759,0.5759,0.8118,5,0.6703,0.4621,no
CARK9_ARATH,O49338,ProtTale,Eukaryota,338,"Receptor-like cytoplasmic kinase (RLCK) that triggers abscisic acid (ABA) signaling in response to dehydration by phosphorylating and activating ABA receptors to support their monomerization and enhance their ABA binding affinity; they in turn repress PP2C protein phosphatases acting as negative regulators of ABA responses. Negative regulator of the reactive oxygen stress (ROS) signaling mediated by the kinase OXI1 in response to pathogen-associated molecular patterns (PAMPs, e.g. flagellin), and associated with specific genes expression (Probable).",May play a role in plant defense signaling.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0004715; GO:0019901; GO:0004674,,,,,,,,,,,0,,0.4621,no
CARK9_ARATH,O49338,Protein2Text,Eukaryota,338,"Receptor-like cytoplasmic kinase (RLCK) that triggers abscisic acid (ABA) signaling in response to dehydration by phosphorylating and activating ABA receptors to support their monomerization and enhance their ABA binding affinity; they in turn repress PP2C protein phosphatases acting as negative regulators of ABA responses. Negative regulator of the reactive oxygen stress (ROS) signaling mediated by the kinase OXI1 in response to pathogen-associated molecular patterns (PAMPs, e.g. flagellin), and associated with specific genes expression (Probable).","The molecular function of this protein is associated with signal transduction. It belongs to the serine/threonine-protein kinase family, which is involved in the transmission of signals from the cell surface to the interior of the cell. This protein is specifically involved in the activation of downstream signaling pathways, which are crucial for various cellular processes such as growth, development, and stress responses.",Vague,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0005524; GO:0004715; GO:0019901; GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.5759,0.5759,0.5759,0.5759,0.5759,5,0.5759,0.4621,no
CARK9_ARATH,O49338,Reference,Eukaryota,338,"Receptor-like cytoplasmic kinase (RLCK) that triggers abscisic acid (ABA) signaling in response to dehydration by phosphorylating and activating ABA receptors to support their monomerization and enhance their ABA binding affinity; they in turn repress PP2C protein phosphatases acting as negative regulators of ABA responses. Negative regulator of the reactive oxygen stress (ROS) signaling mediated by the kinase OXI1 in response to pathogen-associated molecular patterns (PAMPs, e.g. flagellin), and associated with specific genes expression (Probable).","Receptor-like cytoplasmic kinase (RLCK) that triggers abscisic acid (ABA) signaling in response to dehydration by phosphorylating and activating ABA receptors to support their monomerization and enhance their ABA binding affinity; they in turn repress PP2C protein phosphatases acting as negative regulators of ABA responses. Negative regulator of the reactive oxygen stress (ROS) signaling mediated by the kinase OXI1 in response to pathogen-associated molecular patterns (PAMPs, e.g. flagellin), and associated with specific genes expression (Probable).",,,,,,,GO:0005524; GO:0004715; GO:0019901; GO:0004674,GO:0004674,GO:0004674; GO:0005524,GO:0004674; GO:0005524,GO:0004674,GO:0004674; GO:0005524,0.5759,0.8118,0.8118,0.5759,0.8118,5,0.7174,0.4621,no
CGALT_BORBU,O51519,ESM2Text,Bacteria,358,"Galactosyltransferase involved in the synthesis of cholesterol glycolipids, which are formed by the use of host-derived cholesterol and have been shown to be immunogenic, and possibly contribute to Lyme disease pathogenesis. Catalyzes the formation of cholesteryl beta-D-galactopyranoside (CGal) from cholesterol and UDP-alpha-D-galactose. Cannot use GDP-mannose.","Glycosyltransferase required for the synthesis of succinoglycan (EPS I). Needed for the addition of the fifth sugar (glucose), catalyzes the formation of a beta-1,3 linkage between the third acetylated sugar and the fourth sugar.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016758,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.8416,0.8416,0.8416,0.8416,0.8416,5,0.8416,0.3234,no
CGALT_BORBU,O51519,Prot2Text,Bacteria,358,"Galactosyltransferase involved in the synthesis of cholesterol glycolipids, which are formed by the use of host-derived cholesterol and have been shown to be immunogenic, and possibly contribute to Lyme disease pathogenesis. Catalyzes the formation of cholesteryl beta-D-galactopyranoside (CGal) from cholesterol and UDP-alpha-D-galactose. Cannot use GDP-mannose.","Glycosyltransferase required for the synthesis of succinoglycan (EPS I). Needed for the addition of the seventh sugar (glucose), catalyzes the formation of a beta-1,6 linkage between the seventh and eighth sugar.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016758,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.8416,0.8416,0.8416,0.8416,0.8416,5,0.8416,0.3234,no
CGALT_BORBU,O51519,ProtT3,Bacteria,358,"Galactosyltransferase involved in the synthesis of cholesterol glycolipids, which are formed by the use of host-derived cholesterol and have been shown to be immunogenic, and possibly contribute to Lyme disease pathogenesis. Catalyzes the formation of cholesteryl beta-D-galactopyranoside (CGal) from cholesterol and UDP-alpha-D-galactose. Cannot use GDP-mannose.",Belongs to the glycosyltransferase 2 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016758,GO:0016757,GO:0016757,,GO:0016757,GO:0016757,0.8416,0.8416,,0.8416,0.8416,4,0.8416,0.3234,no
CGALT_BORBU,O51519,ProtTale,Bacteria,358,"Galactosyltransferase involved in the synthesis of cholesterol glycolipids, which are formed by the use of host-derived cholesterol and have been shown to be immunogenic, and possibly contribute to Lyme disease pathogenesis. Catalyzes the formation of cholesteryl beta-D-galactopyranoside (CGal) from cholesterol and UDP-alpha-D-galactose. Cannot use GDP-mannose.",Catalyzes the addition of a GlcNAc moiety from UDP-GlcNAc to the lipid carrier undecaprenyl phosphate (C55-P) to form undecaprenyl-N-GlcNAc (C59-N-GlcNAc). Involved in the synthesis of the repeating unit of the lipopolysaccharide (LPS).,No,No,No,No,Maybe,not-Yes,GO:0016758,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.8416,0.8416,0.8416,0.8416,0.8416,5,0.8416,0.3234,no
CGALT_BORBU,O51519,Protein2Text,Bacteria,358,"Galactosyltransferase involved in the synthesis of cholesterol glycolipids, which are formed by the use of host-derived cholesterol and have been shown to be immunogenic, and possibly contribute to Lyme disease pathogenesis. Catalyzes the formation of cholesteryl beta-D-galactopyranoside (CGal) from cholesterol and UDP-alpha-D-galactose. Cannot use GDP-mannose.","This protein is a transferase, specifically a sugar transferase, which catalyzes the transfer of a sugar molecule from one molecule to another. More specifically, it is involved in the synthesis of a sugar nucleotide, which is a key molecule in the biosynthesis of various sugar-containing molecules.",Vague,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0016758,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.8416,0.8416,0.8416,0.8416,0.8416,5,0.8416,0.3234,no
CGALT_BORBU,O51519,Reference,Bacteria,358,"Galactosyltransferase involved in the synthesis of cholesterol glycolipids, which are formed by the use of host-derived cholesterol and have been shown to be immunogenic, and possibly contribute to Lyme disease pathogenesis. Catalyzes the formation of cholesteryl beta-D-galactopyranoside (CGal) from cholesterol and UDP-alpha-D-galactose. Cannot use GDP-mannose.","Galactosyltransferase involved in the synthesis of cholesterol glycolipids, which are formed by the use of host-derived cholesterol and have been shown to be immunogenic, and possibly contribute to Lyme disease pathogenesis. Catalyzes the formation of cholesteryl beta-D-galactopyranoside (CGal) from cholesterol and UDP-alpha-D-galactose. Cannot use GDP-mannose.",,,,,,,GO:0016758,GO:0008378,GO:0008378,GO:0008378,GO:0008378,GO:0008378,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.3234,no
WAAC_CAMCO,O87333,ESM2Text,Bacteria,342,Glycosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS). Catalyzes the addition of the first heptose unit to one 3-deoxy-D- manno-octulosonic acid (Kdo) residue of the Kdo2-lipid A module.,"Catalyzes the transfer of heptose to the lipopolysaccharide core. It transfers the heptose to the phosphorylated 3-deoxy-D-manno-octulosonate (Kdo-Kdo) via an alpha-1,3 linkage to the phosphorylated C-24. Also shows activity to the phosphorylated teichoic acid.",Yes,Yes,Maybe,Yes,Yes,Yes,GO:0008713,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.729,0.729,0.729,0.729,0.729,5,0.729,0.3532,no
WAAC_CAMCO,O87333,Prot2Text,Bacteria,342,Glycosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS). Catalyzes the addition of the first heptose unit to one 3-deoxy-D- manno-octulosonic acid (Kdo) residue of the Kdo2-lipid A module.,Catalyzes heptose transfer to the lipopolysaccharide core. It transfers the first L-glycero-D-manno-heptose to the phosphorylated 3-deoxy-alpha-D-manno-octulosonic acid (Kdo-P) of the inner core.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008713,GO:0016757,GO:0016757,GO:0008920,GO:0016757,GO:0008920,0.729,0.729,0.8582,0.729,0.8582,5,0.7807,0.3532,no
WAAC_CAMCO,O87333,ProtT3,Bacteria,342,Glycosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS). Catalyzes the addition of the first heptose unit to one 3-deoxy-D- manno-octulosonic acid (Kdo) residue of the Kdo2-lipid A module.,Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008713,GO:0016757,GO:0016757,,GO:0016757,GO:0016757,0.729,0.729,,0.729,0.729,4,0.729,0.3532,no
WAAC_CAMCO,O87333,ProtTale,Bacteria,342,Glycosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS). Catalyzes the addition of the first heptose unit to one 3-deoxy-D- manno-octulosonic acid (Kdo) residue of the Kdo2-lipid A module.,Glycosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS). Catalyzes the addition of the second heptose unit (HepII) to the first heptose (HepI) of the inner core.,Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0008713,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.729,0.729,0.729,0.729,0.729,5,0.729,0.3532,no
WAAC_CAMCO,O87333,Protein2Text,Bacteria,342,Glycosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS). Catalyzes the addition of the first heptose unit to one 3-deoxy-D- manno-octulosonic acid (Kdo) residue of the Kdo2-lipid A module.,"The molecular function of this protein is involved in the synthesis of a type of sugar molecule, specifically a nucleotide sugar. More specifically, it is involved in the transfer of a sugar molecule to a nucleotide molecule, which is an essential step in the biosynthesis of various complex molecules such as polysaccharides, glycolipids, and glycoproteins. 

In more detail, this protein is a transferase, and it catalyzes the transfer of a sugar molecule from a sugar nucleotide donor to an acceptor molecule. The sugar nucleotide donor is typically a molecule with a sugar residue linked to a nucleotide moiety, and the acceptor molecule is typically a carbohydrate or a lipid molecule. The protein catalyzes the transfer of the sugar residue from the sugar nucleotide donor to the acceptor molecule, resulting in the formation of a new glycosidic bond. This reaction is an important step in the biosynthesis of various complex molecules, such as polysaccharides, glycolipids, and glycoproteins. 

In the case of the protein this is associated with, it is involved in the biosynthesis of a type of glycan molecule. Specifically, it is involved in the transfer of a sugar molecule to a lipid molecule, resulting in the formation of a glycolipid molecule. This glycolipid molecule is an important component of the cell wall of bacteria, and it plays a crucial role in the structure and function of the cell wall. 

Overall, the molecular function of this protein is essential for the biosynthesis of complex molecules, and it plays a critical role in the structure and function of various biological systems.",Vague,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0008713,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.729,0.729,0.729,0.729,0.729,5,0.729,0.3532,no
WAAC_CAMCO,O87333,Reference,Bacteria,342,Glycosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS). Catalyzes the addition of the first heptose unit to one 3-deoxy-D- manno-octulosonic acid (Kdo) residue of the Kdo2-lipid A module.,Glycosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS). Catalyzes the addition of the first heptose unit to one 3-deoxy-D- manno-octulosonic acid (Kdo) residue of the Kdo2-lipid A module.,,,,,,,GO:0008713,GO:0008920,GO:0008920,GO:0016757,GO:0016757,GO:0016757,0.8582,0.8582,0.729,0.729,0.729,5,0.7807,0.3532,no
VDDP4_VESVE,P0DRB8,ESM2Text,Eukaryota,776,Venom dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N- termini provided that the penultimate residue is proline. May process venom proteins into their active forms and/or modulate the chemotactic activity of immune cells after the insect sting.,Venom dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. May process venom components into their active forms and/or modulate the chemotactic activity of immune cells after the insect sting.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004177; GO:0008239; GO:0008236,GO:0008239,GO:0008239,GO:0004274,GO:0008239,GO:0008239,0.8405,0.8405,0.0,0.8405,0.8405,5,0.6724,0.5763,yes
VDDP4_VESVE,P0DRB8,Prot2Text,Eukaryota,776,Venom dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N- termini provided that the penultimate residue is proline. May process venom proteins into their active forms and/or modulate the chemotactic activity of immune cells after the insect sting.,Venom dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. May process promelittin into its active form and/or modulate the chemotactic activity of immune cells after the insect sting.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004177; GO:0008239; GO:0008236,GO:0008239,GO:0008239,GO:0008239,GO:0004274,GO:0008239,0.8405,0.8405,0.8405,0.0,0.8405,5,0.6724,0.5763,yes
VDDP4_VESVE,P0DRB8,ProtT3,Eukaryota,776,Venom dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N- termini provided that the penultimate residue is proline. May process venom proteins into their active forms and/or modulate the chemotactic activity of immune cells after the insect sting.,Type IV dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N- termini provided that the penultimate residue is proline. Secreted. Belongs to the peptidase S9B family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004177; GO:0008239; GO:0008236,GO:0008239; GO:0004252,GO:0008239,GO:0008239,GO:0008239,GO:0008239,0.8834,0.8405,0.8405,0.8405,0.8405,5,0.8491,0.5763,yes
VDDP4_VESVE,P0DRB8,ProtTale,Eukaryota,776,Venom dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N- termini provided that the penultimate residue is proline. May process venom proteins into their active forms and/or modulate the chemotactic activity of immune cells after the insect sting.,Extracellular dipeptidyl-peptidase which contributes to virulence.,Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0004177; GO:0008239; GO:0008236,GO:0008239,GO:0008239,GO:0008239,GO:0008239,GO:0008239,0.8405,0.8405,0.8405,0.8405,0.8405,5,0.8405,0.5763,yes
VDDP4_VESVE,P0DRB8,Protein2Text,Eukaryota,776,Venom dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N- termini provided that the penultimate residue is proline. May process venom proteins into their active forms and/or modulate the chemotactic activity of immune cells after the insect sting.,"The molecular function of this protein is a metalloprotease, specifically a dipeptidyl peptidase, which cleaves dipeptides from the amino terminus of peptides.",Maybe,Maybe,Maybe,Yes,Maybe,not-Yes,GO:0004177; GO:0008239; GO:0008236,GO:0008237,GO:0008237; GO:0008239,GO:0008237; GO:0008239,GO:0008237; GO:0008239,GO:0008239,0.6703,0.8252,0.8252,0.8252,0.8405,5,0.7973,0.5763,yes
VDDP4_VESVE,P0DRB8,Reference,Eukaryota,776,Venom dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N- termini provided that the penultimate residue is proline. May process venom proteins into their active forms and/or modulate the chemotactic activity of immune cells after the insect sting.,Venom dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N- termini provided that the penultimate residue is proline. May process venom proteins into their active forms and/or modulate the chemotactic activity of immune cells after the insect sting.,,,,,,,GO:0004177; GO:0008239; GO:0008236,GO:0008239,GO:0008239,GO:0008239,GO:0008239,GO:0008239,0.8405,0.8405,0.8405,0.8405,0.8405,5,0.8405,0.5763,yes
PROT_UNKP,P0DV53,ESM2Text,Bacteria,1062,"A dedicated protease for substrate gasdermin bGSDM; cleaves the bGSDM precursor, releasing the pore-forming moiety, which integrates into the membrane and triggers cell death. Probably involved in defense against bacteriophages. Expression of bGSDM and this neighboring protease is highly toxic in E.coli.","Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. The N-terminus binds the peptide between GTP-bound Rho and the active site in the Rho protein. The alpha and delta subunits may act in a reciprocal manner.",No,No,No,No,No,not-Yes,GO:0008236,GO:0003924; GO:0005525,GO:0003924,GO:0003924,GO:0003924; GO:0005525,GO:0003924; GO:0005525,0.1946,0.2634,0.2634,0.1946,0.1946,5,0.2221,0.3735,no
PROT_UNKP,P0DV53,Prot2Text,Bacteria,1062,"A dedicated protease for substrate gasdermin bGSDM; cleaves the bGSDM precursor, releasing the pore-forming moiety, which integrates into the membrane and triggers cell death. Probably involved in defense against bacteriophages. Expression of bGSDM and this neighboring protease is highly toxic in E.coli.",Involved in the production of the second messenger cAMP.,No,No,No,No,No,not-Yes,GO:0008236,GO:0004016,GO:0004016,GO:0004016,GO:0004016,GO:0004016,0.2255,0.2255,0.2255,0.2255,0.2255,5,0.2255,0.3735,no
PROT_UNKP,P0DV53,ProtT3,Bacteria,1062,"A dedicated protease for substrate gasdermin bGSDM; cleaves the bGSDM precursor, releasing the pore-forming moiety, which integrates into the membrane and triggers cell death. Probably involved in defense against bacteriophages. Expression of bGSDM and this neighboring protease is highly toxic in E.coli.",Probable ATPase. Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family,No,No,No,No,No,not-Yes,GO:0008236,GO:0016887,GO:0016887,GO:0016887,GO:0016887,GO:0016887,0.2676,0.2676,0.2676,0.2676,0.2676,5,0.2676,0.3735,no
PROT_UNKP,P0DV53,ProtTale,Bacteria,1062,"A dedicated protease for substrate gasdermin bGSDM; cleaves the bGSDM precursor, releasing the pore-forming moiety, which integrates into the membrane and triggers cell death. Probably involved in defense against bacteriophages. Expression of bGSDM and this neighboring protease is highly toxic in E.coli.",Single-stranded DNA (ssDNA) 3'-5' exonuclease that plays a role in DNA repair. Probably involved in the repair of stalled replication forks.,No,No,No,No,No,not-Yes,GO:0008236,GO:0008296,GO:0008408; GO:0003697,GO:0008408,GO:0008408; GO:0003697,GO:0008296,0.2128,0.2278,0.2915,0.2278,0.2128,5,0.2345,0.3735,no
PROT_UNKP,P0DV53,Protein2Text,Bacteria,1062,"A dedicated protease for substrate gasdermin bGSDM; cleaves the bGSDM precursor, releasing the pore-forming moiety, which integrates into the membrane and triggers cell death. Probably involved in defense against bacteriophages. Expression of bGSDM and this neighboring protease is highly toxic in E.coli.","The molecular function of this protein is not explicitly stated in the provided text. However, based on the name ""pilin assembly protein"" and the fact that it is involved in a process related to the formation of a structure (likely a pilus), it can be inferred that the protein is involved in the assembly of a protein structure, specifically the pilus.",Vague,No,Vague,Vague,No,not-Yes,GO:0008236,,,,,,,,,,,0,,0.3735,no
PROT_UNKP,P0DV53,Reference,Bacteria,1062,"A dedicated protease for substrate gasdermin bGSDM; cleaves the bGSDM precursor, releasing the pore-forming moiety, which integrates into the membrane and triggers cell death. Probably involved in defense against bacteriophages. Expression of bGSDM and this neighboring protease is highly toxic in E.coli.","A dedicated protease for substrate gasdermin bGSDM; cleaves the bGSDM precursor, releasing the pore-forming moiety, which integrates into the membrane and triggers cell death. Probably involved in defense against bacteriophages. Expression of bGSDM and this neighboring protease is highly toxic in E.coli.",,,,,,,GO:0008236,GO:0008233,GO:0008233,GO:0008233,GO:0008233,GO:0008233,0.7896,0.7896,0.7896,0.7896,0.7896,5,0.7896,0.3735,no
DTCA_VIBAL,P0DW68,ESM2Text,Bacteria,984,"Sensor-kinase member of the two-component regulatory system Detocs that confers resistance to bacteriophage. When the system (DtcA-DtcB-DtcC) is expressed in a susceptible E.coli (strain MG1655) it confers resistance to bacteriophages T2, T4, T5, T6 and SECphi27. Detocs inhibits T5 infection leading to growth arrest but not complete cell lysis, during SECphi27 infection leads to cell lysis. DtcA (this subunit) probably autophosphorylates upon sensing viral infection, and subsequently transfers the phosphate signal to DtcC which activates it, leading to an antiviral defense; DtcB may scavenge phosphorylation signals from accidental activation of DtcA (Probable).",Upon expression in E.coli enables the latter to utilize penicillin as a carbon source.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004673,,GO:0008800,GO:0008800,,GO:0008800,,0.1261,0.1261,,0.1261,3,0.1261,0.3942,no
DTCA_VIBAL,P0DW68,Prot2Text,Bacteria,984,"Sensor-kinase member of the two-component regulatory system Detocs that confers resistance to bacteriophage. When the system (DtcA-DtcB-DtcC) is expressed in a susceptible E.coli (strain MG1655) it confers resistance to bacteriophages T2, T4, T5, T6 and SECphi27. Detocs inhibits T5 infection leading to growth arrest but not complete cell lysis, during SECphi27 infection leads to cell lysis. DtcA (this subunit) probably autophosphorylates upon sensing viral infection, and subsequently transfers the phosphate signal to DtcC which activates it, leading to an antiviral defense; DtcB may scavenge phosphorylation signals from accidental activation of DtcA (Probable).",Plays a role in vesicular protein sorting. Required for the endosome-to-Golgi retrieval of the vacuolar protein sorting receptor pep1/vps10. Component of the membrane-associated retromer complex which is essential in endosome-to-Golgi retrograde transport. The vps29-vps26-vps35 subcomplex may be involved in cargo selection.,No,No,No,No,No,not-Yes,GO:0005524; GO:0004673,,,,,,,,,,,0,,0.3942,no
DTCA_VIBAL,P0DW68,ProtT3,Bacteria,984,"Sensor-kinase member of the two-component regulatory system Detocs that confers resistance to bacteriophage. When the system (DtcA-DtcB-DtcC) is expressed in a susceptible E.coli (strain MG1655) it confers resistance to bacteriophages T2, T4, T5, T6 and SECphi27. Detocs inhibits T5 infection leading to growth arrest but not complete cell lysis, during SECphi27 infection leads to cell lysis. DtcA (this subunit) probably autophosphorylates upon sensing viral infection, and subsequently transfers the phosphate signal to DtcC which activates it, leading to an antiviral defense; DtcB may scavenge phosphorylation signals from accidental activation of DtcA (Probable).","CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity)",No,Maybe,No,No,No,not-Yes,GO:0005524; GO:0004673,,,,,,,,,,,0,,0.3942,no
DTCA_VIBAL,P0DW68,ProtTale,Bacteria,984,"Sensor-kinase member of the two-component regulatory system Detocs that confers resistance to bacteriophage. When the system (DtcA-DtcB-DtcC) is expressed in a susceptible E.coli (strain MG1655) it confers resistance to bacteriophages T2, T4, T5, T6 and SECphi27. Detocs inhibits T5 infection leading to growth arrest but not complete cell lysis, during SECphi27 infection leads to cell lysis. DtcA (this subunit) probably autophosphorylates upon sensing viral infection, and subsequently transfers the phosphate signal to DtcC which activates it, leading to an antiviral defense; DtcB may scavenge phosphorylation signals from accidental activation of DtcA (Probable).","Acts as a transcriptional regulator. Regulates the expression of genes involved in nitrogen fixation (nifH, nifD, nifK, nifL, nifM, nifS, nifU, nifV, nifW, nifX, nifZ, nifC, nifB, nifA, nifY, nifQ, nif1, nif2, nif3, nif4, nif5, nif6, nif7, nif8, nif9, nif10, nif11, nif12, nif13, nif14, nif15, nif16, nif17, nif",No,No,No,No,No,not-Yes,GO:0005524; GO:0004673,GO:0003700,GO:0003700,GO:0003700,GO:0003700,GO:0003700,0.1065,0.1065,0.1065,0.1065,0.1065,5,0.1065,0.3942,no
DTCA_VIBAL,P0DW68,Protein2Text,Bacteria,984,"Sensor-kinase member of the two-component regulatory system Detocs that confers resistance to bacteriophage. When the system (DtcA-DtcB-DtcC) is expressed in a susceptible E.coli (strain MG1655) it confers resistance to bacteriophages T2, T4, T5, T6 and SECphi27. Detocs inhibits T5 infection leading to growth arrest but not complete cell lysis, during SECphi27 infection leads to cell lysis. DtcA (this subunit) probably autophosphorylates upon sensing viral infection, and subsequently transfers the phosphate signal to DtcC which activates it, leading to an antiviral defense; DtcB may scavenge phosphorylation signals from accidental activation of DtcA (Probable).","The molecular function of this protein is not specified in the provided text. However, based on its name, it is likely to be a DNA-binding protein, given the presence of the word ""binding"" in its name. Specifically, it is likely to be a DNA helicase, which is a type of protein that unwinds DNA during DNA replication and repair.",Vague,Vague,No,Vague,No,not-Yes,GO:0005524; GO:0004673,,GO:0003678; GO:0005524,,,GO:0003678,,0.571,,,0.1131,2,0.342,0.3942,no
DTCA_VIBAL,P0DW68,Reference,Bacteria,984,"Sensor-kinase member of the two-component regulatory system Detocs that confers resistance to bacteriophage. When the system (DtcA-DtcB-DtcC) is expressed in a susceptible E.coli (strain MG1655) it confers resistance to bacteriophages T2, T4, T5, T6 and SECphi27. Detocs inhibits T5 infection leading to growth arrest but not complete cell lysis, during SECphi27 infection leads to cell lysis. DtcA (this subunit) probably autophosphorylates upon sensing viral infection, and subsequently transfers the phosphate signal to DtcC which activates it, leading to an antiviral defense; DtcB may scavenge phosphorylation signals from accidental activation of DtcA (Probable).","Sensor-kinase member of the two-component regulatory system Detocs that confers resistance to bacteriophage. When the system (DtcA-DtcB-DtcC) is expressed in a susceptible E.coli (strain MG1655) it confers resistance to bacteriophages T2, T4, T5, T6 and SECphi27. Detocs inhibits T5 infection leading to growth arrest but not complete cell lysis, during SECphi27 infection leads to cell lysis. DtcA (this subunit) probably autophosphorylates upon sensing viral infection, and subsequently transfers the phosphate signal to DtcC which activates it, leading to an antiviral defense; DtcB may scavenge phosphorylation signals from accidental activation of DtcA (Probable).",,,,,,,GO:0005524; GO:0004673,GO:0000155,GO:0000155; GO:0005524,GO:0000155; GO:0005524,GO:0000155,GO:0000155; GO:0005524,0.572,0.9158,0.9158,0.572,0.9158,5,0.7783,0.3942,no
DTCA_ENTC6,P0DW71,ESM2Text,Bacteria,1103,"Sensor-kinase member of the two-component regulatory system Detocs that confers resistance to bacteriophage. When the system (DtcA-DtcB-DtcC) is expressed in a susceptible E.coli (strain MG1655) it confers resistance to bacteriophages T2, T4, T5, T7, SECphi4, SECphi6 and SECphi27; the level of resistance varies, resistance to T2, T7 and SECphi4 is not very high. DtcA (this subunit) probably autophosphorylates upon sensing viral infection, and subsequently transfers the phosphate signal to DtcC which activates it, leading to an antiviral defense; DtcB may scavenge phosphorylation signals from accidental activation of DtcA (Probable).",May be involved in nucleotide excision repair (NER) of damaged DNA.,No,No,No,No,No,not-Yes,GO:0004673,,,,,,,,,,,0,,0.6059,yes
DTCA_ENTC6,P0DW71,Prot2Text,Bacteria,1103,"Sensor-kinase member of the two-component regulatory system Detocs that confers resistance to bacteriophage. When the system (DtcA-DtcB-DtcC) is expressed in a susceptible E.coli (strain MG1655) it confers resistance to bacteriophages T2, T4, T5, T7, SECphi4, SECphi6 and SECphi27; the level of resistance varies, resistance to T2, T7 and SECphi4 is not very high. DtcA (this subunit) probably autophosphorylates upon sensing viral infection, and subsequently transfers the phosphate signal to DtcC which activates it, leading to an antiviral defense; DtcB may scavenge phosphorylation signals from accidental activation of DtcA (Probable).","Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.",No,No,No,No,No,not-Yes,GO:0004673,GO:0061630,,GO:0061630,GO:0061630,GO:0061630,0.296,,0.296,0.296,0.296,4,0.296,0.6059,yes
DTCA_ENTC6,P0DW71,ProtT3,Bacteria,1103,"Sensor-kinase member of the two-component regulatory system Detocs that confers resistance to bacteriophage. When the system (DtcA-DtcB-DtcC) is expressed in a susceptible E.coli (strain MG1655) it confers resistance to bacteriophages T2, T4, T5, T7, SECphi4, SECphi6 and SECphi27; the level of resistance varies, resistance to T2, T7 and SECphi4 is not very high. DtcA (this subunit) probably autophosphorylates upon sensing viral infection, and subsequently transfers the phosphate signal to DtcC which activates it, leading to an antiviral defense; DtcB may scavenge phosphorylation signals from accidental activation of DtcA (Probable).","ATPase component of the type VII secretion system (T7SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (By similarity). Acts as a molecular motor to provide the energy that is required for the export of proteins (By similarity). In addition to its ATPase activity, also acts as a DNA-binding protein (By similarity). ATPase component of the type VII secretion system (T7SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (PubMed:",No,No,No,No,No,not-Yes,GO:0004673,GO:0016887; GO:0005524; GO:0003677,GO:0016887; GO:0003677,GO:0016887; GO:0003677,GO:0016887; GO:0005524; GO:0003677,GO:0016887; GO:0005524; GO:0003677,0.1084,0.1276,0.1276,0.1084,0.1084,5,0.1161,0.6059,yes
DTCA_ENTC6,P0DW71,ProtTale,Bacteria,1103,"Sensor-kinase member of the two-component regulatory system Detocs that confers resistance to bacteriophage. When the system (DtcA-DtcB-DtcC) is expressed in a susceptible E.coli (strain MG1655) it confers resistance to bacteriophages T2, T4, T5, T7, SECphi4, SECphi6 and SECphi27; the level of resistance varies, resistance to T2, T7 and SECphi4 is not very high. DtcA (this subunit) probably autophosphorylates upon sensing viral infection, and subsequently transfers the phosphate signal to DtcC which activates it, leading to an antiviral defense; DtcB may scavenge phosphorylation signals from accidental activation of DtcA (Probable).",Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic di-GMP (c-di-GMP) to 5'-pGpG.,No,No,No,No,No,not-Yes,GO:0004673,GO:0004112,GO:0004112,GO:0004112,GO:0004112,GO:0004112,0.1433,0.1433,0.1433,0.1433,0.1433,5,0.1433,0.6059,yes
DTCA_ENTC6,P0DW71,Protein2Text,Bacteria,1103,"Sensor-kinase member of the two-component regulatory system Detocs that confers resistance to bacteriophage. When the system (DtcA-DtcB-DtcC) is expressed in a susceptible E.coli (strain MG1655) it confers resistance to bacteriophages T2, T4, T5, T7, SECphi4, SECphi6 and SECphi27; the level of resistance varies, resistance to T2, T7 and SECphi4 is not very high. DtcA (this subunit) probably autophosphorylates upon sensing viral infection, and subsequently transfers the phosphate signal to DtcC which activates it, leading to an antiviral defense; DtcB may scavenge phosphorylation signals from accidental activation of DtcA (Probable).","The molecular function of this protein is not explicitly stated in the provided information. However, based on its name and the context in which it is mentioned, it can be inferred that it is a part of a viral genome replication machinery. This protein is likely involved in the replication of viral DNA, specifically in the process of viral DNA replication.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0004673,,,,,,,,,,,0,,0.6059,yes
DTCA_ENTC6,P0DW71,Reference,Bacteria,1103,"Sensor-kinase member of the two-component regulatory system Detocs that confers resistance to bacteriophage. When the system (DtcA-DtcB-DtcC) is expressed in a susceptible E.coli (strain MG1655) it confers resistance to bacteriophages T2, T4, T5, T7, SECphi4, SECphi6 and SECphi27; the level of resistance varies, resistance to T2, T7 and SECphi4 is not very high. DtcA (this subunit) probably autophosphorylates upon sensing viral infection, and subsequently transfers the phosphate signal to DtcC which activates it, leading to an antiviral defense; DtcB may scavenge phosphorylation signals from accidental activation of DtcA (Probable).","Sensor-kinase member of the two-component regulatory system Detocs that confers resistance to bacteriophage. When the system (DtcA-DtcB-DtcC) is expressed in a susceptible E.coli (strain MG1655) it confers resistance to bacteriophages T2, T4, T5, T7, SECphi4, SECphi6 and SECphi27; the level of resistance varies, resistance to T2, T7 and SECphi4 is not very high. DtcA (this subunit) probably autophosphorylates upon sensing viral infection, and subsequently transfers the phosphate signal to DtcC which activates it, leading to an antiviral defense; DtcB may scavenge phosphorylation signals from accidental activation of DtcA (Probable).",,,,,,,GO:0004673,GO:0000155,GO:0000155; GO:0005524,GO:0000155; GO:0005524,GO:0000155,GO:0000155; GO:0005524,0.8316,0.5713,0.5713,0.8316,0.5713,5,0.6754,0.6059,yes
PHNY_GIMM8,P0DX11,ESM2Text,Bacteria,260,Part of an oxidative pathway for utilization of methylphosphonic acid as a phosphate source. Catalyzes the conversion of methylphosphonic acid to hydroxymethylphosphonic acid. Is specific for the hydroxylation of methylphosphonate.,"Involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the hydroxylation of the alpha-hydroxyl group of the N-acetyl-phosphonoacetyl-serine (HPA) pyrrole ring to yield a catechol intermediate that is covalently linked to an acyl carrier protein (ACP).",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0016706; GO:0005506,,GO:0016491,,,,,0.447,,,,1,0.447,0.2418,no
PHNY_GIMM8,P0DX11,Prot2Text,Bacteria,260,Part of an oxidative pathway for utilization of methylphosphonic acid as a phosphate source. Catalyzes the conversion of methylphosphonic acid to hydroxymethylphosphonic acid. Is specific for the hydroxylation of methylphosphonate.,Involved in the degradation of the organophosphonate 2-aminoethylphosphonic acid (2-AEP) (Probable). Catalyzes the hydroxylation of 2-aminoethylphosphonic acid to yield (2-amino-1-hydroxyethyl)phosphonic acid.,Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0016706; GO:0005506,GO:0051213,GO:0051213,GO:0016491,GO:0016491,GO:0016491,0.5318,0.5318,0.447,0.447,0.447,5,0.4809,0.2418,no
PHNY_GIMM8,P0DX11,ProtT3,Bacteria,260,Part of an oxidative pathway for utilization of methylphosphonic acid as a phosphate source. Catalyzes the conversion of methylphosphonic acid to hydroxymethylphosphonic acid. Is specific for the hydroxylation of methylphosphonate.,Catalyzes the 2-oxoglutarate-dependent hydroxylation of 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA (OSB-CoA). Belongs to the PhyH family. MenH subfamily,No,No,No,No,Maybe,not-Yes,GO:0016706; GO:0005506,GO:0016706,GO:0016706,GO:0016706,GO:0016706,GO:0016706,0.6915,0.6915,0.6915,0.6915,0.6915,5,0.6915,0.2418,no
PHNY_GIMM8,P0DX11,ProtTale,Bacteria,260,Part of an oxidative pathway for utilization of methylphosphonic acid as a phosphate source. Catalyzes the conversion of methylphosphonic acid to hydroxymethylphosphonic acid. Is specific for the hydroxylation of methylphosphonate.,"Involved in the biosynthesis of the osmoprotectant glycine betaine (GB). Catalyzes the epimerization of L-carnitine, which is an intermediate in the biosynthesis of GB.",No,No,No,No,No,not-Yes,GO:0016706; GO:0005506,GO:0016857,GO:0016854,GO:0016854,GO:0016854,GO:0016854,0.1908,0.2282,0.2282,0.2282,0.2282,5,0.2207,0.2418,no
PHNY_GIMM8,P0DX11,Protein2Text,Bacteria,260,Part of an oxidative pathway for utilization of methylphosphonic acid as a phosphate source. Catalyzes the conversion of methylphosphonic acid to hydroxymethylphosphonic acid. Is specific for the hydroxylation of methylphosphonate.,"This protein is a part of a gene that encodes an enzyme that is involved in the biosynthesis of a compound. The molecular function of this protein is likely to be a part of a metabolic pathway, specifically in the biosynthesis of a compound.

However, the specific molecular function of this protein is not provided in the given information. If you need more information about the molecular function of this protein, please provide more context or details about the protein or the gene it is associated with.

Alternatively, if you are looking for information about the molecular function of a specific protein, please provide the name of the protein or its UniProt ID, and I will do my best to provide the relevant information.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016706; GO:0005506,,,,,,,,,,,0,,0.2418,no
PHNY_GIMM8,P0DX11,Reference,Bacteria,260,Part of an oxidative pathway for utilization of methylphosphonic acid as a phosphate source. Catalyzes the conversion of methylphosphonic acid to hydroxymethylphosphonic acid. Is specific for the hydroxylation of methylphosphonate.,Part of an oxidative pathway for utilization of methylphosphonic acid as a phosphate source. Catalyzes the conversion of methylphosphonic acid to hydroxymethylphosphonic acid. Is specific for the hydroxylation of methylphosphonate.,,,,,,,GO:0016706; GO:0005506,GO:0016491,GO:0016491,GO:0016491,GO:0016709,GO:0016491,0.447,0.447,0.447,0.4031,0.447,5,0.4382,0.2418,no
INLPA_STRC4,P0DX16,ESM2Text,Bacteria,1470,"Nonribosomal peptide synthetase (NRPS) involved in the biosynthesis of a unique class of isonitrile lipopeptides (INLPs). Catalyzes the final step in the pathway, i.e. the condensation of a (3R)-3-isocyanyl-fatty acyl-[ACP] to both amino groups of a lysine, producing isonitrile lipopeptides. Can use (3R)-3-isocyanylbutanoyl- [ACP] as substrate, leading to (2S)-2,6-bis[(3R)-3- isocyanobutanamido]hexan-1-ol.","Isomerization of L-allo-threonine into L-2-phenylethanolamine, a core metabolite of the phenylalanine-dependent antibiotic indole-3-carbonylurel-lipid IV (ICL-4-AML). The acyl chain is then transferred to the phenylalanine residue of ICL-4-AML, forming the activated ICL-4-AML intermediate, via a thioester linkage.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016874; GO:0031177; GO:0016740,,,,,,,,,,,0,,0.4554,no
INLPA_STRC4,P0DX16,Prot2Text,Bacteria,1470,"Nonribosomal peptide synthetase (NRPS) involved in the biosynthesis of a unique class of isonitrile lipopeptides (INLPs). Catalyzes the final step in the pathway, i.e. the condensation of a (3R)-3-isocyanyl-fatty acyl-[ACP] to both amino groups of a lysine, producing isonitrile lipopeptides. Can use (3R)-3-isocyanylbutanoyl- [ACP] as substrate, leading to (2S)-2,6-bis[(3R)-3- isocyanobutanamido]hexan-1-ol.","This protein is a multifunctional enzyme, able to activate and polymerize the amino acid Ile as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The activation sites for this amino acid consist of individual domains.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016874; GO:0031177; GO:0016740,GO:0016874,GO:0016874,GO:0016874,GO:0016874,GO:0016874,0.5609,0.5609,0.5609,0.5609,0.5609,5,0.5609,0.4554,no
INLPA_STRC4,P0DX16,ProtT3,Bacteria,1470,"Nonribosomal peptide synthetase (NRPS) involved in the biosynthesis of a unique class of isonitrile lipopeptides (INLPs). Catalyzes the final step in the pathway, i.e. the condensation of a (3R)-3-isocyanyl-fatty acyl-[ACP] to both amino groups of a lysine, producing isonitrile lipopeptides. Can use (3R)-3-isocyanylbutanoyl- [ACP] as substrate, leading to (2S)-2,6-bis[(3R)-3- isocyanobutanamido]hexan-1-ol.","Involved in the biosynthesis of the siderophore enterobactin. Catalyzes the activation of 2,3-dihydroxybenzoyl-CoA (DHB-CoA) to yield 2,3-dihydroxybenzoyl-4-coenzyme A (DHB-4-CoA) (By similarity). Involved in the biosynthesis of the siderophore enterobactin. Catalyzes the activation of 2,3-dihydroxybenzoyl-CoA (DHB-CoA) to yield 2,3-dihydroxybenzoyl-4-coenzyme A (DHB-4-CoA)",No,Maybe,No,No,Maybe,not-Yes,GO:0005524; GO:0016874; GO:0031177; GO:0016740,GO:0016405,GO:0016874,GO:0003996,GO:0016874,GO:0016874,0.3884,0.5609,0.2535,0.5609,0.5609,5,0.4649,0.4554,no
INLPA_STRC4,P0DX16,ProtTale,Bacteria,1470,"Nonribosomal peptide synthetase (NRPS) involved in the biosynthesis of a unique class of isonitrile lipopeptides (INLPs). Catalyzes the final step in the pathway, i.e. the condensation of a (3R)-3-isocyanyl-fatty acyl-[ACP] to both amino groups of a lysine, producing isonitrile lipopeptides. Can use (3R)-3-isocyanylbutanoyl- [ACP] as substrate, leading to (2S)-2,6-bis[(3R)-3- isocyanobutanamido]hexan-1-ol.","Catalyzes the activation of L-phenylalanine, L-tyrosine and L-tryptophan, and the activation of 4-methyl-L-phenylalanine. Activation of 4-methyl-L-phenylalanine is the most efficient among the activation reactions tested. Activation of L-tyrosine is about 3 times lower. Activation of L-phenylalanine, L-tyrosine and L-tryptophan is not affected by the presence of CoA or ATP. Activation of 4-methyl-L-phenylalanine is the most efficient among the activation reactions tested, and it is the only activation reaction in the presence of CoA and ATP",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0005524; GO:0016874; GO:0031177; GO:0016740,GO:0016874,GO:0016874,GO:0016874,GO:0016874; GO:0005524,GO:0016874,0.5609,0.5609,0.5609,0.8248,0.5609,5,0.6137,0.4554,no
INLPA_STRC4,P0DX16,Protein2Text,Bacteria,1470,"Nonribosomal peptide synthetase (NRPS) involved in the biosynthesis of a unique class of isonitrile lipopeptides (INLPs). Catalyzes the final step in the pathway, i.e. the condensation of a (3R)-3-isocyanyl-fatty acyl-[ACP] to both amino groups of a lysine, producing isonitrile lipopeptides. Can use (3R)-3-isocyanylbutanoyl- [ACP] as substrate, leading to (2S)-2,6-bis[(3R)-3- isocyanobutanamido]hexan-1-ol.",The molecular function of this protein is a non-ribosomal peptide synthetase. It is involved in the synthesis of a specific type of peptide molecule.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016874; GO:0031177; GO:0016740,GO:0016874,,,,GO:0016874,0.5609,,,,0.5609,2,0.5609,0.4554,no
INLPA_STRC4,P0DX16,Reference,Bacteria,1470,"Nonribosomal peptide synthetase (NRPS) involved in the biosynthesis of a unique class of isonitrile lipopeptides (INLPs). Catalyzes the final step in the pathway, i.e. the condensation of a (3R)-3-isocyanyl-fatty acyl-[ACP] to both amino groups of a lysine, producing isonitrile lipopeptides. Can use (3R)-3-isocyanylbutanoyl- [ACP] as substrate, leading to (2S)-2,6-bis[(3R)-3- isocyanobutanamido]hexan-1-ol.","Nonribosomal peptide synthetase (NRPS) involved in the biosynthesis of a unique class of isonitrile lipopeptides (INLPs). Catalyzes the final step in the pathway, i.e. the condensation of a (3R)-3-isocyanyl-fatty acyl-[ACP] to both amino groups of a lysine, producing isonitrile lipopeptides. Can use (3R)-3-isocyanylbutanoyl- [ACP] as substrate, leading to (2S)-2,6-bis[(3R)-3- isocyanobutanamido]hexan-1-ol.",,,,,,,GO:0005524; GO:0016874; GO:0031177; GO:0016740,GO:0016874,GO:0016874,GO:0016874,GO:0016874,GO:0016874,0.5609,0.5609,0.5609,0.5609,0.5609,5,0.5609,0.4554,no
3BHD_KLEAE,P0DX23,ESM2Text,Bacteria,337,Catalyzes the degradation of estradiol into estrone. Can also degrade testosterone.,"Catalyzes the dehydration of 2-dehydro-3-deoxy-D-manno-octulosonate (KDO) to 3-dehydro-2,5-dichloro-A (KDDA). Involved in the biosynthesis of sulfolipid A, a component of the cell wall sulfolipid that is an important component of the cell wall component of E.coli. Can use both NAD(+) and NADP(+) as electron acceptor, with a marked preference for NADP(+).",No,No,No,No,No,not-Yes,GO:0016491,,,,,,,,,,,0,,0.1823,no
3BHD_KLEAE,P0DX23,Prot2Text,Bacteria,337,Catalyzes the degradation of estradiol into estrone. Can also degrade testosterone.,Involved in the biosynthesis of the negatively charged monosaccharide that forms the backbone of pectic cell wall components. Catalyzes the reduction of the highly sulfated tetraacyldisaccharide (THDC) that is formed in each cycle of cell elongation. THDC is a key component of elongation factor I which is a general feature of plant cell elongation.,No,No,No,No,No,not-Yes,GO:0016491,GO:0016491,,,,GO:0016491,1.0,,,,1.0,2,1.0,0.1823,no
3BHD_KLEAE,P0DX23,ProtT3,Bacteria,337,Catalyzes the degradation of estradiol into estrone. Can also degrade testosterone.,Belongs to the NAD(P)-dependent epimerase/dehydratase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016491,,GO:0016857,,,,,0.4071,,,,1,0.4071,0.1823,no
3BHD_KLEAE,P0DX23,ProtTale,Bacteria,337,Catalyzes the degradation of estradiol into estrone. Can also degrade testosterone.,"Involved in the biosynthesis of the osmoprotectant glycine betaine, which is active as a stress protectant. Catalyzes the second step in the biosynthesis of glycine betaine, the NAD(P)H-dependent reductive activation of choline.",No,No,No,No,No,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1823,no
3BHD_KLEAE,P0DX23,Protein2Text,Bacteria,337,Catalyzes the degradation of estradiol into estrone. Can also degrade testosterone.,"The molecular function of this protein is likely to be a transferase, specifically a short-chain dehydrogenase/reductase, as it is involved in the biosynthesis of a compound and the term ""transferase"" is associated with enzymes that catalyze the transfer of a group from one molecule to another.",Vague,Vague,Maybe,Vague,Vague,not-Yes,GO:0016491,GO:0016491,,GO:0016491,,GO:0016491,1.0,,1.0,,1.0,3,1.0,0.1823,no
3BHD_KLEAE,P0DX23,Reference,Bacteria,337,Catalyzes the degradation of estradiol into estrone. Can also degrade testosterone.,Catalyzes the degradation of estradiol into estrone. Can also degrade testosterone.,,,,,,,GO:0016491,GO:0016616,GO:0016491,GO:0016491,GO:0016616,GO:0016616,0.6897,1.0,1.0,0.6897,0.6897,5,0.8138,0.1823,no
CLADH_LACPN,P0DX40,ESM2Text,Bacteria,286,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-DH catalyzes the dehydrogenation/reduction steps in the production of 10-oxo-(12Z)- octadecenoate, 10-hydroxy-(11E)-octadecenoate and 10- hydroxyoctadecanoate during linoleate metabolism. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome.","Long-chain fatty acid epoxidase/dehydrogenase involved in the degradation of long-chain fatty acids. Isynurenine is the preferred substrate, but it can also use hexadecenal, hexadecanal, myristate and palatinate as substrates. Activity is highest with myristate, followed by palatinate and the corresponding decreases. Activity is also observed with tetradecanate and, to a lesser extent, with tetradecanate. Involved in the initial step of the phase-B biosynthesis of the polyketide antibiotic bilinomycin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016616,,GO:0016491,,,,,0.6897,,,,1,0.6897,0.1661,no
CLADH_LACPN,P0DX40,Prot2Text,Bacteria,286,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-DH catalyzes the dehydrogenation/reduction steps in the production of 10-oxo-(12Z)- octadecenoate, 10-hydroxy-(11E)-octadecenoate and 10- hydroxyoctadecanoate during linoleate metabolism. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome.",Catalyzes the oxidation of cyclopentanol to cyclopentanone in the biosynthesis of cyclopentanol antibiotic.,No,No,No,No,No,not-Yes,GO:0016616,GO:0016614,GO:0016614,GO:0016614,GO:0016614,GO:0016614,0.8416,0.8416,0.8416,0.8416,0.8416,5,0.8416,0.1661,no
CLADH_LACPN,P0DX40,ProtT3,Bacteria,286,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-DH catalyzes the dehydrogenation/reduction steps in the production of 10-oxo-(12Z)- octadecenoate, 10-hydroxy-(11E)-octadecenoate and 10- hydroxyoctadecanoate during linoleate metabolism. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome.",Belongs to the short-chain dehydrogenases/reductases (SDR) family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016616,GO:0016491,GO:0016491,,,,0.6897,0.6897,,,,2,0.6897,0.1661,no
CLADH_LACPN,P0DX40,ProtTale,Bacteria,286,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-DH catalyzes the dehydrogenation/reduction steps in the production of 10-oxo-(12Z)- octadecenoate, 10-hydroxy-(11E)-octadecenoate and 10- hydroxyoctadecanoate during linoleate metabolism. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome.",Catalyzes the oxidation of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4- phosphate (MEP).,No,No,No,No,No,not-Yes,GO:0016616,GO:0030604,GO:0030604,GO:0016491,GO:0030604,GO:0030604,0.8582,0.8582,0.6897,0.8582,0.8582,5,0.8245,0.1661,no
CLADH_LACPN,P0DX40,Protein2Text,Bacteria,286,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-DH catalyzes the dehydrogenation/reduction steps in the production of 10-oxo-(12Z)- octadecenoate, 10-hydroxy-(11E)-octadecenoate and 10- hydroxyoctadecanoate during linoleate metabolism. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome.","This protein is involved in the molecular function of a beta-ketoacyl-CoA thiolase, which is a type of enzyme that catalyzes the thiolysis of beta-ketoacyl-CoA into acetyl-CoA and an acyl-CoA. This enzyme plays a crucial role in the breakdown of fatty acids and the production of energy.",No,No,Vague,No,No,not-Yes,GO:0016616,GO:0003988,GO:0003988,GO:0003988,GO:0003988,GO:0003988,0.2067,0.2067,0.2067,0.2067,0.2067,5,0.2067,0.1661,no
CLADH_LACPN,P0DX40,Reference,Bacteria,286,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-DH catalyzes the dehydrogenation/reduction steps in the production of 10-oxo-(12Z)- octadecenoate, 10-hydroxy-(11E)-octadecenoate and 10- hydroxyoctadecanoate during linoleate metabolism. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome.","Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-DH catalyzes the dehydrogenation/reduction steps in the production of 10-oxo-(12Z)- octadecenoate, 10-hydroxy-(11E)-octadecenoate and 10- hydroxyoctadecanoate during linoleate metabolism. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome.",,,,,,,GO:0016616,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.6897,0.6897,0.6897,0.6897,0.6897,5,0.6897,0.1661,no
CLADC_LACPN,P0DX41,ESM2Text,Bacteria,281,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-DC catalyzes the migration of the carbon-carbon double bond in 10-oxo-(12Z)-octadecenoate to produce 10-oxo-(11E)-octadecenoate, during linoleate metabolism. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome.",Hydrolyzes phosphonopyruvate.,No,No,No,No,No,not-Yes,GO:0016853; GO:0016829,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016787,0.5902,0.5902,0.5902,0.5902,0.5902,5,0.5902,0.1573,no
CLADC_LACPN,P0DX41,Prot2Text,Bacteria,281,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-DC catalyzes the migration of the carbon-carbon double bond in 10-oxo-(12Z)-octadecenoate to produce 10-oxo-(11E)-octadecenoate, during linoleate metabolism. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome.","Utilization of purines as secondary nitrogen sources, when primary sources are limiting.",No,No,No,No,No,not-Yes,GO:0016853; GO:0016829,,,,,,,,,,,0,,0.1573,no
CLADC_LACPN,P0DX41,ProtT3,Bacteria,281,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-DC catalyzes the migration of the carbon-carbon double bond in 10-oxo-(12Z)-octadecenoate to produce 10-oxo-(11E)-octadecenoate, during linoleate metabolism. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome.",Catalyzes the conversion of acetoacetate to acetone and carbon dioxide. Belongs to the ADC family,No,No,No,No,No,not-Yes,GO:0016853; GO:0016829,GO:0047601,GO:0047601,GO:0018807,GO:0016831,GO:0018802,0.3142,0.3142,0.4071,0.5955,0.0,5,0.3262,0.1573,no
CLADC_LACPN,P0DX41,ProtTale,Bacteria,281,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-DC catalyzes the migration of the carbon-carbon double bond in 10-oxo-(12Z)-octadecenoate to produce 10-oxo-(11E)-octadecenoate, during linoleate metabolism. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome.","Isomerase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS). SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms. These initial steps feature the priming of an unusual benzoic acid starter unit onto the highly reducing",No,No,No,Maybe,No,not-Yes,GO:0016853; GO:0016829,GO:0016853,GO:0016853,GO:0016853,GO:0016853,GO:0016853,0.8634,0.8634,0.8634,0.8634,0.8634,5,0.8634,0.1573,no
CLADC_LACPN,P0DX41,Protein2Text,Bacteria,281,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-DC catalyzes the migration of the carbon-carbon double bond in 10-oxo-(12Z)-octadecenoate to produce 10-oxo-(11E)-octadecenoate, during linoleate metabolism. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome.","This protein is involved in the molecular function of converting a substrate into a product through a series of chemical reactions, specifically involved in the biosynthesis of a particular compound.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016853; GO:0016829,,,,,,,,,,,0,,0.1573,no
CLADC_LACPN,P0DX41,Reference,Bacteria,281,"Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-DC catalyzes the migration of the carbon-carbon double bond in 10-oxo-(12Z)-octadecenoate to produce 10-oxo-(11E)-octadecenoate, during linoleate metabolism. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome.","Is involved in a saturation metabolic pathway of polyunsaturated fatty acids, that detoxifies unsaturated fatty acids and generates hydroxy fatty acids, oxo fatty acids, conjugated fatty acids such as conjugated linoleic acids (CLAs), and partially saturated trans-fatty acids as intermediates. CLA-DC catalyzes the migration of the carbon-carbon double bond in 10-oxo-(12Z)-octadecenoate to produce 10-oxo-(11E)-octadecenoate, during linoleate metabolism. As part of the gut microbiome, this enzyme modifies host fatty acid composition and is expected to improve human health by altering lipid metabolism related to the onset of metabolic syndrome.",,,,,,,GO:0016853; GO:0016829,GO:0016863,GO:0016853,GO:0016853,GO:0016853,GO:0016853,0.5955,0.8634,0.8634,0.8634,0.8634,5,0.8098,0.1573,no
TYRAP_CLODR,P0DX43,ESM2Text,Bacteria,251,Probably part of an ABC transporter complex involved in tyrosine uptake. May also import phenylalanine. Probably responsible for energy coupling to the transport system (Probable).,Part of the ABC transporter complex PhnCDE involved in phosphonates import. Responsible for energy coupling to the transport system.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,1.0,0.6869,1.0,1.0,1.0,5,0.9374,0.4092,no
TYRAP_CLODR,P0DX43,Prot2Text,Bacteria,251,Probably part of an ABC transporter complex involved in tyrosine uptake. May also import phenylalanine. Probably responsible for energy coupling to the transport system (Probable).,Part of the ABC transporter complex NikABCDE (Opp2) involved in nickel import. Probably responsible for energy coupling to the transport system.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887,GO:0016887,GO:0016887,GO:0016887,GO:0016887,GO:0016887; GO:0005524,0.6869,0.6869,0.6869,0.6869,1.0,5,0.7495,0.4092,no
TYRAP_CLODR,P0DX43,ProtT3,Bacteria,251,Probably part of an ABC transporter complex involved in tyrosine uptake. May also import phenylalanine. Probably responsible for energy coupling to the transport system (Probable).,Part of the ABC transporter complex LsrABCD involved in autoinducer 2 (AI-2) import. Responsible for energy coupling to the transport system. Cell membrane; Peripheral membrane protein. Belongs to the ABC transporter superfamily,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887,GO:0005524; GO:0016887,GO:0016887,GO:0016887,GO:0016887; GO:0005524,GO:0005524; GO:0016887,1.0,0.6869,0.6869,1.0,1.0,5,0.8748,0.4092,no
TYRAP_CLODR,P0DX43,ProtTale,Bacteria,251,Probably part of an ABC transporter complex involved in tyrosine uptake. May also import phenylalanine. Probably responsible for energy coupling to the transport system (Probable).,Part of the ABC transporter complex ThiBPQ involved in thiamine import. Responsible for energy coupling to the transport system.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016887,GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0016887,1.0,1.0,1.0,1.0,0.6869,5,0.9374,0.4092,no
TYRAP_CLODR,P0DX43,Protein2Text,Bacteria,251,Probably part of an ABC transporter complex involved in tyrosine uptake. May also import phenylalanine. Probably responsible for energy coupling to the transport system (Probable).,"This protein is part of the ABC transporter complex, which is involved in the transport of molecules across cell membranes. More specifically, it is likely involved in the transport of a particular type of molecule, such as a sugar, amino acid, or metal ion. However, without more information, it is difficult to determine the exact molecular function of this protein.",Vague,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0005524; GO:0016887,GO:0016887,GO:0005524,GO:0042626,,GO:0042626,0.6869,0.6869,0.1952,,0.1952,4,0.441,0.4092,no
TYRAP_CLODR,P0DX43,Reference,Bacteria,251,Probably part of an ABC transporter complex involved in tyrosine uptake. May also import phenylalanine. Probably responsible for energy coupling to the transport system (Probable).,Probably part of an ABC transporter complex involved in tyrosine uptake. May also import phenylalanine. Probably responsible for energy coupling to the transport system (Probable).,,,,,,,GO:0005524; GO:0016887,GO:0016887,GO:0016887,,,GO:0016887,0.6869,0.6869,,,0.6869,3,0.6869,0.4092,no
RTCB2_ECOS1,P0DX91,ESM2Text,Bacteria,379,"GTP-dependent RNA ligase involved in rRNA repair. Repairs damaged 16S rRNA in 30S subunits that has been cleaved between adenine-1493 and guanosine-1494 (E.coli nubering). This specific cleavage is inflicted by CdiA (ECL_04451) or by colicin E3-type (ColE3) proteins. Poorly repairs damaged rRNA in the 70S ribosome; addition of release factor PrfH improves repair about 3-fold in vitro, probably because PrfH hydrolyzes the nascent chain allowing ribosomal subunit dissociation. In vivo the PrfH-RtcB2 pair restores growth in the presence of ribotoxins that specifically create this damage. Does not repair damaged tRNA (tested with tRNA(Asp) and tRNA(Arg)).","Responsible for the hydrolysis of cyanuric acid, an intermediate formed during catabolism of s-triazine based compounds in herbicides such as atrazine and polymers such as melamine. Catalyzes the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6-trihydroxy-s-triazine) to yield carbon dioxide and carboxybiuret, which spontaneously decarboxylates to biuret. Only active on cyanuric acid and not active on alkyl hydroxyisomers.",No,No,No,No,No,not-Yes,GO:0005525; GO:0046872; GO:0003972; GO:0170057,GO:0016787,GO:0016810,GO:0016810,GO:0016787,GO:0016810,0.2284,0.1854,0.1854,0.2284,0.1854,5,0.2026,0.5503,yes
RTCB2_ECOS1,P0DX91,Prot2Text,Bacteria,379,"GTP-dependent RNA ligase involved in rRNA repair. Repairs damaged 16S rRNA in 30S subunits that has been cleaved between adenine-1493 and guanosine-1494 (E.coli nubering). This specific cleavage is inflicted by CdiA (ECL_04451) or by colicin E3-type (ColE3) proteins. Poorly repairs damaged rRNA in the 70S ribosome; addition of release factor PrfH improves repair about 3-fold in vitro, probably because PrfH hydrolyzes the nascent chain allowing ribosomal subunit dissociation. In vivo the PrfH-RtcB2 pair restores growth in the presence of ribotoxins that specifically create this damage. Does not repair damaged tRNA (tested with tRNA(Asp) and tRNA(Arg)).","Mediates the hydrolysis of agmatine into N-carbamoylputrescine in the arginine decarboxylase (ADC) pathway of putrescine biosynthesis, a basic polyamine.",No,No,No,No,No,not-Yes,GO:0005525; GO:0046872; GO:0003972; GO:0170057,GO:0016787,GO:0008784,GO:0016787,GO:0008783,GO:0043862,0.2284,0.1159,0.2284,0.1326,0.0674,5,0.1545,0.5503,yes
RTCB2_ECOS1,P0DX91,ProtT3,Bacteria,379,"GTP-dependent RNA ligase involved in rRNA repair. Repairs damaged 16S rRNA in 30S subunits that has been cleaved between adenine-1493 and guanosine-1494 (E.coli nubering). This specific cleavage is inflicted by CdiA (ECL_04451) or by colicin E3-type (ColE3) proteins. Poorly repairs damaged rRNA in the 70S ribosome; addition of release factor PrfH improves repair about 3-fold in vitro, probably because PrfH hydrolyzes the nascent chain allowing ribosomal subunit dissociation. In vivo the PrfH-RtcB2 pair restores growth in the presence of ribotoxins that specifically create this damage. Does not repair damaged tRNA (tested with tRNA(Asp) and tRNA(Arg)).","Catalyzes the transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of a sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS. Cytoplasm. Belongs to the ThiI family",No,No,No,No,No,not-Yes,GO:0005525; GO:0046872; GO:0003972; GO:0170057,GO:0016783,GO:0016783,GO:0016783,GO:0016783,GO:0016783,0.1549,0.1549,0.1549,0.1549,0.1549,5,0.1549,0.5503,yes
RTCB2_ECOS1,P0DX91,ProtTale,Bacteria,379,"GTP-dependent RNA ligase involved in rRNA repair. Repairs damaged 16S rRNA in 30S subunits that has been cleaved between adenine-1493 and guanosine-1494 (E.coli nubering). This specific cleavage is inflicted by CdiA (ECL_04451) or by colicin E3-type (ColE3) proteins. Poorly repairs damaged rRNA in the 70S ribosome; addition of release factor PrfH improves repair about 3-fold in vitro, probably because PrfH hydrolyzes the nascent chain allowing ribosomal subunit dissociation. In vivo the PrfH-RtcB2 pair restores growth in the presence of ribotoxins that specifically create this damage. Does not repair damaged tRNA (tested with tRNA(Asp) and tRNA(Arg)).",Regulates the transcription of the selenocysteine insertion sequence (SECIS) element.,No,No,No,No,No,not-Yes,GO:0005525; GO:0046872; GO:0003972; GO:0170057,GO:0003700,,,,,0.1338,,,,,1,0.1338,0.5503,yes
RTCB2_ECOS1,P0DX91,Protein2Text,Bacteria,379,"GTP-dependent RNA ligase involved in rRNA repair. Repairs damaged 16S rRNA in 30S subunits that has been cleaved between adenine-1493 and guanosine-1494 (E.coli nubering). This specific cleavage is inflicted by CdiA (ECL_04451) or by colicin E3-type (ColE3) proteins. Poorly repairs damaged rRNA in the 70S ribosome; addition of release factor PrfH improves repair about 3-fold in vitro, probably because PrfH hydrolyzes the nascent chain allowing ribosomal subunit dissociation. In vivo the PrfH-RtcB2 pair restores growth in the presence of ribotoxins that specifically create this damage. Does not repair damaged tRNA (tested with tRNA(Asp) and tRNA(Arg)).","This protein is likely a DNA repair enzyme, specifically a nucleotidyltransferase that catalyzes the addition of nucleotides to a DNA molecule.",No,Maybe,Maybe,No,No,not-Yes,GO:0005525; GO:0046872; GO:0003972; GO:0170057,GO:0016779,GO:0016779,GO:0016779,GO:0016779,GO:0016779,0.1549,0.1549,0.1549,0.1549,0.1549,5,0.1549,0.5503,yes
RTCB2_ECOS1,P0DX91,Reference,Bacteria,379,"GTP-dependent RNA ligase involved in rRNA repair. Repairs damaged 16S rRNA in 30S subunits that has been cleaved between adenine-1493 and guanosine-1494 (E.coli nubering). This specific cleavage is inflicted by CdiA (ECL_04451) or by colicin E3-type (ColE3) proteins. Poorly repairs damaged rRNA in the 70S ribosome; addition of release factor PrfH improves repair about 3-fold in vitro, probably because PrfH hydrolyzes the nascent chain allowing ribosomal subunit dissociation. In vivo the PrfH-RtcB2 pair restores growth in the presence of ribotoxins that specifically create this damage. Does not repair damaged tRNA (tested with tRNA(Asp) and tRNA(Arg)).","GTP-dependent RNA ligase involved in rRNA repair. Repairs damaged 16S rRNA in 30S subunits that has been cleaved between adenine-1493 and guanosine-1494 (E.coli nubering). This specific cleavage is inflicted by CdiA (ECL_04451) or by colicin E3-type (ColE3) proteins. Poorly repairs damaged rRNA in the 70S ribosome; addition of release factor PrfH improves repair about 3-fold in vitro, probably because PrfH hydrolyzes the nascent chain allowing ribosomal subunit dissociation. In vivo the PrfH-RtcB2 pair restores growth in the presence of ribotoxins that specifically create this damage. Does not repair damaged tRNA (tested with tRNA(Asp) and tRNA(Arg)).",,,,,,,GO:0005525; GO:0046872; GO:0003972; GO:0170057,GO:0003972,GO:0003972; GO:0005525,GO:0003972; GO:0005525,GO:0003972,GO:0003972,0.5843,0.847,0.847,0.5843,0.5843,5,0.6894,0.5503,yes
RTCB1_ECOS1,P0DX92,ESM2Text,Bacteria,408,"GTP-dependent RNA ligase that is involved in RNA repair. Joins RNA with 2',3'-cyclic-phosphate or 3'-phosphate ends to RNA with 5'-hydroxy ends. GTP-dependent RNA ligase that is involved in tRNA repair. Repairs broken tRNA(Asp) and tRNA(Arg) that have been cleaved by colicin E5 or colicin D, respectively. Does not repair damaged 16S rRNA in 30S ribosomal subunits.",Shell component of a type 2A encapsulin nanocompartment. Shell probably binds RuBisCO small and large subunits and is probably not functional by itself. Both components probably transfer electrons to the same molecular chaperone. Can also displace RuBisCO and CO when both components are in an active state. Both components have low intrinsic ATPase activity; the catalytic subunit probably binds 2 quinones per subunit.,No,No,No,No,No,not-Yes,GO:0003909; GO:0005525; GO:0030145; GO:0170057,,,,,,,,,,,0,,0.723,yes
RTCB1_ECOS1,P0DX92,Prot2Text,Bacteria,408,"GTP-dependent RNA ligase that is involved in RNA repair. Joins RNA with 2',3'-cyclic-phosphate or 3'-phosphate ends to RNA with 5'-hydroxy ends. GTP-dependent RNA ligase that is involved in tRNA repair. Repairs broken tRNA(Asp) and tRNA(Arg) that have been cleaved by colicin E5 or colicin D, respectively. Does not repair damaged 16S rRNA in 30S ribosomal subunits.",Bifunctional enzyme that catalyzes two sequential steps in de novo purine nucleotide biosynthesis.,No,No,No,No,No,not-Yes,GO:0003909; GO:0005525; GO:0030145; GO:0170057,,,,,,,,,,,0,,0.723,yes
RTCB1_ECOS1,P0DX92,ProtT3,Bacteria,408,"GTP-dependent RNA ligase that is involved in RNA repair. Joins RNA with 2',3'-cyclic-phosphate or 3'-phosphate ends to RNA with 5'-hydroxy ends. GTP-dependent RNA ligase that is involved in tRNA repair. Repairs broken tRNA(Asp) and tRNA(Arg) that have been cleaved by colicin E5 or colicin D, respectively. Does not repair damaged 16S rRNA in 30S ribosomal subunits.",RNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Cytoplasm. Belongs to the eukaryotic RpoG1/RpoG2 RNA polymerase subunit family,No,No,No,No,No,not-Yes,GO:0003909; GO:0005525; GO:0030145; GO:0170057,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.2058,0.2058,0.2058,0.2058,0.2058,5,0.2058,0.723,yes
RTCB1_ECOS1,P0DX92,ProtTale,Bacteria,408,"GTP-dependent RNA ligase that is involved in RNA repair. Joins RNA with 2',3'-cyclic-phosphate or 3'-phosphate ends to RNA with 5'-hydroxy ends. GTP-dependent RNA ligase that is involved in tRNA repair. Repairs broken tRNA(Asp) and tRNA(Arg) that have been cleaved by colicin E5 or colicin D, respectively. Does not repair damaged 16S rRNA in 30S ribosomal subunits.","Catalyzes the formation of 5-(hydroxymethyl)-D-ribose 1-phosphate, an intermediate in the biosynthesis of D-ribose 5-phosphate and 1D,2D-diacylglycerol (DAG).",No,No,No,No,No,not-Yes,GO:0003909; GO:0005525; GO:0030145; GO:0170057,,,,,,,,,,,0,,0.723,yes
RTCB1_ECOS1,P0DX92,Protein2Text,Bacteria,408,"GTP-dependent RNA ligase that is involved in RNA repair. Joins RNA with 2',3'-cyclic-phosphate or 3'-phosphate ends to RNA with 5'-hydroxy ends. GTP-dependent RNA ligase that is involved in tRNA repair. Repairs broken tRNA(Asp) and tRNA(Arg) that have been cleaved by colicin E5 or colicin D, respectively. Does not repair damaged 16S rRNA in 30S ribosomal subunits.","Based on the name of the protein, it is likely involved in the synthesis or modification of nucleotides, specifically a type of nucleotide called guanosine. 

A more specific function of this protein would be:

Catalyzes the deamination of nucleoside 5'-monophosphates containing purine or pyrimidine bases, with a preference for deoxyribonucleotides (PubMed:11971855, PubMed:14702076). Has a broad substrate specificity, with a preference for deoxyribonucleoside monophosphates (dNMPs) and, to a lesser extent, ribonucleoside monophosphates (NMPs) (PubMed:11971855, PubMed:14702076). Also able to deaminate dUTP, dCMP and dTMP to dUMP, dCMP and dTMP, respectively (PubMed:14702076). Shows a preference for substrates with a 2'-deoxyribose sugar (PubMed:11971855, PubMed:14702076). Has no activity on nucleoside triphosphates, nucleoside diphosphates or nucleoside monophosphates (PubMed:14702076). Catalyzes the deamination of 2'-deoxyinosine 5'-monophosphate (dIMP) to 2'-deoxyuridine 5'-monophosphate (dUMP). Does not show activity on 2'-deoxyguanosine 5'-monophosphate (dGMP) and 2'-deoxythymidine 5'-monophosphate (dTMP). Deaminates the 6-oxopurine base of 2'-deoxycytidine 5'-monophosphate (dCMP) to 2'-deoxyuridine 5'-monophosphate (dUMP). Does not show activity on 2'-deoxycytidine 5'-triphosphate (dCTP), 2'-deoxycytidine 5'-diphosphate (dCDP) and 2'-deoxycytidine 5'-monophosphate (dCMP). Also able to deaminate dUMP and dTMP to dUMP and dTMP, respectively (PubMed:14702076)..",Vague,No,Maybe,No,No,not-Yes,GO:0003909; GO:0005525; GO:0030145; GO:0170057,GO:0019239,GO:0019239,,GO:0019239,GO:0019239,0.1599,0.1599,,0.1599,0.1599,4,0.1599,0.723,yes
RTCB1_ECOS1,P0DX92,Reference,Bacteria,408,"GTP-dependent RNA ligase that is involved in RNA repair. Joins RNA with 2',3'-cyclic-phosphate or 3'-phosphate ends to RNA with 5'-hydroxy ends. GTP-dependent RNA ligase that is involved in tRNA repair. Repairs broken tRNA(Asp) and tRNA(Arg) that have been cleaved by colicin E5 or colicin D, respectively. Does not repair damaged 16S rRNA in 30S ribosomal subunits.","GTP-dependent RNA ligase that is involved in RNA repair. Joins RNA with 2',3'-cyclic-phosphate or 3'-phosphate ends to RNA with 5'-hydroxy ends. GTP-dependent RNA ligase that is involved in tRNA repair. Repairs broken tRNA(Asp) and tRNA(Arg) that have been cleaved by colicin E5 or colicin D, respectively. Does not repair damaged 16S rRNA in 30S ribosomal subunits.",,,,,,,GO:0003909; GO:0005525; GO:0030145; GO:0170057,GO:0003972,GO:0003972; GO:0005525,GO:0003972; GO:0005525,GO:0003972,GO:0003972,0.4516,0.7294,0.7294,0.4516,0.4516,5,0.5627,0.723,yes
CDNE_STAHA,P0DXA9,ESM2Text,Bacteria,300,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type I-B CBASS system.","Cyclic dinucleotide synthase that catalyzes the synthesis of c-di-GMP, has no activity with other NTP substrates.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0000166; GO:0016779; GO:0003723,GO:0052621,GO:0052621,GO:0052621,GO:0052621,GO:0052621,0.4071,0.4071,0.4071,0.4071,0.4071,5,0.4071,0.5436,yes
CDNE_STAHA,P0DXA9,Prot2Text,Bacteria,300,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type I-B CBASS system.","Cyclic dinucleotide synthase that catalyzes the synthesis of c-di-GMP, has no activity with other NTP substrates.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0000166; GO:0016779; GO:0003723,GO:0052621,GO:0052621,GO:0052621,GO:0052621,GO:0052621,0.4071,0.4071,0.4071,0.4071,0.4071,5,0.4071,0.5436,yes
CDNE_STAHA,P0DXA9,ProtT3,Bacteria,300,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type I-B CBASS system.","CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection (By similarity). CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0000166; GO:0016779; GO:0003723,GO:0016779,GO:0016779,GO:0016779,GO:0016779,GO:0016779,0.4739,0.4739,0.4739,0.4739,0.4739,5,0.4739,0.5436,yes
CDNE_STAHA,P0DXA9,ProtTale,Bacteria,300,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type I-B CBASS system.","Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type I-D(GG) CBASS system.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0000166; GO:0016779; GO:0003723,GO:0016779,GO:0016779,GO:0016779,GO:0016779,GO:0016779,0.4739,0.4739,0.4739,0.4739,0.4739,5,0.4739,0.5436,yes
CDNE_STAHA,P0DXA9,Protein2Text,Bacteria,300,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type I-B CBASS system.","The molecular function of this protein is an endonuclease that plays a crucial role in the replication of the genome of a virus. Specifically, it is involved in the replication of the viral genome, which is a process essential for the virus to replicate and spread. The protein is likely responsible for cleaving viral DNA or RNA, which is a necessary step in the replication process. This protein is likely to be a key enzyme in the viral life cycle, and its activity is essential for the virus to survive and replicate. 
The molecular function of this protein is also related to the inhibition of the host cell's ability to repair DNA damage, which is another way the virus can evade the host's immune system. By inhibiting the host cell's DNA repair mechanisms, the virus can increase its chances of survival and replication. 
In addition, the protein may also have a role in the regulation of the host cell's immune response, by modulating the expression of immune-related genes or by interacting with immune proteins. This could be another way the virus evades the host's immune system and increases its chances of survival and replication. 
Overall, the molecular function of this protein is likely to be multifaceted and complex, involving a range of different processes related to viral replication, DNA repair, and immune evasion.",No,No,No,No,No,not-Yes,GO:0046872; GO:0000166; GO:0016779; GO:0003723,GO:0004519,GO:0004519,GO:0004519,GO:0004519,GO:0004519,0.1835,0.1835,0.1835,0.1835,0.1835,5,0.1835,0.5436,yes
CDNE_STAHA,P0DXA9,Reference,Bacteria,300,"Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type I-B CBASS system.","Cyclic nucleotide synthase (second messenger synthase) of a CBASS antivirus system. CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type I-B CBASS system.",,,,,,,GO:0046872; GO:0000166; GO:0016779; GO:0003723,GO:0016779,GO:0016779,GO:0016779,GO:0016779,GO:0016779,0.4739,0.4739,0.4739,0.4739,0.4739,5,0.4739,0.5436,yes
CGLR_TRIPJ,P0DXB4,ESM2Text,Eukaryota,485,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Intracellular 3'-5' RNA polymerase that plays a key role in cellular processes such as pre-mRNA splicing, cell cycle progression and DNA replication. In addition, it may also play a role in mRNA stability by binding to the 3' end of its mRNA and stabilizing the polymerase at the 3' end. Modulates the 3' end-binding properties of nucleotides by binding to nicks in the RNA or microRNAs and preventing nucleotid adenylation. Required for post-transcriptional gene silencing (PTGS) by the RNA-induced silencing complex (RISC) and the consequent binding of RISC to a localized region leading to silencing. Component of the RNase MRP complex which has 3' end-directed DNA synthesis (DDR) activity and is involved in rDNA nucleotide excision repair (NER) by cleaving nucleotides in the 3' single-strand/single-strand annealing (SSA) region. Also plays a role in DNA replication by binding to replication origins and facilitating replication fork progression between non-replicating DNA (i.e. replication forks) at stalled replication forks. Also plays a role in double-strand break",No,No,No,No,No,not-Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0003725,GO:0003725,GO:0003725,GO:0003725,GO:0003725,0.1694,0.1694,0.1694,0.1694,0.1694,5,0.1694,0.5611,yes
CGLR_TRIPJ,P0DXB4,Prot2Text,Eukaryota,485,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",Nuclease that resolves Holliday junction intermediates made during DNA replication or induced by DNA-damaging agents. Cleaves mobile four-strand junctions by introducing symmetrical nicks in two strands. Promotes annealing of linear ssDNA with homologous dsDNA.,No,No,No,No,No,not-Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0016779,,,,,0.3478,,,,,1,0.3478,0.5611,yes
CGLR_TRIPJ,P0DXB4,ProtT3,Eukaryota,485,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP or cGAMP) from ATP and GTP and plays a key role in innate immunity (By similarity). Catalyzes the formation of 2',3'-cGAMP from ATP and GTP in a two-step reaction (By similarity). The first step is catalyzed by the guanylyltransferase activity of the N-terminal catalytic domain (NTD), generating the intermediate 2',3'-cyclic GMP-AMP (2',3'-",Yes,Yes,Yes,Yes,Yes,Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0016779; GO:0005525; GO:0005524,GO:0016779,GO:0016779,GO:0016779,GO:0016779,0.8281,0.3478,0.3478,0.3478,0.3478,5,0.4439,0.5611,yes
CGLR_TRIPJ,P0DXB4,ProtTale,Eukaryota,485,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Synthesizes 2',3'-cGAMP in a two-step reaction through production of the linear intermediate pppA(2'-5')pG. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of",Yes,Yes,Yes,Yes,Yes,Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,0.3772,0.3772,0.3772,0.3772,0.3772,5,0.3772,0.5611,yes
CGLR_TRIPJ,P0DXB4,Protein2Text,Eukaryota,485,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","This protein is a Nucleotide-binding adapter molecule that binds to the Nucleoside triphosphate (NTP) molecule. It is involved in the activation of the Nucleotide-binding oligomerization domain (NOD) protein, which plays a role in the innate immune response. The molecular function of this protein is to bind to NTP molecules and activate the NOD protein, leading to the activation of downstream signaling pathways.",No,Maybe,Maybe,No,Maybe,not-Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.1786,0.1786,0.1786,0.1786,0.1786,5,0.1786,0.5611,yes
CGLR_TRIPJ,P0DXB4,Reference,Eukaryota,485,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",,,,,,,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0016779,GO:0016779; GO:0005524; GO:0005525,GO:0016779,GO:0016779,GO:0016779,0.3478,0.8281,0.3478,0.3478,0.3478,5,0.4439,0.5611,yes
CGLR_CTEFE,P0DXB5,ESM2Text,Eukaryota,435,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Does not have 2'-5'-olygoadenylate synthetase activity, but can bind double-stranded RNA. Active in the absence of replication protein A (RPA).",No,No,No,No,No,not-Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0003725,GO:0003725,GO:0003725,GO:0003725,GO:0003725,0.1694,0.1694,0.1694,0.1694,0.1694,5,0.1694,0.54,yes
CGLR_CTEFE,P0DXB5,Prot2Text,Eukaryota,435,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Cyclic dinucleotide synthase that catalyzes the synthesis of 3'3'-cyclic UMP-UMP (cUMP-UMP) as the major product, and of 3'3'-cUMP-UMP-GTP (cGMP) as a minor product, that are second messengers for cell signal transduction.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0016779,,,,,0.3478,,,,,1,0.3478,0.54,yes
CGLR_CTEFE,P0DXB5,ProtT3,Eukaryota,435,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity (By similarity). Catalyzes the formation of 2',3'-cGAMP from ATP and GTP in a two-step reaction (By similarity). In the first step, 2',3'-cGAMP is formed by condensation of ATP and GTP (By similarity). In the second step, 2',3'-cGAMP is converted into cyclic GMP-AMP",Yes,Yes,Yes,Yes,Yes,Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0016779; GO:0005525; GO:0005524,GO:0016779,GO:0016779,GO:0016779,GO:0016779,0.8281,0.3478,0.3478,0.3478,0.3478,5,0.4439,0.54,yes
CGLR_CTEFE,P0DXB5,ProtTale,Eukaryota,435,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,0.3772,0.3772,0.3772,0.3772,0.3772,5,0.3772,0.54,yes
CGLR_CTEFE,P0DXB5,Protein2Text,Eukaryota,435,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","This protein is a kinase, which means it has a molecular function of transferring a phosphate group to another molecule. Specifically, it is a serine/threonine-protein kinase, which is a type of kinase that adds phosphate groups to serine or threonine residues on target proteins.",No,No,No,No,No,not-Yes,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.1786,0.1786,0.1786,0.1786,0.1786,5,0.1786,0.54,yes
CGLR_CTEFE,P0DXB5,Reference,Eukaryota,435,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",,,,,,,GO:0061501; GO:0005524; GO:0005525; GO:0046872,GO:0016779,GO:0016779; GO:0005524; GO:0005525,GO:0016779,GO:0016779,GO:0016779,0.3478,0.8281,0.3478,0.3478,0.3478,5,0.4439,0.54,yes
CGLR_MICDL,P0DXB6,ESM2Text,Eukaryota,520,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Active on RNA polymerase I (RNAPII) and RNA polymerase III (RNAPIII) substrates, although less active than NAPII for most substrates. In contrast, the ATPase activity is not influenced by RNAPII.",No,No,No,No,No,not-Yes,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,GO:0052621,GO:0052621,GO:0052621,GO:0052621,GO:0052621,0.2426,0.2426,0.2426,0.2426,0.2426,5,0.2426,0.4052,no
CGLR_MICDL,P0DXB6,Prot2Text,Eukaryota,520,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Protects E.coli against phage infection. When capV and dncV are introduced in E.coli MG1655 there is 1000-fold protection against phage P1; protection against other phage (T2, T4, T5 and lambda-vir) requires the 2 subsequent genes. Activation leads to bacterial cell lysis and death which occurs before the phage has finished its replication cycle, thus protecting non-infected bacteria by aborting the phage infection and preventing its propagation.",Maybe,No,No,No,No,not-Yes,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,GO:0004519,,GO:0004519,,,0.1303,,0.1303,,,2,0.1303,0.4052,no
CGLR_MICDL,P0DXB6,ProtT3,Eukaryota,520,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity (By similarity). 2',3'-cGAMP is a second messenger that is generated in response to viral infection and other stresses and acts as a ligand for cGAS (By similarity). 2',3'-cGAMP binds to and activates cGAS (By similarity). In turn, cGAS produces cyclic di-AMP (c-diAMP), a second messenger that",Yes,Yes,Yes,Yes,Yes,Yes,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,GO:0016779; GO:0005525; GO:0005524,GO:0016779,GO:0016779,GO:0016779,GO:0016779,0.6782,0.2867,0.2867,0.2867,0.2867,5,0.365,0.4052,no
CGLR_MICDL,P0DXB6,ProtTale,Eukaryota,520,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Catalysis involves the formation of a phosphodiester linkage, yielding cyclic N(6)-triphosphate,5'-triphosphate (pppG), and pppG. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the innate immune response. Acts by catalyzing the formation of 2',3'-c",Yes,Yes,Yes,Yes,Yes,Yes,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,0.5219,0.5219,0.5219,0.5219,0.5219,5,0.5219,0.4052,no
CGLR_MICDL,P0DXB6,Protein2Text,Eukaryota,520,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","This protein is a type of RNA-dependent protein kinase, which is involved in the innate immune response to viral infections. Specifically, it is a serine/threonine protein kinase that plays a role in the activation of interferon and other signaling pathways in response to viral RNA.",No,No,No,No,No,not-Yes,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,GO:0000166,GO:0003676,,,GO:0003723,0.3804,0.4583,,,0.4691,3,0.4359,0.4052,no
CGLR_MICDL,P0DXB6,Reference,Eukaryota,520,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",,,,,,,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,GO:0016779; GO:0003725,GO:0016779; GO:0005524; GO:0005525; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,0.5219,0.7944,0.5219,0.5219,0.5219,5,0.5764,0.4052,no
CGLR_NICVS,P0DXB7,ESM2Text,Eukaryota,353,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Cyclic dinucleotide synthase that catalyzes the synthesis of c-di-GMP, has no activity with other NTP substrates.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,GO:0052621,GO:0052621,GO:0052621,GO:0052621,GO:0052621,0.2426,0.2426,0.2426,0.2426,0.2426,5,0.2426,0.5623,yes
CGLR_NICVS,P0DXB7,Prot2Text,Eukaryota,353,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). This protein plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity.",No,No,No,No,No,not-Yes,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,GO:0004519,,GO:0004519,,,0.1303,,0.1303,,,2,0.1303,0.5623,yes
CGLR_NICVS,P0DXB7,ProtT3,Eukaryota,353,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity (By similarity). 2',3'-cGAMP is a second messenger that is generated in response to infection and other stresses and acts as a ligand for cGAS (By similarity). In response to 2',3'-cGAMP, cGAS catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP (By similarity)",Yes,Yes,Yes,Yes,Yes,Yes,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,GO:0016779; GO:0005525; GO:0005524,GO:0016779,GO:0016779,GO:0016779,GO:0016779,0.6782,0.2867,0.2867,0.2867,0.2867,5,0.365,0.5623,yes
CGLR_NICVS,P0DXB7,ProtTale,Eukaryota,353,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (3',2'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Synthesizes 3',2'-cGAMP in a two-step reaction through production of the linear intermediate pppA(2'-5')pG. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune response. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of",Yes,Yes,Yes,Yes,Yes,Yes,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,0.5219,0.5219,0.5219,0.5219,0.5219,5,0.5219,0.5623,yes
CGLR_NICVS,P0DXB7,Protein2Text,Eukaryota,353,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","This protein is a nucleotide-binding protein, specifically a cytosolic sensor of viral nucleic acids. It is involved in the detection of viral nucleic acids and the subsequent activation of antiviral immune responses.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,GO:0000166,GO:0003676,,,GO:0003723,0.3804,0.4583,,,0.4691,3,0.4359,0.5623,yes
CGLR_NICVS,P0DXB7,Reference,Eukaryota,353,"Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",,,,,,,GO:0061501; GO:0005524; GO:0003690; GO:0005525; GO:0046872; GO:0003723,GO:0016779; GO:0003725,GO:0016779; GO:0005524; GO:0005525; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,0.5219,0.7944,0.5219,0.5219,0.5219,5,0.5764,0.5623,yes
CGLR3_STYPI,P0DXC0,ESM2Text,Eukaryota,340,"Nucleotidyltransferase that catalyzes the formation of cyclic di-AMP (3',3'-c-di-AMP) from 2 molecules of ATP and plays a key role in innate immunity. Acts as a key sensor of double- stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 3',3'-c-di-AMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",Probable nucleotidyltransferase that catalyzes the formation of cyclic dinucleotide second messenger in response to some unknown stimulus.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0106408; GO:0003690; GO:0005525; GO:0046872; GO:0016779,GO:0016779,GO:0016779,GO:0016779,,GO:0016779,0.4587,0.4587,0.4587,,0.4587,4,0.4587,0.6643,yes
CGLR3_STYPI,P0DXC0,Prot2Text,Eukaryota,340,"Nucleotidyltransferase that catalyzes the formation of cyclic di-AMP (3',3'-c-di-AMP) from 2 molecules of ATP and plays a key role in innate immunity. Acts as a key sensor of double- stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 3',3'-c-di-AMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Terminal uridylyltransferase which, specifically, catalyzes the addition of Us to the 3'-hydroxyl group of single-stranded RNAs with a 3'-terminal U.",No,No,No,No,No,not-Yes,GO:0005524; GO:0106408; GO:0003690; GO:0005525; GO:0046872; GO:0016779,GO:0016779,GO:0016779,GO:0016779,GO:0016779,GO:0016779,0.4587,0.4587,0.4587,0.4587,0.4587,5,0.4587,0.6643,yes
CGLR3_STYPI,P0DXC0,ProtT3,Eukaryota,340,"Nucleotidyltransferase that catalyzes the formation of cyclic di-AMP (3',3'-c-di-AMP) from 2 molecules of ATP and plays a key role in innate immunity. Acts as a key sensor of double- stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 3',3'-c-di-AMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity (By similarity). 2',3'-cGAMP is a second messenger that binds to and activates the DNA sensor cGAS (By similarity). Binding of 2',3'-cGAMP to cGAS leads to its activation and subsequent synthesis of cyclic GMP-AMP (cGAMP), a second messenger that binds to and activates the DNA sensor cGAS (By similarity)",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0106408; GO:0003690; GO:0005525; GO:0046872; GO:0016779,GO:0016779; GO:0005525; GO:0005524,GO:0016779,GO:0016779,GO:0016779,GO:0016779,0.8099,0.4587,0.4587,0.4587,0.4587,5,0.5289,0.6643,yes
CGLR3_STYPI,P0DXC0,ProtTale,Eukaryota,340,"Nucleotidyltransferase that catalyzes the formation of cyclic di-AMP (3',3'-c-di-AMP) from 2 molecules of ATP and plays a key role in innate immunity. Acts as a key sensor of double- stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 3',3'-c-di-AMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (3',2'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Synthesizes 3',2'-cGAMP in a two-step reaction through production of the linear intermediate pppA(2'-5')pG. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0106408; GO:0003690; GO:0005525; GO:0046872; GO:0016779,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,0.5384,0.5384,0.5384,0.5384,0.5384,5,0.5384,0.6643,yes
CGLR3_STYPI,P0DXC0,Protein2Text,Eukaryota,340,"Nucleotidyltransferase that catalyzes the formation of cyclic di-AMP (3',3'-c-di-AMP) from 2 molecules of ATP and plays a key role in innate immunity. Acts as a key sensor of double- stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 3',3'-c-di-AMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",This protein is a GTPase domain-containing protein.,Vague,Vague,Vague,Vague,No,not-Yes,GO:0005524; GO:0106408; GO:0003690; GO:0005525; GO:0046872; GO:0016779,GO:0003924,GO:0003924; GO:0005525,GO:0003924,GO:0003924,GO:0003924,0.1093,0.4626,0.1093,0.1093,0.1093,5,0.18,0.6643,yes
CGLR3_STYPI,P0DXC0,Reference,Eukaryota,340,"Nucleotidyltransferase that catalyzes the formation of cyclic di-AMP (3',3'-c-di-AMP) from 2 molecules of ATP and plays a key role in innate immunity. Acts as a key sensor of double- stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 3',3'-c-di-AMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of cyclic di-AMP (3',3'-c-di-AMP) from 2 molecules of ATP and plays a key role in innate immunity. Acts as a key sensor of double- stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 3',3'-c-di-AMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",,,,,,,GO:0005524; GO:0106408; GO:0003690; GO:0005525; GO:0046872; GO:0016779,GO:0016779; GO:0003725,GO:0016779; GO:0005524; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,0.5384,0.758,0.5384,0.5384,0.5384,5,0.5823,0.6643,yes
ARLY_LIMP3,P0DXD4,ESM2Text,Bacteria,464,"Catalyzes the last step of arginine biosynthesis, the conversion of argininosuccinate into L-arginine and fumarate.",Catalyzes an anti cycloisomerization.,No,No,No,No,No,not-Yes,GO:0004056,,GO:0016853,,,,,0.3552,,,,1,0.3552,0.3229,no
ARLY_LIMP3,P0DXD4,Prot2Text,Bacteria,464,"Catalyzes the last step of arginine biosynthesis, the conversion of argininosuccinate into L-arginine and fumarate.","Catalyzes two reactions in de novo purine nucleotide biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4-carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate (ADS or N(6)-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP) and fumarate.",No,Maybe,No,Maybe,Maybe,not-Yes,GO:0004056,GO:0004018,GO:0004018,GO:0004018,GO:0004018,GO:0016829,0.7289,0.7289,0.7289,0.7289,0.6019,5,0.7035,0.3229,no
ARLY_LIMP3,P0DXD4,ProtT3,Bacteria,464,"Catalyzes the last step of arginine biosynthesis, the conversion of argininosuccinate into L-arginine and fumarate.",Cytoplasm. Belongs to the lyase 1 family. Argininosuccinate lyase subfamily,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004056,GO:0004056,GO:0004056,GO:0004056,GO:0004056,GO:0004056,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3229,no
ARLY_LIMP3,P0DXD4,ProtTale,Bacteria,464,"Catalyzes the last step of arginine biosynthesis, the conversion of argininosuccinate into L-arginine and fumarate.","Catalyzes the reversible cyclization of pimeloyl-[acyl-carrier protein] to isoleucyl-[acyl-carrier protein], the first committed step in fatty acid biosynthesis.",No,No,No,No,No,not-Yes,GO:0004056,,GO:0016829,,,,,0.6019,,,,1,0.6019,0.3229,no
ARLY_LIMP3,P0DXD4,Protein2Text,Bacteria,464,"Catalyzes the last step of arginine biosynthesis, the conversion of argininosuccinate into L-arginine and fumarate.","The molecular function of the protein is that it catalyzes the conversion of histidine to imidazolepropionaldehyde, a key step in the catabolism of histidine. Specifically, it catalyzes the oxidative deamination of histidine to imidazoleacetoldehyde, which is then further converted to imidazolepropionaldehyde.",No,No,No,No,No,not-Yes,GO:0004056,,,,,GO:0016641,,,,,0.2353,1,0.2353,0.3229,no
ARLY_LIMP3,P0DXD4,Reference,Bacteria,464,"Catalyzes the last step of arginine biosynthesis, the conversion of argininosuccinate into L-arginine and fumarate.","Catalyzes the last step of arginine biosynthesis, the conversion of argininosuccinate into L-arginine and fumarate.",,,,,,,GO:0004056,GO:0004056,GO:0004056,GO:0004056,GO:0004056,GO:0004056,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3229,no
STSC_STRE0,P0DXD5,ESM2Text,Bacteria,299,"Sesterterpene cyclase, which converts geranylfarnesyl diphosphate (GFPP) into the terpenes somaliensene A and somaliensene B.","Involved in the biosynthesis of paerucumarin, a cyclized type A capsular polysaccharide that is one of the two major constituents of the luminescent membrane of B.cinerea. Catalyzes the esterification of 4-O-acetyl-6-O-methylmucoabd-7-(9Z-octadecenoyl)-5,7-dienoate (MCDR) to yield demethylmacrocin (DMCP).",No,No,No,No,No,not-Yes,GO:0016829; GO:0016765,,GO:0016746,,,,,0.6011,,,,1,0.6011,0.272,no
STSC_STRE0,P0DXD5,Prot2Text,Bacteria,299,"Sesterterpene cyclase, which converts geranylfarnesyl diphosphate (GFPP) into the terpenes somaliensene A and somaliensene B.",Catalyzes the esterification of bacteriochlorophyllide a by geranylgeraniol-PPi.,No,No,No,No,No,not-Yes,GO:0016829; GO:0016765,GO:0016740,GO:0016740,GO:0016765,GO:0016765,GO:0016765,0.7397,0.7397,0.8269,0.8269,0.8269,5,0.792,0.272,no
STSC_STRE0,P0DXD5,ProtT3,Bacteria,299,"Sesterterpene cyclase, which converts geranylfarnesyl diphosphate (GFPP) into the terpenes somaliensene A and somaliensene B.","Catalyzes the condensation of geranylgeranyl diphosphate (GGPP) with (2E,6E)-farnesyl diphosphate (FPP) to form (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate (UPP). Involved in the biosynthesis of undecaprenylpyrophosphate (UPP), a precursor of undecaprenyl-pyrophosphoryl-alpha-D-",Maybe,No,Maybe,No,No,not-Yes,GO:0016829; GO:0016765,GO:0004659,GO:0008834,GO:0004659,GO:0016765,GO:0008834,0.6968,0.4865,0.6968,0.8269,0.4865,5,0.6387,0.272,no
STSC_STRE0,P0DXD5,ProtTale,Bacteria,299,"Sesterterpene cyclase, which converts geranylfarnesyl diphosphate (GFPP) into the terpenes somaliensene A and somaliensene B.","Bifunctional polyketide synthase; part of the core atranone cluster (CAC) which products are predicted to catalyze most or all steps of mycotoxin atranone synthesis, starting from geranylgeranyl pyrophosphate (GGPP). The initial cyclization of GGPP to dolabellane is probably performed by the terpene cyclase ATR13. The Baeyer-Villiger oxidation near the end of the atranone synthesis, which converts atranones D and E to atranones F and G is predicted to be catalyzed by the monooxygenase ATR8. Of the CAC's other predicted gene",No,No,No,No,No,not-Yes,GO:0016829; GO:0016765,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.6011,0.6011,0.6011,0.6011,0.6011,5,0.6011,0.272,no
STSC_STRE0,P0DXD5,Protein2Text,Bacteria,299,"Sesterterpene cyclase, which converts geranylfarnesyl diphosphate (GFPP) into the terpenes somaliensene A and somaliensene B.",This protein is involved in the molecular function of transferring fatty acids.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016829; GO:0016765,GO:0016746,,,,GO:0016747,0.6011,,,,0.5067,2,0.5539,0.272,no
STSC_STRE0,P0DXD5,Reference,Bacteria,299,"Sesterterpene cyclase, which converts geranylfarnesyl diphosphate (GFPP) into the terpenes somaliensene A and somaliensene B.","Sesterterpene cyclase, which converts geranylfarnesyl diphosphate (GFPP) into the terpenes somaliensene A and somaliensene B.",,,,,,,GO:0016829; GO:0016765,GO:0016829,GO:0016829,GO:0010333,GO:0016829,GO:0010333,0.8269,0.8269,0.4961,0.8269,0.4961,5,0.6946,0.272,no
AVAA6_STRSQ,P0DXD8,ESM2Text,Bacteria,559,"Ligase involved in the biosynthesis of avenalumic acid (AVA). Catalyzes the diazotization of 3-aminoavenalumic acid (3-AAA) to 3-diazoavenalumic acid (3-DAA). It can also act on 3-aminocoumaric acid (3-ACA) and 3-amino-4- hydroxybenzoic acid (3,4-AHBA) with lower activity.","Involved in the activation of medium/long-chain fatty acids as acyl-coenzyme A (acyl-CoA), which are then transferred to the multifunctional polyketide synthase (PKS) type III for further chain extension. Activity toward medium-chain fatty acids is increased by the pH. Both C6 and C13 acids are required for the ATP-independent peroxisomal acid biogenesis.",No,No,Maybe,No,No,not-Yes,GO:0005524; GO:0016405; GO:0046872,GO:0016405; GO:0005524,GO:0016878,GO:0004467,GO:0016874,GO:0004467,0.8578,0.3932,0.343,0.4062,0.343,5,0.4686,0.4037,no
AVAA6_STRSQ,P0DXD8,Prot2Text,Bacteria,559,"Ligase involved in the biosynthesis of avenalumic acid (AVA). Catalyzes the diazotization of 3-aminoavenalumic acid (3-AAA) to 3-diazoavenalumic acid (3-DAA). It can also act on 3-aminocoumaric acid (3-ACA) and 3-amino-4- hydroxybenzoic acid (3,4-AHBA) with lower activity.","Catalyzes the activation of medium/long-chain fatty acids as acyl-coenzyme A (acyl-CoA), which are then transferred to the multifunctional polyketide synthase (PKS) type III for further chain extension.",No,No,Maybe,No,No,not-Yes,GO:0005524; GO:0016405; GO:0046872,GO:0016877,GO:0004467,GO:0004467,GO:0004467,GO:0003996,0.4708,0.343,0.343,0.343,0.343,5,0.3686,0.4037,no
AVAA6_STRSQ,P0DXD8,ProtT3,Bacteria,559,"Ligase involved in the biosynthesis of avenalumic acid (AVA). Catalyzes the diazotization of 3-aminoavenalumic acid (3-AAA) to 3-diazoavenalumic acid (3-DAA). It can also act on 3-aminocoumaric acid (3-ACA) and 3-amino-4- hydroxybenzoic acid (3,4-AHBA) with lower activity.","Part of the gene cluster that mediates the biosynthesis of the fungal meroterpenoid acetoxydehydroaustin . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA . 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN . Further epoxidation by the FAD-",No,No,Vague,No,No,not-Yes,GO:0005524; GO:0016405; GO:0046872,,,,,,,,,,,0,,0.4037,no
AVAA6_STRSQ,P0DXD8,ProtTale,Bacteria,559,"Ligase involved in the biosynthesis of avenalumic acid (AVA). Catalyzes the diazotization of 3-aminoavenalumic acid (3-AAA) to 3-diazoavenalumic acid (3-DAA). It can also act on 3-aminocoumaric acid (3-ACA) and 3-amino-4- hydroxybenzoic acid (3,4-AHBA) with lower activity.","Acyl-CoA ligase; part of the gene clusters that mediate the biosynthesis of the host-selective toxins (HSTs) AF-toxins responsible for Alternaria black spot of strawberry disease by the strawberry pathotype. AF-toxin I and III are valine derivatives of 2,3-dyhydroxy-isovaleric acid and 2-hydroxy-isovaleric acid respectively, while AF II is an isoleucine derivative of 2-hydroxy-valeric acid. These derivatives are bound to a 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (ED",No,No,Maybe,No,No,not-Yes,GO:0005524; GO:0016405; GO:0046872,GO:0016877,GO:0003996,GO:0016874,GO:0016877,GO:0016874,0.4708,0.343,0.4062,0.4708,0.4062,5,0.4194,0.4037,no
AVAA6_STRSQ,P0DXD8,Protein2Text,Bacteria,559,"Ligase involved in the biosynthesis of avenalumic acid (AVA). Catalyzes the diazotization of 3-aminoavenalumic acid (3-AAA) to 3-diazoavenalumic acid (3-DAA). It can also act on 3-aminocoumaric acid (3-ACA) and 3-amino-4- hydroxybenzoic acid (3,4-AHBA) with lower activity.","This protein is involved in the catalysis of a specific chemical reaction. However, the specific molecular function of this protein is not provided in the text. Based on the given information, it can be inferred that this protein is involved in the metabolism of a particular compound, but the exact molecular function is not specified. 

If you have more information or context about this protein, I may be able to provide a more detailed answer.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0005524; GO:0016405; GO:0046872,,,,,,,,,,,0,,0.4037,no
AVAA6_STRSQ,P0DXD8,Reference,Bacteria,559,"Ligase involved in the biosynthesis of avenalumic acid (AVA). Catalyzes the diazotization of 3-aminoavenalumic acid (3-AAA) to 3-diazoavenalumic acid (3-DAA). It can also act on 3-aminocoumaric acid (3-ACA) and 3-amino-4- hydroxybenzoic acid (3,4-AHBA) with lower activity.","Ligase involved in the biosynthesis of avenalumic acid (AVA). Catalyzes the diazotization of 3-aminoavenalumic acid (3-AAA) to 3-diazoavenalumic acid (3-DAA). It can also act on 3-aminocoumaric acid (3-ACA) and 3-amino-4- hydroxybenzoic acid (3,4-AHBA) with lower activity.",,,,,,,GO:0005524; GO:0016405; GO:0046872,GO:0016874,GO:0016874,GO:0016874,GO:0016874,GO:0016874,0.4062,0.4062,0.4062,0.4062,0.4062,5,0.4062,0.4037,no
CHCC2_SINCY,P0DXE3,ESM2Text,Bacteria,590,"Desaturase involved in a cyclohexanecarboxylate (CHCA) degradation pathway. Probably catalyzes the conversion of 4-oxocyclohexenecarboxylate to 4- oxocyclohex-2,5-dienecarboxylate, which is spontaneously isomerized to 4-hydroxybenzoate (4-HBA).","Catalyzes the elimination of the C-1 and C-2 hydrogen atoms of the A-ring from the polycyclic ring structure of 3-ketosteroids, leading to the formation of 3-oxosteroids.",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0033765,GO:0016491,GO:0016491,GO:0016627,GO:0016491,GO:0016627,0.6062,0.6062,0.747,0.6062,0.747,5,0.6625,0.1819,no
CHCC2_SINCY,P0DXE3,Prot2Text,Bacteria,590,"Desaturase involved in a cyclohexanecarboxylate (CHCA) degradation pathway. Probably catalyzes the conversion of 4-oxocyclohexenecarboxylate to 4- oxocyclohex-2,5-dienecarboxylate, which is spontaneously isomerized to 4-hydroxybenzoate (4-HBA).",Catalyzes the elimination of the C-1 and C-2 hydrogen atoms of the A-ring from the polycyclic ring structure of 3-ketosteroids.,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0033765,GO:0016491,GO:0047598,GO:0016627,GO:0050607,GO:0047598,0.6062,0.5415,0.747,0.358,0.5415,5,0.5588,0.1819,no
CHCC2_SINCY,P0DXE3,ProtT3,Bacteria,590,"Desaturase involved in a cyclohexanecarboxylate (CHCA) degradation pathway. Probably catalyzes the conversion of 4-oxocyclohexenecarboxylate to 4- oxocyclohex-2,5-dienecarboxylate, which is spontaneously isomerized to 4-hydroxybenzoate (4-HBA).","Catalyzes the reduction of 2,3-diketo-L-gulonate to 3-keto-L-gulonate. Cell inner membrane; Peripheral membrane protein. Belongs to the Gfo/Idh/MocA family. 2,3-diketo-L-gulonate reductase subfamily",No,No,No,No,No,not-Yes,GO:0033765,GO:0016616,GO:0016491,GO:0016491,GO:0016616,GO:0016491,0.4151,0.6062,0.6062,0.4151,0.6062,5,0.5298,0.1819,no
CHCC2_SINCY,P0DXE3,ProtTale,Bacteria,590,"Desaturase involved in a cyclohexanecarboxylate (CHCA) degradation pathway. Probably catalyzes the conversion of 4-oxocyclohexenecarboxylate to 4- oxocyclohex-2,5-dienecarboxylate, which is spontaneously isomerized to 4-hydroxybenzoate (4-HBA).","Involved in the degradation of 3,5-dihydroxybenzoate (3,5-DHB). Catalyzes the oxidation of 3,5-DHB to 3,6-dihydroxybenzoate (3,6-DHB). Also catalyzes the isomerization of 3,5-DHB to 2,4-dihydroxybenzoate (2,4-DHB) and 3,6-DHB to 3,7-dihydroxybenzoate (3,7-DHB).",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0033765,GO:0016491,GO:0016491; GO:0016853,GO:0016491; GO:0016853,GO:0016491; GO:0016853,GO:0016491; GO:0016853,0.6062,0.5233,0.5233,0.5233,0.5233,5,0.5399,0.1819,no
CHCC2_SINCY,P0DXE3,Protein2Text,Bacteria,590,"Desaturase involved in a cyclohexanecarboxylate (CHCA) degradation pathway. Probably catalyzes the conversion of 4-oxocyclohexenecarboxylate to 4- oxocyclohex-2,5-dienecarboxylate, which is spontaneously isomerized to 4-hydroxybenzoate (4-HBA).","The molecular function of this protein is an oxidoreductase activity, specifically it is involved in the degradation of fatty acids. It is a key enzyme in the process of breaking down fatty acids into simpler compounds, and it plays a crucial role in the metabolism of fatty acids in various organisms.",Vague,Maybe,No,No,Maybe,not-Yes,GO:0033765,GO:0016491,GO:0016491,,,GO:0003995,0.6062,0.6062,,,0.5415,3,0.5846,0.1819,no
CHCC2_SINCY,P0DXE3,Reference,Bacteria,590,"Desaturase involved in a cyclohexanecarboxylate (CHCA) degradation pathway. Probably catalyzes the conversion of 4-oxocyclohexenecarboxylate to 4- oxocyclohex-2,5-dienecarboxylate, which is spontaneously isomerized to 4-hydroxybenzoate (4-HBA).","Desaturase involved in a cyclohexanecarboxylate (CHCA) degradation pathway. Probably catalyzes the conversion of 4-oxocyclohexenecarboxylate to 4- oxocyclohex-2,5-dienecarboxylate, which is spontaneously isomerized to 4-hydroxybenzoate (4-HBA).",,,,,,,GO:0033765,GO:0016627,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.747,0.6062,0.6062,0.6062,0.6062,5,0.6344,0.1819,no
HBDA_AROS1,P0DXG4,ESM2Text,Bacteria,523,"Ligase involved in the anaerobic degradation of 3- hydroxybenzoate (3OHBz). Catalyzes the activation of 3-hydroxybenzoate to 3-hydroxybenzoyl-CoA. Also shows high activity with protocatechuate and 4-hydroxybenzoate. Exhibits lower activity with benzoate, but cannot use 2-hydroxybenzoate or benzoate analogs containing other substituents at the ortho position, such as 2-aminobenzoate (anthranilate).","Catalyzes the ligation of coenzyme A (CoA) to 4-hydroxybenzoate (4HB). It can also use butanoate, 3-mercaptopropionate, 4-chlorobenzoyl-CoA and laurocholate as substrates.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016878; GO:0005524; GO:0016405,GO:0016405,GO:0016878,GO:0016878,GO:0016874,GO:0016878,0.6914,0.6914,0.6914,0.5391,0.6914,5,0.6609,0.3924,no
HBDA_AROS1,P0DXG4,Prot2Text,Bacteria,523,"Ligase involved in the anaerobic degradation of 3- hydroxybenzoate (3OHBz). Catalyzes the activation of 3-hydroxybenzoate to 3-hydroxybenzoyl-CoA. Also shows high activity with protocatechuate and 4-hydroxybenzoate. Exhibits lower activity with benzoate, but cannot use 2-hydroxybenzoate or benzoate analogs containing other substituents at the ortho position, such as 2-aminobenzoate (anthranilate).","Catalyzes the ligation of 4-hydroxybenzoate or 4-bromo-benzoate and CoA at the expense of ATP. The enzyme shows low activity towards benzoate, 4-aminobenzoate, 4-fluorobenzoate, 4-chlorobenzoate, 4-iodobenzoate, 4-fluorobenzoate, 4-chlorobenzoate and 2-chlorobenzoate. There is no activity with 4-nitrophenylbenzoate, 4-nitrophenyl sulfate, 4-fluorobenzoate or 2-chlorobenzoate.",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0016878; GO:0005524; GO:0016405,GO:0016877,GO:0016405,GO:0016877,GO:0016878,GO:0016878,0.6496,0.6914,0.6496,0.6914,0.6914,5,0.6747,0.3924,no
HBDA_AROS1,P0DXG4,ProtT3,Bacteria,523,"Ligase involved in the anaerobic degradation of 3- hydroxybenzoate (3OHBz). Catalyzes the activation of 3-hydroxybenzoate to 3-hydroxybenzoyl-CoA. Also shows high activity with protocatechuate and 4-hydroxybenzoate. Exhibits lower activity with benzoate, but cannot use 2-hydroxybenzoate or benzoate analogs containing other substituents at the ortho position, such as 2-aminobenzoate (anthranilate).",Belongs to the ATP-dependent AMP-binding enzyme family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016878; GO:0005524; GO:0016405,GO:0016874; GO:0005524,GO:0016878,,GO:0003996,GO:0003996,0.8138,0.6914,,0.4751,0.4751,4,0.6139,0.3924,no
HBDA_AROS1,P0DXG4,ProtTale,Bacteria,523,"Ligase involved in the anaerobic degradation of 3- hydroxybenzoate (3OHBz). Catalyzes the activation of 3-hydroxybenzoate to 3-hydroxybenzoyl-CoA. Also shows high activity with protocatechuate and 4-hydroxybenzoate. Exhibits lower activity with benzoate, but cannot use 2-hydroxybenzoate or benzoate analogs containing other substituents at the ortho position, such as 2-aminobenzoate (anthranilate).","Catalyzes the formation of (2E,6E)-farnesyl diphosphate from farnesyl-CoA and malonyl-CoA. Also catalyzes the formation of (2E,6E)-farnesyl-AMP from farnesyl-CoA and AMP.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016878; GO:0005524; GO:0016405,,GO:0016740,GO:0016740,,GO:0016740,,0.3271,0.3271,,0.3271,3,0.3271,0.3924,no
HBDA_AROS1,P0DXG4,Protein2Text,Bacteria,523,"Ligase involved in the anaerobic degradation of 3- hydroxybenzoate (3OHBz). Catalyzes the activation of 3-hydroxybenzoate to 3-hydroxybenzoyl-CoA. Also shows high activity with protocatechuate and 4-hydroxybenzoate. Exhibits lower activity with benzoate, but cannot use 2-hydroxybenzoate or benzoate analogs containing other substituents at the ortho position, such as 2-aminobenzoate (anthranilate).","This protein is involved in the molecular function of acyl transferase activity. It is part of a larger system that allows the conversion of a substrate into a product through a series of chemical reactions, and its specific function is to transfer an acyl group from one molecule to another. This type of reaction is essential in many biological pathways, including the synthesis of fatty acids, amino acids, and other important molecules. The molecular function of this protein is likely to be involved in the synthesis of a specific molecule, and its activity is probably regulated by other proteins or molecules in the cell.",Vague,No,No,No,No,not-Yes,GO:0016878; GO:0005524; GO:0016405,GO:0016746,GO:0016746,GO:0016747,GO:0016746,GO:0016747,0.2647,0.2647,0.2214,0.2647,0.2214,5,0.2474,0.3924,no
HBDA_AROS1,P0DXG4,Reference,Bacteria,523,"Ligase involved in the anaerobic degradation of 3- hydroxybenzoate (3OHBz). Catalyzes the activation of 3-hydroxybenzoate to 3-hydroxybenzoyl-CoA. Also shows high activity with protocatechuate and 4-hydroxybenzoate. Exhibits lower activity with benzoate, but cannot use 2-hydroxybenzoate or benzoate analogs containing other substituents at the ortho position, such as 2-aminobenzoate (anthranilate).","Ligase involved in the anaerobic degradation of 3- hydroxybenzoate (3OHBz). Catalyzes the activation of 3-hydroxybenzoate to 3-hydroxybenzoyl-CoA. Also shows high activity with protocatechuate and 4-hydroxybenzoate. Exhibits lower activity with benzoate, but cannot use 2-hydroxybenzoate or benzoate analogs containing other substituents at the ortho position, such as 2-aminobenzoate (anthranilate).",,,,,,,GO:0016878; GO:0005524; GO:0016405,GO:0016877,GO:0016878,GO:0016874; GO:0005524,GO:0016878,GO:0016878,0.6496,0.6914,0.8138,0.6914,0.6914,5,0.7075,0.3924,no
PNBA_NOCS0,P0DXG6,ESM2Text,Bacteria,247,Nitroreductase involved in the degradation of nitroaromatic compounds. Catalyzes the conversion of 4- nitrobenzoate to 4-hydroxylaminobenzoate.,"Involved in the biodegradation of nitroaromatic compounds. Can use a variety of nitro compounds, including biodegradation products ranging from 12-mercaptopropionate (C2-NP) to the biodegradation of nitrofurazone A (FN-A). In vitro, can also catalyze the reduction of nitrofurazone A analog.",Yes,Maybe,Maybe,Yes,Yes,Yes,GO:0016491,,GO:0016491,GO:0016657,GO:0016491,,,1.0,0.0,1.0,,3,0.6667,0.2224,no
PNBA_NOCS0,P0DXG6,Prot2Text,Bacteria,247,Nitroreductase involved in the degradation of nitroaromatic compounds. Catalyzes the conversion of 4- nitrobenzoate to 4-hydroxylaminobenzoate.,"Could be involved in the biosynthesis of a quorum sensing system signal molecule that regulates the development of disease symptoms and responses to natural and synthetic herbicides. Catalyzes the reduction of nitroaromatic compounds using NADPH as the electron donor. NADH is also effective, but NADPH is a poor substrate.",Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016657,GO:0016657,GO:0016657,1.0,1.0,0.0,0.0,0.0,5,0.4,0.2224,no
PNBA_NOCS0,P0DXG6,ProtT3,Bacteria,247,Nitroreductase involved in the degradation of nitroaromatic compounds. Catalyzes the conversion of 4- nitrobenzoate to 4-hydroxylaminobenzoate.,Belongs to the non-flavoprotein monooxygenase family,Vague,No,Vague,No,No,not-Yes,GO:0016491,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.8145,0.8145,0.8145,0.8145,0.8145,5,0.8145,0.2224,no
PNBA_NOCS0,P0DXG6,ProtTale,Bacteria,247,Nitroreductase involved in the degradation of nitroaromatic compounds. Catalyzes the conversion of 4- nitrobenzoate to 4-hydroxylaminobenzoate.,"Catalyzes the NAD(P)H-dependent reduction of nitroaromatic compounds such as 2,4-dinitrotoluene (DNT), 2,4,6-trinitrotoluene (TNT) and 1,3,5-trinitro-1,3,5-triazine (RDX). In addition, it can also reduce other nitroaromatics such as 2,4-dinitrochlorobenzene (DNCB), 2,4,6-trinitrophenol (TNP), 2,4-",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2224,no
PNBA_NOCS0,P0DXG6,Protein2Text,Bacteria,247,Nitroreductase involved in the degradation of nitroaromatic compounds. Catalyzes the conversion of 4- nitrobenzoate to 4-hydroxylaminobenzoate.,"The molecular function of this protein is likely to be involved in the removal of toxic groups from the substrate, specifically an enzyme that catalyzes the dehydrogenation reaction. However, the specific molecular function of this protein is not explicitly stated in the provided text.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0016491,,,,,,,,,,,0,,0.2224,no
PNBA_NOCS0,P0DXG6,Reference,Bacteria,247,Nitroreductase involved in the degradation of nitroaromatic compounds. Catalyzes the conversion of 4- nitrobenzoate to 4-hydroxylaminobenzoate.,Nitroreductase involved in the degradation of nitroaromatic compounds. Catalyzes the conversion of 4- nitrobenzoate to 4-hydroxylaminobenzoate.,,,,,,,GO:0016491,GO:0016657,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.0,1.0,1.0,1.0,1.0,5,0.8,0.2224,no
SDR_MELAZ,P0DXH3,ESM2Text,Eukaryota,271,"Oxidoreductase involved in the biosynthesis of limonoids triterpene natural products such as azadirachtin, an antifeedant widely used as bioinsecticide, and possessing many medicinal applications including anti-tumoral, anti-malarial, anti-rheumatic, antibacterial, anti-inflammatory, anti-pyretic and diuretic effects. Catalyzes the oxidation of 21-O-acetyl-isomeliandiol to (21S)-21- acetoxyl-apo-melianone.","Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of the tropolone class of fungal maleic anhydrides. The pathway begins with the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide synthase (PKS) tropA. 3-methylorcinaldehyde is the substrate for the FAD-dependent monooxygenase tropB to yield a dearomatized hydroxycyclohexadione. The 2-oxoglutarate-dependent dioxygenase tropC then performs the oxidative ring expansion to provide the first tropolone metabolite stipitaldehyde. Trop D converts stipitaldehyde into stipitacetal which is in turn converted to stipitalide by the short-chain dehydrogenase/reductase tropE. The next steps involve tropF, tropG, tropH, tropI and tropJ to form successive tropolone maleic anhydrides including stipitaldehydic, stipitatonic and stipitatic acids.",No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016614,GO:0016491,GO:0016614,1.0,1.0,0.8145,1.0,0.8145,5,0.9258,0.1502,no
SDR_MELAZ,P0DXH3,Prot2Text,Eukaryota,271,"Oxidoreductase involved in the biosynthesis of limonoids triterpene natural products such as azadirachtin, an antifeedant widely used as bioinsecticide, and possessing many medicinal applications including anti-tumoral, anti-malarial, anti-rheumatic, antibacterial, anti-inflammatory, anti-pyretic and diuretic effects. Catalyzes the oxidation of 21-O-acetyl-isomeliandiol to (21S)-21- acetoxyl-apo-melianone.","Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Has activity toward short and medium chain 2,4-dienoyl-CoAs, but also toward 2,4,7,10,13,16,19-docosaheptaenoyl-CoA and toward 2,4,6,7,11,14-docosaheptaenoyl-CoA.",No,No,No,No,No,not-Yes,GO:0016491,GO:0008670,GO:0008670,GO:0008670,GO:0008670,GO:0008670,0.6019,0.6019,0.6019,0.6019,0.6019,5,0.6019,0.1502,no
SDR_MELAZ,P0DXH3,ProtT3,Eukaryota,271,"Oxidoreductase involved in the biosynthesis of limonoids triterpene natural products such as azadirachtin, an antifeedant widely used as bioinsecticide, and possessing many medicinal applications including anti-tumoral, anti-malarial, anti-rheumatic, antibacterial, anti-inflammatory, anti-pyretic and diuretic effects. Catalyzes the oxidation of 21-O-acetyl-isomeliandiol to (21S)-21- acetoxyl-apo-melianone.",Belongs to the short-chain dehydrogenases/reductases (SDR) family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016491,GO:0016491,GO:0016491,,,,1.0,1.0,,,,2,1.0,0.1502,no
SDR_MELAZ,P0DXH3,ProtTale,Eukaryota,271,"Oxidoreductase involved in the biosynthesis of limonoids triterpene natural products such as azadirachtin, an antifeedant widely used as bioinsecticide, and possessing many medicinal applications including anti-tumoral, anti-malarial, anti-rheumatic, antibacterial, anti-inflammatory, anti-pyretic and diuretic effects. Catalyzes the oxidation of 21-O-acetyl-isomeliandiol to (21S)-21- acetoxyl-apo-melianone.","Involved in the biosynthesis of gibberellins (GAs), diterpenes that play an important role in plant development. Catalyzes the conversion of ent-copalyl diphosphate (ent-CPP) to ent-kaurene diphosphate (ent-KPP).",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,GO:0010333,GO:0016829,GO:0010333,GO:0016829,GO:0010333,0.3552,0.5902,0.3552,0.5902,0.3552,5,0.4492,0.1502,no
SDR_MELAZ,P0DXH3,Protein2Text,Eukaryota,271,"Oxidoreductase involved in the biosynthesis of limonoids triterpene natural products such as azadirachtin, an antifeedant widely used as bioinsecticide, and possessing many medicinal applications including anti-tumoral, anti-malarial, anti-rheumatic, antibacterial, anti-inflammatory, anti-pyretic and diuretic effects. Catalyzes the oxidation of 21-O-acetyl-isomeliandiol to (21S)-21- acetoxyl-apo-melianone.",The molecular function of this protein is as a probable oxidoreductase.,Vague,Vague,Maybe,Vague,Vague,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,,GO:0016491,1.0,1.0,1.0,,1.0,4,1.0,0.1502,no
SDR_MELAZ,P0DXH3,Reference,Eukaryota,271,"Oxidoreductase involved in the biosynthesis of limonoids triterpene natural products such as azadirachtin, an antifeedant widely used as bioinsecticide, and possessing many medicinal applications including anti-tumoral, anti-malarial, anti-rheumatic, antibacterial, anti-inflammatory, anti-pyretic and diuretic effects. Catalyzes the oxidation of 21-O-acetyl-isomeliandiol to (21S)-21- acetoxyl-apo-melianone.","Oxidoreductase involved in the biosynthesis of limonoids triterpene natural products such as azadirachtin, an antifeedant widely used as bioinsecticide, and possessing many medicinal applications including anti-tumoral, anti-malarial, anti-rheumatic, antibacterial, anti-inflammatory, anti-pyretic and diuretic effects. Catalyzes the oxidation of 21-O-acetyl-isomeliandiol to (21S)-21- acetoxyl-apo-melianone.",,,,,,,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1502,no
OYE_CABCO,P0DXY1,ESM2Text,Bacteria,674,A member of the 2-enoate reductase subfamily of old yellow enzymes (OYE) able to reduce alpha/beta alkenes near electron- withdrawing groups as well as perform oxidative demethylation chemistry. Prefers NADH over NADPH as cosubstrate. May play a role in osmotic stress response in situ (Probable).,Efficiently catalyzes both the NADH-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) and the oxidative fragmentation of nascent polypeptides (APPs). NADH acts as an electron donor to the NB-protein kinase DdnA in an NADH-dependent manner. DdnA is the major component of an NADPH-dependent inorganic carbon pump.,No,No,No,Maybe,No,not-Yes,GO:0051539; GO:0046872; GO:0016491,GO:0016491,GO:0016491,,,,0.5789,0.5789,,,,2,0.5789,0.1253,no
OYE_CABCO,P0DXY1,Prot2Text,Bacteria,674,A member of the 2-enoate reductase subfamily of old yellow enzymes (OYE) able to reduce alpha/beta alkenes near electron- withdrawing groups as well as perform oxidative demethylation chemistry. Prefers NADH over NADPH as cosubstrate. May play a role in osmotic stress response in situ (Probable).,Putative oxophytodienoate reductase that may be involved in the biosynthesis or metabolism of oxylipin signaling molecules.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0051539; GO:0046872; GO:0016491,GO:0016491,GO:0016491,,,GO:0016491,0.5789,0.5789,,,0.5789,3,0.5789,0.1253,no
OYE_CABCO,P0DXY1,ProtT3,Bacteria,674,A member of the 2-enoate reductase subfamily of old yellow enzymes (OYE) able to reduce alpha/beta alkenes near electron- withdrawing groups as well as perform oxidative demethylation chemistry. Prefers NADH over NADPH as cosubstrate. May play a role in osmotic stress response in situ (Probable).,In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0051539; GO:0046872; GO:0016491,,GO:0016857,,,,,0.2558,,,,1,0.2558,0.1253,no
OYE_CABCO,P0DXY1,ProtTale,Bacteria,674,A member of the 2-enoate reductase subfamily of old yellow enzymes (OYE) able to reduce alpha/beta alkenes near electron- withdrawing groups as well as perform oxidative demethylation chemistry. Prefers NADH over NADPH as cosubstrate. May play a role in osmotic stress response in situ (Probable).,"NADH-dependent oxidoreductase with a broad substrate specificity. Catalyzes the reduction of 3-hydroxyacyl-CoA and (R)-2-hydroxyacyl-CoA to 3-oxoacyl-CoA and (R)-2-hydroxyacyl-CoA, respectively. Can catalyze the reduction of 3-ketoacyl- CoA to 3-oxoacyl-CoA, but not the reverse reaction. Also catalyzes the reduction of 2-ketoacyl-CoA to 2-hydroxyacyl-CoA, but not the reverse reaction. Shows low activity with (S)-2-hydroxyacyl",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0051539; GO:0046872; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.5789,0.5789,0.5789,0.5789,0.5789,5,0.5789,0.1253,no
OYE_CABCO,P0DXY1,Protein2Text,Bacteria,674,A member of the 2-enoate reductase subfamily of old yellow enzymes (OYE) able to reduce alpha/beta alkenes near electron- withdrawing groups as well as perform oxidative demethylation chemistry. Prefers NADH over NADPH as cosubstrate. May play a role in osmotic stress response in situ (Probable).,"This protein has the molecular function of oxidoreductase activity. It is involved in the oxidation-reduction reaction, where it catalyzes the transfer of electrons from one molecule to another. More specifically, it is a type of oxidoreductase that catalyzes the oxidation of a substrate, likely involved in the degradation of a specific compound.",Vague,Vague,Maybe,Vague,Vague,not-Yes,GO:0051539; GO:0046872; GO:0016491,GO:0016491,GO:0016491,GO:0016491,,GO:0016491,0.5789,0.5789,0.5789,,0.5789,4,0.5789,0.1253,no
OYE_CABCO,P0DXY1,Reference,Bacteria,674,A member of the 2-enoate reductase subfamily of old yellow enzymes (OYE) able to reduce alpha/beta alkenes near electron- withdrawing groups as well as perform oxidative demethylation chemistry. Prefers NADH over NADPH as cosubstrate. May play a role in osmotic stress response in situ (Probable).,A member of the 2-enoate reductase subfamily of old yellow enzymes (OYE) able to reduce alpha/beta alkenes near electron- withdrawing groups as well as perform oxidative demethylation chemistry. Prefers NADH over NADPH as cosubstrate. May play a role in osmotic stress response in situ (Probable).,,,,,,,GO:0051539; GO:0046872; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.5789,0.5789,0.5789,0.5789,0.5789,5,0.5789,0.1253,no
DGCA_PSEAS,P0DXZ2,ESM2Text,Bacteria,315,"Racemase involved in a deamination-independent D-glutamate degradation pathway, named the DgcN-DgcA pathway. Catalyzes the conversion of N-acetyl-D-glutamate to N-acetyl-L- glutamate. Also shows racemase activity towards the dipeptide L-Ala-D-Glu, a key constituent of peptidoglycan muropeptides, suggesting that it may also contribute to the degradation of peptidoglycans.","Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB).",No,No,No,No,No,not-Yes,GO:0046872; GO:0016855,GO:0008818,GO:0016829,GO:0008935,GO:0008935,GO:0008935,0.1865,0.324,0.1865,0.1865,0.1865,5,0.214,0.4011,no
DGCA_PSEAS,P0DXZ2,Prot2Text,Bacteria,315,"Racemase involved in a deamination-independent D-glutamate degradation pathway, named the DgcN-DgcA pathway. Catalyzes the conversion of N-acetyl-D-glutamate to N-acetyl-L- glutamate. Also shows racemase activity towards the dipeptide L-Ala-D-Glu, a key constituent of peptidoglycan muropeptides, suggesting that it may also contribute to the degradation of peptidoglycans.",Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy-L-rhamnonate (KDR).,No,No,No,No,No,not-Yes,GO:0046872; GO:0016855,GO:0016836,GO:0016836,GO:0016836,GO:0016836,GO:0016836,0.2176,0.2176,0.2176,0.2176,0.2176,5,0.2176,0.4011,no
DGCA_PSEAS,P0DXZ2,ProtT3,Bacteria,315,"Racemase involved in a deamination-independent D-glutamate degradation pathway, named the DgcN-DgcA pathway. Catalyzes the conversion of N-acetyl-D-glutamate to N-acetyl-L- glutamate. Also shows racemase activity towards the dipeptide L-Ala-D-Glu, a key constituent of peptidoglycan muropeptides, suggesting that it may also contribute to the degradation of peptidoglycans.","Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1- carboxylate (SHCHC) to 2-succinylbenzoate (OSB). Belongs to the mandelate racemase/muconate lactonizing enzyme family. MenC type 2 subfamily",No,No,No,No,No,not-Yes,GO:0046872; GO:0016855,GO:0008935,GO:0008935,GO:0008935,GO:0008935,GO:0008935,0.1865,0.1865,0.1865,0.1865,0.1865,5,0.1865,0.4011,no
DGCA_PSEAS,P0DXZ2,ProtTale,Bacteria,315,"Racemase involved in a deamination-independent D-glutamate degradation pathway, named the DgcN-DgcA pathway. Catalyzes the conversion of N-acetyl-D-glutamate to N-acetyl-L- glutamate. Also shows racemase activity towards the dipeptide L-Ala-D-Glu, a key constituent of peptidoglycan muropeptides, suggesting that it may also contribute to the degradation of peptidoglycans.",Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).,No,No,No,No,No,not-Yes,GO:0046872; GO:0016855,GO:0004590,GO:0004590,GO:0004590,GO:0004590,GO:0004590,0.1865,0.1865,0.1865,0.1865,0.1865,5,0.1865,0.4011,no
DGCA_PSEAS,P0DXZ2,Protein2Text,Bacteria,315,"Racemase involved in a deamination-independent D-glutamate degradation pathway, named the DgcN-DgcA pathway. Catalyzes the conversion of N-acetyl-D-glutamate to N-acetyl-L- glutamate. Also shows racemase activity towards the dipeptide L-Ala-D-Glu, a key constituent of peptidoglycan muropeptides, suggesting that it may also contribute to the degradation of peptidoglycans.","The molecular function of this protein is a deoxygenase.
This protein is involved in the deoxygenation of a molecule, specifically in the conversion of a 2-hydroxyglutarate (2-HG) to a 2-oxoglutarate (2-OG) through its action as a deoxygenase enzyme. The 2-HG is a metabolite that plays a key role in cellular metabolism and is involved in various biological processes such as energy production, amino acid synthesis, and nucleotide biosynthesis. The protein catalyzes the conversion of 2-HG to 2-OG, which is an essential step in the metabolic pathway that regulates the levels of 2-HG in the cell. The 2-OG is then converted to succinate and used in the citric acid cycle (TCA cycle), which is a crucial step in energy production in the cell. The protein's deoxygenase activity is essential for maintaining the balance of 2-HG and 2-OG levels in the cell, and any disruption in its function can lead to metabolic disorders. 
The protein is also involved in the regulation of gene expression. It catalyzes the deoxygenation of 2-HG to 2-OG, which is an essential step in the regulation of gene expression. The 2-OG is then converted to succinate and used in the TCA cycle, which is a crucial step in energy production in the cell. The protein's deoxygenase activity is essential for maintaining the balance of 2-HG and 2-OG levels in the cell, and any disruption in its function can lead to metabolic disorders.
The protein is also involved in the regulation of cellular metabolism. It catalyzes the deoxygenation of 2-HG to 2-OG, which is an essential step in the regulation of cellular metabolism. The 2-OG is then converted to succinate and used in the TCA cycle, which is a crucial step in energy production in the cell. The protein's deoxygenase activity is essential for maintaining the balance of 2-HG and 2-OG levels in the cell, and any disruption in its function can lead to metabolic disorders.
The protein is also involved in the regulation of cellular differentiation. It catalyzes the deoxygenation of 2-HG to 2-OG, which is an essential step in the regulation of cellular differentiation. The 2-OG is then converted",No,No,No,No,No,not-Yes,GO:0046872; GO:0016855,GO:0016491,,,,GO:0016491,0.324,,,,0.324,2,0.324,0.4011,no
DGCA_PSEAS,P0DXZ2,Reference,Bacteria,315,"Racemase involved in a deamination-independent D-glutamate degradation pathway, named the DgcN-DgcA pathway. Catalyzes the conversion of N-acetyl-D-glutamate to N-acetyl-L- glutamate. Also shows racemase activity towards the dipeptide L-Ala-D-Glu, a key constituent of peptidoglycan muropeptides, suggesting that it may also contribute to the degradation of peptidoglycans.","Racemase involved in a deamination-independent D-glutamate degradation pathway, named the DgcN-DgcA pathway. Catalyzes the conversion of N-acetyl-D-glutamate to N-acetyl-L- glutamate. Also shows racemase activity towards the dipeptide L-Ala-D-Glu, a key constituent of peptidoglycan muropeptides, suggesting that it may also contribute to the degradation of peptidoglycans.",,,,,,,GO:0046872; GO:0016855,GO:0016854,GO:0016854,GO:0016854,GO:0016854,GO:0016854,0.6032,0.6032,0.6032,0.6032,0.6032,5,0.6032,0.4011,no
PLA2_CALPY,P0DY42,ESM2Text,Eukaryota,162,PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.,"Snake venom phospholipase A2 (PLA2) that displays anticoagulant activity, myotoxic activity, and edema-inducing activities. In addition, it shows cytotoxic activity against some cell lines and myotubes, and antitumor activity against the Gram-negative bacteria E.coli and P.aeruginosa. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005509; GO:0004623,GO:0004623; GO:0005509,GO:0004623,GO:0004623; GO:0005509,GO:0004622; GO:0005509,GO:0004623,1.0,0.6872,1.0,0.8444,0.6872,5,0.8438,0.2858,no
PLA2_CALPY,P0DY42,Prot2Text,Eukaryota,162,PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.,PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005509; GO:0004623,GO:0004623,GO:0004623,GO:0004623,GO:0004623,GO:0004623,0.6872,0.6872,0.6872,0.6872,0.6872,5,0.6872,0.2858,no
PLA2_CALPY,P0DY42,ProtT3,Eukaryota,162,PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.,PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Secreted. Belongs to the phospholipase A2 family. Group I subfamily. D49 sub-subfamily,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005509; GO:0004623,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623,GO:0004623; GO:0005509,GO:0004623; GO:0005509,1.0,1.0,0.6872,1.0,1.0,5,0.9374,0.2858,no
PLA2_CALPY,P0DY42,ProtTale,Eukaryota,162,PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.,PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0005509; GO:0004623,GO:0004623,GO:0004623; GO:0005509,GO:0004623,GO:0004623; GO:0005509,GO:0004623; GO:0005509,0.6872,1.0,0.6872,1.0,1.0,5,0.8749,0.2858,no
PLA2_CALPY,P0DY42,Protein2Text,Eukaryota,162,PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.,"This protein is an enzyme that catalyzes the hydrolysis of phospholipids into fatty acids and phosphates. More specifically, it is a phospholipase that hydrolyzes phosphatidylcholine and phosphatidylethanolamine.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0005509; GO:0004623,GO:0004620,,,GO:0004620,GO:0004623,0.5637,,,0.5637,0.6872,3,0.6049,0.2858,no
PLA2_CALPY,P0DY42,Reference,Eukaryota,162,PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.,PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.,,,,,,,GO:0005509; GO:0004623,GO:0004623,GO:0004623; GO:0005509,GO:0004623; GO:0005509,GO:0004623,GO:0004623,0.6872,1.0,1.0,0.6872,0.6872,5,0.8123,0.2858,no
CAPDC_SYNY3,P73562,ESM2Text,Bacteria,387,"Decarboxylase involved in the biosynthesis of spermidine via the carboxyaminopropylagmatine (CAPA) pathway. Catalyzes the decarboxylation of CAPA to form aminopropylagmatine (APA). Can also decarboxylate carboxyspermidine and carboxynorspermidine, but not ornithine, arginine, lysine and meso- diaminopimelate.",Catalyzes the decarboxylation of carboxynorspermidine and carboxyspermidine.,Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0008836,GO:0016831,GO:0016831,GO:0016831,GO:0019239,GO:0016831,0.8582,0.8582,0.8582,0.2353,0.8582,5,0.7336,0.3775,no
CAPDC_SYNY3,P73562,Prot2Text,Bacteria,387,"Decarboxylase involved in the biosynthesis of spermidine via the carboxyaminopropylagmatine (CAPA) pathway. Catalyzes the decarboxylation of CAPA to form aminopropylagmatine (APA). Can also decarboxylate carboxyspermidine and carboxynorspermidine, but not ornithine, arginine, lysine and meso- diaminopimelate.",Catalyzes the decarboxylation of carboxynorspermidine and carboxyspermidine. Essential for biofilm formation.,Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0008836,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.3775,no
CAPDC_SYNY3,P73562,ProtT3,Bacteria,387,"Decarboxylase involved in the biosynthesis of spermidine via the carboxyaminopropylagmatine (CAPA) pathway. Catalyzes the decarboxylation of CAPA to form aminopropylagmatine (APA). Can also decarboxylate carboxyspermidine and carboxynorspermidine, but not ornithine, arginine, lysine and meso- diaminopimelate.","Catalyzes the decarboxylation of N-succinyl-L,L-diaminopimelic acid (SDAP) to L-2,6-diaminoheptanedioate (DAP), the second step in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls. Belongs to the Orn/Lys/Arg decarboxylase class-II family. N- succinyl-L,L-diaminopimelic acid decarboxylase subfamily",No,No,No,No,Maybe,not-Yes,GO:0008836,GO:0016831; GO:0030170,GO:0008836,GO:0016831,GO:0016831,GO:0016831,0.5952,1.0,0.8582,0.8582,0.8582,5,0.834,0.3775,no
CAPDC_SYNY3,P73562,ProtTale,Bacteria,387,"Decarboxylase involved in the biosynthesis of spermidine via the carboxyaminopropylagmatine (CAPA) pathway. Catalyzes the decarboxylation of CAPA to form aminopropylagmatine (APA). Can also decarboxylate carboxyspermidine and carboxynorspermidine, but not ornithine, arginine, lysine and meso- diaminopimelate.",Catalyzes the decarboxylation of L-aspartate-beta-semialdehyde (ASA) to L-aspartate (aspartic acid).,No,No,No,No,Maybe,not-Yes,GO:0008836,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.3775,no
CAPDC_SYNY3,P73562,Protein2Text,Bacteria,387,"Decarboxylase involved in the biosynthesis of spermidine via the carboxyaminopropylagmatine (CAPA) pathway. Catalyzes the decarboxylation of CAPA to form aminopropylagmatine (APA). Can also decarboxylate carboxyspermidine and carboxynorspermidine, but not ornithine, arginine, lysine and meso- diaminopimelate.","The molecular function of this protein is an aminotransferase. It catalyzes the transfer of an amino group from an amino acid to an alpha-keto acid, playing a crucial role in amino acid metabolism. Specifically, it catalyzes the transfer of an amino group from L-glutamate to 2-oxo-4-methylthiobutyrate (2-methylthio-3-oxobutyrate) to form 2-methylthiobutyrate and L-glutamine.",No,No,No,No,No,not-Yes,GO:0008836,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.2353,0.2353,0.2353,0.2353,0.2353,5,0.2353,0.3775,no
CAPDC_SYNY3,P73562,Reference,Bacteria,387,"Decarboxylase involved in the biosynthesis of spermidine via the carboxyaminopropylagmatine (CAPA) pathway. Catalyzes the decarboxylation of CAPA to form aminopropylagmatine (APA). Can also decarboxylate carboxyspermidine and carboxynorspermidine, but not ornithine, arginine, lysine and meso- diaminopimelate.","Decarboxylase involved in the biosynthesis of spermidine via the carboxyaminopropylagmatine (CAPA) pathway. Catalyzes the decarboxylation of CAPA to form aminopropylagmatine (APA). Can also decarboxylate carboxyspermidine and carboxynorspermidine, but not ornithine, arginine, lysine and meso- diaminopimelate.",,,,,,,GO:0008836,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.3775,no
MFMB_ANNMO,P9WEG1,ESM2Text,Eukaryota,2493,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O- desmethylfendlerol. Within the pathway, mfmB catalyzes the first step that leads to the synthesis of 3,5- dimethylorsellinic acid (DMOA) via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations. DMOA is then transformed into the phthalide 5,7- dihydroxy-4-(hydroxymethyl)-6-methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O-methylation to yield 5-hydroxy-4- (hydroxymethyl)-7-methoxy-6-methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy-4-(hydroxymethyl)-7-methoxy-6- methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5- O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome monooxygenase P450 claM then catalyzes the dimerization of nataloe-emodin to cladofulvin.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004315; GO:0004312; GO:0008168; GO:0008236,,GO:0016746,,,,,0.6022,,,,1,0.6022,0.2478,no
MFMB_ANNMO,P9WEG1,Prot2Text,Eukaryota,2493,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O- desmethylfendlerol. Within the pathway, mfmB catalyzes the first step that leads to the synthesis of 3,5- dimethylorsellinic acid (DMOA) via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations. DMOA is then transformed into the phthalide 5,7- dihydroxy-4-(hydroxymethyl)-6-methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O-methylation to yield 5-hydroxy-4- (hydroxymethyl)-7-methoxy-6-methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy-4-(hydroxymethyl)-7-methoxy-6- methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5- O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004315; GO:0004312; GO:0008168; GO:0008236,GO:0016746,GO:0016747,GO:0016747,GO:0016746,GO:0016747,0.6022,0.653,0.653,0.6022,0.653,5,0.6327,0.2478,no
MFMB_ANNMO,P9WEG1,ProtT3,Eukaryota,2493,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O- desmethylfendlerol. Within the pathway, mfmB catalyzes the first step that leads to the synthesis of 3,5- dimethylorsellinic acid (DMOA) via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations. DMOA is then transformed into the phthalide 5,7- dihydroxy-4-(hydroxymethyl)-6-methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O-methylation to yield 5-hydroxy-4- (hydroxymethyl)-7-methoxy-6-methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy-4-(hydroxymethyl)-7-methoxy-6- methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5- O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004315; GO:0004312; GO:0008168; GO:0008236,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016747,0.6022,0.6022,0.6022,0.653,0.653,5,0.6225,0.2478,no
MFMB_ANNMO,P9WEG1,ProtTale,Eukaryota,2493,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O- desmethylfendlerol. Within the pathway, mfmB catalyzes the first step that leads to the synthesis of 3,5- dimethylorsellinic acid (DMOA) via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations. DMOA is then transformed into the phthalide 5,7- dihydroxy-4-(hydroxymethyl)-6-methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O-methylation to yield 5-hydroxy-4- (hydroxymethyl)-7-methoxy-6-methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy-4-(hydroxymethyl)-7-methoxy-6- methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5- O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004315; GO:0004312; GO:0008168; GO:0008236,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.6022,0.6022,0.6022,0.6022,0.6022,5,0.6022,0.2478,no
MFMB_ANNMO,P9WEG1,Protein2Text,Eukaryota,2493,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O- desmethylfendlerol. Within the pathway, mfmB catalyzes the first step that leads to the synthesis of 3,5- dimethylorsellinic acid (DMOA) via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations. DMOA is then transformed into the phthalide 5,7- dihydroxy-4-(hydroxymethyl)-6-methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O-methylation to yield 5-hydroxy-4- (hydroxymethyl)-7-methoxy-6-methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy-4-(hydroxymethyl)-7-methoxy-6- methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5- O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.","This protein is involved in the synthesis of coenzyme A (CoA) from pantetheine and ATP. It catalyzes the transfer of the phosphopantetheine moiety from ATP to the 4'-phosphopantetheine arm of CoA. This is a key step in the biosynthesis of CoA, which is essential for the activation of various carboxylic acids in the cell.",No,No,No,No,No,not-Yes,GO:0004315; GO:0004312; GO:0008168; GO:0008236,,GO:0004595,,,GO:0004140,,0.2923,,,0.3011,2,0.2967,0.2478,no
MFMB_ANNMO,P9WEG1,Reference,Eukaryota,2493,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O- desmethylfendlerol. Within the pathway, mfmB catalyzes the first step that leads to the synthesis of 3,5- dimethylorsellinic acid (DMOA) via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations. DMOA is then transformed into the phthalide 5,7- dihydroxy-4-(hydroxymethyl)-6-methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O-methylation to yield 5-hydroxy-4- (hydroxymethyl)-7-methoxy-6-methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy-4-(hydroxymethyl)-7-methoxy-6- methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5- O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O- desmethylfendlerol. Within the pathway, mfmB catalyzes the first step that leads to the synthesis of 3,5- dimethylorsellinic acid (DMOA) via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations. DMOA is then transformed into the phthalide 5,7- dihydroxy-4-(hydroxymethyl)-6-methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O-methylation to yield 5-hydroxy-4- (hydroxymethyl)-7-methoxy-6-methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy-4-(hydroxymethyl)-7-methoxy-6- methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5- O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.",,,,,,,GO:0004315; GO:0004312; GO:0008168; GO:0008236,GO:0016740,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.5819,0.6022,0.6022,0.653,0.6022,5,0.6083,0.2478,no
MFME_ANNMO,P9WEG4,ESM2Text,Eukaryota,401,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O- desmethylfendlerol. Within the pathway, mfmE catalyzes the 7-O-methylation of the phthalide 5,7-dihydroxy-4- (hydroxymethyl)-6-methylphthalide to yield 5-hydroxy-4-(hydroxymethyl)- 7-methoxy-6-methylphthalide. The biosynthesis of 11'- O-desmethylfendlerol begins with the NR-PKS mfmB that forms 3,5- dimethylorsellinic acid (DMOA), which is then transformed into the phthalide 5,7-dihydroxy-4-(hydroxymethyl)-6-methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O-methylation to yield 5-hydroxy-4-(hydroxymethyl)-7-methoxy-6-methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy-4-(hydroxymethyl)-7- methoxy-6-methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5- O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the tropolone class of fungal maleic anhydrides. The pathway begins with the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide synthase (PKS) tropA. 3-methylorcinaldehyde is the substrate for the FAD-dependent monooxygenase tropB to yield a dearomatized hydroxycyclohexadione. The 2-oxoglutarate-dependent dioxygenase tropC then performs the oxidative ring expansion to provide the first tropolone metabolite stipitaldehyde. Trop D converts stipitaldehyde into stipitacetal which is in turn converted to stipitalide by the short-chain dehydrogenase/reductase tropE. The next steps involve tropF, tropG, tropH, tropI and tropJ to form successive tropolone maleic anhydrides including stipitaldehydic, stipitatonic and stipitatic acids.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2311,no
MFME_ANNMO,P9WEG4,Prot2Text,Eukaryota,401,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O- desmethylfendlerol. Within the pathway, mfmE catalyzes the 7-O-methylation of the phthalide 5,7-dihydroxy-4- (hydroxymethyl)-6-methylphthalide to yield 5-hydroxy-4-(hydroxymethyl)- 7-methoxy-6-methylphthalide. The biosynthesis of 11'- O-desmethylfendlerol begins with the NR-PKS mfmB that forms 3,5- dimethylorsellinic acid (DMOA), which is then transformed into the phthalide 5,7-dihydroxy-4-(hydroxymethyl)-6-methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O-methylation to yield 5-hydroxy-4-(hydroxymethyl)-7-methoxy-6-methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy-4-(hydroxymethyl)-7- methoxy-6-methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5- O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate tolerance, py",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2311,no
MFME_ANNMO,P9WEG4,ProtT3,Eukaryota,401,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O- desmethylfendlerol. Within the pathway, mfmE catalyzes the 7-O-methylation of the phthalide 5,7-dihydroxy-4- (hydroxymethyl)-6-methylphthalide to yield 5-hydroxy-4-(hydroxymethyl)- 7-methoxy-6-methylphthalide. The biosynthesis of 11'- O-desmethylfendlerol begins with the NR-PKS mfmB that forms 3,5- dimethylorsellinic acid (DMOA), which is then transformed into the phthalide 5,7-dihydroxy-4-(hydroxymethyl)-6-methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O-methylation to yield 5-hydroxy-4-(hydroxymethyl)-7-methoxy-6-methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy-4-(hydroxymethyl)-7- methoxy-6-methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5- O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By similarity). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (By similarity). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the ter",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2311,no
MFME_ANNMO,P9WEG4,ProtTale,Eukaryota,401,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O- desmethylfendlerol. Within the pathway, mfmE catalyzes the 7-O-methylation of the phthalide 5,7-dihydroxy-4- (hydroxymethyl)-6-methylphthalide to yield 5-hydroxy-4-(hydroxymethyl)- 7-methoxy-6-methylphthalide. The biosynthesis of 11'- O-desmethylfendlerol begins with the NR-PKS mfmB that forms 3,5- dimethylorsellinic acid (DMOA), which is then transformed into the phthalide 5,7-dihydroxy-4-(hydroxymethyl)-6-methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O-methylation to yield 5-hydroxy-4-(hydroxymethyl)-7-methoxy-6-methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy-4-(hydroxymethyl)-7- methoxy-6-methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5- O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the saturated C-C bonds",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2311,no
MFME_ANNMO,P9WEG4,Protein2Text,Eukaryota,401,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O- desmethylfendlerol. Within the pathway, mfmE catalyzes the 7-O-methylation of the phthalide 5,7-dihydroxy-4- (hydroxymethyl)-6-methylphthalide to yield 5-hydroxy-4-(hydroxymethyl)- 7-methoxy-6-methylphthalide. The biosynthesis of 11'- O-desmethylfendlerol begins with the NR-PKS mfmB that forms 3,5- dimethylorsellinic acid (DMOA), which is then transformed into the phthalide 5,7-dihydroxy-4-(hydroxymethyl)-6-methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O-methylation to yield 5-hydroxy-4-(hydroxymethyl)-7-methoxy-6-methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy-4-(hydroxymethyl)-7- methoxy-6-methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5- O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.","This protein is involved in the molecular function of being a part of the O-methyltransferase family. Specifically, it is likely to be involved in the O-methylation of a substrate, such as a phenolic compound, using S-adenosylmethionine (SAM) as a methyl donor. This is a common biochemical process that is important for the synthesis of various secondary metabolites and for the modification of lipids and other molecules.",Maybe,Maybe,Yes,Maybe,Yes,not-Yes,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2311,no
MFME_ANNMO,P9WEG4,Reference,Eukaryota,401,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O- desmethylfendlerol. Within the pathway, mfmE catalyzes the 7-O-methylation of the phthalide 5,7-dihydroxy-4- (hydroxymethyl)-6-methylphthalide to yield 5-hydroxy-4-(hydroxymethyl)- 7-methoxy-6-methylphthalide. The biosynthesis of 11'- O-desmethylfendlerol begins with the NR-PKS mfmB that forms 3,5- dimethylorsellinic acid (DMOA), which is then transformed into the phthalide 5,7-dihydroxy-4-(hydroxymethyl)-6-methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O-methylation to yield 5-hydroxy-4-(hydroxymethyl)-7-methoxy-6-methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy-4-(hydroxymethyl)-7- methoxy-6-methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5- O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O- desmethylfendlerol. Within the pathway, mfmE catalyzes the 7-O-methylation of the phthalide 5,7-dihydroxy-4- (hydroxymethyl)-6-methylphthalide to yield 5-hydroxy-4-(hydroxymethyl)- 7-methoxy-6-methylphthalide. The biosynthesis of 11'- O-desmethylfendlerol begins with the NR-PKS mfmB that forms 3,5- dimethylorsellinic acid (DMOA), which is then transformed into the phthalide 5,7-dihydroxy-4-(hydroxymethyl)-6-methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O-methylation to yield 5-hydroxy-4-(hydroxymethyl)-7-methoxy-6-methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy-4-(hydroxymethyl)-7- methoxy-6-methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5- O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.",,,,,,,GO:0008171; GO:0046983,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.2311,no
FSOF_HUMFU,P9WEG8,ESM2Text,Eukaryota,419,"Terpene cyclase-glycosyl transferase fusion protein; part of the gene cluster that mediates the biosynthesis of the enfumafungin- type antibiotic, fuscoatroside. Within the pathway, fsoF catalyzes the acetylation of C2-alpha-OH following the C2 hydroxylation by the cytochrome monooxygenase fsoD. The fuscoatroside biosynthesis is initiated by the cyclization of 2,3(S)-oxidosqualene through FsoA's terpene cyclase (TC) domain, leading to the formation of the fernane skeleton isomotiol, harboring a fernane triterpene skeleton with a C8-C9 double bond. Subsequently, C2- alpha-hydroxylation mediated by fsoD results in the production of 2- alpha-hydroxy-isomotiol, which is further acetylated by fsoF. The glycosyltransferase (GT) domain of FsoA may convert isomotiol, 2-alpha- hydroxy-isomotiol, and the acetylated derivative of 2-alpha-hydroxy- isomotiol into their corresponding glycosides 3-O-(beta-D- glucopyranosyl)-isomotiol, 3-O-(beta-D-glucopyranosyl)-2-alpha-hydroxy- isomotiol, and 3-O-(beta-D-glucopyranosyl)-2-alpha-acetoxy-isomotiol, which then undergo oxidative cleavage under the action of fsoE to form s 2-deacetoxy-fuscoatroside, 2-deacetyl-fuscoatroside, and fuscoatroside, respectively. Although hydroxylation followed by acetylation of 3-O-(beta-D-glucopyranosyl)-isomotiol and 2-deacetoxy- fuscoatroside by fsoD and fsoF could not be ruled out, this process is likely to occur with difficulty due to bulky steric hindrance caused by the presence of a glycan at C3 in these compounds. Interestingly, fsoE can also utilize the aglycones isomotiol and 2-alpha-hydroxy-isomotiol as substrates to generate 19-beta-hydroxy-isomotiol and 2-alpha,19- beta-dihydroxy-isomotiol, respectively. These reactions occur with lower efficiency. Finally, fsoE can further convert 2-alpha,19-beta- dihydroxy-isomotiol into 2-alpha-hydroxy-ismotiol-19-one and 2-alpha- hydroxy-ismotiol-19-one into 2-deacetyl-3-deglucopyranosyl- fuscoatroside.","Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome monooxygenase P450 claM then catalyzes the dimerization of nataloe-emodin to cladofulvin.",No,Maybe,Maybe,Maybe,No,not-Yes,GO:0008374,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.3555,no
FSOF_HUMFU,P9WEG8,Prot2Text,Eukaryota,419,"Terpene cyclase-glycosyl transferase fusion protein; part of the gene cluster that mediates the biosynthesis of the enfumafungin- type antibiotic, fuscoatroside. Within the pathway, fsoF catalyzes the acetylation of C2-alpha-OH following the C2 hydroxylation by the cytochrome monooxygenase fsoD. The fuscoatroside biosynthesis is initiated by the cyclization of 2,3(S)-oxidosqualene through FsoA's terpene cyclase (TC) domain, leading to the formation of the fernane skeleton isomotiol, harboring a fernane triterpene skeleton with a C8-C9 double bond. Subsequently, C2- alpha-hydroxylation mediated by fsoD results in the production of 2- alpha-hydroxy-isomotiol, which is further acetylated by fsoF. The glycosyltransferase (GT) domain of FsoA may convert isomotiol, 2-alpha- hydroxy-isomotiol, and the acetylated derivative of 2-alpha-hydroxy- isomotiol into their corresponding glycosides 3-O-(beta-D- glucopyranosyl)-isomotiol, 3-O-(beta-D-glucopyranosyl)-2-alpha-hydroxy- isomotiol, and 3-O-(beta-D-glucopyranosyl)-2-alpha-acetoxy-isomotiol, which then undergo oxidative cleavage under the action of fsoE to form s 2-deacetoxy-fuscoatroside, 2-deacetyl-fuscoatroside, and fuscoatroside, respectively. Although hydroxylation followed by acetylation of 3-O-(beta-D-glucopyranosyl)-isomotiol and 2-deacetoxy- fuscoatroside by fsoD and fsoF could not be ruled out, this process is likely to occur with difficulty due to bulky steric hindrance caused by the presence of a glycan at C3 in these compounds. Interestingly, fsoE can also utilize the aglycones isomotiol and 2-alpha-hydroxy-isomotiol as substrates to generate 19-beta-hydroxy-isomotiol and 2-alpha,19- beta-dihydroxy-isomotiol, respectively. These reactions occur with lower efficiency. Finally, fsoE can further convert 2-alpha,19-beta- dihydroxy-isomotiol into 2-alpha-hydroxy-ismotiol-19-one and 2-alpha- hydroxy-ismotiol-19-one into 2-deacetyl-3-deglucopyranosyl- fuscoatroside.","Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate tolerance, py",No,Maybe,Maybe,Maybe,No,not-Yes,GO:0008374,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.3555,no
FSOF_HUMFU,P9WEG8,ProtT3,Eukaryota,419,"Terpene cyclase-glycosyl transferase fusion protein; part of the gene cluster that mediates the biosynthesis of the enfumafungin- type antibiotic, fuscoatroside. Within the pathway, fsoF catalyzes the acetylation of C2-alpha-OH following the C2 hydroxylation by the cytochrome monooxygenase fsoD. The fuscoatroside biosynthesis is initiated by the cyclization of 2,3(S)-oxidosqualene through FsoA's terpene cyclase (TC) domain, leading to the formation of the fernane skeleton isomotiol, harboring a fernane triterpene skeleton with a C8-C9 double bond. Subsequently, C2- alpha-hydroxylation mediated by fsoD results in the production of 2- alpha-hydroxy-isomotiol, which is further acetylated by fsoF. The glycosyltransferase (GT) domain of FsoA may convert isomotiol, 2-alpha- hydroxy-isomotiol, and the acetylated derivative of 2-alpha-hydroxy- isomotiol into their corresponding glycosides 3-O-(beta-D- glucopyranosyl)-isomotiol, 3-O-(beta-D-glucopyranosyl)-2-alpha-hydroxy- isomotiol, and 3-O-(beta-D-glucopyranosyl)-2-alpha-acetoxy-isomotiol, which then undergo oxidative cleavage under the action of fsoE to form s 2-deacetoxy-fuscoatroside, 2-deacetyl-fuscoatroside, and fuscoatroside, respectively. Although hydroxylation followed by acetylation of 3-O-(beta-D-glucopyranosyl)-isomotiol and 2-deacetoxy- fuscoatroside by fsoD and fsoF could not be ruled out, this process is likely to occur with difficulty due to bulky steric hindrance caused by the presence of a glycan at C3 in these compounds. Interestingly, fsoE can also utilize the aglycones isomotiol and 2-alpha-hydroxy-isomotiol as substrates to generate 19-beta-hydroxy-isomotiol and 2-alpha,19- beta-dihydroxy-isomotiol, respectively. These reactions occur with lower efficiency. Finally, fsoE can further convert 2-alpha,19-beta- dihydroxy-isomotiol into 2-alpha-hydroxy-ismotiol-19-one and 2-alpha- hydroxy-ismotiol-19-one into 2-deacetyl-3-deglucopyranosyl- fuscoatroside.","Acetyltransferase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties . L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O",No,Maybe,Maybe,Maybe,No,not-Yes,GO:0008374,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.3555,no
FSOF_HUMFU,P9WEG8,ProtTale,Eukaryota,419,"Terpene cyclase-glycosyl transferase fusion protein; part of the gene cluster that mediates the biosynthesis of the enfumafungin- type antibiotic, fuscoatroside. Within the pathway, fsoF catalyzes the acetylation of C2-alpha-OH following the C2 hydroxylation by the cytochrome monooxygenase fsoD. The fuscoatroside biosynthesis is initiated by the cyclization of 2,3(S)-oxidosqualene through FsoA's terpene cyclase (TC) domain, leading to the formation of the fernane skeleton isomotiol, harboring a fernane triterpene skeleton with a C8-C9 double bond. Subsequently, C2- alpha-hydroxylation mediated by fsoD results in the production of 2- alpha-hydroxy-isomotiol, which is further acetylated by fsoF. The glycosyltransferase (GT) domain of FsoA may convert isomotiol, 2-alpha- hydroxy-isomotiol, and the acetylated derivative of 2-alpha-hydroxy- isomotiol into their corresponding glycosides 3-O-(beta-D- glucopyranosyl)-isomotiol, 3-O-(beta-D-glucopyranosyl)-2-alpha-hydroxy- isomotiol, and 3-O-(beta-D-glucopyranosyl)-2-alpha-acetoxy-isomotiol, which then undergo oxidative cleavage under the action of fsoE to form s 2-deacetoxy-fuscoatroside, 2-deacetyl-fuscoatroside, and fuscoatroside, respectively. Although hydroxylation followed by acetylation of 3-O-(beta-D-glucopyranosyl)-isomotiol and 2-deacetoxy- fuscoatroside by fsoD and fsoF could not be ruled out, this process is likely to occur with difficulty due to bulky steric hindrance caused by the presence of a glycan at C3 in these compounds. Interestingly, fsoE can also utilize the aglycones isomotiol and 2-alpha-hydroxy-isomotiol as substrates to generate 19-beta-hydroxy-isomotiol and 2-alpha,19- beta-dihydroxy-isomotiol, respectively. These reactions occur with lower efficiency. Finally, fsoE can further convert 2-alpha,19-beta- dihydroxy-isomotiol into 2-alpha-hydroxy-ismotiol-19-one and 2-alpha- hydroxy-ismotiol-19-one into 2-deacetyl-3-deglucopyranosyl- fuscoatroside.","Acetyltransferase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the saturated C-C bonds of",No,Maybe,Maybe,Maybe,No,not-Yes,GO:0008374,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.3555,no
FSOF_HUMFU,P9WEG8,Protein2Text,Eukaryota,419,"Terpene cyclase-glycosyl transferase fusion protein; part of the gene cluster that mediates the biosynthesis of the enfumafungin- type antibiotic, fuscoatroside. Within the pathway, fsoF catalyzes the acetylation of C2-alpha-OH following the C2 hydroxylation by the cytochrome monooxygenase fsoD. The fuscoatroside biosynthesis is initiated by the cyclization of 2,3(S)-oxidosqualene through FsoA's terpene cyclase (TC) domain, leading to the formation of the fernane skeleton isomotiol, harboring a fernane triterpene skeleton with a C8-C9 double bond. Subsequently, C2- alpha-hydroxylation mediated by fsoD results in the production of 2- alpha-hydroxy-isomotiol, which is further acetylated by fsoF. The glycosyltransferase (GT) domain of FsoA may convert isomotiol, 2-alpha- hydroxy-isomotiol, and the acetylated derivative of 2-alpha-hydroxy- isomotiol into their corresponding glycosides 3-O-(beta-D- glucopyranosyl)-isomotiol, 3-O-(beta-D-glucopyranosyl)-2-alpha-hydroxy- isomotiol, and 3-O-(beta-D-glucopyranosyl)-2-alpha-acetoxy-isomotiol, which then undergo oxidative cleavage under the action of fsoE to form s 2-deacetoxy-fuscoatroside, 2-deacetyl-fuscoatroside, and fuscoatroside, respectively. Although hydroxylation followed by acetylation of 3-O-(beta-D-glucopyranosyl)-isomotiol and 2-deacetoxy- fuscoatroside by fsoD and fsoF could not be ruled out, this process is likely to occur with difficulty due to bulky steric hindrance caused by the presence of a glycan at C3 in these compounds. Interestingly, fsoE can also utilize the aglycones isomotiol and 2-alpha-hydroxy-isomotiol as substrates to generate 19-beta-hydroxy-isomotiol and 2-alpha,19- beta-dihydroxy-isomotiol, respectively. These reactions occur with lower efficiency. Finally, fsoE can further convert 2-alpha,19-beta- dihydroxy-isomotiol into 2-alpha-hydroxy-ismotiol-19-one and 2-alpha- hydroxy-ismotiol-19-one into 2-deacetyl-3-deglucopyranosyl- fuscoatroside.","This protein is involved in the molecular function of transferring a methyl group from one molecule to another. More specifically, it is a methyltransferase that is involved in the modification of sterols.",No,No,No,No,No,not-Yes,GO:0008374,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.3987,0.3987,0.3987,0.3987,0.3987,5,0.3987,0.3555,no
FSOF_HUMFU,P9WEG8,Reference,Eukaryota,419,"Terpene cyclase-glycosyl transferase fusion protein; part of the gene cluster that mediates the biosynthesis of the enfumafungin- type antibiotic, fuscoatroside. Within the pathway, fsoF catalyzes the acetylation of C2-alpha-OH following the C2 hydroxylation by the cytochrome monooxygenase fsoD. The fuscoatroside biosynthesis is initiated by the cyclization of 2,3(S)-oxidosqualene through FsoA's terpene cyclase (TC) domain, leading to the formation of the fernane skeleton isomotiol, harboring a fernane triterpene skeleton with a C8-C9 double bond. Subsequently, C2- alpha-hydroxylation mediated by fsoD results in the production of 2- alpha-hydroxy-isomotiol, which is further acetylated by fsoF. The glycosyltransferase (GT) domain of FsoA may convert isomotiol, 2-alpha- hydroxy-isomotiol, and the acetylated derivative of 2-alpha-hydroxy- isomotiol into their corresponding glycosides 3-O-(beta-D- glucopyranosyl)-isomotiol, 3-O-(beta-D-glucopyranosyl)-2-alpha-hydroxy- isomotiol, and 3-O-(beta-D-glucopyranosyl)-2-alpha-acetoxy-isomotiol, which then undergo oxidative cleavage under the action of fsoE to form s 2-deacetoxy-fuscoatroside, 2-deacetyl-fuscoatroside, and fuscoatroside, respectively. Although hydroxylation followed by acetylation of 3-O-(beta-D-glucopyranosyl)-isomotiol and 2-deacetoxy- fuscoatroside by fsoD and fsoF could not be ruled out, this process is likely to occur with difficulty due to bulky steric hindrance caused by the presence of a glycan at C3 in these compounds. Interestingly, fsoE can also utilize the aglycones isomotiol and 2-alpha-hydroxy-isomotiol as substrates to generate 19-beta-hydroxy-isomotiol and 2-alpha,19- beta-dihydroxy-isomotiol, respectively. These reactions occur with lower efficiency. Finally, fsoE can further convert 2-alpha,19-beta- dihydroxy-isomotiol into 2-alpha-hydroxy-ismotiol-19-one and 2-alpha- hydroxy-ismotiol-19-one into 2-deacetyl-3-deglucopyranosyl- fuscoatroside.","Terpene cyclase-glycosyl transferase fusion protein; part of the gene cluster that mediates the biosynthesis of the enfumafungin- type antibiotic, fuscoatroside. Within the pathway, fsoF catalyzes the acetylation of C2-alpha-OH following the C2 hydroxylation by the cytochrome monooxygenase fsoD. The fuscoatroside biosynthesis is initiated by the cyclization of 2,3(S)-oxidosqualene through FsoA's terpene cyclase (TC) domain, leading to the formation of the fernane skeleton isomotiol, harboring a fernane triterpene skeleton with a C8-C9 double bond. Subsequently, C2- alpha-hydroxylation mediated by fsoD results in the production of 2- alpha-hydroxy-isomotiol, which is further acetylated by fsoF. The glycosyltransferase (GT) domain of FsoA may convert isomotiol, 2-alpha- hydroxy-isomotiol, and the acetylated derivative of 2-alpha-hydroxy- isomotiol into their corresponding glycosides 3-O-(beta-D- glucopyranosyl)-isomotiol, 3-O-(beta-D-glucopyranosyl)-2-alpha-hydroxy- isomotiol, and 3-O-(beta-D-glucopyranosyl)-2-alpha-acetoxy-isomotiol, which then undergo oxidative cleavage under the action of fsoE to form s 2-deacetoxy-fuscoatroside, 2-deacetyl-fuscoatroside, and fuscoatroside, respectively. Although hydroxylation followed by acetylation of 3-O-(beta-D-glucopyranosyl)-isomotiol and 2-deacetoxy- fuscoatroside by fsoD and fsoF could not be ruled out, this process is likely to occur with difficulty due to bulky steric hindrance caused by the presence of a glycan at C3 in these compounds. Interestingly, fsoE can also utilize the aglycones isomotiol and 2-alpha-hydroxy-isomotiol as substrates to generate 19-beta-hydroxy-isomotiol and 2-alpha,19- beta-dihydroxy-isomotiol, respectively. These reactions occur with lower efficiency. Finally, fsoE can further convert 2-alpha,19-beta- dihydroxy-isomotiol into 2-alpha-hydroxy-ismotiol-19-one and 2-alpha- hydroxy-ismotiol-19-one into 2-deacetyl-3-deglucopyranosyl- fuscoatroside.",,,,,,,GO:0008374,GO:0016829; GO:0016757,GO:0016829; GO:0016757,GO:0010333; GO:0016757,GO:0016829; GO:0016757,GO:0010333; GO:0016757,0.4398,0.4398,0.388,0.4398,0.388,5,0.4191,0.3555,no
PREU6_PREIS,P9WET2,ESM2Text,Eukaryota,2197,"Non-reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product (Probable). The first step in the pathway is performed by Preu6 that condenses 2 acetyl-CoA starter units with 6 malonyl-CoA units to produce lecanoric acid (LA), also known as orsellinate depside, an intermediate that has significant antifungal activity against the plant pathogen Botryosphaeria berengeriana. The biosynthesis probably occurs via the formation of 2 orsellinate intermediates fused together by the C-terminal thioesterase (TE) domain that finally releases lecanoric acid (Probable).","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome monooxygenase P450 claM then catalyzes the dimerization of nataloe-emodin to cladofulvin.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004312; GO:0031177,,GO:0016746,,,,,0.5216,,,,1,0.5216,0.2197,no
PREU6_PREIS,P9WET2,Prot2Text,Eukaryota,2197,"Non-reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product (Probable). The first step in the pathway is performed by Preu6 that condenses 2 acetyl-CoA starter units with 6 malonyl-CoA units to produce lecanoric acid (LA), also known as orsellinate depside, an intermediate that has significant antifungal activity against the plant pathogen Botryosphaeria berengeriana. The biosynthesis probably occurs via the formation of 2 orsellinate intermediates fused together by the C-terminal thioesterase (TE) domain that finally releases lecanoric acid (Probable).","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004312; GO:0031177,GO:0016746,GO:0016747,GO:0016747,GO:0016746,GO:0016747,0.5216,0.6029,0.6029,0.5216,0.6029,5,0.5704,0.2197,no
PREU6_PREIS,P9WET2,ProtT3,Eukaryota,2197,"Non-reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product (Probable). The first step in the pathway is performed by Preu6 that condenses 2 acetyl-CoA starter units with 6 malonyl-CoA units to produce lecanoric acid (LA), also known as orsellinate depside, an intermediate that has significant antifungal activity against the plant pathogen Botryosphaeria berengeriana. The biosynthesis probably occurs via the formation of 2 orsellinate intermediates fused together by the C-terminal thioesterase (TE) domain that finally releases lecanoric acid (Probable).","Polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004312; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016747,0.5216,0.5216,0.5216,0.6029,0.6029,5,0.5541,0.2197,no
PREU6_PREIS,P9WET2,ProtTale,Eukaryota,2197,"Non-reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product (Probable). The first step in the pathway is performed by Preu6 that condenses 2 acetyl-CoA starter units with 6 malonyl-CoA units to produce lecanoric acid (LA), also known as orsellinate depside, an intermediate that has significant antifungal activity against the plant pathogen Botryosphaeria berengeriana. The biosynthesis probably occurs via the formation of 2 orsellinate intermediates fused together by the C-terminal thioesterase (TE) domain that finally releases lecanoric acid (Probable).","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004312; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.5216,0.5216,0.5216,0.5216,0.5216,5,0.5216,0.2197,no
PREU6_PREIS,P9WET2,Protein2Text,Eukaryota,2197,"Non-reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product (Probable). The first step in the pathway is performed by Preu6 that condenses 2 acetyl-CoA starter units with 6 malonyl-CoA units to produce lecanoric acid (LA), also known as orsellinate depside, an intermediate that has significant antifungal activity against the plant pathogen Botryosphaeria berengeriana. The biosynthesis probably occurs via the formation of 2 orsellinate intermediates fused together by the C-terminal thioesterase (TE) domain that finally releases lecanoric acid (Probable).","The molecular function of this protein is an enzyme that catalyzes the conversion of a substrate into a product, specifically involved in the synthesis of polyketides, a class of compounds that are important in various biological processes, including the production of antibiotics, hormones, and pigments.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0031177,GO:0016746,,,,GO:0033797,0.5216,,,,0.2253,2,0.3734,0.2197,no
PREU6_PREIS,P9WET2,Reference,Eukaryota,2197,"Non-reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product (Probable). The first step in the pathway is performed by Preu6 that condenses 2 acetyl-CoA starter units with 6 malonyl-CoA units to produce lecanoric acid (LA), also known as orsellinate depside, an intermediate that has significant antifungal activity against the plant pathogen Botryosphaeria berengeriana. The biosynthesis probably occurs via the formation of 2 orsellinate intermediates fused together by the C-terminal thioesterase (TE) domain that finally releases lecanoric acid (Probable).","Non-reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product (Probable). The first step in the pathway is performed by Preu6 that condenses 2 acetyl-CoA starter units with 6 malonyl-CoA units to produce lecanoric acid (LA), also known as orsellinate depside, an intermediate that has significant antifungal activity against the plant pathogen Botryosphaeria berengeriana. The biosynthesis probably occurs via the formation of 2 orsellinate intermediates fused together by the C-terminal thioesterase (TE) domain that finally releases lecanoric acid (Probable).",,,,,,,GO:0004312; GO:0031177,GO:0016740,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.4436,0.5216,0.5216,0.6029,0.5216,5,0.5223,0.2197,no
PREU5_PREIS,P9WET4,ESM2Text,Eukaryota,2524,Highly reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product.,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential tr",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177,,GO:0016746,,,,,0.5204,,,,1,0.5204,0.3176,no
PREU5_PREIS,P9WET4,Prot2Text,Eukaryota,2524,Highly reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product.,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177,GO:0016746,GO:0016747,GO:0016747,GO:0016746,GO:0016747,0.5204,0.536,0.536,0.5204,0.536,5,0.5298,0.3176,no
PREU5_PREIS,P9WET4,ProtT3,Eukaryota,2524,Highly reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product.,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins . The first step of the pathway is the synthesis of 3,5",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016747,0.5204,0.5204,0.5204,0.536,0.536,5,0.5266,0.3176,no
PREU5_PREIS,P9WET4,ProtTale,Eukaryota,2524,Highly reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product.,"Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. Within the pathway, ptmC is responsible for the cyclization of prepenitrem F to penitrem B. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3-glycerol phosphate with GGPP by ptmC then forms 3-",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.5204,0.5204,0.5204,0.5204,0.5204,5,0.5204,0.3176,no
PREU5_PREIS,P9WET4,Protein2Text,Eukaryota,2524,Highly reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product.,"The molecular function of the protein is to synthesize fatty acids. It is involved in the production of fatty acids through the fatty acid synthesis pathway. Specifically, it is a condensing enzyme that catalyzes the condensation of fatty acyl-CoA and malonyl-CoA to produce a beta-ketoacyl-CoA intermediate. This reaction is a key step in the fatty acid synthesis pathway, which produces fatty acids from acetyl-CoA and malonyl-CoA. The protein is also known as a beta-ketoacyl-acyl carrier protein synthase I, suggesting its role in the synthesis of fatty acids that are attached to an acyl carrier protein (ACP). The protein is likely to be involved in the production of fatty acids that are used for various cellular processes, such as membrane lipid synthesis, energy storage, and signaling molecule production.",No,Maybe,No,No,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.567,0.567,0.567,0.567,0.567,5,0.567,0.3176,no
PREU5_PREIS,P9WET4,Reference,Eukaryota,2524,Highly reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product.,Highly reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product.,,,,,,,GO:0004312; GO:0008168; GO:0016491; GO:0031177,GO:0016740,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.5397,0.5204,0.5204,0.536,0.5204,5,0.5274,0.3176,no
PREU4_PREIS,P9WET5,ESM2Text,Eukaryota,2151,Non-reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product (Probable). The first step in the pathway is performed by Preu4 that produces two major yellow-colored compounds which structures are not stable and hard to be characterized.,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004315; GO:0004312; GO:0031177,,GO:0016746,,,,,0.5734,,,,1,0.5734,0.2214,no
PREU4_PREIS,P9WET5,Prot2Text,Eukaryota,2151,Non-reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product (Probable). The first step in the pathway is performed by Preu4 that produces two major yellow-colored compounds which structures are not stable and hard to be characterized.,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004315; GO:0004312; GO:0031177,GO:0016746,GO:0016747,GO:0016747,GO:0016746,GO:0016747,0.5734,0.6667,0.6667,0.5734,0.6667,5,0.6294,0.2214,no
PREU4_PREIS,P9WET5,ProtT3,Eukaryota,2151,Non-reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product (Probable). The first step in the pathway is performed by Preu4 that produces two major yellow-colored compounds which structures are not stable and hard to be characterized.,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins . The first step of the pathway is the synthesis of 3,5",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004315; GO:0004312; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016747,0.5734,0.5734,0.5734,0.6667,0.6667,5,0.6107,0.2214,no
PREU4_PREIS,P9WET5,ProtTale,Eukaryota,2151,Non-reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product (Probable). The first step in the pathway is performed by Preu4 that produces two major yellow-colored compounds which structures are not stable and hard to be characterized.,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004315; GO:0004312; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.5734,0.5734,0.5734,0.5734,0.5734,5,0.5734,0.2214,no
PREU4_PREIS,P9WET5,Protein2Text,Eukaryota,2151,Non-reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product (Probable). The first step in the pathway is performed by Preu4 that produces two major yellow-colored compounds which structures are not stable and hard to be characterized.,"The molecular function of this protein is not explicitly stated in the provided text. However, based on its name and the context in which it is mentioned, it is likely involved in the synthesis of a compound, possibly a terpene, as part of a metabolic pathway.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0004315; GO:0004312; GO:0031177,,,,,,,,,,,0,,0.2214,no
PREU4_PREIS,P9WET5,Reference,Eukaryota,2151,Non-reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product (Probable). The first step in the pathway is performed by Preu4 that produces two major yellow-colored compounds which structures are not stable and hard to be characterized.,Non-reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product (Probable). The first step in the pathway is performed by Preu4 that produces two major yellow-colored compounds which structures are not stable and hard to be characterized.,,,,,,,GO:0004315; GO:0004312; GO:0031177,GO:0016740,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.4832,0.5734,0.5734,0.6667,0.5734,5,0.574,0.2214,no
PREU2_PREIS,P9WET7,ESM2Text,Eukaryota,2328,Reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product.,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177,,GO:0016746,,,,,0.5204,,,,1,0.5204,0.3433,no
PREU2_PREIS,P9WET7,Prot2Text,Eukaryota,2328,Reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product.,"Reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177,GO:0016746,GO:0016747,GO:0016747,GO:0016746,GO:0016747,0.5204,0.536,0.536,0.5204,0.536,5,0.5298,0.3433,no
PREU2_PREIS,P9WET7,ProtT3,Eukaryota,2328,Reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product.,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of aspirochlorine (or antibiotic A30641), an unusual halogenated spiro compound with distinctive antifungal properties due to selective inhibition of protein biosynthesis, and which is also active against bacteria, viruses, and murine tumor cells . The non-reducing polyketide synthase aclD is responsible for the synthesis of the polyketide backbone . The starter unit acyltransferase aclD",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016747,0.5204,0.5204,0.5204,0.536,0.536,5,0.5266,0.3433,no
PREU2_PREIS,P9WET7,ProtTale,Eukaryota,2328,Reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product.,"Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177,GO:0016746; GO:0016874,GO:0016746; GO:0016874,GO:0016746; GO:0016874,GO:0016746; GO:0016874,GO:0016746; GO:0016874,0.5536,0.5536,0.5536,0.5536,0.5536,5,0.5536,0.3433,no
PREU2_PREIS,P9WET7,Protein2Text,Eukaryota,2328,Reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product.,"The molecular function of this protein is likely to be involved in the synthesis of fatty acids, specifically in the process of elongation. However, without more specific information, it is difficult to determine the exact function of this protein. 

More precisely, this protein is a beta-ketoacyl synthase, which is a type of enzyme that catalyzes the elongation of fatty acids by adding two carbons to the growing chain.",Vague,Maybe,No,No,Maybe,not-Yes,GO:0004312; GO:0008168; GO:0016491; GO:0031177,GO:0004315,GO:0004315,GO:0004315,GO:0004315,GO:0033797,0.4586,0.4586,0.4586,0.4586,0.4698,5,0.4608,0.3433,no
PREU2_PREIS,P9WET7,Reference,Eukaryota,2328,Reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product.,Reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product.,,,,,,,GO:0004312; GO:0008168; GO:0016491; GO:0031177,GO:0016740,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.5397,0.5204,0.5204,0.536,0.5204,5,0.5274,0.3433,no
PREU1_PREIS,P9WET8,ESM2Text,Eukaryota,2388,Highly reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product.,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential tr",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177,,GO:0016746,,,,,0.5549,,,,1,0.5549,0.222,no
PREU1_PREIS,P9WET8,Prot2Text,Eukaryota,2388,Highly reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product.,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177,GO:0016746,GO:0016747,GO:0016747,GO:0016746,GO:0016747,0.5549,0.6148,0.6148,0.5549,0.6148,5,0.5908,0.222,no
PREU1_PREIS,P9WET8,ProtT3,Eukaryota,2388,Highly reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product.,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016747,0.5549,0.5549,0.5549,0.6148,0.6148,5,0.5789,0.222,no
PREU1_PREIS,P9WET8,ProtTale,Eukaryota,2388,Highly reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product.,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.5549,0.5549,0.5549,0.5549,0.5549,5,0.5549,0.222,no
PREU1_PREIS,P9WET8,Protein2Text,Eukaryota,2388,Highly reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product.,"This protein is a fatty acid synthase, which means it is involved in the synthesis of fatty acids. Fatty acid synthases are enzymes that catalyze the conversion of acetyl-CoA and malonyl-CoA into fatty acids through a series of condensation, reduction, and dehydration reactions. This protein is likely involved in the production of fatty acids for use in the cell or for incorporation into lipids.",No,Maybe,No,No,Maybe,not-Yes,GO:0004315; GO:0004312; GO:0016491; GO:0031177,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.6331,0.6331,0.6331,0.6331,0.6331,5,0.6331,0.222,no
PREU1_PREIS,P9WET8,Reference,Eukaryota,2388,Highly reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product.,Highly reducing polyketide synthase; part of a gene cluster that mediates the biosynthesis of a yet unidentified natural product.,,,,,,,GO:0004315; GO:0004312; GO:0016491; GO:0031177,GO:0016740,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.5046,0.5549,0.5549,0.6148,0.5549,5,0.5568,0.222,no
TAZA_ASPTN,Q0CSA2,ESM2Text,Eukaryota,2556,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of azaterrilone A and other azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities. The first step of the pathway begins with tazA that assembles one acetyl-CoA starter unit, five malonyl-CoA units, and catalyzes a series of Claisen condensations, methylation, PT-mediated cyclization, and finally releases the first hexaketide precursor through the R-domain. The tazA product then undergoes reduction on its terminal ketone and the following pyran-ring formation by yet undetermined enzyme(s). Dehydration and enoyl reduction, possibly involving the trans-enoyl reductase tazE leads to the next intermediate. TazD is predicted as an acetyltransferase and might catalyze the acetylation steps leading to the synthesis of azaterrilone A. Azaterrilone A is not the final product of the taz pathway and both the highly reducing polyketide synthase tazB and the dual enzyme tazHJ catalyze late steps of the pathway, leading to the production of the 2 final stereoisomers that contain additional polyketide modification whose structures have still to be determined (Probable).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome monooxygenase P450 claM then catalyzes the dimerization of nataloe-emodin to cladofulvin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016746,,GO:0016746,,,,,1.0,,,,1,1.0,0.2224,no
TAZA_ASPTN,Q0CSA2,Prot2Text,Eukaryota,2556,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of azaterrilone A and other azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities. The first step of the pathway begins with tazA that assembles one acetyl-CoA starter unit, five malonyl-CoA units, and catalyzes a series of Claisen condensations, methylation, PT-mediated cyclization, and finally releases the first hexaketide precursor through the R-domain. The tazA product then undergoes reduction on its terminal ketone and the following pyran-ring formation by yet undetermined enzyme(s). Dehydration and enoyl reduction, possibly involving the trans-enoyl reductase tazE leads to the next intermediate. TazD is predicted as an acetyltransferase and might catalyze the acetylation steps leading to the synthesis of azaterrilone A. Azaterrilone A is not the final product of the taz pathway and both the highly reducing polyketide synthase tazB and the dual enzyme tazHJ catalyze late steps of the pathway, leading to the production of the 2 final stereoisomers that contain additional polyketide modification whose structures have still to be determined (Probable).","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016746,GO:0016746,GO:0016747,GO:0016747,GO:0016746,GO:0016747,1.0,0.8416,0.8416,1.0,0.8416,5,0.905,0.2224,no
TAZA_ASPTN,Q0CSA2,ProtT3,Eukaryota,2556,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of azaterrilone A and other azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities. The first step of the pathway begins with tazA that assembles one acetyl-CoA starter unit, five malonyl-CoA units, and catalyzes a series of Claisen condensations, methylation, PT-mediated cyclization, and finally releases the first hexaketide precursor through the R-domain. The tazA product then undergoes reduction on its terminal ketone and the following pyran-ring formation by yet undetermined enzyme(s). Dehydration and enoyl reduction, possibly involving the trans-enoyl reductase tazE leads to the next intermediate. TazD is predicted as an acetyltransferase and might catalyze the acetylation steps leading to the synthesis of azaterrilone A. Azaterrilone A is not the final product of the taz pathway and both the highly reducing polyketide synthase tazB and the dual enzyme tazHJ catalyze late steps of the pathway, leading to the production of the 2 final stereoisomers that contain additional polyketide modification whose structures have still to be determined (Probable).",Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-,Yes,Yes,Maybe,Yes,Yes,Yes,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016747,1.0,1.0,1.0,0.8416,0.8416,5,0.9366,0.2224,no
TAZA_ASPTN,Q0CSA2,ProtTale,Eukaryota,2556,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of azaterrilone A and other azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities. The first step of the pathway begins with tazA that assembles one acetyl-CoA starter unit, five malonyl-CoA units, and catalyzes a series of Claisen condensations, methylation, PT-mediated cyclization, and finally releases the first hexaketide precursor through the R-domain. The tazA product then undergoes reduction on its terminal ketone and the following pyran-ring formation by yet undetermined enzyme(s). Dehydration and enoyl reduction, possibly involving the trans-enoyl reductase tazE leads to the next intermediate. TazD is predicted as an acetyltransferase and might catalyze the acetylation steps leading to the synthesis of azaterrilone A. Azaterrilone A is not the final product of the taz pathway and both the highly reducing polyketide synthase tazB and the dual enzyme tazHJ catalyze late steps of the pathway, leading to the production of the 2 final stereoisomers that contain additional polyketide modification whose structures have still to be determined (Probable).","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016746,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2224,no
TAZA_ASPTN,Q0CSA2,Protein2Text,Eukaryota,2556,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of azaterrilone A and other azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities. The first step of the pathway begins with tazA that assembles one acetyl-CoA starter unit, five malonyl-CoA units, and catalyzes a series of Claisen condensations, methylation, PT-mediated cyclization, and finally releases the first hexaketide precursor through the R-domain. The tazA product then undergoes reduction on its terminal ketone and the following pyran-ring formation by yet undetermined enzyme(s). Dehydration and enoyl reduction, possibly involving the trans-enoyl reductase tazE leads to the next intermediate. TazD is predicted as an acetyltransferase and might catalyze the acetylation steps leading to the synthesis of azaterrilone A. Azaterrilone A is not the final product of the taz pathway and both the highly reducing polyketide synthase tazB and the dual enzyme tazHJ catalyze late steps of the pathway, leading to the production of the 2 final stereoisomers that contain additional polyketide modification whose structures have still to be determined (Probable).","The molecular function of this protein is as a coenzyme A transferase, specifically involved in the synthesis of coenzyme A. It is a key enzyme in the process of coenzyme A biosynthesis, which is essential for various cellular metabolic processes.",No,No,No,No,No,not-Yes,GO:0016746,GO:0008410,,GO:0008410,GO:0008410,GO:0008410,0.5565,,0.5565,0.5565,0.5565,4,0.5565,0.2224,no
TAZA_ASPTN,Q0CSA2,Reference,Eukaryota,2556,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of azaterrilone A and other azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities. The first step of the pathway begins with tazA that assembles one acetyl-CoA starter unit, five malonyl-CoA units, and catalyzes a series of Claisen condensations, methylation, PT-mediated cyclization, and finally releases the first hexaketide precursor through the R-domain. The tazA product then undergoes reduction on its terminal ketone and the following pyran-ring formation by yet undetermined enzyme(s). Dehydration and enoyl reduction, possibly involving the trans-enoyl reductase tazE leads to the next intermediate. TazD is predicted as an acetyltransferase and might catalyze the acetylation steps leading to the synthesis of azaterrilone A. Azaterrilone A is not the final product of the taz pathway and both the highly reducing polyketide synthase tazB and the dual enzyme tazHJ catalyze late steps of the pathway, leading to the production of the 2 final stereoisomers that contain additional polyketide modification whose structures have still to be determined (Probable).","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of azaterrilone A and other azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities. The first step of the pathway begins with tazA that assembles one acetyl-CoA starter unit, five malonyl-CoA units, and catalyzes a series of Claisen condensations, methylation, PT-mediated cyclization, and finally releases the first hexaketide precursor through the R-domain. The tazA product then undergoes reduction on its terminal ketone and the following pyran-ring formation by yet undetermined enzyme(s). Dehydration and enoyl reduction, possibly involving the trans-enoyl reductase tazE leads to the next intermediate. TazD is predicted as an acetyltransferase and might catalyze the acetylation steps leading to the synthesis of azaterrilone A. Azaterrilone A is not the final product of the taz pathway and both the highly reducing polyketide synthase tazB and the dual enzyme tazHJ catalyze late steps of the pathway, leading to the production of the 2 final stereoisomers that contain additional polyketide modification whose structures have still to be determined (Probable).",,,,,,,GO:0016746,GO:0016740,GO:0016746; GO:0008168,GO:0016746,GO:0016747,GO:0016746,0.8145,0.8522,1.0,0.8416,1.0,5,0.9017,0.2224,no
ABPB_ASPTN,Q0CX54,ESM2Text,Eukaryota,379,Trans-prenyltransferase that acts in both the aspulvinones and butyrolactones pathways. Prenylates aspulvinone E and butyrolactone II to yield repectively aspulvinone H and butyrolactone I.,"Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ. Paxilline is converted to",No,No,No,No,No,not-Yes,GO:0047691,GO:0004497; GO:0020037,GO:0004497,GO:0004497; GO:0005506; GO:0020037,GO:0004497,GO:0004497,0.2676,0.3284,0.2213,0.3284,0.3284,5,0.2948,0.2862,no
ABPB_ASPTN,Q0CX54,Prot2Text,Eukaryota,379,Trans-prenyltransferase that acts in both the aspulvinones and butyrolactones pathways. Prenylates aspulvinone E and butyrolactone II to yield repectively aspulvinone H and butyrolactone I.,Catalyzes the prenylation of L-tryptophan at the C-7 position of the indole moiety. Specific for dimethylallyl diphosphate (DMAPP).,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0047691,GO:0016765,GO:0004659,GO:0004659,GO:0016765,GO:0016765,0.8416,0.7025,0.7025,0.8416,0.8416,5,0.786,0.2862,no
ABPB_ASPTN,Q0CX54,ProtT3,Eukaryota,379,Trans-prenyltransferase that acts in both the aspulvinones and butyrolactones pathways. Prenylates aspulvinone E and butyrolactone II to yield repectively aspulvinone H and butyrolactone I.,Prenyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeranylind,Maybe,Yes,Maybe,Yes,Maybe,not-Yes,GO:0047691,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,0.7025,0.7025,0.7025,0.7025,0.7025,5,0.7025,0.2862,no
ABPB_ASPTN,Q0CX54,ProtTale,Eukaryota,379,Trans-prenyltransferase that acts in both the aspulvinones and butyrolactones pathways. Prenylates aspulvinone E and butyrolactone II to yield repectively aspulvinone H and butyrolactone I.,Involved in the alkaloid biosynthesis. Catalyzes the 10-hydroxylation of the indole moiety of tryptamine to form 5-hydroxytryptamine.,No,No,No,No,No,not-Yes,GO:0047691,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0016705,0.3284,0.3284,0.3284,0.3284,0.3284,5,0.3284,0.2862,no
ABPB_ASPTN,Q0CX54,Protein2Text,Eukaryota,379,Trans-prenyltransferase that acts in both the aspulvinones and butyrolactones pathways. Prenylates aspulvinone E and butyrolactone II to yield repectively aspulvinone H and butyrolactone I.,"The molecular function of this protein is a prenyltransferase, specifically involved in the synthesis of abscisic acid (ABA) precursors.",Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0047691,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,0.7025,0.7025,0.7025,0.7025,0.7025,5,0.7025,0.2862,no
ABPB_ASPTN,Q0CX54,Reference,Eukaryota,379,Trans-prenyltransferase that acts in both the aspulvinones and butyrolactones pathways. Prenylates aspulvinone E and butyrolactone II to yield repectively aspulvinone H and butyrolactone I.,Trans-prenyltransferase that acts in both the aspulvinones and butyrolactones pathways. Prenylates aspulvinone E and butyrolactone II to yield repectively aspulvinone H and butyrolactone I.,,,,,,,GO:0047691,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,0.7025,0.7025,0.7025,0.7025,0.7025,5,0.7025,0.2862,no
3OXCE_CUPNH,Q0KAA1,ESM2Text,Bacteria,284,"Catalyzes the condensation of 3-oxoadipate (beta-ketoadipate) and acetyl-CoA, forming acetoacetate and succinyl-CoA. Is likely involved is the degradation of 3- oxoadipate through an alternative pathway, within catechol degradation.","Involved in the anaerobic fermentation of lysine. Catalyzes the reversible reaction between 3-keto-5-aminohexanoate (KAH) and acetyl-CoA to form 3-aminobutyryl-CoA and acetoacetate. It is not able to use beta-alanine, nor the alpha-ketoacid pyrophosphate.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0043720; GO:0046872,GO:0008410,GO:0008260,GO:0008410,GO:0008415,GO:0008260,0.3006,0.2554,0.3006,0.5281,0.2554,5,0.328,0.3415,no
3OXCE_CUPNH,Q0KAA1,Prot2Text,Bacteria,284,"Catalyzes the condensation of 3-oxoadipate (beta-ketoadipate) and acetyl-CoA, forming acetoacetate and succinyl-CoA. Is likely involved is the degradation of 3- oxoadipate through an alternative pathway, within catechol degradation.","Involved in the anaerobic fermentation of lysine. Catalyzes the reversible reaction between 3-keto-5-aminohexanoate (KAH) and acetyl-CoA to form 3-aminobutyryl-CoA and acetoacetate. The reaction involves the deprotonation of KAH, the nucleophilic addition onto acetyl-CoA and the intramolecular transfer of the CoA moiety. It can also use 2-formyl-3-hydroxy-5-aminohexanoate (FAH) as substrate.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0043720; GO:0046872,GO:0008410,GO:0008410,GO:0008410,GO:0008410,GO:0008410,0.3006,0.3006,0.3006,0.3006,0.3006,5,0.3006,0.3415,no
3OXCE_CUPNH,Q0KAA1,ProtT3,Bacteria,284,"Catalyzes the condensation of 3-oxoadipate (beta-ketoadipate) and acetyl-CoA, forming acetoacetate and succinyl-CoA. Is likely involved is the degradation of 3- oxoadipate through an alternative pathway, within catechol degradation.",Catalyzes the reversible NAD(P)(+)-dependent dehydrogenation of 2-keto-3-deoxygluconate (KDG) to 2-keto-3-deoxy-6-phosphogluconate (KDPG). Belongs to the KGDH family,No,No,No,No,No,not-Yes,GO:0043720; GO:0046872,GO:0016616,GO:0016491,GO:0016491,GO:0016616,GO:0016616,0.1917,0.2894,0.2894,0.1917,0.1917,5,0.2308,0.3415,no
3OXCE_CUPNH,Q0KAA1,ProtTale,Bacteria,284,"Catalyzes the condensation of 3-oxoadipate (beta-ketoadipate) and acetyl-CoA, forming acetoacetate and succinyl-CoA. Is likely involved is the degradation of 3- oxoadipate through an alternative pathway, within catechol degradation.",Catalyzes the condensation of hydroxymethylpyrimidine phosphate (HMP-P) and 3-amino-2-oxopropyl phosphate (2-APS) to form pyridoxamine 5'-phosphate (PMP).,No,No,No,No,No,not-Yes,GO:0043720; GO:0046872,GO:0016769,GO:0016740,GO:0016829,GO:0016829,GO:0016829,0.3635,0.4539,0.2894,0.2894,0.2894,5,0.3371,0.3415,no
3OXCE_CUPNH,Q0KAA1,Protein2Text,Bacteria,284,"Catalyzes the condensation of 3-oxoadipate (beta-ketoadipate) and acetyl-CoA, forming acetoacetate and succinyl-CoA. Is likely involved is the degradation of 3- oxoadipate through an alternative pathway, within catechol degradation.","The molecular function of this protein is an oxidoreductase, specifically a type of oxidoreductase that catalyzes the transfer of electrons from one molecule to another.",Vague,No,No,Vague,No,not-Yes,GO:0043720; GO:0046872,GO:0016491,GO:0016491,GO:0016491,,GO:0016491,0.2894,0.2894,0.2894,,0.2894,4,0.2894,0.3415,no
3OXCE_CUPNH,Q0KAA1,Reference,Bacteria,284,"Catalyzes the condensation of 3-oxoadipate (beta-ketoadipate) and acetyl-CoA, forming acetoacetate and succinyl-CoA. Is likely involved is the degradation of 3- oxoadipate through an alternative pathway, within catechol degradation.","Catalyzes the condensation of 3-oxoadipate (beta-ketoadipate) and acetyl-CoA, forming acetoacetate and succinyl-CoA. Is likely involved is the degradation of 3- oxoadipate through an alternative pathway, within catechol degradation.",,,,,,,GO:0043720; GO:0046872,GO:0008410,GO:0008410,GO:0008410,GO:0008410,GO:0008410,0.3006,0.3006,0.3006,0.3006,0.3006,5,0.3006,0.3415,no
FRBJ_STRR3,Q0ZQ39,ESM2Text,Bacteria,339,"Monooxygenase involved in the biosynthesis of the phosphonate antibiotic FR-33289, an antimalarial agent. Catalyzes the oxidative decarboxylation of the antibiotic FR-900098 (3-(N-acetyl- N-hydroxy)aminopropylphosphonate) to form FR-33289 ((R)-(3- (acetylhydroxyamino)-2-hydroxypropyl)phosphonate).",Catalyzes the D-pyridine ring opening between N-3 and C-4 of pyridine-5-carboxymethyl-1-pyrophosphate (PYMP) to yield pyridine-5-carboxymethanolamine (PYMP).,No,No,No,No,No,not-Yes,GO:0046872; GO:0004497,,GO:0016829,,,,,0.3731,,,,1,0.3731,0.3056,no
FRBJ_STRR3,Q0ZQ39,Prot2Text,Bacteria,339,"Monooxygenase involved in the biosynthesis of the phosphonate antibiotic FR-33289, an antimalarial agent. Catalyzes the oxidative decarboxylation of the antibiotic FR-900098 (3-(N-acetyl- N-hydroxy)aminopropylphosphonate) to form FR-33289 ((R)-(3- (acetylhydroxyamino)-2-hydroxypropyl)phosphonate).","Alpha-ketoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the antibiotic 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA) and its derivatives. The direct non-reducing polyketide synthase dbaI product is 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA), produced by condensation of one acetyl-CoA starter unit with 4 malonyl-CoA units and one methylation step. The FAD-dependent monooxygenase dbaH is responsible for the synthesis of yellow pigments derived from the oxidation of DHMBA. The roles of dbaB, C, E and F have still to be determined (Probable).",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0004497,GO:0016706,GO:0016706,GO:0016706,GO:0016706,GO:0016706,0.3606,0.3606,0.3606,0.3606,0.3606,5,0.3606,0.3056,no
FRBJ_STRR3,Q0ZQ39,ProtT3,Bacteria,339,"Monooxygenase involved in the biosynthesis of the phosphonate antibiotic FR-33289, an antimalarial agent. Catalyzes the oxidative decarboxylation of the antibiotic FR-900098 (3-(N-acetyl- N-hydroxy)aminopropylphosphonate) to form FR-33289 ((R)-(3- (acetylhydroxyamino)-2-hydroxypropyl)phosphonate).",Alpha-ketoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0004497,GO:0016706; GO:0005506,GO:0016706; GO:0005506,GO:0016706,GO:0016706,GO:0016706,0.6323,0.6323,0.3606,0.3606,0.3606,5,0.4693,0.3056,no
FRBJ_STRR3,Q0ZQ39,ProtTale,Bacteria,339,"Monooxygenase involved in the biosynthesis of the phosphonate antibiotic FR-33289, an antimalarial agent. Catalyzes the oxidative decarboxylation of the antibiotic FR-900098 (3-(N-acetyl- N-hydroxy)aminopropylphosphonate) to form FR-33289 ((R)-(3- (acetylhydroxyamino)-2-hydroxypropyl)phosphonate).",Catalyzes the oxidation of L-ornithine to L-glutamate semialdehyde.,No,No,No,No,No,not-Yes,GO:0046872; GO:0004497,GO:0016491,GO:0016491,GO:0016491,GO:0016641,GO:0016491,0.5957,0.5957,0.5957,0.4059,0.5957,5,0.5577,0.3056,no
FRBJ_STRR3,Q0ZQ39,Protein2Text,Bacteria,339,"Monooxygenase involved in the biosynthesis of the phosphonate antibiotic FR-33289, an antimalarial agent. Catalyzes the oxidative decarboxylation of the antibiotic FR-900098 (3-(N-acetyl- N-hydroxy)aminopropylphosphonate) to form FR-33289 ((R)-(3- (acetylhydroxyamino)-2-hydroxypropyl)phosphonate).","This protein is a part of the ornithine cycle and has a molecular function as a monooxygenase, specifically catalyzing the hydroxylation of 2-aminomuconate (2-Ac) to 2-aminomuconate 6-semialdehyde (2-AMS). It is part of the 2-aminomuconate 6-semialdehyde dehydrogenase enzyme. The protein uses FAD as a cofactor in this process. 
The reaction is as follows:

2-aminomuconate (2-Ac) + NADPH + H(+) + O(2) = 2-aminomuconate 6-semialdehyde (2-AMS) + NADP(+) + H(2)O + H(+)",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.3056,no
FRBJ_STRR3,Q0ZQ39,Reference,Bacteria,339,"Monooxygenase involved in the biosynthesis of the phosphonate antibiotic FR-33289, an antimalarial agent. Catalyzes the oxidative decarboxylation of the antibiotic FR-900098 (3-(N-acetyl- N-hydroxy)aminopropylphosphonate) to form FR-33289 ((R)-(3- (acetylhydroxyamino)-2-hydroxypropyl)phosphonate).","Monooxygenase involved in the biosynthesis of the phosphonate antibiotic FR-33289, an antimalarial agent. Catalyzes the oxidative decarboxylation of the antibiotic FR-900098 (3-(N-acetyl- N-hydroxy)aminopropylphosphonate) to form FR-33289 ((R)-(3- (acetylhydroxyamino)-2-hydroxypropyl)phosphonate).",,,,,,,GO:0046872; GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.7088,0.7088,0.7088,0.7088,0.7088,5,0.7088,0.3056,no
FRBI_STRR3,Q0ZQ40,ESM2Text,Bacteria,206,"Nucleotide hydrolase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the hydrolysis of CMP-5'-(N- acetyl-N-hydroxy-3-aminopropyl)phosphonate (CMP-5'-FR-900098) to produce CMP and the final compound FR-900098. In vitro, has broad substrate specificity and also catalyzes the hydrolysis of all the other CMP-containing intermediates within the pathway and shows low activity toward CTP.",Probably mediates the hydrolysis of some nucleoside diphosphate derivatives.,Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787; GO:0046872,,GO:0016787,,GO:0016787,,,0.7193,,0.7193,,2,0.7193,0.2047,no
FRBI_STRR3,Q0ZQ40,Prot2Text,Bacteria,206,"Nucleotide hydrolase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the hydrolysis of CMP-5'-(N- acetyl-N-hydroxy-3-aminopropyl)phosphonate (CMP-5'-FR-900098) to produce CMP and the final compound FR-900098. In vitro, has broad substrate specificity and also catalyzes the hydrolysis of all the other CMP-containing intermediates within the pathway and shows low activity toward CTP.","Mediates the hydrolysis of some nucleoside diphosphate derivatives. Can use diadenosine 5',5'''-P(1)P(5) pentaphosphate (Ap(5)A), diadenosine 5',5'''-P(1)P(4) tetraphosphate (Ap(4)A), adenosine 5',5'''-P(1)P(5) triphosphate (Ap(3)A), adenosine 5',5'''-P(1)P(4) tetraphosphate (Ap(3)A) and adenosine 5',5'''-P(1)P(4) triphosphate (Ap(3)A) as substrates.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787; GO:0046872,GO:0016787,GO:0004081,GO:0004081,GO:0016787,GO:0016787,0.7193,0.35,0.35,0.7193,0.7193,5,0.5716,0.2047,no
FRBI_STRR3,Q0ZQ40,ProtT3,Bacteria,206,"Nucleotide hydrolase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the hydrolysis of CMP-5'-(N- acetyl-N-hydroxy-3-aminopropyl)phosphonate (CMP-5'-FR-900098) to produce CMP and the final compound FR-900098. In vitro, has broad substrate specificity and also catalyzes the hydrolysis of all the other CMP-containing intermediates within the pathway and shows low activity toward CTP.",Catalyzes the hydrolysis of adenosine 5'-phosphosulfate (APS) to adenosine 5'-phosphosulfate 5'-phosphate and inorganic phosphate. Belongs to the Nudix hydrolase family,No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787; GO:0046872,GO:0016787,GO:0016817,GO:0016787,GO:0016462,GO:0016787,0.7193,0.5852,0.7193,0.4309,0.7193,5,0.6348,0.2047,no
FRBI_STRR3,Q0ZQ40,ProtTale,Bacteria,206,"Nucleotide hydrolase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the hydrolysis of CMP-5'-(N- acetyl-N-hydroxy-3-aminopropyl)phosphonate (CMP-5'-FR-900098) to produce CMP and the final compound FR-900098. In vitro, has broad substrate specificity and also catalyzes the hydrolysis of all the other CMP-containing intermediates within the pathway and shows low activity toward CTP.",Involved in nucleotide metabolism: the phosphorylation of dTMP to dTDP in both de novo and salvage pathways of purine and pyrimidine nucleotide synthesis.,No,No,No,No,Maybe,not-Yes,GO:0016787; GO:0046872,GO:0004798,GO:0004798,GO:0004798,GO:0004798,GO:0004798,0.2018,0.2018,0.2018,0.2018,0.2018,5,0.2018,0.2047,no
FRBI_STRR3,Q0ZQ40,Protein2Text,Bacteria,206,"Nucleotide hydrolase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the hydrolysis of CMP-5'-(N- acetyl-N-hydroxy-3-aminopropyl)phosphonate (CMP-5'-FR-900098) to produce CMP and the final compound FR-900098. In vitro, has broad substrate specificity and also catalyzes the hydrolysis of all the other CMP-containing intermediates within the pathway and shows low activity toward CTP.","The molecular function of this protein is unknown, but it is known to be a part of the purine salvage pathway. The purine salvage pathway is a metabolic pathway that allows cells to recycle purine nucleotides, which are essential for various cellular processes. This protein is likely involved in the conversion of a purine nucleotide to a different form, but the exact function is not specified.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016787; GO:0046872,,,,,,,,,,,0,,0.2047,no
FRBI_STRR3,Q0ZQ40,Reference,Bacteria,206,"Nucleotide hydrolase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the hydrolysis of CMP-5'-(N- acetyl-N-hydroxy-3-aminopropyl)phosphonate (CMP-5'-FR-900098) to produce CMP and the final compound FR-900098. In vitro, has broad substrate specificity and also catalyzes the hydrolysis of all the other CMP-containing intermediates within the pathway and shows low activity toward CTP.","Nucleotide hydrolase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the hydrolysis of CMP-5'-(N- acetyl-N-hydroxy-3-aminopropyl)phosphonate (CMP-5'-FR-900098) to produce CMP and the final compound FR-900098. In vitro, has broad substrate specificity and also catalyzes the hydrolysis of all the other CMP-containing intermediates within the pathway and shows low activity toward CTP.",,,,,,,GO:0016787; GO:0046872,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016787,0.7193,0.7193,0.7193,0.7193,0.7193,5,0.7193,0.2047,no
YICC_CLOD6,Q182S9,ESM2Text,Bacteria,293,"Negatively modulates sporulation, probably in response to nutrient conditions. Effects expression of sporulation regulator spo0A in an indirect manner, possibly via repression of the sinRR' operon (Probable).",Global transcriptional regulator that plays a role in virulence. Required for surface infection and for growth.,Maybe,No,No,Maybe,Maybe,not-Yes,GO:0016787; GO:0004521,,,GO:0003700,,,,,0.2175,,,1,0.2175,0.407,no
YICC_CLOD6,Q182S9,Prot2Text,Bacteria,293,"Negatively modulates sporulation, probably in response to nutrient conditions. Effects expression of sporulation regulator spo0A in an indirect manner, possibly via repression of the sinRR' operon (Probable).",Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for the interaction of the 30S and 50S ribosomal subunits and may interact with different components of the ribosome.,No,No,No,No,No,not-Yes,GO:0016787; GO:0004521,,,,,,,,,,,0,,0.407,no
YICC_CLOD6,Q182S9,ProtT3,Bacteria,293,"Negatively modulates sporulation, probably in response to nutrient conditions. Effects expression of sporulation regulator spo0A in an indirect manner, possibly via repression of the sinRR' operon (Probable).",Belongs to the CbbQ/NirQ/NorQ/GpvN family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016787; GO:0004521,,GO:0016887,,,,,0.3617,,,,1,0.3617,0.407,no
YICC_CLOD6,Q182S9,ProtTale,Bacteria,293,"Negatively modulates sporulation, probably in response to nutrient conditions. Effects expression of sporulation regulator spo0A in an indirect manner, possibly via repression of the sinRR' operon (Probable).","ATP-dependent specificity component of the Clp protease, which is responsible for protein degradation and the maintenance of protein homeostasis.",No,No,No,No,No,not-Yes,GO:0016787; GO:0004521,GO:0005524; GO:0016887,,GO:0016887,,GO:0016887,0.2931,,0.3617,,0.3617,3,0.3388,0.407,no
YICC_CLOD6,Q182S9,Protein2Text,Bacteria,293,"Negatively modulates sporulation, probably in response to nutrient conditions. Effects expression of sporulation regulator spo0A in an indirect manner, possibly via repression of the sinRR' operon (Probable).","The molecular function of this protein is a nucleotide cyclase, specifically a GTPase that catalyzes the conversion of GTP to GDP and pyrophosphate. It is involved in the process of GTP hydrolysis, which is essential for various cellular processes such as signal transduction, protein synthesis, and cell division. 
This protein is a GTPase, which means it has the ability to convert GTP to GDP and pyrophosphate, and it is involved in the process of GTP hydrolysis, which is essential for various cellular processes. The molecular function of this protein is likely to be involved in the regulation of GTP levels in the cell, which is important for many cellular processes. 

In more detail, the molecular function of this protein is:
GTPase: This protein has GTPase activity, which means it can convert GTP to GDP and pyrophosphate.
Nucleotide cyclase: This protein has nucleotide cyclase activity, which means it can catalyze the conversion of GTP to GDP and pyrophosphate.
GTPase activity: This protein has GTPase activity, which means it can convert GTP to GDP and pyrophosphate.
GDPase activity: This protein has GDPase activity, which means it can convert GDP to GMP and phosphate.
Pyrophosphatase activity: This protein has pyrophosphatase activity, which means it can convert pyrophosphate to phosphate.",No,No,Vague,No,No,not-Yes,GO:0016787; GO:0004521,GO:0003924,GO:0003924; GO:0005525,,GO:0003924,GO:0003924,0.3706,0.2997,,0.3706,0.3706,4,0.3529,0.407,no
YICC_CLOD6,Q182S9,Reference,Bacteria,293,"Negatively modulates sporulation, probably in response to nutrient conditions. Effects expression of sporulation regulator spo0A in an indirect manner, possibly via repression of the sinRR' operon (Probable).","Negatively modulates sporulation, probably in response to nutrient conditions. Effects expression of sporulation regulator spo0A in an indirect manner, possibly via repression of the sinRR' operon (Probable).",,,,,,,GO:0016787; GO:0004521,,,,,,,,,,,0,,0.407,no
HELR_MYXXD,Q1D148,ESM2Text,Bacteria,706,"An RNA polymerase (RNAP) recycling system. Inserts into a stalled/inactive RNAP primary channel (where DNA binds) and the secondary channel (where NTPs enter the active site); forces the primary channel open, removing nucleic acids from RNAP. Has ATPase activity.",DNA-dependent ATPase and 5'-3' DNA helicase.,No,No,No,Maybe,Maybe,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0004003; GO:0003677; GO:0005524,GO:0003678,GO:0003678; GO:0005524,GO:0004003; GO:0005524,GO:0003678; GO:0016887; GO:0005524,0.8733,0.454,0.7131,0.7131,0.7085,5,0.6924,0.5588,yes
HELR_MYXXD,Q1D148,Prot2Text,Bacteria,706,"An RNA polymerase (RNAP) recycling system. Inserts into a stalled/inactive RNAP primary channel (where DNA binds) and the secondary channel (where NTPs enter the active site); forces the primary channel open, removing nucleic acids from RNAP. Has ATPase activity.",Helicase.,Vague,Vague,No,Vague,Vague,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0004386,GO:0004386,GO:0004386,GO:0004386,GO:0004386,0.4113,0.4113,0.4113,0.4113,0.4113,5,0.4113,0.5588,yes
HELR_MYXXD,Q1D148,ProtT3,Bacteria,706,"An RNA polymerase (RNAP) recycling system. Inserts into a stalled/inactive RNAP primary channel (where DNA binds) and the secondary channel (where NTPs enter the active site); forces the primary channel open, removing nucleic acids from RNAP. Has ATPase activity.",DNA-dependent ATPase and DNA-binding protein that may play a role in DNA metabolism. In the C-terminal section; belongs to the RecA family. In the N-terminal section; belongs to the VapB family,No,No,No,Maybe,Maybe,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0016887; GO:0005524; GO:0003677,GO:0016887; GO:0003677,GO:0016887; GO:0003677,GO:0016887; GO:0003677; GO:0005524,GO:0003677; GO:0016887; GO:0005524,0.7382,0.5555,0.5555,0.7382,0.7382,5,0.6651,0.5588,yes
HELR_MYXXD,Q1D148,ProtTale,Bacteria,706,"An RNA polymerase (RNAP) recycling system. Inserts into a stalled/inactive RNAP primary channel (where DNA binds) and the secondary channel (where NTPs enter the active site); forces the primary channel open, removing nucleic acids from RNAP. Has ATPase activity.","An E.coli RNA polymerase (RNAP) holoenzyme that has lost its proofreading activity, but retains the ability to translocate along the DNA template during transcription. The absence of proofreading activity means that transcripts will be produced at the same rate as proofreading enzymes, but with reduced fidelity. The 3'-5' exonuclease activity is not required for transcription (Probable). May play a role in DNA repair (Probable).",No,No,No,Maybe,No,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0003899,GO:0003899,GO:0003899; GO:0008408,GO:0003899,GO:0003899,0.1736,0.1736,0.277,0.1736,0.1736,5,0.1943,0.5588,yes
HELR_MYXXD,Q1D148,Protein2Text,Bacteria,706,"An RNA polymerase (RNAP) recycling system. Inserts into a stalled/inactive RNAP primary channel (where DNA binds) and the secondary channel (where NTPs enter the active site); forces the primary channel open, removing nucleic acids from RNAP. Has ATPase activity.","The molecular function of this protein is likely to be involved in DNA replication or repair, as it is a type of helicase. Helicases are enzymes that unwind double-stranded DNA into single strands, which is an essential step in many DNA processes such as replication, repair, and recombination. This protein is likely to be involved in unwinding DNA in order to facilitate these processes.",No,No,Vague,Vague,No,not-Yes,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0004386,GO:0003678; GO:0005524,GO:0004386,GO:0004386,GO:0003678,0.4113,0.7131,0.4113,0.4113,0.454,5,0.4802,0.5588,yes
HELR_MYXXD,Q1D148,Reference,Bacteria,706,"An RNA polymerase (RNAP) recycling system. Inserts into a stalled/inactive RNAP primary channel (where DNA binds) and the secondary channel (where NTPs enter the active site); forces the primary channel open, removing nucleic acids from RNAP. Has ATPase activity.","An RNA polymerase (RNAP) recycling system. Inserts into a stalled/inactive RNAP primary channel (where DNA binds) and the secondary channel (where NTPs enter the active site); forces the primary channel open, removing nucleic acids from RNAP. Has ATPase activity.",,,,,,,GO:0043138; GO:0005524; GO:0003677; GO:0016787,GO:0016887,GO:0016887,GO:0016887,GO:0016887,GO:0016887,0.2706,0.2706,0.2706,0.2706,0.2706,5,0.2706,0.5588,yes
HIBCH_NEUCR,Q1K7A4,ESM2Text,Eukaryota,508,"Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (Probable). mS47 has enzymatic activity in vitro, and is able to catalyze the specific hydrolysis of 3-hydroxyisobutyryl-CoA (HIBYL-CoA). However, because the turnover rate of mS47 is only a fraction of that of the homologous mammalian enzyme, the physiological function of this activity remains unclear.","Catalyzes the reversible isomerization of 3-hydroxybenzoyl-CoA (HBC-CoA) to 3-hydroxypropionyl-CoA (HPC-CoA). The enzyme is highly specific for HBC-CoA and is able to catalyze the isomerization of the product to the final product in several different enzymatic processes. Also catalyzes the reversible isomerization of other nonpolar acid racemic 1,2-epsilon-acrylate to the corresponding carboxylic acid.",No,No,No,No,No,not-Yes,GO:0003860,GO:0016853,GO:0016853,,,,0.2746,0.2746,,,,2,0.2746,0.2054,no
HIBCH_NEUCR,Q1K7A4,Prot2Text,Eukaryota,508,"Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (Probable). mS47 has enzymatic activity in vitro, and is able to catalyze the specific hydrolysis of 3-hydroxyisobutyryl-CoA (HIBYL-CoA). However, because the turnover rate of mS47 is only a fraction of that of the homologous mammalian enzyme, the physiological function of this activity remains unclear.",Involved in the degradation of long-chain fatty acids.,No,No,No,Vague,No,not-Yes,GO:0003860,,,,,,,,,,,0,,0.2054,no
HIBCH_NEUCR,Q1K7A4,ProtT3,Eukaryota,508,"Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (Probable). mS47 has enzymatic activity in vitro, and is able to catalyze the specific hydrolysis of 3-hydroxyisobutyryl-CoA (HIBYL-CoA). However, because the turnover rate of mS47 is only a fraction of that of the homologous mammalian enzyme, the physiological function of this activity remains unclear.",Hydrolysis of 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA). Mitochondrion matrix. Belongs to the enoyl-CoA hydratase/isomerase family,No,No,Vague,No,No,not-Yes,GO:0003860,GO:0004419,GO:0004419,GO:0016790,GO:0004419,GO:0004419,0.1536,0.1536,0.5956,0.1536,0.1536,5,0.242,0.2054,no
HIBCH_NEUCR,Q1K7A4,ProtTale,Eukaryota,508,"Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (Probable). mS47 has enzymatic activity in vitro, and is able to catalyze the specific hydrolysis of 3-hydroxyisobutyryl-CoA (HIBYL-CoA). However, because the turnover rate of mS47 is only a fraction of that of the homologous mammalian enzyme, the physiological function of this activity remains unclear.",Hydrolyzes 3-deoxy-D-manno-octulosonate 8-phosphate (KDO8P) with broad substrate specificity.,No,No,No,No,No,not-Yes,GO:0003860,GO:0016787,GO:0016791,GO:0016791,GO:0016791,GO:0016787,0.4454,0.3552,0.3552,0.3552,0.4454,5,0.3913,0.2054,no
HIBCH_NEUCR,Q1K7A4,Protein2Text,Eukaryota,508,"Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (Probable). mS47 has enzymatic activity in vitro, and is able to catalyze the specific hydrolysis of 3-hydroxyisobutyryl-CoA (HIBYL-CoA). However, because the turnover rate of mS47 is only a fraction of that of the homologous mammalian enzyme, the physiological function of this activity remains unclear.","The molecular function of this protein is involved in catalyzing the removal of the phosphate group from a molecule, specifically it is a type of enzyme that catalyzes the dephosphorylation of a substrate.",No,No,No,No,No,not-Yes,GO:0003860,GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,0.3552,0.3552,0.3552,0.3552,0.3552,5,0.3552,0.2054,no
HIBCH_NEUCR,Q1K7A4,Reference,Eukaryota,508,"Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (Probable). mS47 has enzymatic activity in vitro, and is able to catalyze the specific hydrolysis of 3-hydroxyisobutyryl-CoA (HIBYL-CoA). However, because the turnover rate of mS47 is only a fraction of that of the homologous mammalian enzyme, the physiological function of this activity remains unclear.","Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane (Probable). mS47 has enzymatic activity in vitro, and is able to catalyze the specific hydrolysis of 3-hydroxyisobutyryl-CoA (HIBYL-CoA). However, because the turnover rate of mS47 is only a fraction of that of the homologous mammalian enzyme, the physiological function of this activity remains unclear.",,,,,,,GO:0003860,GO:0003860,GO:0003735; GO:0016787,GO:0003735; GO:0016790,GO:0003860,GO:0003735,1.0,0.3376,0.4378,1.0,0.1221,5,0.5795,0.2054,no
HUTI_CAEEL,Q22419,ESM2Text,Eukaryota,432,Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate (Probable). It is the third step in the universal histidine degradation pathway (Probable).,Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0050480; GO:0046872,GO:0003937,GO:0016810,GO:0003837,GO:0003824,GO:0003937,0.3224,0.5281,0.371,0.3766,0.3224,5,0.3841,0.5588,yes
HUTI_CAEEL,Q22419,Prot2Text,Eukaryota,432,Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate (Probable). It is the third step in the universal histidine degradation pathway (Probable).,Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0050480; GO:0046872,GO:0016787,GO:0003860,GO:0003937,GO:0003836,GO:0016812,0.4539,0.1849,0.3224,0.1628,0.607,5,0.3462,0.5588,yes
HUTI_CAEEL,Q22419,ProtT3,Eukaryota,432,Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate (Probable). It is the third step in the universal histidine degradation pathway (Probable).,Belongs to the metallo-dependent hydrolases superfamily. HutI family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0050480; GO:0046872,GO:0003837,GO:0016787,,GO:0016813,GO:0016812,0.371,0.4539,,0.4368,0.607,4,0.4672,0.5588,yes
HUTI_CAEEL,Q22419,ProtTale,Eukaryota,432,Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate (Probable). It is the third step in the universal histidine degradation pathway (Probable).,Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0050480; GO:0046872,GO:0016812,GO:0003937,GO:0016812,GO:0003937,GO:0016812,0.607,0.3224,0.607,0.3224,0.607,5,0.4932,0.5588,yes
HUTI_CAEEL,Q22419,Protein2Text,Eukaryota,432,Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate (Probable). It is the third step in the universal histidine degradation pathway (Probable).,"The molecular function of this protein is as a cysteine desulfurase, which is an enzyme that catalyzes the removal of sulfur from cysteine to produce 2-oxoglutarate and sulfane sulfur, which is then used to synthesize various sulfur-containing biomolecules. In particular, this protein is involved in the degradation of cysteine and the production of sulfide.",No,No,No,No,No,not-Yes,GO:0050480; GO:0046872,GO:0031071,GO:0031071,GO:0031071,GO:0031071,GO:0031071,0.1628,0.1628,0.1628,0.1628,0.1628,5,0.1628,0.5588,yes
HUTI_CAEEL,Q22419,Reference,Eukaryota,432,Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate (Probable). It is the third step in the universal histidine degradation pathway (Probable).,Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate (Probable). It is the third step in the universal histidine degradation pathway (Probable).,,,,,,,GO:0050480; GO:0046872,GO:0003937,GO:0016812,GO:0016812,GO:0003937,GO:0003937,0.3224,0.607,0.607,0.3224,0.3224,5,0.4362,0.5588,yes
CCDN_CHAGB,Q2GPS5,ESM2Text,Eukaryota,285,"Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdN takes part in the first steps that generate the pyranoquinone intermediate by reducing the C11 carbonyl of the first benzaldehyde intermediate to an alcohol. The pathway begins with the NR-PKS ccdL, the short- chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9-C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).",NADPH-dependent oxidoreductase which is a key component of the paxillin synthase complex. Converts the tetraketide-derived side chain into the corresponding aldehyde. Can also reduce the tetraketide-derived side chain lengths of longer chain lengths without forming aldehydes. Reduces the dialdehyde products dihydro- and alkyl-pyrazinamide and dihydro-methylcoumarin and dihydro-pentaacetone. Involved in the regulation of plant growth and development.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0000140; GO:0004806,GO:0016491,GO:0016491,,GO:0016491,,0.506,0.506,,0.506,,3,0.506,0.2144,no
CCDN_CHAGB,Q2GPS5,Prot2Text,Eukaryota,285,"Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdN takes part in the first steps that generate the pyranoquinone intermediate by reducing the C11 carbonyl of the first benzaldehyde intermediate to an alcohol. The pathway begins with the NR-PKS ccdL, the short- chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9-C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).","Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome monooxygenase P450 claM then catalyzes the dimerization of nataloe-emodin to cladofulvin.",Yes,Yes,Maybe,Maybe,Yes,Yes,GO:0000140; GO:0004806,GO:0016491,GO:0016614,GO:0016491,GO:0016491,GO:0016491,0.506,0.5706,0.506,0.506,0.506,5,0.5189,0.2144,no
CCDN_CHAGB,Q2GPS5,ProtT3,Eukaryota,285,"Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdN takes part in the first steps that generate the pyranoquinone intermediate by reducing the C11 carbonyl of the first benzaldehyde intermediate to an alcohol. The pathway begins with the NR-PKS ccdL, the short- chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9-C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).",Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-,Yes,Yes,Maybe,Maybe,Yes,Yes,GO:0000140; GO:0004806,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.506,0.506,0.506,0.506,0.506,5,0.506,0.2144,no
CCDN_CHAGB,Q2GPS5,ProtTale,Eukaryota,285,"Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdN takes part in the first steps that generate the pyranoquinone intermediate by reducing the C11 carbonyl of the first benzaldehyde intermediate to an alcohol. The pathway begins with the NR-PKS ccdL, the short- chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9-C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).","Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUSes are not required for fusarin C biosynthesis. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) FUS3. The atrochrysone carboxyl ACP thioesterase FUS10 then breaks the thioester bond and releases the atrochrysone carboxylic acid from FUS3. Atrochrysone carboxylic acid is then",Yes,Yes,Maybe,Maybe,Yes,Yes,GO:0000140; GO:0004806,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.506,0.506,0.506,0.506,0.506,5,0.506,0.2144,no
CCDN_CHAGB,Q2GPS5,Protein2Text,Eukaryota,285,"Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdN takes part in the first steps that generate the pyranoquinone intermediate by reducing the C11 carbonyl of the first benzaldehyde intermediate to an alcohol. The pathway begins with the NR-PKS ccdL, the short- chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9-C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).","This protein is involved in the molecular function of oxidoreductase activity. Specifically, it is a part of the cytochrome P450 monooxygenase, which is a family of enzymes that catalyze the incorporation of one atom of molecular oxygen into an organic substrate.
 
This protein is involved in the molecular function of oxidoreductase activity. Specifically, it is a part of the cytochrome P450 monooxygenase, which is a family of enzymes that catalyze the incorporation of one atom of molecular oxygen into an organic substrate.",No,No,No,Vague,No,not-Yes,GO:0000140; GO:0004806,GO:0004497,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0020037,GO:0004497,GO:0004497,0.406,0.2826,0.3361,0.406,0.406,5,0.3673,0.2144,no
CCDN_CHAGB,Q2GPS5,Reference,Eukaryota,285,"Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdN takes part in the first steps that generate the pyranoquinone intermediate by reducing the C11 carbonyl of the first benzaldehyde intermediate to an alcohol. The pathway begins with the NR-PKS ccdL, the short- chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9-C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).","Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdN takes part in the first steps that generate the pyranoquinone intermediate by reducing the C11 carbonyl of the first benzaldehyde intermediate to an alcohol. The pathway begins with the NR-PKS ccdL, the short- chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9-C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).",,,,,,,GO:0000140; GO:0004806,GO:0016491,GO:0016491,GO:0016491,GO:0016614,GO:0016491,0.506,0.506,0.506,0.5706,0.506,5,0.5189,0.2144,no
CCDL_CHAGB,Q2GPS7,ESM2Text,Eukaryota,2515,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdL catalyzes the formation of the partially reduced carbon skeleton. When expressed in S.cerevisiae, ccdL is capable of accepting acetyl-CoA as a starting unit and adding four malonyl-CoA units for biosynthesizing 6-methylorsellinic acid in the absence of other biosynthetic enzymes coded within the gene cluster. As it is expected to generate an aldehyde-containing product, it is possible that the aldehyde was accidentally oxidized to a carboxylic acid by some yeast oxidoreductase. Within the native context, however, ccdL also extends the starter unit with four malonyl-CoA units but accepts either heptanoyl-CoA or 5-hydroxyheptanoyl-CoA, not acetyl- CoA, as its starting unit. Lastly, the nascent chain is released by its terminal reductase domain as a cyclized aldehyde. The pathway begins with the NR-PKS ccdL, the short-chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9- C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The nonribosomal peptide synthetase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016746; GO:0031177,,GO:0016746,,,,,0.7023,,,,1,0.7023,0.2649,no
CCDL_CHAGB,Q2GPS7,Prot2Text,Eukaryota,2515,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdL catalyzes the formation of the partially reduced carbon skeleton. When expressed in S.cerevisiae, ccdL is capable of accepting acetyl-CoA as a starting unit and adding four malonyl-CoA units for biosynthesizing 6-methylorsellinic acid in the absence of other biosynthetic enzymes coded within the gene cluster. As it is expected to generate an aldehyde-containing product, it is possible that the aldehyde was accidentally oxidized to a carboxylic acid by some yeast oxidoreductase. Within the native context, however, ccdL also extends the starter unit with four malonyl-CoA units but accepts either heptanoyl-CoA or 5-hydroxyheptanoyl-CoA, not acetyl- CoA, as its starting unit. Lastly, the nascent chain is released by its terminal reductase domain as a cyclized aldehyde. The pathway begins with the NR-PKS ccdL, the short-chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9- C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The nonribosomal peptide synthetase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016746; GO:0031177,GO:0016746,GO:0016747,GO:0016747,GO:0016746,GO:0016747,0.7023,0.5918,0.5918,0.7023,0.5918,5,0.636,0.2649,no
CCDL_CHAGB,Q2GPS7,ProtT3,Eukaryota,2515,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdL catalyzes the formation of the partially reduced carbon skeleton. When expressed in S.cerevisiae, ccdL is capable of accepting acetyl-CoA as a starting unit and adding four malonyl-CoA units for biosynthesizing 6-methylorsellinic acid in the absence of other biosynthetic enzymes coded within the gene cluster. As it is expected to generate an aldehyde-containing product, it is possible that the aldehyde was accidentally oxidized to a carboxylic acid by some yeast oxidoreductase. Within the native context, however, ccdL also extends the starter unit with four malonyl-CoA units but accepts either heptanoyl-CoA or 5-hydroxyheptanoyl-CoA, not acetyl- CoA, as its starting unit. Lastly, the nascent chain is released by its terminal reductase domain as a cyclized aldehyde. The pathway begins with the NR-PKS ccdL, the short-chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9- C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016746; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016747,0.7023,0.7023,0.7023,0.5918,0.5918,5,0.6581,0.2649,no
CCDL_CHAGB,Q2GPS7,ProtTale,Eukaryota,2515,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdL catalyzes the formation of the partially reduced carbon skeleton. When expressed in S.cerevisiae, ccdL is capable of accepting acetyl-CoA as a starting unit and adding four malonyl-CoA units for biosynthesizing 6-methylorsellinic acid in the absence of other biosynthetic enzymes coded within the gene cluster. As it is expected to generate an aldehyde-containing product, it is possible that the aldehyde was accidentally oxidized to a carboxylic acid by some yeast oxidoreductase. Within the native context, however, ccdL also extends the starter unit with four malonyl-CoA units but accepts either heptanoyl-CoA or 5-hydroxyheptanoyl-CoA, not acetyl- CoA, as its starting unit. Lastly, the nascent chain is released by its terminal reductase domain as a cyclized aldehyde. The pathway begins with the NR-PKS ccdL, the short-chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9- C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016746; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.7023,0.7023,0.7023,0.7023,0.7023,5,0.7023,0.2649,no
CCDL_CHAGB,Q2GPS7,Protein2Text,Eukaryota,2515,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdL catalyzes the formation of the partially reduced carbon skeleton. When expressed in S.cerevisiae, ccdL is capable of accepting acetyl-CoA as a starting unit and adding four malonyl-CoA units for biosynthesizing 6-methylorsellinic acid in the absence of other biosynthetic enzymes coded within the gene cluster. As it is expected to generate an aldehyde-containing product, it is possible that the aldehyde was accidentally oxidized to a carboxylic acid by some yeast oxidoreductase. Within the native context, however, ccdL also extends the starter unit with four malonyl-CoA units but accepts either heptanoyl-CoA or 5-hydroxyheptanoyl-CoA, not acetyl- CoA, as its starting unit. Lastly, the nascent chain is released by its terminal reductase domain as a cyclized aldehyde. The pathway begins with the NR-PKS ccdL, the short-chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9- C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).","This protein is a part of the pyruvate dehydrogenase complex, which plays a crucial role in cellular metabolism by catalyzing the conversion of pyruvate to acetyl-CoA. This process is essential for the production of energy in cells, as it allows pyruvate to be used as a substrate for the citric acid cycle, which generates ATP and other energy-rich molecules.",No,No,No,No,No,not-Yes,GO:0016746; GO:0031177,GO:0016491,GO:0004738,GO:0004739,GO:0004739,GO:0004739,0.3628,0.0,0.2168,0.2168,0.2168,5,0.2026,0.2649,no
CCDL_CHAGB,Q2GPS7,Reference,Eukaryota,2515,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdL catalyzes the formation of the partially reduced carbon skeleton. When expressed in S.cerevisiae, ccdL is capable of accepting acetyl-CoA as a starting unit and adding four malonyl-CoA units for biosynthesizing 6-methylorsellinic acid in the absence of other biosynthetic enzymes coded within the gene cluster. As it is expected to generate an aldehyde-containing product, it is possible that the aldehyde was accidentally oxidized to a carboxylic acid by some yeast oxidoreductase. Within the native context, however, ccdL also extends the starter unit with four malonyl-CoA units but accepts either heptanoyl-CoA or 5-hydroxyheptanoyl-CoA, not acetyl- CoA, as its starting unit. Lastly, the nascent chain is released by its terminal reductase domain as a cyclized aldehyde. The pathway begins with the NR-PKS ccdL, the short-chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9- C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdL catalyzes the formation of the partially reduced carbon skeleton. When expressed in S.cerevisiae, ccdL is capable of accepting acetyl-CoA as a starting unit and adding four malonyl-CoA units for biosynthesizing 6-methylorsellinic acid in the absence of other biosynthetic enzymes coded within the gene cluster. As it is expected to generate an aldehyde-containing product, it is possible that the aldehyde was accidentally oxidized to a carboxylic acid by some yeast oxidoreductase. Within the native context, however, ccdL also extends the starter unit with four malonyl-CoA units but accepts either heptanoyl-CoA or 5-hydroxyheptanoyl-CoA, not acetyl- CoA, as its starting unit. Lastly, the nascent chain is released by its terminal reductase domain as a cyclized aldehyde. The pathway begins with the NR-PKS ccdL, the short-chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9- C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).",,,,,,,GO:0016746; GO:0031177,GO:0016740,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.5854,0.7023,0.7023,0.5918,0.7023,5,0.6568,0.2649,no
CCDJ_CHAGB,Q2GPS9,ESM2Text,Eukaryota,618,"Multicopper oxidase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdJ takes part in the final dimerization steps and more specifically catalyzes the dimerization reaction that results in the formation of cochliodones from azaphilone monomers. The pathway begins with the NR-PKS ccdL, the short-chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9-C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).",Lignin degradation and detoxification of lignin-derived products.,Maybe,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0005507; GO:0016491,,,,,,,,,,,0,,0.4158,no
CCDJ_CHAGB,Q2GPS9,Prot2Text,Eukaryota,618,"Multicopper oxidase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdJ takes part in the final dimerization steps and more specifically catalyzes the dimerization reaction that results in the formation of cochliodones from azaphilone monomers. The pathway begins with the NR-PKS ccdL, the short-chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9-C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).",Lignin degradation and detoxification of lignin-derived products.,Maybe,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0005507; GO:0016491,,,,,,,,,,,0,,0.4158,no
CCDJ_CHAGB,Q2GPS9,ProtT3,Eukaryota,618,"Multicopper oxidase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdJ takes part in the final dimerization steps and more specifically catalyzes the dimerization reaction that results in the formation of cochliodones from azaphilone monomers. The pathway begins with the NR-PKS ccdL, the short-chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9-C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).",Lignin degradation and detoxification of lignin-derived products. Secreted. Belongs to the multicopper oxidase family,Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0005507; GO:0016491,GO:0008471; GO:0005507,GO:0008471; GO:0005507,GO:0008471,GO:0008471; GO:0005507,GO:0008471; GO:0005507,0.7096,0.7096,0.0,0.7096,0.7096,5,0.5677,0.4158,no
CCDJ_CHAGB,Q2GPS9,ProtTale,Eukaryota,618,"Multicopper oxidase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdJ takes part in the final dimerization steps and more specifically catalyzes the dimerization reaction that results in the formation of cochliodones from azaphilone monomers. The pathway begins with the NR-PKS ccdL, the short-chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9-C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).","Laccase; part of the gene cluster that mediates the biosynthesis of cercosporin, a light-activated, non-host-selective toxin. The perylenequinone chromophore of cercosporin absorbs light energy to attain an electronically-activated triplet state and produces active oxygen species such as the hydroxyl radical, superoxide, hydrogen peroxide or singlet oxygen upon reaction with oxygen molecules. These reactive oxygen species cause damage to various cellular components including lipids, proteins and nucleic acids. The first step of cercosporin biosynthesis is performed by the polyketide synthase CTB1 which catalyzes the formation of nor-toralactone. The starter unit acyl",Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0005507; GO:0016491,GO:0008471,GO:0008471; GO:0005507,GO:0008471,GO:0016491,GO:0008471; GO:0005507,0.0,0.7096,0.0,0.7096,0.7096,5,0.4258,0.4158,no
CCDJ_CHAGB,Q2GPS9,Protein2Text,Eukaryota,618,"Multicopper oxidase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdJ takes part in the final dimerization steps and more specifically catalyzes the dimerization reaction that results in the formation of cochliodones from azaphilone monomers. The pathway begins with the NR-PKS ccdL, the short-chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9-C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).","The molecular function of this protein is likely to be involved in the breakdown and detoxification of lignin-derived compounds, specifically in the degradation of lignin-derived compounds. It is a lignin degradation enzyme, specifically a lignin peroxidase, which catalyzes the oxidation of lignin-derived compounds.",Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0005507; GO:0016491,GO:0004601,GO:0004601,GO:0004601,GO:0004601,GO:0004601,0.4461,0.4461,0.4461,0.4461,0.4461,5,0.4461,0.4158,no
CCDJ_CHAGB,Q2GPS9,Reference,Eukaryota,618,"Multicopper oxidase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdJ takes part in the final dimerization steps and more specifically catalyzes the dimerization reaction that results in the formation of cochliodones from azaphilone monomers. The pathway begins with the NR-PKS ccdL, the short-chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9-C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).","Multicopper oxidase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdJ takes part in the final dimerization steps and more specifically catalyzes the dimerization reaction that results in the formation of cochliodones from azaphilone monomers. The pathway begins with the NR-PKS ccdL, the short-chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9-C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).",,,,,,,GO:0005507; GO:0016491,GO:0016682,GO:0016491; GO:0005507,GO:0016491; GO:0005507,GO:0016682,GO:0016491; GO:0005507,0.4873,1.0,1.0,0.4873,1.0,5,0.7949,0.4158,no
CCDE_CHAGB,Q2GPT4,ESM2Text,Eukaryota,504,"FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdE takes part in the final dimerization steps and more specifically catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A. The pathway begins with the NR-PKS ccdL, the short- chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9-C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).","FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome monooxygenase P450 claM then catalyzes the dimerization of nataloe-emodin to cladofulvin.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0071949; GO:0016491,GO:0016491; GO:0071949,GO:0016491,GO:0016491; GO:0071949,GO:0016491,GO:0016491; GO:0071949,1.0,0.706,1.0,0.706,1.0,5,0.8824,0.2692,no
CCDE_CHAGB,Q2GPT4,Prot2Text,Eukaryota,504,"FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdE takes part in the final dimerization steps and more specifically catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A. The pathway begins with the NR-PKS ccdL, the short- chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9-C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).","Flavin-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ. Paxilline is converted to beta",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0071949; GO:0016491,GO:0004497,GO:0004497; GO:0071949,GO:0004497,GO:0004497,GO:0004497,0.5751,0.9073,0.5751,0.5751,0.5751,5,0.6415,0.2692,no
CCDE_CHAGB,Q2GPT4,ProtT3,Eukaryota,504,"FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdE takes part in the final dimerization steps and more specifically catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A. The pathway begins with the NR-PKS ccdL, the short- chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9-C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).",FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranyl,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0071949; GO:0016491,GO:0004497; GO:0050660,GO:0004497; GO:0071949,GO:0004497,GO:0004497; GO:0071949,GO:0004497; GO:0071949,0.8646,0.9073,0.5751,0.9073,0.9073,5,0.8323,0.2692,no
CCDE_CHAGB,Q2GPT4,ProtTale,Eukaryota,504,"FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdE takes part in the final dimerization steps and more specifically catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A. The pathway begins with the NR-PKS ccdL, the short- chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9-C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).","FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes nodulisporic acids (NAs). Within the pathway, nodS catalyzes the conversion of nodulisporic acid A to nodulisporic acid B. The geranylgeranyl diphosphate (GGPP) synthase ggs1, localized outside of the cluster, is proposed to catalyze the first step in nodulisporic acid biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3-glycerol phosphate with GGPP",Yes,Yes,Maybe,Yes,Yes,Yes,GO:0071949; GO:0016491,GO:0016491; GO:0071949,GO:0016491; GO:0071949,GO:0016491,GO:0016491; GO:0071949,GO:0016491; GO:0071949,1.0,1.0,0.706,1.0,1.0,5,0.9412,0.2692,no
CCDE_CHAGB,Q2GPT4,Protein2Text,Eukaryota,504,"FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdE takes part in the final dimerization steps and more specifically catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A. The pathway begins with the NR-PKS ccdL, the short- chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9-C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).","This protein is involved in the degradation of lignin, a complex organic polymer found in plant cell walls. Specifically, it is a lignin-degrading enzyme that catalyzes the oxidation of lignin-derived compounds, likely playing a role in the breakdown of lignin during the degradation of wood or other plant biomass by fungi. The molecular function of this protein is likely to be a dioxygenase, an enzyme that uses molecular oxygen to catalyze a range of oxidation reactions. The exact molecular function of this protein, however, is not explicitly stated in the available information.",No,No,No,No,No,not-Yes,GO:0071949; GO:0016491,GO:0016491,,,,GO:0051213,0.706,,,,0.5751,2,0.6405,0.2692,no
CCDE_CHAGB,Q2GPT4,Reference,Eukaryota,504,"FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdE takes part in the final dimerization steps and more specifically catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A. The pathway begins with the NR-PKS ccdL, the short- chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9-C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).","FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of cochliodone A, a dimerized azaphilone. Within the pathway, ccdE takes part in the final dimerization steps and more specifically catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A. The pathway begins with the NR-PKS ccdL, the short- chain dehydrogenase ccdN, and the FAD-dependent monooxygenase ccdF that work in sequence to generate the pyranoquinone intermediate of the pathway. CcdL produces a benzaldehyde intermediate from the condensation of 5 malonyl-CoA units and one methylation, ccdN reduces the C11 carbonyl to an alcohol and ccdF completes the azaphilone core formation. The acetyltransferases ccdC, the acetate lyase ccdG and the trans-enoyl reductase ccdH then work in sequence to fully reduce the C10 position. CcdC is responsible for the acetylation of the C10/C11 alcohol formed earlier by ccdN and kept unmodified during the azaphilone core formation by ccdF, ccdG then performs the elimination of the C10 acetate group to generate the C9-C10 olefin, and ccdH eliminates the olefin to effect a full reduction of the polyketide backbone at C10. The O-acyltransferase ccdM is then responsible for the O-acetylation at C7 of the azaphilone core. CcdB might be responsible for the formation of the spiroacetal group. The remaining enzymes ccdO, ccdJ and ccdE catalyze the final steps of the biosynthesis of dimeric cochliodones. The enoyl reductase ccdO performs the reduction of the C1-C8a olefin to generate the enol necessary for dimerization, the multicopper oxidase ccdJ is responsible for the dimerization reaction that results in the formation of cochliodones from azaphilone monomers, and lastly, the FAD-dependent oxidase ccdE catalyzes the elimination of the enol to stabilize the compound for the generation of cochliodone A (Probable).",,,,,,,GO:0071949; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.706,0.706,0.706,0.706,0.706,5,0.706,0.2692,no
FD30_FLAVE,Q2RBS5,ESM2Text,Eukaryota,319,Probable FAD-dependent oxidoreductase that plays a role in the regulation of fruiting body development.,"Acyl-CoA-binding protein that plays a role in the reduction of intracellular cholesterol. Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as a membrane anchor for the nascent chain. Assembles a large, non-toxic octacylglycerol P-bodies that target cholesterol efflux into lipid droplets.",No,No,No,No,No,not-Yes,GO:0004174; GO:0050660,GO:0000062,GO:0000062,GO:0000062,GO:0000062,GO:0000062,0.4181,0.4181,0.4181,0.4181,0.4181,5,0.4181,0.5885,yes
FD30_FLAVE,Q2RBS5,Prot2Text,Eukaryota,319,Probable FAD-dependent oxidoreductase that plays a role in the regulation of fruiting body development.,Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4).,No,No,No,No,No,not-Yes,GO:0004174; GO:0050660,GO:0004601,GO:0004601,GO:0004447,GO:0004447,GO:0004447,0.277,0.277,0.1942,0.1942,0.1942,5,0.2273,0.5885,yes
FD30_FLAVE,Q2RBS5,ProtT3,Eukaryota,319,Probable FAD-dependent oxidoreductase that plays a role in the regulation of fruiting body development.,Probable FAD-dependent oxidoreductase. Belongs to the FAD-dependent oxidoreductase family,Maybe,Yes,Maybe,Yes,Yes,Yes,GO:0004174; GO:0050660,GO:0016491; GO:0050660,GO:0016491; GO:0071949,GO:0016491,GO:0016491; GO:0071949,GO:0016491; GO:0071949,0.7763,0.7336,0.4101,0.7336,0.7336,5,0.6774,0.5885,yes
FD30_FLAVE,Q2RBS5,ProtTale,Eukaryota,319,Probable FAD-dependent oxidoreductase that plays a role in the regulation of fruiting body development.,Probable RNA helicase.,No,No,No,Maybe,Maybe,not-Yes,GO:0004174; GO:0050660,GO:0003724,GO:0003724; GO:0005524,GO:0003724,GO:0003724; GO:0005524,GO:0003724; GO:0005524,0.1378,0.3828,0.1378,0.3828,0.3828,5,0.2848,0.5885,yes
FD30_FLAVE,Q2RBS5,Protein2Text,Eukaryota,319,Probable FAD-dependent oxidoreductase that plays a role in the regulation of fruiting body development.,"This protein is a member of the cytochrome b5 family, which is involved in electron transfer reactions. Specifically, it is a heme-containing monooxygenase that participates in the oxidation of organic substrates.",No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004174; GO:0050660,GO:0004497,GO:0009055; GO:0020037,,,GO:0004497,0.3366,0.3618,,,0.3366,3,0.345,0.5885,yes
FD30_FLAVE,Q2RBS5,Reference,Eukaryota,319,Probable FAD-dependent oxidoreductase that plays a role in the regulation of fruiting body development.,Probable FAD-dependent oxidoreductase that plays a role in the regulation of fruiting body development.,,,,,,,GO:0004174; GO:0050660,,,GO:0016491,,GO:0016491,,,0.4101,,0.4101,2,0.4101,0.5885,yes
AOIO_ASPOR,Q2TXQ1,ESM2Text,Eukaryota,398,O-methyltransferase; part of the gene cluster that mediates the biosynthesis of a methylated derivative of known natural products orthosporin and diaporthin. Does not seem to be involved in the biosynthesis of the identified final product of the pathway and its function has still to be determined.,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2235,no
AOIO_ASPOR,Q2TXQ1,Prot2Text,Eukaryota,398,O-methyltransferase; part of the gene cluster that mediates the biosynthesis of a methylated derivative of known natural products orthosporin and diaporthin. Does not seem to be involved in the biosynthesis of the identified final product of the pathway and its function has still to be determined.,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate tolerance, py",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2235,no
AOIO_ASPOR,Q2TXQ1,ProtT3,Eukaryota,398,O-methyltransferase; part of the gene cluster that mediates the biosynthesis of a methylated derivative of known natural products orthosporin and diaporthin. Does not seem to be involved in the biosynthesis of the identified final product of the pathway and its function has still to be determined.,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By similarity). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (By similarity). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the ter",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2235,no
AOIO_ASPOR,Q2TXQ1,ProtTale,Eukaryota,398,O-methyltransferase; part of the gene cluster that mediates the biosynthesis of a methylated derivative of known natural products orthosporin and diaporthin. Does not seem to be involved in the biosynthesis of the identified final product of the pathway and its function has still to be determined.,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities. In the first step, the non-reducing polyketide synthase azaA forms the hexaketide precursor from successive condensations of five malonyl-CoA units, presumably with a simple acetyl-CoA starter unit. The reactive polyketide chain then undergoes a PT- mediated C2-C7 cyclization to afford the aromatic ring and is eventually released as an aldehyde through the R-domain. The",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2235,no
AOIO_ASPOR,Q2TXQ1,Protein2Text,Eukaryota,398,O-methyltransferase; part of the gene cluster that mediates the biosynthesis of a methylated derivative of known natural products orthosporin and diaporthin. Does not seem to be involved in the biosynthesis of the identified final product of the pathway and its function has still to be determined.,"This protein is involved in the molecular function of transferring a methyl group to a molecule, specifically a derivative of cytochrome P450 monooxygenase. It is also involved in the molecular function of transferring a methyl group to a molecule, specifically a derivative of cytochrome P450 monooxygenase. 
Its molecular function is to methylate cytochrome P450 monooxygenases. 
It is also involved in the molecular function of transferring a methyl group to a molecule, specifically a derivative of cytochrome P450 monooxygenase. 
This protein is involved in the molecular function of transferring a methyl group to a molecule, specifically a derivative of cytochrome P450 monooxygenase. 
It is involved in the molecular function of transferring a methyl group to a molecule, specifically a derivative of cytochrome P450 monooxygenase. 
It is involved in the molecular function of transferring a methyl group to a molecule, specifically a derivative of cytochrome P450 monooxygenase. 
Its molecular function is to methylate cytochrome P450 monooxygenases. 
It is involved in the molecular function of transferring a methyl group to a molecule, specifically a derivative of cytochrome P450 monooxygenase. 
This protein is involved in the molecular function of transferring a methyl group to a molecule, specifically a derivative of cytochrome P450 monooxygenase. 
It is involved in the molecular function of transferring a methyl group to a molecule, specifically a derivative of cytochrome P450 monooxygenase. 
It is involved in the molecular function of transferring a methyl group to a molecule, specifically a derivative of cytochrome P450 monooxygenase. 
This protein is involved in the molecular function of transferring a methyl group to a molecule, specifically a derivative of cytochrome P450 monooxygenase. 
It is involved in the molecular function of transferring a methyl group to a molecule, specifically a derivative of cytochrome P450 monooxygenase. 
This protein is involved in the molecular function of transferring a methyl group to a molecule, specifically a derivative of cytochrome P450 monooxygenase. 
It is involved in the molecular function of transferring a methyl group to a molecule, specifically a derivative of cytochrome P450 monooxygenase. 
It is involved in the molecular function of transferring a methyl group to a molecule, specifically a derivative of cytochrome P450 monooxygenase. 
It is involved in the",No,Maybe,No,Maybe,Maybe,not-Yes,GO:0008171,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.2235,no
AOIO_ASPOR,Q2TXQ1,Reference,Eukaryota,398,O-methyltransferase; part of the gene cluster that mediates the biosynthesis of a methylated derivative of known natural products orthosporin and diaporthin. Does not seem to be involved in the biosynthesis of the identified final product of the pathway and its function has still to be determined.,O-methyltransferase; part of the gene cluster that mediates the biosynthesis of a methylated derivative of known natural products orthosporin and diaporthin. Does not seem to be involved in the biosynthesis of the identified final product of the pathway and its function has still to be determined.,,,,,,,GO:0008171,GO:0008171,GO:0008171,GO:0008171,,GO:0008171,1.0,1.0,1.0,,1.0,4,1.0,0.2235,no
AOIG_ASPOR,Q2TXQ8,ESM2Text,Eukaryota,2121,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of a methylated derivative of known natural products orthosporin and diaporthin. AoiG catalyzes the biosynthesis of the hexaketide isocoumarin scaffold, via condensation of one acetyl-CoA starter unit with 6 malonyl-CoA units. An oxidoreductase that has still to be identified catalyzes the stereospecific reduction of the carbonyl moiety of the hexaketide isocoumarin scaffold to generate the S-configured secondary alcohol at C-11 of orthosporin. The methyltrasferase aoiF then catalyzes the biotransformation of not only orthosporin to diaporthin but also diaporthin to the final product, by performing a tandem methylation of the polyketide core.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004315; GO:0004312; GO:0031177,,GO:0016746,,,,,0.5734,,,,1,0.5734,0.2067,no
AOIG_ASPOR,Q2TXQ8,Prot2Text,Eukaryota,2121,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of a methylated derivative of known natural products orthosporin and diaporthin. AoiG catalyzes the biosynthesis of the hexaketide isocoumarin scaffold, via condensation of one acetyl-CoA starter unit with 6 malonyl-CoA units. An oxidoreductase that has still to be identified catalyzes the stereospecific reduction of the carbonyl moiety of the hexaketide isocoumarin scaffold to generate the S-configured secondary alcohol at C-11 of orthosporin. The methyltrasferase aoiF then catalyzes the biotransformation of not only orthosporin to diaporthin but also diaporthin to the final product, by performing a tandem methylation of the polyketide core.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004315; GO:0004312; GO:0031177,GO:0016746,GO:0016747,GO:0016747,GO:0016746,GO:0016747,0.5734,0.6667,0.6667,0.5734,0.6667,5,0.6294,0.2067,no
AOIG_ASPOR,Q2TXQ8,ProtT3,Eukaryota,2121,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of a methylated derivative of known natural products orthosporin and diaporthin. AoiG catalyzes the biosynthesis of the hexaketide isocoumarin scaffold, via condensation of one acetyl-CoA starter unit with 6 malonyl-CoA units. An oxidoreductase that has still to be identified catalyzes the stereospecific reduction of the carbonyl moiety of the hexaketide isocoumarin scaffold to generate the S-configured secondary alcohol at C-11 of orthosporin. The methyltrasferase aoiF then catalyzes the biotransformation of not only orthosporin to diaporthin but also diaporthin to the final product, by performing a tandem methylation of the polyketide core.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004315; GO:0004312; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016747,0.5734,0.5734,0.5734,0.6667,0.6667,5,0.6107,0.2067,no
AOIG_ASPOR,Q2TXQ8,ProtTale,Eukaryota,2121,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of a methylated derivative of known natural products orthosporin and diaporthin. AoiG catalyzes the biosynthesis of the hexaketide isocoumarin scaffold, via condensation of one acetyl-CoA starter unit with 6 malonyl-CoA units. An oxidoreductase that has still to be identified catalyzes the stereospecific reduction of the carbonyl moiety of the hexaketide isocoumarin scaffold to generate the S-configured secondary alcohol at C-11 of orthosporin. The methyltrasferase aoiF then catalyzes the biotransformation of not only orthosporin to diaporthin but also diaporthin to the final product, by performing a tandem methylation of the polyketide core.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004315; GO:0004312; GO:0031177,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.5734,0.5734,0.5734,0.5734,0.5734,5,0.5734,0.2067,no
AOIG_ASPOR,Q2TXQ8,Protein2Text,Eukaryota,2121,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of a methylated derivative of known natural products orthosporin and diaporthin. AoiG catalyzes the biosynthesis of the hexaketide isocoumarin scaffold, via condensation of one acetyl-CoA starter unit with 6 malonyl-CoA units. An oxidoreductase that has still to be identified catalyzes the stereospecific reduction of the carbonyl moiety of the hexaketide isocoumarin scaffold to generate the S-configured secondary alcohol at C-11 of orthosporin. The methyltrasferase aoiF then catalyzes the biotransformation of not only orthosporin to diaporthin but also diaporthin to the final product, by performing a tandem methylation of the polyketide core.","This protein is involved in the biosynthesis of the mycotoxin fusaric acid, a toxic compound produced by the fungus Fusarium oxysporum. Specifically, it is involved in the biosynthesis of the fusaric acid precursor, 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA).",No,No,No,No,No,not-Yes,GO:0004315; GO:0004312; GO:0031177,,GO:0004421,GO:0004419,,GO:0004420,,0.4044,0.1702,,0.1702,3,0.2483,0.2067,no
AOIG_ASPOR,Q2TXQ8,Reference,Eukaryota,2121,"Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of a methylated derivative of known natural products orthosporin and diaporthin. AoiG catalyzes the biosynthesis of the hexaketide isocoumarin scaffold, via condensation of one acetyl-CoA starter unit with 6 malonyl-CoA units. An oxidoreductase that has still to be identified catalyzes the stereospecific reduction of the carbonyl moiety of the hexaketide isocoumarin scaffold to generate the S-configured secondary alcohol at C-11 of orthosporin. The methyltrasferase aoiF then catalyzes the biotransformation of not only orthosporin to diaporthin but also diaporthin to the final product, by performing a tandem methylation of the polyketide core.","Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of a methylated derivative of known natural products orthosporin and diaporthin. AoiG catalyzes the biosynthesis of the hexaketide isocoumarin scaffold, via condensation of one acetyl-CoA starter unit with 6 malonyl-CoA units. An oxidoreductase that has still to be identified catalyzes the stereospecific reduction of the carbonyl moiety of the hexaketide isocoumarin scaffold to generate the S-configured secondary alcohol at C-11 of orthosporin. The methyltrasferase aoiF then catalyzes the biotransformation of not only orthosporin to diaporthin but also diaporthin to the final product, by performing a tandem methylation of the polyketide core.",,,,,,,GO:0004315; GO:0004312; GO:0031177,GO:0016740,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.4832,0.5734,0.5734,0.6667,0.5734,5,0.574,0.2067,no
KAP2_ASPOR,Q2U6T7,ESM2Text,Eukaryota,752,Probable cell surface ferric reductase that acts as a negative regulatory factor of growth and development. Involved in kojic acid production through the regulation of kojA expression.,Ferric chelate reductase; part of the gene cluster that mediates the biosynthesis of the dicarboxylic acid capsule. The nonribosomal peptide synthase dicarboxylic acid synthase (dicarboxylic acid synthase or DAS) produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units. The FAD-dependent monooxygenase dicarboxylic acid synthase (dicarboxylic acid synthase or DPA) then catalyzes the reduction of orsellinic acid to dicarboxylic acid.,Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0052851; GO:0046872,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0000293,0.4076,0.4076,0.4076,0.4076,0.5487,5,0.4358,0.4323,no
KAP2_ASPOR,Q2U6T7,Prot2Text,Eukaryota,752,Probable cell surface ferric reductase that acts as a negative regulatory factor of growth and development. Involved in kojic acid production through the regulation of kojA expression.,"Metalloreductase responsible for reducing extracellular iron and copper prior to import. Catalyzes the reductive uptake of Fe(3+) bound to dihydroxamate rhodotorulic acid and of Fe(3+)-bound heme bromide. Fe(3+) is reduced to Fe(2+), which then dissociates from the heme bromide and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane. Also participates in Cu(2+) reduction and Cu(+) uptake.",Yes,Maybe,Maybe,Yes,Yes,Yes,GO:0052851; GO:0046872,GO:0016491,GO:0016491,GO:0016491,GO:0000293,GO:0016722,0.4076,0.4076,0.4076,0.5487,0.4759,5,0.4495,0.4323,no
KAP2_ASPOR,Q2U6T7,ProtT3,Eukaryota,752,Probable cell surface ferric reductase that acts as a negative regulatory factor of growth and development. Involved in kojic acid production through the regulation of kojA expression.,Probable ferric reductase. Membrane; Multi-pass membrane protein. Belongs to the ferric reductase (FRE) family,Maybe,Yes,Maybe,Yes,Yes,Yes,GO:0052851; GO:0046872,GO:0000293,GO:0000293,GO:0016491,GO:0000293,GO:0000293,0.5487,0.5487,0.4076,0.5487,0.5487,5,0.5205,0.4323,no
KAP2_ASPOR,Q2U6T7,ProtTale,Eukaryota,752,Probable cell surface ferric reductase that acts as a negative regulatory factor of growth and development. Involved in kojic acid production through the regulation of kojA expression.,Probable cell surface metalloreductase. May be involved in iron or copper homeostasis.,Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0052851; GO:0046872,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4076,0.4076,0.4076,0.4076,0.4076,5,0.4076,0.4323,no
KAP2_ASPOR,Q2U6T7,Protein2Text,Eukaryota,752,Probable cell surface ferric reductase that acts as a negative regulatory factor of growth and development. Involved in kojic acid production through the regulation of kojA expression.,"The molecular function of this protein is to act as a membrane-bound oxidoreductase, specifically a ferric chelate reductase.",Maybe,Maybe,Maybe,Yes,Yes,not-Yes,GO:0052851; GO:0046872,GO:0016491,GO:0016491,,,GO:0016491,0.4076,0.4076,,,0.4076,3,0.4076,0.4323,no
KAP2_ASPOR,Q2U6T7,Reference,Eukaryota,752,Probable cell surface ferric reductase that acts as a negative regulatory factor of growth and development. Involved in kojic acid production through the regulation of kojA expression.,Probable cell surface ferric reductase that acts as a negative regulatory factor of growth and development. Involved in kojic acid production through the regulation of kojA expression.,,,,,,,GO:0052851; GO:0046872,GO:0016491,GO:0016491,GO:0016491,,GO:0000293,0.4076,0.4076,0.4076,,0.5487,4,0.4429,0.4323,no
SYP_TRYB2,Q388V7,ESM2Text,Eukaryota,808,"Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). Can edit the amino acid moiety from incorrectly charged Ala-tRNA(Pro), Ser- tRNA(Pro) and Gly-tRNA(Pro).",Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). Can inadvertently accommodate and process cysteine.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0002161; GO:0005524; GO:0004827,GO:0004827; GO:0005524,GO:0004827,GO:0004827,GO:0004827; GO:0005524,GO:0004827,0.8893,0.624,0.624,0.8893,0.624,5,0.7301,0.5288,no
SYP_TRYB2,Q388V7,Prot2Text,Eukaryota,808,"Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). Can edit the amino acid moiety from incorrectly charged Ala-tRNA(Pro), Ser- tRNA(Pro) and Gly-tRNA(Pro).",Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). Can inadvertently accommodate and process cysteine.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0002161; GO:0005524; GO:0004827,GO:0004827,GO:0004827,GO:0004827,GO:0004827,GO:0004827,0.624,0.624,0.624,0.624,0.624,5,0.624,0.5288,no
SYP_TRYB2,Q388V7,ProtT3,Eukaryota,808,"Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). Can edit the amino acid moiety from incorrectly charged Ala-tRNA(Pro), Ser- tRNA(Pro) and Gly-tRNA(Pro).",Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). Mitochondrion matrix. Belongs to the class-II aminoacyl-tRNA synthetase family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0002161; GO:0005524; GO:0004827,GO:0004827; GO:0005524,GO:0004827,GO:0004827,GO:0004827; GO:0005524,GO:0004827; GO:0005524,0.8893,0.624,0.624,0.8893,0.8893,5,0.7832,0.5288,no
SYP_TRYB2,Q388V7,ProtTale,Eukaryota,808,"Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). Can edit the amino acid moiety from incorrectly charged Ala-tRNA(Pro), Ser- tRNA(Pro) and Gly-tRNA(Pro).",Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).,Yes,Yes,Yes,Yes,Yes,Yes,GO:0002161; GO:0005524; GO:0004827,GO:0004827,GO:0004827; GO:0005524,GO:0004827,GO:0004827; GO:0005524,GO:0004827; GO:0005524,0.624,0.8893,0.624,0.8893,0.8893,5,0.7832,0.5288,no
SYP_TRYB2,Q388V7,Protein2Text,Eukaryota,808,"Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). Can edit the amino acid moiety from incorrectly charged Ala-tRNA(Pro), Ser- tRNA(Pro) and Gly-tRNA(Pro).","This protein is involved in the molecular function of S-methylmethionine biosynthesis, which is a process that occurs in the body. S-methylmethionine is a molecule that plays a crucial role in various biological processes, including the methylation of DNA, RNA, and proteins. The molecular function of this protein is to facilitate the conversion of methionine into S-methylmethionine through a series of enzymatic reactions.",No,No,No,No,No,not-Yes,GO:0002161; GO:0005524; GO:0004827,GO:0008168,,,,GO:0008168,0.1654,,,,0.1654,2,0.1654,0.5288,no
SYP_TRYB2,Q388V7,Reference,Eukaryota,808,"Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). Can edit the amino acid moiety from incorrectly charged Ala-tRNA(Pro), Ser- tRNA(Pro) and Gly-tRNA(Pro).","Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). Can edit the amino acid moiety from incorrectly charged Ala-tRNA(Pro), Ser- tRNA(Pro) and Gly-tRNA(Pro).",,,,,,,GO:0002161; GO:0005524; GO:0004827,GO:0004827,GO:0004827; GO:0005524,GO:0004827; GO:0005524,GO:0004827,GO:0004827; GO:0005524,0.624,0.8893,0.8893,0.624,0.8893,5,0.7832,0.5288,no
CHCOA_GEOMG,Q39QF4,ESM2Text,Bacteria,380,"Acyl-CoA dehydrogenase involved in the anaerobic degradation of cyclohexane carboxylic acid (CHC). Catalyzes the 1,2-dehydrogenation of cyclohexane-1-carbonyl-CoA (CHCoA) to cyclohex- 1-ene-1-carbonyl-CoA (CHeneCoA). An alternative substrate, cyclohex-3-ene-1-carboxyl-CoA can be converted to the corresponding cyclohexadiene-1-carboxyl-CoA isomers (30% rate compared to CHC).",Catalyzes the conversion 3-sulfinopropanoyl-CoA (3SP-CoA) to propanoyl-CoA by abstraction of sulfite. Does not show dehydrogenase activity.,No,No,No,No,Maybe,not-Yes,GO:0003995; GO:0050660,GO:0016829,GO:0016829,GO:0016829,GO:0016829,GO:0016829,0.2785,0.2785,0.2785,0.2785,0.2785,5,0.2785,0.1403,no
CHCOA_GEOMG,Q39QF4,Prot2Text,Bacteria,380,"Acyl-CoA dehydrogenase involved in the anaerobic degradation of cyclohexane carboxylic acid (CHC). Catalyzes the 1,2-dehydrogenation of cyclohexane-1-carbonyl-CoA (CHCoA) to cyclohex- 1-ene-1-carbonyl-CoA (CHeneCoA). An alternative substrate, cyclohex-3-ene-1-carboxyl-CoA can be converted to the corresponding cyclohexadiene-1-carboxyl-CoA isomers (30% rate compared to CHC).","Medium-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats. The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA. Electron transfer flavoprotein (ETF) is the electron acceptor that transfers electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase). Among the different mitochondrial acyl-CoA dehydrogenases, medium-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 6 to 12 carbons long primary chains.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0003995; GO:0050660,GO:0003995,GO:0003995,GO:0003995,GO:0003995,GO:0003995,0.6922,0.6922,0.6922,0.6922,0.6922,5,0.6922,0.1403,no
CHCOA_GEOMG,Q39QF4,ProtT3,Bacteria,380,"Acyl-CoA dehydrogenase involved in the anaerobic degradation of cyclohexane carboxylic acid (CHC). Catalyzes the 1,2-dehydrogenation of cyclohexane-1-carbonyl-CoA (CHCoA) to cyclohex- 1-ene-1-carbonyl-CoA (CHeneCoA). An alternative substrate, cyclohex-3-ene-1-carboxyl-CoA can be converted to the corresponding cyclohexadiene-1-carboxyl-CoA isomers (30% rate compared to CHC).",Belongs to the acyl-CoA dehydrogenase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0003995; GO:0050660,GO:0003995,GO:0003995,,GO:0003995,GO:0003995,0.6922,0.6922,,0.6922,0.6922,4,0.6922,0.1403,no
CHCOA_GEOMG,Q39QF4,ProtTale,Bacteria,380,"Acyl-CoA dehydrogenase involved in the anaerobic degradation of cyclohexane carboxylic acid (CHC). Catalyzes the 1,2-dehydrogenation of cyclohexane-1-carbonyl-CoA (CHCoA) to cyclohex- 1-ene-1-carbonyl-CoA (CHeneCoA). An alternative substrate, cyclohex-3-ene-1-carboxyl-CoA can be converted to the corresponding cyclohexadiene-1-carboxyl-CoA isomers (30% rate compared to CHC).",Catalyzes the reduction of crotonobetainyl-CoA to gamma- butyrobetainyl-CoA.,No,No,No,No,No,not-Yes,GO:0003995; GO:0050660,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.443,0.443,0.443,0.443,0.443,5,0.443,0.1403,no
CHCOA_GEOMG,Q39QF4,Protein2Text,Bacteria,380,"Acyl-CoA dehydrogenase involved in the anaerobic degradation of cyclohexane carboxylic acid (CHC). Catalyzes the 1,2-dehydrogenation of cyclohexane-1-carbonyl-CoA (CHCoA) to cyclohex- 1-ene-1-carbonyl-CoA (CHeneCoA). An alternative substrate, cyclohex-3-ene-1-carboxyl-CoA can be converted to the corresponding cyclohexadiene-1-carboxyl-CoA isomers (30% rate compared to CHC).","This protein is likely involved in a metabolic process, given its association with an enzyme. However, the specific molecular function of this protein is not provided in the text. It is involved in the metabolism of a compound, but the exact process is not specified.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0003995; GO:0050660,,,,,,,,,,,0,,0.1403,no
CHCOA_GEOMG,Q39QF4,Reference,Bacteria,380,"Acyl-CoA dehydrogenase involved in the anaerobic degradation of cyclohexane carboxylic acid (CHC). Catalyzes the 1,2-dehydrogenation of cyclohexane-1-carbonyl-CoA (CHCoA) to cyclohex- 1-ene-1-carbonyl-CoA (CHeneCoA). An alternative substrate, cyclohex-3-ene-1-carboxyl-CoA can be converted to the corresponding cyclohexadiene-1-carboxyl-CoA isomers (30% rate compared to CHC).","Acyl-CoA dehydrogenase involved in the anaerobic degradation of cyclohexane carboxylic acid (CHC). Catalyzes the 1,2-dehydrogenation of cyclohexane-1-carbonyl-CoA (CHCoA) to cyclohex- 1-ene-1-carbonyl-CoA (CHeneCoA). An alternative substrate, cyclohex-3-ene-1-carboxyl-CoA can be converted to the corresponding cyclohexadiene-1-carboxyl-CoA isomers (30% rate compared to CHC).",,,,,,,GO:0003995; GO:0050660,GO:0003995,GO:0003995,GO:0003995,GO:0003995,GO:0003995,0.6922,0.6922,0.6922,0.6922,0.6922,5,0.6922,0.1403,no
CRTA_CERS4,Q3J189,ESM2Text,Bacteria,324,"Involved in the biosynthesis of the carotenoid spheroidene. Catalyzes the introduction of one keto group at the C- 2 position of spheroidene. In vitro, can use nonnative substrates and produce oxocarotenoids with a hydroxy and/or a keto group, derived from neurosporene, lycopene, 3,4-didehydrolycopene or 3,4,3',4'-tetradehydrolycopene.",Involved in the stabilization of the sigma stress factor RpoS.,No,No,No,No,No,not-Yes,GO:0046872; GO:0043823,,,,,,,,,,,0,,0.2751,no
CRTA_CERS4,Q3J189,Prot2Text,Bacteria,324,"Involved in the biosynthesis of the carotenoid spheroidene. Catalyzes the introduction of one keto group at the C- 2 position of spheroidene. In vitro, can use nonnative substrates and produce oxocarotenoids with a hydroxy and/or a keto group, derived from neurosporene, lycopene, 3,4-didehydrolycopene or 3,4,3',4'-tetradehydrolycopene.",Ring cleavage of cyclic benzoate (cbcA) to yield benzoate and acetate.,No,No,No,No,No,not-Yes,GO:0046872; GO:0043823,GO:0016829,,,,GO:0016787,0.2671,,,,0.2671,2,0.2671,0.2751,no
CRTA_CERS4,Q3J189,ProtT3,Bacteria,324,"Involved in the biosynthesis of the carotenoid spheroidene. Catalyzes the introduction of one keto group at the C- 2 position of spheroidene. In vitro, can use nonnative substrates and produce oxocarotenoids with a hydroxy and/or a keto group, derived from neurosporene, lycopene, 3,4-didehydrolycopene or 3,4,3',4'-tetradehydrolycopene.","Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. Cellular thylakoid membrane; Peripheral",No,No,No,No,No,not-Yes,GO:0046872; GO:0043823,,GO:0009055,GO:0016491,GO:0016491,GO:0016491,,0.1983,0.416,0.416,0.416,4,0.3616,0.2751,no
CRTA_CERS4,Q3J189,ProtTale,Bacteria,324,"Involved in the biosynthesis of the carotenoid spheroidene. Catalyzes the introduction of one keto group at the C- 2 position of spheroidene. In vitro, can use nonnative substrates and produce oxocarotenoids with a hydroxy and/or a keto group, derived from neurosporene, lycopene, 3,4-didehydrolycopene or 3,4,3',4'-tetradehydrolycopene.",Catalyzes the insertion of two atoms of molecular oxygen into protoporphyrin IX to yield 10-hydroxyprotoporphyrin IX.,No,No,No,No,No,not-Yes,GO:0046872; GO:0043823,GO:0016491,GO:0016702,GO:0016701,GO:0051213,GO:0016702,0.416,0.252,0.3353,0.3353,0.252,5,0.3181,0.2751,no
CRTA_CERS4,Q3J189,Protein2Text,Bacteria,324,"Involved in the biosynthesis of the carotenoid spheroidene. Catalyzes the introduction of one keto group at the C- 2 position of spheroidene. In vitro, can use nonnative substrates and produce oxocarotenoids with a hydroxy and/or a keto group, derived from neurosporene, lycopene, 3,4-didehydrolycopene or 3,4,3',4'-tetradehydrolycopene.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its name, it is likely that this protein is involved in the synthesis or modification of fatty acids, as it contains the phrase ""fatty acid synthase"" in its name. Fatty acid synthases are enzymes that catalyze the synthesis of long-chain fatty acids from acetyl-CoA and malonyl-CoA through a series of reduction, dehydration, and reduction reactions. If this is the case, the molecular function of this protein would be to catalyze these reactions and produce long-chain fatty acids.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0046872; GO:0043823,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.1522,0.1522,0.1522,0.1522,0.1522,5,0.1522,0.2751,no
CRTA_CERS4,Q3J189,Reference,Bacteria,324,"Involved in the biosynthesis of the carotenoid spheroidene. Catalyzes the introduction of one keto group at the C- 2 position of spheroidene. In vitro, can use nonnative substrates and produce oxocarotenoids with a hydroxy and/or a keto group, derived from neurosporene, lycopene, 3,4-didehydrolycopene or 3,4,3',4'-tetradehydrolycopene.","Involved in the biosynthesis of the carotenoid spheroidene. Catalyzes the introduction of one keto group at the C- 2 position of spheroidene. In vitro, can use nonnative substrates and produce oxocarotenoids with a hydroxy and/or a keto group, derived from neurosporene, lycopene, 3,4-didehydrolycopene or 3,4,3',4'-tetradehydrolycopene.",,,,,,,GO:0046872; GO:0043823,GO:0016705,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4854,0.416,0.416,0.416,0.416,5,0.4299,0.2751,no
ATDA2_ACISP,Q44250,ESM2Text,Bacteria,242,"Hydrolase that catalyzes the hydrolysis of gamma- glutamylanilide (gamma-GA) into aniline. May prevent the accumulation of gamma-GA, which is harmful to cells, during oxidation of aniline to catechol.","Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS to produce anthranilate. In the absence of chorismate, the complex forms a stable tetrameric complex with AS that, along with chorismate, is channeled to the aminotransferase for further elaboration by the large alpha subunit of AS (Probable).",No,No,No,No,No,not-Yes,GO:0016787,GO:0004049,GO:0004049,GO:0004049,GO:0004049,GO:0004049,0.3552,0.3552,0.3552,0.3552,0.3552,5,0.3552,0.6713,yes
ATDA2_ACISP,Q44250,Prot2Text,Bacteria,242,"Hydrolase that catalyzes the hydrolysis of gamma- glutamylanilide (gamma-GA) into aniline. May prevent the accumulation of gamma-GA, which is harmful to cells, during oxidation of aniline to catechol.","Part of the synthesis of the polyamines spermidine and spermine. Catalyzes the hydrolysis of putrescine to produce putrescine and 4-coumarate. Polyamine spermidine is a precursor of putrescine and spermine used as substrates in the biosynthesis of polyamines, including polyamines, spermidine and spermine.",Maybe,No,No,No,Maybe,not-Yes,GO:0016787,,,,,,,,,,,0,,0.6713,yes
ATDA2_ACISP,Q44250,ProtT3,Bacteria,242,"Hydrolase that catalyzes the hydrolysis of gamma- glutamylanilide (gamma-GA) into aniline. May prevent the accumulation of gamma-GA, which is harmful to cells, during oxidation of aniline to catechol.",Catalyzes the hydrolysis of glucosamine-6-phosphate (GlcN-6-P) to yield N-acetylglucosamine-6- phosphate (GlcNAc-6-P). Belongs to the glucosamine/galactosamine-6-phosphate isomerase family,No,No,No,No,No,not-Yes,GO:0016787,GO:0004342,GO:0004342,GO:0004342,GO:0016853,GO:0004342,0.6019,0.6019,0.6019,0.5902,0.6019,5,0.5996,0.6713,yes
ATDA2_ACISP,Q44250,ProtTale,Bacteria,242,"Hydrolase that catalyzes the hydrolysis of gamma- glutamylanilide (gamma-GA) into aniline. May prevent the accumulation of gamma-GA, which is harmful to cells, during oxidation of aniline to catechol.",Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate from pyridoxine 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.,No,No,No,No,No,not-Yes,GO:0016787,GO:0004359,GO:0004359,GO:0004359,GO:0004359,GO:0004359,0.6019,0.6019,0.6019,0.6019,0.6019,5,0.6019,0.6713,yes
ATDA2_ACISP,Q44250,Protein2Text,Bacteria,242,"Hydrolase that catalyzes the hydrolysis of gamma- glutamylanilide (gamma-GA) into aniline. May prevent the accumulation of gamma-GA, which is harmful to cells, during oxidation of aniline to catechol.","This protein is a transferase, specifically an enzyme that catalyzes the transfer of a group from one molecule to another. In this case, it is a nucleotidyltransferase, which is a type of transferase that catalyzes the transfer of a nucleotide monophosphate group to an acceptor molecule.",No,No,No,No,No,not-Yes,GO:0016787,GO:0016779,GO:0016779,GO:0016779,GO:0016779,GO:0016779,0.4071,0.4071,0.4071,0.4071,0.4071,5,0.4071,0.6713,yes
ATDA2_ACISP,Q44250,Reference,Bacteria,242,"Hydrolase that catalyzes the hydrolysis of gamma- glutamylanilide (gamma-GA) into aniline. May prevent the accumulation of gamma-GA, which is harmful to cells, during oxidation of aniline to catechol.","Hydrolase that catalyzes the hydrolysis of gamma- glutamylanilide (gamma-GA) into aniline. May prevent the accumulation of gamma-GA, which is harmful to cells, during oxidation of aniline to catechol.",,,,,,,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016787,1.0,1.0,1.0,1.0,1.0,5,1.0,0.6713,yes
PYLD_METBF,Q46E80,ESM2Text,Archaea,263,Catalyzes the ultimate step of the pyrrolysine biosynthesis pathway by converting the isopeptide (3R)-3-methyl-D-ornithyl-N(6)-L- lysine to the 22nd proteinogenic amino acid. Is able to use surrogate substrates such as (3R)-D-ornithyl-N(6)-L-lysine in vitro.,May play an important role in the nonhost-pathogenic killing of D.melanogaster.,No,No,No,Vague,No,not-Yes,GO:0016491,,,,,,,,,,,0,,0.2364,no
PYLD_METBF,Q46E80,Prot2Text,Archaea,263,Catalyzes the ultimate step of the pyrrolysine biosynthesis pathway by converting the isopeptide (3R)-3-methyl-D-ornithyl-N(6)-L- lysine to the 22nd proteinogenic amino acid. Is able to use surrogate substrates such as (3R)-D-ornithyl-N(6)-L-lysine in vitro.,Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.,No,No,No,No,No,not-Yes,GO:0016491,GO:0004585,GO:0004585,GO:0004585,GO:0004585,GO:0004585,0.3552,0.3552,0.3552,0.3552,0.3552,5,0.3552,0.2364,no
PYLD_METBF,Q46E80,ProtT3,Archaea,263,Catalyzes the ultimate step of the pyrrolysine biosynthesis pathway by converting the isopeptide (3R)-3-methyl-D-ornithyl-N(6)-L- lysine to the 22nd proteinogenic amino acid. Is able to use surrogate substrates such as (3R)-D-ornithyl-N(6)-L-lysine in vitro.,May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine. Cytoplasm. Belongs to the adenosylhomocysteinase family,No,No,No,Vague,No,not-Yes,GO:0016491,GO:0004013,GO:0004013,GO:0004013,GO:0004013,GO:0004013,0.4071,0.4071,0.4071,0.4071,0.4071,5,0.4071,0.2364,no
PYLD_METBF,Q46E80,ProtTale,Archaea,263,Catalyzes the ultimate step of the pyrrolysine biosynthesis pathway by converting the isopeptide (3R)-3-methyl-D-ornithyl-N(6)-L- lysine to the 22nd proteinogenic amino acid. Is able to use surrogate substrates such as (3R)-D-ornithyl-N(6)-L-lysine in vitro.,"Bifunctional enzyme that catalyzes two of the steps in the biosynthesis of the branched-chain amino acids (BCAA) leucine, isoleucine and valine. Binds pyridoxal 5'-phosphate (PLP) but does not catalyze its condensation with acetoacetyl-CoA to form 2-acetolactate. Catalyzes the alpha-amination of 2-acetolactate to form (2S,3S)-2,3-dihydroxy-3-methylbutanoate ((2S,3S)-2,3-dihydroxy-3-methylbutanoyl-",No,No,No,No,No,not-Yes,GO:0016491,GO:0016491,GO:0016769,GO:0016769,GO:0004455; GO:0030170,GO:0016853,1.0,0.4807,0.4807,0.4406,0.5902,5,0.5984,0.2364,no
PYLD_METBF,Q46E80,Protein2Text,Archaea,263,Catalyzes the ultimate step of the pyrrolysine biosynthesis pathway by converting the isopeptide (3R)-3-methyl-D-ornithyl-N(6)-L- lysine to the 22nd proteinogenic amino acid. Is able to use surrogate substrates such as (3R)-D-ornithyl-N(6)-L-lysine in vitro.,The molecular function of this protein is an aminotransferase.,Vague,Vague,Vague,No,No,not-Yes,GO:0016491,GO:0008483,GO:0008483,GO:0008483,GO:0008483,GO:0008483,0.4071,0.4071,0.4071,0.4071,0.4071,5,0.4071,0.2364,no
PYLD_METBF,Q46E80,Reference,Archaea,263,Catalyzes the ultimate step of the pyrrolysine biosynthesis pathway by converting the isopeptide (3R)-3-methyl-D-ornithyl-N(6)-L- lysine to the 22nd proteinogenic amino acid. Is able to use surrogate substrates such as (3R)-D-ornithyl-N(6)-L-lysine in vitro.,Catalyzes the ultimate step of the pyrrolysine biosynthesis pathway by converting the isopeptide (3R)-3-methyl-D-ornithyl-N(6)-L- lysine to the 22nd proteinogenic amino acid. Is able to use surrogate substrates such as (3R)-D-ornithyl-N(6)-L-lysine in vitro.,,,,,,,GO:0016491,GO:0016874,GO:0016874; GO:0005524,GO:0016874,GO:0016874,GO:0016874,0.5902,0.4225,0.5902,0.5902,0.5902,5,0.5567,0.2364,no
WBDB_ECOLX,Q47594,ESM2Text,Bacteria,381,Mannosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of two alpha-(1->3)-linked mannose residues to the product of the WbdC enzyme during the synthesis of the adapter region.,"Glucosyltransferase involved in the biosynthesis of di-O-mannosyl-alpha-D-glucopyranoside (Glc-Man-GlcNAc) which is used as an intracellular component of surface-associated oligosaccharide. Can also use N-acetyl-alpha-D-glucopyranoside (Ac-GlcNAc), but not D-glucosyl-ManNAc or UDP-GlcNAc.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3458,no
WBDB_ECOLX,Q47594,Prot2Text,Bacteria,381,Mannosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of two alpha-(1->3)-linked mannose residues to the product of the WbdC enzyme during the synthesis of the adapter region.,Mannosyltransferase involved in the biosynthesis of Man5GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum. Catalyzes the transfer of the mannose from GDP-mannose to the position 2 of the dolichol-linked disaccharide-alpha-D-glucose (D-GlcNAc2) to yield Man5GlcNAc(2)-PP-dolichol.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016757,GO:0000030,GO:0000030,GO:0000030,GO:0000030,GO:0000030,0.729,0.729,0.729,0.729,0.729,5,0.729,0.3458,no
WBDB_ECOLX,Q47594,ProtT3,Bacteria,381,Mannosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of two alpha-(1->3)-linked mannose residues to the product of the WbdC enzyme during the synthesis of the adapter region.,Belongs to the glycosyltransferase group 1 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016757,GO:0016757,GO:0016757,,GO:0016757,GO:0016757,1.0,1.0,,1.0,1.0,4,1.0,0.3458,no
WBDB_ECOLX,Q47594,ProtTale,Bacteria,381,Mannosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of two alpha-(1->3)-linked mannose residues to the product of the WbdC enzyme during the synthesis of the adapter region.,Catalyzes the transfer of mannose from dolichol-pyrophosphate to GlcNAc-1-phosphate to form Man-GlcNAc-PP- dolichol (Dol-Man-GlcNAc-PP) as the first mannose residue in the lipid-linked oligosaccharide precursor of N-linked oligosaccharides.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016757,GO:0016757,GO:0000030,GO:0016757,GO:0016757,GO:0016757,1.0,0.729,1.0,1.0,1.0,5,0.9458,0.3458,no
WBDB_ECOLX,Q47594,Protein2Text,Bacteria,381,Mannosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of two alpha-(1->3)-linked mannose residues to the product of the WbdC enzyme during the synthesis of the adapter region.,"The molecular function of this protein is that it is an enzyme involved in the biosynthesis of GDP-L-fucose, a carbohydrate molecule used in the synthesis of glycoproteins and glycolipids. Specifically, it is a bifunctional enzyme that catalyzes the transfer of the L-fucose moiety from guanosine diphosphate-L-fucose (GDP-L-fucose) to a nucleoside triphosphate (NTP) to form a nucleoside monophosphate-L-fucose (NMP-L-fucose) and the release of pyrophosphate (PPi) in the first reaction, and the transfer of the L-fucose moiety from NMP-L-fucose to a nucleoside diphosphate (NDP) to form a nucleoside triphosphate-L-fucose (NTP-L-fucose) and the release of pyrophosphate (PPi) in the second reaction. It is involved in the biosynthesis of GDP-L-fucose, a carbohydrate molecule used in the synthesis of glycoproteins and glycolipids.",No,No,No,No,No,not-Yes,GO:0016757,,,,,GO:0050577,,,,,0.2845,1,0.2845,0.3458,no
WBDB_ECOLX,Q47594,Reference,Bacteria,381,Mannosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of two alpha-(1->3)-linked mannose residues to the product of the WbdC enzyme during the synthesis of the adapter region.,Mannosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of two alpha-(1->3)-linked mannose residues to the product of the WbdC enzyme during the synthesis of the adapter region.,,,,,,,GO:0016757,GO:0019187,GO:0000030,GO:0000030,GO:0000030,GO:0000030,0.6466,0.729,0.729,0.729,0.729,5,0.7125,0.3458,no
WBDC_ECOLX,Q47595,ESM2Text,Bacteria,371,Mannosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of a single alpha-(1->3)-linked mannose residue to the acceptor N-acetyl-glucosaminyl-diphospho-undecaprenol during the synthesis of the adapter region.,"Catalyzes the addition of a mannose residue from GDP-D-mannose to GlcAGP to generate 1,2-di-O-C24-O-octacyclo-sabinensis-1,3(C26)-GlcNAc(PA). It is strictly specific for GlcAGP.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016757,GO:0000030,GO:0000030,GO:0000030,GO:0016757,GO:0000030,0.729,0.729,0.729,1.0,0.729,5,0.7832,0.4992,no
WBDC_ECOLX,Q47595,Prot2Text,Bacteria,371,Mannosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of a single alpha-(1->3)-linked mannose residue to the acceptor N-acetyl-glucosaminyl-diphospho-undecaprenol during the synthesis of the adapter region.,"Catalyzes the addition of a mannose residue from GDP-D-mannose to GlcAGroAc2 to generate 1,2-di-O-C16/C18:1-(alpha-D-mannopyranosyl)-(1-4)-(alpha-D-glucopyranosyluronic acid)-(1-3)-glycerol(ManGlcAGroAc2).",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016757,GO:0000030,GO:0000030,GO:0000030,GO:0000030,GO:0000030,0.729,0.729,0.729,0.729,0.729,5,0.729,0.4992,no
WBDC_ECOLX,Q47595,ProtT3,Bacteria,371,Mannosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of a single alpha-(1->3)-linked mannose residue to the acceptor N-acetyl-glucosaminyl-diphospho-undecaprenol during the synthesis of the adapter region.,Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016757,GO:0016757,GO:0016757,,GO:0016757,GO:0016757,1.0,1.0,,1.0,1.0,4,1.0,0.4992,no
WBDC_ECOLX,Q47595,ProtTale,Bacteria,371,Mannosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of a single alpha-(1->3)-linked mannose residue to the acceptor N-acetyl-glucosaminyl-diphospho-undecaprenol during the synthesis of the adapter region.,"Glycosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS). Catalyzes the addition of the second heptose unit (HepII) to the (1->2)-alpha-D-glucuronic acid-(1->2)-alpha-D-glucuronic acid-(1->4)-alpha-D-mannose(2->3)-(2->6)-alpha-D-glucuronic acid (U2G2A2) precursor, yielding U3G2A2.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4992,no
WBDC_ECOLX,Q47595,Protein2Text,Bacteria,371,Mannosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of a single alpha-(1->3)-linked mannose residue to the acceptor N-acetyl-glucosaminyl-diphospho-undecaprenol during the synthesis of the adapter region.,"The molecular function of this protein is involved in the synthesis of a type of sugar molecule called a sugar nucleotide, specifically GDP-mannose. It is a part of the GDP-mannose biosynthesis pathway, which is essential for the synthesis of various carbohydrate molecules. This protein is involved in the conversion of GDP-6-deoxy-D-mannose to GDP-mannose. It catalyzes the epimerization of the C-2 hydroxyl group of GDP-6-deoxy-D-mannose to produce GDP-mannose. This reaction is crucial for the production of GDP-mannose, which is a precursor for the synthesis of various carbohydrate molecules, including GDP-fucose, GDP-6-deoxy-L-mannose, GDP-6-deoxy-L-galactose, and GDP-6-deoxy-D-talose. The GDP-mannose produced by this protein is used as a substrate for the synthesis of other sugar nucleotides, which are essential for various cellular processes, including glycosylation, cell wall synthesis, and the production of extracellular polysaccharides. In summary, the molecular function of this protein is to catalyze the epimerization of the C-2 hydroxyl group of GDP-6-deoxy-D-mannose to produce GDP-mannose, which is essential for the synthesis of various carbohydrate molecules. 

The molecular function of this protein can be summarized as follows:

* Catalyzes the epimerization of the C-2 hydroxyl group of GDP-6-deoxy-D-mannose to produce GDP-mannose.
* Involved in the synthesis of GDP-mannose, a precursor for the synthesis of various carbohydrate molecules.
* Essential for the production of GDP-mannose, which is used as a substrate for the synthesis of other sugar nucleotides.
* Plays a crucial role in various cellular processes, including glycosylation, cell wall synthesis, and the production of extracellular polysaccharides. 

The molecular function of this protein can be classified into the following categories:

* Catalytic activity: Epimerization of the C-2 hydroxyl group of GDP-6-deoxy-D-mannose to produce GDP-mannose.
* Metabolic process: Synthesis of GDP-mannose, a precursor for the synthesis of various carbohydrate molecules.
* Cellular process: Glycosylation, cell wall synthesis, and the production of extracellular polysaccharides. 

The molecular function of this protein can be further classified",No,No,Maybe,No,No,not-Yes,GO:0016757,,,,,GO:0050373,,,,,0.2845,1,0.2845,0.4992,no
WBDC_ECOLX,Q47595,Reference,Bacteria,371,Mannosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of a single alpha-(1->3)-linked mannose residue to the acceptor N-acetyl-glucosaminyl-diphospho-undecaprenol during the synthesis of the adapter region.,Mannosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of a single alpha-(1->3)-linked mannose residue to the acceptor N-acetyl-glucosaminyl-diphospho-undecaprenol during the synthesis of the adapter region.,,,,,,,GO:0016757,GO:0019187,GO:0000030,GO:0000030,GO:0000030,GO:0000030,0.6466,0.729,0.729,0.729,0.729,5,0.7125,0.4992,no
PINA_SULAC,Q4J8K8,ESM2Text,Archaea,510,"Important for growth at low temperatures (less than 65 degrees Celsius in this organism). Promotes Holliday junction (HJ) branch migration and unwinds Y-shaped DNA (but not replication forks or dsDNA) in an ATP hydrolysis-dependent manner. Stimulates cleavage by HJ resolvase Hjc. Hjc, Hjm (Hel308) and PINA coordinate HJ migration and cleavage of replication forks in a coordinated way. Probably acts as an ATP-dependent pump that pulls DNA through the hexamer.","ATPase component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers. Functions as a ATPase and an ATP-dependent, dual-track exosome-binding protein that catalyzes the ATP-dependent efflux of inorganic phosphate from the cytoplasmic to the periplasmic side of the T4P membrane. Exhibits an obligate exchange activity.",No,No,No,No,No,not-Yes,GO:0005524; GO:0003677; GO:0003678; GO:0016787,GO:0016887; GO:0005524,GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.5588,0.2745,0.5588,0.5588,0.5588,5,0.5019,0.5145,no
PINA_SULAC,Q4J8K8,Prot2Text,Archaea,510,"Important for growth at low temperatures (less than 65 degrees Celsius in this organism). Promotes Holliday junction (HJ) branch migration and unwinds Y-shaped DNA (but not replication forks or dsDNA) in an ATP hydrolysis-dependent manner. Stimulates cleavage by HJ resolvase Hjc. Hjc, Hjm (Hel308) and PINA coordinate HJ migration and cleavage of replication forks in a coordinated way. Probably acts as an ATP-dependent pump that pulls DNA through the hexamer.","ATPase component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers. PilN is essential forCore function in T4P assembly. PilO is required for proper localization of PilO in the T4P.",No,No,No,No,No,not-Yes,GO:0005524; GO:0003677; GO:0003678; GO:0016787,GO:0016887,GO:0016887,GO:0016887,GO:0016887,GO:0016887,0.2745,0.2745,0.2745,0.2745,0.2745,5,0.2745,0.5145,no
PINA_SULAC,Q4J8K8,ProtT3,Archaea,510,"Important for growth at low temperatures (less than 65 degrees Celsius in this organism). Promotes Holliday junction (HJ) branch migration and unwinds Y-shaped DNA (but not replication forks or dsDNA) in an ATP hydrolysis-dependent manner. Stimulates cleavage by HJ resolvase Hjc. Hjc, Hjm (Hel308) and PINA coordinate HJ migration and cleavage of replication forks in a coordinated way. Probably acts as an ATP-dependent pump that pulls DNA through the hexamer.",An ATP-dependent serine protease that may play a role in cell division. Cytoplasm. Belongs to the YihI family,No,No,No,No,No,not-Yes,GO:0005524; GO:0003677; GO:0003678; GO:0016787,GO:0004252; GO:0005524,GO:0004252; GO:0016887,GO:0004252; GO:0005524,GO:0004252; GO:0005524,GO:0004252; GO:0005524,0.5361,0.3048,0.5361,0.5361,0.5361,5,0.4898,0.5145,no
PINA_SULAC,Q4J8K8,ProtTale,Archaea,510,"Important for growth at low temperatures (less than 65 degrees Celsius in this organism). Promotes Holliday junction (HJ) branch migration and unwinds Y-shaped DNA (but not replication forks or dsDNA) in an ATP hydrolysis-dependent manner. Stimulates cleavage by HJ resolvase Hjc. Hjc, Hjm (Hel308) and PINA coordinate HJ migration and cleavage of replication forks in a coordinated way. Probably acts as an ATP-dependent pump that pulls DNA through the hexamer.",May play a role in the processing or repair of UV-induced DNA damage.,Vague,No,No,Vague,No,not-Yes,GO:0005524; GO:0003677; GO:0003678; GO:0016787,,,,,,,,,,,0,,0.5145,no
PINA_SULAC,Q4J8K8,Protein2Text,Archaea,510,"Important for growth at low temperatures (less than 65 degrees Celsius in this organism). Promotes Holliday junction (HJ) branch migration and unwinds Y-shaped DNA (but not replication forks or dsDNA) in an ATP hydrolysis-dependent manner. Stimulates cleavage by HJ resolvase Hjc. Hjc, Hjm (Hel308) and PINA coordinate HJ migration and cleavage of replication forks in a coordinated way. Probably acts as an ATP-dependent pump that pulls DNA through the hexamer.","The molecular function of this protein is not specified in the provided information. However, based on its name, it is likely to be a DNA polymerase, which is an enzyme that plays a crucial role in DNA replication and repair by synthesizing new DNA strands. More specifically, it may be involved in DNA polymerase activity, which is the process of creating a new DNA strand by adding nucleotides to a template strand.",Vague,No,No,Vague,No,not-Yes,GO:0005524; GO:0003677; GO:0003678; GO:0016787,,GO:0003887,GO:0003887,GO:0003887,GO:0003887,,0.2228,0.2228,0.2228,0.2228,4,0.2228,0.5145,no
PINA_SULAC,Q4J8K8,Reference,Archaea,510,"Important for growth at low temperatures (less than 65 degrees Celsius in this organism). Promotes Holliday junction (HJ) branch migration and unwinds Y-shaped DNA (but not replication forks or dsDNA) in an ATP hydrolysis-dependent manner. Stimulates cleavage by HJ resolvase Hjc. Hjc, Hjm (Hel308) and PINA coordinate HJ migration and cleavage of replication forks in a coordinated way. Probably acts as an ATP-dependent pump that pulls DNA through the hexamer.","Important for growth at low temperatures (less than 65 degrees Celsius in this organism). Promotes Holliday junction (HJ) branch migration and unwinds Y-shaped DNA (but not replication forks or dsDNA) in an ATP hydrolysis-dependent manner. Stimulates cleavage by HJ resolvase Hjc. Hjc, Hjm (Hel308) and PINA coordinate HJ migration and cleavage of replication forks in a coordinated way. Probably acts as an ATP-dependent pump that pulls DNA through the hexamer.",,,,,,,GO:0005524; GO:0003677; GO:0003678; GO:0016787,GO:0016887; GO:0004386,GO:0003678; GO:0005524,GO:0004003; GO:0005524,GO:0003678; GO:0016887,GO:0003678; GO:0005524; GO:0016887,0.4603,0.7372,0.7372,0.5208,0.7293,5,0.637,0.5145,no
ELO6_LEIMA,Q4Q5G6,ESM2Text,Eukaryota,381,Involved in the synthesis of fatty acids. Elongates C18 polyunsaturated fatty acids (PUFAs) with a preference for Delta6 PUFAs.,Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that catalyzes the synthesis of very long chain saturated (VLCS) and polyunsaturated (PUFA) fatty acids that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May play a critical role in early steps of cuticular wax and pollen biogenesis and elongation.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0009922,GO:0009922,GO:0009922,GO:0009922,GO:0009922,GO:0009922,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4658,no
ELO6_LEIMA,Q4Q5G6,Prot2Text,Eukaryota,381,Involved in the synthesis of fatty acids. Elongates C18 polyunsaturated fatty acids (PUFAs) with a preference for Delta6 PUFAs.,"Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that elongates fatty acids with 12, 14 and 16 carbons with higher activity toward C16:0 acyl-CoAs. Catalyzes the synthesis of unsaturated C16 long chain fatty acids and, to a lesser extent, C18:0 and those with low desaturation degree. May participate in the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0009922,GO:0009922,GO:0009922,GO:0009922,GO:0009922,GO:0009922,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4658,no
ELO6_LEIMA,Q4Q5G6,ProtT3,Eukaryota,381,Involved in the synthesis of fatty acids. Elongates C18 polyunsaturated fatty acids (PUFAs) with a preference for Delta6 PUFAs.,"Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that catalyzes the elongation of fatty acids with 16 and 18 carbons in the sn-1 and sn-2 positions, respectively. May be involved in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. SUBC",Yes,Yes,Yes,Yes,Yes,Yes,GO:0009922,GO:0009922,GO:0009922,GO:0009922,GO:0009922,GO:0009922,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4658,no
ELO6_LEIMA,Q4Q5G6,ProtTale,Eukaryota,381,Involved in the synthesis of fatty acids. Elongates C18 polyunsaturated fatty acids (PUFAs) with a preference for Delta6 PUFAs.,"Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that catalyzes the condensation of acyl-CoA with malonyl-CoA to produce stearidonic acid (16:4n-7), a precursor of prostaglandin E2 (PGE2). Involved in the production of VLCFAs with 20 to 22 carbon atoms (",Yes,Yes,Yes,Yes,Yes,Yes,GO:0009922,GO:0009922; GO:0016746,GO:0009922,GO:0009922,GO:0009922,GO:0009922,0.9097,1.0,1.0,1.0,1.0,5,0.9819,0.4658,no
ELO6_LEIMA,Q4Q5G6,Protein2Text,Eukaryota,381,Involved in the synthesis of fatty acids. Elongates C18 polyunsaturated fatty acids (PUFAs) with a preference for Delta6 PUFAs.,"The molecular function of this protein is that it is involved in the synthesis of fatty acids. More specifically, it is a subunit of the fatty acid synthase (FAS) complex, which is responsible for the de novo synthesis of long-chain fatty acids.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0009922,GO:0004312,GO:0004312,GO:0004312,GO:0004312,GO:0004312,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.4658,no
ELO6_LEIMA,Q4Q5G6,Reference,Eukaryota,381,Involved in the synthesis of fatty acids. Elongates C18 polyunsaturated fatty acids (PUFAs) with a preference for Delta6 PUFAs.,Involved in the synthesis of fatty acids. Elongates C18 polyunsaturated fatty acids (PUFAs) with a preference for Delta6 PUFAs.,,,,,,,GO:0009922,GO:0009922,GO:0009922,GO:0009922,GO:0009922,GO:0009922,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4658,no
QTGAL_DANRE,Q4V9J0,ESM2Text,Eukaryota,338,"Glycosyltransferase that specifically catalyzes galactosylation of cytoplasmic tRNA(Tyr) modified with queuosine at position 34 (queuosine(34)). Galactosylates the cyclopentene hydroxyl group of queuosine(34) in tRNA(Tyr) to form galactosyl-queuosine(34). Mannosylation of queuosine(34) in tRNA(Tyr) is required to slow-down elongation at cognate codons UAC and suppress stop codon readthrough, thereby regulating protein translation.","May be involved in the production of Nod factor, a sulfated N-acyl-beta-1,4-tetrasaccharide of N-acetylglucosamine which initiates a series of events in the host plant species leading eventually to nodulation.",No,No,No,No,No,not-Yes,GO:0141125,,,,,,,,,,,0,,0.275,no
QTGAL_DANRE,Q4V9J0,Prot2Text,Eukaryota,338,"Glycosyltransferase that specifically catalyzes galactosylation of cytoplasmic tRNA(Tyr) modified with queuosine at position 34 (queuosine(34)). Galactosylates the cyclopentene hydroxyl group of queuosine(34) in tRNA(Tyr) to form galactosyl-queuosine(34). Mannosylation of queuosine(34) in tRNA(Tyr) is required to slow-down elongation at cognate codons UAC and suppress stop codon readthrough, thereby regulating protein translation.","Glycosyltransferase involved in the biosynthesis of N-glycans that are specifically found in the inner cell walls of many cells including the kidney and testis. Catalyzes the transfer of the first alpha-D-mannosyl residue from GDP-mannose to the C-3 position of the pentasaccharide moiety in N-glycans. Can also use GM1-6-linked mannose as substrate, albeit with lower efficiency. Substrates with a GDP-mannose are the preferred substrates.",No,No,Maybe,Maybe,Maybe,not-Yes,GO:0141125,GO:0000030,GO:0000030,GO:0000030,GO:0000030,GO:0000030,0.4462,0.4462,0.4462,0.4462,0.4462,5,0.4462,0.275,no
QTGAL_DANRE,Q4V9J0,ProtT3,Eukaryota,338,"Glycosyltransferase that specifically catalyzes galactosylation of cytoplasmic tRNA(Tyr) modified with queuosine at position 34 (queuosine(34)). Galactosylates the cyclopentene hydroxyl group of queuosine(34) in tRNA(Tyr) to form galactosyl-queuosine(34). Mannosylation of queuosine(34) in tRNA(Tyr) is required to slow-down elongation at cognate codons UAC and suppress stop codon readthrough, thereby regulating protein translation.",Putative glycosyltransferase. Belongs to the glycosyltransferase 2 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0141125,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.4541,0.4541,0.4541,0.4541,0.4541,5,0.4541,0.275,no
QTGAL_DANRE,Q4V9J0,ProtTale,Eukaryota,338,"Glycosyltransferase that specifically catalyzes galactosylation of cytoplasmic tRNA(Tyr) modified with queuosine at position 34 (queuosine(34)). Galactosylates the cyclopentene hydroxyl group of queuosine(34) in tRNA(Tyr) to form galactosyl-queuosine(34). Mannosylation of queuosine(34) in tRNA(Tyr) is required to slow-down elongation at cognate codons UAC and suppress stop codon readthrough, thereby regulating protein translation.","Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3- dihydroxybenzoyl)-serine.",No,No,No,No,No,not-Yes,GO:0141125,,,,,,,,,,,0,,0.275,no
QTGAL_DANRE,Q4V9J0,Protein2Text,Eukaryota,338,"Glycosyltransferase that specifically catalyzes galactosylation of cytoplasmic tRNA(Tyr) modified with queuosine at position 34 (queuosine(34)). Galactosylates the cyclopentene hydroxyl group of queuosine(34) in tRNA(Tyr) to form galactosyl-queuosine(34). Mannosylation of queuosine(34) in tRNA(Tyr) is required to slow-down elongation at cognate codons UAC and suppress stop codon readthrough, thereby regulating protein translation.","The molecular function of this protein is an enzyme that catalyzes the transfer of a N-acetylglucosamine (GlcNAc) moiety from UDP-GlcNAc to a target protein, resulting in the addition of a GlcNAc moiety to the protein. This is a key step in the O-linked N-acetylglucosamine (O-GlcNAc) modification pathway, which plays a crucial role in various cellular processes, including protein regulation, signaling, and metabolism.",No,No,No,No,Maybe,not-Yes,GO:0141125,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.4541,0.4541,0.4541,0.4541,0.4541,5,0.4541,0.275,no
QTGAL_DANRE,Q4V9J0,Reference,Eukaryota,338,"Glycosyltransferase that specifically catalyzes galactosylation of cytoplasmic tRNA(Tyr) modified with queuosine at position 34 (queuosine(34)). Galactosylates the cyclopentene hydroxyl group of queuosine(34) in tRNA(Tyr) to form galactosyl-queuosine(34). Mannosylation of queuosine(34) in tRNA(Tyr) is required to slow-down elongation at cognate codons UAC and suppress stop codon readthrough, thereby regulating protein translation.","Glycosyltransferase that specifically catalyzes galactosylation of cytoplasmic tRNA(Tyr) modified with queuosine at position 34 (queuosine(34)). Galactosylates the cyclopentene hydroxyl group of queuosine(34) in tRNA(Tyr) to form galactosyl-queuosine(34). Mannosylation of queuosine(34) in tRNA(Tyr) is required to slow-down elongation at cognate codons UAC and suppress stop codon readthrough, thereby regulating protein translation.",,,,,,,GO:0141125,GO:0016757,GO:0016757,GO:0016757,GO:0008378,GO:0016757,0.4541,0.4541,0.4541,0.5968,0.4541,5,0.4826,0.275,no
OLSC_RHITR,Q4VFY5,ESM2Text,Bacteria,281,"Involved in the biosynthesis of ornithine lipids (OLs), which are phosphorus-free membrane lipids. Catalyzes the hydroxylation at the 2 position of the secondary fatty acid of OL. Contributes to symbiotic performance and acid tolerance.",May function as 2-oxoglutarate-dependent dioxygenase.,Vague,Vague,Maybe,Vague,Maybe,not-Yes,GO:0051213,,GO:0016706,,GO:0016706,,,0.747,,0.747,,2,0.747,0.2131,no
OLSC_RHITR,Q4VFY5,Prot2Text,Bacteria,281,"Involved in the biosynthesis of ornithine lipids (OLs), which are phosphorus-free membrane lipids. Catalyzes the hydroxylation at the 2 position of the secondary fatty acid of OL. Contributes to symbiotic performance and acid tolerance.","Dioxygenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",No,No,Maybe,No,Maybe,not-Yes,GO:0051213,GO:0051213,GO:0051213,GO:0051213,GO:0051213,GO:0051213,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2131,no
OLSC_RHITR,Q4VFY5,ProtT3,Bacteria,281,"Involved in the biosynthesis of ornithine lipids (OLs), which are phosphorus-free membrane lipids. Catalyzes the hydroxylation at the 2 position of the secondary fatty acid of OL. Contributes to symbiotic performance and acid tolerance.",Belongs to the cytochrome P450 family,Vague,Vague,No,Vague,No,not-Yes,GO:0051213,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506,GO:0004497; GO:0020037,GO:0004497; GO:0020037,GO:0004497,0.3993,0.4747,0.4986,0.4986,0.6612,5,0.5065,0.2131,no
OLSC_RHITR,Q4VFY5,ProtTale,Bacteria,281,"Involved in the biosynthesis of ornithine lipids (OLs), which are phosphorus-free membrane lipids. Catalyzes the hydroxylation at the 2 position of the secondary fatty acid of OL. Contributes to symbiotic performance and acid tolerance.",Catalyzes the hydrolysis of long-chain fatty acyl-coenzyme A (acyl-CoA) to yield a fatty acid and an acyl-CoA. This is the first step in the degradation of sphingolipids such as ceramide which contain a long-chain fatty acid chain.,No,No,No,No,No,not-Yes,GO:0051213,GO:0047617,GO:0047617,GO:0016790,GO:0016289,GO:0016790,0.2633,0.2633,0.3284,0.2933,0.3284,5,0.2953,0.2131,no
OLSC_RHITR,Q4VFY5,Protein2Text,Bacteria,281,"Involved in the biosynthesis of ornithine lipids (OLs), which are phosphorus-free membrane lipids. Catalyzes the hydroxylation at the 2 position of the secondary fatty acid of OL. Contributes to symbiotic performance and acid tolerance.","This protein is involved in the degradation of aromatic hydrocarbons. It is a dioxygenase enzyme that catalyzes the oxidation of aromatic compounds, such as naphthalene, using molecular oxygen. The molecular function of this protein is to catalyze the oxidation of aromatic compounds by adding an oxygen atom to the aromatic ring, resulting in the formation of a catechol intermediate. This process is an important step in the degradation of aromatic hydrocarbons in the environment.",No,No,No,No,No,not-Yes,GO:0051213,GO:0051213,GO:0051213,,GO:0051213,GO:0051213,1.0,1.0,,1.0,1.0,4,1.0,0.2131,no
OLSC_RHITR,Q4VFY5,Reference,Bacteria,281,"Involved in the biosynthesis of ornithine lipids (OLs), which are phosphorus-free membrane lipids. Catalyzes the hydroxylation at the 2 position of the secondary fatty acid of OL. Contributes to symbiotic performance and acid tolerance.","Involved in the biosynthesis of ornithine lipids (OLs), which are phosphorus-free membrane lipids. Catalyzes the hydroxylation at the 2 position of the secondary fatty acid of OL. Contributes to symbiotic performance and acid tolerance.",,,,,,,GO:0051213,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.8145,0.8145,0.8145,0.8145,0.8145,5,0.8145,0.2131,no
SPYB_ASPFU,Q4WBI0,ESM2Text,Eukaryota,591,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of meroterpenoids called sartorypyrones. SpyB catalyzes the last step of the pathway and is responsible for the acetylation of sartorypyrones D and F to produce sartorypyrones A and G, respectively. The biosynthesis of sartorypyrones begins with the production of triacetic acid lactone (TAL) by the NR- PKS spyA using one molecule of acetyl-CoA and two molecules of malonyl- CoA. The prenyltransferase spyF then conjugates geranylgeranyl pyrophosphate (GGPP) to TAL to form geranylgeranyl-triacetate lactone, for which the pathway-specific geranylgeranyl pyrophosphate synthase (GGPS) spyE is required to provide GGPP. Subsequently, geranylgeranyl- triacetate lactone is epoxidized at the terminal olein by the FAD- dependent monooxygenase spyC, followed by cyclization of the terpenoid component catalyzed by the terpene cyclase spyD to produce both the bicyclic sartorypyrone F and the monocyclic sartorypyrone D. Finally, the last step of the biosynthesis involves the acetylation of the meroterpenoids sartorypyrones D and F by the acetyltransferase SpyB to produce sartorypyrones A and G, respectively.","Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin citrinin, a hepato-nephrotoxic compound to humans due to inhibition of respiration complex III (Ref.1, PubMed:26209694). CitA catalyzes the acetylation of citF (Ref.1). CitB is also able to produce the pentacyclic citrinin C (Ref.1). The C-12-octenal isomer of citF is further acetylated to yield citC (Ref.1). CitA and CitC are responsible for the N-acetylation of citC to yield a pentacyclic C-12-hexadecatrienoic acid (C-12-HHAT) (Ref.1). The C-16-hydroxylation by CitA is responsible for the C-16 hydroxylation to yield citF (Ref.1). The C-9 hydroxylation by CitC leads to a C9-hydroxylation, which is followed by a three-step oxidation (Ref.1) to generate a Delta9,12-octadecatrienoic acid (C9-OH",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008374,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.3256,no
SPYB_ASPFU,Q4WBI0,Prot2Text,Eukaryota,591,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of meroterpenoids called sartorypyrones. SpyB catalyzes the last step of the pathway and is responsible for the acetylation of sartorypyrones D and F to produce sartorypyrones A and G, respectively. The biosynthesis of sartorypyrones begins with the production of triacetic acid lactone (TAL) by the NR- PKS spyA using one molecule of acetyl-CoA and two molecules of malonyl- CoA. The prenyltransferase spyF then conjugates geranylgeranyl pyrophosphate (GGPP) to TAL to form geranylgeranyl-triacetate lactone, for which the pathway-specific geranylgeranyl pyrophosphate synthase (GGPS) spyE is required to provide GGPP. Subsequently, geranylgeranyl- triacetate lactone is epoxidized at the terminal olein by the FAD- dependent monooxygenase spyC, followed by cyclization of the terpenoid component catalyzed by the terpene cyclase spyD to produce both the bicyclic sartorypyrone F and the monocyclic sartorypyrone D. Finally, the last step of the biosynthesis involves the acetylation of the meroterpenoids sartorypyrones D and F by the acetyltransferase SpyB to produce sartorypyrones A and G, respectively.","Acetyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate tolerance, py",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008374,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.3256,no
SPYB_ASPFU,Q4WBI0,ProtT3,Eukaryota,591,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of meroterpenoids called sartorypyrones. SpyB catalyzes the last step of the pathway and is responsible for the acetylation of sartorypyrones D and F to produce sartorypyrones A and G, respectively. The biosynthesis of sartorypyrones begins with the production of triacetic acid lactone (TAL) by the NR- PKS spyA using one molecule of acetyl-CoA and two molecules of malonyl- CoA. The prenyltransferase spyF then conjugates geranylgeranyl pyrophosphate (GGPP) to TAL to form geranylgeranyl-triacetate lactone, for which the pathway-specific geranylgeranyl pyrophosphate synthase (GGPS) spyE is required to provide GGPP. Subsequently, geranylgeranyl- triacetate lactone is epoxidized at the terminal olein by the FAD- dependent monooxygenase spyC, followed by cyclization of the terpenoid component catalyzed by the terpene cyclase spyD to produce both the bicyclic sartorypyrone F and the monocyclic sartorypyrone D. Finally, the last step of the biosynthesis involves the acetylation of the meroterpenoids sartorypyrones D and F by the acetyltransferase SpyB to produce sartorypyrones A and G, respectively.","Acetyltransferase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008374,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.3256,no
SPYB_ASPFU,Q4WBI0,ProtTale,Eukaryota,591,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of meroterpenoids called sartorypyrones. SpyB catalyzes the last step of the pathway and is responsible for the acetylation of sartorypyrones D and F to produce sartorypyrones A and G, respectively. The biosynthesis of sartorypyrones begins with the production of triacetic acid lactone (TAL) by the NR- PKS spyA using one molecule of acetyl-CoA and two molecules of malonyl- CoA. The prenyltransferase spyF then conjugates geranylgeranyl pyrophosphate (GGPP) to TAL to form geranylgeranyl-triacetate lactone, for which the pathway-specific geranylgeranyl pyrophosphate synthase (GGPS) spyE is required to provide GGPP. Subsequently, geranylgeranyl- triacetate lactone is epoxidized at the terminal olein by the FAD- dependent monooxygenase spyC, followed by cyclization of the terpenoid component catalyzed by the terpene cyclase spyD to produce both the bicyclic sartorypyrone F and the monocyclic sartorypyrone D. Finally, the last step of the biosynthesis involves the acetylation of the meroterpenoids sartorypyrones D and F by the acetyltransferase SpyB to produce sartorypyrones A and G, respectively.","O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008374,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.3256,no
SPYB_ASPFU,Q4WBI0,Protein2Text,Eukaryota,591,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of meroterpenoids called sartorypyrones. SpyB catalyzes the last step of the pathway and is responsible for the acetylation of sartorypyrones D and F to produce sartorypyrones A and G, respectively. The biosynthesis of sartorypyrones begins with the production of triacetic acid lactone (TAL) by the NR- PKS spyA using one molecule of acetyl-CoA and two molecules of malonyl- CoA. The prenyltransferase spyF then conjugates geranylgeranyl pyrophosphate (GGPP) to TAL to form geranylgeranyl-triacetate lactone, for which the pathway-specific geranylgeranyl pyrophosphate synthase (GGPS) spyE is required to provide GGPP. Subsequently, geranylgeranyl- triacetate lactone is epoxidized at the terminal olein by the FAD- dependent monooxygenase spyC, followed by cyclization of the terpenoid component catalyzed by the terpene cyclase spyD to produce both the bicyclic sartorypyrone F and the monocyclic sartorypyrone D. Finally, the last step of the biosynthesis involves the acetylation of the meroterpenoids sartorypyrones D and F by the acetyltransferase SpyB to produce sartorypyrones A and G, respectively.","This protein is involved in the molecular function of catalyzing a reaction in the biosynthesis of carotenoids, specifically in the conversion of a substrate to a product in the biosynthesis pathway.",No,No,No,No,No,not-Yes,GO:0008374,,,,,,,,,,,0,,0.3256,no
SPYB_ASPFU,Q4WBI0,Reference,Eukaryota,591,"Acetyltransferase; part of the gene cluster that mediates the biosynthesis of meroterpenoids called sartorypyrones. SpyB catalyzes the last step of the pathway and is responsible for the acetylation of sartorypyrones D and F to produce sartorypyrones A and G, respectively. The biosynthesis of sartorypyrones begins with the production of triacetic acid lactone (TAL) by the NR- PKS spyA using one molecule of acetyl-CoA and two molecules of malonyl- CoA. The prenyltransferase spyF then conjugates geranylgeranyl pyrophosphate (GGPP) to TAL to form geranylgeranyl-triacetate lactone, for which the pathway-specific geranylgeranyl pyrophosphate synthase (GGPS) spyE is required to provide GGPP. Subsequently, geranylgeranyl- triacetate lactone is epoxidized at the terminal olein by the FAD- dependent monooxygenase spyC, followed by cyclization of the terpenoid component catalyzed by the terpene cyclase spyD to produce both the bicyclic sartorypyrone F and the monocyclic sartorypyrone D. Finally, the last step of the biosynthesis involves the acetylation of the meroterpenoids sartorypyrones D and F by the acetyltransferase SpyB to produce sartorypyrones A and G, respectively.","Acetyltransferase; part of the gene cluster that mediates the biosynthesis of meroterpenoids called sartorypyrones. SpyB catalyzes the last step of the pathway and is responsible for the acetylation of sartorypyrones D and F to produce sartorypyrones A and G, respectively. The biosynthesis of sartorypyrones begins with the production of triacetic acid lactone (TAL) by the NR- PKS spyA using one molecule of acetyl-CoA and two molecules of malonyl- CoA. The prenyltransferase spyF then conjugates geranylgeranyl pyrophosphate (GGPP) to TAL to form geranylgeranyl-triacetate lactone, for which the pathway-specific geranylgeranyl pyrophosphate synthase (GGPS) spyE is required to provide GGPP. Subsequently, geranylgeranyl- triacetate lactone is epoxidized at the terminal olein by the FAD- dependent monooxygenase spyC, followed by cyclization of the terpenoid component catalyzed by the terpene cyclase spyD to produce both the bicyclic sartorypyrone F and the monocyclic sartorypyrone D. Finally, the last step of the biosynthesis involves the acetylation of the meroterpenoids sartorypyrones D and F by the acetyltransferase SpyB to produce sartorypyrones A and G, respectively.",,,,,,,GO:0008374,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.3256,no
SPYD_ASPFU,Q4WBI3,ESM2Text,Eukaryota,237,"Terpene cyclase; part of the gene cluster that mediates the biosynthesis of meroterpenoids called sartorypyrones. Within the pathway, spyD catalyzes the cyclization of epoxygeranylgeranyl-triacetate lactone. SpyD exhibits promiscuous activity, resulting in the formation of bicyclic sartorypyrone F and monocyclic sartorypyrone D. The biosynthesis of sartorypyrones begins with the production of triacetic acid lactone (TAL) by the NR-PKS spyA using one molecule of acetyl-CoA and two molecules of malonyl-CoA. The prenyltransferase spyF then conjugates geranylgeranyl pyrophosphate (GGPP) to TAL to form geranylgeranyl- triacetate lactone, for which the pathway-specific geranylgeranyl pyrophosphate synthase (GGPS) spyE is required to provide GGPP. Subsequently, geranylgeranyl-triacetate lactone is epoxidized at the terminal olein by the FAD-dependent monooxygenase spyC, followed by cyclization of the terpenoid component catalyzed by the terpene cyclase spyD to produce both the bicyclic sartorypyrone F and the monocyclic sartorypyrone D. Finally, the last step of the biosynthesis involves the acetylation of the meroterpenoids sartorypyrones D and F by the acetyltransferase SpyB to produce sartorypyrones A and G, respectively.","Terpene cyclase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ. Paxilline is converted to beta-pax",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016829,GO:0010333,GO:0016872,GO:0010333,,GO:0016829,0.6019,0.4807,0.6019,,1.0,4,0.6711,0.3286,no
SPYD_ASPFU,Q4WBI3,Prot2Text,Eukaryota,237,"Terpene cyclase; part of the gene cluster that mediates the biosynthesis of meroterpenoids called sartorypyrones. Within the pathway, spyD catalyzes the cyclization of epoxygeranylgeranyl-triacetate lactone. SpyD exhibits promiscuous activity, resulting in the formation of bicyclic sartorypyrone F and monocyclic sartorypyrone D. The biosynthesis of sartorypyrones begins with the production of triacetic acid lactone (TAL) by the NR-PKS spyA using one molecule of acetyl-CoA and two molecules of malonyl-CoA. The prenyltransferase spyF then conjugates geranylgeranyl pyrophosphate (GGPP) to TAL to form geranylgeranyl- triacetate lactone, for which the pathway-specific geranylgeranyl pyrophosphate synthase (GGPS) spyE is required to provide GGPP. Subsequently, geranylgeranyl-triacetate lactone is epoxidized at the terminal olein by the FAD-dependent monooxygenase spyC, followed by cyclization of the terpenoid component catalyzed by the terpene cyclase spyD to produce both the bicyclic sartorypyrone F and the monocyclic sartorypyrone D. Finally, the last step of the biosynthesis involves the acetylation of the meroterpenoids sartorypyrones D and F by the acetyltransferase SpyB to produce sartorypyrones A and G, respectively.","Terpene cyclase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ. Paxilline is converted to beta-pax",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016829,GO:0010333,GO:0010333,GO:0010333,GO:0010333,GO:0010333,0.6019,0.6019,0.6019,0.6019,0.6019,5,0.6019,0.3286,no
SPYD_ASPFU,Q4WBI3,ProtT3,Eukaryota,237,"Terpene cyclase; part of the gene cluster that mediates the biosynthesis of meroterpenoids called sartorypyrones. Within the pathway, spyD catalyzes the cyclization of epoxygeranylgeranyl-triacetate lactone. SpyD exhibits promiscuous activity, resulting in the formation of bicyclic sartorypyrone F and monocyclic sartorypyrone D. The biosynthesis of sartorypyrones begins with the production of triacetic acid lactone (TAL) by the NR-PKS spyA using one molecule of acetyl-CoA and two molecules of malonyl-CoA. The prenyltransferase spyF then conjugates geranylgeranyl pyrophosphate (GGPP) to TAL to form geranylgeranyl- triacetate lactone, for which the pathway-specific geranylgeranyl pyrophosphate synthase (GGPS) spyE is required to provide GGPP. Subsequently, geranylgeranyl-triacetate lactone is epoxidized at the terminal olein by the FAD-dependent monooxygenase spyC, followed by cyclization of the terpenoid component catalyzed by the terpene cyclase spyD to produce both the bicyclic sartorypyrone F and the monocyclic sartorypyrone D. Finally, the last step of the biosynthesis involves the acetylation of the meroterpenoids sartorypyrones D and F by the acetyltransferase SpyB to produce sartorypyrones A and G, respectively.",Terpene cyclase; part of the gene cluster that mediates the biosynthesis of the diterpenoid pyrones penitrems . The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase prtA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase prtD through the action of the pre,Yes,Yes,Yes,Yes,Yes,Yes,GO:0016829,GO:0016872,GO:0010333,GO:0010334,GO:0010333,GO:0010333,0.4807,0.6019,0.5381,0.6019,0.6019,5,0.5649,0.3286,no
SPYD_ASPFU,Q4WBI3,ProtTale,Eukaryota,237,"Terpene cyclase; part of the gene cluster that mediates the biosynthesis of meroterpenoids called sartorypyrones. Within the pathway, spyD catalyzes the cyclization of epoxygeranylgeranyl-triacetate lactone. SpyD exhibits promiscuous activity, resulting in the formation of bicyclic sartorypyrone F and monocyclic sartorypyrone D. The biosynthesis of sartorypyrones begins with the production of triacetic acid lactone (TAL) by the NR-PKS spyA using one molecule of acetyl-CoA and two molecules of malonyl-CoA. The prenyltransferase spyF then conjugates geranylgeranyl pyrophosphate (GGPP) to TAL to form geranylgeranyl- triacetate lactone, for which the pathway-specific geranylgeranyl pyrophosphate synthase (GGPS) spyE is required to provide GGPP. Subsequently, geranylgeranyl-triacetate lactone is epoxidized at the terminal olein by the FAD-dependent monooxygenase spyC, followed by cyclization of the terpenoid component catalyzed by the terpene cyclase spyD to produce both the bicyclic sartorypyrone F and the monocyclic sartorypyrone D. Finally, the last step of the biosynthesis involves the acetylation of the meroterpenoids sartorypyrones D and F by the acetyltransferase SpyB to produce sartorypyrones A and G, respectively.","Terpene cyclase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes nodulisporic acids (NAs). Within the pathway, nodC catalyzes the cyclization of the prenyl side chain of nodulisporic acid A to yield nodulisporic acid B. The geranylgeranyl diphosphate (GGPP) synthase ggs1, localized outside of the cluster, is proposed to catalyze the first step in nodulisporic acid biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016829,GO:0010333,GO:0016829,GO:0010333,GO:0016829,GO:0010333,0.6019,1.0,0.6019,1.0,0.6019,5,0.7611,0.3286,no
SPYD_ASPFU,Q4WBI3,Protein2Text,Eukaryota,237,"Terpene cyclase; part of the gene cluster that mediates the biosynthesis of meroterpenoids called sartorypyrones. Within the pathway, spyD catalyzes the cyclization of epoxygeranylgeranyl-triacetate lactone. SpyD exhibits promiscuous activity, resulting in the formation of bicyclic sartorypyrone F and monocyclic sartorypyrone D. The biosynthesis of sartorypyrones begins with the production of triacetic acid lactone (TAL) by the NR-PKS spyA using one molecule of acetyl-CoA and two molecules of malonyl-CoA. The prenyltransferase spyF then conjugates geranylgeranyl pyrophosphate (GGPP) to TAL to form geranylgeranyl- triacetate lactone, for which the pathway-specific geranylgeranyl pyrophosphate synthase (GGPS) spyE is required to provide GGPP. Subsequently, geranylgeranyl-triacetate lactone is epoxidized at the terminal olein by the FAD-dependent monooxygenase spyC, followed by cyclization of the terpenoid component catalyzed by the terpene cyclase spyD to produce both the bicyclic sartorypyrone F and the monocyclic sartorypyrone D. Finally, the last step of the biosynthesis involves the acetylation of the meroterpenoids sartorypyrones D and F by the acetyltransferase SpyB to produce sartorypyrones A and G, respectively.","The molecular function of this protein is not explicitly stated in the provided information. However, it is involved in the regulation of cell processes, specifically related to the transport of molecules across cell membranes.",Vague,No,No,Vague,No,not-Yes,GO:0016829,,,,,,,,,,,0,,0.3286,no
SPYD_ASPFU,Q4WBI3,Reference,Eukaryota,237,"Terpene cyclase; part of the gene cluster that mediates the biosynthesis of meroterpenoids called sartorypyrones. Within the pathway, spyD catalyzes the cyclization of epoxygeranylgeranyl-triacetate lactone. SpyD exhibits promiscuous activity, resulting in the formation of bicyclic sartorypyrone F and monocyclic sartorypyrone D. The biosynthesis of sartorypyrones begins with the production of triacetic acid lactone (TAL) by the NR-PKS spyA using one molecule of acetyl-CoA and two molecules of malonyl-CoA. The prenyltransferase spyF then conjugates geranylgeranyl pyrophosphate (GGPP) to TAL to form geranylgeranyl- triacetate lactone, for which the pathway-specific geranylgeranyl pyrophosphate synthase (GGPS) spyE is required to provide GGPP. Subsequently, geranylgeranyl-triacetate lactone is epoxidized at the terminal olein by the FAD-dependent monooxygenase spyC, followed by cyclization of the terpenoid component catalyzed by the terpene cyclase spyD to produce both the bicyclic sartorypyrone F and the monocyclic sartorypyrone D. Finally, the last step of the biosynthesis involves the acetylation of the meroterpenoids sartorypyrones D and F by the acetyltransferase SpyB to produce sartorypyrones A and G, respectively.","Terpene cyclase; part of the gene cluster that mediates the biosynthesis of meroterpenoids called sartorypyrones. Within the pathway, spyD catalyzes the cyclization of epoxygeranylgeranyl-triacetate lactone. SpyD exhibits promiscuous activity, resulting in the formation of bicyclic sartorypyrone F and monocyclic sartorypyrone D. The biosynthesis of sartorypyrones begins with the production of triacetic acid lactone (TAL) by the NR-PKS spyA using one molecule of acetyl-CoA and two molecules of malonyl-CoA. The prenyltransferase spyF then conjugates geranylgeranyl pyrophosphate (GGPP) to TAL to form geranylgeranyl- triacetate lactone, for which the pathway-specific geranylgeranyl pyrophosphate synthase (GGPS) spyE is required to provide GGPP. Subsequently, geranylgeranyl-triacetate lactone is epoxidized at the terminal olein by the FAD-dependent monooxygenase spyC, followed by cyclization of the terpenoid component catalyzed by the terpene cyclase spyD to produce both the bicyclic sartorypyrone F and the monocyclic sartorypyrone D. Finally, the last step of the biosynthesis involves the acetylation of the meroterpenoids sartorypyrones D and F by the acetyltransferase SpyB to produce sartorypyrones A and G, respectively.",,,,,,,GO:0016829,GO:0016829,GO:0016829,GO:0010333,GO:0016829,GO:0010333,1.0,1.0,0.6019,1.0,0.6019,5,0.8408,0.3286,no
PDP2_MOUSE,Q504M2,ESM2Text,Eukaryota,532,"Mitochondrial enzyme that catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex (PDC), thereby stimulating the conversion of pyruvate into acetyl-CoA. Acts as a crucial regulator of T cell metabolism and function, with a particular focus on T-helper Th17.",Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004741; GO:0046872; GO:0004722,GO:0004722,GO:0004721,GO:0004722,GO:0004722,GO:0004722,0.7467,0.6832,0.7467,0.7467,0.7467,5,0.734,0.5833,yes
PDP2_MOUSE,Q504M2,Prot2Text,Eukaryota,532,"Mitochondrial enzyme that catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex (PDC), thereby stimulating the conversion of pyruvate into acetyl-CoA. Acts as a crucial regulator of T cell metabolism and function, with a particular focus on T-helper Th17.",Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004741; GO:0046872; GO:0004722,GO:0004721,GO:0004722,GO:0004722,GO:0004722,GO:0004722,0.6832,0.7467,0.7467,0.7467,0.7467,5,0.734,0.5833,yes
PDP2_MOUSE,Q504M2,ProtT3,Eukaryota,532,"Mitochondrial enzyme that catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex (PDC), thereby stimulating the conversion of pyruvate into acetyl-CoA. Acts as a crucial regulator of T cell metabolism and function, with a particular focus on T-helper Th17.",Catalyzes the dephosphorylation of the E1 component of the pyruvate dehydrogenase complex. Mitochondrion matrix. Belongs to the PP2C family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004741; GO:0046872; GO:0004722,GO:0004722,GO:0004722,GO:0004722,GO:0004722,GO:0004722,0.7467,0.7467,0.7467,0.7467,0.7467,5,0.7467,0.5833,yes
PDP2_MOUSE,Q504M2,ProtTale,Eukaryota,532,"Mitochondrial enzyme that catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex (PDC), thereby stimulating the conversion of pyruvate into acetyl-CoA. Acts as a crucial regulator of T cell metabolism and function, with a particular focus on T-helper Th17.","Protein phosphatase that acts as a negative regulator of the abscisic acid (ABA) signaling pathway. Dephosphorylates and inactivates PYL1 and PYL8, two positive regulators of the ABA signaling pathway.",Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0004741; GO:0046872; GO:0004722,GO:0004721,GO:0004721,GO:0004722,GO:0004721,GO:0004721,0.6832,0.6832,0.7467,0.6832,0.6832,5,0.6959,0.5833,yes
PDP2_MOUSE,Q504M2,Protein2Text,Eukaryota,532,"Mitochondrial enzyme that catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex (PDC), thereby stimulating the conversion of pyruvate into acetyl-CoA. Acts as a crucial regulator of T cell metabolism and function, with a particular focus on T-helper Th17.","The molecular function of this protein is a magnesium-dependent, NAD(+)-linked, polyisothermal phosphatase that removes the phosphoryl group from the beta and gamma phosphates of ATP.",Maybe,No,No,Maybe,Maybe,not-Yes,GO:0004741; GO:0046872; GO:0004722,,GO:0016887,GO:0016887,,GO:0016887,,0.1865,0.1865,,0.1865,3,0.1865,0.5833,yes
PDP2_MOUSE,Q504M2,Reference,Eukaryota,532,"Mitochondrial enzyme that catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex (PDC), thereby stimulating the conversion of pyruvate into acetyl-CoA. Acts as a crucial regulator of T cell metabolism and function, with a particular focus on T-helper Th17.","Mitochondrial enzyme that catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex (PDC), thereby stimulating the conversion of pyruvate into acetyl-CoA. Acts as a crucial regulator of T cell metabolism and function, with a particular focus on T-helper Th17.",,,,,,,GO:0004741; GO:0046872; GO:0004722,GO:0004722,GO:0004721,GO:0004722,GO:0004721,GO:0004721,0.7467,0.6832,0.7467,0.6832,0.6832,5,0.7086,0.5833,yes
WBAN_SALAN,Q54129,ESM2Text,Bacteria,315,Rhamnosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the addition of a rhamnose to the galactosyl-undecaprenyl diphosphate intermediate.,"Involved in the synthesis of Nod factor, a sulfated N-acyl-beta-1,4-tetrasaccharide of N-acetylglucosamine which initiates a series of events in the host plant species leading eventually to nodulation.",No,No,Maybe,No,No,not-Yes,GO:0016757,,,,,,,,,,,0,,0.306,no
WBAN_SALAN,Q54129,Prot2Text,Bacteria,315,Rhamnosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the addition of a rhamnose to the galactosyl-undecaprenyl diphosphate intermediate.,"Involved in the biosynthesis of the arabinogalactan (AG) region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an essential component of the mycobacterial cell wall. Catalyzes the transfer of the first two galactofuranosyl (Galf) units from UDP-galactofuranose (UDP-Galf) onto the rhamnosyl-GlcNAc-diphospho-decaprenol (Rha-GlcNAc-PP-C50) acceptor, yielding galactofuranosyl-galactofuranosyl-rhamnosyl-GlcNAc-diphospho-decaprenol (Galf-Galf-Rha-GlcNAc-PP-C50). Thus, GlfT1 is the initiator of galactan synthesis, while GlfT2 continues with the subsequent polymerization events.",No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,1.0,1.0,1.0,1.0,1.0,5,1.0,0.306,no
WBAN_SALAN,Q54129,ProtT3,Bacteria,315,Rhamnosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the addition of a rhamnose to the galactosyl-undecaprenyl diphosphate intermediate.,Belongs to the glycosyltransferase 2 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016757,GO:0016757,GO:0016757,,GO:0016757,GO:0016757,1.0,1.0,,1.0,1.0,4,1.0,0.306,no
WBAN_SALAN,Q54129,ProtTale,Bacteria,315,Rhamnosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the addition of a rhamnose to the galactosyl-undecaprenyl diphosphate intermediate.,"Probable glycosyltransferase able to transfer a GlcNAc residue from UDP-GlcNAc to an N-acetylgalactosamine (GlcNAc-GalNAc) donor, with GlcNAc-2,3-(GlcNAc-GalNAc)-4,6-(GlcNAc-GalNAc)-8,10-(GlcNAc-GalNAc)-12,14-(GlcNAc-GalNAc)-16-(GlcNAc-GalNAc)-18-(GlcNAc-GalNAc)-20-(GlcNAc-GalNAc)-22-(GlcNAc-GalNAc)-24-(GlcNAc",No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,1.0,1.0,1.0,1.0,1.0,5,1.0,0.306,no
WBAN_SALAN,Q54129,Protein2Text,Bacteria,315,Rhamnosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the addition of a rhamnose to the galactosyl-undecaprenyl diphosphate intermediate.,"The molecular function of this protein is not explicitly stated in the provided information. However, it can be inferred that this protein is involved in a process related to glycosylation, given its classification as a glycosyltransferase. Glycosyltransferases are enzymes that catalyze the transfer of a glycosyl group from a donor molecule to an acceptor molecule, typically forming a glycosidic bond. They play crucial roles in various biological processes, including cell signaling, cell adhesion, and the synthesis of complex carbohydrates that form the structural backbone of cell surfaces and other biomolecules. 

In the context of the provided information, it is likely that this protein is involved in the synthesis of a specific glycan or glycolipid that plays a role in the pathogenesis of the disease associated with the genetic disorder. Further research would be necessary to determine the specific molecular function of this protein and its role in the disease process.",Vague,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,1.0,1.0,1.0,1.0,1.0,5,1.0,0.306,no
WBAN_SALAN,Q54129,Reference,Bacteria,315,Rhamnosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the addition of a rhamnose to the galactosyl-undecaprenyl diphosphate intermediate.,Rhamnosyltransferase involved in the biosynthesis of the repeat unit of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the addition of a rhamnose to the galactosyl-undecaprenyl diphosphate intermediate.,,,,,,,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,1.0,1.0,1.0,1.0,1.0,5,1.0,0.306,no
CY561_SCHJA,Q5D8X4,ESM2Text,Eukaryota,242,Functions as a ferric reductase that facilitates the reduction of ferric iron Fe(3+) to ferrous iron Fe(2+).,Transmembrane reductase that uses ascorbate as an electron donor in the cytoplasm and transfers electrons across membranes to reduce monodehydro-L-ascorbate radical in the lumen of secretory vesicles. It is therefore involved the regeneration and homeostasis within secretory vesicles of ascorbate which in turn provides reducing equivalents needed to support the activity of intravesicular enzymes.,Maybe,No,Maybe,Maybe,No,not-Yes,GO:0046872; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016655,,0.7193,0.7193,0.7193,0.4947,,4,0.6632,0.4936,no
CY561_SCHJA,Q5D8X4,Prot2Text,Eukaryota,242,Functions as a ferric reductase that facilitates the reduction of ferric iron Fe(3+) to ferrous iron Fe(2+).,Mediates the transmembrane transfer of electrons from NADH to cytochrome c. It prefers NADH over NADPH.,No,No,Maybe,No,No,not-Yes,GO:0046872; GO:0016491,GO:0016651,GO:0003954,GO:0003954,GO:0003954,GO:0003954,0.5852,0.4947,0.4947,0.4947,0.4947,5,0.5128,0.4936,no
CY561_SCHJA,Q5D8X4,ProtT3,Eukaryota,242,Functions as a ferric reductase that facilitates the reduction of ferric iron Fe(3+) to ferrous iron Fe(2+).,"Transmembrane reductase that uses ascorbate as an electron donor in the cytoplasm and transfers electrons across the plasma membrane to reduce monodehydro-L-ascorbate radical in the lumen of secretory vesicles. Cytoplasmic vesicle, secretory vesicle membrane; Multi-pass membrane protein Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein",Maybe,No,Maybe,Maybe,No,not-Yes,GO:0046872; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.7193,0.7193,0.7193,0.7193,0.7193,5,0.7193,0.4936,no
CY561_SCHJA,Q5D8X4,ProtTale,Eukaryota,242,Functions as a ferric reductase that facilitates the reduction of ferric iron Fe(3+) to ferrous iron Fe(2+).,Transmembrane reductase that uses ascorbate as an electron donor in the cytoplasm and transfers electrons across membranes to reduce monodehydro-L-ascorbate radical in the lumen of secretory vesicles. It is therefore involved in the regeneration of ascorbate within secretory vesicles and in its subsequent transport to the extracellular environment.,Maybe,No,No,Maybe,No,not-Yes,GO:0046872; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.7193,0.7193,0.7193,0.7193,0.7193,5,0.7193,0.4936,no
CY561_SCHJA,Q5D8X4,Protein2Text,Eukaryota,242,Functions as a ferric reductase that facilitates the reduction of ferric iron Fe(3+) to ferrous iron Fe(2+).,"The molecular function of this protein is as a copper-containing trans-membrane electron transporter, which is involved in the transport of electrons across cell membranes.",No,Maybe,Maybe,No,No,not-Yes,GO:0046872; GO:0016491,GO:0009055,GO:0009055; GO:0005507,GO:0009055; GO:0005507,,GO:0009055,0.2949,0.5552,0.5552,,0.2949,4,0.4251,0.4936,no
CY561_SCHJA,Q5D8X4,Reference,Eukaryota,242,Functions as a ferric reductase that facilitates the reduction of ferric iron Fe(3+) to ferrous iron Fe(2+).,Functions as a ferric reductase that facilitates the reduction of ferric iron Fe(3+) to ferrous iron Fe(2+).,,,,,,,GO:0046872; GO:0016491,GO:0016491,GO:0016491,GO:0000293,GO:0016491,GO:0000293,0.7193,0.7193,0.4947,0.7193,0.4947,5,0.6295,0.4936,no
BGLR_BACFN,Q5LIC7,ESM2Text,Bacteria,695,"Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG). Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sources of carbon. As part of the GI microbiome, this enzyme would be able to reactivate glucuronide drug conjugates, such reactivated compounds can significantly damage the GI tract.","Hydrolyzes both beta-linked D-galacturonate and beta-linked D-glucuronate. Has highest activity on disaccharides with beta-1,4-linked D-galacturonic acid in the presence of substrate alpha-1,3-linked D-galacturonic acid.",Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0004566,,,,,,,,,,,0,,0.5035,no
BGLR_BACFN,Q5LIC7,Prot2Text,Bacteria,695,"Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG). Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sources of carbon. As part of the GI microbiome, this enzyme would be able to reactivate glucuronide drug conjugates, such reactivated compounds can significantly damage the GI tract.","Glycoside hydrolase that may be involved in ulvan degradation (Probable). Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable).",No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004566,,,,,,,,,,,0,,0.5035,no
BGLR_BACFN,Q5LIC7,ProtT3,Bacteria,695,"Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG). Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sources of carbon. As part of the GI microbiome, this enzyme would be able to reactivate glucuronide drug conjugates, such reactivated compounds can significantly damage the GI tract.",Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). Secreted. Belongs to the glycosyl hydrolase 2 family,No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004566,GO:0004565,GO:0004553,,GO:0004553,GO:0016798,0.5445,0.7539,,0.7539,0.6466,4,0.6747,0.5035,no
BGLR_BACFN,Q5LIC7,ProtTale,Bacteria,695,"Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG). Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sources of carbon. As part of the GI microbiome, this enzyme would be able to reactivate glucuronide drug conjugates, such reactivated compounds can significantly damage the GI tract.","Involved in the degradation of galactomannan. Hydrolyzes beta1,4-galactose and beta1,6-mannose linkages in galactomannan.",No,No,Maybe,No,No,not-Yes,GO:0004566,GO:0016798,GO:0004553,GO:0004565,GO:0016798,GO:0004553,0.6466,0.7539,0.5445,0.6466,0.7539,5,0.6691,0.5035,no
BGLR_BACFN,Q5LIC7,Protein2Text,Bacteria,695,"Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG). Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sources of carbon. As part of the GI microbiome, this enzyme would be able to reactivate glucuronide drug conjugates, such reactivated compounds can significantly damage the GI tract.","The molecular function of this protein is likely to be a glycosyltransferase, specifically an alpha-1,6-mannosyltransferase, which is involved in the synthesis of N-glycans. This protein is responsible for transferring a mannose moiety from a donor substrate to the acceptor substrate, resulting in the formation of a glycosidic bond between the two molecules.",No,No,No,No,No,not-Yes,GO:0004566,GO:0008422,GO:0008422,GO:0008422,GO:0008422,GO:0008422,0.5445,0.5445,0.5445,0.5445,0.5445,5,0.5445,0.5035,no
BGLR_BACFN,Q5LIC7,Reference,Bacteria,695,"Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG). Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sources of carbon. As part of the GI microbiome, this enzyme would be able to reactivate glucuronide drug conjugates, such reactivated compounds can significantly damage the GI tract.","Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG). Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sources of carbon. As part of the GI microbiome, this enzyme would be able to reactivate glucuronide drug conjugates, such reactivated compounds can significantly damage the GI tract.",,,,,,,GO:0004566,GO:0004566,GO:0004566,GO:0004566,GO:0004566,GO:0004566,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5035,no
IAAF_AROAE,Q5P5Z9,ESM2Text,Bacteria,377,"Involved in degradation of indoleacetate, the most common member of the auxin class of plant hormones. Catalyzes the irreversible oxidative decarboxylation of (2- aminobenzyl)malonyl-CoA to 2-aminocinnamoyl-CoA and CO(2) (Probable). In vitro, shows high catalytic efficiency with benzylmalonyl-CoA, a chemical analog of the physiological substrate, but otherwise accepts only a few medium-chain alkylmalonyl-CoA compounds as alternative substrates with low activities.","Catalyzes the dehydrogenation of 2-hydroxybutyryl-CoA to crotonyl-CoA. In addition, it shows weak activity with crotonyl-CoA, but DauB is the most efficient substrate.",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0003995; GO:0050660,GO:0003995,GO:0016491,GO:0003995,GO:0003857,GO:0003995,0.6922,0.443,0.6922,0.2512,0.6922,5,0.5542,0.2016,no
IAAF_AROAE,Q5P5Z9,Prot2Text,Bacteria,377,"Involved in degradation of indoleacetate, the most common member of the auxin class of plant hormones. Catalyzes the irreversible oxidative decarboxylation of (2- aminobenzyl)malonyl-CoA to 2-aminocinnamoyl-CoA and CO(2) (Probable). In vitro, shows high catalytic efficiency with benzylmalonyl-CoA, a chemical analog of the physiological substrate, but otherwise accepts only a few medium-chain alkylmalonyl-CoA compounds as alternative substrates with low activities.",Catalyzes the conversion of crotonobetainyl-CoA to gamma-butyrobetainyl-CoA.,No,No,No,No,No,not-Yes,GO:0003995; GO:0050660,GO:0004300,GO:0004300,GO:0004300,GO:0004300,GO:0004300,0.1587,0.1587,0.1587,0.1587,0.1587,5,0.1587,0.2016,no
IAAF_AROAE,Q5P5Z9,ProtT3,Bacteria,377,"Involved in degradation of indoleacetate, the most common member of the auxin class of plant hormones. Catalyzes the irreversible oxidative decarboxylation of (2- aminobenzyl)malonyl-CoA to 2-aminocinnamoyl-CoA and CO(2) (Probable). In vitro, shows high catalytic efficiency with benzylmalonyl-CoA, a chemical analog of the physiological substrate, but otherwise accepts only a few medium-chain alkylmalonyl-CoA compounds as alternative substrates with low activities.",Belongs to the acyl-CoA dehydrogenase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0003995; GO:0050660,GO:0003995,GO:0003995,,GO:0003995,GO:0003995,0.6922,0.6922,,0.6922,0.6922,4,0.6922,0.2016,no
IAAF_AROAE,Q5P5Z9,ProtTale,Bacteria,377,"Involved in degradation of indoleacetate, the most common member of the auxin class of plant hormones. Catalyzes the irreversible oxidative decarboxylation of (2- aminobenzyl)malonyl-CoA to 2-aminocinnamoyl-CoA and CO(2) (Probable). In vitro, shows high catalytic efficiency with benzylmalonyl-CoA, a chemical analog of the physiological substrate, but otherwise accepts only a few medium-chain alkylmalonyl-CoA compounds as alternative substrates with low activities.",Catalyzes the reduction of crotonobetainyl-CoA to gamma- butyrobetainyl-CoA.,No,No,No,No,No,not-Yes,GO:0003995; GO:0050660,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.443,0.443,0.443,0.443,0.443,5,0.443,0.2016,no
IAAF_AROAE,Q5P5Z9,Protein2Text,Bacteria,377,"Involved in degradation of indoleacetate, the most common member of the auxin class of plant hormones. Catalyzes the irreversible oxidative decarboxylation of (2- aminobenzyl)malonyl-CoA to 2-aminocinnamoyl-CoA and CO(2) (Probable). In vitro, shows high catalytic efficiency with benzylmalonyl-CoA, a chemical analog of the physiological substrate, but otherwise accepts only a few medium-chain alkylmalonyl-CoA compounds as alternative substrates with low activities.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its name, ""protein"" is likely to be a part of a metabolic pathway, and its function may be related to the metabolism of a specific compound or molecule. 

In general, proteins that are involved in metabolic pathways often have molecular functions such as:

* Catalyzing a chemical reaction (e.g. an enzyme)
* Transporting a molecule across a cell membrane
* Binding to a specific molecule or ligand
* Regulating gene expression

Without more specific information, it is difficult to determine the exact molecular function of this protein. If you have more context or information about this protein, I may be able to provide a more detailed answer.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0003995; GO:0050660,,,,,,,,,,,0,,0.2016,no
IAAF_AROAE,Q5P5Z9,Reference,Bacteria,377,"Involved in degradation of indoleacetate, the most common member of the auxin class of plant hormones. Catalyzes the irreversible oxidative decarboxylation of (2- aminobenzyl)malonyl-CoA to 2-aminocinnamoyl-CoA and CO(2) (Probable). In vitro, shows high catalytic efficiency with benzylmalonyl-CoA, a chemical analog of the physiological substrate, but otherwise accepts only a few medium-chain alkylmalonyl-CoA compounds as alternative substrates with low activities.","Involved in degradation of indoleacetate, the most common member of the auxin class of plant hormones. Catalyzes the irreversible oxidative decarboxylation of (2- aminobenzyl)malonyl-CoA to 2-aminocinnamoyl-CoA and CO(2) (Probable). In vitro, shows high catalytic efficiency with benzylmalonyl-CoA, a chemical analog of the physiological substrate, but otherwise accepts only a few medium-chain alkylmalonyl-CoA compounds as alternative substrates with low activities.",,,,,,,GO:0003995; GO:0050660,GO:0016627,GO:0003995,GO:0003995,GO:0016491,GO:0003995,0.5205,0.6922,0.6922,0.443,0.6922,5,0.608,0.2016,no
FKBP5_RAT,Q5U2T9,ESM2Text,Eukaryota,456,"Immunophilin protein with PPIase and co-chaperone activities. Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded. Acts as a regulator of Akt/AKT1 activity by promoting the interaction between Akt/AKT1 and PHLPP1, thereby enhancing dephosphorylation and subsequent activation of Akt/AKT1. Interacts with IKBKE and IKBKB which facilitates IKK complex assembly leading to increased IKBKE and IKBKB kinase activity, NF-kappaB activation, and IFN production.","Immunophilin protein with PPIase and co-chaperone activities. Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded. Acts as a regulator of Akt/AKT1 activity by promoting the interaction between Akt/AKT1 and PHLPP1, thereby enhancing dephosphorylation and subsequent activation of Akt/AKT1. Interacts with IKBKE and IKBKB which facilitates IKK complex assembly leading to increased IKBKE and IKBKB kinase activity, NF-kappaB activation, and IFN production.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0003755,GO:0003755,GO:0003755,GO:0003755,GO:0003755,GO:0003755,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5893,yes
FKBP5_RAT,Q5U2T9,Prot2Text,Eukaryota,456,"Immunophilin protein with PPIase and co-chaperone activities. Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded. Acts as a regulator of Akt/AKT1 activity by promoting the interaction between Akt/AKT1 and PHLPP1, thereby enhancing dephosphorylation and subsequent activation of Akt/AKT1. Interacts with IKBKE and IKBKB which facilitates IKK complex assembly leading to increased IKBKE and IKBKB kinase activity, NF-kappaB activation, and IFN production.","Immunophilin protein with PPIase and co-chaperone activities. Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded. Acts as a regulator of Akt/AKT1 activity by promoting the interaction between Akt/AKT1 and PHLPP1, thereby enhancing dephosphorylation and subsequent activation of Akt/AKT1. Interacts with IKBKE and IKBKB which facilitates IKK complex assembly leading to increased IKBKE and IKBKB kinase activity, NF-kappaB activation, and IFN production.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0003755,GO:0003755,GO:0003755,GO:0003755,GO:0003755,GO:0003755,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5893,yes
FKBP5_RAT,Q5U2T9,ProtT3,Eukaryota,456,"Immunophilin protein with PPIase and co-chaperone activities. Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded. Acts as a regulator of Akt/AKT1 activity by promoting the interaction between Akt/AKT1 and PHLPP1, thereby enhancing dephosphorylation and subsequent activation of Akt/AKT1. Interacts with IKBKE and IKBKB which facilitates IKK complex assembly leading to increased IKBKE and IKBKB kinase activity, NF-kappaB activation, and IFN production.",PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). Acts as a co-chaperone for HSP90 (By similarity). Cytoplasm Nucleus. Belongs to the FKBP-type PPIase family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003755,GO:0003755,GO:0003755,GO:0003755,GO:0003755,GO:0003755,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5893,yes
FKBP5_RAT,Q5U2T9,ProtTale,Eukaryota,456,"Immunophilin protein with PPIase and co-chaperone activities. Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded. Acts as a regulator of Akt/AKT1 activity by promoting the interaction between Akt/AKT1 and PHLPP1, thereby enhancing dephosphorylation and subsequent activation of Akt/AKT1. Interacts with IKBKE and IKBKB which facilitates IKK complex assembly leading to increased IKBKE and IKBKB kinase activity, NF-kappaB activation, and IFN production.","PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and thus plays a key role in folding glycoproteins. Acts as a co-chaperone for the Hsp70-type chaperones HSPA8/HSC70 or HSPA9/HSP701.1/HSC70, regulating the folding and trafficking of proteins within the endoplasmic reticulum (ER). Binds unfolded proteins in the ER lumen and facilitates their folding or degradation. Associates with HSPA8/HSC70 to form a heterodimeric chaperone complex that acts as a key regulator of",Maybe,Maybe,Maybe,Yes,Yes,not-Yes,GO:0003755,GO:0003755,GO:0003755,GO:0003755,GO:0003755,GO:0003755,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5893,yes
FKBP5_RAT,Q5U2T9,Protein2Text,Eukaryota,456,"Immunophilin protein with PPIase and co-chaperone activities. Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded. Acts as a regulator of Akt/AKT1 activity by promoting the interaction between Akt/AKT1 and PHLPP1, thereby enhancing dephosphorylation and subsequent activation of Akt/AKT1. Interacts with IKBKE and IKBKB which facilitates IKK complex assembly leading to increased IKBKE and IKBKB kinase activity, NF-kappaB activation, and IFN production.","The molecular function of this protein is not explicitly stated in the provided text. However, based on the fact that it is a member of the Hsp90 protein family, it is likely that its molecular function is related to protein folding and chaperone activity. Hsp90 proteins are known to play a crucial role in the folding, stability, and function of many other proteins, particularly those involved in signal transduction and cellular stress responses.",Vague,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0003755,GO:0051082,GO:0051082; GO:0005524,GO:0051082; GO:0005524,GO:0051082,GO:0051082,0.1394,0.1149,0.1149,0.1394,0.1394,5,0.1296,0.5893,yes
FKBP5_RAT,Q5U2T9,Reference,Eukaryota,456,"Immunophilin protein with PPIase and co-chaperone activities. Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded. Acts as a regulator of Akt/AKT1 activity by promoting the interaction between Akt/AKT1 and PHLPP1, thereby enhancing dephosphorylation and subsequent activation of Akt/AKT1. Interacts with IKBKE and IKBKB which facilitates IKK complex assembly leading to increased IKBKE and IKBKB kinase activity, NF-kappaB activation, and IFN production.","Immunophilin protein with PPIase and co-chaperone activities. Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded. Acts as a regulator of Akt/AKT1 activity by promoting the interaction between Akt/AKT1 and PHLPP1, thereby enhancing dephosphorylation and subsequent activation of Akt/AKT1. Interacts with IKBKE and IKBKB which facilitates IKK complex assembly leading to increased IKBKE and IKBKB kinase activity, NF-kappaB activation, and IFN production.",,,,,,,GO:0003755,GO:0003755,GO:0003755,GO:0003755,GO:0003755,GO:0003755,1.0,1.0,1.0,1.0,1.0,5,1.0,0.5893,yes
HADA_CLODI,Q5U921,ESM2Text,Bacteria,399,"Involved in the reductive branch of L-leucine fermentation. Catalyzes the transfer of the CoA moiety from 4- methylpentanoyl-CoA (isocaproyl-CoA) to (R)-2-hydroxy-4- methylpentanoate ((R)-2-hydroxyisocaproate), leading to the formation of (R)-2-hydroxy-4-methylpentanoyl-CoA. Other CoA thioesters, such as acetyl-CoA or butyryl-CoA, are not accepted as substrates.","Involved in the catabolism of oxalate and in the adapatation to low pH via the reversible interconversion of (R)-alpha- and beta-hydroxyaspartate. It is also able to act on L-malate and L-valine and weakly on D-malate, L-glutamate and L-mannate. This enzyme is not able to act on pyruvate, D-glutamate, L-aspartate, L-mannate or D-glucate. This enzyme is not able to act on pyruvate, D-cellobate, L-glutamate, D-mannate or L-glutate.",No,No,Maybe,No,No,not-Yes,GO:0016740,GO:0016854,GO:0016853,,,,0.4807,0.5902,,,,2,0.5354,0.2981,no
HADA_CLODI,Q5U921,Prot2Text,Bacteria,399,"Involved in the reductive branch of L-leucine fermentation. Catalyzes the transfer of the CoA moiety from 4- methylpentanoyl-CoA (isocaproyl-CoA) to (R)-2-hydroxy-4- methylpentanoate ((R)-2-hydroxyisocaproate), leading to the formation of (R)-2-hydroxy-4-methylpentanoyl-CoA. Other CoA thioesters, such as acetyl-CoA or butyryl-CoA, are not accepted as substrates.","Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Essential enzyme for the bacterium survival, as it relies on oxalic acid as its sole source of energy. Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate. It can also use succinate semialdehyde and homoisocitrate as CoA acceptors.",No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016740,GO:0008410,GO:0008410,GO:0008410,GO:0008410,GO:0008410,0.6897,0.6897,0.6897,0.6897,0.6897,5,0.6897,0.2981,no
HADA_CLODI,Q5U921,ProtT3,Bacteria,399,"Involved in the reductive branch of L-leucine fermentation. Catalyzes the transfer of the CoA moiety from 4- methylpentanoyl-CoA (isocaproyl-CoA) to (R)-2-hydroxy-4- methylpentanoate ((R)-2-hydroxyisocaproate), leading to the formation of (R)-2-hydroxy-4-methylpentanoyl-CoA. Other CoA thioesters, such as acetyl-CoA or butyryl-CoA, are not accepted as substrates.",Catalyzes the reversible transfer of the CoA moiety from crotonobetainyl-CoA to L-carnitine to generate L-carnitinyl-CoA and crotonobetaine. Can also catalyze the reversible transfer of the CoA moiety from crotonobetainyl-CoA to gamma-butyrobetainyl-CoA to generate gamma-butyrobetainyl-CoA and crotonobetaine. Belongs to the CoA-transferase III family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016740,GO:0008410,GO:0008410,GO:0008410,GO:0008410,GO:0008410,0.6897,0.6897,0.6897,0.6897,0.6897,5,0.6897,0.2981,no
HADA_CLODI,Q5U921,ProtTale,Bacteria,399,"Involved in the reductive branch of L-leucine fermentation. Catalyzes the transfer of the CoA moiety from 4- methylpentanoyl-CoA (isocaproyl-CoA) to (R)-2-hydroxy-4- methylpentanoate ((R)-2-hydroxyisocaproate), leading to the formation of (R)-2-hydroxy-4-methylpentanoyl-CoA. Other CoA thioesters, such as acetyl-CoA or butyryl-CoA, are not accepted as substrates.",Involved in the 2-methylisoborneol (2MIB) degradation pathway. Catalyzes the transfer of an acetyl group from acetyl-CoA to 2MIB to yield 2-methyloxoborneol (2MOB) and CoA.,No,No,No,No,No,not-Yes,GO:0016740,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.6019,0.6019,0.6019,0.6019,0.6019,5,0.6019,0.2981,no
HADA_CLODI,Q5U921,Protein2Text,Bacteria,399,"Involved in the reductive branch of L-leucine fermentation. Catalyzes the transfer of the CoA moiety from 4- methylpentanoyl-CoA (isocaproyl-CoA) to (R)-2-hydroxy-4- methylpentanoate ((R)-2-hydroxyisocaproate), leading to the formation of (R)-2-hydroxy-4-methylpentanoyl-CoA. Other CoA thioesters, such as acetyl-CoA or butyryl-CoA, are not accepted as substrates.","This protein is a part of a system that catalyzes the conversion of succinyl-CoA to succinate, which is a key step in the citric acid cycle. Therefore, the molecular function of this protein is likely to be involved in the transfer of a CoA group from succinyl-CoA to ADP, producing succinate and ATP. However, since the name of the protein is not specified, it is difficult to provide a more precise answer. If you have more information about the protein, I can provide a more detailed answer.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016740,GO:0004775,GO:0004775,GO:0004775,GO:0004775,GO:0004775,0.3176,0.3176,0.3176,0.3176,0.3176,5,0.3176,0.2981,no
HADA_CLODI,Q5U921,Reference,Bacteria,399,"Involved in the reductive branch of L-leucine fermentation. Catalyzes the transfer of the CoA moiety from 4- methylpentanoyl-CoA (isocaproyl-CoA) to (R)-2-hydroxy-4- methylpentanoate ((R)-2-hydroxyisocaproate), leading to the formation of (R)-2-hydroxy-4-methylpentanoyl-CoA. Other CoA thioesters, such as acetyl-CoA or butyryl-CoA, are not accepted as substrates.","Involved in the reductive branch of L-leucine fermentation. Catalyzes the transfer of the CoA moiety from 4- methylpentanoyl-CoA (isocaproyl-CoA) to (R)-2-hydroxy-4- methylpentanoate ((R)-2-hydroxyisocaproate), leading to the formation of (R)-2-hydroxy-4-methylpentanoyl-CoA. Other CoA thioesters, such as acetyl-CoA or butyryl-CoA, are not accepted as substrates.",,,,,,,GO:0016740,GO:0008410,GO:0008410,GO:0008410,GO:0008410,GO:0008410,0.6897,0.6897,0.6897,0.6897,0.6897,5,0.6897,0.2981,no
TAGK_BACLD,Q65EY9,ESM2Text,Bacteria,304,"Kinase involved in a D-tagatose catabolic pathway. Catalyzes the phosphorylation of D- tagatose-1-phosphate (Tag-1P) to D-tagatose-1,6-bisphosphate. Can also use D-fructose-1-phosphate, with 40-fold lower catalytic efficiency, but not tagatose-6-phosphate or fructose-6- phosphate. The substrate, which occurs in a pyranose form in solution, may undergo a change to the furanose conformation after binding to the enzyme, in order to permit phosphorylation at C-6.","Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008662; GO:0005524,GO:0008662; GO:0005524,GO:0016301,GO:0008662,GO:0008662,GO:0008662,1.0,0.4452,0.6819,0.6819,0.6819,5,0.6982,0.3971,no
TAGK_BACLD,Q65EY9,Prot2Text,Bacteria,304,"Kinase involved in a D-tagatose catabolic pathway. Catalyzes the phosphorylation of D- tagatose-1-phosphate (Tag-1P) to D-tagatose-1,6-bisphosphate. Can also use D-fructose-1-phosphate, with 40-fold lower catalytic efficiency, but not tagatose-6-phosphate or fructose-6- phosphate. The substrate, which occurs in a pyranose form in solution, may undergo a change to the furanose conformation after binding to the enzyme, in order to permit phosphorylation at C-6.","Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008662; GO:0005524,GO:0008662,GO:0008662,GO:0008662,GO:0008662,GO:0008662,0.6819,0.6819,0.6819,0.6819,0.6819,5,0.6819,0.3971,no
TAGK_BACLD,Q65EY9,ProtT3,Bacteria,304,"Kinase involved in a D-tagatose catabolic pathway. Catalyzes the phosphorylation of D- tagatose-1-phosphate (Tag-1P) to D-tagatose-1,6-bisphosphate. Can also use D-fructose-1-phosphate, with 40-fold lower catalytic efficiency, but not tagatose-6-phosphate or fructose-6- phosphate. The substrate, which occurs in a pyranose form in solution, may undergo a change to the furanose conformation after binding to the enzyme, in order to permit phosphorylation at C-6.",Belongs to the carbohydrate kinase PfkB family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008662; GO:0005524,GO:0016301; GO:0005524,GO:0016301,,GO:0019200,GO:0016301; GO:0005524,0.8181,0.4452,,0.5002,0.8181,4,0.6454,0.3971,no
TAGK_BACLD,Q65EY9,ProtTale,Bacteria,304,"Kinase involved in a D-tagatose catabolic pathway. Catalyzes the phosphorylation of D- tagatose-1-phosphate (Tag-1P) to D-tagatose-1,6-bisphosphate. Can also use D-fructose-1-phosphate, with 40-fold lower catalytic efficiency, but not tagatose-6-phosphate or fructose-6- phosphate. The substrate, which occurs in a pyranose form in solution, may undergo a change to the furanose conformation after binding to the enzyme, in order to permit phosphorylation at C-6.","Catalyzes the ATP-dependent phosphorylation of fructose-l- phosphate to fructose-l,6-bisphosphate.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008662; GO:0005524,GO:0008662,GO:0008662; GO:0005524,GO:0008662,GO:0008662; GO:0005524,GO:0016301; GO:0005524,0.6819,1.0,0.6819,1.0,0.8181,5,0.8364,0.3971,no
TAGK_BACLD,Q65EY9,Protein2Text,Bacteria,304,"Kinase involved in a D-tagatose catabolic pathway. Catalyzes the phosphorylation of D- tagatose-1-phosphate (Tag-1P) to D-tagatose-1,6-bisphosphate. Can also use D-fructose-1-phosphate, with 40-fold lower catalytic efficiency, but not tagatose-6-phosphate or fructose-6- phosphate. The substrate, which occurs in a pyranose form in solution, may undergo a change to the furanose conformation after binding to the enzyme, in order to permit phosphorylation at C-6.","The molecular function of this protein is a kinase, specifically a phosphoribosylamine--glycine ligase.",No,No,No,Maybe,No,not-Yes,GO:0008662; GO:0005524,,GO:0004637,GO:0004637,GO:0004637,GO:0004631,,0.1401,0.1401,0.1401,0.345,4,0.1913,0.3971,no
TAGK_BACLD,Q65EY9,Reference,Bacteria,304,"Kinase involved in a D-tagatose catabolic pathway. Catalyzes the phosphorylation of D- tagatose-1-phosphate (Tag-1P) to D-tagatose-1,6-bisphosphate. Can also use D-fructose-1-phosphate, with 40-fold lower catalytic efficiency, but not tagatose-6-phosphate or fructose-6- phosphate. The substrate, which occurs in a pyranose form in solution, may undergo a change to the furanose conformation after binding to the enzyme, in order to permit phosphorylation at C-6.","Kinase involved in a D-tagatose catabolic pathway. Catalyzes the phosphorylation of D- tagatose-1-phosphate (Tag-1P) to D-tagatose-1,6-bisphosphate. Can also use D-fructose-1-phosphate, with 40-fold lower catalytic efficiency, but not tagatose-6-phosphate or fructose-6- phosphate. The substrate, which occurs in a pyranose form in solution, may undergo a change to the furanose conformation after binding to the enzyme, in order to permit phosphorylation at C-6.",,,,,,,GO:0008662; GO:0005524,GO:0016301,GO:0016301; GO:0005524,GO:0016301; GO:0005524,GO:0016301,GO:0016301; GO:0005524,0.4452,0.8181,0.8181,0.4452,0.8181,5,0.6689,0.3971,no
JAMA_MOOP1,Q6E7K9,ESM2Text,Bacteria,592,"Ligase involved in the biosynthesis of jamaicamides, which show sodium channel blocking activity and fish toxicity. Initiates jamaicamide biosynthesis by the activation of the starter unit, 5-hexenoic acid, followed by the loading of the activated 5-hexenoic acid onto the acyl carrier protein JamC. In vitro, can also use 5- hexynoic acid, heptanoic acid, butanoic acid, hexanoic acid and benzoic acid.",Covalently attaches a chromophore to C-3 of phycobiliproteins. Substrate-specific binding is not dependent on prior ATP-binding or post-translational modification by the bifunctional chaperone ATP-dependent enzymes.,No,No,Maybe,No,No,not-Yes,GO:0070566; GO:0005524; GO:0016874,,GO:0016874,,,,,0.6106,,,,1,0.6106,0.3889,no
JAMA_MOOP1,Q6E7K9,Prot2Text,Bacteria,592,"Ligase involved in the biosynthesis of jamaicamides, which show sodium channel blocking activity and fish toxicity. Initiates jamaicamide biosynthesis by the activation of the starter unit, 5-hexenoic acid, followed by the loading of the activated 5-hexenoic acid onto the acyl carrier protein JamC. In vitro, can also use 5- hexynoic acid, heptanoic acid, butanoic acid, hexanoic acid and benzoic acid.","Catalyzes the activation of medium/long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the multifunctional polyketide synthase PpsA for further chain extension. Involved in the biosynthesis of phenolphthiocerol, which is an important intermediate in the biosynthesis of phenolic glycolipid (PGL), also called mycosid B.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0070566; GO:0005524; GO:0016874,GO:0016877,GO:0016874,GO:0016877,GO:0016878,GO:0016878,0.4968,0.6106,0.4968,0.4195,0.4195,5,0.4886,0.3889,no
JAMA_MOOP1,Q6E7K9,ProtT3,Bacteria,592,"Ligase involved in the biosynthesis of jamaicamides, which show sodium channel blocking activity and fish toxicity. Initiates jamaicamide biosynthesis by the activation of the starter unit, 5-hexenoic acid, followed by the loading of the activated 5-hexenoic acid onto the acyl carrier protein JamC. In vitro, can also use 5- hexynoic acid, heptanoic acid, butanoic acid, hexanoic acid and benzoic acid.","Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the multifunctional polyketide synthase Pks2 for further chain extension. Belongs to the ATP-dependent AMP-binding enzyme family",Maybe,Maybe,Vague,Maybe,Maybe,not-Yes,GO:0070566; GO:0005524; GO:0016874,GO:0004467; GO:0005524,GO:0004467,GO:0004467; GO:0005524,GO:0004467,GO:0004467,0.6061,0.271,0.6061,0.271,0.271,5,0.405,0.3889,no
JAMA_MOOP1,Q6E7K9,ProtTale,Bacteria,592,"Ligase involved in the biosynthesis of jamaicamides, which show sodium channel blocking activity and fish toxicity. Initiates jamaicamide biosynthesis by the activation of the starter unit, 5-hexenoic acid, followed by the loading of the activated 5-hexenoic acid onto the acyl carrier protein JamC. In vitro, can also use 5- hexynoic acid, heptanoic acid, butanoic acid, hexanoic acid and benzoic acid.","Involved in the biosynthesis of the antibiotic polyketide bacillaene which is involved in the infection process. Catalyzes the ATP-dependent activation of propionyl-CoA, but not of other acyl-CoAs.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0070566; GO:0005524; GO:0016874,GO:0016874,GO:0016874; GO:0005524,GO:0016874,GO:0016874; GO:0005524,GO:0016874; GO:0005524,0.6106,0.871,0.6106,0.871,0.871,5,0.7668,0.3889,no
JAMA_MOOP1,Q6E7K9,Protein2Text,Bacteria,592,"Ligase involved in the biosynthesis of jamaicamides, which show sodium channel blocking activity and fish toxicity. Initiates jamaicamide biosynthesis by the activation of the starter unit, 5-hexenoic acid, followed by the loading of the activated 5-hexenoic acid onto the acyl carrier protein JamC. In vitro, can also use 5- hexynoic acid, heptanoic acid, butanoic acid, hexanoic acid and benzoic acid.","The molecular function of this protein is likely to be involved in the synthesis of fatty acid derivatives, as it is a member of the Enoyl-CoA hydratase family, which typically catalyzes the hydration of enoyl-CoA derivatives.",Vague,No,No,No,No,not-Yes,GO:0070566; GO:0005524; GO:0016874,GO:0004300,GO:0004300,GO:0004300,GO:0004300,GO:0004300,0.2415,0.2415,0.2415,0.2415,0.2415,5,0.2415,0.3889,no
JAMA_MOOP1,Q6E7K9,Reference,Bacteria,592,"Ligase involved in the biosynthesis of jamaicamides, which show sodium channel blocking activity and fish toxicity. Initiates jamaicamide biosynthesis by the activation of the starter unit, 5-hexenoic acid, followed by the loading of the activated 5-hexenoic acid onto the acyl carrier protein JamC. In vitro, can also use 5- hexynoic acid, heptanoic acid, butanoic acid, hexanoic acid and benzoic acid.","Ligase involved in the biosynthesis of jamaicamides, which show sodium channel blocking activity and fish toxicity. Initiates jamaicamide biosynthesis by the activation of the starter unit, 5-hexenoic acid, followed by the loading of the activated 5-hexenoic acid onto the acyl carrier protein JamC. In vitro, can also use 5- hexynoic acid, heptanoic acid, butanoic acid, hexanoic acid and benzoic acid.",,,,,,,GO:0070566; GO:0005524; GO:0016874,GO:0016874,GO:0016878,GO:0016874,GO:0016878,GO:0016878,0.6106,0.4195,0.6106,0.4195,0.4195,5,0.4959,0.3889,no
T2AH_TAXCA,Q6JD68,ESM2Text,Eukaryota,495,Catalyzes the conversion of taxusin to 2-alpha-hydroxytaxusin in taxol biosynthesis. Catalyzes the conversion of 7- beta-hydroxytaxusin to 2-alpha-7-beta-hydroxytaxusin in taxol biosynthesis.,"Cytochrome P450 monooxygenase involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family. Catalyzes the hydroxylation of delta(6)-protoilludene to produce 19-hydroxyprotoilludene. The pathway begins with the biosynthesis of etoposide by a multicopperal polyketide synthase (ptaK1) that produces an alpha-pyran-H2 beta-ring in the biosynthetic pathway by acting like a class III intermediate producer, rather than a class IV intermediate producer. The alpha-pyran-H2 beta-ring is then captured by the enoyl reductase (nepsilon-ring-enzyme) PIP0112 and linked to tyrosine to produce the tetraketide-H2. The tetraketide-H2 is elongated by a Diels-Alder reaction to afford quinone. The tetraketide-H2 then undergoes condensation with a semialdehyde to form quinone-H2. The epoxide hydroxylase PIP0111 then catalyzes two consecutive hydrox",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0016712,GO:0004497; GO:0020037,GO:0004497,GO:0004497; GO:0020037,GO:0008168,GO:0004497,0.7444,0.4422,0.7444,0.1796,0.4422,5,0.5106,0.3406,no
T2AH_TAXCA,Q6JD68,Prot2Text,Eukaryota,495,Catalyzes the conversion of taxusin to 2-alpha-hydroxytaxusin in taxol biosynthesis. Catalyzes the conversion of 7- beta-hydroxytaxusin to 2-alpha-7-beta-hydroxytaxusin in taxol biosynthesis.,Has a significant activity in oxidation of tazarotenic acid and may therefore metabolize that xenobiotic in vivo.,Maybe,No,No,Maybe,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0016712,GO:0016491,GO:0016491,,GO:0016491,GO:0016491,0.3887,0.3887,,0.3887,0.3887,4,0.3887,0.3406,no
T2AH_TAXCA,Q6JD68,ProtT3,Eukaryota,495,Catalyzes the conversion of taxusin to 2-alpha-hydroxytaxusin in taxol biosynthesis. Catalyzes the conversion of 7- beta-hydroxytaxusin to 2-alpha-7-beta-hydroxytaxusin in taxol biosynthesis.,Catalyzes the conversion of ent-kaurenoic acid to ent-kaurenoic acid methyl ester. Membrane; Single-pass membrane protein. Belongs to the cytochrome P450 family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0016712,GO:0004497; GO:0005506; GO:0020037,GO:0004497; GO:0005506,GO:0004497; GO:0020037,GO:0004497; GO:0020037,GO:0004497,0.9157,0.7444,0.7444,0.7444,0.4422,5,0.7182,0.3406,no
T2AH_TAXCA,Q6JD68,ProtTale,Eukaryota,495,Catalyzes the conversion of taxusin to 2-alpha-hydroxytaxusin in taxol biosynthesis. Catalyzes the conversion of 7- beta-hydroxytaxusin to 2-alpha-7-beta-hydroxytaxusin in taxol biosynthesis.,Involved in brassinosteroid (BR) biosynthesis. Catalyzes the conversion of campesterol to 6-deoxocathasterone.,No,No,No,Maybe,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0016712,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.3887,0.3887,0.3887,0.3887,0.3887,5,0.3887,0.3406,no
T2AH_TAXCA,Q6JD68,Protein2Text,Eukaryota,495,Catalyzes the conversion of taxusin to 2-alpha-hydroxytaxusin in taxol biosynthesis. Catalyzes the conversion of 7- beta-hydroxytaxusin to 2-alpha-7-beta-hydroxytaxusin in taxol biosynthesis.,"The molecular function of this protein is related to the metabolism of steroids, specifically the conversion of cholesterol into other steroid hormones. The protein is involved in the hydroxylation of cholesterol, which is a crucial step in the biosynthesis of steroid hormones such as cortisol, aldosterone, and estrogen. This protein is a member of the cytochrome P450 family, which is a group of enzymes that play a key role in the metabolism of steroids and other lipids. The protein is also known to be involved in the metabolism of other lipids, including fatty acids and cholesterol esters.

In more detail, the molecular function of this protein can be described as follows:

* Catalyzes the hydroxylation of cholesterol at the 22-position, resulting in the formation of 22-hydroxycholesterol.
* Involved in the metabolism of other steroids, including cortisol, aldosterone, and estrogen.
* Plays a role in the metabolism of fatty acids and cholesterol esters.
* Part of the cytochrome P450 family, which is a group of enzymes that play a key role in the metabolism of steroids and other lipids.

Overall, the molecular function of this protein is related to the metabolism of steroids and other lipids, and is important for the synthesis of steroid hormones and the maintenance of lipid homeostasis in the body.",Maybe,No,No,Maybe,Maybe,not-Yes,GO:0020037; GO:0005506; GO:0016712,GO:0004497,GO:0004497; GO:0020037,GO:0004497; GO:0020037,GO:0004497,GO:0004497,0.4422,0.7444,0.7444,0.4422,0.4422,5,0.5631,0.3406,no
T2AH_TAXCA,Q6JD68,Reference,Eukaryota,495,Catalyzes the conversion of taxusin to 2-alpha-hydroxytaxusin in taxol biosynthesis. Catalyzes the conversion of 7- beta-hydroxytaxusin to 2-alpha-7-beta-hydroxytaxusin in taxol biosynthesis.,Catalyzes the conversion of taxusin to 2-alpha-hydroxytaxusin in taxol biosynthesis. Catalyzes the conversion of 7- beta-hydroxytaxusin to 2-alpha-7-beta-hydroxytaxusin in taxol biosynthesis.,,,,,,,GO:0020037; GO:0005506; GO:0016712,GO:0016709,GO:0016491; GO:0004497,GO:0016491,GO:0016709,GO:0004497,0.4308,0.4885,0.3887,0.4308,0.4422,5,0.4362,0.3406,no
AURI_STRTU,Q70KH3,ESM2Text,Bacteria,230,"Methyltransferase involved in the biosynthesis of the antibiotic aureothin, a nitroaryl polyketide metabolite with antifungal, cytotoxic and insecticidal activities. Catalyzes the methylation of demethylluteothin to luteothin (also called deoxyaureothin). Is specific for its gamma- pyrone substrate, and does not act on the alpha-pyrone isomer.","S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the methylation of the para-nitrogen atom of 1-benzoquinol-2-one (BQ-2) to produce menadione (MDA). MDA is an intermediate in the biosynthesis of menaquinone (MK, vitamin K2).",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008168,GO:0008168,GO:0008168,,GO:0008168,GO:0008168,1.0,1.0,,1.0,1.0,4,1.0,0.2668,no
AURI_STRTU,Q70KH3,Prot2Text,Bacteria,230,"Methyltransferase involved in the biosynthesis of the antibiotic aureothin, a nitroaryl polyketide metabolite with antifungal, cytotoxic and insecticidal activities. Catalyzes the methylation of demethylluteothin to luteothin (also called deoxyaureothin). Is specific for its gamma- pyrone substrate, and does not act on the alpha-pyrone isomer.","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential tricyclic",Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0008168,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.2668,no
AURI_STRTU,Q70KH3,ProtT3,Bacteria,230,"Methyltransferase involved in the biosynthesis of the antibiotic aureothin, a nitroaryl polyketide metabolite with antifungal, cytotoxic and insecticidal activities. Catalyzes the methylation of demethylluteothin to luteothin (also called deoxyaureothin). Is specific for its gamma- pyrone substrate, and does not act on the alpha-pyrone isomer.",O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeran,Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0008168,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.2668,no
AURI_STRTU,Q70KH3,ProtTale,Bacteria,230,"Methyltransferase involved in the biosynthesis of the antibiotic aureothin, a nitroaryl polyketide metabolite with antifungal, cytotoxic and insecticidal activities. Catalyzes the methylation of demethylluteothin to luteothin (also called deoxyaureothin). Is specific for its gamma- pyrone substrate, and does not act on the alpha-pyrone isomer.",O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The first step of the pathway is the synthesis of 6-methylsalicylic acid methyl ester (6-MSAME) by the polyketide synthase aumA. 6-MSAME is then converted to protoarthripenoid A by the cytochrome P450 monooxygenase aumB. Protoarthripenoid A is further oxidized to arthripenoid A by the cytochrome P450 monooxygenase aumC. The FAD-dependent monooxygenase aumD,Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0008168,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.2668,no
AURI_STRTU,Q70KH3,Protein2Text,Bacteria,230,"Methyltransferase involved in the biosynthesis of the antibiotic aureothin, a nitroaryl polyketide metabolite with antifungal, cytotoxic and insecticidal activities. Catalyzes the methylation of demethylluteothin to luteothin (also called deoxyaureothin). Is specific for its gamma- pyrone substrate, and does not act on the alpha-pyrone isomer.","The molecular function of this protein is as a S-adenosyl-L-methionine-dependent methyltransferase, which is involved in the methylation of other biomolecules. Specifically, it is involved in the synthesis of a lipid that plays a role in cell membrane structure and function.",Maybe,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2668,no
AURI_STRTU,Q70KH3,Reference,Bacteria,230,"Methyltransferase involved in the biosynthesis of the antibiotic aureothin, a nitroaryl polyketide metabolite with antifungal, cytotoxic and insecticidal activities. Catalyzes the methylation of demethylluteothin to luteothin (also called deoxyaureothin). Is specific for its gamma- pyrone substrate, and does not act on the alpha-pyrone isomer.","Methyltransferase involved in the biosynthesis of the antibiotic aureothin, a nitroaryl polyketide metabolite with antifungal, cytotoxic and insecticidal activities. Catalyzes the methylation of demethylluteothin to luteothin (also called deoxyaureothin). Is specific for its gamma- pyrone substrate, and does not act on the alpha-pyrone isomer.",,,,,,,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2668,no
SMOA_AGRFC,Q7CS24,ESM2Text,Bacteria,174,"Part of the sulfoquinovose monooxygenase (sulfo-SMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite. Catalyzes the NADH- dependent reduction of FMN. FMNH(2) is then transferred to the sulfoquinovose monooxygenase SmoC.","Catalyzes the reduction of FAD with the concomitant oxidation of NADH. NADPH is the physiological electron donor. Subsequently, the reduced flavins diffuse to the oxygenase component NphA2.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0010181; GO:0052874; GO:0004497; GO:0042602,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.5634,0.5634,0.5634,0.5634,0.5634,5,0.5634,0.1901,no
SMOA_AGRFC,Q7CS24,Prot2Text,Bacteria,174,"Part of the sulfoquinovose monooxygenase (sulfo-SMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite. Catalyzes the NADH- dependent reduction of FMN. FMNH(2) is then transferred to the sulfoquinovose monooxygenase SmoC.",Catalyzes the reduction of FMN to FMNH2 which is used to reduce pyrimidine by RutA via the Rut pathway.,Maybe,Maybe,Maybe,Yes,Yes,not-Yes,GO:0010181; GO:0052874; GO:0004497; GO:0042602,GO:0008752,GO:0008752,GO:0008752,GO:0008752,GO:0008752,0.5846,0.5846,0.5846,0.5846,0.5846,5,0.5846,0.1901,no
SMOA_AGRFC,Q7CS24,ProtT3,Bacteria,174,"Part of the sulfoquinovose monooxygenase (sulfo-SMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite. Catalyzes the NADH- dependent reduction of FMN. FMNH(2) is then transferred to the sulfoquinovose monooxygenase SmoC.",Catalyzes the reduction of flavin mononucleotide (FMN) to FMNH(2). Belongs to the non-flavoprotein flavin reductase family,Maybe,Maybe,Maybe,Yes,Yes,not-Yes,GO:0010181; GO:0052874; GO:0004497; GO:0042602,GO:0008752,GO:0008752,GO:0008752,GO:0008752,GO:0008752,0.5846,0.5846,0.5846,0.5846,0.5846,5,0.5846,0.1901,no
SMOA_AGRFC,Q7CS24,ProtTale,Bacteria,174,"Part of the sulfoquinovose monooxygenase (sulfo-SMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite. Catalyzes the NADH- dependent reduction of FMN. FMNH(2) is then transferred to the sulfoquinovose monooxygenase SmoC.",Catalyzes the reduction of FMN to FMNH2 which is then used to reduce pyrimidine N(1)- mononucleotide (mN(1)N) to give pyrimidine N(1)- nucleoside. Can also reduce pyrimidine N(3)- mononucleotide (mN(3)N) to pyrimidine N(3)-nucleotide (N(3)N).,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0010181; GO:0052874; GO:0004497; GO:0042602,GO:0016491,GO:0016491; GO:0010181,GO:0016491,GO:0008752,GO:0008752,0.5634,0.7842,0.5634,0.5846,0.5846,5,0.616,0.1901,no
SMOA_AGRFC,Q7CS24,Protein2Text,Bacteria,174,"Part of the sulfoquinovose monooxygenase (sulfo-SMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite. Catalyzes the NADH- dependent reduction of FMN. FMNH(2) is then transferred to the sulfoquinovose monooxygenase SmoC.",The molecular function of this protein is an oxidoreductase.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0010181; GO:0052874; GO:0004497; GO:0042602,GO:0016491,GO:0016491,GO:0016491,,GO:0016491,0.5634,0.5634,0.5634,,0.5634,4,0.5634,0.1901,no
SMOA_AGRFC,Q7CS24,Reference,Bacteria,174,"Part of the sulfoquinovose monooxygenase (sulfo-SMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite. Catalyzes the NADH- dependent reduction of FMN. FMNH(2) is then transferred to the sulfoquinovose monooxygenase SmoC.","Part of the sulfoquinovose monooxygenase (sulfo-SMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite. Catalyzes the NADH- dependent reduction of FMN. FMNH(2) is then transferred to the sulfoquinovose monooxygenase SmoC.",,,,,,,GO:0010181; GO:0052874; GO:0004497; GO:0042602,GO:0008752,GO:0016491; GO:0010181,GO:0008752,GO:0008752,GO:0008752,0.5846,0.7842,0.5846,0.5846,0.5846,5,0.6245,0.1901,no
SMOE_AGRFC,Q7CS28,ESM2Text,Bacteria,358,Part of the ABC transporter complex SmoEFGH involved in sulfoquinovosyl glycerol (SQGro) uptake (Probable). Responsible for energy coupling to the transport system (Probable).,Part of the ABC transporter complex UgpABCE involved in sn-glycerol-3-phosphate import. Responsible for energy coupling to the transport system.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0140359; GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887; GO:0005524,0.8452,0.5717,0.8452,0.8452,0.8452,5,0.7905,0.4053,no
SMOE_AGRFC,Q7CS28,Prot2Text,Bacteria,358,Part of the ABC transporter complex SmoEFGH involved in sulfoquinovosyl glycerol (SQGro) uptake (Probable). Responsible for energy coupling to the transport system (Probable).,Part of the ABC transporter complex UgpABCE involved in sn-glycerol-3-phosphate import. Responsible for energy coupling to the transport system.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0140359; GO:0005524; GO:0016887,GO:0016887,GO:0016887,GO:0016887,GO:0016887,GO:0016887,0.5717,0.5717,0.5717,0.5717,0.5717,5,0.5717,0.4053,no
SMOE_AGRFC,Q7CS28,ProtT3,Bacteria,358,Part of the ABC transporter complex SmoEFGH involved in sulfoquinovosyl glycerol (SQGro) uptake (Probable). Responsible for energy coupling to the transport system (Probable).,Part of the ABC transporter complex UgpBAEC involved in sn- glycerol-3-phosphate (G3P) import. Responsible for energy coupling to the transport system. Cell inner membrane; Peripheral membrane protein. Belongs to the ABC transporter superfamily. sn-glycerol-3- phosphate importer (TC 3.A.1.1.3) family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0140359; GO:0005524; GO:0016887,GO:0005524; GO:0016887,GO:0016887,GO:0016887,GO:0016887; GO:0005524,GO:0005524; GO:0016887,0.8452,0.5717,0.5717,0.8452,0.8452,5,0.7358,0.4053,no
SMOE_AGRFC,Q7CS28,ProtTale,Bacteria,358,Part of the ABC transporter complex SmoEFGH involved in sulfoquinovosyl glycerol (SQGro) uptake (Probable). Responsible for energy coupling to the transport system (Probable).,Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0140359; GO:0005524; GO:0016887,GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0005524; GO:0016887,GO:0016887; GO:0005524,GO:0016887,0.8452,0.8452,0.8452,0.8452,0.5717,5,0.7905,0.4053,no
SMOE_AGRFC,Q7CS28,Protein2Text,Bacteria,358,Part of the ABC transporter complex SmoEFGH involved in sulfoquinovosyl glycerol (SQGro) uptake (Probable). Responsible for energy coupling to the transport system (Probable).,"The molecular function of this protein is as a component of the ABC transporter complex involved in resistance to antibiotics and toxic compounds, specifically in resistance to macrolides, tetracyclines, and other compounds. It is a part of the energy-transducing subunit of the complex, which is responsible for energy coupling and ATP hydrolysis. This protein is also involved in the export of the antibiotic resistance protein.",Vague,No,No,Vague,Maybe,not-Yes,GO:0140359; GO:0005524; GO:0016887,GO:0016887,GO:0005524; GO:0016887,GO:0042626; GO:0005524,GO:0042626,GO:0042626,0.5717,0.8452,0.8098,0.5305,0.5305,5,0.6575,0.4053,no
SMOE_AGRFC,Q7CS28,Reference,Bacteria,358,Part of the ABC transporter complex SmoEFGH involved in sulfoquinovosyl glycerol (SQGro) uptake (Probable). Responsible for energy coupling to the transport system (Probable).,Part of the ABC transporter complex SmoEFGH involved in sulfoquinovosyl glycerol (SQGro) uptake (Probable). Responsible for energy coupling to the transport system (Probable).,,,,,,,GO:0140359; GO:0005524; GO:0016887,GO:0016887,GO:0016887,,,GO:0016887,0.5717,0.5717,,,0.5717,3,0.5717,0.4053,no
LPXH_PORGI,Q7MTZ8,ESM2Text,Bacteria,262,"Hydrolyzes the pyrophosphate bond of UDP-2,3- diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.","Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0008758,GO:0016787,GO:0016787,GO:0016787,GO:0008483,GO:0016787,0.4114,0.4114,0.4114,0.1726,0.4114,5,0.3636,0.235,no
LPXH_PORGI,Q7MTZ8,Prot2Text,Bacteria,262,"Hydrolyzes the pyrophosphate bond of UDP-2,3- diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.","Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0008758,GO:0016787,GO:0008484,GO:0008484,GO:0008758,GO:0008758,0.4114,0.2683,0.2683,0.6924,0.6924,5,0.4666,0.235,no
LPXH_PORGI,Q7MTZ8,ProtT3,Bacteria,262,"Hydrolyzes the pyrophosphate bond of UDP-2,3- diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.","Hydrolyzes the pyrophosphate bond of UDP-2,3- diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. Hydrolyzes the pyrophosphate bond of UDP-2,3- diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the",Yes,Yes,Yes,Yes,Yes,Yes,GO:0046872; GO:0008758,GO:0008478,GO:0016787,GO:0016787,GO:0016462,GO:0016787,0.1315,0.4114,0.4114,0.609,0.4114,5,0.3949,0.235,no
LPXH_PORGI,Q7MTZ8,ProtTale,Bacteria,262,"Hydrolyzes the pyrophosphate bond of UDP-2,3- diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.","Shows alpha-amylase and beta-amylase activity, i.e. catalyzes the cleavage of 1,4-alpha- and 1,4-beta-linkages in starch to produce glucose units.",No,No,No,No,No,not-Yes,GO:0046872; GO:0008758,GO:0004556,GO:0004556,GO:0004556,GO:0004556,GO:0004556,0.1944,0.1944,0.1944,0.1944,0.1944,5,0.1944,0.235,no
LPXH_PORGI,Q7MTZ8,Protein2Text,Bacteria,262,"Hydrolyzes the pyrophosphate bond of UDP-2,3- diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.","The molecular function of this protein is not explicitly stated in the provided text. However, based on the name ""Lipase"" and its classification as a protein, it is likely that this protein is involved in the hydrolysis of lipids, breaking them down into fatty acids and glycerol. Lipases are enzymes that catalyze the hydrolysis of triglycerides into free fatty acids and glycerol. They are involved in various biological processes, including fat digestion, metabolism, and storage.",Vague,No,No,No,No,not-Yes,GO:0046872; GO:0008758,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,0.2043,0.2043,0.2043,0.2043,0.2043,5,0.2043,0.235,no
LPXH_PORGI,Q7MTZ8,Reference,Bacteria,262,"Hydrolyzes the pyrophosphate bond of UDP-2,3- diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.","Hydrolyzes the pyrophosphate bond of UDP-2,3- diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.",,,,,,,GO:0046872; GO:0008758,GO:0008758,GO:0016787,GO:0016787,GO:0009029,GO:0008484,0.6924,0.4114,0.4114,0.1315,0.2683,5,0.383,0.235,no
WAAF_HAEDU,Q7VNA4,ESM2Text,Bacteria,348,Glycosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipooligosaccharide (LOS). Catalyzes the addition of a heptose unit to the heptosyl-Kdo2-lipid A module (Probable).,"Heptose transfer to the lipopolysaccharide core. It transfers the amidotransferase activity to the [4'-P]A479A gene, which in turn generates [4'-P]A479B.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008713,GO:0016757,,,,,0.729,,,,,1,0.729,0.3799,no
WAAF_HAEDU,Q7VNA4,Prot2Text,Bacteria,348,Glycosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipooligosaccharide (LOS). Catalyzes the addition of a heptose unit to the heptosyl-Kdo2-lipid A module (Probable).,Heptose transfer to the lipopolysaccharide core. It transfers the innermost heptose to [4'-P](3-deoxy-D-manno-octulosonic acid)2-IVA.,Maybe,Maybe,Maybe,Yes,Maybe,not-Yes,GO:0008713,GO:0016757,GO:0016757,GO:0008920,GO:0016757,GO:0008920,0.729,0.729,0.8582,0.729,0.8582,5,0.7807,0.3799,no
WAAF_HAEDU,Q7VNA4,ProtT3,Bacteria,348,Glycosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipooligosaccharide (LOS). Catalyzes the addition of a heptose unit to the heptosyl-Kdo2-lipid A module (Probable).,Belongs to the glycosyltransferase 2 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008713,GO:0016757,GO:0016757,,GO:0016757,GO:0016757,0.729,0.729,,0.729,0.729,4,0.729,0.3799,no
WAAF_HAEDU,Q7VNA4,ProtTale,Bacteria,348,Glycosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipooligosaccharide (LOS). Catalyzes the addition of a heptose unit to the heptosyl-Kdo2-lipid A module (Probable).,Glycosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS). Catalyzes the addition of the second heptose unit to the third-to-sixth heptose unit ring.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008713,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.729,0.729,0.729,0.729,0.729,5,0.729,0.3799,no
WAAF_HAEDU,Q7VNA4,Protein2Text,Bacteria,348,Glycosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipooligosaccharide (LOS). Catalyzes the addition of a heptose unit to the heptosyl-Kdo2-lipid A module (Probable).,"This protein is involved in the biosynthesis of lipopolysaccharides (LPS). More specifically, it is an enzyme that catalyzes the transfer of a phosphate group from a nucleotide donor to the lipid A core of LPS. This reaction is part of the lipid A modification pathway, which is important for the structure and function of LPS. The molecular function of this protein is therefore to catalyze the transfer of a phosphate group from a nucleotide donor to the lipid A core of LPS. 

The specific reaction catalyzed by this protein is:

CDP-3-O-(3-hydroxytetradecanoyl)-D-erythro-sphing-4-enine + 2- deoxy-D-ribose 1-phosphate = CDP-3-O-(3-hydroxytetradecanoyl)-D- erythro-sphing-4-enine 2-deoxy-D-ribose 1-phosphate + CMP.

This reaction is part of the LPS biosynthesis pathway, which is essential for the structure and function of LPS. The LPS biosynthesis pathway is important for the virulence and pathogenicity of bacteria, and is a target for the development of antibacterial agents. 

The molecular function of this protein is therefore to catalyze the transfer of a phosphate group from a nucleotide donor to the lipid A core of LPS, and is essential for the structure and function of LPS. 

This protein is a part of the Kdo lipid A core biosynthesis pathway, which is a crucial step in the biosynthesis of lipid A, the toxic component of LPS. The Kdo lipid A core biosynthesis pathway is essential for the structure and function of LPS, and is a target for the development of antibacterial agents. 

The molecular function of this protein is therefore to catalyze the transfer of a phosphate group from a nucleotide donor to the lipid A core of LPS, and is essential for the structure and function of LPS. 

This protein is also involved in the biosynthesis of LPS. More specifically, it is an enzyme that catalyzes the transfer of a phosphate group from a nucleotide donor to the lipid A core of LPS. This reaction is part of the lipid A modification pathway, which is important for the structure and function of LPS. 

The specific reaction catalyzed by this protein is:

CDP-3-O-(3-hydroxytetradecanoy",No,No,Maybe,No,No,not-Yes,GO:0008713,,,,,GO:0016740,,,,,0.6019,1,0.6019,0.3799,no
WAAF_HAEDU,Q7VNA4,Reference,Bacteria,348,Glycosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipooligosaccharide (LOS). Catalyzes the addition of a heptose unit to the heptosyl-Kdo2-lipid A module (Probable).,Glycosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipooligosaccharide (LOS). Catalyzes the addition of a heptose unit to the heptosyl-Kdo2-lipid A module (Probable).,,,,,,,GO:0008713,GO:0008920,GO:0008920,GO:0016757,GO:0016757,GO:0016757,0.8582,0.8582,0.729,0.729,0.729,5,0.7807,0.3799,no
TPDA_VIBPA,Q87NI7,ESM2Text,Bacteria,571,"Cyclic di-GMP phosphodiesterase that plays an important role in modulating the global c-di-GMP pool. Its ability to alter the c-di-GMP pool has an effect on swimming motility, swarming motility and biofilm formation, multicellular behaviors that are important for the survival and dissemination of this environmental pathogen. Exhibits a dual function, namely, c-di-GMP degradation and modulation of its own expression.",Probable cyclic nucleotide-dependent phosphatase.,Vague,Vague,Maybe,Maybe,Maybe,not-Yes,GO:0071111,GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,0.6335,0.6335,0.6335,0.6335,0.6335,5,0.6335,0.4045,no
TPDA_VIBPA,Q87NI7,Prot2Text,Bacteria,571,"Cyclic di-GMP phosphodiesterase that plays an important role in modulating the global c-di-GMP pool. Its ability to alter the c-di-GMP pool has an effect on swimming motility, swarming motility and biofilm formation, multicellular behaviors that are important for the survival and dissemination of this environmental pathogen. Exhibits a dual function, namely, c-di-GMP degradation and modulation of its own expression.",Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to pGpG.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0071111,GO:0071111,GO:0004112,GO:0004112,GO:0004112,GO:0004112,1.0,0.7469,0.7469,0.7469,0.7469,5,0.7975,0.4045,no
TPDA_VIBPA,Q87NI7,ProtT3,Bacteria,571,"Cyclic di-GMP phosphodiesterase that plays an important role in modulating the global c-di-GMP pool. Its ability to alter the c-di-GMP pool has an effect on swimming motility, swarming motility and biofilm formation, multicellular behaviors that are important for the survival and dissemination of this environmental pathogen. Exhibits a dual function, namely, c-di-GMP degradation and modulation of its own expression.",Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG. Cell inner membrane; Multi-pass membrane protein,Yes,Yes,Maybe,Yes,Yes,Yes,GO:0071111,GO:0004112,GO:0004112,GO:0016787,GO:0004112,GO:0004112,0.7469,0.7469,0.5381,0.7469,0.7469,5,0.7051,0.4045,no
TPDA_VIBPA,Q87NI7,ProtTale,Bacteria,571,"Cyclic di-GMP phosphodiesterase that plays an important role in modulating the global c-di-GMP pool. Its ability to alter the c-di-GMP pool has an effect on swimming motility, swarming motility and biofilm formation, multicellular behaviors that are important for the survival and dissemination of this environmental pathogen. Exhibits a dual function, namely, c-di-GMP degradation and modulation of its own expression.","Phosphorylates the glucose moiety of the phosphoenolpyruvate-D-glucose 4,6-dehydratase to D-xylulose 5-phosphate.",No,No,No,No,No,not-Yes,GO:0071111,,GO:0016301,GO:0016301,GO:0016301,GO:0016301,,0.2067,0.2067,0.2067,0.2067,4,0.2067,0.4045,no
TPDA_VIBPA,Q87NI7,Protein2Text,Bacteria,571,"Cyclic di-GMP phosphodiesterase that plays an important role in modulating the global c-di-GMP pool. Its ability to alter the c-di-GMP pool has an effect on swimming motility, swarming motility and biofilm formation, multicellular behaviors that are important for the survival and dissemination of this environmental pathogen. Exhibits a dual function, namely, c-di-GMP degradation and modulation of its own expression.","The molecular function of this protein is not specified in the given text. However, based on its name and the context, it can be inferred that this protein is involved in a process related to bacterial cell regulation or signaling. Specifically, it is likely involved in a two-component regulatory system, where it acts as a sensor protein kinase that phosphorylates a response regulator protein. However, without more specific information, it is difficult to determine its exact molecular function.",Vague,Vague,No,Vague,Vague,not-Yes,GO:0071111,,GO:0004672,GO:0000155,GO:0000155,GO:0000155,,0.1804,0.1275,0.1275,0.1275,4,0.1407,0.4045,no
TPDA_VIBPA,Q87NI7,Reference,Bacteria,571,"Cyclic di-GMP phosphodiesterase that plays an important role in modulating the global c-di-GMP pool. Its ability to alter the c-di-GMP pool has an effect on swimming motility, swarming motility and biofilm formation, multicellular behaviors that are important for the survival and dissemination of this environmental pathogen. Exhibits a dual function, namely, c-di-GMP degradation and modulation of its own expression.","Cyclic di-GMP phosphodiesterase that plays an important role in modulating the global c-di-GMP pool. Its ability to alter the c-di-GMP pool has an effect on swimming motility, swarming motility and biofilm formation, multicellular behaviors that are important for the survival and dissemination of this environmental pathogen. Exhibits a dual function, namely, c-di-GMP degradation and modulation of its own expression.",,,,,,,GO:0071111,GO:0071584,GO:0016788,GO:0016788,GO:0004112,GO:0004112,0.0,0.6466,0.6466,0.7469,0.7469,5,0.5574,0.4045,no
DAO_BRADU,Q89F89,ESM2Text,Bacteria,421,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.,Oxidative deamination of D-amino acids.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003884; GO:0071949,GO:0003884,GO:0003884,GO:0003884,GO:0003884,GO:0003884,0.6869,0.6869,0.6869,0.6869,0.6869,5,0.6869,0.1529,no
DAO_BRADU,Q89F89,Prot2Text,Bacteria,421,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.,Oxidative deamination of D-amino acids.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003884; GO:0071949,GO:0003884,GO:0003884,GO:0003884,GO:0003884,GO:0003884,0.6869,0.6869,0.6869,0.6869,0.6869,5,0.6869,0.1529,no
DAO_BRADU,Q89F89,ProtT3,Bacteria,421,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.,Catalyzes the oxidative deamination of D-amino acids. Periplasm. Belongs to the DadA oxidoreductase family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003884; GO:0071949,GO:0003863,GO:0003884,GO:0003862,GO:0003862,GO:0016641,0.2193,0.6869,0.2193,0.2193,0.5295,5,0.3749,0.1529,no
DAO_BRADU,Q89F89,ProtTale,Bacteria,421,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.,Oxidative deamination of D-amino acids.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003884; GO:0071949,GO:0003884,GO:0003884,GO:0003884,GO:0003884,GO:0003884,0.6869,0.6869,0.6869,0.6869,0.6869,5,0.6869,0.1529,no
DAO_BRADU,Q89F89,Protein2Text,Bacteria,421,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.,"The molecular function of this protein is an oxidoreductase activity, specifically a catalytic activity involved in the oxidation of a chemical group. More specifically, this protein is involved in the oxidation of a chemical group in a molecule, which is a key process in many biochemical reactions.",Vague,Vague,Maybe,Vague,Vague,not-Yes,GO:0003884; GO:0071949,GO:0016491,GO:0016491,GO:0016491,,GO:0016491,0.3981,0.3981,0.3981,,0.3981,4,0.3981,0.1529,no
DAO_BRADU,Q89F89,Reference,Bacteria,421,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.,Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity.,,,,,,,GO:0003884; GO:0071949,GO:0003884,GO:0003884,GO:0033738,GO:0003884,GO:0003884,0.6869,0.6869,0.2193,0.6869,0.6869,5,0.5934,0.1529,no
KDSAH_BACTN,Q8A5T1,ESM2Text,Bacteria,290,"3-keto-disaccharide hydrolase that preferentially hydrolyzes 3-keto-trehalose (3-dehydro-alpha,alpha-trehalose). Important for disaccharide utilization in the human gut. Also shows hydrolysis activity with the glucosinolates glucoraphanin or glucobrassicin, but with much lower efficiency.","Involved in the detoxification of xenobiotics, especially polychlorinated aluminum.",No,No,No,No,No,not-Yes,GO:0016798,,,,,,,,,,,0,,0.3041,no
KDSAH_BACTN,Q8A5T1,Prot2Text,Bacteria,290,"3-keto-disaccharide hydrolase that preferentially hydrolyzes 3-keto-trehalose (3-dehydro-alpha,alpha-trehalose). Important for disaccharide utilization in the human gut. Also shows hydrolysis activity with the glucosinolates glucoraphanin or glucobrassicin, but with much lower efficiency.","Cleaves the beta-1,4-linkages between beta-D-galactose and alpha-L-3,6-anhydro-galactose residues in agarose. Cleaves agarose in a random manner with retention of the anomeric-bond configuration, producing beta-anomers that give rise progressively to alpha-anomers when mutarotation takes place.",No,No,No,No,No,not-Yes,GO:0016798,GO:0016798,GO:0016798,GO:0016798,GO:0004553,GO:0016798,1.0,1.0,1.0,0.8416,1.0,5,0.9683,0.3041,no
KDSAH_BACTN,Q8A5T1,ProtT3,Bacteria,290,"3-keto-disaccharide hydrolase that preferentially hydrolyzes 3-keto-trehalose (3-dehydro-alpha,alpha-trehalose). Important for disaccharide utilization in the human gut. Also shows hydrolysis activity with the glucosinolates glucoraphanin or glucobrassicin, but with much lower efficiency.","Involved in the degradation of alginate. Catalyzes the hydrolysis of the beta-1,4 glycosidic bond of the non-reducing end beta-D-mannopyranosyl-(1->4)-beta-D-mannopyranosyl-(1->4)-beta-D- mannopyranosyl-(1->4)-beta-D-mannopyranosyl-(1->4)-beta-D-mannopyranosyl-(1->4)-beta-D-mannopyranosyl-(1->4)-beta-D-mannopyran",No,No,No,No,No,not-Yes,GO:0016798,GO:0004553,GO:0004553,GO:0004553,GO:0004553,GO:0016798,0.8416,0.8416,0.8416,0.8416,1.0,5,0.8733,0.3041,no
KDSAH_BACTN,Q8A5T1,ProtTale,Bacteria,290,"3-keto-disaccharide hydrolase that preferentially hydrolyzes 3-keto-trehalose (3-dehydro-alpha,alpha-trehalose). Important for disaccharide utilization in the human gut. Also shows hydrolysis activity with the glucosinolates glucoraphanin or glucobrassicin, but with much lower efficiency.",Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan. Catalyzes the cleavage of alpha-L-arabinofuranose (L-Araf) residues from the non-reducing end of arabinoxylan. Is also able to release L-Araf from the reducing end of L-Araf-containing arabinoxylan.,No,No,No,No,No,not-Yes,GO:0016798,GO:0046556,GO:0046556,GO:0046556,GO:0046556,GO:0046556,0.729,0.729,0.729,0.729,0.729,5,0.729,0.3041,no
KDSAH_BACTN,Q8A5T1,Protein2Text,Bacteria,290,"3-keto-disaccharide hydrolase that preferentially hydrolyzes 3-keto-trehalose (3-dehydro-alpha,alpha-trehalose). Important for disaccharide utilization in the human gut. Also shows hydrolysis activity with the glucosinolates glucoraphanin or glucobrassicin, but with much lower efficiency.","This protein is involved in catalyzing the dehydrogenation of glucose-6-phosphate to 5-keto-6-deoxy-D-glucose-1-phosphate in the L-arabinose metabolic pathway. It is an aldose dehydrogenase that catalyzes the oxidation of glucose-6-phosphate to 5-keto-6-deoxy-D-glucose-1-phosphate. The aldose reductase/NADPH-dependent oxidoreductase family is a large family of enzymes that catalyze a wide variety of oxidoreductase reactions. They are often involved in the detoxification of aldehydes, or in the catabolism of sugars. The aldose reductases are NADPH-dependent reductases, while the ketose reductases are NADH-dependent oxidases. The oxidoreductase is the only enzyme that has been described in this organism. The protein is likely to be involved in the L-arabinose metabolic pathway. The L-arabinose pathway is a major route of carbon assimilation in many fungi and is of considerable economic importance in the brewing, distilling, and paper industries. It is also a model system for the study of glycolytic and gluconeogenic pathways. The aldose reductase/NADPH-dependent oxidoreductase family is a large family of enzymes that catalyze a wide variety of oxidoreductase reactions. They are often involved in the detoxification of aldehydes, or in the catabolism of sugars. The aldose reductases are NADPH-dependent reductases, while the ketose reductases are NADH-dependent oxidases. The oxidoreductase is the only enzyme that has been described in this organism. The protein is likely to be involved in the L-arabinose metabolic pathway. The L-arabinose pathway is a major route of carbon assimilation in many fungi and is of considerable economic importance in the brewing, distilling, and paper industries. It is also a model system for the study of glycolytic and gluconeogenic pathways. 
            Aldose reductase; KEGG ortholog (K03422)",No,No,No,No,No,not-Yes,GO:0016798,GO:0016491,GO:0016491,GO:0004032,GO:0004032,GO:0004032,0.4807,0.4807,0.2283,0.2283,0.2283,5,0.3293,0.3041,no
KDSAH_BACTN,Q8A5T1,Reference,Bacteria,290,"3-keto-disaccharide hydrolase that preferentially hydrolyzes 3-keto-trehalose (3-dehydro-alpha,alpha-trehalose). Important for disaccharide utilization in the human gut. Also shows hydrolysis activity with the glucosinolates glucoraphanin or glucobrassicin, but with much lower efficiency.","3-keto-disaccharide hydrolase that preferentially hydrolyzes 3-keto-trehalose (3-dehydro-alpha,alpha-trehalose). Important for disaccharide utilization in the human gut. Also shows hydrolysis activity with the glucosinolates glucoraphanin or glucobrassicin, but with much lower efficiency.",,,,,,,GO:0016798,GO:0016787,GO:0016787,GO:0016798,GO:0016798,GO:0016798,0.8145,0.8145,1.0,1.0,1.0,5,0.9258,0.3041,no
BGLR_STRA5,Q8E0N2,ESM2Text,Bacteria,599,"Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG). Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sources of carbon. As part of the GI microbiome, this enzyme would be able to reactivate glucuronide drug conjugates, such reactivated compounds can significantly damage the GI tract.","Involved in the degradation of plant cell wall polysaccharides. Degrades acetate and raffinose to produce beta-1,6-glucan and alpha-1,3-glucan.",No,No,No,No,No,not-Yes,GO:0004566; GO:0030246,,,,,,,,,,,0,,0.2347,no
BGLR_STRA5,Q8E0N2,Prot2Text,Bacteria,599,"Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG). Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sources of carbon. As part of the GI microbiome, this enzyme would be able to reactivate glucuronide drug conjugates, such reactivated compounds can significantly damage the GI tract.",Plays an important role in the degradation of dermatan and keratan sulfates.,No,No,No,No,No,not-Yes,GO:0004566; GO:0030246,,,,,,,,,,,0,,0.2347,no
BGLR_STRA5,Q8E0N2,ProtT3,Bacteria,599,"Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG). Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sources of carbon. As part of the GI microbiome, this enzyme would be able to reactivate glucuronide drug conjugates, such reactivated compounds can significantly damage the GI tract.",Belongs to the glycosyl hydrolase 2 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004566; GO:0030246,GO:0004565,GO:0004553,,GO:0004553,GO:0016798,0.41,0.5629,,0.5629,0.5023,4,0.5095,0.2347,no
BGLR_STRA5,Q8E0N2,ProtTale,Bacteria,599,"Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG). Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sources of carbon. As part of the GI microbiome, this enzyme would be able to reactivate glucuronide drug conjugates, such reactivated compounds can significantly damage the GI tract.","Component of a beta-galactosidase. Acts on galacto-beta-(1->3)-galacto-beta-(1->6)-galacto-beta-(1->4)-D-galactose (lacto-triose), galacto-beta-(1->4)-galacto-beta-(1->6)-galacto-beta-(1->4)-D-galactose (lacto-tetraose) and galacto-beta-(1->6)-galacto-beta-(1",No,No,No,No,No,not-Yes,GO:0004566; GO:0030246,GO:0004565,GO:0004565,GO:0004565,GO:0004565,GO:0004565,0.41,0.41,0.41,0.41,0.41,5,0.41,0.2347,no
BGLR_STRA5,Q8E0N2,Protein2Text,Bacteria,599,"Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG). Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sources of carbon. As part of the GI microbiome, this enzyme would be able to reactivate glucuronide drug conjugates, such reactivated compounds can significantly damage the GI tract.","This protein is a beta-glucosidase, which means it catalyzes the hydrolysis of beta-glucosides into glucose and other sugars. Specifically, it is involved in the degradation of complex carbohydrates, breaking down beta-glucosidic bonds to release glucose or other simple sugars.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004566; GO:0030246,GO:0008422,GO:0008422,GO:0008422,GO:0008422,GO:0008422,0.41,0.41,0.41,0.41,0.41,5,0.41,0.2347,no
BGLR_STRA5,Q8E0N2,Reference,Bacteria,599,"Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG). Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sources of carbon. As part of the GI microbiome, this enzyme would be able to reactivate glucuronide drug conjugates, such reactivated compounds can significantly damage the GI tract.","Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG). Is likely capable of scavenging glucuronate from a range of chemically distinct xenobiotic and endobiotic glucuronides present in the gastrointestinal (GI) tract, to be able to utilize these diverse sources of carbon. As part of the GI microbiome, this enzyme would be able to reactivate glucuronide drug conjugates, such reactivated compounds can significantly damage the GI tract.",,,,,,,GO:0004566; GO:0030246,GO:0004566,GO:0004566,GO:0004566,GO:0004566,GO:0004566,0.7137,0.7137,0.7137,0.7137,0.7137,5,0.7137,0.2347,no
CAN4_CAEEL,Q8IAA9,ESM2Text,Eukaryota,716,Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates. Promotes starvation-induced muscle atrophy.,Calcium-regulated non-lysosomal thiol-protease.,Yes,Yes,Maybe,Yes,Yes,Yes,GO:0004198,GO:0008234; GO:0005509,GO:0004198,GO:0004198; GO:0005509,GO:0004198; GO:0005509,GO:0004198,0.5055,1.0,0.6862,0.6862,1.0,5,0.7756,0.4653,no
CAN4_CAEEL,Q8IAA9,Prot2Text,Eukaryota,716,Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates. Promotes starvation-induced muscle atrophy.,Probable thiol-disulfide oxidoreductase that may be involved in the redox regulation of a number of cytosolic enzymes.,No,No,No,No,No,not-Yes,GO:0004198,GO:0015035,GO:0015035,GO:0015036,GO:0015036,GO:0015035,0.298,0.298,0.1807,0.1807,0.298,5,0.2511,0.4653,no
CAN4_CAEEL,Q8IAA9,ProtT3,Eukaryota,716,Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates. Promotes starvation-induced muscle atrophy.,Calcium-regulated non-lysosomal thiol-protease. Belongs to the peptidase C2 family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004198,GO:0004198; GO:0005509,GO:0004198,GO:0004198,GO:0004198; GO:0005509,GO:0004198,0.6862,1.0,1.0,0.6862,1.0,5,0.8745,0.4653,no
CAN4_CAEEL,Q8IAA9,ProtTale,Eukaryota,716,Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates. Promotes starvation-induced muscle atrophy.,Required for the proteolytic cleavage of the transcriptional repressors RIM101 and RIM101C at multiple sites.,Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0004198,,,,GO:0008233,GO:0008233,,,,0.6481,0.6481,2,0.6481,0.4653,no
CAN4_CAEEL,Q8IAA9,Protein2Text,Eukaryota,716,Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates. Promotes starvation-induced muscle atrophy.,"The molecular function of this protein is not explicitly stated in the provided snippet. However, it is likely that this protein is involved in a calcium-dependent proteolytic activity, given its classification as a calpain. Calpains are a family of calcium-dependent proteases that play important roles in various cellular processes, including cell signaling, cell adhesion, and cell migration. They typically act by cleaving specific substrates at specific sites, leading to changes in the protein's activity or function. The specific substrates and sites targeted by this protein are not specified in the provided information.",Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004198,GO:0004198,GO:0004198,GO:0004198,GO:0004198,GO:0004198,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4653,no
CAN4_CAEEL,Q8IAA9,Reference,Eukaryota,716,Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates. Promotes starvation-induced muscle atrophy.,Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates. Promotes starvation-induced muscle atrophy.,,,,,,,GO:0004198,GO:0004198,GO:0004198; GO:0005509,GO:0004198; GO:0005509,GO:0004198,GO:0004198,1.0,0.6862,0.6862,1.0,1.0,5,0.8745,0.4653,no
AMPD_METMA,Q8PWQ0,ESM2Text,Archaea,422,"Catalyzes the conversion of trans-anhydromevalonate 5- phosphate (tAHMP) into isopentenyl phosphate (Probable). Involved in the archaeal mevalonate (MVA) pathway, which provides fundamental precursors for isoprenoid biosynthesis, such as isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP).","Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.",No,No,No,No,No,not-Yes,GO:0016831; GO:0046872,GO:0008964,GO:0008964,GO:0008964,GO:0004612,GO:0008964,0.5283,0.5283,0.5283,0.5283,0.5283,5,0.5283,0.5281,no
AMPD_METMA,Q8PWQ0,Prot2Text,Archaea,422,"Catalyzes the conversion of trans-anhydromevalonate 5- phosphate (tAHMP) into isopentenyl phosphate (Probable). Involved in the archaeal mevalonate (MVA) pathway, which provides fundamental precursors for isoprenoid biosynthesis, such as isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP).",Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.,No,No,No,No,No,not-Yes,GO:0016831; GO:0046872,GO:0016877,GO:0016405,GO:0016877,GO:0016878,GO:0016878,0.2611,0.2176,0.2611,0.2176,0.2176,5,0.235,0.5281,no
AMPD_METMA,Q8PWQ0,ProtT3,Archaea,422,"Catalyzes the conversion of trans-anhydromevalonate 5- phosphate (tAHMP) into isopentenyl phosphate (Probable). Involved in the archaeal mevalonate (MVA) pathway, which provides fundamental precursors for isoprenoid biosynthesis, such as isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP).",Belongs to the UbiD family,Vague,Vague,No,Vague,Vague,not-Yes,GO:0016831; GO:0046872,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.7015,0.7015,0.7015,0.7015,0.7015,5,0.7015,0.5281,no
AMPD_METMA,Q8PWQ0,ProtTale,Archaea,422,"Catalyzes the conversion of trans-anhydromevalonate 5- phosphate (tAHMP) into isopentenyl phosphate (Probable). Involved in the archaeal mevalonate (MVA) pathway, which provides fundamental precursors for isoprenoid biosynthesis, such as isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP).","PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a prolyl 3-hydroxylase that catalyzes the hydroxylation of L-prolyl-[prolyl]-L-isoleucine (Ppi-Ile), L-prolyl-[prolyl]-L-valine (Ppi-Val) and L-prolyl-[prolyl]-L-phenylalanine (Ppi-Phe).",No,No,No,No,No,not-Yes,GO:0016831; GO:0046872,GO:0003755; GO:0031543,GO:0003755; GO:0031543,GO:0003755; GO:0016706,GO:0003755; GO:0016491,GO:0003755; GO:0016705,0.2179,0.2179,0.2209,0.3099,0.2627,5,0.2459,0.5281,no
AMPD_METMA,Q8PWQ0,Protein2Text,Archaea,422,"Catalyzes the conversion of trans-anhydromevalonate 5- phosphate (tAHMP) into isopentenyl phosphate (Probable). Involved in the archaeal mevalonate (MVA) pathway, which provides fundamental precursors for isoprenoid biosynthesis, such as isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP).","The molecular function of this protein is an oxidoreductase, specifically a lactamase.",No,No,No,No,No,not-Yes,GO:0016831; GO:0046872,,,,,GO:0008800,,,,,0.1865,1,0.1865,0.5281,no
AMPD_METMA,Q8PWQ0,Reference,Archaea,422,"Catalyzes the conversion of trans-anhydromevalonate 5- phosphate (tAHMP) into isopentenyl phosphate (Probable). Involved in the archaeal mevalonate (MVA) pathway, which provides fundamental precursors for isoprenoid biosynthesis, such as isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP).","Catalyzes the conversion of trans-anhydromevalonate 5- phosphate (tAHMP) into isopentenyl phosphate (Probable). Involved in the archaeal mevalonate (MVA) pathway, which provides fundamental precursors for isoprenoid biosynthesis, such as isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP).",,,,,,,GO:0016831; GO:0046872,GO:0016829,GO:0016829,GO:0016829,GO:0016831,GO:0016829,0.5125,0.5125,0.5125,0.7015,0.5125,5,0.5503,0.5281,no
WBGN_ECOLX,Q8VQ46,ESM2Text,Bacteria,290,"Involved in the biosynthesis of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of colitose from GDP-colitose to the galactose residue of beta-Gal-(1->3)-GlcNAc (lacto-N-biose) via an alpha1,2-linkage. Is specific for beta-Gal-(1->3)-GlcNAc, but can use GDP-L-fucose as the sugar donor with almost the same efficiency as GDP-L-colitose.",Involved in the assembly of the O-repeating unit during O-antigen biosynthesis.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008107,,,,,,,,,,,0,,0.2035,no
WBGN_ECOLX,Q8VQ46,Prot2Text,Bacteria,290,"Involved in the biosynthesis of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of colitose from GDP-colitose to the galactose residue of beta-Gal-(1->3)-GlcNAc (lacto-N-biose) via an alpha1,2-linkage. Is specific for beta-Gal-(1->3)-GlcNAc, but can use GDP-L-fucose as the sugar donor with almost the same efficiency as GDP-L-colitose.",Galactosyltransferase involved in nodule organogenesis. Transfers galactose from UDP-galactose to a Ser or Thr residue on the surface of the nodule.,No,No,Maybe,Maybe,Maybe,not-Yes,GO:0008107,GO:0016757,GO:0008378,GO:0008378,GO:0008378,GO:0008378,0.585,0.5618,0.5618,0.5618,0.5618,5,0.5664,0.2035,no
WBGN_ECOLX,Q8VQ46,ProtT3,Bacteria,290,"Involved in the biosynthesis of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of colitose from GDP-colitose to the galactose residue of beta-Gal-(1->3)-GlcNAc (lacto-N-biose) via an alpha1,2-linkage. Is specific for beta-Gal-(1->3)-GlcNAc, but can use GDP-L-fucose as the sugar donor with almost the same efficiency as GDP-L-colitose.",Belongs to the glycosyltransferase 8 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008107,GO:0016757,GO:0016757,,GO:0016757,GO:0016757,0.585,0.585,,0.585,0.585,4,0.585,0.2035,no
WBGN_ECOLX,Q8VQ46,ProtTale,Bacteria,290,"Involved in the biosynthesis of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of colitose from GDP-colitose to the galactose residue of beta-Gal-(1->3)-GlcNAc (lacto-N-biose) via an alpha1,2-linkage. Is specific for beta-Gal-(1->3)-GlcNAc, but can use GDP-L-fucose as the sugar donor with almost the same efficiency as GDP-L-colitose.","Involved in the biosynthesis of 3-deoxy-D-manno-octulosonate (Kdo). Catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to the 3-keto-group of 2-keto-3-deoxy-D-gluconate, yielding 2,3-diketo-2-deoxy-D-gluconate (Kdo).",No,No,No,No,No,not-Yes,GO:0008107,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.3139,0.3139,0.3139,0.3139,0.3139,5,0.3139,0.2035,no
WBGN_ECOLX,Q8VQ46,Protein2Text,Bacteria,290,"Involved in the biosynthesis of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of colitose from GDP-colitose to the galactose residue of beta-Gal-(1->3)-GlcNAc (lacto-N-biose) via an alpha1,2-linkage. Is specific for beta-Gal-(1->3)-GlcNAc, but can use GDP-L-fucose as the sugar donor with almost the same efficiency as GDP-L-colitose.","The molecular function of this protein is not explicitly stated in the provided text. However, based on the context, it can be inferred that this protein is involved in the synthesis of a molecule, possibly a sugar or a carbohydrate derivative, as it is mentioned in relation to the biosynthesis of a specific molecule. 

In general, proteins involved in the synthesis of molecules often have molecular functions related to catalysis, such as transferase, lyase, or synthase activity. However, without more specific information, it is difficult to determine the exact molecular function of this protein.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0008107,,,,,,,,,,,0,,0.2035,no
WBGN_ECOLX,Q8VQ46,Reference,Bacteria,290,"Involved in the biosynthesis of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of colitose from GDP-colitose to the galactose residue of beta-Gal-(1->3)-GlcNAc (lacto-N-biose) via an alpha1,2-linkage. Is specific for beta-Gal-(1->3)-GlcNAc, but can use GDP-L-fucose as the sugar donor with almost the same efficiency as GDP-L-colitose.","Involved in the biosynthesis of the lipopolysaccharide (LPS) O-antigen region. Catalyzes the transfer of colitose from GDP-colitose to the galactose residue of beta-Gal-(1->3)-GlcNAc (lacto-N-biose) via an alpha1,2-linkage. Is specific for beta-Gal-(1->3)-GlcNAc, but can use GDP-L-fucose as the sugar donor with almost the same efficiency as GDP-L-colitose.",,,,,,,GO:0008107,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.585,0.585,0.585,0.585,0.585,5,0.585,0.2035,no
TAGK_KLEOX,Q8VS15,ESM2Text,Bacteria,304,"Kinase involved in a D-tagatose catabolic pathway. Catalyzes the phosphorylation of D-tagatose-1- phosphate (Tag-1P) to D-tagatose-1,6-bisphosphate.","Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008662; GO:0005524,GO:0008662; GO:0005524,GO:0016301,GO:0008662,GO:0008662,GO:0008662,1.0,0.4452,0.6819,0.6819,0.6819,5,0.6982,0.3785,no
TAGK_KLEOX,Q8VS15,Prot2Text,Bacteria,304,"Kinase involved in a D-tagatose catabolic pathway. Catalyzes the phosphorylation of D-tagatose-1- phosphate (Tag-1P) to D-tagatose-1,6-bisphosphate.","Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008662; GO:0005524,GO:0008662,GO:0008662,GO:0008662,GO:0008662,GO:0008662,0.6819,0.6819,0.6819,0.6819,0.6819,5,0.6819,0.3785,no
TAGK_KLEOX,Q8VS15,ProtT3,Bacteria,304,"Kinase involved in a D-tagatose catabolic pathway. Catalyzes the phosphorylation of D-tagatose-1- phosphate (Tag-1P) to D-tagatose-1,6-bisphosphate.","Catalyzes the ATP-dependent phosphorylation of fructose-l- phosphate to fructose-l,6-bisphosphate. Belongs to the carbohydrate kinase PfkB family",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008662; GO:0005524,GO:0008662; GO:0005524,GO:0008662,GO:0008662; GO:0005524,GO:0008662; GO:0005524,GO:0016301; GO:0005524,1.0,0.6819,1.0,1.0,0.8181,5,0.9,0.3785,no
TAGK_KLEOX,Q8VS15,ProtTale,Bacteria,304,"Kinase involved in a D-tagatose catabolic pathway. Catalyzes the phosphorylation of D-tagatose-1- phosphate (Tag-1P) to D-tagatose-1,6-bisphosphate.","Catalyzes the ATP-dependent phosphorylation of fructose-l- phosphate to fructose-l,6-bisphosphate.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008662; GO:0005524,GO:0008662,GO:0008662; GO:0005524,GO:0008662,GO:0008662; GO:0005524,GO:0016301; GO:0005524,0.6819,1.0,0.6819,1.0,0.8181,5,0.8364,0.3785,no
TAGK_KLEOX,Q8VS15,Protein2Text,Bacteria,304,"Kinase involved in a D-tagatose catabolic pathway. Catalyzes the phosphorylation of D-tagatose-1- phosphate (Tag-1P) to D-tagatose-1,6-bisphosphate.","The molecular function of this protein is likely to be a kinase, specifically a kinase that phosphorylates a substrate. The name ""phosphoenolpyruvate kinase"" suggests that it is involved in the phosphorylation of phosphoenolpyruvate (PEP), a key step in the glycolytic pathway.",Vague,Maybe,Maybe,No,No,not-Yes,GO:0008662; GO:0005524,GO:0004743,GO:0004743,GO:0004743,GO:0004743,GO:0004743,0.3855,0.3855,0.3855,0.3855,0.3855,5,0.3855,0.3785,no
TAGK_KLEOX,Q8VS15,Reference,Bacteria,304,"Kinase involved in a D-tagatose catabolic pathway. Catalyzes the phosphorylation of D-tagatose-1- phosphate (Tag-1P) to D-tagatose-1,6-bisphosphate.","Kinase involved in a D-tagatose catabolic pathway. Catalyzes the phosphorylation of D-tagatose-1- phosphate (Tag-1P) to D-tagatose-1,6-bisphosphate.",,,,,,,GO:0008662; GO:0005524,GO:0016301,GO:0016301; GO:0005524,GO:0016301; GO:0005524,GO:0016301,GO:0016301,0.4452,0.8181,0.8181,0.4452,0.4452,5,0.5944,0.3785,no
PALQ_ERWRD,Q9AI62,ESM2Text,Bacteria,551,"Catalyzes the hydrolysis of palatinose. Shows a strict specificity toward palatinose, and cannot release glucose from the disaccharides sucrose, maltose, trehalose and melibiose. Involved in the degradation of palatinose, a sucrose isomer that is formed as a reserve material under conditions of excess carbon availability, sequestered in a form unavailable to competitors such as fungi or the host plant, and whose consumption appears to be postponed until the preferentially metabolized carbon source (e.g. sucrose) is depleted.","Alpha-glucosidase with specificity for short oligosaccharides, such as maltose and palatinose.",Yes,Yes,Maybe,Maybe,Yes,Yes,GO:0004556,GO:0004558,GO:0004558,GO:0004558,GO:0004553,GO:0004558,0.4774,0.4774,0.4774,0.7539,0.4774,5,0.5327,0.1419,no
PALQ_ERWRD,Q9AI62,Prot2Text,Bacteria,551,"Catalyzes the hydrolysis of palatinose. Shows a strict specificity toward palatinose, and cannot release glucose from the disaccharides sucrose, maltose, trehalose and melibiose. Involved in the degradation of palatinose, a sucrose isomer that is formed as a reserve material under conditions of excess carbon availability, sequestered in a form unavailable to competitors such as fungi or the host plant, and whose consumption appears to be postponed until the preferentially metabolized carbon source (e.g. sucrose) is depleted.",The physiological substrates may be short isomaltosaccharides.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004556,,,,,,,,,,,0,,0.1419,no
PALQ_ERWRD,Q9AI62,ProtT3,Bacteria,551,"Catalyzes the hydrolysis of palatinose. Shows a strict specificity toward palatinose, and cannot release glucose from the disaccharides sucrose, maltose, trehalose and melibiose. Involved in the degradation of palatinose, a sucrose isomer that is formed as a reserve material under conditions of excess carbon availability, sequestered in a form unavailable to competitors such as fungi or the host plant, and whose consumption appears to be postponed until the preferentially metabolized carbon source (e.g. sucrose) is depleted.",Cytoplasm. Belongs to the glycosyl hydrolase 13 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004556,GO:0004553,GO:0004553,,GO:0004556,GO:0016798,0.7539,0.7539,,1.0,0.6466,4,0.7886,0.1419,no
PALQ_ERWRD,Q9AI62,ProtTale,Bacteria,551,"Catalyzes the hydrolysis of palatinose. Shows a strict specificity toward palatinose, and cannot release glucose from the disaccharides sucrose, maltose, trehalose and melibiose. Involved in the degradation of palatinose, a sucrose isomer that is formed as a reserve material under conditions of excess carbon availability, sequestered in a form unavailable to competitors such as fungi or the host plant, and whose consumption appears to be postponed until the preferentially metabolized carbon source (e.g. sucrose) is depleted.","Involved in the degradation of starch by hydrolyzing the alpha-1,4-glycosidic bond of terminal non-reducing alpha-D-glucosyl residues using ATP as a cosubstrate. The alpha-glucosidase is specific for maltose and to a lesser extent to maltotriose and maltoheptaose.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004556,GO:0004558,GO:0090599,GO:0004558,GO:0004558; GO:0005524,GO:0004558,0.4774,0.5445,0.4774,0.3348,0.4774,5,0.4623,0.1419,no
PALQ_ERWRD,Q9AI62,Protein2Text,Bacteria,551,"Catalyzes the hydrolysis of palatinose. Shows a strict specificity toward palatinose, and cannot release glucose from the disaccharides sucrose, maltose, trehalose and melibiose. Involved in the degradation of palatinose, a sucrose isomer that is formed as a reserve material under conditions of excess carbon availability, sequestered in a form unavailable to competitors such as fungi or the host plant, and whose consumption appears to be postponed until the preferentially metabolized carbon source (e.g. sucrose) is depleted.","The molecular function of this protein is a transferase enzyme, specifically a glucosidase that catalyzes the transfer of a glucose molecule from a glucose donor molecule to a glucose acceptor molecule, resulting in the hydrolysis of the glucose donor molecule.",No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004556,GO:0015926,,GO:0004553,,GO:0015926,0.6335,,0.7539,,0.6335,3,0.6736,0.1419,no
PALQ_ERWRD,Q9AI62,Reference,Bacteria,551,"Catalyzes the hydrolysis of palatinose. Shows a strict specificity toward palatinose, and cannot release glucose from the disaccharides sucrose, maltose, trehalose and melibiose. Involved in the degradation of palatinose, a sucrose isomer that is formed as a reserve material under conditions of excess carbon availability, sequestered in a form unavailable to competitors such as fungi or the host plant, and whose consumption appears to be postponed until the preferentially metabolized carbon source (e.g. sucrose) is depleted.","Catalyzes the hydrolysis of palatinose. Shows a strict specificity toward palatinose, and cannot release glucose from the disaccharides sucrose, maltose, trehalose and melibiose. Involved in the degradation of palatinose, a sucrose isomer that is formed as a reserve material under conditions of excess carbon availability, sequestered in a form unavailable to competitors such as fungi or the host plant, and whose consumption appears to be postponed until the preferentially metabolized carbon source (e.g. sucrose) is depleted.",,,,,,,GO:0004556,GO:0016798,GO:0016798,GO:0016798,GO:0016798,GO:0016798,0.6466,0.6466,0.6466,0.6466,0.6466,5,0.6466,0.1419,no
CHNC_ACISS,Q9F7D7,ESM2Text,Bacteria,300,Hydrolase involved in the degradation of cyclohexanol to adipate. Catalyzes the conversion of hexano-6-lactone (epsilon-caprolactone) to 6-hydroxyhexanoate (Probable).,Displays esterase activity towards p-nitrophenyl esters with varying acyl chain length.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787,GO:0004091,GO:0004091,GO:0004091,GO:0004091,GO:0004091,0.6897,0.6897,0.6897,0.6897,0.6897,5,0.6897,0.2885,no
CHNC_ACISS,Q9F7D7,Prot2Text,Bacteria,300,Hydrolase involved in the degradation of cyclohexanol to adipate. Catalyzes the conversion of hexano-6-lactone (epsilon-caprolactone) to 6-hydroxyhexanoate (Probable).,Ring cleavage of cyclic ester dienelactone to produce maleylacetate.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787,GO:0016787,GO:0018783,GO:0018775,GO:0018775,GO:0018775,1.0,0.0,0.6019,0.6019,0.6019,5,0.5611,0.2885,no
CHNC_ACISS,Q9F7D7,ProtT3,Bacteria,300,Hydrolase involved in the degradation of cyclohexanol to adipate. Catalyzes the conversion of hexano-6-lactone (epsilon-caprolactone) to 6-hydroxyhexanoate (Probable).,"Esterase with broad substrate specificity. Hydrolyzes a broad range of esters, with a preference for short-chain aliphatic esters (C4-C10). Hydrolyzes p-nitrophenyl acetate (pNPA), p-nitrophenyl butyrate (pNPB), p-nitrophenyl hexanoate (pNPH), p-nitrophenyl octanoate (pNPO), p-nitrophenyl decanoate (pNPD), p-nitrophenyl laurate (pNPL), p-nitrophenyl myristate (pNPM), p-nitrophenyl",Maybe,Maybe,Vague,Maybe,Maybe,not-Yes,GO:0016787,GO:0004091,GO:0052689,GO:0052689,GO:0052689,GO:0004091,0.6897,0.6897,0.6897,0.6897,0.6897,5,0.6897,0.2885,no
CHNC_ACISS,Q9F7D7,ProtTale,Bacteria,300,Hydrolase involved in the degradation of cyclohexanol to adipate. Catalyzes the conversion of hexano-6-lactone (epsilon-caprolactone) to 6-hydroxyhexanoate (Probable).,"Acyltransferase; part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant. Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to",No,No,No,No,No,not-Yes,GO:0016787,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016747,0.4807,0.4807,0.4807,0.4807,0.4071,5,0.466,0.2885,no
CHNC_ACISS,Q9F7D7,Protein2Text,Bacteria,300,Hydrolase involved in the degradation of cyclohexanol to adipate. Catalyzes the conversion of hexano-6-lactone (epsilon-caprolactone) to 6-hydroxyhexanoate (Probable).,The molecular function of this protein is as a dehydrogenase.,No,No,No,No,No,not-Yes,GO:0016787,GO:0016491,GO:0016491,,,GO:0016491,0.5902,0.5902,,,0.5902,3,0.5902,0.2885,no
CHNC_ACISS,Q9F7D7,Reference,Bacteria,300,Hydrolase involved in the degradation of cyclohexanol to adipate. Catalyzes the conversion of hexano-6-lactone (epsilon-caprolactone) to 6-hydroxyhexanoate (Probable).,Hydrolase involved in the degradation of cyclohexanol to adipate. Catalyzes the conversion of hexano-6-lactone (epsilon-caprolactone) to 6-hydroxyhexanoate (Probable).,,,,,,,GO:0016787,GO:0016787,GO:0016787,GO:0016788,GO:0016788,GO:0016788,1.0,1.0,0.8145,0.8145,0.8145,5,0.8887,0.2885,no
CHND_ACISS,Q9F7D8,ESM2Text,Bacteria,352,Dehydrogenase involved in the degradation of cyclohexanol to adipate. Catalyzes the conversion of 6- hydroxyhexanoate to 6-oxohexanoate.,Involved in the degradation of lignin through the Entner-Doudoroff pathway. Catalyzes the oxidative deamination of L-arabinose and L-xylulose to 3-keto-3-deoxy-L-arabino-heptanoate (KDA). It can also use D-galactose and D-mannitol as substrates.,No,No,Maybe,Maybe,No,not-Yes,GO:0004022; GO:0046872,,,,,,,,,,,0,,0.2422,no
CHND_ACISS,Q9F7D8,Prot2Text,Bacteria,352,Dehydrogenase involved in the degradation of cyclohexanol to adipate. Catalyzes the conversion of 6- hydroxyhexanoate to 6-oxohexanoate.,"Multifunctional alcohol dehydrogenase exhibiting NAD(+)-dependent dehydrogenase activities for 2,3-butanediol, ethanol and acetaldehyde, and reductase activities for acetoin (NADH-dependent), and diacetyl and acetaldehyde (independently of whether NADH or NADPH is the reductant). The rate of oxidation of 2,3-butanediol is much higher than for the oxidation of ethanol. Has acetaldehyde dehydrogenase activity leading to acetate formation. May function in the release of excess reducing power in the absence of exogenous hydrogen acceptors such as oxygen.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004022; GO:0046872,GO:0004022,GO:0004022,GO:0004022,GO:0004022,GO:0004022,0.6924,0.6924,0.6924,0.6924,0.6924,5,0.6924,0.2422,no
CHND_ACISS,Q9F7D8,ProtT3,Bacteria,352,Dehydrogenase involved in the degradation of cyclohexanol to adipate. Catalyzes the conversion of 6- hydroxyhexanoate to 6-oxohexanoate.,Belongs to the zinc-containing alcohol dehydrogenase family,Vague,Vague,No,Vague,Vague,not-Yes,GO:0004022; GO:0046872,GO:0016491; GO:0008270,GO:0016491; GO:0008270,,GO:0016616; GO:0008270,GO:0004024,0.6544,0.6544,,0.7623,0.0,4,0.5178,0.2422,no
CHND_ACISS,Q9F7D8,ProtTale,Bacteria,352,Dehydrogenase involved in the degradation of cyclohexanol to adipate. Catalyzes the conversion of 6- hydroxyhexanoate to 6-oxohexanoate.,Catalyzes the NAD(P)H-dependent reduction of a range of aldehydes and ketones. In vitro also catalyzes the reduction of 4-nitrobenzaldehyde to 4-aminobenzoate.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004022; GO:0046872,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4114,0.4114,0.4114,0.4114,0.4114,5,0.4114,0.2422,no
CHND_ACISS,Q9F7D8,Protein2Text,Bacteria,352,Dehydrogenase involved in the degradation of cyclohexanol to adipate. Catalyzes the conversion of 6- hydroxyhexanoate to 6-oxohexanoate.,"The molecular function of this protein is an oxidoreductase activity, specifically a glucose dehydrogenase activity.",No,Maybe,No,Maybe,No,not-Yes,GO:0004022; GO:0046872,GO:0016491,GO:0016491,GO:0016614,,GO:0047936,0.4114,0.4114,0.4732,,0.409,4,0.4263,0.2422,no
CHND_ACISS,Q9F7D8,Reference,Bacteria,352,Dehydrogenase involved in the degradation of cyclohexanol to adipate. Catalyzes the conversion of 6- hydroxyhexanoate to 6-oxohexanoate.,Dehydrogenase involved in the degradation of cyclohexanol to adipate. Catalyzes the conversion of 6- hydroxyhexanoate to 6-oxohexanoate.,,,,,,,GO:0004022; GO:0046872,GO:0016614,GO:0016491,GO:0016491,GO:0016614,GO:0016491,0.4732,0.4114,0.4114,0.4732,0.4114,5,0.4361,0.2422,no
GLYAR_HALSA,Q9HHR2,ESM2Text,Archaea,365,"Oxidoreductase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the reduction of glycolaldehyde to ethylene glycol. Cannot catalyze the oxidation of glycerol 1-phosphate nor the reduction of dihydroxyacetone phosphate (DHAP).",Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-phosphate (G1P). The G1P thus generated is probably used for the synthesis of phospholipids in Gram-positive bacterial species.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008888; GO:0046872,GO:0016491,GO:0004367,GO:0004367,GO:0016616,GO:0004367,0.4539,0.5156,0.5156,0.607,0.5156,5,0.5215,0.1773,no
GLYAR_HALSA,Q9HHR2,Prot2Text,Archaea,365,"Oxidoreductase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the reduction of glycolaldehyde to ethylene glycol. Cannot catalyze the oxidation of glycerol 1-phosphate nor the reduction of dihydroxyacetone phosphate (DHAP).",Catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). Allows microorganisms to utilize glycerol as a source of carbon under anaerobic conditions.,No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008888; GO:0046872,GO:0016614,GO:0008888,GO:0004022,GO:0016614,GO:0004367,0.5281,0.6963,0.4481,0.5281,0.5156,5,0.5432,0.1773,no
GLYAR_HALSA,Q9HHR2,ProtT3,Archaea,365,"Oxidoreductase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the reduction of glycolaldehyde to ethylene glycol. Cannot catalyze the oxidation of glycerol 1-phosphate nor the reduction of dihydroxyacetone phosphate (DHAP).",Catalyzes the NAD(P)(+)-dependent oxidation of glycerol to dihydroxyacetone phosphate (DHAP or glycerone phosphate). Is involved in the anaerobic degradation of glycerol. Belongs to the iron-containing alcohol dehydrogenase family,No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008888; GO:0046872,GO:0016616,GO:0016491,GO:0016616,GO:0016616,GO:0016616,0.607,0.4539,0.607,0.607,0.607,5,0.5764,0.1773,no
GLYAR_HALSA,Q9HHR2,ProtTale,Archaea,365,"Oxidoreductase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the reduction of glycolaldehyde to ethylene glycol. Cannot catalyze the oxidation of glycerol 1-phosphate nor the reduction of dihydroxyacetone phosphate (DHAP).",Catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone.,No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008888; GO:0046872,GO:0016491,GO:0047952,GO:0016491,GO:0016491,GO:0016616,0.4539,0.5156,0.4539,0.4539,0.607,5,0.4969,0.1773,no
GLYAR_HALSA,Q9HHR2,Protein2Text,Archaea,365,"Oxidoreductase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the reduction of glycolaldehyde to ethylene glycol. Cannot catalyze the oxidation of glycerol 1-phosphate nor the reduction of dihydroxyacetone phosphate (DHAP).","The molecular function of this protein is involved in catalyzing a chemical reaction. The specific reaction catalyzed by this protein is the reduction of dihydroxyacetone phosphate (DHAP) to glycerol 3-phosphate (G3P). This is a key step in glycolysis, as G3P is a crucial intermediate in the breakdown of glucose to produce energy. The protein uses NADH as a cofactor to reduce DHAP to G3P.",Maybe,Maybe,Maybe,Maybe,No,not-Yes,GO:0008888; GO:0046872,GO:0004367,GO:0004367,GO:0004367,GO:0004367,GO:0004367,0.5156,0.5156,0.5156,0.5156,0.5156,5,0.5156,0.1773,no
GLYAR_HALSA,Q9HHR2,Reference,Archaea,365,"Oxidoreductase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the reduction of glycolaldehyde to ethylene glycol. Cannot catalyze the oxidation of glycerol 1-phosphate nor the reduction of dihydroxyacetone phosphate (DHAP).","Oxidoreductase involved in the non-carboxylating pentose bisphosphate pathway, a nucleoside degradation pathway present in some halophilic archaea. Catalyzes the reduction of glycolaldehyde to ethylene glycol. Cannot catalyze the oxidation of glycerol 1-phosphate nor the reduction of dihydroxyacetone phosphate (DHAP).",,,,,,,GO:0008888; GO:0046872,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4539,0.4539,0.4539,0.4539,0.4539,5,0.4539,0.1773,no
CDHB_PSEAE,Q9HTH9,ESM2Text,Bacteria,159,"Catalyzes the cleavage of betainyl-CoA (N,N,N- trimethylglycyl-CoA) into glycine betaine and coenzyme A. Is involved in a L-carnitine degradation pathway that allows P.aeruginosa to grow on L-carnitine as the sole source of carbon and nitrogen.","Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA), a reaction involved in phylloquinone (vitamin K1) biosynthesis.",No,No,No,No,Maybe,not-Yes,GO:0047617,GO:0016790,GO:0016790,GO:0016790,GO:0016790,GO:0016790,0.7055,0.7055,0.7055,0.7055,0.7055,5,0.7055,0.3716,no
CDHB_PSEAE,Q9HTH9,Prot2Text,Bacteria,159,"Catalyzes the cleavage of betainyl-CoA (N,N,N- trimethylglycyl-CoA) into glycine betaine and coenzyme A. Is involved in a L-carnitine degradation pathway that allows P.aeruginosa to grow on L-carnitine as the sole source of carbon and nitrogen.","Shows transactivation activity towards various acetylated phenylacetyl-CoA substrates, including 4-hydroxybenzoyl-CoA and salicylic-CoA.",No,No,No,No,No,not-Yes,GO:0047617,,,,,GO:0016746,,,,,0.2633,1,0.2633,0.3716,no
CDHB_PSEAE,Q9HTH9,ProtT3,Bacteria,159,"Catalyzes the cleavage of betainyl-CoA (N,N,N- trimethylglycyl-CoA) into glycine betaine and coenzyme A. Is involved in a L-carnitine degradation pathway that allows P.aeruginosa to grow on L-carnitine as the sole source of carbon and nitrogen.",Involved in the biosynthesis of unsaturated fatty acids. Catalyzes the hydrolysis of (3R)-3-hydroxyacyl-ACP to (3R)-3-hydroxyacyl-CoA (By similarity). Belongs to the thioesterase PaaI family,Vague,No,No,No,Maybe,not-Yes,GO:0047617,GO:0016790,GO:0016790,GO:0016790,GO:0016790,GO:0016790,0.7055,0.7055,0.7055,0.7055,0.7055,5,0.7055,0.3716,no
CDHB_PSEAE,Q9HTH9,ProtTale,Bacteria,159,"Catalyzes the cleavage of betainyl-CoA (N,N,N- trimethylglycyl-CoA) into glycine betaine and coenzyme A. Is involved in a L-carnitine degradation pathway that allows P.aeruginosa to grow on L-carnitine as the sole source of carbon and nitrogen.",Transforms 2-succinylbenzoate (OSB) into 2-succinylbenzoyl-CoA (OSB-CoA).,No,No,No,No,No,not-Yes,GO:0047617,GO:0008756,GO:0008756,GO:0016874,GO:0008756,GO:0008756,0.1762,0.1762,0.3207,0.1762,0.1762,5,0.2051,0.3716,no
CDHB_PSEAE,Q9HTH9,Protein2Text,Bacteria,159,"Catalyzes the cleavage of betainyl-CoA (N,N,N- trimethylglycyl-CoA) into glycine betaine and coenzyme A. Is involved in a L-carnitine degradation pathway that allows P.aeruginosa to grow on L-carnitine as the sole source of carbon and nitrogen.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its name, it is likely to be involved in a process related to the transfer of groups, possibly in a biochemical reaction. A common function of proteins with names ending in '-transferase' is to catalyze the transfer of a group from one molecule to another.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0047617,,,,,,,,,,,0,,0.3716,no
CDHB_PSEAE,Q9HTH9,Reference,Bacteria,159,"Catalyzes the cleavage of betainyl-CoA (N,N,N- trimethylglycyl-CoA) into glycine betaine and coenzyme A. Is involved in a L-carnitine degradation pathway that allows P.aeruginosa to grow on L-carnitine as the sole source of carbon and nitrogen.","Catalyzes the cleavage of betainyl-CoA (N,N,N- trimethylglycyl-CoA) into glycine betaine and coenzyme A. Is involved in a L-carnitine degradation pathway that allows P.aeruginosa to grow on L-carnitine as the sole source of carbon and nitrogen.",,,,,,,GO:0047617,GO:0016787,GO:0016787,GO:0016790,GO:0016790,GO:0016787,0.5122,0.5122,0.7055,0.7055,0.5122,5,0.5895,0.3716,no
LIPA_PENCY,Q9P451,ESM2Text,Eukaryota,285,"Secreted alkaline lipase that hydrolyzes acylglycerol lipids such as triacylglycerols and consequently releases free fatty acid. Is able to hydrolyze tributyrin (1,2,3-tributyryl- glycerin).","Degrades chitin, a structural polymer of the cell wall that serves as a structural anchor of the cell wall.",No,No,No,No,No,not-Yes,GO:0004806,GO:0004568,GO:0004568,GO:0004568,GO:0004568,GO:0004568,0.3055,0.3055,0.3055,0.3055,0.3055,5,0.3055,0.2466,no
LIPA_PENCY,Q9P451,Prot2Text,Eukaryota,285,"Secreted alkaline lipase that hydrolyzes acylglycerol lipids such as triacylglycerols and consequently releases free fatty acid. Is able to hydrolyze tributyrin (1,2,3-tributyryl- glycerin).",Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone.,No,No,No,No,No,not-Yes,GO:0004806,GO:0016788,GO:0016290,GO:0016290,GO:0016290,GO:0016788,0.6506,0.0,0.0,0.0,0.6506,5,0.2602,0.2466,no
LIPA_PENCY,Q9P451,ProtT3,Eukaryota,285,"Secreted alkaline lipase that hydrolyzes acylglycerol lipids such as triacylglycerols and consequently releases free fatty acid. Is able to hydrolyze tributyrin (1,2,3-tributyryl- glycerin).",Catalyzes the hydrolysis of triacylglycerols (TAG) into free fatty acids and glycerol. Secreted. Belongs to the AB hydrolase superfamily. Lipase family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2466,no
LIPA_PENCY,Q9P451,ProtTale,Eukaryota,285,"Secreted alkaline lipase that hydrolyzes acylglycerol lipids such as triacylglycerols and consequently releases free fatty acid. Is able to hydrolyze tributyrin (1,2,3-tributyryl- glycerin).","Secreted lipase involved in Dandruff and seborrheic dermatitis (D/SD) probably via lipase-mediated breakdown of sebaceous lipids and release of irritating free fatty acids. Shows activity against monoglyceride and diglyceride substrates, but not triolein. Able to cleave oleic acid from 1,2-dioleoyl-sn-glycero-3-phosphocholine (18:2-POPC), a major component of cell membranes. Has no activity against 1,2-dioleoyl-sn-glycero-3-phosphoethanol",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004806,GO:0016298,GO:0016298; GO:0004620,GO:0016298,GO:0016298,GO:0016298,0.7707,0.705,0.7707,0.7707,0.7707,5,0.7576,0.2466,no
LIPA_PENCY,Q9P451,Protein2Text,Eukaryota,285,"Secreted alkaline lipase that hydrolyzes acylglycerol lipids such as triacylglycerols and consequently releases free fatty acid. Is able to hydrolyze tributyrin (1,2,3-tributyryl- glycerin).","This protein is involved in the degradation of insoluble substrates, specifically in the hydrolysis of insoluble substrates such as cellulose and starch. It is a key enzyme in the degradation of plant biomass.",Vague,No,Vague,Vague,Vague,not-Yes,GO:0004806,GO:0008810,GO:0004553,GO:0008810,GO:0008810,GO:0008810,0.3055,0.358,0.3055,0.3055,0.3055,5,0.316,0.2466,no
LIPA_PENCY,Q9P451,Reference,Eukaryota,285,"Secreted alkaline lipase that hydrolyzes acylglycerol lipids such as triacylglycerols and consequently releases free fatty acid. Is able to hydrolyze tributyrin (1,2,3-tributyryl- glycerin).","Secreted alkaline lipase that hydrolyzes acylglycerol lipids such as triacylglycerols and consequently releases free fatty acid. Is able to hydrolyze tributyrin (1,2,3-tributyryl- glycerin).",,,,,,,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,GO:0004806,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2466,no
SKS14_ARATH,Q9SMW3,ESM2Text,Eukaryota,549,Probable oxidoreductase that may be involved in pollen tube growth.,Probable oxidase that may be involved in reproductive development.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005507; GO:0016491,,,,,,,,,,,0,,0.4077,no
SKS14_ARATH,Q9SMW3,Prot2Text,Eukaryota,549,Probable oxidoreductase that may be involved in pollen tube growth.,Probable oxidase that may be involved in pollen tube growth.,Yes,Yes,Maybe,Yes,Yes,Yes,GO:0005507; GO:0016491,,,,,,,,,,,0,,0.4077,no
SKS14_ARATH,Q9SMW3,ProtT3,Eukaryota,549,Probable oxidoreductase that may be involved in pollen tube growth.,"Secreted, extracellular space, apoplast. Belongs to the multicopper oxidase family",Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0005507; GO:0016491,GO:0016491; GO:0005507,GO:0016491; GO:0005507,,GO:0016491; GO:0005507,GO:0016491; GO:0005507,1.0,1.0,,1.0,1.0,4,1.0,0.4077,no
SKS14_ARATH,Q9SMW3,ProtTale,Eukaryota,549,Probable oxidoreductase that may be involved in pollen tube growth.,Lignin degradation and detoxification of lignin-derived products.,No,No,No,No,Maybe,not-Yes,GO:0005507; GO:0016491,,,,,,,,,,,0,,0.4077,no
SKS14_ARATH,Q9SMW3,Protein2Text,Eukaryota,549,Probable oxidoreductase that may be involved in pollen tube growth.,"The molecular function of this protein is associated with the breakdown and degradation of lignin, a complex organic polymer that provides structural support to plant cell walls. The protein likely plays a role in the oxidation and cleavage of lignin, possibly through the use of peroxidase enzymes. This process is important for the release of lignin-derived compounds, which can be used as a source of energy for the plant or as a defense against pathogens. 

In more detail, the protein is likely a peroxidase that uses hydrogen peroxide (H2O2) as a co-factor to oxidize lignin and break it down into smaller fragments. This process involves the formation of reactive oxygen species (ROS) and the generation of hydroxyl radicals, which are capable of cleaving lignin bonds and releasing lignin-derived compounds. The protein may also play a role in the detoxification of ROS and the maintenance of redox balance in the plant cell. 

Overall, the molecular function of this protein is essential for the degradation of lignin and the release of lignin-derived compounds, which are important for plant growth and development.",No,No,No,No,Maybe,not-Yes,GO:0005507; GO:0016491,GO:0004601,GO:0004601,GO:0004601,GO:0004601,GO:0004601,0.4461,0.4461,0.4461,0.4461,0.4461,5,0.4461,0.4077,no
SKS14_ARATH,Q9SMW3,Reference,Eukaryota,549,Probable oxidoreductase that may be involved in pollen tube growth.,Probable oxidoreductase that may be involved in pollen tube growth.,,,,,,,GO:0005507; GO:0016491,,,,,GO:0016491,,,,,0.7096,1,0.7096,0.4077,no
YELLH_DROME,Q9V4C0,ESM2Text,Eukaryota,463,"Catalyzes the conversion of dopaminechrome to 5,6- dihydroxyindole in the eumelanin biosynthetic pathway originating from dopamine. Catalyzes tautomerization of dopaminechrome to 5,6-dihydroxyindole during eumelanin biosynthesis. Acts both dopaminechrome and N-methyl dopaminechrome but not on dopachrome or other aminochromes tested.",Heme-binding protein that promotes neuronal but not astrocyte differentiation. Modulates chemotaxis and neurite outgrowth by controlling the concentration of dendrites and intermediate filaments within the neuromuscular junction complex.,No,No,No,No,No,not-Yes,GO:0106417,GO:0020037,GO:0020037,GO:0020037,,GO:0020037,0.1264,0.1264,0.1264,,0.1264,4,0.1264,0.3993,no
YELLH_DROME,Q9V4C0,Prot2Text,Eukaryota,463,"Catalyzes the conversion of dopaminechrome to 5,6- dihydroxyindole in the eumelanin biosynthetic pathway originating from dopamine. Catalyzes tautomerization of dopaminechrome to 5,6-dihydroxyindole during eumelanin biosynthesis. Acts both dopaminechrome and N-methyl dopaminechrome but not on dopachrome or other aminochromes tested.","Catalyzes the stereospecific condensation of tryptamine with secologanin to form strictosidine, the key intermediate of indole alkaloid biosynthesis.",No,No,No,No,No,not-Yes,GO:0106417,GO:0016829,GO:0016844,GO:0016844,GO:0016844,GO:0016844,0.3552,0.2353,0.2353,0.2353,0.2353,5,0.2593,0.3993,no
YELLH_DROME,Q9V4C0,ProtT3,Eukaryota,463,"Catalyzes the conversion of dopaminechrome to 5,6- dihydroxyindole in the eumelanin biosynthetic pathway originating from dopamine. Catalyzes tautomerization of dopaminechrome to 5,6-dihydroxyindole during eumelanin biosynthesis. Acts both dopaminechrome and N-methyl dopaminechrome but not on dopachrome or other aminochromes tested.",This protein is responsible for the color of the eggshell. Secreted. Belongs to the chorion protein family,Vague,No,No,No,No,not-Yes,GO:0106417,,,,,,,,,,,0,,0.3993,no
YELLH_DROME,Q9V4C0,ProtTale,Eukaryota,463,"Catalyzes the conversion of dopaminechrome to 5,6- dihydroxyindole in the eumelanin biosynthetic pathway originating from dopamine. Catalyzes tautomerization of dopaminechrome to 5,6-dihydroxyindole during eumelanin biosynthesis. Acts both dopaminechrome and N-methyl dopaminechrome but not on dopachrome or other aminochromes tested.",Probable lipid-binding protein.,Vague,Vague,No,Vague,No,not-Yes,GO:0106417,GO:0008289,GO:0008289,GO:0008289,GO:0008289,GO:0008289,0.1579,0.1579,0.1579,0.1579,0.1579,5,0.1579,0.3993,no
YELLH_DROME,Q9V4C0,Protein2Text,Eukaryota,463,"Catalyzes the conversion of dopaminechrome to 5,6- dihydroxyindole in the eumelanin biosynthetic pathway originating from dopamine. Catalyzes tautomerization of dopaminechrome to 5,6-dihydroxyindole during eumelanin biosynthesis. Acts both dopaminechrome and N-methyl dopaminechrome but not on dopachrome or other aminochromes tested.","The molecular function of this protein is not specified in the given text. However, based on its name, it is likely that it has a role in binding and transporting molecules, possibly as part of a signaling pathway or in the regulation of cellular processes. Further research would be needed to determine the exact molecular function of this protein. 

In general, proteins that are involved in binding and transporting molecules are often referred to as transport proteins or binding proteins. They may play a role in facilitating the movement of molecules across cell membranes, regulating the concentration of molecules within cells, or participating in signaling pathways that control various cellular processes. 

Some examples of transport proteins include membrane transport proteins, such as ion channels and transporters, and cytosolic transport proteins, such as chaperones and shuttles. Binding proteins, on the other hand, may bind to specific molecules and regulate their activity or availability. 

It's worth noting that the exact molecular function of a protein can only be determined through experimental research, such as biochemical assays or structural biology techniques. The name of a protein can provide clues about its function, but it is not a definitive indicator of its molecular function. 

If you have any further information about this protein, such as its name or any known functions, I may be able to provide more specific information about its molecular function. 

In this case, the protein is a part of a pathway that is involved in the regulation of cell signaling, and it is likely that it plays a role in binding and transporting molecules involved in this process. However, further research would be needed to determine the exact molecular function of this protein.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0106417,,,,,,,,,,,0,,0.3993,no
YELLH_DROME,Q9V4C0,Reference,Eukaryota,463,"Catalyzes the conversion of dopaminechrome to 5,6- dihydroxyindole in the eumelanin biosynthetic pathway originating from dopamine. Catalyzes tautomerization of dopaminechrome to 5,6-dihydroxyindole during eumelanin biosynthesis. Acts both dopaminechrome and N-methyl dopaminechrome but not on dopachrome or other aminochromes tested.","Catalyzes the conversion of dopaminechrome to 5,6- dihydroxyindole in the eumelanin biosynthetic pathway originating from dopamine. Catalyzes tautomerization of dopaminechrome to 5,6-dihydroxyindole during eumelanin biosynthesis. Acts both dopaminechrome and N-methyl dopaminechrome but not on dopachrome or other aminochromes tested.",,,,,,,GO:0106417,GO:0016853,GO:0016853,GO:0016853,GO:0016853,GO:0016853,0.6019,0.6019,0.6019,0.6019,0.6019,5,0.6019,0.3993,no
BHMT_DROME,Q9VJ31,ESM2Text,Eukaryota,331,"Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively.","Catalyzes the methylation of selenocysteine with S-methylmethionine as donor. Methylates cysteine, selenium arsenate, antimony methanol, and M-chloro-S-methylmethionine to produce M-chloro-S-methylmethionine. No activity with selenocysteine, selenium arsenate or methylated selenium arsenicals. Involved in selenium detoxification.",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0047150; GO:0008898; GO:0061627; GO:0008270,GO:0008168,GO:0008168,,,,0.6047,0.6047,,,,2,0.6047,0.3206,no
BHMT_DROME,Q9VJ31,Prot2Text,Eukaryota,331,"Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively.",Catalyzes the methylation of selenocysteine with S-methylmethionine as donor. Methylates also selenocysteine. Participates in selenoprotein biosynthesis.,Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0047150; GO:0008898; GO:0061627; GO:0008270,GO:0008168,GO:0008168,GO:0008168,,GO:0008168,0.6047,0.6047,0.6047,,0.6047,4,0.6047,0.3206,no
BHMT_DROME,Q9VJ31,ProtT3,Eukaryota,331,"Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively.",Catalyzes the methylation of S-adenosyl-L-methionine (AdoMet) to form S-adenosyl-L-homocysteine (AdoHcy). Cytoplasm. Belongs to the class I-like SAM-binding methyltransferase superfamily,No,No,No,No,No,not-Yes,GO:0047150; GO:0008898; GO:0061627; GO:0008270,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.6047,0.6047,0.6047,0.6047,0.6047,5,0.6047,0.3206,no
BHMT_DROME,Q9VJ31,ProtTale,Eukaryota,331,"Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively.",Catalyzes the reduction of S-adenosyl-L-methionine (AdoMet) to S- adenosyl-L-homocysteine.,No,No,No,No,No,not-Yes,GO:0047150; GO:0008898; GO:0061627; GO:0008270,,GO:0016491,,GO:0016491,,,0.2727,,0.2727,,2,0.2727,0.3206,no
BHMT_DROME,Q9VJ31,Protein2Text,Eukaryota,331,"Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively.","This protein is involved in the molecular function of catalyzing the decarboxylation of pyridoxal 5'-phosphate (PLP), a vitamin B6 derivative. Specifically, it catalyzes the decarboxylation of PLP to form pyridoxal, which is an essential step in the metabolism of vitamin B6. This reaction is a crucial step in the synthesis of various B6 vitamers, which are essential for various cellular processes, including amino acid metabolism, neurotransmitter synthesis, and energy production.",No,No,No,No,No,not-Yes,GO:0047150; GO:0008898; GO:0061627; GO:0008270,,,,,,,,,,,0,,0.3206,no
BHMT_DROME,Q9VJ31,Reference,Eukaryota,331,"Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively.","Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively.",,,,,,,GO:0047150; GO:0008898; GO:0061627; GO:0008270,GO:0030592,GO:0047150; GO:0008168,GO:0004592,GO:0047150,GO:0008168,0.0,0.7116,0.1493,0.6967,0.6047,5,0.4325,0.3206,no
CMT_TOXGM,S8F527,ESM2Text,Eukaryota,1283,Capping enzyme with methyltransferase activity; methylates the guanine N7 position of the GpppRNA.,Responsible for methylating the 5'-cap structure of tRNA(Arg)(CCU) and tRNA(Arg)(UCU) to form the corresponding 5'-cap structure (m5C) in tRNAs. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the 5'-cap structure.,No,Maybe,No,Maybe,Maybe,not-Yes,GO:0004482; GO:0003723,GO:0008173,GO:0008173,GO:0008173,GO:0008173,GO:0008175,0.5277,0.5277,0.5277,0.5277,0.4394,5,0.51,0.4931,no
CMT_TOXGM,S8F527,Prot2Text,Eukaryota,1283,Capping enzyme with methyltransferase activity; methylates the guanine N7 position of the GpppRNA.,Responsible for methylating the 5'-cap structure of tRNA(Arg)(CCU) and tRNA(Arg)(UCU) to form the corresponding 5'-cap structure (m5C) in tRNAs. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the 5'-cap structure.,No,Maybe,No,Maybe,Maybe,not-Yes,GO:0004482; GO:0003723,GO:0008168,GO:0008175,GO:0008175,,GO:0008168,0.405,0.4394,0.4394,,0.405,4,0.4222,0.4931,no
CMT_TOXGM,S8F527,ProtT3,Eukaryota,1283,Capping enzyme with methyltransferase activity; methylates the guanine N7 position of the GpppRNA.,Specifically methylates the 5'-cap structure of mRNAs. Nucleus. Belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0 methyltransferase family,Yes,Yes,Maybe,Yes,Yes,Yes,GO:0004482; GO:0003723,GO:0004482,GO:0004482,GO:0004482,GO:0004482,GO:0004482,0.6927,0.6927,0.6927,0.6927,0.6927,5,0.6927,0.4931,no
CMT_TOXGM,S8F527,ProtTale,Eukaryota,1283,Capping enzyme with methyltransferase activity; methylates the guanine N7 position of the GpppRNA.,"Histone methyltransferase that specifically mono-, di- and trimethylates histone H3 at 'Lys-9' to form H3K9me1, H3K9me2 and H3K9me3. H3K9me1, H3K9me2 and H3K9me3 represent key modifications in the chromatin that are required for a wide variety of cellular processes including transcriptional activation, DNA repair, chromosome segregation and telomere maintenance. Recruited to promoters by transcription factors, thereby playing a key role in the regulation of gene expression.",No,No,No,No,No,not-Yes,GO:0004482; GO:0003723,GO:0018024,GO:0018024,GO:0018024,GO:0042054,GO:0018024,0.0,0.0,0.0,0.2792,0.0,5,0.0558,0.4931,no
CMT_TOXGM,S8F527,Protein2Text,Eukaryota,1283,Capping enzyme with methyltransferase activity; methylates the guanine N7 position of the GpppRNA.,"The molecular function of the protein is unknown, but it is involved in the regulation of muscle cell differentiation and muscle atrophy. It may also play a role in the regulation of the ubiquitin-proteasome system.",No,No,No,Vague,No,not-Yes,GO:0004482; GO:0003723,,,,,,,,,,,0,,0.4931,no
CMT_TOXGM,S8F527,Reference,Eukaryota,1283,Capping enzyme with methyltransferase activity; methylates the guanine N7 position of the GpppRNA.,Capping enzyme with methyltransferase activity; methylates the guanine N7 position of the GpppRNA.,,,,,,,GO:0004482; GO:0003723,GO:0004482,GO:0004482,GO:0004482,GO:0004482,GO:0004482,0.6927,0.6927,0.6927,0.6927,0.6927,5,0.6927,0.4931,no
MCDA_GLOK1,U5QDF4,ESM2Text,Bacteria,216,"McdA and McdB together mediate carboxysome (Cb) spacing, size, ultrastructure and probably inheritance in the cell, together they prevent Cb aggregation. McdA is an ATPase that forms dynamic gradients on the nucleoid in response to adapter protein McdB, which associates with carboxysomes. The interplay between McdA gradients on the nucleoid and McdB-bound carboxysomes result in the equal spacing of Cbs along the cell length.",Involved in chromosome partitioning; required for the formation of the inner spore coat and for the formation of the outer spore coat.,No,No,No,Maybe,No,not-Yes,GO:0005524; GO:0016787; GO:0046872,,,,,,,,,,,0,,0.3492,no
MCDA_GLOK1,U5QDF4,Prot2Text,Bacteria,216,"McdA and McdB together mediate carboxysome (Cb) spacing, size, ultrastructure and probably inheritance in the cell, together they prevent Cb aggregation. McdA is an ATPase that forms dynamic gradients on the nucleoid in response to adapter protein McdB, which associates with carboxysomes. The interplay between McdA gradients on the nucleoid and McdB-bound carboxysomes result in the equal spacing of Cbs along the cell length.",A global protein that might be required for efficient placement of pectin synthesis and/or maintenance.,No,No,No,No,No,not-Yes,GO:0005524; GO:0016787; GO:0046872,,,,,,,,,,,0,,0.3492,no
MCDA_GLOK1,U5QDF4,ProtT3,Bacteria,216,"McdA and McdB together mediate carboxysome (Cb) spacing, size, ultrastructure and probably inheritance in the cell, together they prevent Cb aggregation. McdA is an ATPase that forms dynamic gradients on the nucleoid in response to adapter protein McdB, which associates with carboxysomes. The interplay between McdA gradients on the nucleoid and McdB-bound carboxysomes result in the equal spacing of Cbs along the cell length.",Belongs to the ParA family,Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0005524; GO:0016787; GO:0046872,GO:0016887; GO:0005524,GO:0016887,,,GO:0016887,0.6457,0.2732,,,0.2732,3,0.3974,0.3492,no
MCDA_GLOK1,U5QDF4,ProtTale,Bacteria,216,"McdA and McdB together mediate carboxysome (Cb) spacing, size, ultrastructure and probably inheritance in the cell, together they prevent Cb aggregation. McdA is an ATPase that forms dynamic gradients on the nucleoid in response to adapter protein McdB, which associates with carboxysomes. The interplay between McdA gradients on the nucleoid and McdB-bound carboxysomes result in the equal spacing of Cbs along the cell length.",Required for chromosome segregation. May be involved in regulating chromosome replication and transcription.,Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0005524; GO:0016787; GO:0046872,,,,,,,,,,,0,,0.3492,no
MCDA_GLOK1,U5QDF4,Protein2Text,Bacteria,216,"McdA and McdB together mediate carboxysome (Cb) spacing, size, ultrastructure and probably inheritance in the cell, together they prevent Cb aggregation. McdA is an ATPase that forms dynamic gradients on the nucleoid in response to adapter protein McdB, which associates with carboxysomes. The interplay between McdA gradients on the nucleoid and McdB-bound carboxysomes result in the equal spacing of Cbs along the cell length.","The molecular function of this protein is not explicitly stated in the provided text. However, based on the name ""RecA"" and the context of the research, it can be inferred that this protein is involved in DNA recombination and repair. RecA is a well-known protein that plays a crucial role in homologous recombination and repair of DNA damage in bacteria. It is likely that this protein is involved in a similar process.",Vague,No,Vague,No,No,not-Yes,GO:0005524; GO:0016787; GO:0046872,,GO:0005524; GO:0003697,,,GO:0008094; GO:0005524,,0.541,,,0.6095,2,0.5753,0.3492,no
MCDA_GLOK1,U5QDF4,Reference,Bacteria,216,"McdA and McdB together mediate carboxysome (Cb) spacing, size, ultrastructure and probably inheritance in the cell, together they prevent Cb aggregation. McdA is an ATPase that forms dynamic gradients on the nucleoid in response to adapter protein McdB, which associates with carboxysomes. The interplay between McdA gradients on the nucleoid and McdB-bound carboxysomes result in the equal spacing of Cbs along the cell length.","McdA and McdB together mediate carboxysome (Cb) spacing, size, ultrastructure and probably inheritance in the cell, together they prevent Cb aggregation. McdA is an ATPase that forms dynamic gradients on the nucleoid in response to adapter protein McdB, which associates with carboxysomes. The interplay between McdA gradients on the nucleoid and McdB-bound carboxysomes result in the equal spacing of Cbs along the cell length.",,,,,,,GO:0005524; GO:0016787; GO:0046872,GO:0016887,GO:0016887; GO:0005524,GO:0016887; GO:0005524,GO:0016887,GO:0016887; GO:0005524,0.2732,0.6457,0.6457,0.2732,0.6457,5,0.4967,0.3492,no
BMP2_PSEL2,V4HJ70,ESM2Text,Bacteria,406,"Brominase involved in the biosynthesis of polybrominated aromatic organic compounds. Catalyzes three successive rounds of bromination of pyrrolyl-S-Bmp1 to produce mono-, di- and tribromopyrrolyl-S-Bmp1.","Catalyzes the double cyclization reaction which converts lycopene to beta-carotene. It also catalyzes the double cyclization reaction which converts neurosporene to 7,8-dihydro-beta-carotene.",No,No,No,No,No,not-Yes,GO:0071949; GO:0016491,GO:0045436,GO:0016829,GO:0045436,GO:0045436,GO:0045436,0.2805,0.4328,0.2805,0.2805,0.2805,5,0.311,0.2131,no
BMP2_PSEL2,V4HJ70,Prot2Text,Bacteria,406,"Brominase involved in the biosynthesis of polybrominated aromatic organic compounds. Catalyzes three successive rounds of bromination of pyrrolyl-S-Bmp1 to produce mono-, di- and tribromopyrrolyl-S-Bmp1.",Could be required for the formation of a threonylcarbamoyl group on the F ring of ergothione (Probable). The protein prenyltransferase electron transferase (PTE) is a multifunctional protein that catalyzes the formation of prenylated phenylacetic acids by transfer of a methyl group from S-adenosyl-L-methionine (SAM) to the oxygenase component prenyltransferase. Mediates the addition of a methyl group at the C9 position of geranylgeranyl diphosphate (GGPP) to yield prenylacyl GGPP (Probable).,No,No,No,No,No,not-Yes,GO:0071949; GO:0016491,,,,,,,,,,,0,,0.2131,no
BMP2_PSEL2,V4HJ70,ProtT3,Bacteria,406,"Brominase involved in the biosynthesis of polybrominated aromatic organic compounds. Catalyzes three successive rounds of bromination of pyrrolyl-S-Bmp1 to produce mono-, di- and tribromopyrrolyl-S-Bmp1.",Catalyzes the chlorination of biliverdin IX-alpha to form biliverdin IX-beta. Belongs to the biliverdin reductase family,No,No,No,Maybe,Maybe,not-Yes,GO:0071949; GO:0016491,GO:0004074,GO:0004074,GO:0004074,GO:0004074,GO:0004074,0.4244,0.4244,0.4244,0.4244,0.4244,5,0.4244,0.2131,no
BMP2_PSEL2,V4HJ70,ProtTale,Bacteria,406,"Brominase involved in the biosynthesis of polybrominated aromatic organic compounds. Catalyzes three successive rounds of bromination of pyrrolyl-S-Bmp1 to produce mono-, di- and tribromopyrrolyl-S-Bmp1.","Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3- dihydroxymalonyl)-L-aspartate. Catalyzes the transfer of a phenylacetyl moiety from L-phenylacetyl-S-adenosylmethionine (PS-AdoMet) to 3,4-dihydroxybenzoate (3,4-DHB) to generate 4,5-dihydroxybenzoate (4,5-DHB). Can use L-phenylacetyl-S-adenosylmethionine (PS-A",No,No,No,No,No,not-Yes,GO:0071949; GO:0016491,GO:0016746,GO:0016740,GO:0016746,GO:0016746,GO:0016740,0.3526,0.4328,0.3526,0.3526,0.4328,5,0.3847,0.2131,no
BMP2_PSEL2,V4HJ70,Protein2Text,Bacteria,406,"Brominase involved in the biosynthesis of polybrominated aromatic organic compounds. Catalyzes three successive rounds of bromination of pyrrolyl-S-Bmp1 to produce mono-, di- and tribromopyrrolyl-S-Bmp1.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its name and the fact that it is involved in a biochemical reaction, it is likely that this protein is a flavin-containing monooxygenase, which is an enzyme that catalyzes the oxidation of a substrate using a flavin cofactor.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0071949; GO:0016491,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.5751,0.5751,0.5751,0.5751,0.5751,5,0.5751,0.2131,no
BMP2_PSEL2,V4HJ70,Reference,Bacteria,406,"Brominase involved in the biosynthesis of polybrominated aromatic organic compounds. Catalyzes three successive rounds of bromination of pyrrolyl-S-Bmp1 to produce mono-, di- and tribromopyrrolyl-S-Bmp1.","Brominase involved in the biosynthesis of polybrominated aromatic organic compounds. Catalyzes three successive rounds of bromination of pyrrolyl-S-Bmp1 to produce mono-, di- and tribromopyrrolyl-S-Bmp1.",,,,,,,GO:0071949; GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.706,0.706,0.706,0.706,0.706,5,0.706,0.2131,no
AMBP2_FISAU,V5TF61,ESM2Text,Bacteria,346,"Prenyltransferase involved in the biosynthesis of ambiguines, a family of hapalindole-type alkaloids. Catalyzes the addition of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to form geranyl pyrophosphate (GPP). Cannot use farnesyl diphosphate (FPP) or geranylgeranyl diphosphate (GGPP).",Catalyzes the condensation of farnesyl diphosphate (FPP) and isopentenyl diphosphate (IPP) to yield geranylgeranyl diphosphate (GGPP) needed for biosynthesis of carotenoids and diterpenes.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004161; GO:0046872,GO:0004337,GO:0004311,GO:0004311,GO:0004337,GO:0004311,0.5237,0.5237,0.5237,0.5237,0.5237,5,0.5237,0.2194,no
AMBP2_FISAU,V5TF61,Prot2Text,Bacteria,346,"Prenyltransferase involved in the biosynthesis of ambiguines, a family of hapalindole-type alkaloids. Catalyzes the addition of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to form geranyl pyrophosphate (GPP). Cannot use farnesyl diphosphate (FPP) or geranylgeranyl diphosphate (GGPP).",Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004161; GO:0046872,GO:0004337,GO:0004337,GO:0004337,GO:0016765,GO:0004337,0.5237,0.5237,0.5237,0.4732,0.5237,5,0.5136,0.2194,no
AMBP2_FISAU,V5TF61,ProtT3,Bacteria,346,"Prenyltransferase involved in the biosynthesis of ambiguines, a family of hapalindole-type alkaloids. Catalyzes the addition of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to form geranyl pyrophosphate (GPP). Cannot use farnesyl diphosphate (FPP) or geranylgeranyl diphosphate (GGPP).",Cytoplasm. Belongs to the FPP/GGPP synthase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004161; GO:0046872,GO:0004659,GO:0004337,,GO:0004337,GO:0004659,0.5374,0.5237,,0.5237,0.5374,4,0.5306,0.2194,no
AMBP2_FISAU,V5TF61,ProtTale,Bacteria,346,"Prenyltransferase involved in the biosynthesis of ambiguines, a family of hapalindole-type alkaloids. Catalyzes the addition of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to form geranyl pyrophosphate (GPP). Cannot use farnesyl diphosphate (FPP) or geranylgeranyl diphosphate (GGPP).","Catalyzes the condensation of isopentenyl pyrophosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield geranylgeranyl diphosphate (GGPP).",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004161; GO:0046872,GO:0016765,GO:0016765,GO:0004311,GO:0016765,GO:0004337,0.4732,0.4732,0.5237,0.4732,0.5237,5,0.4934,0.2194,no
AMBP2_FISAU,V5TF61,Protein2Text,Bacteria,346,"Prenyltransferase involved in the biosynthesis of ambiguines, a family of hapalindole-type alkaloids. Catalyzes the addition of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to form geranyl pyrophosphate (GPP). Cannot use farnesyl diphosphate (FPP) or geranylgeranyl diphosphate (GGPP).","The molecular function of this protein is a farnesyl transferase, which is an enzyme that catalyzes the transfer of a farnesyl group from farnesyl diphosphate to a cysteine residue in a protein. This is a crucial step in the post-translational modification of proteins, particularly those involved in signal transduction and cellular regulation.",No,No,No,No,No,not-Yes,GO:0004161; GO:0046872,GO:0004660,GO:0004660,GO:0004660,GO:0004660,GO:0004660,0.3767,0.3767,0.3767,0.3767,0.3767,5,0.3767,0.2194,no
AMBP2_FISAU,V5TF61,Reference,Bacteria,346,"Prenyltransferase involved in the biosynthesis of ambiguines, a family of hapalindole-type alkaloids. Catalyzes the addition of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to form geranyl pyrophosphate (GPP). Cannot use farnesyl diphosphate (FPP) or geranylgeranyl diphosphate (GGPP).","Prenyltransferase involved in the biosynthesis of ambiguines, a family of hapalindole-type alkaloids. Catalyzes the addition of isopentenyl diphosphate (IPP) onto dimethylallyl diphosphate (DMAPP) to form geranyl pyrophosphate (GPP). Cannot use farnesyl diphosphate (FPP) or geranylgeranyl diphosphate (GGPP).",,,,,,,GO:0004161; GO:0046872,GO:0004659,GO:0004337,GO:0004337,GO:0004659,GO:0004337,0.5374,0.5237,0.5237,0.5374,0.5237,5,0.5292,0.2194,no
GEPH_OGAPD,W1QDJ3,ESM2Text,Eukaryota,625,"Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released. Required for growth on nitrate as a sole nitrogen source.",Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.,Maybe,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0046872; GO:0061598; GO:0061599,,GO:0016740,,GO:0003824,,,0.4825,,0.3939,,2,0.4382,0.5474,yes
GEPH_OGAPD,W1QDJ3,Prot2Text,Eukaryota,625,"Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released. Required for growth on nitrate as a sole nitrogen source.","Has also a catalytic activity and catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0046872; GO:0061598; GO:0061599,,,GO:0061598,,,,,0.5109,,,1,0.5109,0.5474,yes
GEPH_OGAPD,W1QDJ3,ProtT3,Eukaryota,625,"Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released. Required for growth on nitrate as a sole nitrogen source.",Involved in the biosynthesis of the molybdenum cofactor. Catalyzes the insertion of molybdopterin into molybdopterin guanine dinucleotide (MGD) cofactor. Belongs to the MoaB/Mog family,Maybe,Yes,Maybe,Yes,Yes,Yes,GO:0005524; GO:0046872; GO:0061598; GO:0061599,GO:0016779,GO:0061598,GO:0016779,GO:0016779,GO:0003824,0.4464,0.5109,0.4464,0.4464,0.3939,5,0.4488,0.5474,yes
GEPH_OGAPD,W1QDJ3,ProtTale,Eukaryota,625,"Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released. Required for growth on nitrate as a sole nitrogen source.",Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.,Maybe,Yes,Yes,Yes,Yes,Yes,GO:0005524; GO:0046872; GO:0061598; GO:0061599,,GO:0016740,,,GO:0016740,,0.4825,,,0.4825,2,0.4825,0.5474,yes
GEPH_OGAPD,W1QDJ3,Protein2Text,Eukaryota,625,"Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released. Required for growth on nitrate as a sole nitrogen source.","The molecular function of this protein is not explicitly stated in the provided information. However, as a phosphatase, it is likely to catalyze the hydrolysis of phosphate esters, releasing inorganic phosphate and a phosphorylated substrate. This function is typically associated with enzymes that remove phosphate groups from molecules, such as proteins, lipids, or nucleotides.",No,No,No,No,No,not-Yes,GO:0005524; GO:0046872; GO:0061598; GO:0061599,GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,0.1774,0.1774,0.1774,0.1774,0.1774,5,0.1774,0.5474,yes
GEPH_OGAPD,W1QDJ3,Reference,Eukaryota,625,"Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released. Required for growth on nitrate as a sole nitrogen source.","Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released. Required for growth on nitrate as a sole nitrogen source.",,,,,,,GO:0005524; GO:0046872; GO:0061598; GO:0061599,GO:0016874,GO:0016779,GO:0030366; GO:0061598,GO:0016779,GO:0030366,0.3048,0.4464,0.5181,0.4464,0.2805,5,0.3992,0.5474,yes
ANUA_PENRF,W6QDA2,ESM2Text,Eukaryota,2130,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of annullatin D, an alkylated aromatic polyketide with a fused dihydrobenzofuran lactone ring system that exhibits potent agonistic activities toward the cannabinoid receptors. The annullatin backbone 2-hydroxymethyl-3- pentylphenol is assembled from one acetyl-CoA starter unit and 5 malonyl-CoA elongation units by cooperation of the highly reducing polyketide synthase anuA, the short-chain dehydrogenase anuB and the oxidoreductase anuC, before being hydroxylated at the C-5 alkyl chain by the cytochrome P450 monooxygenase anuE to form (8S)-annullatin E. The prenyltransferase anuH subsequently installs one isoprenyl group at the benzene ring to form (8S)-annullatin J. Enzymatic or nonenzymatic dihydro-benzofuran ring formation between the prenyl and the phenolic hydroxyl groups in (8S)-annullatin J results in two diastereomers (2S,9S)-annullatin H and compound 12. The intermediate (2S,9S)- annullatin H is then converted to (2S,9S)-annullatin D by the FAD- linked oxidoreductase anuG-catalyzed five-member lactone ring formation. The isomer 12 acts as a substrate for the short-chain dehydrogenase anuF and is oxidized to (2R)-annullatin F, which is subsequently acetylated by an acetyltransferase leading to (2R)- annullatin G formation. The remaining enzymes identified within the cluster, anuD, anuI and anuJ, seem not to be involved in annullatin biosynthesis (Probable).","Diketide monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ. Paxilline is converted to beta",No,No,No,No,No,not-Yes,GO:0004312; GO:0016491,GO:0004497,GO:0004497,GO:0004497; GO:0071949,GO:0004497,GO:0004497,0.6379,0.6379,0.5079,0.6379,0.6379,5,0.6119,0.3182,no
ANUA_PENRF,W6QDA2,Prot2Text,Eukaryota,2130,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of annullatin D, an alkylated aromatic polyketide with a fused dihydrobenzofuran lactone ring system that exhibits potent agonistic activities toward the cannabinoid receptors. The annullatin backbone 2-hydroxymethyl-3- pentylphenol is assembled from one acetyl-CoA starter unit and 5 malonyl-CoA elongation units by cooperation of the highly reducing polyketide synthase anuA, the short-chain dehydrogenase anuB and the oxidoreductase anuC, before being hydroxylated at the C-5 alkyl chain by the cytochrome P450 monooxygenase anuE to form (8S)-annullatin E. The prenyltransferase anuH subsequently installs one isoprenyl group at the benzene ring to form (8S)-annullatin J. Enzymatic or nonenzymatic dihydro-benzofuran ring formation between the prenyl and the phenolic hydroxyl groups in (8S)-annullatin J results in two diastereomers (2S,9S)-annullatin H and compound 12. The intermediate (2S,9S)- annullatin H is then converted to (2S,9S)-annullatin D by the FAD- linked oxidoreductase anuG-catalyzed five-member lactone ring formation. The isomer 12 acts as a substrate for the short-chain dehydrogenase anuF and is oxidized to (2R)-annullatin F, which is subsequently acetylated by an acetyltransferase leading to (2R)- annullatin G formation. The remaining enzymes identified within the cluster, anuD, anuI and anuJ, seem not to be involved in annullatin biosynthesis (Probable).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004312; GO:0016491,GO:0016746,GO:0016747,GO:0016747,GO:0016746,GO:0016747,0.6462,0.7078,0.7078,0.6462,0.7078,5,0.6832,0.3182,no
ANUA_PENRF,W6QDA2,ProtT3,Eukaryota,2130,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of annullatin D, an alkylated aromatic polyketide with a fused dihydrobenzofuran lactone ring system that exhibits potent agonistic activities toward the cannabinoid receptors. The annullatin backbone 2-hydroxymethyl-3- pentylphenol is assembled from one acetyl-CoA starter unit and 5 malonyl-CoA elongation units by cooperation of the highly reducing polyketide synthase anuA, the short-chain dehydrogenase anuB and the oxidoreductase anuC, before being hydroxylated at the C-5 alkyl chain by the cytochrome P450 monooxygenase anuE to form (8S)-annullatin E. The prenyltransferase anuH subsequently installs one isoprenyl group at the benzene ring to form (8S)-annullatin J. Enzymatic or nonenzymatic dihydro-benzofuran ring formation between the prenyl and the phenolic hydroxyl groups in (8S)-annullatin J results in two diastereomers (2S,9S)-annullatin H and compound 12. The intermediate (2S,9S)- annullatin H is then converted to (2S,9S)-annullatin D by the FAD- linked oxidoreductase anuG-catalyzed five-member lactone ring formation. The isomer 12 acts as a substrate for the short-chain dehydrogenase anuF and is oxidized to (2R)-annullatin F, which is subsequently acetylated by an acetyltransferase leading to (2R)- annullatin G formation. The remaining enzymes identified within the cluster, anuD, anuI and anuJ, seem not to be involved in annullatin biosynthesis (Probable).",Bifunctional non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0016491,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016747,0.6462,0.6462,0.6462,0.7078,0.7078,5,0.6708,0.3182,no
ANUA_PENRF,W6QDA2,ProtTale,Eukaryota,2130,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of annullatin D, an alkylated aromatic polyketide with a fused dihydrobenzofuran lactone ring system that exhibits potent agonistic activities toward the cannabinoid receptors. The annullatin backbone 2-hydroxymethyl-3- pentylphenol is assembled from one acetyl-CoA starter unit and 5 malonyl-CoA elongation units by cooperation of the highly reducing polyketide synthase anuA, the short-chain dehydrogenase anuB and the oxidoreductase anuC, before being hydroxylated at the C-5 alkyl chain by the cytochrome P450 monooxygenase anuE to form (8S)-annullatin E. The prenyltransferase anuH subsequently installs one isoprenyl group at the benzene ring to form (8S)-annullatin J. Enzymatic or nonenzymatic dihydro-benzofuran ring formation between the prenyl and the phenolic hydroxyl groups in (8S)-annullatin J results in two diastereomers (2S,9S)-annullatin H and compound 12. The intermediate (2S,9S)- annullatin H is then converted to (2S,9S)-annullatin D by the FAD- linked oxidoreductase anuG-catalyzed five-member lactone ring formation. The isomer 12 acts as a substrate for the short-chain dehydrogenase anuF and is oxidized to (2R)-annullatin F, which is subsequently acetylated by an acetyltransferase leading to (2R)- annullatin G formation. The remaining enzymes identified within the cluster, anuD, anuI and anuJ, seem not to be involved in annullatin biosynthesis (Probable).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004312; GO:0016491,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.6462,0.6462,0.6462,0.6462,0.6462,5,0.6462,0.3182,no
ANUA_PENRF,W6QDA2,Protein2Text,Eukaryota,2130,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of annullatin D, an alkylated aromatic polyketide with a fused dihydrobenzofuran lactone ring system that exhibits potent agonistic activities toward the cannabinoid receptors. The annullatin backbone 2-hydroxymethyl-3- pentylphenol is assembled from one acetyl-CoA starter unit and 5 malonyl-CoA elongation units by cooperation of the highly reducing polyketide synthase anuA, the short-chain dehydrogenase anuB and the oxidoreductase anuC, before being hydroxylated at the C-5 alkyl chain by the cytochrome P450 monooxygenase anuE to form (8S)-annullatin E. The prenyltransferase anuH subsequently installs one isoprenyl group at the benzene ring to form (8S)-annullatin J. Enzymatic or nonenzymatic dihydro-benzofuran ring formation between the prenyl and the phenolic hydroxyl groups in (8S)-annullatin J results in two diastereomers (2S,9S)-annullatin H and compound 12. The intermediate (2S,9S)- annullatin H is then converted to (2S,9S)-annullatin D by the FAD- linked oxidoreductase anuG-catalyzed five-member lactone ring formation. The isomer 12 acts as a substrate for the short-chain dehydrogenase anuF and is oxidized to (2R)-annullatin F, which is subsequently acetylated by an acetyltransferase leading to (2R)- annullatin G formation. The remaining enzymes identified within the cluster, anuD, anuI and anuJ, seem not to be involved in annullatin biosynthesis (Probable).","This protein is involved in the synthesis of polyketides, which are a class of secondary metabolites. Specifically, it is a polyketide synthase (PKS), which is an enzyme that catalyzes the condensation of acetate units to form polyketides.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004312; GO:0016491,GO:0016746,,,,GO:0033797,0.6462,,,,0.6379,2,0.6421,0.3182,no
ANUA_PENRF,W6QDA2,Reference,Eukaryota,2130,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of annullatin D, an alkylated aromatic polyketide with a fused dihydrobenzofuran lactone ring system that exhibits potent agonistic activities toward the cannabinoid receptors. The annullatin backbone 2-hydroxymethyl-3- pentylphenol is assembled from one acetyl-CoA starter unit and 5 malonyl-CoA elongation units by cooperation of the highly reducing polyketide synthase anuA, the short-chain dehydrogenase anuB and the oxidoreductase anuC, before being hydroxylated at the C-5 alkyl chain by the cytochrome P450 monooxygenase anuE to form (8S)-annullatin E. The prenyltransferase anuH subsequently installs one isoprenyl group at the benzene ring to form (8S)-annullatin J. Enzymatic or nonenzymatic dihydro-benzofuran ring formation between the prenyl and the phenolic hydroxyl groups in (8S)-annullatin J results in two diastereomers (2S,9S)-annullatin H and compound 12. The intermediate (2S,9S)- annullatin H is then converted to (2S,9S)-annullatin D by the FAD- linked oxidoreductase anuG-catalyzed five-member lactone ring formation. The isomer 12 acts as a substrate for the short-chain dehydrogenase anuF and is oxidized to (2R)-annullatin F, which is subsequently acetylated by an acetyltransferase leading to (2R)- annullatin G formation. The remaining enzymes identified within the cluster, anuD, anuI and anuJ, seem not to be involved in annullatin biosynthesis (Probable).","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of annullatin D, an alkylated aromatic polyketide with a fused dihydrobenzofuran lactone ring system that exhibits potent agonistic activities toward the cannabinoid receptors. The annullatin backbone 2-hydroxymethyl-3- pentylphenol is assembled from one acetyl-CoA starter unit and 5 malonyl-CoA elongation units by cooperation of the highly reducing polyketide synthase anuA, the short-chain dehydrogenase anuB and the oxidoreductase anuC, before being hydroxylated at the C-5 alkyl chain by the cytochrome P450 monooxygenase anuE to form (8S)-annullatin E. The prenyltransferase anuH subsequently installs one isoprenyl group at the benzene ring to form (8S)-annullatin J. Enzymatic or nonenzymatic dihydro-benzofuran ring formation between the prenyl and the phenolic hydroxyl groups in (8S)-annullatin J results in two diastereomers (2S,9S)-annullatin H and compound 12. The intermediate (2S,9S)- annullatin H is then converted to (2S,9S)-annullatin D by the FAD- linked oxidoreductase anuG-catalyzed five-member lactone ring formation. The isomer 12 acts as a substrate for the short-chain dehydrogenase anuF and is oxidized to (2R)-annullatin F, which is subsequently acetylated by an acetyltransferase leading to (2R)- annullatin G formation. The remaining enzymes identified within the cluster, anuD, anuI and anuJ, seem not to be involved in annullatin biosynthesis (Probable).",,,,,,,GO:0004312; GO:0016491,GO:0016740,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.598,0.6462,0.6462,0.7078,0.6462,5,0.6489,0.3182,no
RUSA_PENRF,W6QN79,ESM2Text,Eukaryota,2355,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the N-hydroxyethylisoindolinone derivatives roquesalins. RusA catalyzes the first step of the pathway by condensing one acetyl-CoA starter unit and 5 malonyl-CoA elongation units and releases stachysalicyloid D in association with the short-chain dehydrogenase rusB, the oxidoreductase rusC and the short-chain dehydrogenase rusD. The biosynthesis begins with the roquesalin backbone assembly by the cooperation of the highly reducing polyketide synthase rusA, the short- chain dehydrogenase rusB, the oxidoreductase rusC and the short-chain dehydrogenase rusD and released as stachysalicyloid D. Stachysalicyloid D can be reduced to stachysalicyloid B by an unknown enzyme and the FAD-linked oxidoreductase rusE oxidizes stachysalicyloid B back to stachysalicyloid D to ensure the oxidation state of the backbone for further reactions. After the oxidation at C-8 by the membrane-bound cytochrome P450 monooxygenase rusF, the widely distributed ethanolamine in the cell membrane can be loaded onto the alkyl salicylaldehyde scaffold to form an isoindole intermediate. Hydroxylation at C-10 catalyzed by the FAD-linked oxidoreductase rusG completes the biosynthesis of major pathway product roquesalin B.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential tr",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004315; GO:0004312,,GO:0016746,,,,,0.729,,,,1,0.729,0.288,no
RUSA_PENRF,W6QN79,Prot2Text,Eukaryota,2355,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the N-hydroxyethylisoindolinone derivatives roquesalins. RusA catalyzes the first step of the pathway by condensing one acetyl-CoA starter unit and 5 malonyl-CoA elongation units and releases stachysalicyloid D in association with the short-chain dehydrogenase rusB, the oxidoreductase rusC and the short-chain dehydrogenase rusD. The biosynthesis begins with the roquesalin backbone assembly by the cooperation of the highly reducing polyketide synthase rusA, the short- chain dehydrogenase rusB, the oxidoreductase rusC and the short-chain dehydrogenase rusD and released as stachysalicyloid D. Stachysalicyloid D can be reduced to stachysalicyloid B by an unknown enzyme and the FAD-linked oxidoreductase rusE oxidizes stachysalicyloid B back to stachysalicyloid D to ensure the oxidation state of the backbone for further reactions. After the oxidation at C-8 by the membrane-bound cytochrome P450 monooxygenase rusF, the widely distributed ethanolamine in the cell membrane can be loaded onto the alkyl salicylaldehyde scaffold to form an isoindole intermediate. Hydroxylation at C-10 catalyzed by the FAD-linked oxidoreductase rusG completes the biosynthesis of major pathway product roquesalin B.","Dehydrogenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",No,No,Maybe,No,No,not-Yes,GO:0004315; GO:0004312,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.3552,0.3552,0.3552,0.3552,0.3552,5,0.3552,0.288,no
RUSA_PENRF,W6QN79,ProtT3,Eukaryota,2355,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the N-hydroxyethylisoindolinone derivatives roquesalins. RusA catalyzes the first step of the pathway by condensing one acetyl-CoA starter unit and 5 malonyl-CoA elongation units and releases stachysalicyloid D in association with the short-chain dehydrogenase rusB, the oxidoreductase rusC and the short-chain dehydrogenase rusD. The biosynthesis begins with the roquesalin backbone assembly by the cooperation of the highly reducing polyketide synthase rusA, the short- chain dehydrogenase rusB, the oxidoreductase rusC and the short-chain dehydrogenase rusD and released as stachysalicyloid D. Stachysalicyloid D can be reduced to stachysalicyloid B by an unknown enzyme and the FAD-linked oxidoreductase rusE oxidizes stachysalicyloid B back to stachysalicyloid D to ensure the oxidation state of the backbone for further reactions. After the oxidation at C-8 by the membrane-bound cytochrome P450 monooxygenase rusF, the widely distributed ethanolamine in the cell membrane can be loaded onto the alkyl salicylaldehyde scaffold to form an isoindole intermediate. Hydroxylation at C-10 catalyzed by the FAD-linked oxidoreductase rusG completes the biosynthesis of major pathway product roquesalin B.",Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004315; GO:0004312,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016747,0.729,0.729,0.729,0.8582,0.8582,5,0.7807,0.288,no
RUSA_PENRF,W6QN79,ProtTale,Eukaryota,2355,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the N-hydroxyethylisoindolinone derivatives roquesalins. RusA catalyzes the first step of the pathway by condensing one acetyl-CoA starter unit and 5 malonyl-CoA elongation units and releases stachysalicyloid D in association with the short-chain dehydrogenase rusB, the oxidoreductase rusC and the short-chain dehydrogenase rusD. The biosynthesis begins with the roquesalin backbone assembly by the cooperation of the highly reducing polyketide synthase rusA, the short- chain dehydrogenase rusB, the oxidoreductase rusC and the short-chain dehydrogenase rusD and released as stachysalicyloid D. Stachysalicyloid D can be reduced to stachysalicyloid B by an unknown enzyme and the FAD-linked oxidoreductase rusE oxidizes stachysalicyloid B back to stachysalicyloid D to ensure the oxidation state of the backbone for further reactions. After the oxidation at C-8 by the membrane-bound cytochrome P450 monooxygenase rusF, the widely distributed ethanolamine in the cell membrane can be loaded onto the alkyl salicylaldehyde scaffold to form an isoindole intermediate. Hydroxylation at C-10 catalyzed by the FAD-linked oxidoreductase rusG completes the biosynthesis of major pathway product roquesalin B.","Highly reducing polyketide synthase (HR-PKS); part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. Within the pathway, ptmC catalyzes the conversion of 13-dehydro-penitrem D1 to penitrem E1. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3-glycerol phosphate with GGPP by ptm",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004315; GO:0004312,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016746,0.729,0.729,0.729,0.729,0.729,5,0.729,0.288,no
RUSA_PENRF,W6QN79,Protein2Text,Eukaryota,2355,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the N-hydroxyethylisoindolinone derivatives roquesalins. RusA catalyzes the first step of the pathway by condensing one acetyl-CoA starter unit and 5 malonyl-CoA elongation units and releases stachysalicyloid D in association with the short-chain dehydrogenase rusB, the oxidoreductase rusC and the short-chain dehydrogenase rusD. The biosynthesis begins with the roquesalin backbone assembly by the cooperation of the highly reducing polyketide synthase rusA, the short- chain dehydrogenase rusB, the oxidoreductase rusC and the short-chain dehydrogenase rusD and released as stachysalicyloid D. Stachysalicyloid D can be reduced to stachysalicyloid B by an unknown enzyme and the FAD-linked oxidoreductase rusE oxidizes stachysalicyloid B back to stachysalicyloid D to ensure the oxidation state of the backbone for further reactions. After the oxidation at C-8 by the membrane-bound cytochrome P450 monooxygenase rusF, the widely distributed ethanolamine in the cell membrane can be loaded onto the alkyl salicylaldehyde scaffold to form an isoindole intermediate. Hydroxylation at C-10 catalyzed by the FAD-linked oxidoreductase rusG completes the biosynthesis of major pathway product roquesalin B.","The molecular function of this protein is not explicitly stated in the provided information. However, based on the fact that it is classified as a protein that is involved in the biosynthesis of a fatty acid, it is likely that its molecular function is related to the synthesis or modification of fatty acids. 

More specifically, it is a type of fatty acid synthase, which is a multi-enzyme complex that catalyzes the formation of fatty acids from acetyl-CoA and malonyl-CoA. This protein is likely to be a component of this complex, and its molecular function would be to catalyze a specific step in the fatty acid synthesis pathway. 

Without more specific information, it is difficult to determine the exact molecular function of this protein. If you have any additional information or context, I may be able to provide a more specific answer.",Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0004315; GO:0004312,GO:0004312,GO:0004312,GO:0004312,,GO:0004312,0.9096,0.9096,0.9096,,0.9096,4,0.9096,0.288,no
RUSA_PENRF,W6QN79,Reference,Eukaryota,2355,"Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the N-hydroxyethylisoindolinone derivatives roquesalins. RusA catalyzes the first step of the pathway by condensing one acetyl-CoA starter unit and 5 malonyl-CoA elongation units and releases stachysalicyloid D in association with the short-chain dehydrogenase rusB, the oxidoreductase rusC and the short-chain dehydrogenase rusD. The biosynthesis begins with the roquesalin backbone assembly by the cooperation of the highly reducing polyketide synthase rusA, the short- chain dehydrogenase rusB, the oxidoreductase rusC and the short-chain dehydrogenase rusD and released as stachysalicyloid D. Stachysalicyloid D can be reduced to stachysalicyloid B by an unknown enzyme and the FAD-linked oxidoreductase rusE oxidizes stachysalicyloid B back to stachysalicyloid D to ensure the oxidation state of the backbone for further reactions. After the oxidation at C-8 by the membrane-bound cytochrome P450 monooxygenase rusF, the widely distributed ethanolamine in the cell membrane can be loaded onto the alkyl salicylaldehyde scaffold to form an isoindole intermediate. Hydroxylation at C-10 catalyzed by the FAD-linked oxidoreductase rusG completes the biosynthesis of major pathway product roquesalin B.","Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the N-hydroxyethylisoindolinone derivatives roquesalins. RusA catalyzes the first step of the pathway by condensing one acetyl-CoA starter unit and 5 malonyl-CoA elongation units and releases stachysalicyloid D in association with the short-chain dehydrogenase rusB, the oxidoreductase rusC and the short-chain dehydrogenase rusD. The biosynthesis begins with the roquesalin backbone assembly by the cooperation of the highly reducing polyketide synthase rusA, the short- chain dehydrogenase rusB, the oxidoreductase rusC and the short-chain dehydrogenase rusD and released as stachysalicyloid D. Stachysalicyloid D can be reduced to stachysalicyloid B by an unknown enzyme and the FAD-linked oxidoreductase rusE oxidizes stachysalicyloid B back to stachysalicyloid D to ensure the oxidation state of the backbone for further reactions. After the oxidation at C-8 by the membrane-bound cytochrome P450 monooxygenase rusF, the widely distributed ethanolamine in the cell membrane can be loaded onto the alkyl salicylaldehyde scaffold to form an isoindole intermediate. Hydroxylation at C-10 catalyzed by the FAD-linked oxidoreductase rusG completes the biosynthesis of major pathway product roquesalin B.",,,,,,,GO:0004315; GO:0004312,GO:0016740,GO:0016746,GO:0016746,GO:0016747,GO:0016746,0.6019,0.729,0.729,0.8582,0.729,5,0.7294,0.288,no
ZBD1_GIBM7,W7L9C2,ESM2Text,Eukaryota,364,"Zinc-binding dehydrogenase that acts as a genetic repressor of fumonisin production. With the ABC-type transporter ABC3, is involved in tolerance to pyrrocidines, inhibitors of growth of Gibberella moniliformis produced by the competitor fungus Sarocladium zeae. Under pyrrocidine challenge, abundant ZBD1 sequesters zinc, and decreases zinc availability in the cell, thereby inhibiting fumonisin biosynthesis via competitive inhibition of FUM21 (Probable). ZBD1 enzyme is then active and abundantly present in the cytoplasm where its enoyl reductase domain may detoxify pyrrocidine A by reducing its double-bonded lactam ring to yield pyrrocidine B, at which point the ABC-type transporter ABC3 can then effectively pump pyrrocidine B out of the cell (Probable).","Component of the seco-iridoid and derivatives monoterpenoid indole alkaloids (MIAs, e.g. vinblastine, catharanthine, tabersonine, vincadifformine, quinine and strychnine) biosynthesis pathway. Catalyzes the conversion of loganin into secologanin A.",No,No,No,Maybe,Maybe,not-Yes,GO:0070402; GO:0016651,GO:0004497,GO:0004497,GO:0016491,GO:0004497,GO:0004497,0.4698,0.4698,0.5783,0.4698,0.4698,5,0.4915,0.146,no
ZBD1_GIBM7,W7L9C2,Prot2Text,Eukaryota,364,"Zinc-binding dehydrogenase that acts as a genetic repressor of fumonisin production. With the ABC-type transporter ABC3, is involved in tolerance to pyrrocidines, inhibitors of growth of Gibberella moniliformis produced by the competitor fungus Sarocladium zeae. Under pyrrocidine challenge, abundant ZBD1 sequesters zinc, and decreases zinc availability in the cell, thereby inhibiting fumonisin biosynthesis via competitive inhibition of FUM21 (Probable). ZBD1 enzyme is then active and abundantly present in the cytoplasm where its enoyl reductase domain may detoxify pyrrocidine A by reducing its double-bonded lactam ring to yield pyrrocidine B, at which point the ABC-type transporter ABC3 can then effectively pump pyrrocidine B out of the cell (Probable).","Dehydrogenase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0070402; GO:0016651,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.5783,0.5783,0.5783,0.5783,0.5783,5,0.5783,0.146,no
ZBD1_GIBM7,W7L9C2,ProtT3,Eukaryota,364,"Zinc-binding dehydrogenase that acts as a genetic repressor of fumonisin production. With the ABC-type transporter ABC3, is involved in tolerance to pyrrocidines, inhibitors of growth of Gibberella moniliformis produced by the competitor fungus Sarocladium zeae. Under pyrrocidine challenge, abundant ZBD1 sequesters zinc, and decreases zinc availability in the cell, thereby inhibiting fumonisin biosynthesis via competitive inhibition of FUM21 (Probable). ZBD1 enzyme is then active and abundantly present in the cytoplasm where its enoyl reductase domain may detoxify pyrrocidine A by reducing its double-bonded lactam ring to yield pyrrocidine B, at which point the ABC-type transporter ABC3 can then effectively pump pyrrocidine B out of the cell (Probable).","Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of notoamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first step of notoamide biosynthesis involves coupling of L-proline and L-tryptophan by the bimodular NRPS notE, to produce cyclo-L-tryptophan-L-proline called brevianamide F . The reverse pre",No,Maybe,Maybe,No,Maybe,not-Yes,GO:0070402; GO:0016651,GO:0016631,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.3424,0.5783,0.5783,0.5783,0.5783,5,0.5311,0.146,no
ZBD1_GIBM7,W7L9C2,ProtTale,Eukaryota,364,"Zinc-binding dehydrogenase that acts as a genetic repressor of fumonisin production. With the ABC-type transporter ABC3, is involved in tolerance to pyrrocidines, inhibitors of growth of Gibberella moniliformis produced by the competitor fungus Sarocladium zeae. Under pyrrocidine challenge, abundant ZBD1 sequesters zinc, and decreases zinc availability in the cell, thereby inhibiting fumonisin biosynthesis via competitive inhibition of FUM21 (Probable). ZBD1 enzyme is then active and abundantly present in the cytoplasm where its enoyl reductase domain may detoxify pyrrocidine A by reducing its double-bonded lactam ring to yield pyrrocidine B, at which point the ABC-type transporter ABC3 can then effectively pump pyrrocidine B out of the cell (Probable).","Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of oxaleimides, cytotoxic compounds containing an unusual disubstituted succinimide moiety. The first step of the pathway is provided by the HR-PKS poxF that serves in a new mode of collaborative biosynthesis with the PKS-NRPS poxE, by providing the olefin containing amino acid substrate via the synthesis of an ACP- bound dec-4-enoate. The cytochrome P450 monooxygenase poxM-catalyzed oxidation at the alpha-position creates the enzyme-bound 2-hydroxydec-4-enoyl-",No,Maybe,Maybe,No,Maybe,not-Yes,GO:0070402; GO:0016651,GO:0016491,GO:0016491,GO:0016491,GO:0016631,GO:0016491,0.5783,0.5783,0.5783,0.3424,0.5783,5,0.5311,0.146,no
ZBD1_GIBM7,W7L9C2,Protein2Text,Eukaryota,364,"Zinc-binding dehydrogenase that acts as a genetic repressor of fumonisin production. With the ABC-type transporter ABC3, is involved in tolerance to pyrrocidines, inhibitors of growth of Gibberella moniliformis produced by the competitor fungus Sarocladium zeae. Under pyrrocidine challenge, abundant ZBD1 sequesters zinc, and decreases zinc availability in the cell, thereby inhibiting fumonisin biosynthesis via competitive inhibition of FUM21 (Probable). ZBD1 enzyme is then active and abundantly present in the cytoplasm where its enoyl reductase domain may detoxify pyrrocidine A by reducing its double-bonded lactam ring to yield pyrrocidine B, at which point the ABC-type transporter ABC3 can then effectively pump pyrrocidine B out of the cell (Probable).","The molecular function of this protein is a fatty acid transferase. It is involved in the transfer of fatty acids, specifically in the metabolism of fatty acids.",No,No,Vague,No,No,not-Yes,GO:0070402; GO:0016651,GO:0016746,,,,GO:0016747,0.2891,,,,0.2434,2,0.2662,0.146,no
ZBD1_GIBM7,W7L9C2,Reference,Eukaryota,364,"Zinc-binding dehydrogenase that acts as a genetic repressor of fumonisin production. With the ABC-type transporter ABC3, is involved in tolerance to pyrrocidines, inhibitors of growth of Gibberella moniliformis produced by the competitor fungus Sarocladium zeae. Under pyrrocidine challenge, abundant ZBD1 sequesters zinc, and decreases zinc availability in the cell, thereby inhibiting fumonisin biosynthesis via competitive inhibition of FUM21 (Probable). ZBD1 enzyme is then active and abundantly present in the cytoplasm where its enoyl reductase domain may detoxify pyrrocidine A by reducing its double-bonded lactam ring to yield pyrrocidine B, at which point the ABC-type transporter ABC3 can then effectively pump pyrrocidine B out of the cell (Probable).","Zinc-binding dehydrogenase that acts as a genetic repressor of fumonisin production. With the ABC-type transporter ABC3, is involved in tolerance to pyrrocidines, inhibitors of growth of Gibberella moniliformis produced by the competitor fungus Sarocladium zeae. Under pyrrocidine challenge, abundant ZBD1 sequesters zinc, and decreases zinc availability in the cell, thereby inhibiting fumonisin biosynthesis via competitive inhibition of FUM21 (Probable). ZBD1 enzyme is then active and abundantly present in the cytoplasm where its enoyl reductase domain may detoxify pyrrocidine A by reducing its double-bonded lactam ring to yield pyrrocidine B, at which point the ABC-type transporter ABC3 can then effectively pump pyrrocidine B out of the cell (Probable).",,,,,,,GO:0070402; GO:0016651,GO:0016491,GO:0016491; GO:0008270,GO:0016491,GO:0016491,GO:0016491; GO:0008270,0.5783,0.5498,0.5783,0.5783,0.5498,5,0.5669,0.146,no
OGT2_PHACM,A0A0G2EC47,ESM2Text,Eukaryota,455,"Catalyzes the second glycosylation step during phaeomoniecin D biosynthesis, the further O-galactosylation of exophillic acid (produced by the O-glycosyltransferase OGT1) to yield the 4-O-beta-D- galactoside phaeomoniecin D.","Catalyzes the glycosylation reaction which converts zeaxanthin to chrysanthemol. The reaction proceeds in two steps, an ATP-dependent phosphorylation at the C-8 position, followed by an ATP-dependent phosphorylation at the C-3 position. Has a strong preference for chrysanthemol as the phosphoryl donor. Cannot use UDP-glucose, UDP-galactose, UDP-xylose, UDP-glucuronic acid, UDP-glucuronide, UDP-xylobiose, and UDP-glucuronic acid as substrates.",No,No,No,Maybe,Maybe,not-Yes,GO:0016758; GO:0008194,,,,,,,,,,,0,,0.3543,no
OGT2_PHACM,A0A0G2EC47,Prot2Text,Eukaryota,455,"Catalyzes the second glycosylation step during phaeomoniecin D biosynthesis, the further O-galactosylation of exophillic acid (produced by the O-glycosyltransferase OGT1) to yield the 4-O-beta-D- galactoside phaeomoniecin D.","Involved in the biosynthesis of the exopolysaccharide acetan, a water-soluble polysaccharide involved in production of bacterial cellulose (BC). Catalyzes the addition of a mannose residue from GDP-mannose (GDP-Man) to the position 2 of 3-phospho-D-glycerate (3-PGA) to form beta-D-glucose-3-phosphate-D-glycerate (GPG). It can also use GDP-Man, but at a lower rate than GDP-Fucose. The reaction is reversible, the equilibrium strongly favors the formation of beta-D-glucose-3-phosphate-D-glycerate (GPG).",No,Maybe,No,Maybe,Maybe,not-Yes,GO:0016758; GO:0008194,GO:0016757,GO:0000030,GO:0000030,GO:0016757,GO:0000030,0.8416,0.7731,0.7731,0.8416,0.7731,5,0.8005,0.3543,no
OGT2_PHACM,A0A0G2EC47,ProtT3,Eukaryota,455,"Catalyzes the second glycosylation step during phaeomoniecin D biosynthesis, the further O-galactosylation of exophillic acid (produced by the O-glycosyltransferase OGT1) to yield the 4-O-beta-D- galactoside phaeomoniecin D.",Catalyzes the transfer of glucosamine (GlcN) from UDP-GlcN to 3-O-beta-D-glucopyranosyl-N-acetyl-D-glucosamine (GlcNAc-GlcN) to form 3-O-beta-D-glucopyranosyl-N-acetyl-3-O-beta-D- glucopyranosyl-N-acetyl-glucosamine (GlcNAc-GlcNAc-GlcN). Belongs to the glycosyltransferase 2 family,No,Maybe,No,Maybe,Maybe,not-Yes,GO:0016758; GO:0008194,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.8416,0.8416,0.8416,0.8416,0.8416,5,0.8416,0.3543,no
OGT2_PHACM,A0A0G2EC47,ProtTale,Eukaryota,455,"Catalyzes the second glycosylation step during phaeomoniecin D biosynthesis, the further O-galactosylation of exophillic acid (produced by the O-glycosyltransferase OGT1) to yield the 4-O-beta-D- galactoside phaeomoniecin D.","Catalyzes the addition of beta-D-mannose 1,4-beta-D- glucopyranoside to N-acetyl-D-glucosamine (GlcNAc) to form GlcNAc-beta-1,4-(1->6)-beta-D- mannosyl-(1<->6)-GlcNAc. In vitro, can also use GlcNAc-beta-1,4-(1->6)-beta-D- mannosyl-(1<->6)-GlcNAc as a donor substrate.",No,Maybe,No,Maybe,Maybe,not-Yes,GO:0016758; GO:0008194,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.8416,0.8416,0.8416,0.8416,0.8416,5,0.8416,0.3543,no
OGT2_PHACM,A0A0G2EC47,Protein2Text,Eukaryota,455,"Catalyzes the second glycosylation step during phaeomoniecin D biosynthesis, the further O-galactosylation of exophillic acid (produced by the O-glycosyltransferase OGT1) to yield the 4-O-beta-D- galactoside phaeomoniecin D.","The molecular function of this protein is an enzyme that catalyzes the conversion of certain organic compounds. Specifically, it is involved in the biosynthesis of plant secondary metabolites, and it may play a role in the production of terpenoids, a class of compounds that have been shown to have various biological activities. The exact molecular function of this protein is likely to be a cytochrome P450 monooxygenase, which is a type of enzyme that uses molecular oxygen to catalyze the oxidation of organic compounds. However, the specific function of this protein is not well-characterized and may require further research to determine its exact role in the biosynthesis of plant secondary metabolites.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0016758; GO:0008194,GO:0004497,GO:0004497; GO:0020037,GO:0004497,GO:0004497,GO:0004497,0.3284,0.2828,0.3284,0.3284,0.3284,5,0.3193,0.3543,no
OGT2_PHACM,A0A0G2EC47,Reference,Eukaryota,455,"Catalyzes the second glycosylation step during phaeomoniecin D biosynthesis, the further O-galactosylation of exophillic acid (produced by the O-glycosyltransferase OGT1) to yield the 4-O-beta-D- galactoside phaeomoniecin D.","Catalyzes the second glycosylation step during phaeomoniecin D biosynthesis, the further O-galactosylation of exophillic acid (produced by the O-glycosyltransferase OGT1) to yield the 4-O-beta-D- galactoside phaeomoniecin D.",,,,,,,GO:0016758; GO:0008194,GO:0008378,GO:0008378,GO:0008378,GO:0008378,GO:0016757,0.7731,0.7731,0.7731,0.7731,0.8416,5,0.7868,0.3543,no
JAND_ESCWE,A0A0M8MZA1,ESM2Text,Eukaryota,413,"Aromatic prenyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpene shearinine D, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Shearinine D inhibits the ant defensive actinobacterial symbiont Pseudonocardia and reduces worker behavioral defenses and is ultimately lethal when it accumulates in ant tissues. The geranylgeranyl diphosphate (GGPP) synthase janG catalyzes the first step in shearinine D biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase janC then forms 3- geranylgeranylindole (3-GGI). Epoxidation by the FAD-dependent monooxygenase janM leads to a epoxidized-GGI that is substrate of the terpene cyclase janB for cyclization to yield paspaline. Paspaline is subsequently converted the cytochrome P450 monooxygenases janP and janQ, as well as by the indole diterpene prenyltransferase janD and probably additional enzymes for oxidation and cyclization to generate shearinine D (Probable).","Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The nonribosomal peptide synthetase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin. The function of ktnA within the pathway has not been determined yet.",No,No,No,No,No,not-Yes,GO:0016765,GO:0016874,GO:0016874,,,,0.4807,0.4807,,,,2,0.4807,0.2468,no
JAND_ESCWE,A0A0M8MZA1,Prot2Text,Eukaryota,413,"Aromatic prenyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpene shearinine D, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Shearinine D inhibits the ant defensive actinobacterial symbiont Pseudonocardia and reduces worker behavioral defenses and is ultimately lethal when it accumulates in ant tissues. The geranylgeranyl diphosphate (GGPP) synthase janG catalyzes the first step in shearinine D biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase janC then forms 3- geranylgeranylindole (3-GGI). Epoxidation by the FAD-dependent monooxygenase janM leads to a epoxidized-GGI that is substrate of the terpene cyclase janB for cyclization to yield paspaline. Paspaline is subsequently converted the cytochrome P450 monooxygenases janP and janQ, as well as by the indole diterpene prenyltransferase janD and probably additional enzymes for oxidation and cyclization to generate shearinine D (Probable).","Dehydrogenase involved in the conversion of monodictyphenone to the prenyl xanthones such as emericellin, shamixanthone and epishamixanthone. Monodictyphenone is first converted to variecoxanthone A via a paeciloxanthone intermediate by the consecutive actions of the FAD-dependent monooxygenase mdpD and the xanthone prenyltransferase xptB. XptB catalyzes regular O-prenylation at the hydroxy group of C-7 of the xanthone ring. Variecoxanthone A is further prenylated to emericellin by xptA before being reduced to shamixanthone and epishamixanthone by the dehydrogenase xptC.",No,No,No,No,No,not-Yes,GO:0016765,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4807,0.4807,0.4807,0.4807,0.4807,5,0.4807,0.2468,no
JAND_ESCWE,A0A0M8MZA1,ProtT3,Eukaryota,413,"Aromatic prenyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpene shearinine D, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Shearinine D inhibits the ant defensive actinobacterial symbiont Pseudonocardia and reduces worker behavioral defenses and is ultimately lethal when it accumulates in ant tissues. The geranylgeranyl diphosphate (GGPP) synthase janG catalyzes the first step in shearinine D biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase janC then forms 3- geranylgeranylindole (3-GGI). Epoxidation by the FAD-dependent monooxygenase janM leads to a epoxidized-GGI that is substrate of the terpene cyclase janB for cyclization to yield paspaline. Paspaline is subsequently converted the cytochrome P450 monooxygenases janP and janQ, as well as by the indole diterpene prenyltransferase janD and probably additional enzymes for oxidation and cyclization to generate shearinine D (Probable).","Prenyltransferase; part of the gene cluster that mediates the biosynthesis of the host-selective toxins (HSTs) AF-toxins responsible for Alternaria black spot of strawberry disease by the strawberry pathotype . AF-toxins are cyclic depsipeptides containing the 3 residues 2-hydroxy-isovaleric acid (2-HIV), dehydroalanine, L-alanine which are common for all 3 AF-toxins I to III. The fourth precursor is L-alpha-amino-methoxy-valeric acid (",Maybe,Maybe,Maybe,Yes,Yes,not-Yes,GO:0016765,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,0.8416,0.8416,0.8416,0.8416,0.8416,5,0.8416,0.2468,no
JAND_ESCWE,A0A0M8MZA1,ProtTale,Eukaryota,413,"Aromatic prenyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpene shearinine D, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Shearinine D inhibits the ant defensive actinobacterial symbiont Pseudonocardia and reduces worker behavioral defenses and is ultimately lethal when it accumulates in ant tissues. The geranylgeranyl diphosphate (GGPP) synthase janG catalyzes the first step in shearinine D biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase janC then forms 3- geranylgeranylindole (3-GGI). Epoxidation by the FAD-dependent monooxygenase janM leads to a epoxidized-GGI that is substrate of the terpene cyclase janB for cyclization to yield paspaline. Paspaline is subsequently converted the cytochrome P450 monooxygenases janP and janQ, as well as by the indole diterpene prenyltransferase janD and probably additional enzymes for oxidation and cyclization to generate shearinine D (Probable).",Facilitates virus attachment to plant cells. May be involved in virus movement.,No,No,No,No,No,not-Yes,GO:0016765,,,,,,,,,,,0,,0.2468,no
JAND_ESCWE,A0A0M8MZA1,Protein2Text,Eukaryota,413,"Aromatic prenyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpene shearinine D, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Shearinine D inhibits the ant defensive actinobacterial symbiont Pseudonocardia and reduces worker behavioral defenses and is ultimately lethal when it accumulates in ant tissues. The geranylgeranyl diphosphate (GGPP) synthase janG catalyzes the first step in shearinine D biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase janC then forms 3- geranylgeranylindole (3-GGI). Epoxidation by the FAD-dependent monooxygenase janM leads to a epoxidized-GGI that is substrate of the terpene cyclase janB for cyclization to yield paspaline. Paspaline is subsequently converted the cytochrome P450 monooxygenases janP and janQ, as well as by the indole diterpene prenyltransferase janD and probably additional enzymes for oxidation and cyclization to generate shearinine D (Probable).","The molecular function of this protein is that of a prenyltransferase, which is involved in the biosynthesis of prenylated compounds. More specifically, it is involved in the synthesis of prenylated compounds such as carotenoids and related compounds.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016765,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,0.8416,0.8416,0.8416,0.8416,0.8416,5,0.8416,0.2468,no
JAND_ESCWE,A0A0M8MZA1,Reference,Eukaryota,413,"Aromatic prenyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpene shearinine D, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Shearinine D inhibits the ant defensive actinobacterial symbiont Pseudonocardia and reduces worker behavioral defenses and is ultimately lethal when it accumulates in ant tissues. The geranylgeranyl diphosphate (GGPP) synthase janG catalyzes the first step in shearinine D biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase janC then forms 3- geranylgeranylindole (3-GGI). Epoxidation by the FAD-dependent monooxygenase janM leads to a epoxidized-GGI that is substrate of the terpene cyclase janB for cyclization to yield paspaline. Paspaline is subsequently converted the cytochrome P450 monooxygenases janP and janQ, as well as by the indole diterpene prenyltransferase janD and probably additional enzymes for oxidation and cyclization to generate shearinine D (Probable).","Aromatic prenyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpene shearinine D, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Shearinine D inhibits the ant defensive actinobacterial symbiont Pseudonocardia and reduces worker behavioral defenses and is ultimately lethal when it accumulates in ant tissues. The geranylgeranyl diphosphate (GGPP) synthase janG catalyzes the first step in shearinine D biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase janC then forms 3- geranylgeranylindole (3-GGI). Epoxidation by the FAD-dependent monooxygenase janM leads to a epoxidized-GGI that is substrate of the terpene cyclase janB for cyclization to yield paspaline. Paspaline is subsequently converted the cytochrome P450 monooxygenases janP and janQ, as well as by the indole diterpene prenyltransferase janD and probably additional enzymes for oxidation and cyclization to generate shearinine D (Probable).",,,,,,,GO:0016765,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,0.8416,0.8416,0.8416,0.8416,0.8416,5,0.8416,0.2468,no
ETPG_ESCWE,A0A0M8N8I0,ESM2Text,Eukaryota,239,"Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster- specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","Glutathione S-transferase-like protein; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004364,,GO:0004364,GO:0004364,,GO:0004364,,1.0,1.0,,1.0,3,1.0,0.3575,no
ETPG_ESCWE,A0A0M8N8I0,Prot2Text,Eukaryota,239,"Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster- specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of aspirochlorine (or antibiotic A30641), an unusual halogenated spiro compound with distinctive antifungal properties due to selective inhibition of protein biosynthesis, and which is also active against bacteria, viruses, and murine tumor cells. The non-ribosomal peptide synthetase (NRPS) aclP is responsible the formation of the diketopiperazine (DKP) core from the condensation of 2 phenylalanine residues. One Phe residue is tailored into chlorotyrosine by hydroxylation and chlorination, whereas the second Phe undergoes an unprecedented C-C bond cleavage to be converted into glycine. After formation of the DKP, sulfur is incorporated into the DKP by conjugation with glutathione by aclG, followed by its stepwise degradation to the thiol by aclI, aclJ and aclK, and the dithiol oxidation by aclT. In addition, oxygenases (aclB, aclC, aclL and aclO) and O-methyltransferases (aclM and a",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004364,GO:0004364,GO:0004364,GO:0004364,GO:0004364,GO:0004364,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3575,no
ETPG_ESCWE,A0A0M8N8I0,ProtT3,Eukaryota,239,"Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster- specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004364,GO:0004364,GO:0004364,GO:0004364,GO:0004364,GO:0004364,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3575,no
ETPG_ESCWE,A0A0M8N8I0,ProtTale,Eukaryota,239,"Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster- specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","Glutamate-S-transferase-like protein; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004364,,,GO:0004364,,,,,1.0,,,1,1.0,0.3575,no
ETPG_ESCWE,A0A0M8N8I0,Protein2Text,Eukaryota,239,"Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster- specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","The molecular function of this protein is glutathione S-transferase activity. It is involved in the conjugation of glutathione to a wide variety of endogenous and exogenous electrophilic compounds, which helps to detoxify these compounds and protect the cell from oxidative stress.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004364,GO:0004364,GO:0004364,GO:0004364,GO:0004364,GO:0004364,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3575,no
ETPG_ESCWE,A0A0M8N8I0,Reference,Eukaryota,239,"Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster- specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","Glutathione S-transferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster- specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).",,,,,,,GO:0004364,GO:0004364,GO:0004364,GO:0004364,GO:0004364,GO:0004364,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3575,no
ETPK_ESCWE,A0A0M8N9Q3,ESM2Text,Eukaryota,122,"Gamma-glutamyl cyclotransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster- specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","Enzyme of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein).",No,No,No,No,No,not-Yes,GO:0016740,GO:0004190,GO:0004190,GO:0004190,GO:0004175,GO:0004190,0.2926,0.2926,0.2926,0.3666,0.2926,5,0.3074,0.4869,no
ETPK_ESCWE,A0A0M8N9Q3,Prot2Text,Eukaryota,122,"Gamma-glutamyl cyclotransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster- specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).",Accepts the ubiquitin-like protein NEDD8/RUB1 from the UBA3-ULA1 E1 complex and catalyzes its covalent attachment to other proteins.,No,No,No,No,No,not-Yes,GO:0016740,GO:0061650,GO:0061650,GO:0061656,,GO:0061650,0.5122,0.5122,0.4286,,0.5122,4,0.4913,0.4869,no
ETPK_ESCWE,A0A0M8N9Q3,ProtT3,Eukaryota,122,"Gamma-glutamyl cyclotransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster- specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol- cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water",No,No,No,No,No,not-Yes,GO:0016740,GO:0004129; GO:0005507; GO:0020037,GO:0004129,GO:0004129,GO:0004129; GO:0020037,GO:0004129,0.1691,0.1204,0.1204,0.1826,0.1204,5,0.1426,0.4869,no
ETPK_ESCWE,A0A0M8N9Q3,ProtTale,Eukaryota,122,"Gamma-glutamyl cyclotransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster- specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","Plays a role in the inhibition of the host NF-kappa-B pathway. This inhibition occurs at the receptor level, by preventing the signaling of TNFRSF12A/TNFR1 and TNFRSF12B/TNFR2.",No,No,No,No,No,not-Yes,GO:0016740,,,,,,,,,,,0,,0.4869,no
ETPK_ESCWE,A0A0M8N9Q3,Protein2Text,Eukaryota,122,"Gamma-glutamyl cyclotransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster- specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).",This protein is involved in the molecular function of catalyzing the hydrolysis of the diphosphate ester bond in compounds containing a diphosphate group.,No,No,No,No,No,not-Yes,GO:0016740,GO:0016462,GO:0004427,,,GO:0016462,0.3552,0.3176,,,0.3552,3,0.3427,0.4869,no
ETPK_ESCWE,A0A0M8N9Q3,Reference,Eukaryota,122,"Gamma-glutamyl cyclotransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster- specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","Gamma-glutamyl cyclotransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster- specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).",,,,,,,GO:0016740,GO:0003839,GO:0003839,GO:0003839,GO:0003839,GO:0003839,0.3552,0.3552,0.3552,0.3552,0.3552,5,0.3552,0.4869,no
EMOM_ESCWE,A0A0M9VUJ4,ESM2Text,Eukaryota,192,"Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of emodin, a minor compound produced during pathogenesis. Within the pathway, mdpH-2 catalyzes the oxidation of emodinanthrone to emodin (Probable). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) emoG. The atrochrysone carboxyl ACP thioesterase emoF then breaks the thioester bond and releases the atrochrysone carboxylic acid from emoG. Decarboxylation by emoH and dehydration by emoM complete emodin production (Probable).",Hydrolysis of the beta-barrel phosphoanhydride bond of phosphatidylcholine at the C-terminal position to form phosphatidylcholine and choline.,No,No,Yes,No,No,not-Yes,GO:0004497,,GO:0016787,,GO:0016787,,,0.4807,,0.4807,,2,0.4807,0.453,no
EMOM_ESCWE,A0A0M9VUJ4,Prot2Text,Eukaryota,192,"Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of emodin, a minor compound produced during pathogenesis. Within the pathway, mdpH-2 catalyzes the oxidation of emodinanthrone to emodin (Probable). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) emoG. The atrochrysone carboxyl ACP thioesterase emoF then breaks the thioester bond and releases the atrochrysone carboxylic acid from emoG. Decarboxylation by emoH and dehydration by emoM complete emodin production (Probable).","Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of a family of the mycotoxins cytochalasins E and K. The hybrid PKS-NRPS synthetase ccsA and the enoyl reductase ccsC are responsible for fusion of phenylalanine with an octaketide backbone and subsequent release of the stable tetramic acid precursor. The polyketide synthase module (PKS) of the PKS-NRPS ccsA is responsible for the synthesis of the octaketide backbone. The downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the octaketide with a phenylalanine. A reductase-like domain (R) at the C-terminus catalyzes the reductive release of the polyketide-amino acid intermediate. Because ccsA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase ccsC. Upon formation of the 11-membered carbocycle-fused perhydroisoindolone intermediate, a number of oxidative steps are required to yield the needed",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004497,GO:0016491,GO:0016705,GO:0016705,GO:0016705,GO:0016491,0.8145,0.6612,0.6612,0.6612,0.8145,5,0.7225,0.453,no
EMOM_ESCWE,A0A0M9VUJ4,ProtT3,Eukaryota,192,"Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of emodin, a minor compound produced during pathogenesis. Within the pathway, mdpH-2 catalyzes the oxidation of emodinanthrone to emodin (Probable). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) emoG. The atrochrysone carboxyl ACP thioesterase emoF then breaks the thioester bond and releases the atrochrysone carboxylic acid from emoG. Decarboxylation by emoH and dehydration by emoM complete emodin production (Probable).",Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeranylindole (3-GGI,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004497,GO:0004497,GO:0016701,GO:0016705,GO:0016702,GO:0016701,1.0,0.6612,0.6612,0.4939,0.6612,5,0.6955,0.453,no
EMOM_ESCWE,A0A0M9VUJ4,ProtTale,Eukaryota,192,"Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of emodin, a minor compound produced during pathogenesis. Within the pathway, mdpH-2 catalyzes the oxidation of emodinanthrone to emodin (Probable). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) emoG. The atrochrysone carboxyl ACP thioesterase emoF then breaks the thioester bond and releases the atrochrysone carboxylic acid from emoG. Decarboxylation by emoH and dehydration by emoM complete emodin production (Probable).","Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the saturated C-C",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004497,GO:0016491,GO:0016705,GO:0016491,GO:0016491; GO:0004497,GO:0016705,0.8145,0.6612,0.8145,0.9382,0.6612,5,0.7779,0.453,no
EMOM_ESCWE,A0A0M9VUJ4,Protein2Text,Eukaryota,192,"Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of emodin, a minor compound produced during pathogenesis. Within the pathway, mdpH-2 catalyzes the oxidation of emodinanthrone to emodin (Probable). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) emoG. The atrochrysone carboxyl ACP thioesterase emoF then breaks the thioester bond and releases the atrochrysone carboxylic acid from emoG. Decarboxylation by emoH and dehydration by emoM complete emodin production (Probable).","This protein is involved in catalyzing the conversion of porphobilinogen to hydroxymethylbilane in the heme biosynthetic pathway. Specifically, it catalyzes the condensation of 4 molecules of porphobilinogen with pyridoxal 5'-phosphate (PLP) to form a hydroxymethylbilane (HMB) in a reaction that involves the formation of a 4-aminobutanone intermediate. It is also involved in the transfer of the HMB to the next enzyme in the pathway for further processing into heme. It can also use other amines such as dopamine and 4-aminobutanal to form adducts with PLP. It also has aminotransferase activity in vitro.
            It is also involved in the regulation of dopamine levels. 
            It is also involved in the regulation of cellular redox state. 
            It is also involved in the regulation of apoptosis. 
            It is also involved in the regulation of cellular proliferation. 
            It is also involved in the regulation of cell migration. 
            It is also involved in the regulation of cell adhesion. 
            It is also involved in the regulation of cell cycle progression. 
            It is also involved in the regulation of the cell cycle. 
            It is also involved in the regulation of cell differentiation. 
            It is also involved in the regulation of cellular senescence. 
            It is also involved in the regulation of the immune response. 
            It is also involved in the regulation of inflammation. 
            It is also involved in the regulation of the inflammatory response. 
            It is also involved in the regulation of the innate immune response. 
            It is also involved in the regulation of the adaptive immune response. 
            It is also involved in the regulation of the humoral immune response. 
            It is also involved in the regulation of the cellular immune response. 
            It is also involved in the regulation of the inflammatory response. 
            It is also involved in the regulation of the immune response. 
            It is also involved in the regulation of the adaptive immune response. 
            It is also involved in the regulation of the humoral immune response. 
            It is also involved in the regulation of the cellular immune response. 
            It is also involved in the regulation of the immune response. 
            It is also involved in the regulation of the inflammatory response. 
            It is also involved in the regulation of the immune",No,No,No,No,No,not-Yes,GO:0004497,GO:0004418,GO:0004418,GO:0004418,GO:0004418,GO:0004418,0.3284,0.3284,0.3284,0.3284,0.3284,5,0.3284,0.453,no
EMOM_ESCWE,A0A0M9VUJ4,Reference,Eukaryota,192,"Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of emodin, a minor compound produced during pathogenesis. Within the pathway, mdpH-2 catalyzes the oxidation of emodinanthrone to emodin (Probable). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) emoG. The atrochrysone carboxyl ACP thioesterase emoF then breaks the thioester bond and releases the atrochrysone carboxylic acid from emoG. Decarboxylation by emoH and dehydration by emoM complete emodin production (Probable).","Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of emodin, a minor compound produced during pathogenesis. Within the pathway, mdpH-2 catalyzes the oxidation of emodinanthrone to emodin (Probable). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) emoG. The atrochrysone carboxyl ACP thioesterase emoF then breaks the thioester bond and releases the atrochrysone carboxylic acid from emoG. Decarboxylation by emoH and dehydration by emoM complete emodin production (Probable).",,,,,,,GO:0004497,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.8145,0.8145,0.8145,0.8145,0.8145,5,0.8145,0.453,no
ETPN_ESCWE,A0A0M9VX54,ESM2Text,Eukaryota,290,"N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","Methyltransferase; part of the gene cluster that mediates the biosynthesis of the tropolone class of fungal maleic anhydrides. The pathway begins with the synthesis of 3-methylorcinaldehyde performed by the non-reducing polyketide synthase (PKS) tropA. 3-methylorcinaldehyde is the substrate for the FAD-dependent monooxygenase tropB to yield a dearomatized hydroxycyclohexadione. The 2-oxoglutarate-dependent dioxygenase tropC then performs the oxidative ring expansion to provide the first tropolone metabolite stipitaldehyde. Trop D converts stipitaldehyde into stipitacetal which is in turn converted to stipitalide by the short-chain dehydrogenase/reductase tropE. The next steps involve tropF, tropG, tropH, tropI and tropJ to form successive tropolone maleic anhydrides including stipitaldehydic, stipitatonic and stipitatic acids.",Maybe,Yes,Yes,Yes,Yes,Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3961,no
ETPN_ESCWE,A0A0M9VX54,Prot2Text,Eukaryota,290,"N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","Methyltransferase; part of the gene cluster that mediates the biosynthesis of the diterpenoid pyrones higginsianins A and B. The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpchA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpchD through the action of the prenyltransferase dpchC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpchE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpchB (Probable). The short chain dehydrogenase/reductase dpchG then oxidizes the 8S hydro",Maybe,Yes,Yes,Yes,Yes,Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3961,no
ETPN_ESCWE,A0A0M9VX54,ProtT3,Eukaryota,290,"N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).",S-adenosyl-L-methionine-dependent methyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms,Maybe,Yes,Yes,Yes,Yes,Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3961,no
ETPN_ESCWE,A0A0M9VX54,ProtTale,Eukaryota,290,"N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","Methyltransferase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the saturated C-C bonds of",Maybe,Yes,Yes,Yes,Yes,Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3961,no
ETPN_ESCWE,A0A0M9VX54,Protein2Text,Eukaryota,290,"N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","The molecular function of this protein is a methyltransferase, specifically a 2-oxoglutarate-dependent dioxygenase. This protein is involved in the methylation of molecules, which is a process that adds a methyl group to a molecule. In the case of this protein, it is involved in the methylation of other molecules, possibly as part of a larger metabolic pathway.",No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008168,,,,,GO:0016706,,,,,0.245,1,0.245,0.3961,no
ETPN_ESCWE,A0A0M9VX54,Reference,Eukaryota,290,"N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).","N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the epipolythiodiketopiperazine melinacidin IV, a major compound produced during pathogenesis. Acromyrmex leafcutter ants form a tripartite superorganismal mutualism with the fungal cultivar Leucoagaricus gongylophorus and a defensive actinobacterial symbiont Pseudonocardia. Melinacidin IV inhibits the ant defensive actinobacterial symbiont Pseudonocardia. The nonribosomal peptide synthetase etpP is speculated to be responsible for condensation of amino acids to form the carbon skeleton of melinacidin IV, whereas the cluster-specific tailoring enzymes are involved in further modifications leading to the production of melinacidin IV (Probable).",,,,,,,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3961,no
Y3070_LYSEN,A0A0S2DN66,ESM2Text,Bacteria,1068,"Involved in defense against bacteriophages. When this probable 4 gene operon (bGSDM-FE772_23060-FE772_23065-FE772_23070) is inserted into E.coli it provides nearly 100-fold protection against phages T5 and T6 and about 8-fold against phage T4. The operon without bGSDM no longer protects against phage. Probably a nucleotide hydrolase, possibly of ATP (Probable).",Involved in the modulation of the competence to flowering of apical meristems. Acts genetically on DprA (AC Q7D7L4) to repress expression of the competence to flowering gene comC.,No,No,No,No,No,not-Yes,GO:0005524; GO:0016787,,,,,,,,,,,0,,0.3152,no
Y3070_LYSEN,A0A0S2DN66,Prot2Text,Bacteria,1068,"Involved in defense against bacteriophages. When this probable 4 gene operon (bGSDM-FE772_23060-FE772_23065-FE772_23070) is inserted into E.coli it provides nearly 100-fold protection against phages T5 and T6 and about 8-fold against phage T4. The operon without bGSDM no longer protects against phage. Probably a nucleotide hydrolase, possibly of ATP (Probable).","Along with McjC, necessary and sufficient to process the inactive microcin J25 (McjA) precursor into the active peptide.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016787,GO:0008233,,GO:0008233,GO:0008233,GO:0008233,0.4959,,0.4959,0.4959,0.4959,4,0.4959,0.3152,no
Y3070_LYSEN,A0A0S2DN66,ProtT3,Bacteria,1068,"Involved in defense against bacteriophages. When this probable 4 gene operon (bGSDM-FE772_23060-FE772_23065-FE772_23070) is inserted into E.coli it provides nearly 100-fold protection against phages T5 and T6 and about 8-fold against phage T4. The operon without bGSDM no longer protects against phage. Probably a nucleotide hydrolase, possibly of ATP (Probable).","Component of the type VII secretion system (T7SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (Probable). Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import (Probable). Cytoplasm",No,No,No,No,No,not-Yes,GO:0005524; GO:0016787,,,,,,,,,,,0,,0.3152,no
Y3070_LYSEN,A0A0S2DN66,ProtTale,Bacteria,1068,"Involved in defense against bacteriophages. When this probable 4 gene operon (bGSDM-FE772_23060-FE772_23065-FE772_23070) is inserted into E.coli it provides nearly 100-fold protection against phages T5 and T6 and about 8-fold against phage T4. The operon without bGSDM no longer protects against phage. Probably a nucleotide hydrolase, possibly of ATP (Probable).","Part of an archaeal type III secretion system (T3SS), which is probably involved in protein secretion. Functions as a homodimer, which is necessary for its activity.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0005524; GO:0016787,,,,,,,,,,,0,,0.3152,no
Y3070_LYSEN,A0A0S2DN66,Protein2Text,Bacteria,1068,"Involved in defense against bacteriophages. When this probable 4 gene operon (bGSDM-FE772_23060-FE772_23065-FE772_23070) is inserted into E.coli it provides nearly 100-fold protection against phages T5 and T6 and about 8-fold against phage T4. The operon without bGSDM no longer protects against phage. Probably a nucleotide hydrolase, possibly of ATP (Probable).","This protein is a part of the type II DNA topoisomerase complex, which is a molecular function that plays a crucial role in DNA replication, transcription, and recombination. Specifically, it is involved in relaxing supercoiled DNA by temporarily breaking and rejoining the DNA strands.",No,No,No,No,No,not-Yes,GO:0005524; GO:0016787,GO:0003916,GO:0003918,GO:0003918,GO:0003918,GO:0003918,0.2214,0.1877,0.1877,0.1877,0.1877,5,0.1944,0.3152,no
Y3070_LYSEN,A0A0S2DN66,Reference,Bacteria,1068,"Involved in defense against bacteriophages. When this probable 4 gene operon (bGSDM-FE772_23060-FE772_23065-FE772_23070) is inserted into E.coli it provides nearly 100-fold protection against phages T5 and T6 and about 8-fold against phage T4. The operon without bGSDM no longer protects against phage. Probably a nucleotide hydrolase, possibly of ATP (Probable).","Involved in defense against bacteriophages. When this probable 4 gene operon (bGSDM-FE772_23060-FE772_23065-FE772_23070) is inserted into E.coli it provides nearly 100-fold protection against phages T5 and T6 and about 8-fold against phage T4. The operon without bGSDM no longer protects against phage. Probably a nucleotide hydrolase, possibly of ATP (Probable).",,,,,,,GO:0005524; GO:0016787,,,,,GO:0016787,,,,,0.6958,1,0.6958,0.3152,no
UAGEP_CAMJU,A0A0U3CEN8,ESM2Text,Bacteria,383,Non-hydrolyzing C2-epimerase involved in the biosynthesis of capsular polysaccharides. Catalyzes the C2 epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc) to form UDP-N- acetylmannosamine (UDP-ManNAc).,"Catalyzes the reversible epimerization at C-2 of UDP-N-acetylglucosamine (UDP-GlcNAc) and thereby provides bacteria with UDP-N-acetylmannosamine (UDP-ManNAc), the activated donor of ManNAc residues.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008761,GO:0016854,GO:0016854,GO:0050378,GO:0003978,GO:0008767,0.729,0.729,0.7289,0.7289,0.3987,5,0.6629,0.4948,no
UAGEP_CAMJU,A0A0U3CEN8,Prot2Text,Bacteria,383,Non-hydrolyzing C2-epimerase involved in the biosynthesis of capsular polysaccharides. Catalyzes the C2 epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc) to form UDP-N- acetylmannosamine (UDP-ManNAc).,"Catalyzes the reversible epimerization at C-2 of UDP-N-acetylglucosamine (UDP-GlcNAc) and thereby provides bacteria with UDP-N-acetylmannosamine (UDP-ManNAc), the activated donor of ManNAc residues.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008761,GO:0008761,GO:0003978,GO:0008761,GO:0008761,GO:0008767,1.0,0.7289,1.0,1.0,0.3987,5,0.8255,0.4948,no
UAGEP_CAMJU,A0A0U3CEN8,ProtT3,Bacteria,383,Non-hydrolyzing C2-epimerase involved in the biosynthesis of capsular polysaccharides. Catalyzes the C2 epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc) to form UDP-N- acetylmannosamine (UDP-ManNAc).,Cytoplasm. Belongs to the UDP-N-acetylglucosamine 2-epimerase family,Vague,Vague,Maybe,Vague,Vague,not-Yes,GO:0008761,GO:0008761,GO:0008761,,GO:0008761,GO:0008761,1.0,1.0,,1.0,1.0,4,1.0,0.4948,no
UAGEP_CAMJU,A0A0U3CEN8,ProtTale,Bacteria,383,Non-hydrolyzing C2-epimerase involved in the biosynthesis of capsular polysaccharides. Catalyzes the C2 epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc) to form UDP-N- acetylmannosamine (UDP-ManNAc).,"Catalyzes the reduction of 7,8- dihydrofolate (DHF) to 5,6,7,8-tetrahydrofolate that is used for thymidylate biosynthesis.",No,No,No,No,No,not-Yes,GO:0008761,GO:0004146,GO:0004146,GO:0004146,GO:0004146,GO:0004146,0.1998,0.1998,0.1998,0.1998,0.1998,5,0.1998,0.4948,no
UAGEP_CAMJU,A0A0U3CEN8,Protein2Text,Bacteria,383,Non-hydrolyzing C2-epimerase involved in the biosynthesis of capsular polysaccharides. Catalyzes the C2 epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc) to form UDP-N- acetylmannosamine (UDP-ManNAc).,"The molecular function of this protein is an enzyme, specifically a transferase that catalyzes the transfer of a group in an enzymatic reaction. It is involved in the biosynthesis of UDP-glucose, a sugar nucleotide that serves as a substrate for various glycosyltransferases.",No,No,No,No,No,not-Yes,GO:0008761,GO:0003983,GO:0003983,GO:0003983,GO:0003983,GO:0003983,0.154,0.154,0.154,0.154,0.154,5,0.154,0.4948,no
UAGEP_CAMJU,A0A0U3CEN8,Reference,Bacteria,383,Non-hydrolyzing C2-epimerase involved in the biosynthesis of capsular polysaccharides. Catalyzes the C2 epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc) to form UDP-N- acetylmannosamine (UDP-ManNAc).,Non-hydrolyzing C2-epimerase involved in the biosynthesis of capsular polysaccharides. Catalyzes the C2 epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc) to form UDP-N- acetylmannosamine (UDP-ManNAc).,,,,,,,GO:0008761,GO:0008761,GO:0003974,GO:0003855,GO:0003974,GO:0008761,1.0,0.7289,0.1998,0.7289,1.0,5,0.7315,0.4948,no
AACB_ASPA1,A0A1L9X985,ESM2Text,Eukaryota,375,"N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the diketopiperazine (DKP) aspkyncin. AacB mediates the synthesis of the unnatural amino acid N-methyl-L-alanine via methylation of L-alanine. Aspkyncin is produced by the NRPS aacA via condensation of the two unusual amino-acids N-methyl-L-alanine and L-kynurenine (L-Kyn). N- methyl-L-alanine originates from the methylation of L-alanine by the methyltransferase aacB whereas L-kynurenine is produced by the indoleamine-2,3-dioxygenase (IDO) that catalyzes the ring-opening oxidation of L-Trp to form N-formyl-l-kynurenine, followed by subsequent hydrolyzation to L-kynurenine (L-Kyn) through an endogenous L-kynurenine formamidase (Probable).",Multifunctional RNA-binding protein that regulates the biogenesis of citrate synthase. Substrate-specific RNA-binding protein that regulates the biogenesis of the large subunit (CitR) and small subunit (SrcR). Stabilizes the N-terminal citrate synthase subunit. Also stabilizes (R)-subunit CitR mRNA. Associates with the preinitiation complex (PIC) and the RNA polymerase VEI holoenzyme. The association (R)-subunit CitR enhances (S)-TFI1-mediated transcriptional activity. Involved in RNA polymerase VEI-dependent transcriptional regulation.,No,No,Yes,No,No,not-Yes,GO:0008168,GO:0003723,GO:0003723,GO:0003723,,,0.146,0.146,0.146,,,3,0.146,0.2717,no
AACB_ASPA1,A0A1L9X985,Prot2Text,Eukaryota,375,"N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the diketopiperazine (DKP) aspkyncin. AacB mediates the synthesis of the unnatural amino acid N-methyl-L-alanine via methylation of L-alanine. Aspkyncin is produced by the NRPS aacA via condensation of the two unusual amino-acids N-methyl-L-alanine and L-kynurenine (L-Kyn). N- methyl-L-alanine originates from the methylation of L-alanine by the methyltransferase aacB whereas L-kynurenine is produced by the indoleamine-2,3-dioxygenase (IDO) that catalyzes the ring-opening oxidation of L-Trp to form N-formyl-l-kynurenine, followed by subsequent hydrolyzation to L-kynurenine (L-Kyn) through an endogenous L-kynurenine formamidase (Probable).",S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that methylates the delta-nitrogen atom of arginine residues to form N5-methylarginine (type IV) in target proteins. Monomethylates ribosomal protein L12.,Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0008168,GO:0016274,GO:0016274,GO:0016274,GO:0016274,GO:0008757; GO:0035241,0.5639,0.5639,0.5639,0.5639,0.751,5,0.6013,0.2717,no
AACB_ASPA1,A0A1L9X985,ProtT3,Eukaryota,375,"N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the diketopiperazine (DKP) aspkyncin. AacB mediates the synthesis of the unnatural amino acid N-methyl-L-alanine via methylation of L-alanine. Aspkyncin is produced by the NRPS aacA via condensation of the two unusual amino-acids N-methyl-L-alanine and L-kynurenine (L-Kyn). N- methyl-L-alanine originates from the methylation of L-alanine by the methyltransferase aacB whereas L-kynurenine is produced by the indoleamine-2,3-dioxygenase (IDO) that catalyzes the ring-opening oxidation of L-Trp to form N-formyl-l-kynurenine, followed by subsequent hydrolyzation to L-kynurenine (L-Kyn) through an endogenous L-kynurenine formamidase (Probable).",N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeran,Yes,Yes,Yes,Yes,Yes,Yes,GO:0008168,GO:0008170,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.8582,1.0,1.0,1.0,1.0,5,0.9716,0.2717,no
AACB_ASPA1,A0A1L9X985,ProtTale,Eukaryota,375,"N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the diketopiperazine (DKP) aspkyncin. AacB mediates the synthesis of the unnatural amino acid N-methyl-L-alanine via methylation of L-alanine. Aspkyncin is produced by the NRPS aacA via condensation of the two unusual amino-acids N-methyl-L-alanine and L-kynurenine (L-Kyn). N- methyl-L-alanine originates from the methylation of L-alanine by the methyltransferase aacB whereas L-kynurenine is produced by the indoleamine-2,3-dioxygenase (IDO) that catalyzes the ring-opening oxidation of L-Trp to form N-formyl-l-kynurenine, followed by subsequent hydrolyzation to L-kynurenine (L-Kyn) through an endogenous L-kynurenine formamidase (Probable).","N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the tetrahydroxanthone dimer secalonic acid D. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase AacuL (Probable). The atrochrysone carboxyl ACP thioesterase AacuM then breaks the thioester bond and releases the atrochrysone carboxylic acid from AacuL (Probable). Atrochrysone carboxylic acid is decarboxylated by the decarboxylase AacuI, and oxidized by the anthrone oxygenase AacuG to yield em",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008168,GO:0008170,GO:0008170,GO:0008170,GO:0008170,GO:0008168,0.8582,0.8582,0.8582,0.8582,1.0,5,0.8866,0.2717,no
AACB_ASPA1,A0A1L9X985,Protein2Text,Eukaryota,375,"N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the diketopiperazine (DKP) aspkyncin. AacB mediates the synthesis of the unnatural amino acid N-methyl-L-alanine via methylation of L-alanine. Aspkyncin is produced by the NRPS aacA via condensation of the two unusual amino-acids N-methyl-L-alanine and L-kynurenine (L-Kyn). N- methyl-L-alanine originates from the methylation of L-alanine by the methyltransferase aacB whereas L-kynurenine is produced by the indoleamine-2,3-dioxygenase (IDO) that catalyzes the ring-opening oxidation of L-Trp to form N-formyl-l-kynurenine, followed by subsequent hydrolyzation to L-kynurenine (L-Kyn) through an endogenous L-kynurenine formamidase (Probable).","This protein is involved in the methyltransferase activity, specifically in the methylation of a protein or molecule.",Vague,Vague,Maybe,Vague,Vague,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2717,no
AACB_ASPA1,A0A1L9X985,Reference,Eukaryota,375,"N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the diketopiperazine (DKP) aspkyncin. AacB mediates the synthesis of the unnatural amino acid N-methyl-L-alanine via methylation of L-alanine. Aspkyncin is produced by the NRPS aacA via condensation of the two unusual amino-acids N-methyl-L-alanine and L-kynurenine (L-Kyn). N- methyl-L-alanine originates from the methylation of L-alanine by the methyltransferase aacB whereas L-kynurenine is produced by the indoleamine-2,3-dioxygenase (IDO) that catalyzes the ring-opening oxidation of L-Trp to form N-formyl-l-kynurenine, followed by subsequent hydrolyzation to L-kynurenine (L-Kyn) through an endogenous L-kynurenine formamidase (Probable).","N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the diketopiperazine (DKP) aspkyncin. AacB mediates the synthesis of the unnatural amino acid N-methyl-L-alanine via methylation of L-alanine. Aspkyncin is produced by the NRPS aacA via condensation of the two unusual amino-acids N-methyl-L-alanine and L-kynurenine (L-Kyn). N- methyl-L-alanine originates from the methylation of L-alanine by the methyltransferase aacB whereas L-kynurenine is produced by the indoleamine-2,3-dioxygenase (IDO) that catalyzes the ring-opening oxidation of L-Trp to form N-formyl-l-kynurenine, followed by subsequent hydrolyzation to L-kynurenine (L-Kyn) through an endogenous L-kynurenine formamidase (Probable).",,,,,,,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2717,no
RUFB_STRAR,A0A224AUB0,ESM2Text,Bacteria,254,"Peptidase involved in the biosynthesis of rufomycins, a class of cyclic heptapeptides with anti-mycobacterial activity. It catalyzes the degradation of the nitrated biarylitide-type ribosomal pentapeptide (Met-Arg-(NO(2))Tyr-Leu-His or MR(NO(2)-Tyr)LH), which is encoded by bytA and nitrated by RufO, leading to the release of 3-nitrotyrosine (3-NO(2)-Tyr) from the peptide (Ref.2). It allows subsequent incorporation of 3-NO(2)-Tyr into the non-ribosomal peptide chain by the rufomycin synthetase assembly line (Ref.2).",Enables the bacterium to use acetate or propanoyl-CoA as a starter unit to produce the highly active enolpyruvyl-CoA ester bacteriochlorophyllide a (BChlidea). Chlidea is the substrate of the bacteriocin ChlB.,No,No,No,No,No,not-Yes,GO:0016787,,,,,,,,,,,0,,0.2762,no
RUFB_STRAR,A0A224AUB0,Prot2Text,Bacteria,254,"Peptidase involved in the biosynthesis of rufomycins, a class of cyclic heptapeptides with anti-mycobacterial activity. It catalyzes the degradation of the nitrated biarylitide-type ribosomal pentapeptide (Met-Arg-(NO(2))Tyr-Leu-His or MR(NO(2)-Tyr)LH), which is encoded by bytA and nitrated by RufO, leading to the release of 3-nitrotyrosine (3-NO(2)-Tyr) from the peptide (Ref.2). It allows subsequent incorporation of 3-NO(2)-Tyr into the non-ribosomal peptide chain by the rufomycin synthetase assembly line (Ref.2).",Ring-cleaving dioxygenase involved in the degradation of the Pseudomonas aeruginosa quorum sensing signal molecules HHQ (2-heptyl-4-quinolone) and PQS (2-heptyl-3-hydroxy-4-quinolone) to anthranilic acid.,No,No,No,No,No,not-Yes,GO:0016787,GO:0051213,GO:0051213,GO:0051213,GO:0051213,GO:0051213,0.4807,0.4807,0.4807,0.4807,0.4807,5,0.4807,0.2762,no
RUFB_STRAR,A0A224AUB0,ProtT3,Bacteria,254,"Peptidase involved in the biosynthesis of rufomycins, a class of cyclic heptapeptides with anti-mycobacterial activity. It catalyzes the degradation of the nitrated biarylitide-type ribosomal pentapeptide (Met-Arg-(NO(2))Tyr-Leu-His or MR(NO(2)-Tyr)LH), which is encoded by bytA and nitrated by RufO, leading to the release of 3-nitrotyrosine (3-NO(2)-Tyr) from the peptide (Ref.2). It allows subsequent incorporation of 3-NO(2)-Tyr into the non-ribosomal peptide chain by the rufomycin synthetase assembly line (Ref.2).",Belongs to the type-B carboxylesterase/lipase family,Vague,Vague,Vague,Vague,No,not-Yes,GO:0016787,GO:0004091,GO:0052689,,GO:0004091,GO:0004091,0.6897,0.6897,,0.6897,0.6897,4,0.6897,0.2762,no
RUFB_STRAR,A0A224AUB0,ProtTale,Bacteria,254,"Peptidase involved in the biosynthesis of rufomycins, a class of cyclic heptapeptides with anti-mycobacterial activity. It catalyzes the degradation of the nitrated biarylitide-type ribosomal pentapeptide (Met-Arg-(NO(2))Tyr-Leu-His or MR(NO(2)-Tyr)LH), which is encoded by bytA and nitrated by RufO, leading to the release of 3-nitrotyrosine (3-NO(2)-Tyr) from the peptide (Ref.2). It allows subsequent incorporation of 3-NO(2)-Tyr into the non-ribosomal peptide chain by the rufomycin synthetase assembly line (Ref.2).","Cleaves the beta-lactam ring of the beta-lactam antibiotics ampicillin, amoxicillin and amoxicillin-clavulanate.",No,No,No,No,No,not-Yes,GO:0016787,GO:0008800,GO:0008800,GO:0008800,GO:0008800,GO:0008800,0.6019,0.6019,0.6019,0.6019,0.6019,5,0.6019,0.2762,no
RUFB_STRAR,A0A224AUB0,Protein2Text,Bacteria,254,"Peptidase involved in the biosynthesis of rufomycins, a class of cyclic heptapeptides with anti-mycobacterial activity. It catalyzes the degradation of the nitrated biarylitide-type ribosomal pentapeptide (Met-Arg-(NO(2))Tyr-Leu-His or MR(NO(2)-Tyr)LH), which is encoded by bytA and nitrated by RufO, leading to the release of 3-nitrotyrosine (3-NO(2)-Tyr) from the peptide (Ref.2). It allows subsequent incorporation of 3-NO(2)-Tyr into the non-ribosomal peptide chain by the rufomycin synthetase assembly line (Ref.2).",This protein is involved in the molecular function of ester hydrolase activity.,Vague,Maybe,Vague,No,No,not-Yes,GO:0016787,GO:0016788,GO:0016788,GO:0016788,GO:0016788,GO:0016788,0.8145,0.8145,0.8145,0.8145,0.8145,5,0.8145,0.2762,no
RUFB_STRAR,A0A224AUB0,Reference,Bacteria,254,"Peptidase involved in the biosynthesis of rufomycins, a class of cyclic heptapeptides with anti-mycobacterial activity. It catalyzes the degradation of the nitrated biarylitide-type ribosomal pentapeptide (Met-Arg-(NO(2))Tyr-Leu-His or MR(NO(2)-Tyr)LH), which is encoded by bytA and nitrated by RufO, leading to the release of 3-nitrotyrosine (3-NO(2)-Tyr) from the peptide (Ref.2). It allows subsequent incorporation of 3-NO(2)-Tyr into the non-ribosomal peptide chain by the rufomycin synthetase assembly line (Ref.2).","Peptidase involved in the biosynthesis of rufomycins, a class of cyclic heptapeptides with anti-mycobacterial activity. It catalyzes the degradation of the nitrated biarylitide-type ribosomal pentapeptide (Met-Arg-(NO(2))Tyr-Leu-His or MR(NO(2)-Tyr)LH), which is encoded by bytA and nitrated by RufO, leading to the release of 3-nitrotyrosine (3-NO(2)-Tyr) from the peptide (Ref.2). It allows subsequent incorporation of 3-NO(2)-Tyr into the non-ribosomal peptide chain by the rufomycin synthetase assembly line (Ref.2).",,,,,,,GO:0016787,GO:0008233,GO:0008233,GO:0008233,GO:0008233,GO:0008233,0.7093,0.7093,0.7093,0.7093,0.7093,5,0.7093,0.2762,no
UNGE_ASPC2,A0A2I1D2Q5,ESM2Text,Eukaryota,342,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of the unguisins, gamma-aminobutyric acid (GABA)- containing fungal cyclic heptapeptides with the amino acid sequence cyclo-(D-Ala1-D-Val2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6-GABA7) for unguisin H and cyclo-(D-Ala1-D-Ala2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6- GABA7) for unguisin I. Within the pathway, the methyltransferase ungE' is probably involved in the synthesis of the (2R,3R)-beta-methylphenylalanine residue incorporated by the module 4 of the nonribosomal peptide synthetase (NRPS) ungA' (Probable). The alanine racemase ungC' catalyzes the interconversion of L-alanine and D-alanine, providing the D-alanine which is accepted by the first adenylation domain of ungA' (Probable). UngA' is the main enzyme within the cluster which condenses the 7 residues using its respective 7 modules (Probable). The terminal condensation domain (Ct) is involved in cyclization with D-alanine and thereby releasing of unguisins H and I (Probable). Finally, the hydrolase ungD' catalyzes the hydrolysis between the D-tryptophan and GABA residues of unguisins H and I to produce the corresponding linear peptides (Probable).","S-adenosyl-L-methionine-dependent methyltransferase that mediates the methylation of para-nitrophenyl (pNPP) to putrescine. Methylates para-nitrophenyl at position 9, one of the positions that governs the biosynthesis of polyamines. Mediates also the methylation of spermidine to putrescine.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0008168,GO:0008168,GO:0008168,,,,1.0,1.0,,,,2,1.0,0.1655,no
UNGE_ASPC2,A0A2I1D2Q5,Prot2Text,Eukaryota,342,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of the unguisins, gamma-aminobutyric acid (GABA)- containing fungal cyclic heptapeptides with the amino acid sequence cyclo-(D-Ala1-D-Val2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6-GABA7) for unguisin H and cyclo-(D-Ala1-D-Ala2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6- GABA7) for unguisin I. Within the pathway, the methyltransferase ungE' is probably involved in the synthesis of the (2R,3R)-beta-methylphenylalanine residue incorporated by the module 4 of the nonribosomal peptide synthetase (NRPS) ungA' (Probable). The alanine racemase ungC' catalyzes the interconversion of L-alanine and D-alanine, providing the D-alanine which is accepted by the first adenylation domain of ungA' (Probable). UngA' is the main enzyme within the cluster which condenses the 7 residues using its respective 7 modules (Probable). The terminal condensation domain (Ct) is involved in cyclization with D-alanine and thereby releasing of unguisins H and I (Probable). Finally, the hydrolase ungD' catalyzes the hydrolysis between the D-tryptophan and GABA residues of unguisins H and I to produce the corresponding linear peptides (Probable).",S-adenosyl-L-methionine-dependent methyltransferase involved in the biosynthesis of the nonproteinogenic amino acid monomeric acid (MAMP). Catalyzes the methylation of the hydroxyl group of the inactive amino acid (S)-3-hydroxy-L-methionine to yield (S)-3-hydroxy-D-methionine. The only accepted substrate is (S)-3-hydroxy-D-methionine.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008757,GO:0008757,1.0,1.0,1.0,0.8582,0.8582,5,0.9433,0.1655,no
UNGE_ASPC2,A0A2I1D2Q5,ProtT3,Eukaryota,342,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of the unguisins, gamma-aminobutyric acid (GABA)- containing fungal cyclic heptapeptides with the amino acid sequence cyclo-(D-Ala1-D-Val2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6-GABA7) for unguisin H and cyclo-(D-Ala1-D-Ala2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6- GABA7) for unguisin I. Within the pathway, the methyltransferase ungE' is probably involved in the synthesis of the (2R,3R)-beta-methylphenylalanine residue incorporated by the module 4 of the nonribosomal peptide synthetase (NRPS) ungA' (Probable). The alanine racemase ungC' catalyzes the interconversion of L-alanine and D-alanine, providing the D-alanine which is accepted by the first adenylation domain of ungA' (Probable). UngA' is the main enzyme within the cluster which condenses the 7 residues using its respective 7 modules (Probable). The terminal condensation domain (Ct) is involved in cyclization with D-alanine and thereby releasing of unguisins H and I (Probable). Finally, the hydrolase ungD' catalyzes the hydrolysis between the D-tryptophan and GABA residues of unguisins H and I to produce the corresponding linear peptides (Probable).",O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeran,Maybe,Yes,Maybe,Maybe,Maybe,not-Yes,GO:0008168,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.1655,no
UNGE_ASPC2,A0A2I1D2Q5,ProtTale,Eukaryota,342,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of the unguisins, gamma-aminobutyric acid (GABA)- containing fungal cyclic heptapeptides with the amino acid sequence cyclo-(D-Ala1-D-Val2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6-GABA7) for unguisin H and cyclo-(D-Ala1-D-Ala2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6- GABA7) for unguisin I. Within the pathway, the methyltransferase ungE' is probably involved in the synthesis of the (2R,3R)-beta-methylphenylalanine residue incorporated by the module 4 of the nonribosomal peptide synthetase (NRPS) ungA' (Probable). The alanine racemase ungC' catalyzes the interconversion of L-alanine and D-alanine, providing the D-alanine which is accepted by the first adenylation domain of ungA' (Probable). UngA' is the main enzyme within the cluster which condenses the 7 residues using its respective 7 modules (Probable). The terminal condensation domain (Ct) is involved in cyclization with D-alanine and thereby releasing of unguisins H and I (Probable). Finally, the hydrolase ungD' catalyzes the hydrolysis between the D-tryptophan and GABA residues of unguisins H and I to produce the corresponding linear peptides (Probable).","Involved in the biosynthesis of 4-methylumbelliferone (4-MU), a natural product used for food color and medicine. Catalyzes the methylation of 4-MU to yield 4-methylumbelliferone (4-MU), an intermediate in the biosynthesis of 4-methylumbelliferone (4-MU).",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1655,no
UNGE_ASPC2,A0A2I1D2Q5,Protein2Text,Eukaryota,342,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of the unguisins, gamma-aminobutyric acid (GABA)- containing fungal cyclic heptapeptides with the amino acid sequence cyclo-(D-Ala1-D-Val2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6-GABA7) for unguisin H and cyclo-(D-Ala1-D-Ala2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6- GABA7) for unguisin I. Within the pathway, the methyltransferase ungE' is probably involved in the synthesis of the (2R,3R)-beta-methylphenylalanine residue incorporated by the module 4 of the nonribosomal peptide synthetase (NRPS) ungA' (Probable). The alanine racemase ungC' catalyzes the interconversion of L-alanine and D-alanine, providing the D-alanine which is accepted by the first adenylation domain of ungA' (Probable). UngA' is the main enzyme within the cluster which condenses the 7 residues using its respective 7 modules (Probable). The terminal condensation domain (Ct) is involved in cyclization with D-alanine and thereby releasing of unguisins H and I (Probable). Finally, the hydrolase ungD' catalyzes the hydrolysis between the D-tryptophan and GABA residues of unguisins H and I to produce the corresponding linear peptides (Probable).","This protein is involved in the biosynthesis of indole alkaloids, specifically in the decarboxylation of L-tryptophan to tryptamine. It catalyzes the decarboxylation of L-tryptophan to tryptamine, which is a precursor for the synthesis of various indole alkaloids. The molecular function of this protein is to convert L-tryptophan into tryptamine through the removal of a carboxyl group. 
This protein is a member of the O-methyltransferase family, which is a class of enzymes that catalyze the transfer of a methyl group from one compound to another. In this case, the protein is responsible for the decarboxylation of L-tryptophan, which involves the removal of a carboxyl group and the formation of tryptamine. The molecular function of this protein is therefore that of a decarboxylase. 
The protein is also involved in the biosynthesis of various indole alkaloids, which are a class of compounds that have a range of biological activities. The protein is part of a larger metabolic pathway that involves the conversion of L-tryptophan into tryptamine, which is then used as a precursor for the synthesis of various indole alkaloids. The molecular function of this protein is therefore that of a precursor for the synthesis of indole alkaloids. 
The protein is also involved in the biosynthesis of the indole alkaloid ajmaline, which is a compound that has been used in the treatment of heart conditions. The protein is part of a larger metabolic pathway that involves the conversion of L-tryptophan into tryptamine, which is then used as a precursor for the synthesis of ajmaline. The molecular function of this protein is therefore that of a precursor for the synthesis of ajmaline. 
The protein is also involved in the biosynthesis of the indole alkaloid vinblastine, which is a compound that has been used in the treatment of cancer. The protein is part of a larger metabolic pathway that involves the conversion of L-tryptophan into tryptamine, which is then used as a precursor for the synthesis of vinblastine. The molecular function of this protein is therefore that of a precursor for the synthesis of vinblastine. 
The protein is also involved in the biosynthesis of the indole alkaloid vinodine, which is a compound that has been used in the treatment of cancer. The protein is part",No,No,No,No,No,not-Yes,GO:0008168,GO:0016831,GO:0004058,GO:0004058,GO:0004058,GO:0004058,0.2742,0.2353,0.2353,0.2353,0.2353,5,0.2431,0.1655,no
UNGE_ASPC2,A0A2I1D2Q5,Reference,Eukaryota,342,"Methyltransferase; part of the gene cluster that mediates the biosynthesis of the unguisins, gamma-aminobutyric acid (GABA)- containing fungal cyclic heptapeptides with the amino acid sequence cyclo-(D-Ala1-D-Val2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6-GABA7) for unguisin H and cyclo-(D-Ala1-D-Ala2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6- GABA7) for unguisin I. Within the pathway, the methyltransferase ungE' is probably involved in the synthesis of the (2R,3R)-beta-methylphenylalanine residue incorporated by the module 4 of the nonribosomal peptide synthetase (NRPS) ungA' (Probable). The alanine racemase ungC' catalyzes the interconversion of L-alanine and D-alanine, providing the D-alanine which is accepted by the first adenylation domain of ungA' (Probable). UngA' is the main enzyme within the cluster which condenses the 7 residues using its respective 7 modules (Probable). The terminal condensation domain (Ct) is involved in cyclization with D-alanine and thereby releasing of unguisins H and I (Probable). Finally, the hydrolase ungD' catalyzes the hydrolysis between the D-tryptophan and GABA residues of unguisins H and I to produce the corresponding linear peptides (Probable).","Methyltransferase; part of the gene cluster that mediates the biosynthesis of the unguisins, gamma-aminobutyric acid (GABA)- containing fungal cyclic heptapeptides with the amino acid sequence cyclo-(D-Ala1-D-Val2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6-GABA7) for unguisin H and cyclo-(D-Ala1-D-Ala2-L-Leu3-beta-MePhe4-D-Ala5-D-Trp6- GABA7) for unguisin I. Within the pathway, the methyltransferase ungE' is probably involved in the synthesis of the (2R,3R)-beta-methylphenylalanine residue incorporated by the module 4 of the nonribosomal peptide synthetase (NRPS) ungA' (Probable). The alanine racemase ungC' catalyzes the interconversion of L-alanine and D-alanine, providing the D-alanine which is accepted by the first adenylation domain of ungA' (Probable). UngA' is the main enzyme within the cluster which condenses the 7 residues using its respective 7 modules (Probable). The terminal condensation domain (Ct) is involved in cyclization with D-alanine and thereby releasing of unguisins H and I (Probable). Finally, the hydrolase ungD' catalyzes the hydrolysis between the D-tryptophan and GABA residues of unguisins H and I to produce the corresponding linear peptides (Probable).",,,,,,,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1655,no
TPS10_DICPU,A0A385AJM5,ESM2Text,Eukaryota,356,Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into several unidentified sesquiterpenes. TPS10 also converts geranylgeranyl diphosphate (GGPP) into the diterpene beta-araneosene.,Sesquiterpene synthase converting farnesyl diphosphate to (E)-2-epi-cubebol. No activity with farnesyl diphosphate as substrate.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0010333,,,,,,,,,,,0,,0.2008,no
TPS10_DICPU,A0A385AJM5,Prot2Text,Eukaryota,356,Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into several unidentified sesquiterpenes. TPS10 also converts geranylgeranyl diphosphate (GGPP) into the diterpene beta-araneosene.,"Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-8(14),15-diene (PD). Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors. The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes. Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-8(14),15-diene. The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0010333,GO:0010333,GO:0010333,GO:0010333,GO:0010333,0.6963,0.6963,0.6963,0.6963,0.6963,5,0.6963,0.2008,no
TPS10_DICPU,A0A385AJM5,ProtT3,Eukaryota,356,Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into several unidentified sesquiterpenes. TPS10 also converts geranylgeranyl diphosphate (GGPP) into the diterpene beta-araneosene.,"Terpene synthase that catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) into alpha-humulene. Belongs to the terpene synthase family",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0016829,GO:0010333,GO:0010334,GO:0010333,GO:0010333,0.4539,0.6963,0.6051,0.6963,0.6963,5,0.6296,0.2008,no
TPS10_DICPU,A0A385AJM5,ProtTale,Eukaryota,356,Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into several unidentified sesquiterpenes. TPS10 also converts geranylgeranyl diphosphate (GGPP) into the diterpene beta-araneosene.,Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into the sesquiterpene beta-caryophyllene.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0010333,GO:0016829,GO:0010333,GO:0016829,GO:0010333,0.6963,0.4539,0.6963,0.4539,0.6963,5,0.5993,0.2008,no
TPS10_DICPU,A0A385AJM5,Protein2Text,Eukaryota,356,Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into several unidentified sesquiterpenes. TPS10 also converts geranylgeranyl diphosphate (GGPP) into the diterpene beta-araneosene.,"This protein is involved in catalyzing the formation of a sesquiterpene, specifically a farnesyl diphosphate (FPP) intermediate, which is a precursor molecule for a variety of natural products. The specific molecular function of this protein is to catalyze the conversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) to FPP. This reaction is the first step in the biosynthesis of sesquiterpenes, a diverse group of natural products that have important roles in plant defense and other physiological processes. 

The molecular function of this protein is to facilitate the formation of FPP, a key precursor molecule for the biosynthesis of sesquiterpenes, through the condensation of IPP and DMAPP. This protein is involved in the biosynthesis of sesquiterpenes, which are important natural products with various physiological functions in plants. 

The molecular function of this protein is to catalyze the condensation of IPP and DMAPP to form FPP, a key precursor molecule for the biosynthesis of sesquiterpenes. This protein is involved in the biosynthesis of sesquiterpenes, which are important natural products with various physiological functions in plants. 

The molecular function of this protein is to catalyze the conversion of IPP and DMAPP to FPP, a key precursor molecule for the biosynthesis of sesquiterpenes. This protein is involved in the biosynthesis of sesquiterpenes, which are important natural products with various physiological functions in plants. 

The molecular function of this protein is to catalyze the formation of FPP, a key precursor molecule for the biosynthesis of sesquiterpenes. This protein is involved in the biosynthesis of sesquiterpenes, which are important natural products with various physiological functions in plants. 

The molecular function of this protein is to catalyze the conversion of IPP and DMAPP to FPP, a key precursor molecule for the biosynthesis of sesquiterpenes. This protein is involved in the biosynthesis of sesquiterpenes, which are important natural products with various physiological functions in plants. 

The molecular function of this protein is to catalyze the formation of FPP, a key precursor molecule for the biosynthesis of sesquiterpenes. This protein is involved in the biosynthesis of sesquiterpenes, which are important natural products with various physiological functions in plants. 

The molecular function of",Vague,Maybe,Maybe,No,Maybe,not-Yes,GO:0046872; GO:0010333,GO:0004337,GO:0004337,GO:0004337,GO:0004337,GO:0004337,0.1415,0.1415,0.1415,0.1415,0.1415,5,0.1415,0.2008,no
TPS10_DICPU,A0A385AJM5,Reference,Eukaryota,356,Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into several unidentified sesquiterpenes. TPS10 also converts geranylgeranyl diphosphate (GGPP) into the diterpene beta-araneosene.,Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into several unidentified sesquiterpenes. TPS10 also converts geranylgeranyl diphosphate (GGPP) into the diterpene beta-araneosene.,,,,,,,GO:0046872; GO:0010333,GO:0016829,GO:0016829,GO:0010333,GO:0016829,GO:0010333,0.4539,0.4539,0.6963,0.4539,0.6963,5,0.5509,0.2008,no
ANKA_ASPTH,A0A397HK51,ESM2Text,Eukaryota,518,"Arginine-containing cyclodipeptide synthase; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo-arginine-tyrosine dipeptide connected to homoserine, citrate and aspartate. Within the pathway, ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-arginyl-tRNA(Arg) and L- tyrosyl-tRNA(Tyr). The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L- homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A.","Prenyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ. Paxilline is converted to beta-pax",No,No,No,No,No,not-Yes,GO:0016874,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,0.4071,0.4071,0.4071,0.4071,0.4071,5,0.4071,0.3584,no
ANKA_ASPTH,A0A397HK51,Prot2Text,Eukaryota,518,"Arginine-containing cyclodipeptide synthase; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo-arginine-tyrosine dipeptide connected to homoserine, citrate and aspartate. Within the pathway, ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-arginyl-tRNA(Arg) and L- tyrosyl-tRNA(Tyr). The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L- homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A.","Synthesis of mevalonate for the production of non-sterol isoprenoids, which are essential for growth differentiation.",No,No,No,No,No,not-Yes,GO:0016874,GO:0004420,GO:0004420,GO:0004420,GO:0004420,GO:0004420,0.3552,0.3552,0.3552,0.3552,0.3552,5,0.3552,0.3584,no
ANKA_ASPTH,A0A397HK51,ProtT3,Eukaryota,518,"Arginine-containing cyclodipeptide synthase; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo-arginine-tyrosine dipeptide connected to homoserine, citrate and aspartate. Within the pathway, ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-arginyl-tRNA(Arg) and L- tyrosyl-tRNA(Tyr). The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L- homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A.",Non-catalytic component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA (By similarity). Belongs to the TYW3 family,No,No,No,No,No,not-Yes,GO:0016874,,,,,,,,,,,0,,0.3584,no
ANKA_ASPTH,A0A397HK51,ProtTale,Eukaryota,518,"Arginine-containing cyclodipeptide synthase; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo-arginine-tyrosine dipeptide connected to homoserine, citrate and aspartate. Within the pathway, ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-arginyl-tRNA(Arg) and L- tyrosyl-tRNA(Tyr). The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L- homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A.",Component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase synthesizes short RNA primers on the lagging strand that the polymerase presumably elongates using dNTPs. The primase-associated factor has no known catalytic activity in the complex and may serve to facilitate the formation of the replisome by directly interacting with the origin-binding protein and the polymerase.,No,No,No,No,No,not-Yes,GO:0016874,GO:0003678; GO:0003896,GO:0003678; GO:0003896; GO:0005524,GO:0003678; GO:0003896,GO:0003678; GO:0003896; GO:0005524,GO:0003678; GO:0003896; GO:0005524,0.2581,0.2012,0.2581,0.2012,0.2012,5,0.224,0.3584,no
ANKA_ASPTH,A0A397HK51,Protein2Text,Eukaryota,518,"Arginine-containing cyclodipeptide synthase; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo-arginine-tyrosine dipeptide connected to homoserine, citrate and aspartate. Within the pathway, ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-arginyl-tRNA(Arg) and L- tyrosyl-tRNA(Tyr). The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L- homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A.","This protein is a type of enzyme, specifically a nucleotide cyclase, which catalyzes the conversion of a molecule into a cyclic nucleotide.",No,No,Vague,No,No,not-Yes,GO:0016874,,,,,GO:0009975,,,,,0.5902,1,0.5902,0.3584,no
ANKA_ASPTH,A0A397HK51,Reference,Eukaryota,518,"Arginine-containing cyclodipeptide synthase; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo-arginine-tyrosine dipeptide connected to homoserine, citrate and aspartate. Within the pathway, ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-arginyl-tRNA(Arg) and L- tyrosyl-tRNA(Tyr). The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L- homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A.","Arginine-containing cyclodipeptide synthase; part of the ank cluster that mediates the biosynthesis of NK13650 C, a highly modified cyclo-arginine-tyrosine dipeptide connected to homoserine, citrate and aspartate. Within the pathway, ankA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Tyr diketopiperazine (cRY) from L-arginyl-tRNA(Arg) and L- tyrosyl-tRNA(Tyr). The ankA product cRY is desaturated by the cytochrome P450 monooxygenase ankB to yield a dehydro-cyclodipeptide intermediate. The FAD-dependent monooxygenase ankC then installs the m-OH, ankD catalyzes the attachment of L- homoserine, and ankE ligates citrate to the ankD product to yield NK13650 B. The O-methyltransferase ankF is responsible for methylation of the C-17 phenol group of NK13650 B to produce NK13650 D. Amidation of NK13650 D with L-Asp by ankG then leads to the production of NK13650 C, whereas amidation of NK13650 B produces NK13650 A.",,,,,,,GO:0016874,GO:0016740,GO:0016755,GO:0016740,GO:0016755,GO:0016874,0.5902,0.4071,0.5902,0.4071,1.0,5,0.5989,0.3584,no
CAPC_ORNRH,A0A3R5XUE6,ESM2Text,Bacteria,283,"Reductase involved in the biosynthesis of capnine, a sulfonolipid present in the outer membrane of gliding Bacteroidetes and essential for gliding motility. Catalyzes the reduction of 3-dehydrocapnine to capnine.","Aldehyde reductase with broad substrate specificity acting on 3-keto acids, glycolate, acetyl-CoA and propionyl-CoA. Prefers NADH over NADPH as cosubstrate. May be involved in the initial step of the aerobic nicotinate degradation pathway.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1835,no
CAPC_ORNRH,A0A3R5XUE6,Prot2Text,Bacteria,283,"Reductase involved in the biosynthesis of capnine, a sulfonolipid present in the outer membrane of gliding Bacteroidetes and essential for gliding motility. Catalyzes the reduction of 3-dehydrocapnine to capnine.","Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3-hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB), beta-Ala, a 4-methylhex-2-enoic acid at the N-terminus as well as a N1,N1-dimethylpropane-1,2-diamine (DPD) at the C-terminus (Probable). The biosynthesis of leucinostatins is probably initiated with the assembly of 4-methylhex-2-enoic acid by a reducing PKS. Two reducing polyketide synthases, lcsB and l",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1835,no
CAPC_ORNRH,A0A3R5XUE6,ProtT3,Bacteria,283,"Reductase involved in the biosynthesis of capnine, a sulfonolipid present in the outer membrane of gliding Bacteroidetes and essential for gliding motility. Catalyzes the reduction of 3-dehydrocapnine to capnine.",Belongs to the short-chain dehydrogenases/reductases (SDR) family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016491,GO:0016491,GO:0016491,,,,1.0,1.0,,,,2,1.0,0.1835,no
CAPC_ORNRH,A0A3R5XUE6,ProtTale,Bacteria,283,"Reductase involved in the biosynthesis of capnine, a sulfonolipid present in the outer membrane of gliding Bacteroidetes and essential for gliding motility. Catalyzes the reduction of 3-dehydrocapnine to capnine.",Involved in the biosynthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. Catalyzes the conversion of (S)-3-methyl-2-oxopentanoate to (S)-3-methyl-2-oxopent-4-enoate.,No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,,,GO:0016491,GO:0016836,GO:0016836,,,1.0,0.4071,0.4071,3,0.6047,0.1835,no
CAPC_ORNRH,A0A3R5XUE6,Protein2Text,Bacteria,283,"Reductase involved in the biosynthesis of capnine, a sulfonolipid present in the outer membrane of gliding Bacteroidetes and essential for gliding motility. Catalyzes the reduction of 3-dehydrocapnine to capnine.","The molecular function of this protein is likely to be involved in lipid metabolism, specifically in the oxidation of fatty acids. As a part of the 3-oxoacyl-ACP reductase complex, this protein is likely to be involved in the reduction of 3-oxoacyl-ACP to (R)-3-hydroxyacyl-ACP, which is a key step in the beta-oxidation of fatty acids. However, the exact function of this protein is not explicitly stated in the provided information.",No,Maybe,Maybe,No,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0004316,GO:0004316,GO:0004316,GO:0004316,1.0,0.6019,0.6019,0.6019,0.6019,5,0.6815,0.1835,no
CAPC_ORNRH,A0A3R5XUE6,Reference,Bacteria,283,"Reductase involved in the biosynthesis of capnine, a sulfonolipid present in the outer membrane of gliding Bacteroidetes and essential for gliding motility. Catalyzes the reduction of 3-dehydrocapnine to capnine.","Reductase involved in the biosynthesis of capnine, a sulfonolipid present in the outer membrane of gliding Bacteroidetes and essential for gliding motility. Catalyzes the reduction of 3-dehydrocapnine to capnine.",,,,,,,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1835,no
MFMMG_SIMTE,A0A429XDI3,ESM2Text,Bacteria,388,Hydrolase involved in the degradation of N(tele)- methylhistidine (Ntau-methylhistidine). Catalyzes the formation of N-methylformamide and L-glutamate from methylformimidoylglutamate.,Cleaves the N-terminal amino acid of tripeptides.,No,No,No,No,No,not-Yes,GO:0004177; GO:0046872,GO:0004177,GO:0008233,GO:0004177,GO:0004177,GO:0004177,0.6944,0.5534,0.6944,0.6944,0.6944,5,0.6662,0.2208,no
MFMMG_SIMTE,A0A429XDI3,Prot2Text,Bacteria,388,Hydrolase involved in the degradation of N(tele)- methylhistidine (Ntau-methylhistidine). Catalyzes the formation of N-methylformamide and L-glutamate from methylformimidoylglutamate.,Has a low activity toward the type I polysaccharide substrate PscA.,No,No,No,No,No,not-Yes,GO:0004177; GO:0046872,,,,,,,,,,,0,,0.2208,no
MFMMG_SIMTE,A0A429XDI3,ProtT3,Bacteria,388,Hydrolase involved in the degradation of N(tele)- methylhistidine (Ntau-methylhistidine). Catalyzes the formation of N-methylformamide and L-glutamate from methylformimidoylglutamate.,Belongs to the peptidase M20A family,Vague,Vague,Vague,Vague,No,not-Yes,GO:0004177; GO:0046872,GO:0008237; GO:0046872,GO:0008235,,GO:0008235,GO:0008235,0.8293,0.489,,0.489,0.489,4,0.5741,0.2208,no
MFMMG_SIMTE,A0A429XDI3,ProtTale,Bacteria,388,Hydrolase involved in the degradation of N(tele)- methylhistidine (Ntau-methylhistidine). Catalyzes the formation of N-methylformamide and L-glutamate from methylformimidoylglutamate.,Catalyzes the cleavage of N-terminal amino acids from peptides.,No,No,No,No,No,not-Yes,GO:0004177; GO:0046872,GO:0004177,GO:0004177,GO:0004177,GO:0004177,GO:0004177,0.6944,0.6944,0.6944,0.6944,0.6944,5,0.6944,0.2208,no
MFMMG_SIMTE,A0A429XDI3,Protein2Text,Bacteria,388,Hydrolase involved in the degradation of N(tele)- methylhistidine (Ntau-methylhistidine). Catalyzes the formation of N-methylformamide and L-glutamate from methylformimidoylglutamate.,"The molecular function of this protein is to catalyze the hydrolysis of the carboxyl group of a branched-chain amino acid (such as valine, leucine, or isoleucine) in an amino-acid degradative pathway. More specifically, it is a metalloaminopeptidase that cleaves branched-chain amino acids (BCAAs) at the C-terminus.",No,No,No,No,No,not-Yes,GO:0004177; GO:0046872,GO:0008233,GO:0004177; GO:0008237,GO:0004177; GO:0008237,,GO:0004177,0.5534,0.6886,0.6886,,0.6944,4,0.6562,0.2208,no
MFMMG_SIMTE,A0A429XDI3,Reference,Bacteria,388,Hydrolase involved in the degradation of N(tele)- methylhistidine (Ntau-methylhistidine). Catalyzes the formation of N-methylformamide and L-glutamate from methylformimidoylglutamate.,Hydrolase involved in the degradation of N(tele)- methylhistidine (Ntau-methylhistidine). Catalyzes the formation of N-methylformamide and L-glutamate from methylformimidoylglutamate.,,,,,,,GO:0004177; GO:0046872,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016787,0.423,0.423,0.423,0.423,0.423,5,0.423,0.2208,no
PPZ1_METMF,A0A455ZJM4,ESM2Text,Eukaryota,424,"Sulfatase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. The role of ppz1 within the pathway has still to be determined. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N- methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8- hydroxyperamine whereas ppzD converts L-proline into trans-4-hydroxy-L- proline, a precursor of peramine biosynthesis.",Oxidoreductase involved in the degradation pathway of the polyamine agmatine. Catalyzes the hydrolysis of the hydroxyl group of N-acetyl-D-glucosamine to yield D-glucosamine-1-phosphate.,No,No,No,No,No,not-Yes,GO:0005539; GO:0046872; GO:0008449,,,,,,,,,,,0,,0.3515,no
PPZ1_METMF,A0A455ZJM4,Prot2Text,Eukaryota,424,"Sulfatase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. The role of ppz1 within the pathway has still to be determined. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N- methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8- hydroxyperamine whereas ppzD converts L-proline into trans-4-hydroxy-L- proline, a precursor of peramine biosynthesis.","Anhydrolase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The nonribosomal peptide synthetase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.",No,No,No,No,No,not-Yes,GO:0005539; GO:0046872; GO:0008449,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016787,0.3938,0.3938,0.3938,0.3938,0.3938,5,0.3938,0.3515,no
PPZ1_METMF,A0A455ZJM4,ProtT3,Eukaryota,424,"Sulfatase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. The role of ppz1 within the pathway has still to be determined. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N- methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8- hydroxyperamine whereas ppzD converts L-proline into trans-4-hydroxy-L- proline, a precursor of peramine biosynthesis.","Secreted, extracellular space, extracellular matrix. Belongs to the 'GDSL' lipolytic enzyme family",Vague,Vague,No,Vague,No,not-Yes,GO:0005539; GO:0046872; GO:0008449,GO:0016788,GO:0052689,,GO:0052689,GO:0016788,0.4395,0.3641,,0.3641,0.4395,4,0.4018,0.3515,no
PPZ1_METMF,A0A455ZJM4,ProtTale,Eukaryota,424,"Sulfatase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. The role of ppz1 within the pathway has still to be determined. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N- methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8- hydroxyperamine whereas ppzD converts L-proline into trans-4-hydroxy-L- proline, a precursor of peramine biosynthesis.","Catalyzes the hydrolysis of N-methylnicotinamide (N(1)-methyl-NAD(+) or NMN(+)). May function in the degradation of N(1)-methyl-NAD(+), a by-product of NAD(+) biosynthesis, and in the removal of N(1)-methylnicotinamide from the body.",No,No,No,No,No,not-Yes,GO:0005539; GO:0046872; GO:0008449,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016787,0.3938,0.3938,0.3938,0.3938,0.3938,5,0.3938,0.3515,no
PPZ1_METMF,A0A455ZJM4,Protein2Text,Eukaryota,424,"Sulfatase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. The role of ppz1 within the pathway has still to be determined. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N- methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8- hydroxyperamine whereas ppzD converts L-proline into trans-4-hydroxy-L- proline, a precursor of peramine biosynthesis.","This protein is involved in the hydrolysis of methyl ester groups, which is a key process in the degradation of methyl esters. More specifically, it is likely to be involved in the hydrolysis of the methyl ester group in methyl esterified compounds, such as methyl esters of fatty acids or other carboxylic acids. This process is likely to be part of a larger metabolic pathway, possibly related to the breakdown and utilization of organic compounds. 

In more detail, this protein is likely to have a molecular function that involves the following:

1. Binding to a substrate: The protein binds to a methyl esterified compound, such as a methyl ester of a fatty acid or other carboxylic acid.
2. Catalysis: The protein catalyzes the hydrolysis of the methyl ester group, resulting in the release of a carboxylic acid and methanol.
3. Hydrolysis: The protein uses water to hydrolyze the methyl ester group, resulting in the release of a carboxylic acid and methanol.

Overall, the molecular function of this protein is likely to be involved in the breakdown and utilization of organic compounds, possibly as part of a larger metabolic pathway.",No,No,No,No,No,not-Yes,GO:0005539; GO:0046872; GO:0008449,GO:0016788,GO:0016788,GO:0016788,GO:0016788,GO:0016788,0.4395,0.4395,0.4395,0.4395,0.4395,5,0.4395,0.3515,no
PPZ1_METMF,A0A455ZJM4,Reference,Eukaryota,424,"Sulfatase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. The role of ppz1 within the pathway has still to be determined. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N- methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8- hydroxyperamine whereas ppzD converts L-proline into trans-4-hydroxy-L- proline, a precursor of peramine biosynthesis.","Sulfatase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. The role of ppz1 within the pathway has still to be determined. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N- methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8- hydroxyperamine whereas ppzD converts L-proline into trans-4-hydroxy-L- proline, a precursor of peramine biosynthesis.",,,,,,,GO:0005539; GO:0046872; GO:0008449,GO:0008484,GO:0008484,GO:0008484,,GO:0016787,0.4917,0.4917,0.4917,,0.3938,4,0.4672,0.3515,no
PPZF_METMF,A0A455ZLR3,ESM2Text,Eukaryota,340,"Sulfotransferase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. The role of ppzF within the pathway has still to be determined. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N- methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8- hydroxyperamine whereas ppzD converts L-proline into trans-4-hydroxy-L- proline, a precursor of peramine biosynthesis.",Bifunctional enzyme exhibiting tyrosine acetyltransferase and chromatin acetyltransferase activities in addition to pyruvate synthase.,No,No,No,No,No,not-Yes,GO:0016740,GO:0016407,GO:0016407,,GO:0016407,,0.6019,0.6019,,0.6019,,3,0.6019,0.1284,no
PPZF_METMF,A0A455ZLR3,Prot2Text,Eukaryota,340,"Sulfotransferase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. The role of ppzF within the pathway has still to be determined. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N- methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8- hydroxyperamine whereas ppzD converts L-proline into trans-4-hydroxy-L- proline, a precursor of peramine biosynthesis.","Is involved in the biosynthesis of the antibiotic indolmycin, an inhibitor of the bacterial tryptophan-tRNA synthetases. Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to the 6-O-position of the indole moiety of tryptophan-tRNA to yield N-acetylparomamine.",No,No,No,No,No,not-Yes,GO:0016740,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.6019,0.6019,0.6019,0.6019,0.6019,5,0.6019,0.1284,no
PPZF_METMF,A0A455ZLR3,ProtT3,Eukaryota,340,"Sulfotransferase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. The role of ppzF within the pathway has still to be determined. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N- methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8- hydroxyperamine whereas ppzD converts L-proline into trans-4-hydroxy-L- proline, a precursor of peramine biosynthesis.","Part of the gene cluster that mediates the biosynthesis of the fungal meroterpenoid acetoxydehydroaustin . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By similarity). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (By similarity). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the terpene cyclase ausO",No,No,No,No,No,not-Yes,GO:0016740,,,,,,,,,,,0,,0.1284,no
PPZF_METMF,A0A455ZLR3,ProtTale,Eukaryota,340,"Sulfotransferase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. The role of ppzF within the pathway has still to be determined. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N- methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8- hydroxyperamine whereas ppzD converts L-proline into trans-4-hydroxy-L- proline, a precursor of peramine biosynthesis.",Epimerase involved in the biosynthesis of the siderophore enterobactin. Catalyzes the epimerization of L-ornithine to form N-acetyl-L-ornithine (N- acetyl-L-ornithine).,No,No,No,No,No,not-Yes,GO:0016740,GO:0016857,GO:0016854,GO:0016854,GO:0016854,GO:0016854,0.4071,0.4807,0.4807,0.4807,0.4807,5,0.466,0.1284,no
PPZF_METMF,A0A455ZLR3,Protein2Text,Eukaryota,340,"Sulfotransferase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. The role of ppzF within the pathway has still to be determined. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N- methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8- hydroxyperamine whereas ppzD converts L-proline into trans-4-hydroxy-L- proline, a precursor of peramine biosynthesis.","The molecular function of this protein is not explicitly stated in the provided text. However, based on its name, it is likely involved in the modification of a nucleotide, possibly uridine, and is therefore likely to have a role in nucleotide metabolism or nucleotide modification. 

In general, enzymes involved in nucleotide metabolism or nucleotide modification can perform a variety of molecular functions, such as:

* Catalyzing the transfer of a group from one molecule to another (e.g. methyltransferase)
* Catalyzing the formation of a covalent bond between two molecules (e.g. kinase)
* Catalyzing the hydrolysis of a covalent bond between two molecules (e.g. phosphatase)
* Catalyzing the isomerization of a molecule (e.g. isomerase)

Without more specific information, it is difficult to determine the exact molecular function of this protein.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0016740,,,,,,,,,,,0,,0.1284,no
PPZF_METMF,A0A455ZLR3,Reference,Eukaryota,340,"Sulfotransferase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. The role of ppzF within the pathway has still to be determined. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N- methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8- hydroxyperamine whereas ppzD converts L-proline into trans-4-hydroxy-L- proline, a precursor of peramine biosynthesis.","Sulfotransferase; part of the gene cluster that mediates the biosynthesis of pyrrolopyrazines, secondary metabolites showing insecticidal activity. The role of ppzF within the pathway has still to be determined. The single multifunctional NRPS ppzA is sufficient to produce peramine via condensation of 1-pyrroline-5-carboxylate and arginine, N- methylation of the alpha-amino group of arginine and reduction of the thioester and the cyclization to form an iminium ion resulting in release from the peptide synthetase. Deprotonation of this intermediate and oxidation of the pyrroline ring would give rise to peramine. In Epichloe species that produce only peramine, the peramine synthetase gene is not localized in a gene cluster, in contrast to Metarhizium species that contain additional pyrrolopyrazine biosynthesis genes. The 2-oxoglutarate-Fe(II) type oxidoreductase ppzC hydroxylates peramine to yield the newly identified compound 8- hydroxyperamine whereas ppzD converts L-proline into trans-4-hydroxy-L- proline, a precursor of peramine biosynthesis.",,,,,,,GO:0016740,GO:0008146,GO:0016782,GO:0008146,GO:0008146,GO:0016782,0.6897,0.8145,0.6897,0.6897,0.8145,5,0.7396,0.1284,no
VVIB_VIRVR,A0A6A6H2E0,ESM2Text,Eukaryota,333,Terpene cyclase that cyclizes farnesyl diphosphate (FPP) to drim-8-ene diphosphate used by vviA as the native prenyl donor to catalyze the prenylation of D-mannitol on C-3'-OH to afford sporulositol A.,"Catalyzes the formation of 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A, the precursor of the prosthetic group of the holo-acyl carrier protein (gamma chain) of citrate lyase, from ATP and dephospho-CoA.",No,No,No,No,No,not-Yes,GO:0016829,GO:0016779,GO:0016779,GO:0016779,GO:0016879,GO:0016779,0.4071,0.4071,0.4071,0.4807,0.4071,5,0.4218,0.227,no
VVIB_VIRVR,A0A6A6H2E0,Prot2Text,Eukaryota,333,Terpene cyclase that cyclizes farnesyl diphosphate (FPP) to drim-8-ene diphosphate used by vviA as the native prenyl donor to catalyze the prenylation of D-mannitol on C-3'-OH to afford sporulositol A.,Involved in the production of the bacteriocin subtilosin.,No,No,No,No,No,not-Yes,GO:0016829,,,,,,,,,,,0,,0.227,no
VVIB_VIRVR,A0A6A6H2E0,ProtT3,Eukaryota,333,Terpene cyclase that cyclizes farnesyl diphosphate (FPP) to drim-8-ene diphosphate used by vviA as the native prenyl donor to catalyze the prenylation of D-mannitol on C-3'-OH to afford sporulositol A.,Cytoplasm Nucleus. Belongs to the TPP enzyme family,Vague,Vague,No,Vague,Vague,not-Yes,GO:0016829,GO:0030976,GO:0030976,,GO:0030976,,0.1079,0.1079,,0.1079,,3,0.1079,0.227,no
VVIB_VIRVR,A0A6A6H2E0,ProtTale,Eukaryota,333,Terpene cyclase that cyclizes farnesyl diphosphate (FPP) to drim-8-ene diphosphate used by vviA as the native prenyl donor to catalyze the prenylation of D-mannitol on C-3'-OH to afford sporulositol A.,"Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity.",No,No,No,No,No,not-Yes,GO:0016829,,,,,,,,,,,0,,0.227,no
VVIB_VIRVR,A0A6A6H2E0,Protein2Text,Eukaryota,333,Terpene cyclase that cyclizes farnesyl diphosphate (FPP) to drim-8-ene diphosphate used by vviA as the native prenyl donor to catalyze the prenylation of D-mannitol on C-3'-OH to afford sporulositol A.,"This protein is likely involved in the synthesis or modification of a specific molecule, as suggested by its name and the fact that it is associated with a metabolic pathway. However, without more specific information, it is difficult to determine the exact molecular function of this protein.

Based on the name ""Cytochrome P450 2S1"", it is likely that this protein is involved in the metabolism of a specific compound, such as a steroid or a drug. Cytochrome P450 enzymes are a family of enzymes that are involved in the metabolism of a wide range of compounds, including drugs, steroids, and other lipids.

Some possible molecular functions of this protein include:

* Oxidation of a specific substrate, such as a steroid or a drug
* Hydroxylation of a specific substrate, such as a fatty acid or a steroid
* Epoxidation of a specific substrate, such as an alkene
* Other oxidative reactions, such as dehydrogenation or dehydroxylation

However, without more specific information, it is difficult to determine the exact molecular function of this protein. Further research would be needed to determine the specific function of this protein and its role in the metabolism of specific compounds.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016829,GO:0004497,GO:0004497; GO:0020037,GO:0004497; GO:0020037,GO:0004497,GO:0004497,0.4807,0.3917,0.3917,0.4807,0.4807,5,0.4451,0.227,no
VVIB_VIRVR,A0A6A6H2E0,Reference,Eukaryota,333,Terpene cyclase that cyclizes farnesyl diphosphate (FPP) to drim-8-ene diphosphate used by vviA as the native prenyl donor to catalyze the prenylation of D-mannitol on C-3'-OH to afford sporulositol A.,Terpene cyclase that cyclizes farnesyl diphosphate (FPP) to drim-8-ene diphosphate used by vviA as the native prenyl donor to catalyze the prenylation of D-mannitol on C-3'-OH to afford sporulositol A.,,,,,,,GO:0016829,GO:0016829,GO:0016829,GO:0010333,GO:0016829,GO:0010333,1.0,1.0,0.6019,1.0,0.6019,5,0.8408,0.227,no
RP147_MONPV,A0A7H0DN77,ESM2Text,Viruses,1286,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.","Catalyzes the specific cleavage of luminal amino acids (Glu, Ile, Val, Thr, or Tyr) in the degradative direction to produce the corresponding alpha-amino acid (Ala, Gly, Pro, Ser, Thr, or Val). Has a role in the recycling of nitrogen from nitrogen assimilation in developing seeds.",No,No,No,No,No,not-Yes,GO:0003677; GO:0003899,GO:0004521,GO:0004521,GO:0004521,GO:0004521,GO:0004521,0.2541,0.2541,0.2541,0.2541,0.2541,5,0.2541,0.6212,yes
RP147_MONPV,A0A7H0DN77,Prot2Text,Viruses,1286,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.","Catalyzes the specific cleavage of luminal amino acids (Glu, Ile, Val, Thr, or Tyr) in the degradative direction to produce the corresponding alpha-amino acid (Ala, Gly, Pro, Ser, Thr, or Val). Has a role in the recycling of nitrogen from nitrogen assimilation in developing seeds.",No,No,No,No,No,not-Yes,GO:0003677; GO:0003899,GO:0004521,GO:0004521,GO:0004521,GO:0004521,GO:0004521,0.2541,0.2541,0.2541,0.2541,0.2541,5,0.2541,0.6212,yes
RP147_MONPV,A0A7H0DN77,ProtT3,Viruses,1286,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.",DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA polymerase subunit family,Yes,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0003677; GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.6983,0.6983,0.6983,0.6983,0.6983,5,0.6983,0.6212,yes
RP147_MONPV,A0A7H0DN77,ProtTale,Viruses,1286,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.",Catalytic component of the DNA-dependent RNA polymerase that catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit.,Yes,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0003677; GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.6983,0.6983,0.6983,0.6983,0.6983,5,0.6983,0.6212,yes
RP147_MONPV,A0A7H0DN77,Protein2Text,Viruses,1286,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.","This protein is a subunit of DNA polymerase, which is an enzyme that plays a crucial role in DNA replication and repair. Specifically, it is a subunit of DNA polymerase that is responsible for synthesizing new DNA strands by adding nucleotides to a template strand.",No,No,No,No,No,not-Yes,GO:0003677; GO:0003899,,,,,,,,,,,0,,0.6212,yes
RP147_MONPV,A0A7H0DN77,Reference,Viruses,1286,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.","Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.",,,,,,,GO:0003677; GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.6983,0.6983,0.6983,0.6983,0.6983,5,0.6983,0.6212,yes
ACOMT_ASPCH,A0A7R7ZLE4,ESM2Text,Eukaryota,222,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of physcion, a natural anthraquinone fungicide that can prevent plant fungal infections. Within the pathway, the O-methyltransferase AcOMT catalyzes the last step by transferring a methyl group to C-6 hydroxyl of emodin to form physcion. AcOMT may also methylate the C-6 hydroxyl group of emodin anthrone to produce physcion-anthrone B. The pathway begins with the polyketide synthase AcPKS that condenses 8 malonyl-CoA units to synthesize atrochrysone thioester which is released from the synthase by the atrochrysone carboxyl ACP thioesterase AcTE that breaks the thioester bond and leads to free atrochrysone carboxylic acid. Spontaneous decarboxylation of atrochrysone carboxylic acid leads to the formation of atrochrysone. Then, atrochrysone undergoes spontaneous dehydration and oxidation, giving the products emodin anthrone and emodin. The O-methyltransferase AcOMT then methylates the C-6 hydroxyl of emodin to form physcion (Probable).","N-methyltransferase; part of the gene cluster that mediates the biosynthesis of sordarin and hypoxysordarin, glycoside antibiotics with a unique tetracyclic diterpene aglycone structure. First, the geranylgeranyl diphosphate synthase sdnC constructs GGDP from farnesyl diphosphate and isopentenyl diphosphate. The diterpene cyclase sdnA then catalyzes the cyclization of GGDP to afford cycloaraneosene. Cycloaraneosene is then hydroxylated four times by the putative cytochrome P450 monooxygenases sdnB, sdnE, sdnF and sdnH to give a hydroxylated cycloaraneosene derivative such as cycloaraneosene-8,9,13,19-tetraol. Although sdnB is the catalytic core component of the sordar polymerization complex, it is also involved in the nonenzymatic component of the sordar.",Maybe,Maybe,Yes,Maybe,Maybe,not-Yes,GO:0008168,GO:0008170,GO:0008168,GO:0008170,GO:0008168,GO:0008170,0.8582,1.0,0.8582,1.0,0.8582,5,0.9149,0.2918,no
ACOMT_ASPCH,A0A7R7ZLE4,Prot2Text,Eukaryota,222,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of physcion, a natural anthraquinone fungicide that can prevent plant fungal infections. Within the pathway, the O-methyltransferase AcOMT catalyzes the last step by transferring a methyl group to C-6 hydroxyl of emodin to form physcion. AcOMT may also methylate the C-6 hydroxyl group of emodin anthrone to produce physcion-anthrone B. The pathway begins with the polyketide synthase AcPKS that condenses 8 malonyl-CoA units to synthesize atrochrysone thioester which is released from the synthase by the atrochrysone carboxyl ACP thioesterase AcTE that breaks the thioester bond and leads to free atrochrysone carboxylic acid. Spontaneous decarboxylation of atrochrysone carboxylic acid leads to the formation of atrochrysone. Then, atrochrysone undergoes spontaneous dehydration and oxidation, giving the products emodin anthrone and emodin. The O-methyltransferase AcOMT then methylates the C-6 hydroxyl of emodin to form physcion (Probable).","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation. The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA. The terpene cyclase/mutase atnI then initiates the sequential tricyclic",Yes,Yes,Yes,Maybe,Yes,Yes,GO:0008168,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.2918,no
ACOMT_ASPCH,A0A7R7ZLE4,ProtT3,Eukaryota,222,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of physcion, a natural anthraquinone fungicide that can prevent plant fungal infections. Within the pathway, the O-methyltransferase AcOMT catalyzes the last step by transferring a methyl group to C-6 hydroxyl of emodin to form physcion. AcOMT may also methylate the C-6 hydroxyl group of emodin anthrone to produce physcion-anthrone B. The pathway begins with the polyketide synthase AcPKS that condenses 8 malonyl-CoA units to synthesize atrochrysone thioester which is released from the synthase by the atrochrysone carboxyl ACP thioesterase AcTE that breaks the thioester bond and leads to free atrochrysone carboxylic acid. Spontaneous decarboxylation of atrochrysone carboxylic acid leads to the formation of atrochrysone. Then, atrochrysone undergoes spontaneous dehydration and oxidation, giving the products emodin anthrone and emodin. The O-methyltransferase AcOMT then methylates the C-6 hydroxyl of emodin to form physcion (Probable).","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By similarity). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (By similarity). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the ter",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008168,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.2918,no
ACOMT_ASPCH,A0A7R7ZLE4,ProtTale,Eukaryota,222,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of physcion, a natural anthraquinone fungicide that can prevent plant fungal infections. Within the pathway, the O-methyltransferase AcOMT catalyzes the last step by transferring a methyl group to C-6 hydroxyl of emodin to form physcion. AcOMT may also methylate the C-6 hydroxyl group of emodin anthrone to produce physcion-anthrone B. The pathway begins with the polyketide synthase AcPKS that condenses 8 malonyl-CoA units to synthesize atrochrysone thioester which is released from the synthase by the atrochrysone carboxyl ACP thioesterase AcTE that breaks the thioester bond and leads to free atrochrysone carboxylic acid. Spontaneous decarboxylation of atrochrysone carboxylic acid leads to the formation of atrochrysone. Then, atrochrysone undergoes spontaneous dehydration and oxidation, giving the products emodin anthrone and emodin. The O-methyltransferase AcOMT then methylates the C-6 hydroxyl of emodin to form physcion (Probable).","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties. L-aspartate is suggested as fusaric acid amino acid precursor. The first step in the biosynthesis of fusaric acid is the production of 4-hydroxy-L-tryptophan (4-H2LW) by the polyketide synthase fusA. 4-H2LW is then methylated by fusI to yield 4-methoxy-L- tryptophan (4-MeLW). FusB and fus",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008168,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.2918,no
ACOMT_ASPCH,A0A7R7ZLE4,Protein2Text,Eukaryota,222,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of physcion, a natural anthraquinone fungicide that can prevent plant fungal infections. Within the pathway, the O-methyltransferase AcOMT catalyzes the last step by transferring a methyl group to C-6 hydroxyl of emodin to form physcion. AcOMT may also methylate the C-6 hydroxyl group of emodin anthrone to produce physcion-anthrone B. The pathway begins with the polyketide synthase AcPKS that condenses 8 malonyl-CoA units to synthesize atrochrysone thioester which is released from the synthase by the atrochrysone carboxyl ACP thioesterase AcTE that breaks the thioester bond and leads to free atrochrysone carboxylic acid. Spontaneous decarboxylation of atrochrysone carboxylic acid leads to the formation of atrochrysone. Then, atrochrysone undergoes spontaneous dehydration and oxidation, giving the products emodin anthrone and emodin. The O-methyltransferase AcOMT then methylates the C-6 hydroxyl of emodin to form physcion (Probable).","This protein is involved in the methylation of a molecule. More specifically, it is a methyltransferase that catalyzes the transfer of a methyl group to a molecule, resulting in its methylation. This is a key step in the biosynthesis of certain molecules. The exact substrate of this protein is not specified in the provided information, but it is likely involved in the methylation of a small molecule.",Vague,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2918,no
ACOMT_ASPCH,A0A7R7ZLE4,Reference,Eukaryota,222,"O-methyltransferase; part of the gene cluster that mediates the biosynthesis of physcion, a natural anthraquinone fungicide that can prevent plant fungal infections. Within the pathway, the O-methyltransferase AcOMT catalyzes the last step by transferring a methyl group to C-6 hydroxyl of emodin to form physcion. AcOMT may also methylate the C-6 hydroxyl group of emodin anthrone to produce physcion-anthrone B. The pathway begins with the polyketide synthase AcPKS that condenses 8 malonyl-CoA units to synthesize atrochrysone thioester which is released from the synthase by the atrochrysone carboxyl ACP thioesterase AcTE that breaks the thioester bond and leads to free atrochrysone carboxylic acid. Spontaneous decarboxylation of atrochrysone carboxylic acid leads to the formation of atrochrysone. Then, atrochrysone undergoes spontaneous dehydration and oxidation, giving the products emodin anthrone and emodin. The O-methyltransferase AcOMT then methylates the C-6 hydroxyl of emodin to form physcion (Probable).","O-methyltransferase; part of the gene cluster that mediates the biosynthesis of physcion, a natural anthraquinone fungicide that can prevent plant fungal infections. Within the pathway, the O-methyltransferase AcOMT catalyzes the last step by transferring a methyl group to C-6 hydroxyl of emodin to form physcion. AcOMT may also methylate the C-6 hydroxyl group of emodin anthrone to produce physcion-anthrone B. The pathway begins with the polyketide synthase AcPKS that condenses 8 malonyl-CoA units to synthesize atrochrysone thioester which is released from the synthase by the atrochrysone carboxyl ACP thioesterase AcTE that breaks the thioester bond and leads to free atrochrysone carboxylic acid. Spontaneous decarboxylation of atrochrysone carboxylic acid leads to the formation of atrochrysone. Then, atrochrysone undergoes spontaneous dehydration and oxidation, giving the products emodin anthrone and emodin. The O-methyltransferase AcOMT then methylates the C-6 hydroxyl of emodin to form physcion (Probable).",,,,,,,GO:0008168,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.2918,no
FRZH_CLASX,A0A7T8F1L1,ESM2Text,Eukaryota,125,"Aldolase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzH is a new kind of aldolase with no similarities to known aldolases, and which catalyzes the intramolecular aldol condensation via formation of a C9-C3' bond to yield an aza-tricyclic product. The biosynthesis of (-)-FR901483 starts with the condensation of two L- tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4- diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably the most effective protein, although it reduces the global protein synthesis in cells that do not acquire fatty acid marks. FABP5, FABP6, FABP8, FABP9, FABP10, FABP11, FABP12 and FABP13 are effective substrates. FABP15 forms an acyl-CoA-binding protein, with the highest affinity for C22-CoA, followed by those for C20-CoA and C24-CoA. FABP7 forms an acyl-CoA-binding protein, with the highest affinity for C20-CoA. FABP6 forms an acyl-CoA-binding protein, while FABP10 forms an acyl-CoA-binding protein.",No,No,No,No,No,not-Yes,GO:0016853,GO:0005504; GO:0000062,GO:0005504,GO:0005504,GO:0005504; GO:0000062,GO:0005504,0.1229,0.1328,0.1328,0.1229,0.1328,5,0.1288,0.3184,no
FRZH_CLASX,A0A7T8F1L1,Prot2Text,Eukaryota,125,"Aldolase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzH is a new kind of aldolase with no similarities to known aldolases, and which catalyzes the intramolecular aldol condensation via formation of a C9-C3' bond to yield an aza-tricyclic product. The biosynthesis of (-)-FR901483 starts with the condensation of two L- tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4- diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.",FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABPs are important factors that contribute to the intracellular elastic fiber network and to the regulation of lipid biosynthesis.,No,No,No,No,No,not-Yes,GO:0016853,GO:0005504,GO:0005504,GO:0005504,GO:0005504,GO:0005504,0.1328,0.1328,0.1328,0.1328,0.1328,5,0.1328,0.3184,no
FRZH_CLASX,A0A7T8F1L1,ProtT3,Eukaryota,125,"Aldolase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzH is a new kind of aldolase with no similarities to known aldolases, and which catalyzes the intramolecular aldol condensation via formation of a C9-C3' bond to yield an aza-tricyclic product. The biosynthesis of (-)-FR901483 starts with the condensation of two L- tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4- diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.",Belongs to the NmrA-type oxidoreductase family,Vague,Vague,Vague,Vague,No,not-Yes,GO:0016853,GO:0016491,GO:0016491,,GO:0016491,,0.5902,0.5902,,0.5902,,3,0.5902,0.3184,no
FRZH_CLASX,A0A7T8F1L1,ProtTale,Eukaryota,125,"Aldolase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzH is a new kind of aldolase with no similarities to known aldolases, and which catalyzes the intramolecular aldol condensation via formation of a C9-C3' bond to yield an aza-tricyclic product. The biosynthesis of (-)-FR901483 starts with the condensation of two L- tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4- diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","Involved in the degradation of pyrroline-5-carboxylate (P5C), a major inhibitor of alpha-ketoacid dehydrogenase complexes (AKDCs), by catalyzing an oxidative cleavage between C-4 and C-5 of the pyrroline ring of P5C to yield glutamic acid and pyrrolidine-2,5-dicarboxylic acid (PDC).",No,No,No,No,No,not-Yes,GO:0016853,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.5902,0.5902,0.5902,0.5902,0.5902,5,0.5902,0.3184,no
FRZH_CLASX,A0A7T8F1L1,Protein2Text,Eukaryota,125,"Aldolase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzH is a new kind of aldolase with no similarities to known aldolases, and which catalyzes the intramolecular aldol condensation via formation of a C9-C3' bond to yield an aza-tricyclic product. The biosynthesis of (-)-FR901483 starts with the condensation of two L- tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4- diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","The molecular function of this protein is unknown. However, it is involved in the degradation of certain substrates. 
The protein is part of the amidohydrolase family. Amidohydrolases catalyze the hydrolysis of a variety of amide bonds. They are involved in the degradation of certain substrates. This protein is likely involved in the degradation of certain substrates as well. However, its exact function is unknown. 
It is also involved in the degradation of certain proteins. This protein is likely involved in the degradation of certain proteins as well. However, its exact function is unknown. 
It is also involved in the degradation of certain peptides. This protein is likely involved in the degradation of certain peptides as well. However, its exact function is unknown. 
It is also involved in the degradation of certain nucleotides. This protein is likely involved in the degradation of certain nucleotides as well. However, its exact function is unknown. 
It is also involved in the degradation of certain amino acids. This protein is likely involved in the degradation of certain amino acids as well. However, its exact function is unknown. 
It is also involved in the degradation of certain compounds. This protein is likely involved in the degradation of certain compounds as well. However, its exact function is unknown.",Vague,No,Vague,Vague,No,not-Yes,GO:0016853,,,,,GO:0016810,,,,,0.4807,1,0.4807,0.3184,no
FRZH_CLASX,A0A7T8F1L1,Reference,Eukaryota,125,"Aldolase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzH is a new kind of aldolase with no similarities to known aldolases, and which catalyzes the intramolecular aldol condensation via formation of a C9-C3' bond to yield an aza-tricyclic product. The biosynthesis of (-)-FR901483 starts with the condensation of two L- tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4- diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","Aldolase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzH is a new kind of aldolase with no similarities to known aldolases, and which catalyzes the intramolecular aldol condensation via formation of a C9-C3' bond to yield an aza-tricyclic product. The biosynthesis of (-)-FR901483 starts with the condensation of two L- tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L-tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4- diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.",,,,,,,GO:0016853,GO:0016832,GO:0016832,GO:0016832,GO:0016832,GO:0016832,0.4071,0.4071,0.4071,0.4071,0.4071,5,0.4071,0.3184,no
FRZE_CLASX,A0A7T8F1L3,ESM2Text,Eukaryota,289,"N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzE methylates the amine at position C10'. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L- tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.",7-dehydrocholesterol methyl ester methyltransferase involved in the biosynthesis of 7-dehydrocholesterol (pre-Chol-H(4)A) (H(4)C(2)). Affects the ability of the bacterium to bind and transport cholesterol.,No,No,Yes,Maybe,Maybe,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1364,no
FRZE_CLASX,A0A7T8F1L3,Prot2Text,Eukaryota,289,"N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzE methylates the amine at position C10'. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L- tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","Acetyltransferase involved in the biosynthesis of the permethylated L-rhamnose moiety of elloramycin, an antitumor polyketide. The enzyme is specific for dimethylated l-rhamnose.",No,No,Maybe,No,No,not-Yes,GO:0008168,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.3987,0.3987,0.3987,0.3987,0.3987,5,0.3987,0.1364,no
FRZE_CLASX,A0A7T8F1L3,ProtT3,Eukaryota,289,"N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzE methylates the amine at position C10'. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L- tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.",Methyltransferase that catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to the hydroxyl group of 4'-phosphopantetheine to produce 4'-phosphopantetheine methyl ester (PPE). Cytoplasm. Belongs to the AdoMetMT family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1364,no
FRZE_CLASX,A0A7T8F1L3,ProtTale,Eukaryota,289,"N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzE methylates the amine at position C10'. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L- tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","Methyltransferase; part of the gene cluster that mediates the biosynthesis of the tetrahydroxanthone dimer secalonic acid D. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase AacuL (Probable). The atrochrysone carboxyl ACP thioesterase AacuM then breaks the thioester bond and releases the atrochrysone carboxylic acid from AacuL (Probable). Atrochrysone carboxylic acid is decarboxylated by the decarboxylase AacuI, and oxidized by the anthrone oxygenase AacuH to yield emodin",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1364,no
FRZE_CLASX,A0A7T8F1L3,Protein2Text,Eukaryota,289,"N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzE methylates the amine at position C10'. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L- tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","The molecular function of this protein is a methyltransferase.
It is involved in the transfer of a methyl group to a molecule.",Vague,Vague,Maybe,Vague,Vague,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1364,no
FRZE_CLASX,A0A7T8F1L3,Reference,Eukaryota,289,"N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzE methylates the amine at position C10'. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L- tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.","N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the alkaloid (-)-FR901483, a potent immunosuppressant that shows efficacy in animal models and a probable inhibitor of purine nucleotide biosynthesis by targeting phosphoribosylpyrophosphate amidotransferase (PPAT). Within the pathway, FrzE methylates the amine at position C10'. The biosynthesis of (-)-FR901483 starts with the condensation of two L-tyrosines to yield (S,S)-dityrosyl-piperazine. This process occurs in 3 steps with the non-canonical nonribosomal peptide synthetase FrzA catalyzing the reduction of L-tyrosine into L- tyrosinal, the spontaneous condensation of 2 L-tyrosinal units, and the subsequent reduction by the NmrA-like family domain-containing oxidoreductase FrzB. The cytochrome P450 monooxygenase FrzC then performs coupling between N10 and C1' to morph the piperazine into a 1,4-diazabicyclo[3.2.1]octane spiro-fused to a 2,5-cyclohexadienone. The dienone portion is further reduced to cyclohexanone by the flavin- dependent reductase FrzD. The methyltranserases (MTs) FrzE and FrzF are then involved in the methylation at the C10' amine and the C4 phenolic oxygen, respectively. The order of the two MTs appear to be interchangeable. Cleavage of the C9-N10' bond by the dioxygenase FrzG then leads to formation of a conjugated iminium. In addition to the oxidation of C9, an additional dehydrogenation between C7 and C8 can occur to give a likely shunt product. The next biosynthetic step is the intramolecular aldol condensation catalyzed by the newly identified aldolase FrzH to yield an aza-tricyclic product with the formation of a C9-C3' bond. The short-chain dehydrogenase/reductase FrzI then produces dephospho-(-)-FR901483 that is phosphorylated at C4'-OH into (-)-FR901483 by the phosphotransferase FrzJ.",,,,,,,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1364,no
FSCH_FUSEQ,A0A823A413,ESM2Text,Eukaryota,299,"Kynurenine formamidase-like hydrolase; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan-derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscH converts the product of fscD into 4-hydroxykyrunenine (Probable). The first step of the pathway is the epimerization of L-tryptophan to D- tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6- hydroxylase fscE to yield 6-hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4-hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).","Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites.",Yes,Yes,Maybe,Yes,Yes,Yes,GO:0016787,GO:0004061,GO:0004061,GO:0004061,GO:0004061,GO:0004061,0.6019,0.6019,0.6019,0.6019,0.6019,5,0.6019,0.3246,no
FSCH_FUSEQ,A0A823A413,Prot2Text,Eukaryota,299,"Kynurenine formamidase-like hydrolase; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan-derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscH converts the product of fscD into 4-hydroxykyrunenine (Probable). The first step of the pathway is the epimerization of L-tryptophan to D- tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6- hydroxylase fscE to yield 6-hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4-hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).",Overproduction of nonspecific esterases is a common mechanism of resistance to organophosphate insecticides.,No,No,No,No,No,not-Yes,GO:0016787,GO:0004091,GO:0004091,GO:0004091,GO:0004091,GO:0004091,0.6897,0.6897,0.6897,0.6897,0.6897,5,0.6897,0.3246,no
FSCH_FUSEQ,A0A823A413,ProtT3,Eukaryota,299,"Kynurenine formamidase-like hydrolase; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan-derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscH converts the product of fscD into 4-hydroxykyrunenine (Probable). The first step of the pathway is the epimerization of L-tryptophan to D- tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6- hydroxylase fscE to yield 6-hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4-hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).","Catalyzes the hydrolysis of N-formyl-L-kynurenine to L- kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Belongs to the kynurenine formamidase family",Yes,Yes,Maybe,Yes,Yes,Yes,GO:0016787,GO:0004061,GO:0004061,GO:0004061,GO:0004061,GO:0004061,0.6019,0.6019,0.6019,0.6019,0.6019,5,0.6019,0.3246,no
FSCH_FUSEQ,A0A823A413,ProtTale,Eukaryota,299,"Kynurenine formamidase-like hydrolase; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan-derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscH converts the product of fscD into 4-hydroxykyrunenine (Probable). The first step of the pathway is the epimerization of L-tryptophan to D- tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6- hydroxylase fscE to yield 6-hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4-hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).","Catalyzes the hydrolysis of N-formyl-L-kynurenine to L- kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016787,GO:0004061,GO:0004061,GO:0004061,GO:0004061,GO:0004061,0.6019,0.6019,0.6019,0.6019,0.6019,5,0.6019,0.3246,no
FSCH_FUSEQ,A0A823A413,Protein2Text,Eukaryota,299,"Kynurenine formamidase-like hydrolase; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan-derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscH converts the product of fscD into 4-hydroxykyrunenine (Probable). The first step of the pathway is the epimerization of L-tryptophan to D- tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6- hydroxylase fscE to yield 6-hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4-hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).","The molecular function of this protein is not explicitly stated in the provided text. However, based on the name ""decarboxylase,"" it is likely that the protein's molecular function is related to the removal of a carboxyl group from a molecule, possibly as part of a metabolic pathway or enzyme reaction.",Vague,No,No,No,No,not-Yes,GO:0016787,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.4071,0.4071,0.4071,0.4071,0.4071,5,0.4071,0.3246,no
FSCH_FUSEQ,A0A823A413,Reference,Eukaryota,299,"Kynurenine formamidase-like hydrolase; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan-derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscH converts the product of fscD into 4-hydroxykyrunenine (Probable). The first step of the pathway is the epimerization of L-tryptophan to D- tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6- hydroxylase fscE to yield 6-hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4-hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).","Kynurenine formamidase-like hydrolase; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan-derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscH converts the product of fscD into 4-hydroxykyrunenine (Probable). The first step of the pathway is the epimerization of L-tryptophan to D- tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6- hydroxylase fscE to yield 6-hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4-hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).",,,,,,,GO:0016787,GO:0004061,GO:0016787,GO:0004061,GO:0004061,GO:0004061,0.6019,1.0,0.6019,0.6019,0.6019,5,0.6815,0.3246,no
FSCI_FUSEQ,A0A823A767,ESM2Text,Eukaryota,258,"Oxidoreductase; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan-derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscI catalyzes the formation of the chromene ring from the prenyl moity added by the prenyltransferase fscG (Probable). The first step of the pathway is the epimerization of L-tryptophan to D-tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6-hydroxylase fscE to yield 6- hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4- hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).","Dehydrogenase involved in the biosynthesis of endocrocin, a simple anthraquinone interesting for many biotechnological applications. Converts allylpyruvate to allylpyruvate with a corresponding slow enzymatic rate. Also able to catalyze the reverse reaction.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,,GO:0016491,,GO:0016491,,,1.0,,1.0,,2,1.0,0.1736,no
FSCI_FUSEQ,A0A823A767,Prot2Text,Eukaryota,258,"Oxidoreductase; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan-derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscI catalyzes the formation of the chromene ring from the prenyl moity added by the prenyltransferase fscG (Probable). The first step of the pathway is the epimerization of L-tryptophan to D-tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6-hydroxylase fscE to yield 6- hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4- hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).","Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome monooxygenase P450 claM then catalyzes the dimerization of nataloe-emodin to cladofulvin.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1736,no
FSCI_FUSEQ,A0A823A767,ProtT3,Eukaryota,258,"Oxidoreductase; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan-derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscI catalyzes the formation of the chromene ring from the prenyl moity added by the prenyltransferase fscG (Probable). The first step of the pathway is the epimerization of L-tryptophan to D-tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6-hydroxylase fscE to yield 6- hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4- hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).",Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeranylindole (,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1736,no
FSCI_FUSEQ,A0A823A767,ProtTale,Eukaryota,258,"Oxidoreductase; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan-derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscI catalyzes the formation of the chromene ring from the prenyl moity added by the prenyltransferase fscG (Probable). The first step of the pathway is the epimerization of L-tryptophan to D-tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6-hydroxylase fscE to yield 6- hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4- hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).","Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1736,no
FSCI_FUSEQ,A0A823A767,Protein2Text,Eukaryota,258,"Oxidoreductase; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan-derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscI catalyzes the formation of the chromene ring from the prenyl moity added by the prenyltransferase fscG (Probable). The first step of the pathway is the epimerization of L-tryptophan to D-tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6-hydroxylase fscE to yield 6- hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4- hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).","The molecular function of this protein is an oxidoreductase activity, specifically involved in the metabolism of flavonoids. It catalyzes the reduction of flavonoids, such as quercetin, kaempferol, and isorhapontigenin, to their respective flavonol 3-O-glucosides. This enzyme is also able to reduce quercetin and kaempferol to their respective dihydroflavonols, 3,4- dihydroquercetin and 3,4-dihydrokaempferol, respectively. Additionally, this protein is also able to reduce the 3- and 4-hydroxy groups of flavonols. It is also involved in the reduction of dihydroflavonols to flavanols. This protein is also able to reduce dihydroflavonols to flavanols.
 
This protein is also able to reduce the 3- and 4-hydroxy groups of flavonols.
 
This protein is also able to reduce dihydroflavonols to flavanols.
 
This protein is also able to reduce the 3- and 4-hydroxy groups of flavonols.
 
This protein is also able to reduce dihydroflavonols to flavanols.",Vague,No,No,Maybe,No,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1736,no
FSCI_FUSEQ,A0A823A767,Reference,Eukaryota,258,"Oxidoreductase; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan-derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscI catalyzes the formation of the chromene ring from the prenyl moity added by the prenyltransferase fscG (Probable). The first step of the pathway is the epimerization of L-tryptophan to D-tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6-hydroxylase fscE to yield 6- hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4- hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).","Oxidoreductase; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan-derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscI catalyzes the formation of the chromene ring from the prenyl moity added by the prenyltransferase fscG (Probable). The first step of the pathway is the epimerization of L-tryptophan to D-tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6-hydroxylase fscE to yield 6- hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4- hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).",,,,,,,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1736,no
FSCG_FUSEQ,A0A823A8X6,ESM2Text,Eukaryota,435,"DMATS-type prenyltransferase; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan- derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscG catalyzes the prenylation of the primary alcohol produced by fscA which is necessary for the formation of the chromene ring by the oxidoreductase fscI (Probable). The first step of the pathway is the epimerization of L-tryptophan to D-tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6-hydroxylase fscE to yield 6-hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4-hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).","Prenyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase penM leads to a epoxidized-GGI that is substrate of the terpene cyclase penB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase penP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase penQ. Paxilline is converted to beta-paxitriol via C-10",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3941,no
FSCG_FUSEQ,A0A823A8X6,Prot2Text,Eukaryota,435,"DMATS-type prenyltransferase; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan- derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscG catalyzes the prenylation of the primary alcohol produced by fscA which is necessary for the formation of the chromene ring by the oxidoreductase fscI (Probable). The first step of the pathway is the epimerization of L-tryptophan to D-tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6-hydroxylase fscE to yield 6-hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4-hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).","Indole diterpene prenyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase penM leads to a epoxidized-GGI that is substrate of the terpene cyclase penB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase penP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase penQ. Paxilline is converted to beta-pax",Yes,Yes,Yes,Yes,Yes,Yes,GO:0004659,GO:0016765,GO:0004659,GO:0004659,GO:0016765,GO:0016765,0.8416,1.0,1.0,0.8416,0.8416,5,0.905,0.3941,no
FSCG_FUSEQ,A0A823A8X6,ProtT3,Eukaryota,435,"DMATS-type prenyltransferase; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan- derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscG catalyzes the prenylation of the primary alcohol produced by fscA which is necessary for the formation of the chromene ring by the oxidoreductase fscI (Probable). The first step of the pathway is the epimerization of L-tryptophan to D-tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6-hydroxylase fscE to yield 6-hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4-hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).",Terpene cyclase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeran,No,Maybe,Maybe,No,No,not-Yes,GO:0004659,GO:0016872,GO:0010333,GO:0010334,GO:0010333,GO:0010333,0.3284,0.2353,0.2067,0.2353,0.2353,5,0.2482,0.3941,no
FSCG_FUSEQ,A0A823A8X6,ProtTale,Eukaryota,435,"DMATS-type prenyltransferase; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan- derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscG catalyzes the prenylation of the primary alcohol produced by fscA which is necessary for the formation of the chromene ring by the oxidoreductase fscI (Probable). The first step of the pathway is the epimerization of L-tryptophan to D-tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6-hydroxylase fscE to yield 6-hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4-hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).","Prenyltransferase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS). SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms. These initial steps feature the priming of an unusual benzoic acid starter unit onto the highly",Yes,Yes,Maybe,Yes,Yes,Yes,GO:0004659,GO:0004659,GO:0016765,GO:0004659,GO:0004659,GO:0004659,1.0,0.8416,1.0,1.0,1.0,5,0.9683,0.3941,no
FSCG_FUSEQ,A0A823A8X6,Protein2Text,Eukaryota,435,"DMATS-type prenyltransferase; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan- derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscG catalyzes the prenylation of the primary alcohol produced by fscA which is necessary for the formation of the chromene ring by the oxidoreductase fscI (Probable). The first step of the pathway is the epimerization of L-tryptophan to D-tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6-hydroxylase fscE to yield 6-hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4-hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).","The molecular function of the protein is to catalyze the conversion of a precursor molecule to a product molecule, specifically in the synthesis of a particular molecule. The protein is a part of the biosynthesis pathway of a specific molecule, and it plays a crucial role in this process. The protein's molecular function is likely to be related to its involvement in the synthesis of a particular molecule, and it may be involved in the transfer of a group or the formation of a bond. 

Given the name of the protein, it is likely to be a prenyltransferase, which is an enzyme that catalyzes the transfer of a prenyl group (a molecule consisting of an isoprenoid chain) from one molecule to another. Prenyltransferases are involved in the biosynthesis of various molecules, including cholesterol, steroids, and terpenes. 

The specific molecular function of this protein would depend on the details of its substrate specificity and the products it catalyzes. However, based on its name, it is likely to be involved in the transfer of a prenyl group to a molecule, which would be a key step in the biosynthesis of a particular molecule.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3941,no
FSCG_FUSEQ,A0A823A8X6,Reference,Eukaryota,435,"DMATS-type prenyltransferase; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan- derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscG catalyzes the prenylation of the primary alcohol produced by fscA which is necessary for the formation of the chromene ring by the oxidoreductase fscI (Probable). The first step of the pathway is the epimerization of L-tryptophan to D-tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6-hydroxylase fscE to yield 6-hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4-hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).","DMATS-type prenyltransferase; part of the fragmented gene cluster that mediates the biosynthesis of fusarochromene, a tryptophan- derived metabolite closely related to a group of mycotoxins including fusarochromanone. Within the pathway, fscG catalyzes the prenylation of the primary alcohol produced by fscA which is necessary for the formation of the chromene ring by the oxidoreductase fscI (Probable). The first step of the pathway is the epimerization of L-tryptophan to D-tryptophan in the presence of the NRPS-like tryptophan epimerase fscC. D-tryptophan is subsequently hydroxylated by the tryptophan 6-hydroxylase fscE to yield 6-hydroxytryptophan. The pyrrole ring undergoes cleavaged by the tryptophan 2,3-dioxygenase fscD and is finally converted to 4-hydroxykyrunenine by the hydrolase fscH. The NRPS-like oxidoreductase fscA reduces the carboxyl group to primary alcohol and the DMATS-type prenyltransferase fscG performs prenylation, followed by the formation of a chromene ring catalyzed by the oxidoreductase fscI, which leads to desacetylfusarochromene. Epoxidation by fscF and rearrangement reactions of chromene double bonds convert compound desacetylfusarochromene to fusarochromanones. Although specific acetyltransferases were not found near the fsc gene cluster, several predicted enzymes containing the N-acetyltransferase superfamily domain are present in the genome of F.equiseti. These predicted enzymes may have the potential to convert desacetylfusarochromene to fusarochromene (Probable).",,,,,,,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3941,no
ISRC_AMPFL,A0A8B0M616,ESM2Text,Eukaryota,482,"Acyltransferase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The isariin synthetase isrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1 (Probable).","Dehydrogenase involved in the biosynthesis of acetic acid, a metabolite of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide. Acetic acid serves as a sensor of the intracellular levels of acetyl-CoA, and modulates the activity of ODO1 to control levels of O-acetyl-CoA, which is important for toxin biosynthesis. In vitro, catalyzes the acetic acid-dependent sulfoxidation of 1,2-diene-1,4-dialdehyde to 1,2-diene-1,4-dialdehyde, as well as the subsequent sulfoxidation of the intermediate 1,2-diene-1,4-oligone.",No,No,No,No,No,not-Yes,GO:0016746,,GO:0016491,,GO:0016491,,,0.4807,,0.4807,,2,0.4807,0.2161,no
ISRC_AMPFL,A0A8B0M616,Prot2Text,Eukaryota,482,"Acyltransferase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The isariin synthetase isrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1 (Probable).","Malonyltransferase involved in the biosynthesis of methyl-branched fatty acids such as mycolipanoic, mycolipenic and mycolipenic acids, phlein and papaverine. Can use caffeoyl-CoA and 5-hydroxyferulic acid as substrates, but not malonyl-CoA or sinapoyl-CoA.",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0016746,GO:0016746,GO:0016747,GO:0016746,GO:0016746,GO:0016746,1.0,0.8416,1.0,1.0,1.0,5,0.9683,0.2161,no
ISRC_AMPFL,A0A8B0M616,ProtT3,Eukaryota,482,"Acyltransferase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The isariin synthetase isrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1 (Probable).",O-acetyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylger,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016746,GO:0016413,GO:0016413,GO:0016407,GO:0016407,GO:0016407,0.5794,0.5794,0.729,0.729,0.729,5,0.6692,0.2161,no
ISRC_AMPFL,A0A8B0M616,ProtTale,Eukaryota,482,"Acyltransferase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The isariin synthetase isrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1 (Probable).","O-acyltransferase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the saturated C-C",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016746,GO:0016747,1.0,1.0,1.0,1.0,0.8416,5,0.9683,0.2161,no
ISRC_AMPFL,A0A8B0M616,Protein2Text,Eukaryota,482,"Acyltransferase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The isariin synthetase isrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1 (Probable).","The molecular function of this protein is not explicitly stated in the provided text. However, based on the context, it appears to be involved in the metabolism of a specific compound, possibly a fatty acid or a related molecule, as it is associated with a fatty acid synthase. Therefore, a possible molecular function of this protein could be involved in fatty acid metabolism, specifically in the synthesis or modification of fatty acids. 

Please note that this is a hypothetical function and more information would be needed to confirm it.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016746,,,,,GO:0004312,,,,,0.729,1,0.729,0.2161,no
ISRC_AMPFL,A0A8B0M616,Reference,Eukaryota,482,"Acyltransferase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The isariin synthetase isrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1 (Probable).","Acyltransferase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The isariin synthetase isrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1 (Probable).",,,,,,,GO:0016746,GO:0016747,GO:0016746,GO:0016746,GO:0016747,GO:0016747,0.8416,1.0,1.0,0.8416,0.8416,5,0.905,0.2161,no
ISRB_AMPFL,A0A8B0M9A0,ESM2Text,Eukaryota,574,"Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The isariin synthetase isrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1 (Probable).","Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The nonribosomal peptide synthetase ktnA converts itaconic acid to kotanin. The putative CoA ligase ktnB, the cytochrome P450 monooxygenase ktnC, the FAD-dependent monooxygenase ktnE and the putative FAD-dependent monooxygenase ktnF are probably responsible for each and each step of kotanin biosynthesis. The FAD-dependent monooxygenase ktnF may be responsible for each step of kotanin biosynthesis. For the biosynthesis of kotanin, carbon monoxide is probably provided by the C-3 hydroxylation of carbon atom B into acetyl-CoA, followed by several steps of reduction involving mainly cytochrome P450 monooxygenase and the FAD-dependent monooxygenase ktnB. Kotanin can be further modified by the O-methyltransferase ktnC, the methyltransferase ktnE, the enoyl reductase ktnF and the F",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016405,GO:0016405,GO:0016878,GO:0016878,GO:0016874,GO:0016878,1.0,0.7025,0.7025,0.6897,0.7025,5,0.7594,0.3586,no
ISRB_AMPFL,A0A8B0M9A0,Prot2Text,Eukaryota,574,"Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The isariin synthetase isrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1 (Probable).","Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of the linear tetracyclic TAN-1612 neuropeptide Y receptor antagonist. The decaketide backbone of TAN-1612 is synthesized by the non-reducing polyketide synthase adaA via condensation of one acetyl-CoA starter unit with 9 malonyl-CoA units. The FAD-dependent monooxygenase adaC then performs hydroxylation at C2 while the polaketide chain is still attached to the NRPKS adaA. The alpha-hydroxylation step at C2 appears to be crucial for the following C18-C1 Claisen cyclization and release of the C9-hydroxyl version of TAN-1612 from the NRPKS adaA, two steps performed by the lactamase-like protein adaB. Finally, the O-methyltransferase adaD performs the C9 O-methylation to complete the biosynthesis of TAN-1612.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016405,GO:0016877,GO:0016405,GO:0016877,GO:0016878,GO:0016878,0.8416,1.0,0.8416,0.7025,0.7025,5,0.8176,0.3586,no
ISRB_AMPFL,A0A8B0M9A0,ProtT3,Eukaryota,574,"Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The isariin synthetase isrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1 (Probable).","Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), B4 (FB4), and B5 (FB5), a group of polyketide-derived furanocoumarins called fumonisins",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016405,GO:0016405,GO:0003996,GO:0003996; GO:0005524,GO:0003996,GO:0003996,1.0,0.6204,0.4347,0.6204,0.6204,5,0.6592,0.3586,no
ISRB_AMPFL,A0A8B0M9A0,ProtTale,Eukaryota,574,"Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The isariin synthetase isrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1 (Probable).","Acyl-CoA ligase; part of the gene clusters that mediate the biosynthesis of the host-selective toxins (HSTs) AF-toxins responsible for Alternaria black spot of strawberry disease by the strawberry pathotype. AF-toxin I and III are valine derivatives of 2,3-dyhydroxy-isovaleric acid and 2-hydroxy-isovaleric acid respectively, while AF II is an isoleucine derivative of 2-hydroxy-valeric acid. These derivatives are bound to a 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (ED",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016405,GO:0016877,GO:0003996,GO:0016874,GO:0016877,GO:0016874,0.8416,0.6204,0.6897,0.8416,0.6897,5,0.7366,0.3586,no
ISRB_AMPFL,A0A8B0M9A0,Protein2Text,Eukaryota,574,"Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The isariin synthetase isrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1 (Probable).","This protein is involved in the biosynthesis of amino acids, specifically in the production of amino acids. It is a part of a pathway that produces a certain type of amino acid, which is an essential component of proteins. 
The molecular function of this protein is likely to be a decarboxylase, which is an enzyme that catalyzes the decarboxylation of an amino acid, resulting in the production of a different amino acid. Decarboxylases are important in various biological processes, including the production of amino acids, hormones, and other biomolecules. 

In this case, the protein is likely to be a decarboxylase that catalyzes the decarboxylation of a specific amino acid, resulting in the production of a different amino acid. This reaction is an important step in the biosynthesis of amino acids and is likely to be regulated by various mechanisms to ensure the proper production of amino acids. 

However, without more specific information, it is difficult to determine the exact molecular function of this protein. Further research would be necessary to determine the specific function of this protein in the production of amino acids.",No,No,No,No,No,not-Yes,GO:0016405,GO:0016831,GO:0016831,,,GO:0016831,0.2742,0.2742,,,0.2742,3,0.2742,0.3586,no
ISRB_AMPFL,A0A8B0M9A0,Reference,Eukaryota,574,"Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The isariin synthetase isrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1 (Probable).","Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of isariins (ISRs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The isariin synthetase isrA possesses six modules but lacks an A domain in module 1. Based on the structures of ISRs, module 1 selects a high saturated polyketide as the starter unit. The PKS isrD probably generates the polyketide residue, which is activated by the CoA ligase isrB, and transferred by the acyltransferase isrC to the PCP1/T1 domain in module 1 (Probable).",,,,,,,GO:0016405,GO:0016877,GO:0016878,GO:0016874,GO:0016878,GO:0016878,0.8416,0.7025,0.6897,0.7025,0.7025,5,0.7278,0.3586,no
P5CR2_AMPFL,A0A8B0M9S9,ESM2Text,Eukaryota,313,"Pyrroline-5-carboxylate reductase involved in the biosynthesis of (3S)-methyl-L-proline, one of the building blocks od destruxins (DTXs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The (3S)-methyl-L-proline building block is required for biosynthesis of DTXs including felinotoxins A to E, roseotoxins A to C, [3-Me-Pro] destruxin E chlorohydrin, as well as isaridins (ISDs) B and D. The 2-oxoglutarate-dependent dioxygenase detxE uses L-isoleucine as substrate to produce (4S,5S)-4-methyl-delta1-pyrroline- 5-carboxylate, whereas the pyrroline-5-carboxylate reductases 1 and/or 2 perform the reduction of (4S,5S)-4-methyl-delta1-pyrroline-5- carboxylate to (3S)-methyl-L-proline.","Enzyme that catalyzes the last step in proline biosynthesis. Proline is synthesized from either glutamate or ornithine; both are converted to pyrroline-5-carboxylate (P5C), and then to proline via pyrroline-5-carboxylate reductases (PYCRs). PYCRL is exclusively linked to the reaction mechanism.",Yes,Maybe,Maybe,Yes,Yes,Yes,GO:0004735,GO:0004735,GO:0004735,GO:0004735,GO:0003842,GO:0004735,1.0,1.0,1.0,0.3386,1.0,5,0.8677,0.2393,no
P5CR2_AMPFL,A0A8B0M9S9,Prot2Text,Eukaryota,313,"Pyrroline-5-carboxylate reductase involved in the biosynthesis of (3S)-methyl-L-proline, one of the building blocks od destruxins (DTXs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The (3S)-methyl-L-proline building block is required for biosynthesis of DTXs including felinotoxins A to E, roseotoxins A to C, [3-Me-Pro] destruxin E chlorohydrin, as well as isaridins (ISDs) B and D. The 2-oxoglutarate-dependent dioxygenase detxE uses L-isoleucine as substrate to produce (4S,5S)-4-methyl-delta1-pyrroline- 5-carboxylate, whereas the pyrroline-5-carboxylate reductases 1 and/or 2 perform the reduction of (4S,5S)-4-methyl-delta1-pyrroline-5- carboxylate to (3S)-methyl-L-proline.","Bifunctional enzyme that catalyzes the GSH-dependent reduction of 2-oxoglutarate to 2-oxobutanoate, the first step in the biosynthesis of glutathione.",No,No,No,No,No,not-Yes,GO:0004735,GO:0004735,GO:0004735,GO:0004735,GO:0004735,GO:0004735,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2393,no
P5CR2_AMPFL,A0A8B0M9S9,ProtT3,Eukaryota,313,"Pyrroline-5-carboxylate reductase involved in the biosynthesis of (3S)-methyl-L-proline, one of the building blocks od destruxins (DTXs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The (3S)-methyl-L-proline building block is required for biosynthesis of DTXs including felinotoxins A to E, roseotoxins A to C, [3-Me-Pro] destruxin E chlorohydrin, as well as isaridins (ISDs) B and D. The 2-oxoglutarate-dependent dioxygenase detxE uses L-isoleucine as substrate to produce (4S,5S)-4-methyl-delta1-pyrroline- 5-carboxylate, whereas the pyrroline-5-carboxylate reductases 1 and/or 2 perform the reduction of (4S,5S)-4-methyl-delta1-pyrroline-5- carboxylate to (3S)-methyl-L-proline.",Belongs to the pyrroline-5-carboxylate reductase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004735,GO:0004735,GO:0004735,,GO:0004735,GO:0004735,1.0,1.0,,1.0,1.0,4,1.0,0.2393,no
P5CR2_AMPFL,A0A8B0M9S9,ProtTale,Eukaryota,313,"Pyrroline-5-carboxylate reductase involved in the biosynthesis of (3S)-methyl-L-proline, one of the building blocks od destruxins (DTXs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The (3S)-methyl-L-proline building block is required for biosynthesis of DTXs including felinotoxins A to E, roseotoxins A to C, [3-Me-Pro] destruxin E chlorohydrin, as well as isaridins (ISDs) B and D. The 2-oxoglutarate-dependent dioxygenase detxE uses L-isoleucine as substrate to produce (4S,5S)-4-methyl-delta1-pyrroline- 5-carboxylate, whereas the pyrroline-5-carboxylate reductases 1 and/or 2 perform the reduction of (4S,5S)-4-methyl-delta1-pyrroline-5- carboxylate to (3S)-methyl-L-proline.","Oxidoreductase; part of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. Leucinostatin A contains nine amino acid residues, including the unusual amino acid 4-methyl-L-proline (MePro), 2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (AHyMeOA), 3- hydroxyleucine (HyLeu), alpha-aminoisobutyric acid (AIB),",No,Maybe,Maybe,Maybe,No,not-Yes,GO:0004735,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.6019,0.6019,0.6019,0.6019,0.6019,5,0.6019,0.2393,no
P5CR2_AMPFL,A0A8B0M9S9,Protein2Text,Eukaryota,313,"Pyrroline-5-carboxylate reductase involved in the biosynthesis of (3S)-methyl-L-proline, one of the building blocks od destruxins (DTXs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The (3S)-methyl-L-proline building block is required for biosynthesis of DTXs including felinotoxins A to E, roseotoxins A to C, [3-Me-Pro] destruxin E chlorohydrin, as well as isaridins (ISDs) B and D. The 2-oxoglutarate-dependent dioxygenase detxE uses L-isoleucine as substrate to produce (4S,5S)-4-methyl-delta1-pyrroline- 5-carboxylate, whereas the pyrroline-5-carboxylate reductases 1 and/or 2 perform the reduction of (4S,5S)-4-methyl-delta1-pyrroline-5- carboxylate to (3S)-methyl-L-proline.","The molecular function of this protein is a kinase, specifically a phosphomannomutase. It catalyzes the interconversion of mannose 6-phosphate and mannose 1-phosphate.",No,No,Vague,No,No,not-Yes,GO:0004735,GO:0016491,,,,GO:0016491,0.6019,,,,0.6019,2,0.6019,0.2393,no
P5CR2_AMPFL,A0A8B0M9S9,Reference,Eukaryota,313,"Pyrroline-5-carboxylate reductase involved in the biosynthesis of (3S)-methyl-L-proline, one of the building blocks od destruxins (DTXs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The (3S)-methyl-L-proline building block is required for biosynthesis of DTXs including felinotoxins A to E, roseotoxins A to C, [3-Me-Pro] destruxin E chlorohydrin, as well as isaridins (ISDs) B and D. The 2-oxoglutarate-dependent dioxygenase detxE uses L-isoleucine as substrate to produce (4S,5S)-4-methyl-delta1-pyrroline- 5-carboxylate, whereas the pyrroline-5-carboxylate reductases 1 and/or 2 perform the reduction of (4S,5S)-4-methyl-delta1-pyrroline-5- carboxylate to (3S)-methyl-L-proline.","Pyrroline-5-carboxylate reductase involved in the biosynthesis of (3S)-methyl-L-proline, one of the building blocks od destruxins (DTXs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The (3S)-methyl-L-proline building block is required for biosynthesis of DTXs including felinotoxins A to E, roseotoxins A to C, [3-Me-Pro] destruxin E chlorohydrin, as well as isaridins (ISDs) B and D. The 2-oxoglutarate-dependent dioxygenase detxE uses L-isoleucine as substrate to produce (4S,5S)-4-methyl-delta1-pyrroline- 5-carboxylate, whereas the pyrroline-5-carboxylate reductases 1 and/or 2 perform the reduction of (4S,5S)-4-methyl-delta1-pyrroline-5- carboxylate to (3S)-methyl-L-proline.",,,,,,,GO:0004735,GO:0004735,GO:0016491,GO:0004735,GO:0004735,GO:0004735,1.0,0.6019,1.0,1.0,1.0,5,0.9204,0.2393,no
P5CR1_AMPFL,A0A8B0M9T7,ESM2Text,Eukaryota,287,"Pyrroline-5-carboxylate reductase involved in the biosynthesis of (3S)-methyl-L-proline, one of the building blocks od destruxins (DTXs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The (3S)-methyl-L-proline building block is required for biosynthesis of DTXs including felinotoxins A to E, roseotoxins A to C, [3-Me-Pro] destruxin E chlorohydrin, as well as isaridins (ISDs) B and D. The 2-oxoglutarate-dependent dioxygenase detxE uses L-isoleucine as substrate to produce (4S,5S)-4-methyl-delta1-pyrroline- 5-carboxylate, whereas the pyrroline-5-carboxylate reductases 1 and/or 2 perform the reduction of (4S,5S)-4-methyl-delta1-pyrroline-5- carboxylate to (3S)-methyl-L-proline.",Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004735,GO:0004735,GO:0004735,GO:0004735,GO:0003842,GO:0004735,1.0,1.0,1.0,0.3386,1.0,5,0.8677,0.4827,no
P5CR1_AMPFL,A0A8B0M9T7,Prot2Text,Eukaryota,287,"Pyrroline-5-carboxylate reductase involved in the biosynthesis of (3S)-methyl-L-proline, one of the building blocks od destruxins (DTXs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The (3S)-methyl-L-proline building block is required for biosynthesis of DTXs including felinotoxins A to E, roseotoxins A to C, [3-Me-Pro] destruxin E chlorohydrin, as well as isaridins (ISDs) B and D. The 2-oxoglutarate-dependent dioxygenase detxE uses L-isoleucine as substrate to produce (4S,5S)-4-methyl-delta1-pyrroline- 5-carboxylate, whereas the pyrroline-5-carboxylate reductases 1 and/or 2 perform the reduction of (4S,5S)-4-methyl-delta1-pyrroline-5- carboxylate to (3S)-methyl-L-proline.",Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0004735,GO:0004735,GO:0004735,GO:0004735,GO:0004735,GO:0004735,1.0,1.0,1.0,1.0,1.0,5,1.0,0.4827,no
P5CR1_AMPFL,A0A8B0M9T7,ProtT3,Eukaryota,287,"Pyrroline-5-carboxylate reductase involved in the biosynthesis of (3S)-methyl-L-proline, one of the building blocks od destruxins (DTXs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The (3S)-methyl-L-proline building block is required for biosynthesis of DTXs including felinotoxins A to E, roseotoxins A to C, [3-Me-Pro] destruxin E chlorohydrin, as well as isaridins (ISDs) B and D. The 2-oxoglutarate-dependent dioxygenase detxE uses L-isoleucine as substrate to produce (4S,5S)-4-methyl-delta1-pyrroline- 5-carboxylate, whereas the pyrroline-5-carboxylate reductases 1 and/or 2 perform the reduction of (4S,5S)-4-methyl-delta1-pyrroline-5- carboxylate to (3S)-methyl-L-proline.",Belongs to the pyrroline-5-carboxylate reductase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004735,GO:0004735,GO:0004735,,GO:0004735,GO:0004735,1.0,1.0,,1.0,1.0,4,1.0,0.4827,no
P5CR1_AMPFL,A0A8B0M9T7,ProtTale,Eukaryota,287,"Pyrroline-5-carboxylate reductase involved in the biosynthesis of (3S)-methyl-L-proline, one of the building blocks od destruxins (DTXs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The (3S)-methyl-L-proline building block is required for biosynthesis of DTXs including felinotoxins A to E, roseotoxins A to C, [3-Me-Pro] destruxin E chlorohydrin, as well as isaridins (ISDs) B and D. The 2-oxoglutarate-dependent dioxygenase detxE uses L-isoleucine as substrate to produce (4S,5S)-4-methyl-delta1-pyrroline- 5-carboxylate, whereas the pyrroline-5-carboxylate reductases 1 and/or 2 perform the reduction of (4S,5S)-4-methyl-delta1-pyrroline-5- carboxylate to (3S)-methyl-L-proline.",Catalyzes the conversion of 5-aminolevulinate (ALA) to porphobilinogen (PBG) with the concomitant reduction of NADP(+).,No,No,No,No,No,not-Yes,GO:0004735,GO:0004655,GO:0004655,GO:0004655,GO:0004655,GO:0004655,0.1998,0.1998,0.1998,0.1998,0.1998,5,0.1998,0.4827,no
P5CR1_AMPFL,A0A8B0M9T7,Protein2Text,Eukaryota,287,"Pyrroline-5-carboxylate reductase involved in the biosynthesis of (3S)-methyl-L-proline, one of the building blocks od destruxins (DTXs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The (3S)-methyl-L-proline building block is required for biosynthesis of DTXs including felinotoxins A to E, roseotoxins A to C, [3-Me-Pro] destruxin E chlorohydrin, as well as isaridins (ISDs) B and D. The 2-oxoglutarate-dependent dioxygenase detxE uses L-isoleucine as substrate to produce (4S,5S)-4-methyl-delta1-pyrroline- 5-carboxylate, whereas the pyrroline-5-carboxylate reductases 1 and/or 2 perform the reduction of (4S,5S)-4-methyl-delta1-pyrroline-5- carboxylate to (3S)-methyl-L-proline.","The molecular function of this protein is a vitamin B6-dependent dehydrogenase, which is involved in the metabolism of glutamate.",No,No,No,No,No,not-Yes,GO:0004735,GO:0016491,,,,GO:0016491,0.6019,,,,0.6019,2,0.6019,0.4827,no
P5CR1_AMPFL,A0A8B0M9T7,Reference,Eukaryota,287,"Pyrroline-5-carboxylate reductase involved in the biosynthesis of (3S)-methyl-L-proline, one of the building blocks od destruxins (DTXs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The (3S)-methyl-L-proline building block is required for biosynthesis of DTXs including felinotoxins A to E, roseotoxins A to C, [3-Me-Pro] destruxin E chlorohydrin, as well as isaridins (ISDs) B and D. The 2-oxoglutarate-dependent dioxygenase detxE uses L-isoleucine as substrate to produce (4S,5S)-4-methyl-delta1-pyrroline- 5-carboxylate, whereas the pyrroline-5-carboxylate reductases 1 and/or 2 perform the reduction of (4S,5S)-4-methyl-delta1-pyrroline-5- carboxylate to (3S)-methyl-L-proline.","Pyrroline-5-carboxylate reductase involved in the biosynthesis of (3S)-methyl-L-proline, one of the building blocks od destruxins (DTXs), cyclohexadepsipeptides that contain unusual nonproteinogenic amino acid-building blocks and possess a range of antiviral, antibacterial, and other activities. The (3S)-methyl-L-proline building block is required for biosynthesis of DTXs including felinotoxins A to E, roseotoxins A to C, [3-Me-Pro] destruxin E chlorohydrin, as well as isaridins (ISDs) B and D. The 2-oxoglutarate-dependent dioxygenase detxE uses L-isoleucine as substrate to produce (4S,5S)-4-methyl-delta1-pyrroline- 5-carboxylate, whereas the pyrroline-5-carboxylate reductases 1 and/or 2 perform the reduction of (4S,5S)-4-methyl-delta1-pyrroline-5- carboxylate to (3S)-methyl-L-proline.",,,,,,,GO:0004735,GO:0004735,GO:0016491,GO:0004735,GO:0004735,GO:0004735,1.0,0.6019,1.0,1.0,1.0,5,0.9204,0.4827,no
CGLR2_CRAVI,A0A8B8EY61,ESM2Text,Eukaryota,632,"Nucleotidyltransferase that catalyzes the formation of some cyclic nucleotide and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",Polymerase component of the spindle assembly checkpoint which participates in checkpoint activity to prevent cells from prematurely exiting mitosis. The complex polymerizes to form a complex with ssup2 and ssup4 and is required to promote disassembly of the checkpoint independent of ssup2.,No,No,No,No,No,not-Yes,GO:0046872; GO:0016779,,,,,,,,,,,0,,0.5962,yes
CGLR2_CRAVI,A0A8B8EY61,Prot2Text,Eukaryota,632,"Nucleotidyltransferase that catalyzes the formation of some cyclic nucleotide and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","3'-5' RNA exonuclease which cleaves in situ on specific transcripts in both nucleus and mitochondrion. Involved in nucleolar pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex, one of the building blocks of the spliceosome. Required for the assembly of the U4/U6-U5 tri-snRNP complex at the spliceosome.",No,No,No,No,No,not-Yes,GO:0046872; GO:0016779,GO:0000175,GO:0000175,GO:0000175,GO:0000175,GO:0000175,0.1131,0.1131,0.1131,0.1131,0.1131,5,0.1131,0.5962,yes
CGLR2_CRAVI,A0A8B8EY61,ProtT3,Eukaryota,632,"Nucleotidyltransferase that catalyzes the formation of some cyclic nucleotide and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Catalyzes the addition of a 3'-terminal 2',3'-cyclic phosphate to RNA via an ATP-dependent reaction to produce 2',3'-capped RNA (By similarity). 3'-terminal 2',3'-cyclic phosphate is a modification present at the 3'-end of many cellular and viral RNAs (By similarity). Acts as a negative regulator of Toll-like receptor (TLR) signaling pathway by mediating 3'-terminal 2',3'-cyclic phosphate addition to the 3'-end",No,Maybe,No,No,No,not-Yes,GO:0046872; GO:0016779,GO:0016779; GO:0005524,GO:0016779,GO:0016874; GO:0005524,GO:0004075,GO:0005524,0.6444,0.7015,0.3479,0.2176,0.2136,5,0.425,0.5962,yes
CGLR2_CRAVI,A0A8B8EY61,ProtTale,Eukaryota,632,"Nucleotidyltransferase that catalyzes the formation of some cyclic nucleotide and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Putative nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity. Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses. Directly binds dsRNA, activating the nucleotidyltransferase activity, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor",Yes,Yes,Maybe,Maybe,Yes,Yes,GO:0046872; GO:0016779,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,GO:0016779; GO:0003725,0.6176,0.6176,0.6176,0.6176,0.6176,5,0.6176,0.5962,yes
CGLR2_CRAVI,A0A8B8EY61,Protein2Text,Eukaryota,632,"Nucleotidyltransferase that catalyzes the formation of some cyclic nucleotide and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","This protein is a nucleoside triphosphate hydrolase, which suggests its molecular function is to catalyze the hydrolysis of nucleoside triphosphates, such as ATP, GTP, CTP, TTP, and UTP.",No,No,No,No,No,not-Yes,GO:0046872; GO:0016779,GO:0017111,GO:0017111,GO:0017111,GO:0017111,GO:0017111,0.1635,0.1635,0.1635,0.1635,0.1635,5,0.1635,0.5962,yes
CGLR2_CRAVI,A0A8B8EY61,Reference,Eukaryota,632,"Nucleotidyltransferase that catalyzes the formation of some cyclic nucleotide and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.","Nucleotidyltransferase that catalyzes the formation of some cyclic nucleotide and plays a key role in innate immunity. Directly binds some unknown ligand, activating the nucleotidyltransferase activity, leading to synthesis of a second messenger that binds to and activates Sting, thereby triggering the immune response via activation of the NF-kappa-B transcription factor.",,,,,,,GO:0046872; GO:0016779,GO:0016779,GO:0016779,GO:0016779,GO:0016779,GO:0016779,0.7015,0.7015,0.7015,0.7015,0.7015,5,0.7015,0.5962,yes
PYDG_ACRSP,A0A8F4NUL3,ESM2Text,Eukaryota,426,"Alpha/beta hydrolasee; part of the gene cluster that mediates the biosynthesis of pyrrocidines, fungal natural products containing a macrocyclic para-cyclophane connected to a decahydrofluorene ring system that show potent antibiotic activities toward Gram-negative bacteria. Within the pathway, pydG catalyzes the Knoevenagel condensation that affords the 3-pyrrolin-2-one ring, using as substrate the polyketide-tyrosyl acyl thioester product of pydA. The pathway begins with the PKS-NRPS pydA which, with the help of the trans-enoyl reductase pydC, synthesizes the polyketide-tyrosyl acyl thioester product which can be reductively off- loaded by the terminal reductase (R) domain in pydA. The alpha/beta hydrolase pydG is then required to catalyze the subsequent Knoevenagel condensation that affords the 3-pyrrolin-2-one ring, whereas the four proteins pydB, pydE, pydX and pydZ then function synergistically to form the cyclophane. PydB and the membrane-bound pydX and pydZ are lipid-binding proteins that can sequester and mold the pdyG product into the inverse S-shape. Binding of the medium chain reductase pydE to the complex would trigger the cascade oxidative cyclization. PydY is involved in the Diels-Alder cycloaddition that forms the decahydrofluorene core. Additional non-enzymatic hydroxylation yields pyrrocidine A2 which can be further reduced into pyrrocidine B by an endogenous reductase (Probable).","Alkylhydrolase; part of the gene cluster that mediates the biosynthesis of the mycotoxin citrinin, a hepato-nephrotoxic compound to humans due to inhibition of respiration complex III (Ref.1). The cluster encodes a FKS-type chaperone with alkylhydrolase activity and catalyzes the formation of the heptaketide naphtopyran-7,7-diene. The naphtopyran-7,7-diene is then heptaketide ferricrocin (Ref.1). The chaperone ferricrocin is then responsible for the chlorination of the C3-C4 intermediate to yield a citrinin (Ref.1). Citrinin is further acetylated by the acetyltransferase citrA to produce citrinin B (Ref.1). Citrinin B is further acetylated to produce quercetin (Ref.1). The cluster encodes a cytochrome P450 monooxygenase that catalyzes the two-step epoxidation of citrinin B, citrinin A and citrinin C (Ref.1).",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787,,GO:0016787,GO:0016787,,,,1.0,1.0,,,2,1.0,0.1804,no
PYDG_ACRSP,A0A8F4NUL3,Prot2Text,Eukaryota,426,"Alpha/beta hydrolasee; part of the gene cluster that mediates the biosynthesis of pyrrocidines, fungal natural products containing a macrocyclic para-cyclophane connected to a decahydrofluorene ring system that show potent antibiotic activities toward Gram-negative bacteria. Within the pathway, pydG catalyzes the Knoevenagel condensation that affords the 3-pyrrolin-2-one ring, using as substrate the polyketide-tyrosyl acyl thioester product of pydA. The pathway begins with the PKS-NRPS pydA which, with the help of the trans-enoyl reductase pydC, synthesizes the polyketide-tyrosyl acyl thioester product which can be reductively off- loaded by the terminal reductase (R) domain in pydA. The alpha/beta hydrolase pydG is then required to catalyze the subsequent Knoevenagel condensation that affords the 3-pyrrolin-2-one ring, whereas the four proteins pydB, pydE, pydX and pydZ then function synergistically to form the cyclophane. PydB and the membrane-bound pydX and pydZ are lipid-binding proteins that can sequester and mold the pdyG product into the inverse S-shape. Binding of the medium chain reductase pydE to the complex would trigger the cascade oxidative cyclization. PydY is involved in the Diels-Alder cycloaddition that forms the decahydrofluorene core. Additional non-enzymatic hydroxylation yields pyrrocidine A2 which can be further reduced into pyrrocidine B by an endogenous reductase (Probable).","Hydrolyase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787,GO:0016787,GO:0016836,GO:0016836,GO:0016836,GO:0016787,1.0,0.4071,0.4071,0.4071,1.0,5,0.6443,0.1804,no
PYDG_ACRSP,A0A8F4NUL3,ProtT3,Eukaryota,426,"Alpha/beta hydrolasee; part of the gene cluster that mediates the biosynthesis of pyrrocidines, fungal natural products containing a macrocyclic para-cyclophane connected to a decahydrofluorene ring system that show potent antibiotic activities toward Gram-negative bacteria. Within the pathway, pydG catalyzes the Knoevenagel condensation that affords the 3-pyrrolin-2-one ring, using as substrate the polyketide-tyrosyl acyl thioester product of pydA. The pathway begins with the PKS-NRPS pydA which, with the help of the trans-enoyl reductase pydC, synthesizes the polyketide-tyrosyl acyl thioester product which can be reductively off- loaded by the terminal reductase (R) domain in pydA. The alpha/beta hydrolase pydG is then required to catalyze the subsequent Knoevenagel condensation that affords the 3-pyrrolin-2-one ring, whereas the four proteins pydB, pydE, pydX and pydZ then function synergistically to form the cyclophane. PydB and the membrane-bound pydX and pydZ are lipid-binding proteins that can sequester and mold the pdyG product into the inverse S-shape. Binding of the medium chain reductase pydE to the complex would trigger the cascade oxidative cyclization. PydY is involved in the Diels-Alder cycloaddition that forms the decahydrofluorene core. Additional non-enzymatic hydroxylation yields pyrrocidine A2 which can be further reduced into pyrrocidine B by an endogenous reductase (Probable).",Probable hydrolase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylger,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016787,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1804,no
PYDG_ACRSP,A0A8F4NUL3,ProtTale,Eukaryota,426,"Alpha/beta hydrolasee; part of the gene cluster that mediates the biosynthesis of pyrrocidines, fungal natural products containing a macrocyclic para-cyclophane connected to a decahydrofluorene ring system that show potent antibiotic activities toward Gram-negative bacteria. Within the pathway, pydG catalyzes the Knoevenagel condensation that affords the 3-pyrrolin-2-one ring, using as substrate the polyketide-tyrosyl acyl thioester product of pydA. The pathway begins with the PKS-NRPS pydA which, with the help of the trans-enoyl reductase pydC, synthesizes the polyketide-tyrosyl acyl thioester product which can be reductively off- loaded by the terminal reductase (R) domain in pydA. The alpha/beta hydrolase pydG is then required to catalyze the subsequent Knoevenagel condensation that affords the 3-pyrrolin-2-one ring, whereas the four proteins pydB, pydE, pydX and pydZ then function synergistically to form the cyclophane. PydB and the membrane-bound pydX and pydZ are lipid-binding proteins that can sequester and mold the pdyG product into the inverse S-shape. Binding of the medium chain reductase pydE to the complex would trigger the cascade oxidative cyclization. PydY is involved in the Diels-Alder cycloaddition that forms the decahydrofluorene core. Additional non-enzymatic hydroxylation yields pyrrocidine A2 which can be further reduced into pyrrocidine B by an endogenous reductase (Probable).","Hydrolyzing enzyme; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C. Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production. The other FUS cluster members are not essential for fusarin C biosynthesis.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016787,GO:0016787,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1804,no
PYDG_ACRSP,A0A8F4NUL3,Protein2Text,Eukaryota,426,"Alpha/beta hydrolasee; part of the gene cluster that mediates the biosynthesis of pyrrocidines, fungal natural products containing a macrocyclic para-cyclophane connected to a decahydrofluorene ring system that show potent antibiotic activities toward Gram-negative bacteria. Within the pathway, pydG catalyzes the Knoevenagel condensation that affords the 3-pyrrolin-2-one ring, using as substrate the polyketide-tyrosyl acyl thioester product of pydA. The pathway begins with the PKS-NRPS pydA which, with the help of the trans-enoyl reductase pydC, synthesizes the polyketide-tyrosyl acyl thioester product which can be reductively off- loaded by the terminal reductase (R) domain in pydA. The alpha/beta hydrolase pydG is then required to catalyze the subsequent Knoevenagel condensation that affords the 3-pyrrolin-2-one ring, whereas the four proteins pydB, pydE, pydX and pydZ then function synergistically to form the cyclophane. PydB and the membrane-bound pydX and pydZ are lipid-binding proteins that can sequester and mold the pdyG product into the inverse S-shape. Binding of the medium chain reductase pydE to the complex would trigger the cascade oxidative cyclization. PydY is involved in the Diels-Alder cycloaddition that forms the decahydrofluorene core. Additional non-enzymatic hydroxylation yields pyrrocidine A2 which can be further reduced into pyrrocidine B by an endogenous reductase (Probable).","The molecular function of this protein is a hydrolase. Specifically, it is a thiolesterase, which catalyzes the hydrolysis of thiolesters, such as thioacyl esters, into a thiol and a carboxylic acid.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787,GO:0016790,GO:0016790,GO:0016790,GO:0016790,GO:0016790,0.6897,0.6897,0.6897,0.6897,0.6897,5,0.6897,0.1804,no
PYDG_ACRSP,A0A8F4NUL3,Reference,Eukaryota,426,"Alpha/beta hydrolasee; part of the gene cluster that mediates the biosynthesis of pyrrocidines, fungal natural products containing a macrocyclic para-cyclophane connected to a decahydrofluorene ring system that show potent antibiotic activities toward Gram-negative bacteria. Within the pathway, pydG catalyzes the Knoevenagel condensation that affords the 3-pyrrolin-2-one ring, using as substrate the polyketide-tyrosyl acyl thioester product of pydA. The pathway begins with the PKS-NRPS pydA which, with the help of the trans-enoyl reductase pydC, synthesizes the polyketide-tyrosyl acyl thioester product which can be reductively off- loaded by the terminal reductase (R) domain in pydA. The alpha/beta hydrolase pydG is then required to catalyze the subsequent Knoevenagel condensation that affords the 3-pyrrolin-2-one ring, whereas the four proteins pydB, pydE, pydX and pydZ then function synergistically to form the cyclophane. PydB and the membrane-bound pydX and pydZ are lipid-binding proteins that can sequester and mold the pdyG product into the inverse S-shape. Binding of the medium chain reductase pydE to the complex would trigger the cascade oxidative cyclization. PydY is involved in the Diels-Alder cycloaddition that forms the decahydrofluorene core. Additional non-enzymatic hydroxylation yields pyrrocidine A2 which can be further reduced into pyrrocidine B by an endogenous reductase (Probable).","Alpha/beta hydrolasee; part of the gene cluster that mediates the biosynthesis of pyrrocidines, fungal natural products containing a macrocyclic para-cyclophane connected to a decahydrofluorene ring system that show potent antibiotic activities toward Gram-negative bacteria. Within the pathway, pydG catalyzes the Knoevenagel condensation that affords the 3-pyrrolin-2-one ring, using as substrate the polyketide-tyrosyl acyl thioester product of pydA. The pathway begins with the PKS-NRPS pydA which, with the help of the trans-enoyl reductase pydC, synthesizes the polyketide-tyrosyl acyl thioester product which can be reductively off- loaded by the terminal reductase (R) domain in pydA. The alpha/beta hydrolase pydG is then required to catalyze the subsequent Knoevenagel condensation that affords the 3-pyrrolin-2-one ring, whereas the four proteins pydB, pydE, pydX and pydZ then function synergistically to form the cyclophane. PydB and the membrane-bound pydX and pydZ are lipid-binding proteins that can sequester and mold the pdyG product into the inverse S-shape. Binding of the medium chain reductase pydE to the complex would trigger the cascade oxidative cyclization. PydY is involved in the Diels-Alder cycloaddition that forms the decahydrofluorene core. Additional non-enzymatic hydroxylation yields pyrrocidine A2 which can be further reduced into pyrrocidine B by an endogenous reductase (Probable).",,,,,,,GO:0016787,GO:0016829,GO:0016787,GO:0016829,GO:0016829,GO:0016829,0.5902,1.0,0.5902,0.5902,0.5902,5,0.6722,0.1804,no
MAND_DREDA,A0AAD6IYT8,ESM2Text,Eukaryota,441,"Probable endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Involved in trapping nematodes.","Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016985,GO:0016985,GO:0004553,GO:0016985,GO:0016985,GO:0016985,1.0,0.6757,1.0,1.0,1.0,5,0.9351,0.1487,no
MAND_DREDA,A0AAD6IYT8,Prot2Text,Eukaryota,441,"Probable endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Involved in trapping nematodes.","Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016985,GO:0016985,GO:0016985,GO:0016985,GO:0016985,GO:0016985,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1487,no
MAND_DREDA,A0AAD6IYT8,ProtT3,Eukaryota,441,"Probable endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Involved in trapping nematodes.",Secreted. Belongs to the glycosyl hydrolase 5 (cellulase A) family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016985,GO:0008810,GO:0004553,,GO:0008810,GO:0008810,0.5618,0.6757,,0.5618,0.5618,4,0.5903,0.1487,no
MAND_DREDA,A0AAD6IYT8,ProtTale,Eukaryota,441,"Probable endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Involved in trapping nematodes.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.",No,No,No,No,No,not-Yes,GO:0016985,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,0.4774,0.4774,0.4774,0.4774,0.4774,5,0.4774,0.1487,no
MAND_DREDA,A0AAD6IYT8,Protein2Text,Eukaryota,441,"Probable endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Involved in trapping nematodes.","This protein is involved in breaking down cellulose, a complex carbohydrate found in plant cell walls. It is an endoglucanase, which means it acts on the internal bonds of cellulose, rather than on the surface. Its molecular function is likely to be catalyzing the hydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, allowing it to break down cellulose into smaller fragments. This is an important step in the degradation of cellulose, as it allows other enzymes to access and break down the cellulose further. 

In more detail, the molecular function of this protein is to catalyze the hydrolysis of the glycosidic bond between two glucose molecules in cellulose, resulting in the release of glucose. This reaction is an important step in the degradation of cellulose, as it allows other enzymes to access and break down the cellulose further. The protein uses a catalytic mechanism involving a nucleophile that attacks the glycosidic bond, resulting in the formation of a glucosyl-enzyme intermediate that is then released as glucose. 

The molecular function of this protein is likely to be important for the degradation of cellulose in a variety of environments, including soil and the rumen of herbivorous animals. It may also be important for the degradation of cellulose in industrial processes, such as the production of biofuels. 

It is worth noting that the specific molecular function of this protein may depend on the specific isoform or variant of the protein, as well as the specific conditions in which it is acting. However, in general, the molecular function of this protein is likely to be important for the degradation of cellulose. 

References:
- ""Cellulase"" by Wikipedia
- ""Endoglucanase"" by Wikipedia
- ""Cellulose degradation"" by Wikipedia
- ""Glycosidic bond"" by Wikipedia
- ""Nucleophile"" by Wikipedia
- ""Catalytic mechanism"" by Wikipedia
- ""Glucosyl-enzyme intermediate"" by Wikipedia
- ""Glucose"" by Wikipedia
- ""Cellulose degradation in soil"" by Wikipedia
- ""Cellulose degradation in the rumen"" by Wikipedia
- ""Biofuel production"" by Wikipedia
- ""Industrial processes"" by Wikipedia
- ""Isoform"" by Wikipedia
- ""Variant"" by Wikipedia
- ""Conditions"" by Wikipedia
- ""Specificity"" by Wikipedia
- ""Molecular function"" by Wikipedia",No,Maybe,No,No,No,not-Yes,GO:0016985,GO:0008810,GO:0008810,GO:0008810,GO:0008810,GO:0008810,0.5618,0.5618,0.5618,0.5618,0.5618,5,0.5618,0.1487,no
MAND_DREDA,A0AAD6IYT8,Reference,Eukaryota,441,"Probable endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Involved in trapping nematodes.","Probable endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Involved in trapping nematodes.",,,,,,,GO:0016985,GO:0016985,GO:0016985,GO:0016985,GO:0016985,GO:0016985,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1487,no
BAM_TRIV3,A2FBF3,ESM2Text,Eukaryota,377,Digests glycogen releasing maltose units.,"Hydrolyzes 1,4-beta-D-glucan.",No,No,No,No,No,not-Yes,GO:0016161,GO:0008810,GO:0008810,GO:0008810,GO:0008810,GO:0008810,0.6335,0.6335,0.6335,0.6335,0.6335,5,0.6335,0.178,no
BAM_TRIV3,A2FBF3,Prot2Text,Eukaryota,377,Digests glycogen releasing maltose units.,Could be a chitinase.,No,No,No,Vague,No,not-Yes,GO:0016161,,,,,,,,,,,0,,0.178,no
BAM_TRIV3,A2FBF3,ProtT3,Eukaryota,377,Digests glycogen releasing maltose units.,Belongs to the glycosyl hydrolase 14 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016161,GO:0016161,GO:0016161,,GO:0016161,GO:0016161,1.0,1.0,,1.0,1.0,4,1.0,0.178,no
BAM_TRIV3,A2FBF3,ProtTale,Eukaryota,377,Digests glycogen releasing maltose units.,"Alpha-galactosidase that specifically cleaves terminal alpha-1,2-linked galactose residues from N-glycans in glycoproteins. Involved in the degradation of complex N-glycans during N-glycosylation processing. Catalyzes the hydrolysis of terminal alpha-1,2-linked galactose residues from N-glycans in glycoproteins such as alpha-dystroglycan (DAG1), laminin G domain- containing proteins (LMNG1, LMNG2, LMNG3 and LMNG4), transferrin receptor 1 (TFR1) and integrin beta-1 subunit (ITGB1).",No,No,No,No,No,not-Yes,GO:0016161,GO:0004557,GO:0004557,GO:0004557,GO:0004557,GO:0004557,0.5445,0.5445,0.5445,0.5445,0.5445,5,0.5445,0.178,no
BAM_TRIV3,A2FBF3,Protein2Text,Eukaryota,377,Digests glycogen releasing maltose units.,"The molecular function of this protein is to catalyze the hydrolysis of glucans, specifically the cleavage of internal glucosidic bonds in a glucan chain. In other words, it is a glucanohydrolase enzyme that breaks down glucans, a type of polysaccharide composed of glucose residues, into smaller units.",Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016161,GO:0016798,GO:0004553,GO:0004553,GO:0004553,GO:0004553,0.6466,0.7539,0.7539,0.7539,0.7539,5,0.7324,0.178,no
BAM_TRIV3,A2FBF3,Reference,Eukaryota,377,Digests glycogen releasing maltose units.,Digests glycogen releasing maltose units.,,,,,,,GO:0016161,GO:0016161,GO:0016161,GO:0016798,GO:0016161,GO:0016161,1.0,1.0,0.6466,1.0,1.0,5,0.9293,0.178,no
HODMG_ECTM1,A4XXZ0,ESM2Text,Bacteria,376,"Component of the heme-dependent oxidative N-demethylase (HODM) enzyme, that catalyzes the NADPH-dependent oxidation of dimethylamine (DMA) to methylamine (MA) and formaldehyde. Functions in bacterial methylated amine catabolism, linking alkylamine oxidation to the tetrahydrofolate C1 pool. The gamma subunit of HODM may act as an aminomethyltransferase involved in the detoxification of formaldehyde released by the alpha subunit; this process requires tetrahydrofolate (THF).","Involved in the biosynthesis of albonoursin (cyclo[(alpha,beta-dehydro-Phe)-(alpha,beta-dehydro-Leu)]), a cyclic structural analog of the antibiotic mannopeptimycin. Catalyzes the reversible pyridoxal-2'-phosphate-dependent phosphorylation of dihydroxyacetone phosphate (DHAP or dephosphocholate) to yield dihydroxyacetone phosphate (DHAP or deoxyacetone phosphate). It can also use beta-anomeric DHAP and pyridoxal-5'-phosphate (p-anomeric DHAP).",No,No,No,No,No,not-Yes,GO:0008483,,,,,,,,,,,0,,0.2033,no
HODMG_ECTM1,A4XXZ0,Prot2Text,Bacteria,376,"Component of the heme-dependent oxidative N-demethylase (HODM) enzyme, that catalyzes the NADPH-dependent oxidation of dimethylamine (DMA) to methylamine (MA) and formaldehyde. Functions in bacterial methylated amine catabolism, linking alkylamine oxidation to the tetrahydrofolate C1 pool. The gamma subunit of HODM may act as an aminomethyltransferase involved in the detoxification of formaldehyde released by the alpha subunit; this process requires tetrahydrofolate (THF).","Catalyzes the reversible decarboxylation of aromatic carboxylic acids like ferulic acid, p-coumaric acid or cinnamic acid, producing the corresponding vinyl derivatives 4-vinylphenol, 4-vinylguaiacol, and styrene, respectively, which play the role of aroma metabolites.",No,No,No,No,No,not-Yes,GO:0008483,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.2742,0.2742,0.2742,0.2742,0.2742,5,0.2742,0.2033,no
HODMG_ECTM1,A4XXZ0,ProtT3,Bacteria,376,"Component of the heme-dependent oxidative N-demethylase (HODM) enzyme, that catalyzes the NADPH-dependent oxidation of dimethylamine (DMA) to methylamine (MA) and formaldehyde. Functions in bacterial methylated amine catabolism, linking alkylamine oxidation to the tetrahydrofolate C1 pool. The gamma subunit of HODM may act as an aminomethyltransferase involved in the detoxification of formaldehyde released by the alpha subunit; this process requires tetrahydrofolate (THF).",The glycine cleavage system catalyzes the degradation of glycine. Belongs to the GcvT family,No,Maybe,No,No,No,not-Yes,GO:0008483,GO:0004047,GO:0004047,GO:0004047,GO:0004047,GO:0004047,0.3987,0.3987,0.3987,0.3987,0.3987,5,0.3987,0.2033,no
HODMG_ECTM1,A4XXZ0,ProtTale,Bacteria,376,"Component of the heme-dependent oxidative N-demethylase (HODM) enzyme, that catalyzes the NADPH-dependent oxidation of dimethylamine (DMA) to methylamine (MA) and formaldehyde. Functions in bacterial methylated amine catabolism, linking alkylamine oxidation to the tetrahydrofolate C1 pool. The gamma subunit of HODM may act as an aminomethyltransferase involved in the detoxification of formaldehyde released by the alpha subunit; this process requires tetrahydrofolate (THF).",The glycine cleavage system catalyzes the degradation of glycine.,No,Maybe,No,No,No,not-Yes,GO:0008483,,,,,,,,,,,0,,0.2033,no
HODMG_ECTM1,A4XXZ0,Protein2Text,Bacteria,376,"Component of the heme-dependent oxidative N-demethylase (HODM) enzyme, that catalyzes the NADPH-dependent oxidation of dimethylamine (DMA) to methylamine (MA) and formaldehyde. Functions in bacterial methylated amine catabolism, linking alkylamine oxidation to the tetrahydrofolate C1 pool. The gamma subunit of HODM may act as an aminomethyltransferase involved in the detoxification of formaldehyde released by the alpha subunit; this process requires tetrahydrofolate (THF).","The molecular function of this protein is an oxidoreductase, specifically an oxidoreductase that acts on the CH-OH group of donors with NAD(+) or NADP(+) as electron acceptor. It is also a member of the aldehyde dehydrogenase family.",Vague,No,No,No,Vague,not-Yes,GO:0008483,GO:0016620,GO:0004029,GO:0016620,GO:0004029,GO:0016620,0.2742,0.2067,0.2742,0.2067,0.2742,5,0.2472,0.2033,no
HODMG_ECTM1,A4XXZ0,Reference,Bacteria,376,"Component of the heme-dependent oxidative N-demethylase (HODM) enzyme, that catalyzes the NADPH-dependent oxidation of dimethylamine (DMA) to methylamine (MA) and formaldehyde. Functions in bacterial methylated amine catabolism, linking alkylamine oxidation to the tetrahydrofolate C1 pool. The gamma subunit of HODM may act as an aminomethyltransferase involved in the detoxification of formaldehyde released by the alpha subunit; this process requires tetrahydrofolate (THF).","Component of the heme-dependent oxidative N-demethylase (HODM) enzyme, that catalyzes the NADPH-dependent oxidation of dimethylamine (DMA) to methylamine (MA) and formaldehyde. Functions in bacterial methylated amine catabolism, linking alkylamine oxidation to the tetrahydrofolate C1 pool. The gamma subunit of HODM may act as an aminomethyltransferase involved in the detoxification of formaldehyde released by the alpha subunit; this process requires tetrahydrofolate (THF).",,,,,,,GO:0008483,GO:0004047,GO:0016491,GO:0016491,GO:0016491,GO:0004047,0.3987,0.4071,0.4071,0.4071,0.3987,5,0.4037,0.2033,no
CEL1_SCLS1,A7E584,ESM2Text,Eukaryota,389,Endoglucanase that plays an important role in biomass degradation. Binds onto plant cell walls to participate in the hydrolysis of cellulose.,"Endoglucanase that plays an important function in biomass degradation by catalyzing the hydrolysis of cellulose and other beta-D-glucans. Hydrolyzes 1,3-beta-glucan, cellobiose, laminaribiose, beta-D-glucan and heteroglucan. Also hydrolyzes 1,4-beta-glucan, mannan, beta-D-glucan and beta-D-mannan.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008810,GO:0008810; GO:0004553,GO:0008810,GO:0008810; GO:0004553,GO:0008810; GO:0004553,GO:0008810,0.9527,1.0,0.9527,0.9527,1.0,5,0.9716,0.2009,no
CEL1_SCLS1,A7E584,Prot2Text,Eukaryota,389,Endoglucanase that plays an important role in biomass degradation. Binds onto plant cell walls to participate in the hydrolysis of cellulose.,"Endoglucanase that plays an important role in biomass degradation by catalyzing the hydrolysis of the non-reducing end beta-1,4-glucosidic linkages in cellulose and cellotetraose to release cellobiose. Hydrolyzes crystalline and amorphous cellulose but is inactive on hydroxyethyl cellulose, mannan, galactomannan, xyloglucan, arabinoxylan, arabinan, xylan, and pectin.",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008810,GO:0008810,GO:0008810,GO:0008810,GO:0008810,GO:0008810,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2009,no
CEL1_SCLS1,A7E584,ProtT3,Eukaryota,389,Endoglucanase that plays an important role in biomass degradation. Binds onto plant cell walls to participate in the hydrolysis of cellulose.,"The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose. Secreted. Belongs to the glycosyl hydrolase 5 (cellul",Yes,Yes,Yes,Yes,Yes,Yes,GO:0008810,GO:0008810,GO:0008810,GO:0008810,GO:0008810,GO:0008810,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2009,no
CEL1_SCLS1,A7E584,ProtTale,Eukaryota,389,Endoglucanase that plays an important role in biomass degradation. Binds onto plant cell walls to participate in the hydrolysis of cellulose.,"Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.",No,No,No,No,No,not-Yes,GO:0008810,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,0.6335,0.6335,0.6335,0.6335,0.6335,5,0.6335,0.2009,no
CEL1_SCLS1,A7E584,Protein2Text,Eukaryota,389,Endoglucanase that plays an important role in biomass degradation. Binds onto plant cell walls to participate in the hydrolysis of cellulose.,"The molecular function of this protein is not explicitly stated in the provided information. However, based on the context, it is likely that the protein plays a role in breaking down or degrading cellulose, as it is involved in a process related to its function. More specific information about its molecular function would be required to confirm this. 
In general, the molecular functions of proteins can include a wide range of activities, such as:
* Enzyme activity: catalyzing specific chemical reactions, such as hydrolysis or oxidation
* Binding activity: interacting with other molecules, such as proteins, DNA, or small molecules
* Catalytic activity: catalyzing a specific chemical reaction, such as breaking or forming chemical bonds
* GTPase activity: hydrolyzing GTP to GDP
* Hydrolase activity: breaking chemical bonds in a substrate using water
* Isomerase activity: catalyzing the rearrangement of chemical bonds within a molecule
* Kinase activity: transferring a phosphate group from ATP to a substrate molecule
* Lyase activity: breaking chemical bonds in a substrate using a variety of mechanisms
* Nucleoside- triphosphate phosphatase activity: catalyzing the hydrolysis of nucleoside triphosphates
* Oxidoreductase activity: catalyzing the transfer of electrons from one molecule to another
* Phosphatase activity: catalyzing the hydrolysis of phosphate groups from a substrate molecule
* Protein kinase activity: transferring a phosphate group from ATP to a substrate protein molecule
* Transcriptional regulator activity: regulating the expression of genes by binding to DNA or other regulatory elements
* Transferase activity: catalyzing the transfer of a chemical group from one molecule to another

These are just a few examples of the many molecular functions that proteins can have. The specific molecular function of a protein can depend on its sequence, structure, and interactions with other molecules. 

Please note that this is a general answer and more specific information about the protein would be required to provide a more accurate answer. 
If you have any more specific information about the protein, such as its name or sequence, I would be happy to try to provide a more detailed answer.",Vague,Vague,Vague,Vague,Maybe,not-Yes,GO:0008810,,,,,,,,,,,0,,0.2009,no
CEL1_SCLS1,A7E584,Reference,Eukaryota,389,Endoglucanase that plays an important role in biomass degradation. Binds onto plant cell walls to participate in the hydrolysis of cellulose.,Endoglucanase that plays an important role in biomass degradation. Binds onto plant cell walls to participate in the hydrolysis of cellulose.,,,,,,,GO:0008810,GO:0008810,GO:0008810,GO:0008810,GO:0008810,GO:0008810,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2009,no
DDDY_SHEWM,B1KN81,ESM2Text,Bacteria,414,Catalyzes the cleavage of dimethylsulfoniopropionate (DMSP) into dimethyl sulfide (DMS) and acrylate.,"Induces differentiation and growth of neomycetes. It is capable of degrading a variety of compounds including a variety of compounds including D-galacturonate, D-glucuronate, methyl-alpha-D-galactopyranoside, propyl-alpha-D-galactopyranoside, methyl-alpha-D-glucuronate, methyl-alpha-D-glucuronate, methyl-alpha-D-mannopyranoside, methyl-alpha-D-glucuronate, methyl-alpha-L-arabinofuranoside, methyl-alpha-D-glucuronate and methyl-alpha-D-mannopyranoside. The enzyme is also able to degrade a variety of filamentous polysaccharides.",No,No,No,No,No,not-Yes,GO:0047869,,GO:0004553,,,,,0.2742,,,,1,0.2742,0.4302,no
DDDY_SHEWM,B1KN81,Prot2Text,Bacteria,414,Catalyzes the cleavage of dimethylsulfoniopropionate (DMSP) into dimethyl sulfide (DMS) and acrylate.,Larval storage protein (LSP) which may serve as a store of amino acids for synthesis of adult proteins.,No,No,No,No,No,not-Yes,GO:0047869,,,,,,,,,,,0,,0.4302,no
DDDY_SHEWM,B1KN81,ProtT3,Bacteria,414,Catalyzes the cleavage of dimethylsulfoniopropionate (DMSP) into dimethyl sulfide (DMS) and acrylate.,Cytoplasm. Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family,Vague,Vague,No,Vague,No,not-Yes,GO:0047869,GO:0009039; GO:0046872,GO:0009039,GO:0009039,GO:0009039,GO:0009039,0.1917,0.2353,0.2353,0.2353,0.2353,5,0.2266,0.4302,no
DDDY_SHEWM,B1KN81,ProtTale,Bacteria,414,Catalyzes the cleavage of dimethylsulfoniopropionate (DMSP) into dimethyl sulfide (DMS) and acrylate.,Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) into two phosphate ions and 2'-deoxyinosine monophosphate (2'-dIMP). This is the first step in the biosynthesis pathway of purine nucleotides in the purine salvage pathway.,No,No,No,No,No,not-Yes,GO:0047869,GO:0004427,GO:0004427,GO:0004427,GO:0004427,GO:0004427,0.2067,0.2067,0.2067,0.2067,0.2067,5,0.2067,0.4302,no
DDDY_SHEWM,B1KN81,Protein2Text,Bacteria,414,Catalyzes the cleavage of dimethylsulfoniopropionate (DMSP) into dimethyl sulfide (DMS) and acrylate.,"This protein is involved in the synthesis of a specific type of molecule, likely a carbohydrate or glycan, which is a common function of enzymes in this family. The molecular function of this protein is likely to catalyze a specific biochemical reaction, such as glycosylation or glycosidic bond formation. However, without more specific information, it is difficult to determine the exact molecular function of this protein.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0047869,,,,,,,,,,,0,,0.4302,no
DDDY_SHEWM,B1KN81,Reference,Bacteria,414,Catalyzes the cleavage of dimethylsulfoniopropionate (DMSP) into dimethyl sulfide (DMS) and acrylate.,Catalyzes the cleavage of dimethylsulfoniopropionate (DMSP) into dimethyl sulfide (DMS) and acrylate.,,,,,,,GO:0047869,GO:0016829,GO:0016829,GO:0016829,GO:0016829,GO:0016829,0.6897,0.6897,0.6897,0.6897,0.6897,5,0.6897,0.4302,no
KOJP_HALOH,B8D049,ESM2Text,Bacteria,780,"Catalyzes the reversible phosphorolysis of kojibiose into beta-D-glucose 1-phosphate (Glc1P) and D-glucose. In the reverse direction, uses Glc1P as acceptor to produce alpha-1,2- glucans up to a degree of polymerization of 6.","Catalyzes the phosphorolysis of maltose, leading to the formation of glucose and glucose 1-P. In the absence of glucose, mediates the cleavage of anionic phospho-alpha-D-glucopyranoside (p-nitrophenyl phosphate) and bis(beta-D-glucopyranosyl) p-nitrophenyl phosphate in vitro; however, the physiological substrate may be different. In vitro, catalyzes the phosphorolysis of phospho-D-mannobiose (p-Man); however, the physiological substrate may be different. Phosphorolysis is not the major reaction in the phosphorolysis of phospho-mannobiose found in D-glucopyran, and the enzymes involved in it are unknown.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0030246; GO:0004553; GO:0033831,GO:0004645,GO:0004645,GO:0050084,GO:0004645,GO:0050084,0.4151,0.4151,0.2477,0.4151,0.2477,5,0.3481,0.3528,no
KOJP_HALOH,B8D049,Prot2Text,Bacteria,780,"Catalyzes the reversible phosphorolysis of kojibiose into beta-D-glucose 1-phosphate (Glc1P) and D-glucose. In the reverse direction, uses Glc1P as acceptor to produce alpha-1,2- glucans up to a degree of polymerization of 6.","Catalyzes the phosphorolysis of maltose, leading to the formation of glucose and glucose 1-P. Is not able to act on other maltose-6'-P-esters, such as maltulose, maltitol, maltulofluorose, maltitol, trehalulose, trehalulose, trehalulopentaose, trehalulopentaose, trehalulopentaose, trehalulopentaose, trehalulopentaose, trehalulopentaose, trehalulopentaose, trehalulopentaose, trehalulopentaose, trehalulopentaose, trehalulopentaose, trehalulopentaose, or trehalopentaose as substrates.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0030246; GO:0004553; GO:0033831,GO:0016740,GO:0050840,GO:0050082,GO:0050504,GO:0050082,0.4364,0.3756,0.3592,0.4151,0.3592,5,0.3891,0.3528,no
KOJP_HALOH,B8D049,ProtT3,Bacteria,780,"Catalyzes the reversible phosphorolysis of kojibiose into beta-D-glucose 1-phosphate (Glc1P) and D-glucose. In the reverse direction, uses Glc1P as acceptor to produce alpha-1,2- glucans up to a degree of polymerization of 6.",Belongs to the glycosyl hydrolase 13 family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0030246; GO:0004553; GO:0033831,GO:0004553,GO:0004553,,GO:0004556,GO:0016798,0.5969,0.5969,,0.4495,0.5373,4,0.5452,0.3528,no
KOJP_HALOH,B8D049,ProtTale,Bacteria,780,"Catalyzes the reversible phosphorolysis of kojibiose into beta-D-glucose 1-phosphate (Glc1P) and D-glucose. In the reverse direction, uses Glc1P as acceptor to produce alpha-1,2- glucans up to a degree of polymerization of 6.",Catalyzes the reversible phosphorolysis of alpha-D-glucose 1-phosphate (Glc1P) into alpha-D-glucose 6-phosphate (Glc6P). Is also able to phosphorylate alpha-D-glucose 1-phosphate (Glc1P) into alpha-D-glucose 6-phosphate (Glc6P) in vitro.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0030246; GO:0004553; GO:0033831,GO:0004614,GO:0004614,GO:0004614,GO:0004614,GO:0004614,0.2005,0.2005,0.2005,0.2005,0.2005,5,0.2005,0.3528,no
KOJP_HALOH,B8D049,Protein2Text,Bacteria,780,"Catalyzes the reversible phosphorolysis of kojibiose into beta-D-glucose 1-phosphate (Glc1P) and D-glucose. In the reverse direction, uses Glc1P as acceptor to produce alpha-1,2- glucans up to a degree of polymerization of 6.","This protein is involved in the breakdown of starch, specifically the hydrolysis of alpha-1,6-glucosidic linkages. It catalyzes the hydrolysis of alpha-1,6-glucosidic linkages in glycogen and starch to release glucose.",No,No,No,No,No,not-Yes,GO:0030246; GO:0004553; GO:0033831,GO:0004553,GO:0004135,GO:0004135,GO:0004135,GO:0004135,0.5969,0.4027,0.4027,0.4027,0.4027,5,0.4415,0.3528,no
KOJP_HALOH,B8D049,Reference,Bacteria,780,"Catalyzes the reversible phosphorolysis of kojibiose into beta-D-glucose 1-phosphate (Glc1P) and D-glucose. In the reverse direction, uses Glc1P as acceptor to produce alpha-1,2- glucans up to a degree of polymerization of 6.","Catalyzes the reversible phosphorolysis of kojibiose into beta-D-glucose 1-phosphate (Glc1P) and D-glucose. In the reverse direction, uses Glc1P as acceptor to produce alpha-1,2- glucans up to a degree of polymerization of 6.",,,,,,,GO:0030246; GO:0004553; GO:0033831,GO:0016757,GO:0004645,GO:0004645,GO:0004645,GO:0004645,0.4588,0.4151,0.4151,0.4151,0.4151,5,0.4238,0.3528,no
NPAC_METRA,E9F689,ESM2Text,Eukaryota,357,"Nitronate monooxygenase; part of the gene cluster that mediates the biosynthesis of the deadly neurotoxic nitroalkane 3- nitropropanoic acid (3-NPA) that acts as an antimetabolite of succinate and irreversibly inhibits succinate dehydrogenase and disrupts mitochondrial oxidative phosphorylation. Catalyzes the oxidation of 3-NPA to nitrite and malonic semialdehyde. NpaC is not conserved in all fungal npa clusters and, while it is possible that it serves as a self-protection mechanism against accumulation of 3-NPA (by npaA and npaB) in the producing host, the more likely scenario may be the three enzymes representing an alternative catabolic pathway of aspartate to generate readily metabolizable nitrogen and carbon sources.",Involved in the biosynthesis of the antibiotic bialaphosin B.,No,No,No,No,No,not-Yes,GO:0018580; GO:0000166,,,,,,,,,,,0,,0.1732,no
NPAC_METRA,E9F689,Prot2Text,Eukaryota,357,"Nitronate monooxygenase; part of the gene cluster that mediates the biosynthesis of the deadly neurotoxic nitroalkane 3- nitropropanoic acid (3-NPA) that acts as an antimetabolite of succinate and irreversibly inhibits succinate dehydrogenase and disrupts mitochondrial oxidative phosphorylation. Catalyzes the oxidation of 3-NPA to nitrite and malonic semialdehyde. NpaC is not conserved in all fungal npa clusters and, while it is possible that it serves as a self-protection mechanism against accumulation of 3-NPA (by npaA and npaB) in the producing host, the more likely scenario may be the three enzymes representing an alternative catabolic pathway of aspartate to generate readily metabolizable nitrogen and carbon sources.","Nitronate monooxygenase that uses molecular oxygen to catalyze the oxidative denitrification of alkyl nitronates. Acts on propionate 3-nitronate (P3N), the presumed physiological substrate. Probably functions in the detoxification of P3N, a metabolic poison produced by plants and fungi as a defense mechanism.",Yes,Yes,Maybe,Yes,Yes,Yes,GO:0018580; GO:0000166,GO:0004497,GO:0018580,GO:0018580,GO:0018580,GO:0018580,0.4897,0.6988,0.6988,0.6988,0.6988,5,0.657,0.1732,no
NPAC_METRA,E9F689,ProtT3,Eukaryota,357,"Nitronate monooxygenase; part of the gene cluster that mediates the biosynthesis of the deadly neurotoxic nitroalkane 3- nitropropanoic acid (3-NPA) that acts as an antimetabolite of succinate and irreversibly inhibits succinate dehydrogenase and disrupts mitochondrial oxidative phosphorylation. Catalyzes the oxidation of 3-NPA to nitrite and malonic semialdehyde. NpaC is not conserved in all fungal npa clusters and, while it is possible that it serves as a self-protection mechanism against accumulation of 3-NPA (by npaA and npaB) in the producing host, the more likely scenario may be the three enzymes representing an alternative catabolic pathway of aspartate to generate readily metabolizable nitrogen and carbon sources.","Catalyzes the oxidative cleavage of the carbon-halogen bond in halogenated organic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. Belongs to the MIO family",No,No,No,No,No,not-Yes,GO:0018580; GO:0000166,GO:0016491,GO:0016787,GO:0016491,GO:0016787,GO:0016829,0.4195,0.2706,0.4195,0.2706,0.2706,5,0.3302,0.1732,no
NPAC_METRA,E9F689,ProtTale,Eukaryota,357,"Nitronate monooxygenase; part of the gene cluster that mediates the biosynthesis of the deadly neurotoxic nitroalkane 3- nitropropanoic acid (3-NPA) that acts as an antimetabolite of succinate and irreversibly inhibits succinate dehydrogenase and disrupts mitochondrial oxidative phosphorylation. Catalyzes the oxidation of 3-NPA to nitrite and malonic semialdehyde. NpaC is not conserved in all fungal npa clusters and, while it is possible that it serves as a self-protection mechanism against accumulation of 3-NPA (by npaA and npaB) in the producing host, the more likely scenario may be the three enzymes representing an alternative catabolic pathway of aspartate to generate readily metabolizable nitrogen and carbon sources.",Catalyzes the oxidation of 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-M) to 2-amino-4-methylthiolane (AMT).,No,No,No,No,No,not-Yes,GO:0018580; GO:0000166,,GO:0016491,GO:0016491,GO:0016491,GO:0016491,,0.4195,0.4195,0.4195,0.4195,4,0.4195,0.1732,no
NPAC_METRA,E9F689,Protein2Text,Eukaryota,357,"Nitronate monooxygenase; part of the gene cluster that mediates the biosynthesis of the deadly neurotoxic nitroalkane 3- nitropropanoic acid (3-NPA) that acts as an antimetabolite of succinate and irreversibly inhibits succinate dehydrogenase and disrupts mitochondrial oxidative phosphorylation. Catalyzes the oxidation of 3-NPA to nitrite and malonic semialdehyde. NpaC is not conserved in all fungal npa clusters and, while it is possible that it serves as a self-protection mechanism against accumulation of 3-NPA (by npaA and npaB) in the producing host, the more likely scenario may be the three enzymes representing an alternative catabolic pathway of aspartate to generate readily metabolizable nitrogen and carbon sources.","This protein is involved in the catalysis of a biochemical reaction, specifically the reduction of a keto group in a molecule. It is likely to be a type of oxidoreductase enzyme, which catalyzes the transfer of electrons from one molecule to another.",Vague,No,Vague,No,Vague,not-Yes,GO:0018580; GO:0000166,GO:0016491,GO:0016491,GO:0016491,,GO:0016491,0.4195,0.4195,0.4195,,0.4195,4,0.4195,0.1732,no
NPAC_METRA,E9F689,Reference,Eukaryota,357,"Nitronate monooxygenase; part of the gene cluster that mediates the biosynthesis of the deadly neurotoxic nitroalkane 3- nitropropanoic acid (3-NPA) that acts as an antimetabolite of succinate and irreversibly inhibits succinate dehydrogenase and disrupts mitochondrial oxidative phosphorylation. Catalyzes the oxidation of 3-NPA to nitrite and malonic semialdehyde. NpaC is not conserved in all fungal npa clusters and, while it is possible that it serves as a self-protection mechanism against accumulation of 3-NPA (by npaA and npaB) in the producing host, the more likely scenario may be the three enzymes representing an alternative catabolic pathway of aspartate to generate readily metabolizable nitrogen and carbon sources.","Nitronate monooxygenase; part of the gene cluster that mediates the biosynthesis of the deadly neurotoxic nitroalkane 3- nitropropanoic acid (3-NPA) that acts as an antimetabolite of succinate and irreversibly inhibits succinate dehydrogenase and disrupts mitochondrial oxidative phosphorylation. Catalyzes the oxidation of 3-NPA to nitrite and malonic semialdehyde. NpaC is not conserved in all fungal npa clusters and, while it is possible that it serves as a self-protection mechanism against accumulation of 3-NPA (by npaA and npaB) in the producing host, the more likely scenario may be the three enzymes representing an alternative catabolic pathway of aspartate to generate readily metabolizable nitrogen and carbon sources.",,,,,,,GO:0018580; GO:0000166,GO:0018580,GO:0018580,GO:0018580,GO:0018580,GO:0018580,0.6988,0.6988,0.6988,0.6988,0.6988,5,0.6988,0.1732,no
FGR4_GIBZE,I1S6W0,ESM2Text,Eukaryota,150,"Probable cyclase; part of the gene cluster that mediates the biosynthesis of the tetraketides fugralins such as linear fugralin A and cyclic fugralin B, volatile compounds that play a role in the asexual reproductive cycle but are not involved in pathogenicity. Fugralin B is similar to fugralin A except for a cyclization between the carboxylic acid C-8 and the alcohol on C-4 resulting in a six membered lactone ring, probably catalyzed by the cyclase FGR4 (Probable). One of the key features of fugralins is the presence of a double methyl group, which is only rarely encountered in fungal secondary metabolites. As the fugralins cluster does not contain an independent methyltransferase, the PKS FGR1 is probably responsible for adding two methyl groups to the same carbon atom (Probable). The exact role of the individual cluster genes remains unknown and further work is needed to unravel the biosynthetic pathway (Probable).","FAD-dependent oxidoreductase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The nonribosomal peptide synthetase ktnS assembles the carbon backbone of the polyketide-amino acid precursor of the polyketide part of kotanin. As kotanin is a tetramic acid precursor of 7-mercaptopropionate (7-MPA), the assembled tetramate must be stereolyzed to yield the tetramate moiety. The 7-mercaptopropionate must be dehydrated to yield the tetramate core. The methyltransferase ktnB then catalyzes the methylation of the 8R-hydroxyl group of 7-mercaptopropionate (7-MPA) to yield the 8R,8S-dihydroxy-kotanin. The domains in the 8R-hydroxyl group are then probably differentially bound by ktnC to afford the 8R,8S-dihydroxy-kotanin. Thereby, the entire regioselective part of kotanin biosynthesis probably occurs via",No,No,No,No,No,not-Yes,GO:0016829,GO:0016491,GO:0016491,GO:0016491; GO:0071949,GO:0016491,,0.5902,0.5902,0.4328,0.5902,,4,0.5508,0.1556,no
FGR4_GIBZE,I1S6W0,Prot2Text,Eukaryota,150,"Probable cyclase; part of the gene cluster that mediates the biosynthesis of the tetraketides fugralins such as linear fugralin A and cyclic fugralin B, volatile compounds that play a role in the asexual reproductive cycle but are not involved in pathogenicity. Fugralin B is similar to fugralin A except for a cyclization between the carboxylic acid C-8 and the alcohol on C-4 resulting in a six membered lactone ring, probably catalyzed by the cyclase FGR4 (Probable). One of the key features of fugralins is the presence of a double methyl group, which is only rarely encountered in fungal secondary metabolites. As the fugralins cluster does not contain an independent methyltransferase, the PKS FGR1 is probably responsible for adding two methyl groups to the same carbon atom (Probable). The exact role of the individual cluster genes remains unknown and further work is needed to unravel the biosynthetic pathway (Probable).","Oxidoreductase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome P450 monooxygenase P450 claM then catalyzes the dimerization of nataloe-emodin to cladofulvin.",No,No,No,No,No,not-Yes,GO:0016829,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.5902,0.5902,0.5902,0.5902,0.5902,5,0.5902,0.1556,no
FGR4_GIBZE,I1S6W0,ProtT3,Eukaryota,150,"Probable cyclase; part of the gene cluster that mediates the biosynthesis of the tetraketides fugralins such as linear fugralin A and cyclic fugralin B, volatile compounds that play a role in the asexual reproductive cycle but are not involved in pathogenicity. Fugralin B is similar to fugralin A except for a cyclization between the carboxylic acid C-8 and the alcohol on C-4 resulting in a six membered lactone ring, probably catalyzed by the cyclase FGR4 (Probable). One of the key features of fugralins is the presence of a double methyl group, which is only rarely encountered in fungal secondary metabolites. As the fugralins cluster does not contain an independent methyltransferase, the PKS FGR1 is probably responsible for adding two methyl groups to the same carbon atom (Probable). The exact role of the individual cluster genes remains unknown and further work is needed to unravel the biosynthetic pathway (Probable).",Involved in the degradation of 4-hydroxybenzoate (4-HBA). Catalyzes the oxidation of 4-hydroxybenzoate (4-HBA) to 4-hydroxybenzaldehyde (4-HBA-CHO). Belongs to the 4-hydroxybenzoate 6-monooxygenase family,No,No,No,No,No,not-Yes,GO:0016829,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0016491,0.4807,0.4807,0.4807,0.4807,0.5902,5,0.5026,0.1556,no
FGR4_GIBZE,I1S6W0,ProtTale,Eukaryota,150,"Probable cyclase; part of the gene cluster that mediates the biosynthesis of the tetraketides fugralins such as linear fugralin A and cyclic fugralin B, volatile compounds that play a role in the asexual reproductive cycle but are not involved in pathogenicity. Fugralin B is similar to fugralin A except for a cyclization between the carboxylic acid C-8 and the alcohol on C-4 resulting in a six membered lactone ring, probably catalyzed by the cyclase FGR4 (Probable). One of the key features of fugralins is the presence of a double methyl group, which is only rarely encountered in fungal secondary metabolites. As the fugralins cluster does not contain an independent methyltransferase, the PKS FGR1 is probably responsible for adding two methyl groups to the same carbon atom (Probable). The exact role of the individual cluster genes remains unknown and further work is needed to unravel the biosynthetic pathway (Probable).","Scytalone dehydratase-like protein; part of the gene cluster that mediates the biosynthesis of sordarin and hypoxysordarin, glycoside antibiotics with a unique tetracyclic diterpene aglycone structure. First, the geranylgeranyl diphosphate synthase sdnC constructs GGDP from farnesyl diphosphate and isopentenyl diphosphate. The diterpene cyclase sdnA then catalyzes the cyclization of GGDP to afford cycloaraneosene. Cycloaraneosene is then hydroxylated four times by the putative cytochrome P450 monooxygenases sdnB, sdnE, sdnF",No,No,No,No,No,not-Yes,GO:0016829,GO:0016836,,GO:0016836,,GO:0016836,0.6897,,0.6897,,0.6897,3,0.6897,0.1556,no
FGR4_GIBZE,I1S6W0,Protein2Text,Eukaryota,150,"Probable cyclase; part of the gene cluster that mediates the biosynthesis of the tetraketides fugralins such as linear fugralin A and cyclic fugralin B, volatile compounds that play a role in the asexual reproductive cycle but are not involved in pathogenicity. Fugralin B is similar to fugralin A except for a cyclization between the carboxylic acid C-8 and the alcohol on C-4 resulting in a six membered lactone ring, probably catalyzed by the cyclase FGR4 (Probable). One of the key features of fugralins is the presence of a double methyl group, which is only rarely encountered in fungal secondary metabolites. As the fugralins cluster does not contain an independent methyltransferase, the PKS FGR1 is probably responsible for adding two methyl groups to the same carbon atom (Probable). The exact role of the individual cluster genes remains unknown and further work is needed to unravel the biosynthetic pathway (Probable).","This protein has a molecular function of catalyzing the conversion of a substrate into a product, specifically the oxidation of a nitroaromatic compound. It is a monooxygenase enzyme that uses molecular oxygen to catalyze the reaction.",No,No,No,No,No,not-Yes,GO:0016829,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.4807,0.4807,0.4807,0.4807,0.4807,5,0.4807,0.1556,no
FGR4_GIBZE,I1S6W0,Reference,Eukaryota,150,"Probable cyclase; part of the gene cluster that mediates the biosynthesis of the tetraketides fugralins such as linear fugralin A and cyclic fugralin B, volatile compounds that play a role in the asexual reproductive cycle but are not involved in pathogenicity. Fugralin B is similar to fugralin A except for a cyclization between the carboxylic acid C-8 and the alcohol on C-4 resulting in a six membered lactone ring, probably catalyzed by the cyclase FGR4 (Probable). One of the key features of fugralins is the presence of a double methyl group, which is only rarely encountered in fungal secondary metabolites. As the fugralins cluster does not contain an independent methyltransferase, the PKS FGR1 is probably responsible for adding two methyl groups to the same carbon atom (Probable). The exact role of the individual cluster genes remains unknown and further work is needed to unravel the biosynthetic pathway (Probable).","Probable cyclase; part of the gene cluster that mediates the biosynthesis of the tetraketides fugralins such as linear fugralin A and cyclic fugralin B, volatile compounds that play a role in the asexual reproductive cycle but are not involved in pathogenicity. Fugralin B is similar to fugralin A except for a cyclization between the carboxylic acid C-8 and the alcohol on C-4 resulting in a six membered lactone ring, probably catalyzed by the cyclase FGR4 (Probable). One of the key features of fugralins is the presence of a double methyl group, which is only rarely encountered in fungal secondary metabolites. As the fugralins cluster does not contain an independent methyltransferase, the PKS FGR1 is probably responsible for adding two methyl groups to the same carbon atom (Probable). The exact role of the individual cluster genes remains unknown and further work is needed to unravel the biosynthetic pathway (Probable).",,,,,,,GO:0016829,GO:0016829,GO:0016829,,,GO:0016829,1.0,1.0,,,1.0,3,1.0,0.1556,no
SQWI_CLOS9,J0MXJ0,ESM2Text,Bacteria,159,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes the isomerization of 4-deoxy-4-sulfo-D-erythrose (SE) to 4-deoxy-4-sulfo-D-erythrulose (SEu) (Ref.2).",Catalyzes the interconversion of ribulose-5-P and ribose-5-P.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004751,GO:0004751,GO:0004751,GO:0004751,GO:0004751,GO:0004751,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3018,no
SQWI_CLOS9,J0MXJ0,Prot2Text,Bacteria,159,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes the isomerization of 4-deoxy-4-sulfo-D-erythrose (SE) to 4-deoxy-4-sulfo-D-erythrulose (SEu) (Ref.2).",Catalyzes the interconversion of ribulose-5-P and ribose-5-P.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004751,GO:0004751,GO:0004751,GO:0004751,GO:0004751,GO:0004751,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3018,no
SQWI_CLOS9,J0MXJ0,ProtT3,Bacteria,159,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes the isomerization of 4-deoxy-4-sulfo-D-erythrose (SE) to 4-deoxy-4-sulfo-D-erythrulose (SEu) (Ref.2).",Belongs to the LacAB/RpiB family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004751,,,,,,,,,,,0,,0.3018,no
SQWI_CLOS9,J0MXJ0,ProtTale,Bacteria,159,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes the isomerization of 4-deoxy-4-sulfo-D-erythrose (SE) to 4-deoxy-4-sulfo-D-erythrulose (SEu) (Ref.2).","Catalyzes the isomerization of D-ribulose 5-phosphate to D-ribulose 1,5-bisphosphate.",Maybe,No,No,Maybe,Maybe,not-Yes,GO:0004751,,GO:0016853,,GO:0008974,GO:0016853,,0.6019,,0.1803,0.6019,3,0.4614,0.3018,no
SQWI_CLOS9,J0MXJ0,Protein2Text,Bacteria,159,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes the isomerization of 4-deoxy-4-sulfo-D-erythrose (SE) to 4-deoxy-4-sulfo-D-erythrulose (SEu) (Ref.2).","The molecular function of this protein is not explicitly stated in the provided information. However, based on the name of the protein, it is likely that it is involved in the transfer of a molecule, possibly a phosphate group, in a biological process. The name suggests that it is a transferase, which is a class of enzymes that catalyze the transfer of a group from one molecule to another. 

If you have more information about this protein, I may be able to provide a more specific answer.",Vague,Vague,No,Vague,No,not-Yes,GO:0004751,,,,,,,,,,,0,,0.3018,no
SQWI_CLOS9,J0MXJ0,Reference,Bacteria,159,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes the isomerization of 4-deoxy-4-sulfo-D-erythrose (SE) to 4-deoxy-4-sulfo-D-erythrulose (SEu) (Ref.2).","Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes the isomerization of 4-deoxy-4-sulfo-D-erythrose (SE) to 4-deoxy-4-sulfo-D-erythrulose (SEu) (Ref.2).",,,,,,,GO:0004751,GO:0016853,GO:0016853,GO:0016853,GO:0016853,GO:0016853,0.6019,0.6019,0.6019,0.6019,0.6019,5,0.6019,0.3018,no
SQVD_CLOS9,J1H1H5,ESM2Text,Bacteria,447,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes the isomerization of sulfoquinovose (SQ) to 6-deoxy- 6-sulfo-D-fructose (SF) (Ref.2).","Isocyanide synthase involved in the biosynthesis of isocyanides (or isonitriles), a class of microbial secondary metabolites. The presence of an isonitrile moiety within a compound imparts unique biological (cytotoxic, antibacterial, and antiprotozoal) and chemical (transition metal coordination) properties and enables synthetic and biochemical applications.",No,No,No,No,No,not-Yes,GO:0061593,,GO:0016829,,,,,0.3552,,,,1,0.3552,0.2939,no
SQVD_CLOS9,J1H1H5,Prot2Text,Bacteria,447,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes the isomerization of sulfoquinovose (SQ) to 6-deoxy- 6-sulfo-D-fructose (SF) (Ref.2).",Catalyzes the dehydration of galactarate to form 5-dehydro-2-deoxy-D-glucarate (5-KDG).,No,No,No,No,No,not-Yes,GO:0061593,GO:0016836,GO:0008868,GO:0008867,GO:0008867,GO:0016836,0.2353,0.1998,0.1998,0.1998,0.2353,5,0.214,0.2939,no
SQVD_CLOS9,J1H1H5,ProtT3,Bacteria,447,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes the isomerization of sulfoquinovose (SQ) to 6-deoxy- 6-sulfo-D-fructose (SF) (Ref.2).","Catalyzes the conversion of 2,5-dihydroxyphenylacetate (2,5-DHPA) to 2,5-dihydroxybenzoate (2,5-DHB). Belongs to the DHP synthase family",No,No,No,No,No,not-Yes,GO:0061593,GO:0016829,GO:0016829,GO:0016829,GO:0016829,GO:0016829,0.3552,0.3552,0.3552,0.3552,0.3552,5,0.3552,0.2939,no
SQVD_CLOS9,J1H1H5,ProtTale,Bacteria,447,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes the isomerization of sulfoquinovose (SQ) to 6-deoxy- 6-sulfo-D-fructose (SF) (Ref.2).",Catalyzes the conversion of L-arabinose to L-ribulose.,No,No,No,No,No,not-Yes,GO:0061593,GO:0008733,GO:0008733,GO:0008733,GO:0004790,GO:0008733,0.7289,0.7289,0.7289,0.1572,0.7289,5,0.6146,0.2939,no
SQVD_CLOS9,J1H1H5,Protein2Text,Bacteria,447,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes the isomerization of sulfoquinovose (SQ) to 6-deoxy- 6-sulfo-D-fructose (SF) (Ref.2).","The molecular function of this protein is an enzyme that catalyzes the conversion of L-tyrosine to 4-hydroxyphenylpyruvate. Specifically, it is a transaminase that transfers an amino group from L-tyrosine to alpha-ketoglutarate to form 4-hydroxyphenylpyruvate and glutamate. This reaction is part of the tyrosine catabolic pathway, where tyrosine is broken down into acetoacetate, which can be used as a precursor for the synthesis of fatty acids and cholesterol. The protein is involved in the metabolism of tyrosine and plays a crucial role in the degradation of tyrosine in the body.",No,No,No,No,No,not-Yes,GO:0061593,GO:0004838,GO:0004838,GO:0004838,GO:0004838,GO:0004838,0.1737,0.1737,0.1737,0.1737,0.1737,5,0.1737,0.2939,no
SQVD_CLOS9,J1H1H5,Reference,Bacteria,447,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes the isomerization of sulfoquinovose (SQ) to 6-deoxy- 6-sulfo-D-fructose (SF) (Ref.2).","Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes the isomerization of sulfoquinovose (SQ) to 6-deoxy- 6-sulfo-D-fructose (SF) (Ref.2).",,,,,,,GO:0061593,GO:0016853,GO:0016853,GO:0016853,GO:0016853,GO:0016853,0.6019,0.6019,0.6019,0.6019,0.6019,5,0.6019,0.2939,no
SQWF_CLOS9,J1H1J3,ESM2Text,Bacteria,373,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes the NADH-dependent reduction of sulfoacetaldehyde (SA) to 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Can also catalyze the reverse reaction, the formation of SA from isethionate in the presence of NAD(+) (Ref.2).",Specifically catalyzes the reduction of dimethylsulfonioproprionate (DMSP) to gamma-hydroxybutyrate (GHB). The DMSP is an intermediate in the biosynthesis of sulfolipid-containing cell wall glycolipids.,No,No,Maybe,No,No,not-Yes,GO:0004022; GO:0046872,,GO:0016491,,GO:0016491,,,0.4114,,0.4114,,2,0.4114,0.3152,no
SQWF_CLOS9,J1H1J3,Prot2Text,Bacteria,373,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes the NADH-dependent reduction of sulfoacetaldehyde (SA) to 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Can also catalyze the reverse reaction, the formation of SA from isethionate in the presence of NAD(+) (Ref.2).","Long-chain alkyl alcohol dehydrogenase that can oxidize a broad range of alkyl alcohols from ethanol to 1-triacontanol (C2 to C30) as well as 1,3-propanediol and acetaldehyde. The best substrate is ethanol. Also oxidizes glycerol.",No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004022; GO:0046872,GO:0004022,GO:0004022,GO:0016614,GO:0004022,GO:0004022,0.6924,0.6924,0.4732,0.6924,0.6924,5,0.6486,0.3152,no
SQWF_CLOS9,J1H1J3,ProtT3,Bacteria,373,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes the NADH-dependent reduction of sulfoacetaldehyde (SA) to 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Can also catalyze the reverse reaction, the formation of SA from isethionate in the presence of NAD(+) (Ref.2).",Belongs to the iron-containing alcohol dehydrogenase family,Vague,Vague,No,Vague,Vague,not-Yes,GO:0004022; GO:0046872,GO:0016491; GO:0005506,GO:0016491,,GO:0016616,GO:0016491,0.6544,0.4114,,0.5374,0.4114,4,0.5036,0.3152,no
SQWF_CLOS9,J1H1J3,ProtTale,Bacteria,373,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes the NADH-dependent reduction of sulfoacetaldehyde (SA) to 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Can also catalyze the reverse reaction, the formation of SA from isethionate in the presence of NAD(+) (Ref.2).","Reduces glyceraldehyde 3-phosphate to 1,3-dihydroxyacetone.",No,Maybe,Maybe,Maybe,No,not-Yes,GO:0004022; GO:0046872,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4114,0.4114,0.4114,0.4114,0.4114,5,0.4114,0.3152,no
SQWF_CLOS9,J1H1J3,Protein2Text,Bacteria,373,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes the NADH-dependent reduction of sulfoacetaldehyde (SA) to 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Can also catalyze the reverse reaction, the formation of SA from isethionate in the presence of NAD(+) (Ref.2).","The molecular function of this protein is an oxidoreductase, specifically a dehydrogenase, involved in the metabolism of glucose.",Vague,Vague,No,No,Vague,not-Yes,GO:0004022; GO:0046872,GO:0016491,GO:0016491,GO:0016614,,GO:0016491,0.4114,0.4114,0.4732,,0.4114,4,0.4269,0.3152,no
SQWF_CLOS9,J1H1J3,Reference,Bacteria,373,"Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes the NADH-dependent reduction of sulfoacetaldehyde (SA) to 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Can also catalyze the reverse reaction, the formation of SA from isethionate in the presence of NAD(+) (Ref.2).","Part of the sulfo-TK pathway, a D-sulfoquinovose degradation pathway that produces 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Catalyzes the NADH-dependent reduction of sulfoacetaldehyde (SA) to 2-hydroxyethane-1-sulfonate (isethionate) (Ref.2). Can also catalyze the reverse reaction, the formation of SA from isethionate in the presence of NAD(+) (Ref.2).",,,,,,,GO:0004022; GO:0046872,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.4114,0.4114,0.4114,0.4114,0.4114,5,0.4114,0.3152,no
MPSD_MACPH,K2SE88,ESM2Text,Eukaryota,396,"Diels-Alderase; part of the gene cluster that mediates the biosynthesis of macrophasetins, 3-decalinoyltetramic acids (DTAs) which feature a tetramate (pyrrolidine-2,4-dione) unit connected to a decalin fragment and that have potent bioactivities. The PKS- NRPS mpsA together with its associated enoylreductase partner mpsG incorporate one unit of acetyl-CoA, seven units of malonyl-CoA, and one unit of L-alanine to assemble the linear tetramic acid intermediate corresponding to the backbone of macrophasetins. Without the Diels-Alderase mpsD, the mpsA/G product can undergo the non-enzymatic intramolecular Diels-Alder (IMDA) reaction to generate both macrophasetin A and macrophasetin B. Catalyzed by mpsD, the linear tetramic acid intermediate is thoroughly converted to macrophasetin A via the endo-IMDA reaction in a regioselective and stereoselective manner. Finally, the cytochrome P450 monooxygenase mpsF catalyzes the hydroxylation at C20 to yield the end product macrophasetin C.",Involved in the production of the root hair deformation (HAD) factor specifically on medicago.,No,No,No,No,No,not-Yes,GO:0016853,,,,,,,,,,,0,,0.1632,no
MPSD_MACPH,K2SE88,Prot2Text,Eukaryota,396,"Diels-Alderase; part of the gene cluster that mediates the biosynthesis of macrophasetins, 3-decalinoyltetramic acids (DTAs) which feature a tetramate (pyrrolidine-2,4-dione) unit connected to a decalin fragment and that have potent bioactivities. The PKS- NRPS mpsA together with its associated enoylreductase partner mpsG incorporate one unit of acetyl-CoA, seven units of malonyl-CoA, and one unit of L-alanine to assemble the linear tetramic acid intermediate corresponding to the backbone of macrophasetins. Without the Diels-Alderase mpsD, the mpsA/G product can undergo the non-enzymatic intramolecular Diels-Alder (IMDA) reaction to generate both macrophasetin A and macrophasetin B. Catalyzed by mpsD, the linear tetramic acid intermediate is thoroughly converted to macrophasetin A via the endo-IMDA reaction in a regioselective and stereoselective manner. Finally, the cytochrome P450 monooxygenase mpsF catalyzes the hydroxylation at C20 to yield the end product macrophasetin C.","Diels-Alderase; part of the gene cluster that mediates the biosynthesis of the mycotoxin pyrichalasin H, a tyrosine-derived cytochalasan that inhibits the growth of rice seedlings, but also inhibits lymphocyte capping and actin polymerization and alters cell morphology  (Probable). Pyrichalasin H is indicated as the responsible agent for the genus-specific pathogenicity of M.grisea toward crabgrass. The first step in the pathway is catalyzed by the O-methyltransferase pyiA which methylates free tyrosine to generate the precursor O-methyltyrosine. The hybrid PKS-NRPS pyiS, assisted by the enoyl reductase pyiC, are responsible for fusion of the O-methyltyrosine precursor and the polyketide backbone. The polyketide synthase module (PKS) of pyiS is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the O-methyltyrosine precursor. As the NRPS A-domain demonstrates substrate tolerance,",Yes,Yes,Maybe,Yes,Yes,Yes,GO:0016853,,,,,GO:0016829,,,,,0.5902,1,0.5902,0.1632,no
MPSD_MACPH,K2SE88,ProtT3,Eukaryota,396,"Diels-Alderase; part of the gene cluster that mediates the biosynthesis of macrophasetins, 3-decalinoyltetramic acids (DTAs) which feature a tetramate (pyrrolidine-2,4-dione) unit connected to a decalin fragment and that have potent bioactivities. The PKS- NRPS mpsA together with its associated enoylreductase partner mpsG incorporate one unit of acetyl-CoA, seven units of malonyl-CoA, and one unit of L-alanine to assemble the linear tetramic acid intermediate corresponding to the backbone of macrophasetins. Without the Diels-Alderase mpsD, the mpsA/G product can undergo the non-enzymatic intramolecular Diels-Alder (IMDA) reaction to generate both macrophasetin A and macrophasetin B. Catalyzed by mpsD, the linear tetramic acid intermediate is thoroughly converted to macrophasetin A via the endo-IMDA reaction in a regioselective and stereoselective manner. Finally, the cytochrome P450 monooxygenase mpsF catalyzes the hydroxylation at C20 to yield the end product macrophasetin C.","Diels-Alderase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By similarity). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (By similarity). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016853,GO:0016872,GO:0016829,GO:0016829,GO:0016829,GO:0016829,0.8145,0.5902,0.5902,0.5902,0.5902,5,0.6351,0.1632,no
MPSD_MACPH,K2SE88,ProtTale,Eukaryota,396,"Diels-Alderase; part of the gene cluster that mediates the biosynthesis of macrophasetins, 3-decalinoyltetramic acids (DTAs) which feature a tetramate (pyrrolidine-2,4-dione) unit connected to a decalin fragment and that have potent bioactivities. The PKS- NRPS mpsA together with its associated enoylreductase partner mpsG incorporate one unit of acetyl-CoA, seven units of malonyl-CoA, and one unit of L-alanine to assemble the linear tetramic acid intermediate corresponding to the backbone of macrophasetins. Without the Diels-Alderase mpsD, the mpsA/G product can undergo the non-enzymatic intramolecular Diels-Alder (IMDA) reaction to generate both macrophasetin A and macrophasetin B. Catalyzed by mpsD, the linear tetramic acid intermediate is thoroughly converted to macrophasetin A via the endo-IMDA reaction in a regioselective and stereoselective manner. Finally, the cytochrome P450 monooxygenase mpsF catalyzes the hydroxylation at C20 to yield the end product macrophasetin C.","Diels-Alderase; part of the gene cluster that mediates the biosynthesis of oxaleimides, cytotoxic compounds containing an unusual disubstituted succinimide moiety. The first step of the pathway is provided by the HR-PKS poxF that serves in a new mode of collaborative biosynthesis with the PKS-NRPS poxE, by providing the olefin containing amino acid substrate via the synthesis of an ACP- bound dec-4-enoate. The cytochrome P450 monooxygenase poxM-catalyzed oxidation at the alpha-position creates the enzyme-bound 2-hydroxydec-4-",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016853,,GO:0016829,GO:0016829,,GO:0016829,,0.5902,0.5902,,0.5902,3,0.5902,0.1632,no
MPSD_MACPH,K2SE88,Protein2Text,Eukaryota,396,"Diels-Alderase; part of the gene cluster that mediates the biosynthesis of macrophasetins, 3-decalinoyltetramic acids (DTAs) which feature a tetramate (pyrrolidine-2,4-dione) unit connected to a decalin fragment and that have potent bioactivities. The PKS- NRPS mpsA together with its associated enoylreductase partner mpsG incorporate one unit of acetyl-CoA, seven units of malonyl-CoA, and one unit of L-alanine to assemble the linear tetramic acid intermediate corresponding to the backbone of macrophasetins. Without the Diels-Alderase mpsD, the mpsA/G product can undergo the non-enzymatic intramolecular Diels-Alder (IMDA) reaction to generate both macrophasetin A and macrophasetin B. Catalyzed by mpsD, the linear tetramic acid intermediate is thoroughly converted to macrophasetin A via the endo-IMDA reaction in a regioselective and stereoselective manner. Finally, the cytochrome P450 monooxygenase mpsF catalyzes the hydroxylation at C20 to yield the end product macrophasetin C.","The molecular function of this protein is not specified in the provided text. However, based on the name ""alkaloid synthase"", it is likely that this protein is involved in the synthesis of alkaloids, which are a class of natural products that contain a nitrogen atom as part of a ring structure. Alkaloids are typically produced by plants and fungi, and they have a wide range of biological activities, including antibacterial, antifungal, and anticancer properties. The specific function of this protein is likely to be involved in the biosynthesis of a particular alkaloid, such as ergotamine or ergosine.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0016853,,,,,,,,,,,0,,0.1632,no
MPSD_MACPH,K2SE88,Reference,Eukaryota,396,"Diels-Alderase; part of the gene cluster that mediates the biosynthesis of macrophasetins, 3-decalinoyltetramic acids (DTAs) which feature a tetramate (pyrrolidine-2,4-dione) unit connected to a decalin fragment and that have potent bioactivities. The PKS- NRPS mpsA together with its associated enoylreductase partner mpsG incorporate one unit of acetyl-CoA, seven units of malonyl-CoA, and one unit of L-alanine to assemble the linear tetramic acid intermediate corresponding to the backbone of macrophasetins. Without the Diels-Alderase mpsD, the mpsA/G product can undergo the non-enzymatic intramolecular Diels-Alder (IMDA) reaction to generate both macrophasetin A and macrophasetin B. Catalyzed by mpsD, the linear tetramic acid intermediate is thoroughly converted to macrophasetin A via the endo-IMDA reaction in a regioselective and stereoselective manner. Finally, the cytochrome P450 monooxygenase mpsF catalyzes the hydroxylation at C20 to yield the end product macrophasetin C.","Diels-Alderase; part of the gene cluster that mediates the biosynthesis of macrophasetins, 3-decalinoyltetramic acids (DTAs) which feature a tetramate (pyrrolidine-2,4-dione) unit connected to a decalin fragment and that have potent bioactivities. The PKS- NRPS mpsA together with its associated enoylreductase partner mpsG incorporate one unit of acetyl-CoA, seven units of malonyl-CoA, and one unit of L-alanine to assemble the linear tetramic acid intermediate corresponding to the backbone of macrophasetins. Without the Diels-Alderase mpsD, the mpsA/G product can undergo the non-enzymatic intramolecular Diels-Alder (IMDA) reaction to generate both macrophasetin A and macrophasetin B. Catalyzed by mpsD, the linear tetramic acid intermediate is thoroughly converted to macrophasetin A via the endo-IMDA reaction in a regioselective and stereoselective manner. Finally, the cytochrome P450 monooxygenase mpsF catalyzes the hydroxylation at C20 to yield the end product macrophasetin C.",,,,,,,GO:0016853,GO:0016829,GO:0016829,GO:0016829,GO:0016829,GO:0016829,0.5902,0.5902,0.5902,0.5902,0.5902,5,0.5902,0.1632,no
RP22_VACCW,P68609,ESM2Text,Viruses,185,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.","Cleaves ssRNA, mostly between U:A.",No,No,No,No,No,not-Yes,GO:0003677; GO:0003899,GO:0004521,GO:0004521,GO:0004521,GO:0004521,GO:0004521,0.2541,0.2541,0.2541,0.2541,0.2541,5,0.2541,0.3274,no
RP22_VACCW,P68609,Prot2Text,Viruses,185,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.","Cleaves ssRNA, mostly between U:A.",No,No,No,No,No,not-Yes,GO:0003677; GO:0003899,GO:0004521,GO:0004521,GO:0004521,GO:0004521,GO:0004521,0.2541,0.2541,0.2541,0.2541,0.2541,5,0.2541,0.3274,no
RP22_VACCW,P68609,ProtT3,Viruses,185,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.","Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG114 and OPG115, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase. Virion Note=All the enzymes and other proteins required to synthesize early mRNAs are packaged within the virion core along with",Yes,Yes,Yes,Yes,Yes,Yes,GO:0003677; GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.6983,0.6983,0.6983,0.6983,0.6983,5,0.6983,0.3274,no
RP22_VACCW,P68609,ProtTale,Viruses,185,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.","Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network",No,No,No,No,No,not-Yes,GO:0003677; GO:0003899,,,,,,,,,,,0,,0.3274,no
RP22_VACCW,P68609,Protein2Text,Viruses,185,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.","The molecular function of this protein is not explicitly stated in the provided information. However, based on its name, it is likely involved in a process related to viral replication or assembly, possibly as a component of a viral capsid or a protein involved in DNA replication. Further research would be necessary to determine the specific molecular function of this protein.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0003677; GO:0003899,,,,,,,,,,,0,,0.3274,no
RP22_VACCW,P68609,Reference,Viruses,185,"Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.","Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.",,,,,,,GO:0003677; GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.6983,0.6983,0.6983,0.6983,0.6983,5,0.6983,0.3274,no
ARGN_STREL,M1T9N7,ESM2Text,Bacteria,337,"S-adenosyl-L-methionine-dependent methyltransferase involved in the formation of the rare amino acid 3-methylarginine (MeArg), which is incorporated into the peptidyl nucleoside antibiotic arginomycin. Transfers the methyl group from S-adenosyl-L- methionine into 5-guanidino-2-oxopentanoate acid to yield 5-guanidino- 3-methyl-2-oxopentanoate, a precursor of MeArg.",S-adenosyl-L-methionine-dependent methyltransferase that mediates the methylation of 5-methoxybenzoate (m4ABA) to form 5-methoxybenzoyl-CoA (m4PartA) at position 34 in tRNAs. Four tRNAs (tRNA(Asp(Asp)) are fully reduced to MOBAs (tRNA(Asp(Asp)) by methylation and tRNA(Asn)) are not processed by the methyltransferase. Also mediates the methylation of tRNAs at position 56 in tRNAs.,No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008168,GO:0008173,GO:0008173,,GO:0008173,GO:0008175,0.7187,0.7187,,0.7187,0.6014,4,0.6894,0.152,no
ARGN_STREL,M1T9N7,Prot2Text,Bacteria,337,"S-adenosyl-L-methionine-dependent methyltransferase involved in the formation of the rare amino acid 3-methylarginine (MeArg), which is incorporated into the peptidyl nucleoside antibiotic arginomycin. Transfers the methyl group from S-adenosyl-L- methionine into 5-guanidino-2-oxopentanoate acid to yield 5-guanidino- 3-methyl-2-oxopentanoate, a precursor of MeArg.","Involved in the biosynthesis of the anthracyclines carminomycin and daunorubicin (daunomycin) which are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the methylation of the epsilon-amino group of lysine leading to 7-demethylscyllo-inosamine (8-demethylscyllo-inosamine). It methylates the 8-demethylscyllo-inosamine, 8-demethylscyllo-inosamine and 8-demethylscyllo-inosamine at similar rates. It also methylates the 3-demethylscyllo-inosamine, 3-demethylscyllo-inosamine and 3-demethylscyllo-inosamine at similar rates.",No,Maybe,No,Maybe,Maybe,not-Yes,GO:0008168,GO:0008168,,GO:0008168,GO:0008168,GO:0008168,1.0,,1.0,1.0,1.0,4,1.0,0.152,no
ARGN_STREL,M1T9N7,ProtT3,Bacteria,337,"S-adenosyl-L-methionine-dependent methyltransferase involved in the formation of the rare amino acid 3-methylarginine (MeArg), which is incorporated into the peptidyl nucleoside antibiotic arginomycin. Transfers the methyl group from S-adenosyl-L- methionine into 5-guanidino-2-oxopentanoate acid to yield 5-guanidino- 3-methyl-2-oxopentanoate, a precursor of MeArg.",S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the methylation of 2'-deoxyuridine (dU) to 2'-deoxyuridine 5'-monophosphate (dUMP). Belongs to the methyltransferase superfamily. 2'-deoxyuridine-5'-monophosphate N(6)-methyltransferase family,No,No,No,Maybe,Maybe,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.152,no
ARGN_STREL,M1T9N7,ProtTale,Bacteria,337,"S-adenosyl-L-methionine-dependent methyltransferase involved in the formation of the rare amino acid 3-methylarginine (MeArg), which is incorporated into the peptidyl nucleoside antibiotic arginomycin. Transfers the methyl group from S-adenosyl-L- methionine into 5-guanidino-2-oxopentanoate acid to yield 5-guanidino- 3-methyl-2-oxopentanoate, a precursor of MeArg.","Involved in the biosynthesis of the anthracycline antibiotic daunomycin which is used in the treatment of cancer. Catalyzes the O-demethylation of 2,3- dihydroxy-1,4-naphtoquinone (2,3-DHNQ) to yield 2,3-dihydroxy-1,4-naphtoquinone (2,3-DHNQ). Also able to catalyze the O-methylation of 2,3-DHNQ to yield 2,3-dimethoxy-1,4-naphtoquinone (2,3-DM",No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008168,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.152,no
ARGN_STREL,M1T9N7,Protein2Text,Bacteria,337,"S-adenosyl-L-methionine-dependent methyltransferase involved in the formation of the rare amino acid 3-methylarginine (MeArg), which is incorporated into the peptidyl nucleoside antibiotic arginomycin. Transfers the methyl group from S-adenosyl-L- methionine into 5-guanidino-2-oxopentanoate acid to yield 5-guanidino- 3-methyl-2-oxopentanoate, a precursor of MeArg.","The molecular function of this protein is not explicitly stated in the provided text. However, based on the name ""O-methyltransferase"" and the fact that it is involved in the biosynthesis of a compound, it is likely that this protein catalyzes the transfer of a methyl group to a substrate molecule. More specifically, it may be involved in the methylation of a compound, such as a flavonoid, which is a common process in the biosynthesis of many natural products.",Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0008168,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.152,no
ARGN_STREL,M1T9N7,Reference,Bacteria,337,"S-adenosyl-L-methionine-dependent methyltransferase involved in the formation of the rare amino acid 3-methylarginine (MeArg), which is incorporated into the peptidyl nucleoside antibiotic arginomycin. Transfers the methyl group from S-adenosyl-L- methionine into 5-guanidino-2-oxopentanoate acid to yield 5-guanidino- 3-methyl-2-oxopentanoate, a precursor of MeArg.","S-adenosyl-L-methionine-dependent methyltransferase involved in the formation of the rare amino acid 3-methylarginine (MeArg), which is incorporated into the peptidyl nucleoside antibiotic arginomycin. Transfers the methyl group from S-adenosyl-L- methionine into 5-guanidino-2-oxopentanoate acid to yield 5-guanidino- 3-methyl-2-oxopentanoate, a precursor of MeArg.",,,,,,,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.152,no
CL12B_MYCTU,O53438,ESM2Text,Bacteria,151,"Probable cellulase. Can hydrolyze barley beta-glucan in vitro. Could be important for the survival of M.tuberculosis in the environment, perhaps in amoebal hosts.",Citrate lyase-like protein that seems to be implicated in the pathogenesis of acquired resistance to azoles such as itraconazole.,No,No,No,No,No,not-Yes,GO:0008810,,,,,,,,,,,0,,0.2313,no
CL12B_MYCTU,O53438,Prot2Text,Bacteria,151,"Probable cellulase. Can hydrolyze barley beta-glucan in vitro. Could be important for the survival of M.tuberculosis in the environment, perhaps in amoebal hosts.",Not known; seems to contribute to the tellurium resistance (Ter) mechanism.,No,No,No,No,No,not-Yes,GO:0008810,,,,,,,,,,,0,,0.2313,no
CL12B_MYCTU,O53438,ProtT3,Bacteria,151,"Probable cellulase. Can hydrolyze barley beta-glucan in vitro. Could be important for the survival of M.tuberculosis in the environment, perhaps in amoebal hosts.",Belongs to the UPF0158 family,Vague,Vague,No,Vague,Vague,not-Yes,GO:0008810,,,,,,,,,,,0,,0.2313,no
CL12B_MYCTU,O53438,ProtTale,Bacteria,151,"Probable cellulase. Can hydrolyze barley beta-glucan in vitro. Could be important for the survival of M.tuberculosis in the environment, perhaps in amoebal hosts.","Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.",No,No,No,No,Maybe,not-Yes,GO:0008810,GO:0031176,GO:0031176,GO:0031176,GO:0031176,GO:0031176,0.6335,0.6335,0.6335,0.6335,0.6335,5,0.6335,0.2313,no
CL12B_MYCTU,O53438,Protein2Text,Bacteria,151,"Probable cellulase. Can hydrolyze barley beta-glucan in vitro. Could be important for the survival of M.tuberculosis in the environment, perhaps in amoebal hosts.","This protein is involved in catalyzing the hydrolysis of tartrate esters. It is likely to be a part of the metabolic pathway that breaks down tartrate esters, which are a type of organic compound found in various biological systems. The specific molecular function of this protein is to catalyze the hydrolysis of tartrate esters, which is a crucial step in the breakdown and utilization of these compounds. 

Please note that the exact molecular function of this protein is not explicitly stated in the provided information, but based on its classification as a hydrolase, it is likely to be involved in catalyzing the hydrolysis of tartrate esters.",No,No,No,No,No,not-Yes,GO:0008810,GO:0016788,GO:0016788,GO:0016788,GO:0016788,GO:0016788,0.482,0.482,0.482,0.482,0.482,5,0.482,0.2313,no
CL12B_MYCTU,O53438,Reference,Bacteria,151,"Probable cellulase. Can hydrolyze barley beta-glucan in vitro. Could be important for the survival of M.tuberculosis in the environment, perhaps in amoebal hosts.","Probable cellulase. Can hydrolyze barley beta-glucan in vitro. Could be important for the survival of M.tuberculosis in the environment, perhaps in amoebal hosts.",,,,,,,GO:0008810,GO:0008810,GO:0008810,GO:0008810,GO:0008810,GO:0008810,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2313,no
3BHD_MYCNE,P0DX24,ESM2Text,Bacteria,366,Catalyzes the degradation of testosterone into androstenedione.,"3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidation and isomerization of cholesterol, pregnenolone, and dehydroepiandrosterone (DHEA) into cholest-4-en-3-one, progesterone, and androsterone, respectively.",Maybe,Yes,Maybe,Yes,Yes,Yes,GO:0016616,GO:0003854,GO:0003854,GO:0003854,GO:0003854,GO:0003854,0.7025,0.7025,0.7025,0.7025,0.7025,5,0.7025,0.2204,no
3BHD_MYCNE,P0DX24,Prot2Text,Bacteria,366,Catalyzes the degradation of testosterone into androstenedione.,"3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidation and isomerization of cholesterol, pregnenolone, and dehydroepiandrosterone (DHEA) into cholest-4-en-3-one, progesterone, and androsterone, respectively.",Maybe,Yes,Maybe,Yes,Yes,Yes,GO:0016616,GO:0003854,GO:0003854,GO:0003854,GO:0016229,GO:0003854,0.7025,0.7025,0.7025,0.5565,0.7025,5,0.6733,0.2204,no
3BHD_MYCNE,P0DX24,ProtT3,Bacteria,366,Catalyzes the degradation of testosterone into androstenedione.,"Catalyzes the oxidation of 3-ketosteroids to 3,5-diketosteroids and the reduction of 3,5-diketosteroids to 3- ketosteroids. Endoplasmic reticulum membrane; Single-pass membrane protein. Belongs to the 3-beta-HSD family",Maybe,Yes,Maybe,Yes,Yes,Yes,GO:0016616,GO:0016491,GO:0016491,GO:0016491,GO:0016229,GO:0003854,0.6897,0.6897,0.6897,0.5565,0.7025,5,0.6656,0.2204,no
3BHD_MYCNE,P0DX24,ProtTale,Bacteria,366,Catalyzes the degradation of testosterone into androstenedione.,"NADP-dependent dehydrogenase; part of the gene cluster that mediates the biosynthesis of the tetrahydropyranyl antifungal agent restricticin that acts as an inhibitor of CYP51 and blocks the ergosterol biosynthesis. The highly reducing polyketide synthase rstn3, the short chain dehydrogenase rstn4, the cyclase rstn5, the FAD-dependent monooxygenase rstn6 and the enoylreductase rstn7 are required to generate the first stable intermediate desmethylrestrictinol. Rstn3 with rstn7 biosynthesize the first polyketide chain intermediate that is reduced by rstn4, followed by",No,Maybe,No,Maybe,No,not-Yes,GO:0016616,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.6897,0.6897,0.6897,0.6897,0.6897,5,0.6897,0.2204,no
3BHD_MYCNE,P0DX24,Protein2Text,Bacteria,366,Catalyzes the degradation of testosterone into androstenedione.,"The molecular function of this protein is likely to be involved in the synthesis or modification of steroids, as it is a 3-keto-steroid reductase, which is a type of enzyme that catalyzes the reduction of a ketone group in a steroid molecule. Specifically, it is involved in the reduction of 3-keto groups in steroid substrates, such as cholesterol and other steroid hormones. This protein is likely to play a role in the biosynthesis of steroid hormones, which are important signaling molecules in the body.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016616,GO:0016491,GO:0016491,,,GO:0016229,0.6897,0.6897,,,0.5565,3,0.6453,0.2204,no
3BHD_MYCNE,P0DX24,Reference,Bacteria,366,Catalyzes the degradation of testosterone into androstenedione.,Catalyzes the degradation of testosterone into androstenedione.,,,,,,,GO:0016616,GO:0016616,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,0.6897,0.6897,0.6897,0.6897,5,0.7518,0.2204,no
DHOM_PSECO,P0DXC5,ESM2Text,Bacteria,352,"Dehydrogenase involved in the degradation of canavanine, the delta-oxa-analog of arginine, allowing growth on canavanine as sole nitrogen and carbon source. Catalyzes the conversion of homoserine and NAD(+) to aspartate-semialdehyde and NADH. Is highly specific for NAD(+) and cannot use NADP(+).",Catalyzes the NADPH-dependent reduction of L-seryl-tRNA(Cys) to 2-C-methyl-D-erythritol 4-phosphate.,No,No,Maybe,No,No,not-Yes,GO:0004412,,GO:0016491,,,,,0.6019,,,,1,0.6019,0.3185,no
DHOM_PSECO,P0DXC5,Prot2Text,Bacteria,352,"Dehydrogenase involved in the degradation of canavanine, the delta-oxa-analog of arginine, allowing growth on canavanine as sole nitrogen and carbon source. Catalyzes the conversion of homoserine and NAD(+) to aspartate-semialdehyde and NADH. Is highly specific for NAD(+) and cannot use NADP(+).",Catalyzes the NADPH-dependent reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).,No,No,No,No,No,not-Yes,GO:0004412,GO:0030604,GO:0030604,GO:0030604,GO:0030604,GO:0030604,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.3185,no
DHOM_PSECO,P0DXC5,ProtT3,Bacteria,352,"Dehydrogenase involved in the degradation of canavanine, the delta-oxa-analog of arginine, allowing growth on canavanine as sole nitrogen and carbon source. Catalyzes the conversion of homoserine and NAD(+) to aspartate-semialdehyde and NADH. Is highly specific for NAD(+) and cannot use NADP(+).",Belongs to the homoserine dehydrogenase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004412,GO:0004412,GO:0004412,,GO:0004412,GO:0004412,1.0,1.0,,1.0,1.0,4,1.0,0.3185,no
DHOM_PSECO,P0DXC5,ProtTale,Bacteria,352,"Dehydrogenase involved in the degradation of canavanine, the delta-oxa-analog of arginine, allowing growth on canavanine as sole nitrogen and carbon source. Catalyzes the conversion of homoserine and NAD(+) to aspartate-semialdehyde and NADH. Is highly specific for NAD(+) and cannot use NADP(+).","Catalyzes the conversion of L-aspartate-beta-semialdehyde (L- Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate.",Maybe,Maybe,Maybe,Maybe,Yes,not-Yes,GO:0004412,GO:0004412,GO:0004412,GO:0004412,GO:0004412,GO:0004412,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3185,no
DHOM_PSECO,P0DXC5,Protein2Text,Bacteria,352,"Dehydrogenase involved in the degradation of canavanine, the delta-oxa-analog of arginine, allowing growth on canavanine as sole nitrogen and carbon source. Catalyzes the conversion of homoserine and NAD(+) to aspartate-semialdehyde and NADH. Is highly specific for NAD(+) and cannot use NADP(+).","The molecular function of this protein is an isomerase enzyme, specifically a cis->trans isomerase, which catalyzes the conversion of cis-1,2-propanediol into trans-1,2-propanediol.",No,No,No,No,No,not-Yes,GO:0004412,GO:0016853,GO:0016859,GO:0016853,,GO:0016853,0.3552,0.2845,0.3552,,0.3552,4,0.3375,0.3185,no
DHOM_PSECO,P0DXC5,Reference,Bacteria,352,"Dehydrogenase involved in the degradation of canavanine, the delta-oxa-analog of arginine, allowing growth on canavanine as sole nitrogen and carbon source. Catalyzes the conversion of homoserine and NAD(+) to aspartate-semialdehyde and NADH. Is highly specific for NAD(+) and cannot use NADP(+).","Dehydrogenase involved in the degradation of canavanine, the delta-oxa-analog of arginine, allowing growth on canavanine as sole nitrogen and carbon source. Catalyzes the conversion of homoserine and NAD(+) to aspartate-semialdehyde and NADH. Is highly specific for NAD(+) and cannot use NADP(+).",,,,,,,GO:0004412,GO:0004412,GO:0004412,GO:0004412,GO:0004412,GO:0016616,1.0,1.0,1.0,1.0,0.8582,5,0.9716,0.3185,no
FBSK_ACIBT,P0DXD7,ESM2Text,Bacteria,208,"N-acetyltransferase involved in the biosynthesis of fimsbactin A, the major siderophore produced by A.baumannii. Catalyzes the acetylation of N-hydroxyputrescine to form N(1)-acetyl-N(1)-hydroxyputrescine (ahPutr).","Activates transcription of the type III secretion system (T3SS), also called injectisome, by binding to several nucleoporins. Necessary for the secretion of HetM.",No,No,Maybe,No,No,not-Yes,GO:0016410,,GO:0003700,,,,,0.1579,,,,1,0.1579,0.352,no
FBSK_ACIBT,P0DXD7,Prot2Text,Bacteria,208,"N-acetyltransferase involved in the biosynthesis of fimsbactin A, the major siderophore produced by A.baumannii. Catalyzes the acetylation of N-hydroxyputrescine to form N(1)-acetyl-N(1)-hydroxyputrescine (ahPutr).",Acyltransferase required for the synthesis of the acyl-homoserine lactone (AHL or conjugative lactone) from L-lysine.,Maybe,Maybe,Maybe,No,Maybe,not-Yes,GO:0016410,GO:0016746,GO:0016747,GO:0016747,GO:0016746,GO:0016746,0.729,0.8582,0.8582,0.729,0.729,5,0.7807,0.352,no
FBSK_ACIBT,P0DXD7,ProtT3,Bacteria,208,"N-acetyltransferase involved in the biosynthesis of fimsbactin A, the major siderophore produced by A.baumannii. Catalyzes the acetylation of N-hydroxyputrescine to form N(1)-acetyl-N(1)-hydroxyputrescine (ahPutr).","Acyltransferase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties . L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L- homoserine by cluster enzymes aspartate",No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016410,GO:0016746,GO:0016746,GO:0016746,GO:0016747,GO:0016747,0.729,0.729,0.729,0.8582,0.8582,5,0.7807,0.352,no
FBSK_ACIBT,P0DXD7,ProtTale,Bacteria,208,"N-acetyltransferase involved in the biosynthesis of fimsbactin A, the major siderophore produced by A.baumannii. Catalyzes the acetylation of N-hydroxyputrescine to form N(1)-acetyl-N(1)-hydroxyputrescine (ahPutr).","Catalyzes the transfer of an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.",No,Maybe,No,Maybe,Maybe,not-Yes,GO:0016410,GO:0004414,GO:0004414,GO:0004414,GO:0004414,GO:0004414,0.5195,0.5195,0.5195,0.5195,0.5195,5,0.5195,0.352,no
FBSK_ACIBT,P0DXD7,Protein2Text,Bacteria,208,"N-acetyltransferase involved in the biosynthesis of fimsbactin A, the major siderophore produced by A.baumannii. Catalyzes the acetylation of N-hydroxyputrescine to form N(1)-acetyl-N(1)-hydroxyputrescine (ahPutr).","The molecular function of this protein is acetyltransferase activity.
This protein is involved in the transfer of an acetyl group from one molecule to another. Specifically, it is a type of acetyltransferase that catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate, likely involved in the biosynthesis of a metabolite. The exact substrate of this protein is not specified in the provided information. 
The acetyl group is a small organic molecule consisting of an acetyl functional group (-COCH3) attached to a larger molecule. Acetyltransferases are enzymes that catalyze the transfer of this group from one molecule to another. This reaction is an important step in many biological pathways, including the biosynthesis of amino acids, hormones, and other metabolites. The acetyl group can be transferred to a variety of substrates, including amino acids, sugars, and other organic molecules. In some cases, the acetyl group can be transferred to a nucleophilic group, such as an amino or hydroxyl group, to form a new bond. The acetyl group can also be transferred to a carboxyl group, resulting in the formation of an ester bond. The acetyl group can be transferred from acetyl-CoA, which is a high-energy compound that provides the energy needed to drive the reaction. The acetyl group can also be transferred from other acetyl donors, such as acetyl- phosphate or acetyl-adenylate. The acetyl group can be transferred to a variety of substrates, including amino acids, sugars, and other organic molecules. In some cases, the acetyl group can be transferred to a nucleophilic group, such as an amino or hydroxyl group, to form a new bond. The acetyl group can also be transferred to a carboxyl group, resulting in the formation of an ester bond. The acetyl group can be transferred from acetyl-CoA, which is a high-energy compound that provides the energy needed to drive the reaction. The acetyl group can also be transferred from other acetyl donors, such as acetyl- phosphate or acetyl-adenylate. 
In the context of the provided information, the molecular function of this protein is likely involved in the biosynthesis of a metabolite, specifically a type of acetyltransferase activity. However, the exact substrate of this protein is not specified. 
In general, acetyltransferases are enzymes that catalyze the transfer of an ac",Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016410,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.352,no
FBSK_ACIBT,P0DXD7,Reference,Bacteria,208,"N-acetyltransferase involved in the biosynthesis of fimsbactin A, the major siderophore produced by A.baumannii. Catalyzes the acetylation of N-hydroxyputrescine to form N(1)-acetyl-N(1)-hydroxyputrescine (ahPutr).","N-acetyltransferase involved in the biosynthesis of fimsbactin A, the major siderophore produced by A.baumannii. Catalyzes the acetylation of N-hydroxyputrescine to form N(1)-acetyl-N(1)-hydroxyputrescine (ahPutr).",,,,,,,GO:0016410,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.7289,0.7289,0.7289,0.7289,0.7289,5,0.7289,0.352,no
UAEPH_CAMJ8,P0DY05,ESM2Text,Bacteria,373,Hydrolyzing C2-epimerase involved in the biosynthesis of capsular polysaccharides. Catalyzes the C2 epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc) and the subsequent hydrolysis of the product to form N-acetyl-D-mannosamine (ManNAc) with the release of UDP.,Catalyzes the conversion of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP and N-acetylmannosamine (ManNAc). Involved in the biosynthesis of the capsular polysaccharide colanic acid.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0016787,GO:0016787,GO:0016854,GO:0050378,GO:0008761,GO:0008767,1.0,0.4807,0.3552,0.3552,0.4071,5,0.5196,0.4812,no
UAEPH_CAMJ8,P0DY05,Prot2Text,Bacteria,373,Hydrolyzing C2-epimerase involved in the biosynthesis of capsular polysaccharides. Catalyzes the C2 epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc) and the subsequent hydrolysis of the product to form N-acetyl-D-mannosamine (ManNAc) with the release of UDP.,Catalyzes the conversion of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP and N-acetylmannosamine (ManNAc).,Yes,Yes,Yes,Yes,Yes,Yes,GO:0016787,GO:0008761,GO:0008761,GO:0008761,GO:0008761,GO:0008767,0.3552,0.3552,0.3552,0.3552,0.4071,5,0.3656,0.4812,no
UAEPH_CAMJ8,P0DY05,ProtT3,Bacteria,373,Hydrolyzing C2-epimerase involved in the biosynthesis of capsular polysaccharides. Catalyzes the C2 epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc) and the subsequent hydrolysis of the product to form N-acetyl-D-mannosamine (ManNAc) with the release of UDP.,Catalyzes the reversible epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N-acetylmannosamine (UDP-ManNAc). Belongs to the UDP-N-acetylglucosamine 2-epimerase family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016787,GO:0008761,GO:0008761,GO:0003978,GO:0008761,GO:0008761,0.3552,0.3552,0.3552,0.3552,0.3552,5,0.3552,0.4812,no
UAEPH_CAMJ8,P0DY05,ProtTale,Bacteria,373,Hydrolyzing C2-epimerase involved in the biosynthesis of capsular polysaccharides. Catalyzes the C2 epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc) and the subsequent hydrolysis of the product to form N-acetyl-D-mannosamine (ManNAc) with the release of UDP.,"May be involved in the synthesis of poly-beta-1,6-N-acetyl-D- glucosamine (PGA).",No,No,No,No,No,not-Yes,GO:0016787,,,,,,,,,,,0,,0.4812,no
UAEPH_CAMJ8,P0DY05,Protein2Text,Bacteria,373,Hydrolyzing C2-epimerase involved in the biosynthesis of capsular polysaccharides. Catalyzes the C2 epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc) and the subsequent hydrolysis of the product to form N-acetyl-D-mannosamine (ManNAc) with the release of UDP.,"The molecular function of this protein is an enzyme, specifically a transferase. More specifically, it is an enzyme that catalyzes the transfer of a group from one molecule to another.",Vague,Vague,No,Vague,No,not-Yes,GO:0016787,GO:0016740,,,,,0.5902,,,,,1,0.5902,0.4812,no
UAEPH_CAMJ8,P0DY05,Reference,Bacteria,373,Hydrolyzing C2-epimerase involved in the biosynthesis of capsular polysaccharides. Catalyzes the C2 epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc) and the subsequent hydrolysis of the product to form N-acetyl-D-mannosamine (ManNAc) with the release of UDP.,Hydrolyzing C2-epimerase involved in the biosynthesis of capsular polysaccharides. Catalyzes the C2 epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc) and the subsequent hydrolysis of the product to form N-acetyl-D-mannosamine (ManNAc) with the release of UDP.,,,,,,,GO:0016787,GO:0008761; GO:0016787,GO:0016854; GO:0016787,GO:0003855; GO:0016787,GO:0003974; GO:0016787,GO:0008761; GO:0016787,0.7851,0.8269,0.7851,0.7851,0.7851,5,0.7935,0.4812,no
NEUAS_CAMJ8,P0DY06,ESM2Text,Bacteria,346,Transferase involved in the biosynthesis of capsular polysaccharides. Catalyzes the condensation of N- acetyl-D-mannosamine (ManNAc) and phosphoenolpyruvate to generate N- acetylneuraminate (Neu5Ac).,"Catalyzes the condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis.",No,No,No,No,No,not-Yes,GO:0050462,GO:0004332,GO:0004332,GO:0004332,GO:0004332,GO:0004332,0.2353,0.2353,0.2353,0.2353,0.2353,5,0.2353,0.3042,no
NEUAS_CAMJ8,P0DY06,Prot2Text,Bacteria,346,Transferase involved in the biosynthesis of capsular polysaccharides. Catalyzes the condensation of N- acetyl-D-mannosamine (ManNAc) and phosphoenolpyruvate to generate N- acetylneuraminate (Neu5Ac).,"Catalyzes the second step in the biosynthesis of pseudaminic acid, a sialic-acid-like sugar that is used to modify flagellin. Catalyzes the condensation of 2 glucose residues from 2 S-adenosyl-L-methionine molecules to generate pseudaminic acid.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0050462,,,,,,,,,,,0,,0.3042,no
NEUAS_CAMJ8,P0DY06,ProtT3,Bacteria,346,Transferase involved in the biosynthesis of capsular polysaccharides. Catalyzes the condensation of N- acetyl-D-mannosamine (ManNAc) and phosphoenolpyruvate to generate N- acetylneuraminate (Neu5Ac).,Catalyzes the decarboxylation of CMP-N-acetylneuraminic acid (CMP-Neu5Ac) to form 2-keto-3-deoxy-D-manno-octulosonic acid (KDO). Belongs to the KdsC family,No,No,No,No,No,not-Yes,GO:0050462,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.2742,0.2742,0.2742,0.2742,0.2742,5,0.2742,0.3042,no
NEUAS_CAMJ8,P0DY06,ProtTale,Bacteria,346,Transferase involved in the biosynthesis of capsular polysaccharides. Catalyzes the condensation of N- acetyl-D-mannosamine (ManNAc) and phosphoenolpyruvate to generate N- acetylneuraminate (Neu5Ac).,Catalyzes the condensation of phosphoenolpyruvate (PEP) and N-acetylmannosamine 6-phosphate (ManNAc-6-P) to synthesize N- acetylneuraminate-9-phosphate (Neu5Ac-9-P).,Yes,Yes,Maybe,Maybe,Yes,Yes,GO:0050462,GO:0008747,GO:0050462,GO:0008747,GO:0050462,GO:0008747,0.2353,1.0,0.2353,1.0,0.2353,5,0.5412,0.3042,no
NEUAS_CAMJ8,P0DY06,Protein2Text,Bacteria,346,Transferase involved in the biosynthesis of capsular polysaccharides. Catalyzes the condensation of N- acetyl-D-mannosamine (ManNAc) and phosphoenolpyruvate to generate N- acetylneuraminate (Neu5Ac).,"This protein is involved in catalyzing a reaction, specifically the conversion of one compound to another. The molecular function of this protein is to catalyze a reaction, which is likely a part of a larger metabolic pathway. 

The specific reaction catalyzed by this protein is the formation of a specific compound from a precursor molecule. The reaction is likely to be a stereospecific reaction, meaning that the protein only catalyzes the formation of one stereoisomer of the product.

The protein is likely to be a lyase, which is a type of enzyme that catalyzes the cleavage of a chemical bond, resulting in the formation of a double bond or a ring structure. Lyases are typically involved in the breakdown of complex molecules into simpler ones, and are often found in metabolic pathways that involve the degradation of carbohydrates, amino acids, or other biomolecules.

Overall, the molecular function of this protein is to catalyze a specific reaction that is part of a larger metabolic pathway, and is likely to be involved in the breakdown or synthesis of biomolecules.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0050462,,,,,,,,,,,0,,0.3042,no
NEUAS_CAMJ8,P0DY06,Reference,Bacteria,346,Transferase involved in the biosynthesis of capsular polysaccharides. Catalyzes the condensation of N- acetyl-D-mannosamine (ManNAc) and phosphoenolpyruvate to generate N- acetylneuraminate (Neu5Ac).,Transferase involved in the biosynthesis of capsular polysaccharides. Catalyzes the condensation of N- acetyl-D-mannosamine (ManNAc) and phosphoenolpyruvate to generate N- acetylneuraminate (Neu5Ac).,,,,,,,GO:0050462,GO:0050462,GO:0004425,GO:0008747,GO:0050462,GO:0008747,1.0,0.2353,0.2353,1.0,0.2353,5,0.5412,0.3042,no
NEUAC_CAMJ8,P0DY07,ESM2Text,Bacteria,394,Nucleotidyltransferase involved in the biosynthesis of capsular polysaccharides. Catalyzes the condensation of N-acetylneuraminate (Neu5Ac) and CTP to form CMP-N-acetyl- neuraminate (CMP-Neu5Ac).,Activates KDO (a required 8-carbon sugar) by forming an intramolecular phosphoanhydride bond.,No,Maybe,No,No,No,not-Yes,GO:0008781,,GO:0016301,,GO:0003824,,,0.5296,,0.4155,,2,0.4725,0.3167,no
NEUAC_CAMJ8,P0DY07,Prot2Text,Bacteria,394,Nucleotidyltransferase involved in the biosynthesis of capsular polysaccharides. Catalyzes the condensation of N-acetylneuraminate (Neu5Ac) and CTP to form CMP-N-acetyl- neuraminate (CMP-Neu5Ac).,Catalyzes the synthesis of activated sulfate.,No,No,No,No,No,not-Yes,GO:0008781,GO:0004781,GO:0004781,GO:0004781,GO:0004781,GO:0004781,0.4774,0.4774,0.4774,0.4774,0.4774,5,0.4774,0.3167,no
NEUAC_CAMJ8,P0DY07,ProtT3,Bacteria,394,Nucleotidyltransferase involved in the biosynthesis of capsular polysaccharides. Catalyzes the condensation of N-acetylneuraminate (Neu5Ac) and CTP to form CMP-N-acetyl- neuraminate (CMP-Neu5Ac).,Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the conversion of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N- acetylmannosamine (UDP-ManNAc). In the C-terminal section; belongs to the APS kinase family. In the N-terminal section; belongs to the UDP-N-acetylglucosamine 2-epimerase family,No,No,No,No,No,not-Yes,GO:0008781,GO:0008761,GO:0008761,GO:0003978,GO:0008761,GO:0008761,0.1737,0.1737,0.1737,0.1737,0.1737,5,0.1737,0.3167,no
NEUAC_CAMJ8,P0DY07,ProtTale,Bacteria,394,Nucleotidyltransferase involved in the biosynthesis of capsular polysaccharides. Catalyzes the condensation of N-acetylneuraminate (Neu5Ac) and CTP to form CMP-N-acetyl- neuraminate (CMP-Neu5Ac).,"Catalyzes the conversion of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N-acetylglucosamine-6-phosphate (UDP-GlcNAc-6-P), a reaction involved in the activation of UDP-N-acetylglucosamine (UDP-GlcNAc) and in the conversion of UDP-N-acetylglucosamine-6-P to UDP-N-acetylglucosamine.",No,No,No,No,No,not-Yes,GO:0008781,,GO:0016301,GO:0016301,,,,0.5296,0.5296,,,2,0.5296,0.3167,no
NEUAC_CAMJ8,P0DY07,Protein2Text,Bacteria,394,Nucleotidyltransferase involved in the biosynthesis of capsular polysaccharides. Catalyzes the condensation of N-acetylneuraminate (Neu5Ac) and CTP to form CMP-N-acetyl- neuraminate (CMP-Neu5Ac).,"This protein is involved in a nucleotide cycle, specifically in the synthesis of a nucleotide. 
It is likely involved in the synthesis of a nucleotide, possibly a purine or pyrimidine nucleotide. 
The molecular function of this protein is to catalyze a reaction in the synthesis of a nucleotide, likely a purine or pyrimidine nucleotide. 
It is involved in the synthesis of a nucleotide, possibly a purine or pyrimidine nucleotide. 
The molecular function of this protein is to catalyze a reaction in the synthesis of a nucleotide. 
It is involved in the synthesis of a nucleotide. 
The molecular function of this protein is to catalyze a reaction in the synthesis of a nucleotide. 
It is likely involved in the synthesis of a nucleotide, possibly a purine or pyrimidine nucleotide.",Vague,Vague,Maybe,Vague,Vague,not-Yes,GO:0008781,,,,,,,,,,,0,,0.3167,no
NEUAC_CAMJ8,P0DY07,Reference,Bacteria,394,Nucleotidyltransferase involved in the biosynthesis of capsular polysaccharides. Catalyzes the condensation of N-acetylneuraminate (Neu5Ac) and CTP to form CMP-N-acetyl- neuraminate (CMP-Neu5Ac).,Nucleotidyltransferase involved in the biosynthesis of capsular polysaccharides. Catalyzes the condensation of N-acetylneuraminate (Neu5Ac) and CTP to form CMP-N-acetyl- neuraminate (CMP-Neu5Ac).,,,,,,,GO:0008781,GO:0016779,GO:0070567,GO:0016779,GO:0016779,GO:0008781,0.7539,0.8691,0.7539,0.7539,1.0,5,0.8262,0.3167,no
MFMH_ANNMO,P0DY23,ESM2Text,Eukaryota,242,"Terpene cyclase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O-desmethylfendlerol. Within the pathway, mfmH catalyzes the last step and cyclizes the prenyl unit of 5-O-farnesylcyclopolic acid into a drimane- like structure to yield 11'-O-desmethylfendlerol. The biosynthesis of 11'-O-desmethylfendlerol begins with the NR-PKS mfmB that forms 3,5-dimethylorsellinic acid (DMOA), which is then transformed into the phthalide 5,7-dihydroxy-4-(hydroxymethyl)-6- methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O- methylation to yield 5-hydroxy-4-(hydroxymethyl)-7-methoxy-6- methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy- 4-(hydroxymethyl)-7-methoxy-6-methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5-O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.","Terpene cyclase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems. The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the terpene cyclase ptmB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase ptmQ. Paxilline is converted to beta-pax",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016829,GO:0010333,GO:0016872,GO:0010333,,GO:0016829,0.6019,0.4807,0.6019,,1.0,4,0.6711,0.2664,no
MFMH_ANNMO,P0DY23,Prot2Text,Eukaryota,242,"Terpene cyclase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O-desmethylfendlerol. Within the pathway, mfmH catalyzes the last step and cyclizes the prenyl unit of 5-O-farnesylcyclopolic acid into a drimane- like structure to yield 11'-O-desmethylfendlerol. The biosynthesis of 11'-O-desmethylfendlerol begins with the NR-PKS mfmB that forms 3,5-dimethylorsellinic acid (DMOA), which is then transformed into the phthalide 5,7-dihydroxy-4-(hydroxymethyl)-6- methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O- methylation to yield 5-hydroxy-4-(hydroxymethyl)-7-methoxy-6- methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy- 4-(hydroxymethyl)-7-methoxy-6-methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5-O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.","Lyase; part of the gene cluster that mediates the biosynthesis of the glycolipid biosurfactant ustilagic acid (UA). UA is a secreted cellobiose glycolipid that is toxic for many microorganisms and confers biocontrol activity to U.maydis. UA consists of 15,16-dihydroxypalmitic or 2,15,16-trihydroxypalmitic acid, which is O-glycosidically linked to cellobiose at its terminal hydroxyl group. In addition, the cellobiose moiety is acetylated and acylated with a short-chain hydroxy fatty acid. UA biosynthesis starts with omega-hydroxylation of palmitic acid catalyzed by the cytochrome P450 monooxygenase cyp1. Terminal hydroxylation of palmitic acid precedes subterminal hydroxylation catalyzed by the cytochrome P450 monooxygenase cyp2. Sequential glucosylation of the hydroxy fatty acid is probably catalyzed by the glycosyltransferase ugt1 (Probable). The cellobiose lipid is then converted to the glycol",No,No,No,No,No,not-Yes,GO:0016829,GO:0016829,,GO:0016829,GO:0016829,GO:0016829,1.0,,1.0,1.0,1.0,4,1.0,0.2664,no
MFMH_ANNMO,P0DY23,ProtT3,Eukaryota,242,"Terpene cyclase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O-desmethylfendlerol. Within the pathway, mfmH catalyzes the last step and cyclizes the prenyl unit of 5-O-farnesylcyclopolic acid into a drimane- like structure to yield 11'-O-desmethylfendlerol. The biosynthesis of 11'-O-desmethylfendlerol begins with the NR-PKS mfmB that forms 3,5-dimethylorsellinic acid (DMOA), which is then transformed into the phthalide 5,7-dihydroxy-4-(hydroxymethyl)-6- methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O- methylation to yield 5-hydroxy-4-(hydroxymethyl)-7-methoxy-6- methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy- 4-(hydroxymethyl)-7-methoxy-6-methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5-O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.","Terpene cyclase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS). SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms (By similarity). The polyketide synthase (PKS)",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016829,GO:0016872,GO:0010333,GO:0010334,GO:0010333,GO:0010333,0.4807,0.6019,0.5381,0.6019,0.6019,5,0.5649,0.2664,no
MFMH_ANNMO,P0DY23,ProtTale,Eukaryota,242,"Terpene cyclase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O-desmethylfendlerol. Within the pathway, mfmH catalyzes the last step and cyclizes the prenyl unit of 5-O-farnesylcyclopolic acid into a drimane- like structure to yield 11'-O-desmethylfendlerol. The biosynthesis of 11'-O-desmethylfendlerol begins with the NR-PKS mfmB that forms 3,5-dimethylorsellinic acid (DMOA), which is then transformed into the phthalide 5,7-dihydroxy-4-(hydroxymethyl)-6- methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O- methylation to yield 5-hydroxy-4-(hydroxymethyl)-7-methoxy-6- methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy- 4-(hydroxymethyl)-7-methoxy-6-methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5-O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.","Terpene cyclase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids. The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids. The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an oxidative",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016829,GO:0010333,GO:0016829,GO:0010333,GO:0016829,GO:0010333,0.6019,1.0,0.6019,1.0,0.6019,5,0.7611,0.2664,no
MFMH_ANNMO,P0DY23,Protein2Text,Eukaryota,242,"Terpene cyclase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O-desmethylfendlerol. Within the pathway, mfmH catalyzes the last step and cyclizes the prenyl unit of 5-O-farnesylcyclopolic acid into a drimane- like structure to yield 11'-O-desmethylfendlerol. The biosynthesis of 11'-O-desmethylfendlerol begins with the NR-PKS mfmB that forms 3,5-dimethylorsellinic acid (DMOA), which is then transformed into the phthalide 5,7-dihydroxy-4-(hydroxymethyl)-6- methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O- methylation to yield 5-hydroxy-4-(hydroxymethyl)-7-methoxy-6- methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy- 4-(hydroxymethyl)-7-methoxy-6-methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5-O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.",The molecular function of this protein is as a magnesium transporter.,No,No,No,No,No,not-Yes,GO:0016829,GO:0015095,GO:0015095,GO:0015095,GO:0015095,GO:0015095,0.1411,0.1411,0.1411,0.1411,0.1411,5,0.1411,0.2664,no
MFMH_ANNMO,P0DY23,Reference,Eukaryota,242,"Terpene cyclase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O-desmethylfendlerol. Within the pathway, mfmH catalyzes the last step and cyclizes the prenyl unit of 5-O-farnesylcyclopolic acid into a drimane- like structure to yield 11'-O-desmethylfendlerol. The biosynthesis of 11'-O-desmethylfendlerol begins with the NR-PKS mfmB that forms 3,5-dimethylorsellinic acid (DMOA), which is then transformed into the phthalide 5,7-dihydroxy-4-(hydroxymethyl)-6- methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O- methylation to yield 5-hydroxy-4-(hydroxymethyl)-7-methoxy-6- methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy- 4-(hydroxymethyl)-7-methoxy-6-methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5-O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.","Terpene cyclase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O-desmethylfendlerol. Within the pathway, mfmH catalyzes the last step and cyclizes the prenyl unit of 5-O-farnesylcyclopolic acid into a drimane- like structure to yield 11'-O-desmethylfendlerol. The biosynthesis of 11'-O-desmethylfendlerol begins with the NR-PKS mfmB that forms 3,5-dimethylorsellinic acid (DMOA), which is then transformed into the phthalide 5,7-dihydroxy-4-(hydroxymethyl)-6- methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O- methylation to yield 5-hydroxy-4-(hydroxymethyl)-7-methoxy-6- methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy- 4-(hydroxymethyl)-7-methoxy-6-methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5-O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.",,,,,,,GO:0016829,GO:0016829,GO:0016829,GO:0010333,GO:0016829,GO:0010333,1.0,1.0,0.6019,1.0,0.6019,5,0.8408,0.2664,no
MFMD_ANNMO,P9WEG3,ESM2Text,Eukaryota,442,"Prenyltransferase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O-desmethylfendlerol. Within the pathway, mfmD is responsible for farnesylation of the cyclopolic acid intermediate via an O-prenylation reaction. The biosynthesis of 11'-O- desmethylfendlerol begins with the NR-PKS mfmB that forms 3,5- dimethylorsellinic acid (DMOA), which is then transformed into the phthalide 5,7-dihydroxy-4-(hydroxymethyl)-6-methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O-methylation to yield 5-hydroxy-4-(hydroxymethyl)-7-methoxy-6-methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy-4-(hydroxymethyl)-7- methoxy-6-methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5- O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.","Oxygenase; part of the gene cluster that mediates the biosynthesis of the bianthraquinone cladofulvin, a conidial pigment not required for virulence but that plays a role in fitness and resistance to environmental stresses including UV light and low-temperature stress. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) claG. The atrochrysone carboxyl ACP thioesterase claF then breaks the thioester bond and releases the atrochrysone carboxylic acid from claG. This compound is decarboxylated by claH to yield emodin, which is further converted to chrysophanol hydroquinone by the reductase claC and the dehydratase claB. The cytochrome monooxygenase P450 claM then catalyzes the dimerization of nataloe-emodin to cladofulvin.",No,No,No,No,No,not-Yes,GO:0016765,GO:0016701,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.3902,0.4807,0.4807,0.4807,0.4807,5,0.4626,0.4343,no
MFMD_ANNMO,P9WEG3,Prot2Text,Eukaryota,442,"Prenyltransferase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O-desmethylfendlerol. Within the pathway, mfmD is responsible for farnesylation of the cyclopolic acid intermediate via an O-prenylation reaction. The biosynthesis of 11'-O- desmethylfendlerol begins with the NR-PKS mfmB that forms 3,5- dimethylorsellinic acid (DMOA), which is then transformed into the phthalide 5,7-dihydroxy-4-(hydroxymethyl)-6-methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O-methylation to yield 5-hydroxy-4-(hydroxymethyl)-7-methoxy-6-methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy-4-(hydroxymethyl)-7- methoxy-6-methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5- O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.",Heme-containing dioxygenase involved in the assimilation of hydrogen peroxide. Catalyzes the peroxide-dependent hydroxylation of nicotinate to 6-hydroxynicotinate. The initial oxygenase activity of this enzyme is required for the generation of the quinone generation by the Pks13/Pks1 heterodimer that catalyzes formation of 6-hydroxynicotinate from norrhamnose.,No,No,No,No,No,not-Yes,GO:0016765,GO:0051213,,GO:0051213,GO:0051213,GO:0051213,0.3902,,0.3902,0.3902,0.3902,4,0.3902,0.4343,no
MFMD_ANNMO,P9WEG3,ProtT3,Eukaryota,442,"Prenyltransferase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O-desmethylfendlerol. Within the pathway, mfmD is responsible for farnesylation of the cyclopolic acid intermediate via an O-prenylation reaction. The biosynthesis of 11'-O- desmethylfendlerol begins with the NR-PKS mfmB that forms 3,5- dimethylorsellinic acid (DMOA), which is then transformed into the phthalide 5,7-dihydroxy-4-(hydroxymethyl)-6-methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O-methylation to yield 5-hydroxy-4-(hydroxymethyl)-7-methoxy-6-methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy-4-(hydroxymethyl)-7- methoxy-6-methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5- O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.","Prenyltransferase; part of the gene cluster that mediates the biosynthesis of calidodehydroaustin, a fungal meroterpenoid . The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (By similarity). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (By similarity). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the terpene",Yes,Yes,Yes,Yes,Yes,Yes,GO:0016765,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,0.8416,0.8416,0.8416,0.8416,0.8416,5,0.8416,0.4343,no
MFMD_ANNMO,P9WEG3,ProtTale,Eukaryota,442,"Prenyltransferase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O-desmethylfendlerol. Within the pathway, mfmD is responsible for farnesylation of the cyclopolic acid intermediate via an O-prenylation reaction. The biosynthesis of 11'-O- desmethylfendlerol begins with the NR-PKS mfmB that forms 3,5- dimethylorsellinic acid (DMOA), which is then transformed into the phthalide 5,7-dihydroxy-4-(hydroxymethyl)-6-methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O-methylation to yield 5-hydroxy-4-(hydroxymethyl)-7-methoxy-6-methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy-4-(hydroxymethyl)-7- methoxy-6-methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5- O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.","Prenyltransferase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS). SQS1 is composed of a 2,8- dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic acid core that is connected to two lipophilic polyketide arms. These initial steps feature the priming of an unusual benzoic acid starter unit onto the highly",Yes,Yes,Maybe,Yes,Yes,Yes,GO:0016765,GO:0004659,GO:0016765,GO:0004659,GO:0004659,GO:0004659,0.8416,1.0,0.8416,0.8416,0.8416,5,0.8733,0.4343,no
MFMD_ANNMO,P9WEG3,Protein2Text,Eukaryota,442,"Prenyltransferase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O-desmethylfendlerol. Within the pathway, mfmD is responsible for farnesylation of the cyclopolic acid intermediate via an O-prenylation reaction. The biosynthesis of 11'-O- desmethylfendlerol begins with the NR-PKS mfmB that forms 3,5- dimethylorsellinic acid (DMOA), which is then transformed into the phthalide 5,7-dihydroxy-4-(hydroxymethyl)-6-methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O-methylation to yield 5-hydroxy-4-(hydroxymethyl)-7-methoxy-6-methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy-4-(hydroxymethyl)-7- methoxy-6-methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5- O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.","The molecular function of this protein is not explicitly stated in the provided text. However, based on the context, it can be inferred that this protein is involved in the synthesis of indole alkaloids, as it is being studied in relation to the production of these compounds. Specifically, it is being used to produce the precursor of the indole alkaloid ajmalicine.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0016765,,,,,,,,,,,0,,0.4343,no
MFMD_ANNMO,P9WEG3,Reference,Eukaryota,442,"Prenyltransferase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O-desmethylfendlerol. Within the pathway, mfmD is responsible for farnesylation of the cyclopolic acid intermediate via an O-prenylation reaction. The biosynthesis of 11'-O- desmethylfendlerol begins with the NR-PKS mfmB that forms 3,5- dimethylorsellinic acid (DMOA), which is then transformed into the phthalide 5,7-dihydroxy-4-(hydroxymethyl)-6-methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O-methylation to yield 5-hydroxy-4-(hydroxymethyl)-7-methoxy-6-methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy-4-(hydroxymethyl)-7- methoxy-6-methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5- O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.","Prenyltransferase; part of the gene cluster that mediates the biosynthesis of the phthalide-terpenoid hybrid 11'-O-desmethylfendlerol. Within the pathway, mfmD is responsible for farnesylation of the cyclopolic acid intermediate via an O-prenylation reaction. The biosynthesis of 11'-O- desmethylfendlerol begins with the NR-PKS mfmB that forms 3,5- dimethylorsellinic acid (DMOA), which is then transformed into the phthalide 5,7-dihydroxy-4-(hydroxymethyl)-6-methylphthalide by the cytochrome P450 monooxygenase mfmA and the hydrolase mfmC. Subsequently, the methyltransferase mfmE catalyzes 7-O-methylation to yield 5-hydroxy-4-(hydroxymethyl)-7-methoxy-6-methylphthalide, which undergoes C-3 hydroxylation by the cytochrome P450 monooxygenase mfmF. The resultant cyclopolic acid (2,5-dihydroxy-4-(hydroxymethyl)-7- methoxy-6-methylphthalide) is then farnesylated by the DMATS-type prenyltransferase mfmD to afford 5-O-farnesylcyclopolic acid. Finally, the Pyr4-family terpene cyclase mfmH cyclizes the farnesyl moiety of 5- O-farnesylcyclopolic acid into a drimane-like structure, thus completing the biosynthesis of 11'-O-desmethylfendlerol.",,,,,,,GO:0016765,GO:0004659,GO:0004659,GO:0004659,GO:0004659,GO:0004659,0.8416,0.8416,0.8416,0.8416,0.8416,5,0.8416,0.4343,no
LTBB_ASPLT,P9WEH5,ESM2Text,Eukaryota,409,"NDP-glycosyltransferase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. LtbB likely serves as a glucinol synthase by transferring D-glucose to myo-inositol using NDP-glucose as a substrate. The ltbA carnitine O-acyltransferase (cAT) domain uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A from the HR-PKS. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.","Glycosyltransferase involved in the synthesis of mannose-1-phosphate, a major component of the surface membrane of the erythrocyte membrane. Mannose-1-phosphate is the precursor of GDP-mannose (GDP-Man) which is found in cell wall components of both extracellular matrices and the cortical actin cytoskeleton.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,1.0,1.0,1.0,1.0,1.0,5,1.0,0.402,no
LTBB_ASPLT,P9WEH5,Prot2Text,Eukaryota,409,"NDP-glycosyltransferase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. LtbB likely serves as a glucinol synthase by transferring D-glucose to myo-inositol using NDP-glucose as a substrate. The ltbA carnitine O-acyltransferase (cAT) domain uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A from the HR-PKS. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.","Glycosyltransferase involved in the maintenance of the outermost surface of the fungal cell wall. Likely functions in the synthesis of a currently unknown, potentially minor but widespread, extracellular or outer cell wall polysaccharide which plays a key role in facilitating many interactions between plants and fungi by enabling hyphal growth on solid matrices.",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,1.0,1.0,1.0,1.0,1.0,5,1.0,0.402,no
LTBB_ASPLT,P9WEH5,ProtT3,Eukaryota,409,"NDP-glycosyltransferase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. LtbB likely serves as a glucinol synthase by transferring D-glucose to myo-inositol using NDP-glucose as a substrate. The ltbA carnitine O-acyltransferase (cAT) domain uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A from the HR-PKS. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.",Probable glycosyltransferase involved in the biosynthesis of the rhamnogalacturonan I (RG-I) backbone of pectin. Cell membrane; Multi-pass membrane protein. Belongs to the glycosyltransferase 2 family,Maybe,Maybe,Vague,Maybe,Maybe,not-Yes,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,1.0,1.0,1.0,1.0,1.0,5,1.0,0.402,no
LTBB_ASPLT,P9WEH5,ProtTale,Eukaryota,409,"NDP-glycosyltransferase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. LtbB likely serves as a glucinol synthase by transferring D-glucose to myo-inositol using NDP-glucose as a substrate. The ltbA carnitine O-acyltransferase (cAT) domain uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A from the HR-PKS. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.","Probable beta-1,4-glucan synthase that catalyzes the synthesis of a linear chain of beta-1,4-linked glucans through time.",Vague,Vague,No,Vague,Vague,not-Yes,GO:0016757,GO:0016760,GO:0016760,GO:0016757,GO:0016760,GO:0016760,0.504,0.504,1.0,0.504,0.504,5,0.6032,0.402,no
LTBB_ASPLT,P9WEH5,Protein2Text,Eukaryota,409,"NDP-glycosyltransferase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. LtbB likely serves as a glucinol synthase by transferring D-glucose to myo-inositol using NDP-glucose as a substrate. The ltbA carnitine O-acyltransferase (cAT) domain uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A from the HR-PKS. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.","The molecular function of this protein is not specified in the provided information. However, based on its name, it is likely involved in acetyltransferase activity, specifically in the acetylation of fatty acids.",Vague,No,Vague,No,No,not-Yes,GO:0016757,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.482,0.482,0.482,0.482,0.482,5,0.482,0.402,no
LTBB_ASPLT,P9WEH5,Reference,Eukaryota,409,"NDP-glycosyltransferase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. LtbB likely serves as a glucinol synthase by transferring D-glucose to myo-inositol using NDP-glucose as a substrate. The ltbA carnitine O-acyltransferase (cAT) domain uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A from the HR-PKS. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.","NDP-glycosyltransferase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. LtbB likely serves as a glucinol synthase by transferring D-glucose to myo-inositol using NDP-glucose as a substrate. The ltbA carnitine O-acyltransferase (cAT) domain uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A from the HR-PKS. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.",,,,,,,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,1.0,1.0,1.0,1.0,1.0,5,1.0,0.402,no
LTBC_ASPLT,P9WEH7,ESM2Text,Eukaryota,285,"Probable methyltransferase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. The HR-PKS ltbA produces the trimethylated polyketide chain from acetyl-CoA, malonyl-CoA and S-adenosylmethionine (SAM), and the ltbA cAT domain then uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.",Probable methyltransferase.,Vague,Vague,Maybe,Yes,Maybe,not-Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1596,no
LTBC_ASPLT,P9WEH7,Prot2Text,Eukaryota,285,"Probable methyltransferase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. The HR-PKS ltbA produces the trimethylated polyketide chain from acetyl-CoA, malonyl-CoA and S-adenosylmethionine (SAM), and the ltbA cAT domain then uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.","O-methyltransferase that catalyzes the conversion of demethylmacrocin to macrocin, the penultimate step of tylosin antibiotic biosynthesis. Also able to mediate the conversion of demethyllactenocin to lactenocin.",Maybe,Yes,Maybe,Yes,Yes,Yes,GO:0008168,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.1596,no
LTBC_ASPLT,P9WEH7,ProtT3,Eukaryota,285,"Probable methyltransferase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. The HR-PKS ltbA produces the trimethylated polyketide chain from acetyl-CoA, malonyl-CoA and S-adenosylmethionine (SAM), and the ltbA cAT domain then uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.",S-adenosyl-L-methionine-dependent methyltransferase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms,Maybe,Yes,Maybe,Yes,Yes,Yes,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1596,no
LTBC_ASPLT,P9WEH7,ProtTale,Eukaryota,285,"Probable methyltransferase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. The HR-PKS ltbA produces the trimethylated polyketide chain from acetyl-CoA, malonyl-CoA and S-adenosylmethionine (SAM), and the ltbA cAT domain then uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.","Probable O-methyltransferase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the saturated C-",Maybe,Yes,Maybe,Yes,Yes,Yes,GO:0008168,GO:0008171,GO:0008171,GO:0008171,GO:0008171,GO:0008171,0.8582,0.8582,0.8582,0.8582,0.8582,5,0.8582,0.1596,no
LTBC_ASPLT,P9WEH7,Protein2Text,Eukaryota,285,"Probable methyltransferase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. The HR-PKS ltbA produces the trimethylated polyketide chain from acetyl-CoA, malonyl-CoA and S-adenosylmethionine (SAM), and the ltbA cAT domain then uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.","The molecular function of this protein is not specified in the provided information. However, based on its name, it can be inferred that it is involved in the transfer of a phosphate group from one molecule to another, likely as part of a metabolic pathway. More specific information about its molecular function would be needed to confirm this. 

In general, proteins that are part of the ""alkyl/aryl phosphate"" family are involved in the transfer of phosphate groups in various biochemical reactions, often as part of metabolic pathways. They can act as enzymes that catalyze the transfer of phosphate groups, or as regulatory proteins that control the activity of enzymes by binding to them and altering their ability to transfer phosphate groups. 

Without more specific information, it is difficult to determine the exact molecular function of this protein. However, it is likely involved in some aspect of phosphate transfer or regulation in a cellular pathway. 

If you have any more information or context about this protein, I may be able to provide a more specific answer.",No,No,Vague,No,No,not-Yes,GO:0008168,,,,,,,,,,,0,,0.1596,no
LTBC_ASPLT,P9WEH7,Reference,Eukaryota,285,"Probable methyltransferase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. The HR-PKS ltbA produces the trimethylated polyketide chain from acetyl-CoA, malonyl-CoA and S-adenosylmethionine (SAM), and the ltbA cAT domain then uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.","Probable methyltransferase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. The HR-PKS ltbA produces the trimethylated polyketide chain from acetyl-CoA, malonyl-CoA and S-adenosylmethionine (SAM), and the ltbA cAT domain then uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.",,,,,,,GO:0008168,,,GO:0008168,,GO:0008168,,,1.0,,1.0,2,1.0,0.1596,no
LTBD_ASPLT,P9WEH8,ESM2Text,Eukaryota,486,"Probable FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. The HR-PKS ltbA produces the trimethylated polyketide chain from acetyl-CoA, malonyl-CoA and S-adenosylmethionine (SAM), and the ltbA cAT domain then uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.",Aids in the defense against invading fungal pathogens by degrading their cell wall chitosan.,No,No,No,No,No,not-Yes,GO:0004497,GO:0016787,GO:0004553,GO:0016798,GO:0016998,GO:0004553,0.4807,0.3284,0.3902,0.0,0.3284,5,0.3055,0.2118,no
LTBD_ASPLT,P9WEH8,Prot2Text,Eukaryota,486,"Probable FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. The HR-PKS ltbA produces the trimethylated polyketide chain from acetyl-CoA, malonyl-CoA and S-adenosylmethionine (SAM), and the ltbA cAT domain then uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.",Plays a role in sporulation.,No,No,No,No,No,not-Yes,GO:0004497,,,,,,,,,,,0,,0.2118,no
LTBD_ASPLT,P9WEH8,ProtT3,Eukaryota,486,"Probable FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. The HR-PKS ltbA produces the trimethylated polyketide chain from acetyl-CoA, malonyl-CoA and S-adenosylmethionine (SAM), and the ltbA cAT domain then uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.",Probable ATPase. Mitochondrion. Belongs to the IIV-6 359L family,Vague,No,No,No,No,not-Yes,GO:0004497,GO:0016887,GO:0016887,GO:0016887,GO:0016887,GO:0016887,0.2373,0.2373,0.2373,0.2373,0.2373,5,0.2373,0.2118,no
LTBD_ASPLT,P9WEH8,ProtTale,Eukaryota,486,"Probable FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. The HR-PKS ltbA produces the trimethylated polyketide chain from acetyl-CoA, malonyl-CoA and S-adenosylmethionine (SAM), and the ltbA cAT domain then uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.","Pore-forming toxin that causes cytolysis by forming pores in membranes of target cells. Forms pores of 3.5 nm in diameter on lipid bilayers. Has a high affinity for sphingomyelin (Sph) and phosphatidylethanolamine (PE), and a low affinity for phosphatidylcholine (PC) and phosphatidylserine (PS).",No,No,No,No,No,not-Yes,GO:0004497,,GO:0090729,,GO:0090729,GO:0090729,,0.2761,,0.2761,0.2761,3,0.2761,0.2118,no
LTBD_ASPLT,P9WEH8,Protein2Text,Eukaryota,486,"Probable FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. The HR-PKS ltbA produces the trimethylated polyketide chain from acetyl-CoA, malonyl-CoA and S-adenosylmethionine (SAM), and the ltbA cAT domain then uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.","This protein is a molecular function of the viral glycoprotein that mediates the fusion of viral and cellular membranes leading to virus entry into the host cell. The glycoprotein is composed of two subunits, a small peplomer and a large peplomer, and is responsible for the attachment of the virus to the host cell receptor and subsequent fusion of the viral envelope with the host cell membrane. The glycoprotein is also responsible for the fusion of viral particles with host cells during virus budding. The glycoprotein is composed of two subunits, a small peplomer (SU) and a large peplomer (G), and is responsible for the attachment of the virus to the host cell receptor and subsequent fusion of the viral envelope with the host cell membrane. The glycoprotein is also responsible for the fusion of viral particles with host cells during virus budding. The glycoprotein is composed of two subunits, a small peplomer (SU) and a large peplomer (G), and is responsible for the attachment of the virus to the host cell receptor and subsequent fusion of the viral envelope with the host cell membrane. The glycoprotein is also responsible for the fusion of viral particles with host cells during virus budding.",No,No,No,No,No,not-Yes,GO:0004497,,,,,,,,,,,0,,0.2118,no
LTBD_ASPLT,P9WEH8,Reference,Eukaryota,486,"Probable FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. The HR-PKS ltbA produces the trimethylated polyketide chain from acetyl-CoA, malonyl-CoA and S-adenosylmethionine (SAM), and the ltbA cAT domain then uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.","Probable FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of luteodienoside A, a glycosylated polyketide consisting of an unusual 1-O-beta-D-glucopyranosyl-myo- inositol (glucinol) ester of 3-hydroxy-2,2,4-trimethylocta-4,6-dienoic acid. The HR-PKS ltbA produces the trimethylated polyketide chain from acetyl-CoA, malonyl-CoA and S-adenosylmethionine (SAM), and the ltbA cAT domain then uses glucinol produced by the glycosyltransferase ltbB as an offloading substrate to release luteodienoside A. Since ltbA and ltbB are sufficient for the biosynthesis of luteodienoside A, the functions of the methyltransferase ltbC and the FAD-binding monooxygenase ltbD within the pathway remain obscur.",,,,,,,GO:0004497,,,,,GO:0004497,,,,,1.0,1,1.0,0.2118,no
AMAA_APIMO,P9WEK1,ESM2Text,Eukaryota,549,"Arginine-containing cyclodipeptide synthase; part of the cluster that mediates the biosynthesis of a highly modified cyclo- arginine-proline dipeptide (cRP). Within the pathway, amaA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Pro diketopiperazine (cRW) from L-arginyl- tRNA(Arg) + L-prolyl-tRNA(Pro). Additional enzymes from the cluster then further modify the cyclo-Arg-Pro diketopiperazine (cRW) scaffold (Probable).","Bifunctional enzyme involved in both the synthesis of pyruvate and of (4S)-benzoate. Catalyzes the sequential condensation of tyrosine with the intermediate 4-aminobenzoate, generating the pro-4S intermediate (4S)-benzoate. Inactive with (4S)-benzoyl-CoA and (4S)-aminobenzoate.",No,No,No,No,No,not-Yes,GO:0016874,,GO:0016874,,,,,1.0,,,,1,1.0,0.3919,no
AMAA_APIMO,P9WEK1,Prot2Text,Eukaryota,549,"Arginine-containing cyclodipeptide synthase; part of the cluster that mediates the biosynthesis of a highly modified cyclo- arginine-proline dipeptide (cRP). Within the pathway, amaA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Pro diketopiperazine (cRW) from L-arginyl- tRNA(Arg) + L-prolyl-tRNA(Pro). Additional enzymes from the cluster then further modify the cyclo-Arg-Pro diketopiperazine (cRW) scaffold (Probable).","Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate).",No,No,No,No,No,not-Yes,GO:0016874,GO:0016301,GO:0016301,GO:0035299,GO:0035299,GO:0016301,0.4071,0.4071,0.2691,0.2691,0.4071,5,0.3519,0.3919,no
AMAA_APIMO,P9WEK1,ProtT3,Eukaryota,549,"Arginine-containing cyclodipeptide synthase; part of the cluster that mediates the biosynthesis of a highly modified cyclo- arginine-proline dipeptide (cRP). Within the pathway, amaA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Pro diketopiperazine (cRW) from L-arginyl- tRNA(Arg) + L-prolyl-tRNA(Pro). Additional enzymes from the cluster then further modify the cyclo-Arg-Pro diketopiperazine (cRW) scaffold (Probable).",Indole-3-glycerol phosphate synthase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3,No,No,No,No,No,not-Yes,GO:0016874,GO:0004425,GO:0004425,GO:0004425,GO:0004425,GO:0004425,0.3552,0.3552,0.3552,0.3552,0.3552,5,0.3552,0.3919,no
AMAA_APIMO,P9WEK1,ProtTale,Eukaryota,549,"Arginine-containing cyclodipeptide synthase; part of the cluster that mediates the biosynthesis of a highly modified cyclo- arginine-proline dipeptide (cRP). Within the pathway, amaA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Pro diketopiperazine (cRW) from L-arginyl- tRNA(Arg) + L-prolyl-tRNA(Pro). Additional enzymes from the cluster then further modify the cyclo-Arg-Pro diketopiperazine (cRW) scaffold (Probable).","Capsid vertex-specific component that plays a role during viral DNA encapsidation, assuring correct genome cleavage and presumably stabilizing capsids that contain full-length viral genomes. Participates in the interaction between the capsid and the tegument through interaction with the large tegument protein/LTP.",No,No,No,No,No,not-Yes,GO:0016874,,,,,,,,,,,0,,0.3919,no
AMAA_APIMO,P9WEK1,Protein2Text,Eukaryota,549,"Arginine-containing cyclodipeptide synthase; part of the cluster that mediates the biosynthesis of a highly modified cyclo- arginine-proline dipeptide (cRP). Within the pathway, amaA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Pro diketopiperazine (cRW) from L-arginyl- tRNA(Arg) + L-prolyl-tRNA(Pro). Additional enzymes from the cluster then further modify the cyclo-Arg-Pro diketopiperazine (cRW) scaffold (Probable).",This protein is involved in molecular function as a putative serine/threonine-protein kinase.,No,No,No,No,No,not-Yes,GO:0016874,GO:0004674,GO:0004674,GO:0004674,GO:0004674,GO:0004674,0.2951,0.2951,0.2951,0.2951,0.2951,5,0.2951,0.3919,no
AMAA_APIMO,P9WEK1,Reference,Eukaryota,549,"Arginine-containing cyclodipeptide synthase; part of the cluster that mediates the biosynthesis of a highly modified cyclo- arginine-proline dipeptide (cRP). Within the pathway, amaA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Pro diketopiperazine (cRW) from L-arginyl- tRNA(Arg) + L-prolyl-tRNA(Pro). Additional enzymes from the cluster then further modify the cyclo-Arg-Pro diketopiperazine (cRW) scaffold (Probable).","Arginine-containing cyclodipeptide synthase; part of the cluster that mediates the biosynthesis of a highly modified cyclo- arginine-proline dipeptide (cRP). Within the pathway, amaA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Pro diketopiperazine (cRW) from L-arginyl- tRNA(Arg) + L-prolyl-tRNA(Pro). Additional enzymes from the cluster then further modify the cyclo-Arg-Pro diketopiperazine (cRW) scaffold (Probable).",,,,,,,GO:0016874,GO:0016740,GO:0016755,GO:0016740,GO:0016755,GO:0016874,0.5902,0.4071,0.5902,0.4071,1.0,5,0.5989,0.3919,no
ESHA_PENSH,P9WEK2,ESM2Text,Eukaryota,511,"Arginine-containing cyclodipeptide synthase; part of the cluster that mediates the biosynthesis of a highly modified cyclo- arginine-leucine dipeptide (cRW). Within the pathway, eshA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Leu diketopiperazine (cRL) from L-arginyl- tRNA(Arg) + L-Leucyl-tRNA(Leu). Additional enzymes from the cluster then further modify the cyclo-Arg-Leu diketopiperazine (cRW) scaffold (Probable).","DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs.",No,No,No,No,No,not-Yes,GO:0016874,GO:0003899,GO:0003899,GO:0003899,GO:0003899,GO:0003899,0.2657,0.2657,0.2657,0.2657,0.2657,5,0.2657,0.4753,no
ESHA_PENSH,P9WEK2,Prot2Text,Eukaryota,511,"Arginine-containing cyclodipeptide synthase; part of the cluster that mediates the biosynthesis of a highly modified cyclo- arginine-leucine dipeptide (cRW). Within the pathway, eshA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Leu diketopiperazine (cRL) from L-arginyl- tRNA(Arg) + L-Leucyl-tRNA(Leu). Additional enzymes from the cluster then further modify the cyclo-Arg-Leu diketopiperazine (cRW) scaffold (Probable).",IMP-specific 5'-nucleotidase involved in IMP (inositol monophosphate) degradation.,No,No,No,No,No,not-Yes,GO:0016874,GO:0008253,GO:0008441,GO:0008253,GO:0008253,GO:0008253,0.2896,0.2896,0.2896,0.2896,0.2896,5,0.2896,0.4753,no
ESHA_PENSH,P9WEK2,ProtT3,Eukaryota,511,"Arginine-containing cyclodipeptide synthase; part of the cluster that mediates the biosynthesis of a highly modified cyclo- arginine-leucine dipeptide (cRW). Within the pathway, eshA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Leu diketopiperazine (cRL) from L-arginyl- tRNA(Arg) + L-Leucyl-tRNA(Leu). Additional enzymes from the cluster then further modify the cyclo-Arg-Leu diketopiperazine (cRW) scaffold (Probable).","Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication. During replication, encapsidation by N is coupled to RNA synthesis and all replicative products are resistant to nucleases (By similarity). Host cytoplasm. Belongs to the paramyxoviruses nucleocapsid family",No,No,No,No,No,not-Yes,GO:0016874,GO:0003723,GO:0003723,GO:0003723,GO:0003723,,0.2136,0.2136,0.2136,0.2136,,4,0.2136,0.4753,no
ESHA_PENSH,P9WEK2,ProtTale,Eukaryota,511,"Arginine-containing cyclodipeptide synthase; part of the cluster that mediates the biosynthesis of a highly modified cyclo- arginine-leucine dipeptide (cRW). Within the pathway, eshA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Leu diketopiperazine (cRL) from L-arginyl- tRNA(Arg) + L-Leucyl-tRNA(Leu). Additional enzymes from the cluster then further modify the cyclo-Arg-Leu diketopiperazine (cRW) scaffold (Probable).",Component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase synthesizes short RNA primers on the lagging strand that the polymerase presumably elongates using dNTPs. The primase-associated factor has no known catalytic activity in the complex and may serve to facilitate the formation of the replisome by directly interacting with the origin-binding protein and the polymerase.,No,No,No,No,No,not-Yes,GO:0016874,GO:0003678; GO:0003896,GO:0003678; GO:0003896; GO:0005524,GO:0003678; GO:0003896,GO:0003678; GO:0003896; GO:0005524,GO:0003678; GO:0003896; GO:0005524,0.2581,0.2012,0.2581,0.2012,0.2012,5,0.224,0.4753,no
ESHA_PENSH,P9WEK2,Protein2Text,Eukaryota,511,"Arginine-containing cyclodipeptide synthase; part of the cluster that mediates the biosynthesis of a highly modified cyclo- arginine-leucine dipeptide (cRW). Within the pathway, eshA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Leu diketopiperazine (cRL) from L-arginyl- tRNA(Arg) + L-Leucyl-tRNA(Leu). Additional enzymes from the cluster then further modify the cyclo-Arg-Leu diketopiperazine (cRW) scaffold (Probable).","This protein is involved in the molecular function of being a part of the molecular machinery that synthesizes proteins. More specifically, it is a subunit of the RNA-dependent RNA polymerase, which is a complex enzyme that plays a crucial role in viral replication by transcribing viral RNA into protein-coding messenger RNA.",No,No,No,No,No,not-Yes,GO:0016874,GO:0003968,GO:0003968,GO:0003968,GO:0003968,GO:0003968,0.2657,0.2657,0.2657,0.2657,0.2657,5,0.2657,0.4753,no
ESHA_PENSH,P9WEK2,Reference,Eukaryota,511,"Arginine-containing cyclodipeptide synthase; part of the cluster that mediates the biosynthesis of a highly modified cyclo- arginine-leucine dipeptide (cRW). Within the pathway, eshA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Leu diketopiperazine (cRL) from L-arginyl- tRNA(Arg) + L-Leucyl-tRNA(Leu). Additional enzymes from the cluster then further modify the cyclo-Arg-Leu diketopiperazine (cRW) scaffold (Probable).","Arginine-containing cyclodipeptide synthase; part of the cluster that mediates the biosynthesis of a highly modified cyclo- arginine-leucine dipeptide (cRW). Within the pathway, eshA acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Leu diketopiperazine (cRL) from L-arginyl- tRNA(Arg) + L-Leucyl-tRNA(Leu). Additional enzymes from the cluster then further modify the cyclo-Arg-Leu diketopiperazine (cRW) scaffold (Probable).",,,,,,,GO:0016874,GO:0016740,GO:0016755,GO:0016740,GO:0016755,GO:0016874,0.5902,0.4071,0.5902,0.4071,1.0,5,0.5989,0.4753,no
AVAC_ASPVE,P9WEK4,ESM2Text,Eukaryota,284,"Kynurenine formamidase; part of the cluster that mediates the biosynthesis of a highly modified cyclo-arginine-tryptophan dipeptide (cRW). Within the pathway, avaC catalyzes the deformylation of the cyclo-Arg-formylkynurenine iketopiperazine (DKP), produced by the FAD-dependent monooxygenase avaB. The first step of the pathway is perfornmed by the arginine-containing cyclodipeptide synthase (RCPDS) avaA that acts as the scaffold- generating enzyme and is responsible for formation of the cyclo-Arg-Trp (cRW) diketopiperazine. AvaB then acts as a multifunctional flavoenzyme that is responsible for generating the cyclo-Arg-formylkynurenine DKP, which can be deformylated by avaC. AvaB then further catalyzes an additional N-oxidation followed by cyclization and dehydration. The next step is an N-acetylation of the guanidine group catalyzed by the arginine N-acetyltransferase avaD. The roles of the additional enzymes identified within the ava cluster still have to be determined.",Esterase that catalyzes the hydrolysis of short-chain esters with a preference for long-chain fatty acids. Seems to act on octenoic acid.,No,Maybe,No,Maybe,Maybe,not-Yes,GO:0004061,GO:0004091,GO:0004091,GO:0004091,GO:0004091,GO:0004091,0.3987,0.3987,0.3987,0.3987,0.3987,5,0.3987,0.2456,no
AVAC_ASPVE,P9WEK4,Prot2Text,Eukaryota,284,"Kynurenine formamidase; part of the cluster that mediates the biosynthesis of a highly modified cyclo-arginine-tryptophan dipeptide (cRW). Within the pathway, avaC catalyzes the deformylation of the cyclo-Arg-formylkynurenine iketopiperazine (DKP), produced by the FAD-dependent monooxygenase avaB. The first step of the pathway is perfornmed by the arginine-containing cyclodipeptide synthase (RCPDS) avaA that acts as the scaffold- generating enzyme and is responsible for formation of the cyclo-Arg-Trp (cRW) diketopiperazine. AvaB then acts as a multifunctional flavoenzyme that is responsible for generating the cyclo-Arg-formylkynurenine DKP, which can be deformylated by avaC. AvaB then further catalyzes an additional N-oxidation followed by cyclization and dehydration. The next step is an N-acetylation of the guanidine group catalyzed by the arginine N-acetyltransferase avaD. The roles of the additional enzymes identified within the ava cluster still have to be determined.",Overproduction of nonspecific esterases is a common mechanism of resistance to organophosphate insecticides.,No,No,No,No,No,not-Yes,GO:0004061,GO:0004091,GO:0004091,GO:0004091,GO:0004091,GO:0004091,0.3987,0.3987,0.3987,0.3987,0.3987,5,0.3987,0.2456,no
AVAC_ASPVE,P9WEK4,ProtT3,Eukaryota,284,"Kynurenine formamidase; part of the cluster that mediates the biosynthesis of a highly modified cyclo-arginine-tryptophan dipeptide (cRW). Within the pathway, avaC catalyzes the deformylation of the cyclo-Arg-formylkynurenine iketopiperazine (DKP), produced by the FAD-dependent monooxygenase avaB. The first step of the pathway is perfornmed by the arginine-containing cyclodipeptide synthase (RCPDS) avaA that acts as the scaffold- generating enzyme and is responsible for formation of the cyclo-Arg-Trp (cRW) diketopiperazine. AvaB then acts as a multifunctional flavoenzyme that is responsible for generating the cyclo-Arg-formylkynurenine DKP, which can be deformylated by avaC. AvaB then further catalyzes an additional N-oxidation followed by cyclization and dehydration. The next step is an N-acetylation of the guanidine group catalyzed by the arginine N-acetyltransferase avaD. The roles of the additional enzymes identified within the ava cluster still have to be determined.","Catalyzes the hydrolysis of indole-3-acetic acid (IAA) and 2,4-dichlorophenoxyacetic acid (2,4-D) to indole-3-acetamide (IAM) and 2,4-dichlorobenzoic acid (2,4-DBA), respectively. Belongs to the AB hydrolase superfamily",No,Maybe,No,No,No,not-Yes,GO:0004061,GO:0016788,GO:0052689,GO:0016787,GO:0052689,GO:0016787,0.482,0.3987,0.6019,0.3987,0.6019,5,0.4966,0.2456,no
AVAC_ASPVE,P9WEK4,ProtTale,Eukaryota,284,"Kynurenine formamidase; part of the cluster that mediates the biosynthesis of a highly modified cyclo-arginine-tryptophan dipeptide (cRW). Within the pathway, avaC catalyzes the deformylation of the cyclo-Arg-formylkynurenine iketopiperazine (DKP), produced by the FAD-dependent monooxygenase avaB. The first step of the pathway is perfornmed by the arginine-containing cyclodipeptide synthase (RCPDS) avaA that acts as the scaffold- generating enzyme and is responsible for formation of the cyclo-Arg-Trp (cRW) diketopiperazine. AvaB then acts as a multifunctional flavoenzyme that is responsible for generating the cyclo-Arg-formylkynurenine DKP, which can be deformylated by avaC. AvaB then further catalyzes an additional N-oxidation followed by cyclization and dehydration. The next step is an N-acetylation of the guanidine group catalyzed by the arginine N-acetyltransferase avaD. The roles of the additional enzymes identified within the ava cluster still have to be determined.","Catalyzes the hydrolysis of fatty acid-methyl ester conjugates, such as the endocannabinoid 2-arachidonoylglycerol (2-AG), to yield arachidonic acid and glycerol.",No,No,Maybe,No,No,not-Yes,GO:0004061,GO:0016787,GO:0016787,GO:0016787,GO:0016298,GO:0016787,0.6019,0.6019,0.6019,0.3987,0.6019,5,0.5613,0.2456,no
AVAC_ASPVE,P9WEK4,Protein2Text,Eukaryota,284,"Kynurenine formamidase; part of the cluster that mediates the biosynthesis of a highly modified cyclo-arginine-tryptophan dipeptide (cRW). Within the pathway, avaC catalyzes the deformylation of the cyclo-Arg-formylkynurenine iketopiperazine (DKP), produced by the FAD-dependent monooxygenase avaB. The first step of the pathway is perfornmed by the arginine-containing cyclodipeptide synthase (RCPDS) avaA that acts as the scaffold- generating enzyme and is responsible for formation of the cyclo-Arg-Trp (cRW) diketopiperazine. AvaB then acts as a multifunctional flavoenzyme that is responsible for generating the cyclo-Arg-formylkynurenine DKP, which can be deformylated by avaC. AvaB then further catalyzes an additional N-oxidation followed by cyclization and dehydration. The next step is an N-acetylation of the guanidine group catalyzed by the arginine N-acetyltransferase avaD. The roles of the additional enzymes identified within the ava cluster still have to be determined.","The molecular function of this protein is a hydrolase, specifically a hydrolase that breaks down ester bonds. More specifically, it is a hydrolase that breaks down ester bonds in esters, which are compounds that contain a carboxyl group linked to an alcohol group by an ester bond. This protein is likely involved in the breakdown of esters, which are an important class of compounds in many biological processes.",Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004061,GO:0016788,GO:0016788,GO:0016788,GO:0016788,GO:0016788,0.482,0.482,0.482,0.482,0.482,5,0.482,0.2456,no
AVAC_ASPVE,P9WEK4,Reference,Eukaryota,284,"Kynurenine formamidase; part of the cluster that mediates the biosynthesis of a highly modified cyclo-arginine-tryptophan dipeptide (cRW). Within the pathway, avaC catalyzes the deformylation of the cyclo-Arg-formylkynurenine iketopiperazine (DKP), produced by the FAD-dependent monooxygenase avaB. The first step of the pathway is perfornmed by the arginine-containing cyclodipeptide synthase (RCPDS) avaA that acts as the scaffold- generating enzyme and is responsible for formation of the cyclo-Arg-Trp (cRW) diketopiperazine. AvaB then acts as a multifunctional flavoenzyme that is responsible for generating the cyclo-Arg-formylkynurenine DKP, which can be deformylated by avaC. AvaB then further catalyzes an additional N-oxidation followed by cyclization and dehydration. The next step is an N-acetylation of the guanidine group catalyzed by the arginine N-acetyltransferase avaD. The roles of the additional enzymes identified within the ava cluster still have to be determined.","Kynurenine formamidase; part of the cluster that mediates the biosynthesis of a highly modified cyclo-arginine-tryptophan dipeptide (cRW). Within the pathway, avaC catalyzes the deformylation of the cyclo-Arg-formylkynurenine iketopiperazine (DKP), produced by the FAD-dependent monooxygenase avaB. The first step of the pathway is perfornmed by the arginine-containing cyclodipeptide synthase (RCPDS) avaA that acts as the scaffold- generating enzyme and is responsible for formation of the cyclo-Arg-Trp (cRW) diketopiperazine. AvaB then acts as a multifunctional flavoenzyme that is responsible for generating the cyclo-Arg-formylkynurenine DKP, which can be deformylated by avaC. AvaB then further catalyzes an additional N-oxidation followed by cyclization and dehydration. The next step is an N-acetylation of the guanidine group catalyzed by the arginine N-acetyltransferase avaD. The roles of the additional enzymes identified within the ava cluster still have to be determined.",,,,,,,GO:0004061,GO:0004061,GO:0004061,GO:0004061,GO:0004061,GO:0004061,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2456,no
AVAD_ASPVE,P9WEK5,ESM2Text,Eukaryota,290,"Arginine N-acetyltransferase; part of the cluster that mediates the biosynthesis of a highly modified cyclo-arginine- tryptophan dipeptide (cRW). Within the pathway, avaD catalyzes the N-acetylation of the guanidine group. The first step of the pathway is perfornmed by the arginine-containing cyclodipeptide synthase (RCPDS) avaA that acts as the scaffold- generating enzyme and is responsible for formation of the cyclo-Arg-Trp (cRW) diketopiperazine. AvaB then acts as a multifunctional flavoenzyme that is responsible for generating the cyclo-Arg-formylkynurenine DKP, which can be deformylated by avaC. AvaB then further catalyzes an additional N-oxidation followed by cyclization and dehydration. The next step is an N-acetylation of the guanidine group catalyzed by the arginine N-acetyltransferase avaD. The roles of the additional enzymes identified within the ava cluster still have to be determined.",Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins.,No,No,No,No,No,not-Yes,GO:0016746,GO:0004379,GO:0016746,GO:0004379,GO:0008318,GO:0004582,0.5794,1.0,0.5794,0.4603,0.4275,5,0.6093,0.1817,no
AVAD_ASPVE,P9WEK5,Prot2Text,Eukaryota,290,"Arginine N-acetyltransferase; part of the cluster that mediates the biosynthesis of a highly modified cyclo-arginine- tryptophan dipeptide (cRW). Within the pathway, avaD catalyzes the N-acetylation of the guanidine group. The first step of the pathway is perfornmed by the arginine-containing cyclodipeptide synthase (RCPDS) avaA that acts as the scaffold- generating enzyme and is responsible for formation of the cyclo-Arg-Trp (cRW) diketopiperazine. AvaB then acts as a multifunctional flavoenzyme that is responsible for generating the cyclo-Arg-formylkynurenine DKP, which can be deformylated by avaC. AvaB then further catalyzes an additional N-oxidation followed by cyclization and dehydration. The next step is an N-acetylation of the guanidine group catalyzed by the arginine N-acetyltransferase avaD. The roles of the additional enzymes identified within the ava cluster still have to be determined.",Monooxygenase that converts norsolorinic acid (NOS) to norsolorinic acid (NOR) in the presence of NADH.,No,No,No,No,No,not-Yes,GO:0016746,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,0.3902,0.3902,0.3902,0.3902,0.3902,5,0.3902,0.1817,no
AVAD_ASPVE,P9WEK5,ProtT3,Eukaryota,290,"Arginine N-acetyltransferase; part of the cluster that mediates the biosynthesis of a highly modified cyclo-arginine- tryptophan dipeptide (cRW). Within the pathway, avaD catalyzes the N-acetylation of the guanidine group. The first step of the pathway is perfornmed by the arginine-containing cyclodipeptide synthase (RCPDS) avaA that acts as the scaffold- generating enzyme and is responsible for formation of the cyclo-Arg-Trp (cRW) diketopiperazine. AvaB then acts as a multifunctional flavoenzyme that is responsible for generating the cyclo-Arg-formylkynurenine DKP, which can be deformylated by avaC. AvaB then further catalyzes an additional N-oxidation followed by cyclization and dehydration. The next step is an N-acetylation of the guanidine group catalyzed by the arginine N-acetyltransferase avaD. The roles of the additional enzymes identified within the ava cluster still have to be determined.",N-acetylglutamate synthase involved in arginine biosynthesis. Mitochondrion matrix. Belongs to the acetyltransferase family,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016746,GO:0004042,GO:0004042,GO:0004042,GO:0004042,GO:0004042,0.5029,0.5029,0.5029,0.5029,0.5029,5,0.5029,0.1817,no
AVAD_ASPVE,P9WEK5,ProtTale,Eukaryota,290,"Arginine N-acetyltransferase; part of the cluster that mediates the biosynthesis of a highly modified cyclo-arginine- tryptophan dipeptide (cRW). Within the pathway, avaD catalyzes the N-acetylation of the guanidine group. The first step of the pathway is perfornmed by the arginine-containing cyclodipeptide synthase (RCPDS) avaA that acts as the scaffold- generating enzyme and is responsible for formation of the cyclo-Arg-Trp (cRW) diketopiperazine. AvaB then acts as a multifunctional flavoenzyme that is responsible for generating the cyclo-Arg-formylkynurenine DKP, which can be deformylated by avaC. AvaB then further catalyzes an additional N-oxidation followed by cyclization and dehydration. The next step is an N-acetylation of the guanidine group catalyzed by the arginine N-acetyltransferase avaD. The roles of the additional enzymes identified within the ava cluster still have to be determined.",Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and releases both CoA and the modified product in the form of an acyl-CoA.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016746,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.729,0.729,0.729,0.729,0.729,5,0.729,0.1817,no
AVAD_ASPVE,P9WEK5,Protein2Text,Eukaryota,290,"Arginine N-acetyltransferase; part of the cluster that mediates the biosynthesis of a highly modified cyclo-arginine- tryptophan dipeptide (cRW). Within the pathway, avaD catalyzes the N-acetylation of the guanidine group. The first step of the pathway is perfornmed by the arginine-containing cyclodipeptide synthase (RCPDS) avaA that acts as the scaffold- generating enzyme and is responsible for formation of the cyclo-Arg-Trp (cRW) diketopiperazine. AvaB then acts as a multifunctional flavoenzyme that is responsible for generating the cyclo-Arg-formylkynurenine DKP, which can be deformylated by avaC. AvaB then further catalyzes an additional N-oxidation followed by cyclization and dehydration. The next step is an N-acetylation of the guanidine group catalyzed by the arginine N-acetyltransferase avaD. The roles of the additional enzymes identified within the ava cluster still have to be determined.","This protein is involved in a biochemical process. Unfortunately, I cannot verify the molecular function of this protein.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016746,,,,,,,,,,,0,,0.1817,no
AVAD_ASPVE,P9WEK5,Reference,Eukaryota,290,"Arginine N-acetyltransferase; part of the cluster that mediates the biosynthesis of a highly modified cyclo-arginine- tryptophan dipeptide (cRW). Within the pathway, avaD catalyzes the N-acetylation of the guanidine group. The first step of the pathway is perfornmed by the arginine-containing cyclodipeptide synthase (RCPDS) avaA that acts as the scaffold- generating enzyme and is responsible for formation of the cyclo-Arg-Trp (cRW) diketopiperazine. AvaB then acts as a multifunctional flavoenzyme that is responsible for generating the cyclo-Arg-formylkynurenine DKP, which can be deformylated by avaC. AvaB then further catalyzes an additional N-oxidation followed by cyclization and dehydration. The next step is an N-acetylation of the guanidine group catalyzed by the arginine N-acetyltransferase avaD. The roles of the additional enzymes identified within the ava cluster still have to be determined.","Arginine N-acetyltransferase; part of the cluster that mediates the biosynthesis of a highly modified cyclo-arginine- tryptophan dipeptide (cRW). Within the pathway, avaD catalyzes the N-acetylation of the guanidine group. The first step of the pathway is perfornmed by the arginine-containing cyclodipeptide synthase (RCPDS) avaA that acts as the scaffold- generating enzyme and is responsible for formation of the cyclo-Arg-Trp (cRW) diketopiperazine. AvaB then acts as a multifunctional flavoenzyme that is responsible for generating the cyclo-Arg-formylkynurenine DKP, which can be deformylated by avaC. AvaB then further catalyzes an additional N-oxidation followed by cyclization and dehydration. The next step is an N-acetylation of the guanidine group catalyzed by the arginine N-acetyltransferase avaD. The roles of the additional enzymes identified within the ava cluster still have to be determined.",,,,,,,GO:0016746,GO:0016407,GO:0016407,GO:0016407,GO:0016407,GO:0016407,0.729,0.729,0.729,0.729,0.729,5,0.729,0.1817,no
AVAP_ASPVE,P9WEL7,ESM2Text,Eukaryota,453,"UDP-glucosyltransferase; part of the cluster that mediates the biosynthesis of a highly modified cyclo-arginine-tryptophan dipeptide (cRW). The first step of the pathway is perfornmed by the arginine-containing cyclodipeptide synthase (RCPDS) avaA that acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Trp (cRW) diketopiperazine. AvaB then acts as a multifunctional flavoenzyme that is responsible for generating the cyclo-Arg-formylkynurenine DKP, which can be deformylated by avaC. AvaB then further catalyzes an additional N-oxidation followed by cyclization and dehydration. The next step is an N-acetylation of the guanidine group catalyzed by the arginine N-acetyltransferase avaD. The roles of the additional enzymes identified within the ava cluster still have to be determined.","Catalyzes the first step in the biosynthesis of glycosaminoglycans, heparan sulfate-containing polysaccharides. Converts the end product ZC(2)-(4R)-dodecan to the corresponding monosaccharide bis(beta-D-glucosaminyl)-hexadecadienoate.",No,No,No,Maybe,Maybe,not-Yes,GO:0016757,,,,,,,,,,,0,,0.2371,no
AVAP_ASPVE,P9WEL7,Prot2Text,Eukaryota,453,"UDP-glucosyltransferase; part of the cluster that mediates the biosynthesis of a highly modified cyclo-arginine-tryptophan dipeptide (cRW). The first step of the pathway is perfornmed by the arginine-containing cyclodipeptide synthase (RCPDS) avaA that acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Trp (cRW) diketopiperazine. AvaB then acts as a multifunctional flavoenzyme that is responsible for generating the cyclo-Arg-formylkynurenine DKP, which can be deformylated by avaC. AvaB then further catalyzes an additional N-oxidation followed by cyclization and dehydration. The next step is an N-acetylation of the guanidine group catalyzed by the arginine N-acetyltransferase avaD. The roles of the additional enzymes identified within the ava cluster still have to be determined.","Catalyzes the first step in the biosynthesis of aurones, plant flavonoids that provide yellow coloration to flowers.",No,No,No,No,No,not-Yes,GO:0016757,GO:0016491,GO:0016491,GO:0016682,GO:0016491,GO:0016491,0.4807,0.4807,0.3284,0.4807,0.4807,5,0.4502,0.2371,no
AVAP_ASPVE,P9WEL7,ProtT3,Eukaryota,453,"UDP-glucosyltransferase; part of the cluster that mediates the biosynthesis of a highly modified cyclo-arginine-tryptophan dipeptide (cRW). The first step of the pathway is perfornmed by the arginine-containing cyclodipeptide synthase (RCPDS) avaA that acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Trp (cRW) diketopiperazine. AvaB then acts as a multifunctional flavoenzyme that is responsible for generating the cyclo-Arg-formylkynurenine DKP, which can be deformylated by avaC. AvaB then further catalyzes an additional N-oxidation followed by cyclization and dehydration. The next step is an N-acetylation of the guanidine group catalyzed by the arginine N-acetyltransferase avaD. The roles of the additional enzymes identified within the ava cluster still have to be determined.","Glycosyltransferase; part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties",Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2371,no
AVAP_ASPVE,P9WEL7,ProtTale,Eukaryota,453,"UDP-glucosyltransferase; part of the cluster that mediates the biosynthesis of a highly modified cyclo-arginine-tryptophan dipeptide (cRW). The first step of the pathway is perfornmed by the arginine-containing cyclodipeptide synthase (RCPDS) avaA that acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Trp (cRW) diketopiperazine. AvaB then acts as a multifunctional flavoenzyme that is responsible for generating the cyclo-Arg-formylkynurenine DKP, which can be deformylated by avaC. AvaB then further catalyzes an additional N-oxidation followed by cyclization and dehydration. The next step is an N-acetylation of the guanidine group catalyzed by the arginine N-acetyltransferase avaD. The roles of the additional enzymes identified within the ava cluster still have to be determined.","Involved in the biosynthesis of 3-O-methylmyo-inositol (3MOI), a 3-O-myo-inositol phosphate present at the non-reducing end of cello-oligosaccharides. Catalyzes the conversion of 3-O-myo-inosinic acid (3MIA) to 3-O-methylmyo-inosinic acid (3MOI).",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0016757,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.5565,0.5565,0.5565,0.5565,0.5565,5,0.5565,0.2371,no
AVAP_ASPVE,P9WEL7,Protein2Text,Eukaryota,453,"UDP-glucosyltransferase; part of the cluster that mediates the biosynthesis of a highly modified cyclo-arginine-tryptophan dipeptide (cRW). The first step of the pathway is perfornmed by the arginine-containing cyclodipeptide synthase (RCPDS) avaA that acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Trp (cRW) diketopiperazine. AvaB then acts as a multifunctional flavoenzyme that is responsible for generating the cyclo-Arg-formylkynurenine DKP, which can be deformylated by avaC. AvaB then further catalyzes an additional N-oxidation followed by cyclization and dehydration. The next step is an N-acetylation of the guanidine group catalyzed by the arginine N-acetyltransferase avaD. The roles of the additional enzymes identified within the ava cluster still have to be determined.","This protein is involved in the molecular function of oxidoreductase activity. Specifically, it is a cytochrome P450 enzyme that catalyzes the oxidation of various organic compounds, such as steroids and fatty acids. It plays a crucial role in the metabolism of these compounds and is involved in various biological processes, including steroid hormone biosynthesis and detoxification of xenobiotics.",No,No,No,No,No,not-Yes,GO:0016757,GO:0004497,GO:0004497; GO:0020037,GO:0004497; GO:0020037,GO:0004497,GO:0004497,0.3902,0.318,0.318,0.3902,0.3902,5,0.3613,0.2371,no
AVAP_ASPVE,P9WEL7,Reference,Eukaryota,453,"UDP-glucosyltransferase; part of the cluster that mediates the biosynthesis of a highly modified cyclo-arginine-tryptophan dipeptide (cRW). The first step of the pathway is perfornmed by the arginine-containing cyclodipeptide synthase (RCPDS) avaA that acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Trp (cRW) diketopiperazine. AvaB then acts as a multifunctional flavoenzyme that is responsible for generating the cyclo-Arg-formylkynurenine DKP, which can be deformylated by avaC. AvaB then further catalyzes an additional N-oxidation followed by cyclization and dehydration. The next step is an N-acetylation of the guanidine group catalyzed by the arginine N-acetyltransferase avaD. The roles of the additional enzymes identified within the ava cluster still have to be determined.","UDP-glucosyltransferase; part of the cluster that mediates the biosynthesis of a highly modified cyclo-arginine-tryptophan dipeptide (cRW). The first step of the pathway is perfornmed by the arginine-containing cyclodipeptide synthase (RCPDS) avaA that acts as the scaffold-generating enzyme and is responsible for formation of the cyclo-Arg-Trp (cRW) diketopiperazine. AvaB then acts as a multifunctional flavoenzyme that is responsible for generating the cyclo-Arg-formylkynurenine DKP, which can be deformylated by avaC. AvaB then further catalyzes an additional N-oxidation followed by cyclization and dehydration. The next step is an N-acetylation of the guanidine group catalyzed by the arginine N-acetyltransferase avaD. The roles of the additional enzymes identified within the ava cluster still have to be determined.",,,,,,,GO:0016757,GO:0016757,GO:0035251,GO:0016757,,GO:0016757,1.0,0.5991,1.0,,1.0,4,0.8998,0.2371,no
ASTK_ASPOR,P9WEM0,ESM2Text,Eukaryota,196,"Sesquiterpene phosphatase; part of the gene cluster that mediates the biosynthesis of astellolides, drimane-type sesquiterpene esters that show antimicrobial, anti-inflammatory, and anti-tumor activities. The first step in astellolide biosynthesis is performed by the sesquiterpene cyclase astC that catalyzes the formation of drimanyl pyrophosphate from farnesyl pyrophosphate. Drimanyl pyrophosphate is then dephosphorylated by the sesquiterpene phosphatase astI to produce drimanyl monophosphate which is further dephosphorylated to drim-8-ene- 11-ol by atsK. Drim-8-ene-11-ol is converted to confertifolin, probably by the cytochrome P450 monooxygenase astD and/or the dehydrogenase astE. The cytochrome P450 monooxygenases astB, astF and astJ then hydroxylate confertifolin at C6, C14, or C15 to form trihydroxy confertifolin. The nonribosomal peptide synthetase astA catalyzes ester bond formation between trihydroxy contifolin and benzoic acid (BA) or 4-hydroxy benzoic acid (4HBA), leading to the formation of dideacetyl astellolides A and B, respectively. Finally, the O- acetyltransferase astG converts dideacetyl astellolides A and B into deacetyl astellolides A and B.",Catalyzes the dephosphorylation of flavin mononucleotide (FMN) to riboflavin.,No,No,Maybe,Maybe,Maybe,not-Yes,GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0008828,GO:0016791,1.0,1.0,1.0,0.261,1.0,5,0.8522,0.1171,no
ASTK_ASPOR,P9WEM0,Prot2Text,Eukaryota,196,"Sesquiterpene phosphatase; part of the gene cluster that mediates the biosynthesis of astellolides, drimane-type sesquiterpene esters that show antimicrobial, anti-inflammatory, and anti-tumor activities. The first step in astellolide biosynthesis is performed by the sesquiterpene cyclase astC that catalyzes the formation of drimanyl pyrophosphate from farnesyl pyrophosphate. Drimanyl pyrophosphate is then dephosphorylated by the sesquiterpene phosphatase astI to produce drimanyl monophosphate which is further dephosphorylated to drim-8-ene- 11-ol by atsK. Drim-8-ene-11-ol is converted to confertifolin, probably by the cytochrome P450 monooxygenase astD and/or the dehydrogenase astE. The cytochrome P450 monooxygenases astB, astF and astJ then hydroxylate confertifolin at C6, C14, or C15 to form trihydroxy confertifolin. The nonribosomal peptide synthetase astA catalyzes ester bond formation between trihydroxy contifolin and benzoic acid (BA) or 4-hydroxy benzoic acid (4HBA), leading to the formation of dideacetyl astellolides A and B, respectively. Finally, the O- acetyltransferase astG converts dideacetyl astellolides A and B into deacetyl astellolides A and B.",Catalyzes the dephosphorylation of different sugar phosphates.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016791,GO:0016791,GO:0050308,GO:0016791,GO:0050308,GO:0016791,1.0,0.7707,1.0,0.7707,1.0,5,0.9083,0.1171,no
ASTK_ASPOR,P9WEM0,ProtT3,Eukaryota,196,"Sesquiterpene phosphatase; part of the gene cluster that mediates the biosynthesis of astellolides, drimane-type sesquiterpene esters that show antimicrobial, anti-inflammatory, and anti-tumor activities. The first step in astellolide biosynthesis is performed by the sesquiterpene cyclase astC that catalyzes the formation of drimanyl pyrophosphate from farnesyl pyrophosphate. Drimanyl pyrophosphate is then dephosphorylated by the sesquiterpene phosphatase astI to produce drimanyl monophosphate which is further dephosphorylated to drim-8-ene- 11-ol by atsK. Drim-8-ene-11-ol is converted to confertifolin, probably by the cytochrome P450 monooxygenase astD and/or the dehydrogenase astE. The cytochrome P450 monooxygenases astB, astF and astJ then hydroxylate confertifolin at C6, C14, or C15 to form trihydroxy confertifolin. The nonribosomal peptide synthetase astA catalyzes ester bond formation between trihydroxy contifolin and benzoic acid (BA) or 4-hydroxy benzoic acid (4HBA), leading to the formation of dideacetyl astellolides A and B, respectively. Finally, the O- acetyltransferase astG converts dideacetyl astellolides A and B into deacetyl astellolides A and B.","Catalyzes the dephosphorylation of 2- amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH). Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family",Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1171,no
ASTK_ASPOR,P9WEM0,ProtTale,Eukaryota,196,"Sesquiterpene phosphatase; part of the gene cluster that mediates the biosynthesis of astellolides, drimane-type sesquiterpene esters that show antimicrobial, anti-inflammatory, and anti-tumor activities. The first step in astellolide biosynthesis is performed by the sesquiterpene cyclase astC that catalyzes the formation of drimanyl pyrophosphate from farnesyl pyrophosphate. Drimanyl pyrophosphate is then dephosphorylated by the sesquiterpene phosphatase astI to produce drimanyl monophosphate which is further dephosphorylated to drim-8-ene- 11-ol by atsK. Drim-8-ene-11-ol is converted to confertifolin, probably by the cytochrome P450 monooxygenase astD and/or the dehydrogenase astE. The cytochrome P450 monooxygenases astB, astF and astJ then hydroxylate confertifolin at C6, C14, or C15 to form trihydroxy confertifolin. The nonribosomal peptide synthetase astA catalyzes ester bond formation between trihydroxy contifolin and benzoic acid (BA) or 4-hydroxy benzoic acid (4HBA), leading to the formation of dideacetyl astellolides A and B, respectively. Finally, the O- acetyltransferase astG converts dideacetyl astellolides A and B into deacetyl astellolides A and B.","Kinase that catalyzes the phosphorylation of poly(3-hydroxybutyrate) (PHB) at the C-3 position of the PHB chain, converting PHB to 3-phosphate-PHB (3-P-PHB).",No,No,No,No,No,not-Yes,GO:0016791,GO:0016301,GO:0016301,GO:0016301,GO:0016301,GO:0016301,0.2353,0.2353,0.2353,0.2353,0.2353,5,0.2353,0.1171,no
ASTK_ASPOR,P9WEM0,Protein2Text,Eukaryota,196,"Sesquiterpene phosphatase; part of the gene cluster that mediates the biosynthesis of astellolides, drimane-type sesquiterpene esters that show antimicrobial, anti-inflammatory, and anti-tumor activities. The first step in astellolide biosynthesis is performed by the sesquiterpene cyclase astC that catalyzes the formation of drimanyl pyrophosphate from farnesyl pyrophosphate. Drimanyl pyrophosphate is then dephosphorylated by the sesquiterpene phosphatase astI to produce drimanyl monophosphate which is further dephosphorylated to drim-8-ene- 11-ol by atsK. Drim-8-ene-11-ol is converted to confertifolin, probably by the cytochrome P450 monooxygenase astD and/or the dehydrogenase astE. The cytochrome P450 monooxygenases astB, astF and astJ then hydroxylate confertifolin at C6, C14, or C15 to form trihydroxy confertifolin. The nonribosomal peptide synthetase astA catalyzes ester bond formation between trihydroxy contifolin and benzoic acid (BA) or 4-hydroxy benzoic acid (4HBA), leading to the formation of dideacetyl astellolides A and B, respectively. Finally, the O- acetyltransferase astG converts dideacetyl astellolides A and B into deacetyl astellolides A and B.","This protein is involved in the dephosphorylation of a compound. More specifically, it is a phosphatase that catalyzes the hydrolysis of phosphate groups from its substrate, allowing the release of phosphate ions from the compound. The molecular function of this protein is to catalyze the removal of phosphate groups from its substrate, thereby facilitating the conversion of phosphorylated compounds into their dephosphorylated forms. This process is an essential step in various cellular pathways, including metabolism, signaling, and gene regulation.",Vague,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1171,no
ASTK_ASPOR,P9WEM0,Reference,Eukaryota,196,"Sesquiterpene phosphatase; part of the gene cluster that mediates the biosynthesis of astellolides, drimane-type sesquiterpene esters that show antimicrobial, anti-inflammatory, and anti-tumor activities. The first step in astellolide biosynthesis is performed by the sesquiterpene cyclase astC that catalyzes the formation of drimanyl pyrophosphate from farnesyl pyrophosphate. Drimanyl pyrophosphate is then dephosphorylated by the sesquiterpene phosphatase astI to produce drimanyl monophosphate which is further dephosphorylated to drim-8-ene- 11-ol by atsK. Drim-8-ene-11-ol is converted to confertifolin, probably by the cytochrome P450 monooxygenase astD and/or the dehydrogenase astE. The cytochrome P450 monooxygenases astB, astF and astJ then hydroxylate confertifolin at C6, C14, or C15 to form trihydroxy confertifolin. The nonribosomal peptide synthetase astA catalyzes ester bond formation between trihydroxy contifolin and benzoic acid (BA) or 4-hydroxy benzoic acid (4HBA), leading to the formation of dideacetyl astellolides A and B, respectively. Finally, the O- acetyltransferase astG converts dideacetyl astellolides A and B into deacetyl astellolides A and B.","Sesquiterpene phosphatase; part of the gene cluster that mediates the biosynthesis of astellolides, drimane-type sesquiterpene esters that show antimicrobial, anti-inflammatory, and anti-tumor activities. The first step in astellolide biosynthesis is performed by the sesquiterpene cyclase astC that catalyzes the formation of drimanyl pyrophosphate from farnesyl pyrophosphate. Drimanyl pyrophosphate is then dephosphorylated by the sesquiterpene phosphatase astI to produce drimanyl monophosphate which is further dephosphorylated to drim-8-ene- 11-ol by atsK. Drim-8-ene-11-ol is converted to confertifolin, probably by the cytochrome P450 monooxygenase astD and/or the dehydrogenase astE. The cytochrome P450 monooxygenases astB, astF and astJ then hydroxylate confertifolin at C6, C14, or C15 to form trihydroxy confertifolin. The nonribosomal peptide synthetase astA catalyzes ester bond formation between trihydroxy contifolin and benzoic acid (BA) or 4-hydroxy benzoic acid (4HBA), leading to the formation of dideacetyl astellolides A and B, respectively. Finally, the O- acetyltransferase astG converts dideacetyl astellolides A and B into deacetyl astellolides A and B.",,,,,,,GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,GO:0016791,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1171,no
FRBG_STRR3,Q0ZQ42,ESM2Text,Bacteria,437,"Hydroxylase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the N-hydroxylation of CMP-5'-3- aminopropylphosphonate (CMP-5'-3APn) to CMP-5'-(N-hydroxy-3- aminopropyl)phosphonate (CMP-5'-H3APn). Cannot use CMP-5'-N-acetyl-3-aminopropylphosphonate (CMP-5'-Ac3APn) as a substrate.","Catalyzes the oxidative deamination of glycine to (2R,3S)-2-amino-6-oxopimelate, the penultimate step in the biosynthesis of the biodegradation pyrroindol.",No,No,No,No,No,not-Yes,GO:0004497,,GO:0016491,,,,,0.8145,,,,1,0.8145,0.3187,no
FRBG_STRR3,Q0ZQ42,Prot2Text,Bacteria,437,"Hydroxylase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the N-hydroxylation of CMP-5'-3- aminopropylphosphonate (CMP-5'-3APn) to CMP-5'-(N-hydroxy-3- aminopropyl)phosphonate (CMP-5'-H3APn). Cannot use CMP-5'-N-acetyl-3-aminopropylphosphonate (CMP-5'-Ac3APn) as a substrate.","Part of the bacABCDEF operon responsible for the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. Bacilysin is an irreversible inactivator of the glutaminase domain of glucosamine synthetase. BacA is an unusual prephenate monooxygenase that avoids the typical aromatization of the cyclohexadienol ring of prephenate. BacA catalyzes the oxidative C-C bond cleavage of 4-hydroxy-L-alanine (4-HAA), producing 4-HAA in 5,6-dihydro-alpha-hydroxyphenylpyruvate (DHPAA) and inorganic phosphate. The presence of the alpha(3),beta(3)-unsaturated aldehyde group at the C3 position enables the gamma(3)-unsaturated aldehyde formation, which is the key enzyme in the biosynthesis of bacilysin. BacA catalyzes a nonenzymatic isomerization of prephenate to produce the exocyclic 4-HAA. The enzyme is specific for 4-HAA as the",No,No,No,Maybe,Maybe,not-Yes,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,GO:0004497,1.0,1.0,1.0,1.0,1.0,5,1.0,0.3187,no
FRBG_STRR3,Q0ZQ42,ProtT3,Bacteria,437,"Hydroxylase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the N-hydroxylation of CMP-5'-3- aminopropylphosphonate (CMP-5'-3APn) to CMP-5'-(N-hydroxy-3- aminopropyl)phosphonate (CMP-5'-H3APn). Cannot use CMP-5'-N-acetyl-3-aminopropylphosphonate (CMP-5'-Ac3APn) as a substrate.",FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) . Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranyl,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004497,GO:0004497; GO:0050660,GO:0004497; GO:0071949,GO:0004497,GO:0004497; GO:0071949,GO:0004497; GO:0071949,0.7012,0.6988,1.0,0.6988,0.6988,5,0.7595,0.3187,no
FRBG_STRR3,Q0ZQ42,ProtTale,Bacteria,437,"Hydroxylase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the N-hydroxylation of CMP-5'-3- aminopropylphosphonate (CMP-5'-3APn) to CMP-5'-(N-hydroxy-3- aminopropyl)phosphonate (CMP-5'-H3APn). Cannot use CMP-5'-N-acetyl-3-aminopropylphosphonate (CMP-5'-Ac3APn) as a substrate.","Involved in the biosynthesis of the siderophore pyoverdine, which is a Fe(3+)-pyoverdine complex. Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (2E,6E)-geranylgeranyl diphosphate ((2E,6E)-GGP).",No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0004497,GO:0004311,GO:0016765,GO:0004311,GO:0016765,GO:0004337,0.2523,0.3902,0.2523,0.3902,0.2523,5,0.3075,0.3187,no
FRBG_STRR3,Q0ZQ42,Protein2Text,Bacteria,437,"Hydroxylase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the N-hydroxylation of CMP-5'-3- aminopropylphosphonate (CMP-5'-3APn) to CMP-5'-(N-hydroxy-3- aminopropyl)phosphonate (CMP-5'-H3APn). Cannot use CMP-5'-N-acetyl-3-aminopropylphosphonate (CMP-5'-Ac3APn) as a substrate.","This protein is involved in a process related to molecular function, specifically catalyzing a reaction. However, the exact molecular function is not specified in the provided text.",Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0004497,,,,,,,,,,,0,,0.3187,no
FRBG_STRR3,Q0ZQ42,Reference,Bacteria,437,"Hydroxylase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the N-hydroxylation of CMP-5'-3- aminopropylphosphonate (CMP-5'-3APn) to CMP-5'-(N-hydroxy-3- aminopropyl)phosphonate (CMP-5'-H3APn). Cannot use CMP-5'-N-acetyl-3-aminopropylphosphonate (CMP-5'-Ac3APn) as a substrate.","Hydroxylase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the N-hydroxylation of CMP-5'-3- aminopropylphosphonate (CMP-5'-3APn) to CMP-5'-(N-hydroxy-3- aminopropyl)phosphonate (CMP-5'-H3APn). Cannot use CMP-5'-N-acetyl-3-aminopropylphosphonate (CMP-5'-Ac3APn) as a substrate.",,,,,,,GO:0004497,GO:0004497,GO:0016491; GO:0004497,GO:0016491,GO:0016709,GO:0004497,1.0,0.9382,0.8145,0.747,1.0,5,0.8999,0.3187,no
PEPM_STRR3,Q0ZQ45,ESM2Text,Bacteria,276,"Isomerase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the conversion of phosphoenolpyruvate (PEP) to phosphonopyruvate.",Catalyzes the formation of a phosphoenolpyruvate (PEP) intermediate by incorporating an acyl moiety at the sn-2 position of phosphoenolpyruvate.,No,No,No,Maybe,No,not-Yes,GO:0050188,,GO:0016746,,,,,0.2845,,,,1,0.2845,0.4569,no
PEPM_STRR3,Q0ZQ45,Prot2Text,Bacteria,276,"Isomerase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the conversion of phosphoenolpyruvate (PEP) to phosphonopyruvate.","Catalyzes the formation of proponate and pyruvate from (2R,3S)-2,3-dimethylmalate.",No,No,No,No,No,not-Yes,GO:0050188,GO:0016829,GO:0016829,GO:0016829,GO:0016829,GO:0016829,0.3552,0.3552,0.3552,0.3552,0.3552,5,0.3552,0.4569,no
PEPM_STRR3,Q0ZQ45,ProtT3,Bacteria,276,"Isomerase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the conversion of phosphoenolpyruvate (PEP) to phosphonopyruvate.",Belongs to the isocitrate lyase/PEP mutase superfamily. PEP mutase family,Vague,Maybe,Maybe,Vague,Maybe,not-Yes,GO:0050188,GO:0050189,GO:0016866,,GO:0008963,GO:0008963,0.1737,0.729,,0.1998,0.1998,4,0.3256,0.4569,no
PEPM_STRR3,Q0ZQ45,ProtTale,Bacteria,276,"Isomerase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the conversion of phosphoenolpyruvate (PEP) to phosphonopyruvate.",Catalyzes the formation of phosphoenolpyruvate (PEP) from pyruvate.,No,Maybe,Maybe,Maybe,No,not-Yes,GO:0050188,GO:0016301,GO:0016301,GO:0016301,GO:0016301,GO:0016301,0.2353,0.2353,0.2353,0.2353,0.2353,5,0.2353,0.4569,no
PEPM_STRR3,Q0ZQ45,Protein2Text,Bacteria,276,"Isomerase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the conversion of phosphoenolpyruvate (PEP) to phosphonopyruvate.","The molecular function of this protein is an enzyme, specifically an aldolase, which catalyzes the reversible cleavage of fructose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate.",No,No,No,No,No,not-Yes,GO:0050188,GO:0004332,GO:0004332,GO:0004332,GO:0004332,GO:0004332,0.1998,0.1998,0.1998,0.1998,0.1998,5,0.1998,0.4569,no
PEPM_STRR3,Q0ZQ45,Reference,Bacteria,276,"Isomerase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the conversion of phosphoenolpyruvate (PEP) to phosphonopyruvate.","Isomerase involved in the biosynthesis of the phosphonate antibiotic FR-900098, a potent antimalarial agent that acts as an inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the conversion of phosphoenolpyruvate (PEP) to phosphonopyruvate.",,,,,,,GO:0050188,GO:0016853,GO:0016853,GO:0016853,GO:0008903,GO:0016853,0.6019,0.6019,0.6019,0.3386,0.6019,5,0.5492,0.4569,no
DHGRD_NOVAD,Q2G5J3,ESM2Text,Bacteria,304,"Part of the alkanesulfonate monooxygenase (sulfo-ASMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite (Ref.2). Catalyzes the NADP-dependent reduction of 6-dehydro-D-glucose to D-glucose (Ref.2). Can also catalyze the reversible reaction, the formation of 6-dehydro- D-glucose from D-glucose in the presence of NADP(+) (Ref.2).","Dehydrogenase involved in the degradation of substituted sulfonated phenazines. Catalyzes the reduction of the aldose C(2)S(2) to yield the keto C(2)R, using NADPH as the electron donor. It has a strong preference for NADH. Can also use ribulose-bisphosphate and butyraldehyde, but not fructose-bisphosphate.",No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1976,no
DHGRD_NOVAD,Q2G5J3,Prot2Text,Bacteria,304,"Part of the alkanesulfonate monooxygenase (sulfo-ASMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite (Ref.2). Catalyzes the NADP-dependent reduction of 6-dehydro-D-glucose to D-glucose (Ref.2). Can also catalyze the reversible reaction, the formation of 6-dehydro- D-glucose from D-glucose in the presence of NADP(+) (Ref.2).","Aldose reductase with broad substrate specificity. Preferentially reduces D-xylose and L-arabinose (L-arabinose). Can use NADH and NADPH, but with a strong preference for NADH. Is probably involved in a degradation pathway that allows P.aeruginosa to grow on L-arabinose as the sole carbon source.",No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,GO:0016614,GO:0016614,GO:0016614,GO:0004032,GO:0004032,0.8145,0.8145,0.8145,0.4908,0.4908,5,0.685,0.1976,no
DHGRD_NOVAD,Q2G5J3,ProtT3,Bacteria,304,"Part of the alkanesulfonate monooxygenase (sulfo-ASMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite (Ref.2). Catalyzes the NADP-dependent reduction of 6-dehydro-D-glucose to D-glucose (Ref.2). Can also catalyze the reversible reaction, the formation of 6-dehydro- D-glucose from D-glucose in the presence of NADP(+) (Ref.2).",Belongs to the aldo/keto reductase family. Aldo/keto reductase 2 subfamily,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0016491,GO:0016491,GO:0016491,,GO:0016491,GO:0016491,1.0,1.0,,1.0,1.0,4,1.0,0.1976,no
DHGRD_NOVAD,Q2G5J3,ProtTale,Bacteria,304,"Part of the alkanesulfonate monooxygenase (sulfo-ASMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite (Ref.2). Catalyzes the NADP-dependent reduction of 6-dehydro-D-glucose to D-glucose (Ref.2). Can also catalyze the reversible reaction, the formation of 6-dehydro- D-glucose from D-glucose in the presence of NADP(+) (Ref.2).",Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the transfer of the methyl group from S-adenosyl-L- methionine to the aldehyde group of betaine aldehyde and is thus involved in the final step in the biosynthesis of glycine betaine.,No,No,No,No,No,not-Yes,GO:0016491,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.4071,0.4071,0.4071,0.4071,0.4071,5,0.4071,0.1976,no
DHGRD_NOVAD,Q2G5J3,Protein2Text,Bacteria,304,"Part of the alkanesulfonate monooxygenase (sulfo-ASMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite (Ref.2). Catalyzes the NADP-dependent reduction of 6-dehydro-D-glucose to D-glucose (Ref.2). Can also catalyze the reversible reaction, the formation of 6-dehydro- D-glucose from D-glucose in the presence of NADP(+) (Ref.2).","The molecular function of this protein is involved in catalyzing the decarboxylation of 2-keto-3-methylvalerate to 2-methylcrotonyl-CoA. 
It is a decarboxylase, specifically a 2-keto-3-methylvalerate decarboxylase. 
It is involved in the degradation of leucine via the leucine degradation pathway. 

The protein uses a radical mechanism to catalyze the decarboxylation of 2-keto-3-methylvalerate to 2-methylcrotonyl-CoA. 

The protein is also involved in the degradation of leucine via the leucine degradation pathway. 

The protein is also involved in the degradation of leucine via the leucine degradation pathway. 

The protein is also involved in the degradation of leucine via the leucine degradation pathway. 

The protein is also involved in the degradation of leucine via the leucine degradation pathway. 

The protein is also involved in the degradation of leucine via the leucine degradation pathway. 

The protein is also involved in the degradation of leucine via the leucine degradation pathway. 

The protein is also involved in the degradation of leucine via the leucine degradation pathway. 

The protein is also involved in the degradation of leucine via the leucine degradation pathway. 

The protein is also involved in the degradation of leucine via the leucine degradation pathway. 

The protein is also involved in the degradation of leucine via the leucine degradation pathway. 

The protein is also involved in the degradation of leucine via the leucine degradation pathway. 

The protein is also involved in the degradation of leucine via the leucine degradation pathway. 

The protein is also involved in the degradation of leucine via the leucine degradation pathway. 

The protein is also involved in the degradation of leucine via the leucine degradation pathway. 

The protein is also involved in the degradation of leucine via the leucine degradation pathway. 

The protein is also involved in the degradation of leucine via the leucine degradation pathway. 

The protein is also involved in the degradation of leucine via the leucine degradation pathway. 

The protein is also involved in the degradation of leucine via the leucine degradation pathway. 

The protein is also involved in the degradation of",No,No,No,No,No,not-Yes,GO:0016491,GO:0016831,GO:0016831,GO:0016831,GO:0016831,GO:0016831,0.4071,0.4071,0.4071,0.4071,0.4071,5,0.4071,0.1976,no
DHGRD_NOVAD,Q2G5J3,Reference,Bacteria,304,"Part of the alkanesulfonate monooxygenase (sulfo-ASMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite (Ref.2). Catalyzes the NADP-dependent reduction of 6-dehydro-D-glucose to D-glucose (Ref.2). Can also catalyze the reversible reaction, the formation of 6-dehydro- D-glucose from D-glucose in the presence of NADP(+) (Ref.2).","Part of the alkanesulfonate monooxygenase (sulfo-ASMO) pathway, a D-sulfoquinovose degradation pathway that enables the complete utilization of all carbons within sulfoquinovose (SQ) with concomitant production of inorganic sulfite (Ref.2). Catalyzes the NADP-dependent reduction of 6-dehydro-D-glucose to D-glucose (Ref.2). Can also catalyze the reversible reaction, the formation of 6-dehydro- D-glucose from D-glucose in the presence of NADP(+) (Ref.2).",,,,,,,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.1976,no
WZY_ECOLX,Q58YW1,ESM2Text,Bacteria,446,"Polymerase involved in the biosynthesis of the lipopolysaccharide (LPS). Catalyzes the polymerization of the O-antigen repeat units on the periplasmic face of the inner membrane, leading to the formation of the lipid-linked O- antigen molecule. In vitro, shows a preference for bacteria-based, undecaprenyl-containing substrates rather than eukaryote-based, dolichol-containing substrates.","May link the O-antigen tetrasaccharide units into long chains, giving rise to typical smooth LPS.",Yes,Yes,Maybe,Yes,Yes,Yes,GO:0016740,,,,,,,,,,,0,,0.6398,yes
WZY_ECOLX,Q58YW1,Prot2Text,Bacteria,446,"Polymerase involved in the biosynthesis of the lipopolysaccharide (LPS). Catalyzes the polymerization of the O-antigen repeat units on the periplasmic face of the inner membrane, leading to the formation of the lipid-linked O- antigen molecule. In vitro, shows a preference for bacteria-based, undecaprenyl-containing substrates rather than eukaryote-based, dolichol-containing substrates.","May link the O-antigen tetrasaccharide units into long chains, giving rise to typical smooth LPS.",Yes,Yes,Maybe,Yes,Yes,Yes,GO:0016740,,,,GO:0016757,,,,,0.8145,,1,0.8145,0.6398,yes
WZY_ECOLX,Q58YW1,ProtT3,Bacteria,446,"Polymerase involved in the biosynthesis of the lipopolysaccharide (LPS). Catalyzes the polymerization of the O-antigen repeat units on the periplasmic face of the inner membrane, leading to the formation of the lipid-linked O- antigen molecule. In vitro, shows a preference for bacteria-based, undecaprenyl-containing substrates rather than eukaryote-based, dolichol-containing substrates.",Involved in the biosynthesis of the O-antigen component of lipopolysaccharide. Cell inner membrane; Multi-pass membrane protein,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016740,,,,,,,,,,,0,,0.6398,yes
WZY_ECOLX,Q58YW1,ProtTale,Bacteria,446,"Polymerase involved in the biosynthesis of the lipopolysaccharide (LPS). Catalyzes the polymerization of the O-antigen repeat units on the periplasmic face of the inner membrane, leading to the formation of the lipid-linked O- antigen molecule. In vitro, shows a preference for bacteria-based, undecaprenyl-containing substrates rather than eukaryote-based, dolichol-containing substrates.",Required for the biosynthesis of type 1 capsular polysaccharide.,Maybe,No,Maybe,Maybe,Maybe,not-Yes,GO:0016740,,,,,,,,,,,0,,0.6398,yes
WZY_ECOLX,Q58YW1,Protein2Text,Bacteria,446,"Polymerase involved in the biosynthesis of the lipopolysaccharide (LPS). Catalyzes the polymerization of the O-antigen repeat units on the periplasmic face of the inner membrane, leading to the formation of the lipid-linked O- antigen molecule. In vitro, shows a preference for bacteria-based, undecaprenyl-containing substrates rather than eukaryote-based, dolichol-containing substrates.","This protein is involved in the biosynthesis of a type of antibiotic, specifically the production of tetracyclines. It is likely to be a part of the biosynthetic pathway, possibly involved in the assembly or modification of the antibiotic molecule.",No,No,No,No,No,not-Yes,GO:0016740,,,,,,,,,,,0,,0.6398,yes
WZY_ECOLX,Q58YW1,Reference,Bacteria,446,"Polymerase involved in the biosynthesis of the lipopolysaccharide (LPS). Catalyzes the polymerization of the O-antigen repeat units on the periplasmic face of the inner membrane, leading to the formation of the lipid-linked O- antigen molecule. In vitro, shows a preference for bacteria-based, undecaprenyl-containing substrates rather than eukaryote-based, dolichol-containing substrates.","Polymerase involved in the biosynthesis of the lipopolysaccharide (LPS). Catalyzes the polymerization of the O-antigen repeat units on the periplasmic face of the inner membrane, leading to the formation of the lipid-linked O- antigen molecule. In vitro, shows a preference for bacteria-based, undecaprenyl-containing substrates rather than eukaryote-based, dolichol-containing substrates.",,,,,,,GO:0016740,GO:0016757,GO:0016757,GO:0016757,GO:0016757,GO:0016757,0.8145,0.8145,0.8145,0.8145,0.8145,5,0.8145,0.6398,yes
YICC_SALTY,Q7CPH3,ESM2Text,Bacteria,287,Probably a ssRNA endonuclease.,Plays a role in the resistance to late blight (Phytophthora infestans).,No,No,No,No,No,not-Yes,GO:0016891,,,,,,,,,,,0,,0.3709,no
YICC_SALTY,Q7CPH3,Prot2Text,Bacteria,287,Probably a ssRNA endonuclease.,"Under low constitutive environmental conditions, represses the transcription of several genes including itself, alkA, alkB, alkC, aidB, aidD and aidE.",No,No,No,No,No,not-Yes,GO:0016891,,GO:0003700,GO:0003700,,GO:0003700,,0.1127,0.1127,,0.1127,3,0.1127,0.3709,no
YICC_SALTY,Q7CPH3,ProtT3,Bacteria,287,Probably a ssRNA endonuclease.,Belongs to the UPF0758 family,Vague,Vague,No,Vague,Vague,not-Yes,GO:0016891,,,,,,,,,,,0,,0.3709,no
YICC_SALTY,Q7CPH3,ProtTale,Bacteria,287,Probably a ssRNA endonuclease.,Necessary for high-affinity ATP-dependent protein binding to histidine-containing proteins.,No,No,No,No,No,not-Yes,GO:0016891,,,,,,,,,,,0,,0.3709,no
YICC_SALTY,Q7CPH3,Protein2Text,Bacteria,287,Probably a ssRNA endonuclease.,"The molecular function of this protein is a methyltransferase. More specifically, it is a peptidyl-tRNA hydrolase-like protein that acts as a methyltransferase.
 
 The protein is involved in the biosynthesis of the nucleoside triphosphate cofactors, which are essential for various cellular processes. It catalyzes the transfer of a methyl group to a nucleotide, playing a crucial role in maintaining the balance of these cofactors.
 
 The protein is also involved in the regulation of the expression of certain genes, specifically in the regulation of the expression of the RNA polymerase subunit rpoD. It does so by methylating the RNA polymerase subunit rpoD, which is necessary for the expression of certain genes.
 
 The protein is a part of the RNA degradosome, a complex of enzymes that degrades RNA. It is involved in the degradation of mRNA and rRNA, and it is also involved in the regulation of the expression of certain genes.
 
 The protein is also involved in the regulation of the expression of certain genes, specifically in the regulation of the expression of the ribosomal protein gene rpsA. It does so by methylating the ribosomal protein gene rpsA, which is necessary for the expression of certain genes.
 
 The protein is also involved in the regulation of the expression of certain genes, specifically in the regulation of the expression of the ribosomal protein gene rpsB. It does so by methylating the ribosomal protein gene rpsB, which is necessary for the expression of certain genes.
 
 The protein is also involved in the regulation of the expression of certain genes, specifically in the regulation of the expression of the ribosomal protein gene rpsC. It does so by methylating the ribosomal protein gene rpsC, which is necessary for the expression of certain genes.
 
 The protein is also involved in the regulation of the expression of certain genes, specifically in the regulation of the expression of the ribosomal protein gene rpsD. It does so by methylating the ribosomal protein gene rpsD, which is necessary for the expression of certain genes.
 
 The protein is also involved in the regulation of the expression of certain genes, specifically in the regulation of the expression of the ribosomal protein gene rpsE. It does so by methylating the ribosomal protein gene rpsE, which is necessary for the expression of certain genes.
 
 The protein is also involved in the regulation of the expression of certain genes, specifically in",No,No,No,No,No,not-Yes,GO:0016891,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.1801,0.1801,0.1801,0.1801,0.1801,5,0.1801,0.3709,no
YICC_SALTY,Q7CPH3,Reference,Bacteria,287,Probably a ssRNA endonuclease.,Probably a ssRNA endonuclease.,,,,,,,GO:0016891,GO:0004521,GO:0004521,,GO:0004521,GO:0004521,0.7967,0.7967,,0.7967,0.7967,4,0.7967,0.3709,no
RSMA_SACS2,Q7LXK6,ESM2Text,Archaea,194,Probably dimethylates adenosine 1475 in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S ribosomal particle; the expected dimethylation of A1476 was not seen (Probable).,"Antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the toxic effect of cognate toxin YutE3, but no other RelE or ParE toxin.",No,No,No,No,No,not-Yes,GO:0003723; GO:0000179,,,,,,,,,,,0,,0.4906,no
RSMA_SACS2,Q7LXK6,Prot2Text,Archaea,194,Probably dimethylates adenosine 1475 in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S ribosomal particle; the expected dimethylation of A1476 was not seen (Probable).,Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.,Yes,Yes,Maybe,Yes,Yes,Yes,GO:0003723; GO:0000179,GO:0008649,GO:0008649,GO:0008649,GO:0008649,GO:0008649,0.5758,0.5758,0.5758,0.5758,0.5758,5,0.5758,0.4906,no
RSMA_SACS2,Q7LXK6,ProtT3,Archaea,194,Probably dimethylates adenosine 1475 in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S ribosomal particle; the expected dimethylation of A1476 was not seen (Probable).,Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. Cytoplasm. Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. RsmA subfamily,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003723; GO:0000179,GO:0008649,GO:0008649,GO:0008173,GO:0008173,GO:0008173,0.5758,0.5758,0.4848,0.4848,0.4848,5,0.5212,0.4906,no
RSMA_SACS2,Q7LXK6,ProtTale,Archaea,194,Probably dimethylates adenosine 1475 in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S ribosomal particle; the expected dimethylation of A1476 was not seen (Probable).,Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.,Yes,Yes,Yes,Yes,Yes,Yes,GO:0003723; GO:0000179,GO:0008168; GO:0019843,GO:0008649,GO:0008168; GO:0019843,GO:0008649,GO:0008649,0.6708,0.5758,0.6708,0.5758,0.5758,5,0.6138,0.4906,no
RSMA_SACS2,Q7LXK6,Protein2Text,Archaea,194,Probably dimethylates adenosine 1475 in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S ribosomal particle; the expected dimethylation of A1476 was not seen (Probable).,"The molecular function of this protein is a methyltransferase. It is a part of the DNA repair mechanism, specifically the base excision repair (BER) pathway.",No,No,Maybe,No,No,not-Yes,GO:0003723; GO:0000179,GO:0008168,GO:0008168,GO:0008168,GO:0008168,GO:0008168,0.382,0.382,0.382,0.382,0.382,5,0.382,0.4906,no
RSMA_SACS2,Q7LXK6,Reference,Archaea,194,Probably dimethylates adenosine 1475 in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S ribosomal particle; the expected dimethylation of A1476 was not seen (Probable).,Probably dimethylates adenosine 1475 in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S ribosomal particle; the expected dimethylation of A1476 was not seen (Probable).,,,,,,,GO:0003723; GO:0000179,GO:0008649,GO:0008168,,GO:0008649,GO:0008649,0.5758,0.382,,0.5758,0.5758,4,0.5273,0.4906,no
STC3_RHIME,Q92ZP7,ESM2Text,Bacteria,230,"Reductase involved in the catabolism of stachydrine (L- proline betaine), a source of carbon and nitrogen. Part of a Rieske-type oxygenase system that catalyzes the demethylation of stachydrine to produce N-methyl-L-proline (monomethylproline). This subunit is probably involved in the transfer of electrons from NAD(P)H to the catalytic subunit Stc2 (Probable).",Involved in the degradation of substituted flavins by NADH-dependent reduction of the flavin ring. NADH acts as an electron donor to reduce FAD by FAD without directly affecting FMN. Subunit A is reduced FAD with NADPH and rubredoxin as electron donors. Both subunits A and B bind FAD with high affinity.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0010181; GO:0042602,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.3959,0.3959,0.3959,0.3959,0.3959,5,0.3959,0.2054,no
STC3_RHIME,Q92ZP7,Prot2Text,Bacteria,230,"Reductase involved in the catabolism of stachydrine (L- proline betaine), a source of carbon and nitrogen. Part of a Rieske-type oxygenase system that catalyzes the demethylation of stachydrine to produce N-methyl-L-proline (monomethylproline). This subunit is probably involved in the transfer of electrons from NAD(P)H to the catalytic subunit Stc2 (Probable).",Reductase component of the 4-hydroxyphenylacetate (HPA) 3-hydroxylase. Catalyzes the reduction of FAD by NADH. The reduced flavin is then transferred to the oxygenase component HpaB. Is also able to reduce FMN and riboflavin.,Maybe,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0010181; GO:0042602,GO:0016491,GO:0008752,GO:0016651,GO:0016491,GO:0016491,0.3959,0.4454,0.316,0.3959,0.3959,5,0.3898,0.2054,no
STC3_RHIME,Q92ZP7,ProtT3,Bacteria,230,"Reductase involved in the catabolism of stachydrine (L- proline betaine), a source of carbon and nitrogen. Part of a Rieske-type oxygenase system that catalyzes the demethylation of stachydrine to produce N-methyl-L-proline (monomethylproline). This subunit is probably involved in the transfer of electrons from NAD(P)H to the catalytic subunit Stc2 (Probable).",Belongs to the non-flavoprotein flavin reductase family,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0010181; GO:0042602,GO:0008752,GO:0008752,,GO:0008752,GO:0008752,0.4454,0.4454,,0.4454,0.4454,4,0.4454,0.2054,no
STC3_RHIME,Q92ZP7,ProtTale,Bacteria,230,"Reductase involved in the catabolism of stachydrine (L- proline betaine), a source of carbon and nitrogen. Part of a Rieske-type oxygenase system that catalyzes the demethylation of stachydrine to produce N-methyl-L-proline (monomethylproline). This subunit is probably involved in the transfer of electrons from NAD(P)H to the catalytic subunit Stc2 (Probable).",Converts L-glutamate to L-glutamate 5-semialdehyde.,Maybe,Maybe,No,Maybe,Maybe,not-Yes,GO:0010181; GO:0042602,GO:0004350,GO:0004350,GO:0016491,GO:0016491,GO:0004350,0.2192,0.2192,0.3959,0.3959,0.2192,5,0.2899,0.2054,no
STC3_RHIME,Q92ZP7,Protein2Text,Bacteria,230,"Reductase involved in the catabolism of stachydrine (L- proline betaine), a source of carbon and nitrogen. Part of a Rieske-type oxygenase system that catalyzes the demethylation of stachydrine to produce N-methyl-L-proline (monomethylproline). This subunit is probably involved in the transfer of electrons from NAD(P)H to the catalytic subunit Stc2 (Probable).",The molecular function of this protein is an oxidoreductase.,Vague,Vague,Vague,Vague,Vague,not-Yes,GO:0010181; GO:0042602,GO:0016491,GO:0016491,GO:0016491,,GO:0016491,0.3959,0.3959,0.3959,,0.3959,4,0.3959,0.2054,no
STC3_RHIME,Q92ZP7,Reference,Bacteria,230,"Reductase involved in the catabolism of stachydrine (L- proline betaine), a source of carbon and nitrogen. Part of a Rieske-type oxygenase system that catalyzes the demethylation of stachydrine to produce N-methyl-L-proline (monomethylproline). This subunit is probably involved in the transfer of electrons from NAD(P)H to the catalytic subunit Stc2 (Probable).","Reductase involved in the catabolism of stachydrine (L- proline betaine), a source of carbon and nitrogen. Part of a Rieske-type oxygenase system that catalyzes the demethylation of stachydrine to produce N-methyl-L-proline (monomethylproline). This subunit is probably involved in the transfer of electrons from NAD(P)H to the catalytic subunit Stc2 (Probable).",,,,,,,GO:0010181; GO:0042602,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.3959,0.3959,0.3959,0.3959,0.3959,5,0.3959,0.2054,no
TPASE_PBCV1,Q98500,ESM2Text,Viruses,193,Catalyzes the first stes of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end.,PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing.,No,No,No,No,No,not-Yes,GO:0140818; GO:0004651,GO:0003755,GO:0003755,GO:0003755,GO:0003755,GO:0003755,0.2075,0.2075,0.2075,0.2075,0.2075,5,0.2075,0.304,no
TPASE_PBCV1,Q98500,Prot2Text,Viruses,193,Catalyzes the first stes of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end.,PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing.,No,No,No,No,No,not-Yes,GO:0140818; GO:0004651,GO:0003755,GO:0003755,GO:0003755,GO:0003755,GO:0003755,0.2075,0.2075,0.2075,0.2075,0.2075,5,0.2075,0.304,no
TPASE_PBCV1,Q98500,ProtT3,Viruses,193,Catalyzes the first stes of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end.,"Non-catalytic component of the spliceosome, which catalyzes the first step in pre-mRNA splicing. Transfers the 5'-hydroxyl group of ATP to the 5'-splice site of pre-mRNA to initiate splicing (By similarity). Nucleus. Belongs to the eukaryotic/archaeal ATP-dependent RNA helicase family",No,No,No,No,No,not-Yes,GO:0140818; GO:0004651,GO:0004386; GO:0005524; GO:0003723,GO:0003724; GO:0016887,,GO:0003724; GO:0005524,GO:0003724; GO:0005524,0.1974,0.4254,,0.2351,0.2351,4,0.2732,0.304,no
TPASE_PBCV1,Q98500,ProtTale,Viruses,193,Catalyzes the first stes of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end.,"Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape.",No,No,No,No,No,not-Yes,GO:0140818; GO:0004651,GO:0003678,,GO:0003677; GO:0004386,GO:0003678; GO:0005524,GO:0003678; GO:0005524,0.2163,,0.2334,0.1756,0.1756,4,0.2002,0.304,no
TPASE_PBCV1,Q98500,Protein2Text,Viruses,193,Catalyzes the first stes of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end.,"The molecular function of this protein is not explicitly stated in the provided information. However, based on its name and the context, it can be inferred that this protein is involved in DNA or RNA metabolism, possibly as a component of the DNA or RNA replication machinery.

Given the name of the protein and its involvement in the replication process, a likely molecular function of this protein is to act as a helicase, which is an enzyme that unwinds double-stranded DNA or RNA into single strands. Helicases play a crucial role in DNA replication, repair, and recombination, as well as in RNA metabolism.

However, without further information, it is difficult to determine the exact molecular function of this protein. Further research or additional context would be necessary to confirm its specific function.",Vague,Vague,Vague,Vague,No,not-Yes,GO:0140818; GO:0004651,,GO:0004386; GO:0005524,GO:0004386,GO:0004386,GO:0004386,,0.2187,0.2738,0.2738,0.2738,4,0.26,0.304,no
TPASE_PBCV1,Q98500,Reference,Viruses,193,Catalyzes the first stes of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end.,Catalyzes the first stes of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end.,,,,,,,GO:0140818; GO:0004651,GO:0016787,GO:0004651,GO:0004651,GO:0004651,GO:0004651,0.5127,0.747,0.747,0.747,0.747,5,0.7001,0.304,no
PNBA_PSEPU,Q9FD36,ESM2Text,Bacteria,227,Nitroreductase involved in the degradation of nitroaromatic compounds. Catalyzes the conversion of 4- nitrobenzoate to 4-hydroxylaminobenzoate. Required for the catabolism of 4-nitrotoluene.,Involved in the biosynthesis of the anthracyclines carminomycin and daunorubicin (daunomycin) which are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the reduction of the nitro group at the C-2 position of aklavinone to yield aklavinone. It can also use NAD or NADP but with a lower activity.,No,Maybe,Maybe,Maybe,Maybe,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016491,1.0,1.0,1.0,1.0,1.0,5,1.0,0.2067,no
PNBA_PSEPU,Q9FD36,Prot2Text,Bacteria,227,Nitroreductase involved in the degradation of nitroaromatic compounds. Catalyzes the conversion of 4- nitrobenzoate to 4-hydroxylaminobenzoate. Required for the catabolism of 4-nitrotoluene.,"Involved in the biosynthesis of the antibiotic 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA) and its derivatives. Catalyzes the reduction of nitroaromatic compounds such as 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA) to yield the corresponding hydroxylamine derivatives. In vitro, can use various nitroaromatic compounds, such as 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA), 3-chloro-4-hydroxydodecanoic acid (CDA), 3-chloro-4-hydroxydodecanoic acid (CDA), 3-hydroxydodecanoyl-CoA (HDA-CoA), 3-hydroxydodecanoyl-CoA (HDA-CoA), 3,4-dihydroxy-3,4-dihydroxybenzoic acid (DHB-CoA), 3,4-dihydroxy-4",Maybe,Maybe,Maybe,Yes,Yes,not-Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016657,GO:0016657,GO:0016491,1.0,1.0,0.0,0.0,1.0,5,0.6,0.2067,no
PNBA_PSEPU,Q9FD36,ProtT3,Bacteria,227,Nitroreductase involved in the degradation of nitroaromatic compounds. Catalyzes the conversion of 4- nitrobenzoate to 4-hydroxylaminobenzoate. Required for the catabolism of 4-nitrotoluene.,Catalyzes the reduction of nitroaromatic compounds to the corresponding amines. Belongs to the nitroreductase family,Yes,Yes,Yes,Yes,Yes,Yes,GO:0016491,GO:0016491,GO:0016491,GO:0016491,GO:0016657,GO:0016657,1.0,1.0,1.0,0.0,0.0,5,0.6,0.2067,no
PNBA_PSEPU,Q9FD36,ProtTale,Bacteria,227,Nitroreductase involved in the degradation of nitroaromatic compounds. Catalyzes the conversion of 4- nitrobenzoate to 4-hydroxylaminobenzoate. Required for the catabolism of 4-nitrotoluene.,"Component of the naphthalene dioxygenase system, which catalyzes the O2-dependent cleavage of the C-C bond in the naphthalene ring system to yield catechol as a product. In vitro, can also catalyze the O2-dependent cleavage of 1,4-naphthoquinone (1,4-NQ) and 2,3-dihydroxynaphthalene (2,3-DHN), but not of 1,2-dihydroxynaphthalene (1,2-DHN), 1,3-dihydroxynaphthalene (1,3-DHN), 1",No,No,No,No,No,not-Yes,GO:0016491,GO:0016701,GO:0016701,GO:0016702,GO:0051213,GO:0016702,0.8145,0.8145,0.6062,0.8145,0.6062,5,0.7312,0.2067,no
PNBA_PSEPU,Q9FD36,Protein2Text,Bacteria,227,Nitroreductase involved in the degradation of nitroaromatic compounds. Catalyzes the conversion of 4- nitrobenzoate to 4-hydroxylaminobenzoate. Required for the catabolism of 4-nitrotoluene.,"This protein is likely to have a molecular function related to catalyzing the transfer of a group, as it is described as an enzyme (specifically a transferase) that catalyzes the transfer of a group.",Vague,Vague,No,No,No,not-Yes,GO:0016491,GO:0016740,,,,,0.5902,,,,,1,0.5902,0.2067,no
PNBA_PSEPU,Q9FD36,Reference,Bacteria,227,Nitroreductase involved in the degradation of nitroaromatic compounds. Catalyzes the conversion of 4- nitrobenzoate to 4-hydroxylaminobenzoate. Required for the catabolism of 4-nitrotoluene.,Nitroreductase involved in the degradation of nitroaromatic compounds. Catalyzes the conversion of 4- nitrobenzoate to 4-hydroxylaminobenzoate. Required for the catabolism of 4-nitrotoluene.,,,,,,,GO:0016491,GO:0016657,GO:0016491,GO:0016491,GO:0016491,GO:0016491,0.0,1.0,1.0,1.0,1.0,5,0.8,0.2067,no