interpro_id
string
interpro_numeric_id
int64
name
string
short_name
string
entry_type
string
protein_count
int64
is_llm
bool
is_llm_reviewed
bool
abstract
string
go_ids
list
go_terms
list
go_categories
list
go_count
int64
member_databases
list
member_accessions
list
member_names
list
member_protein_counts
list
member_count
int64
external_databases
list
external_accessions
list
external_xrefs
list
external_xref_count
int64
pdb_ids
list
structure_count
int64
publication_ids
list
pubmed_ids
list
publication_titles
list
publication_years
list
publication_count
int64
parent_ids
list
child_ids
list
parent_count
int64
child_count
int64
tree_depth
float64
taxonomy_names
list
taxonomy_protein_counts
list
taxonomy_count
int64
key_species_names
list
key_species_protein_counts
list
key_species_count
int64
in_entry_list
bool
entry_list_type
string
entry_list_name
string
names_dat_name
string
short_names_dat_name
string
split_bucket
int64
IPR003689
3,689
Zinc/iron permease
ZIP
Family
63,957
false
false
The ZIP family consists of zinc transport proteins and many putative metal transporters found in al cellular organisms, including the Arabidopsis thaliana ZIP protein family which is responsible for zinc uptake in the plant [ ]. ZIP proteins play essential roles in metal metabolism/homeostasis and are widely involved i...
[ "GO:0046873", "GO:0030001", "GO:0055085", "GO:0016020" ]
[ "metal ion transmembrane transporter activity", "metal ion transport", "transmembrane transport", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "cellular_component" ]
4
[ "PFAM" ]
[ "PF02535" ]
[ "Zip" ]
[ 63957 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-442380", "R-CEL-442380", "R-DDI-442380", "R-DME-442380", "R-DRE-442380", "R-HSA-442380", "R-HSA-5619088", "R-MMU-442380", "R-PFA-442380", "R-RNO-442380", "R-SCE-442380", "R-SPO-442380", "R-SSC-442380", "R-XTR-442380" ]
[ "REACTOME:R-BTA-442380", "REACTOME:R-CEL-442380", "REACTOME:R-DDI-442380", "REACTOME:R-DME-442380", "REACTOME:R-DRE-442380", "REACTOME:R-HSA-442380", "REACTOME:R-HSA-5619088", "REACTOME:R-MMU-442380", "REACTOME:R-PFA-442380", "REACTOME:R-RNO-442380", "REACTOME:R-SCE-442380", "REACTOME:R-SPO-44...
14
[ "5tsa", "5tsb", "6pgi", "7z6m", "7z6n", "8czj", "8ght", "8j1m" ]
8
[ "PUB00008168", "PUB00103882", "PUB00103883", "PUB00103884", "PUB00153751" ]
[ "9618566", "31914589", "28875161", "12032886", "25257508" ]
[ "Identification of a family of zinc transporter genes from Arabidopsis that respond to zinc deficiency.", "Asymmetric functions of a binuclear metal center within the transport pathway of a human zinc transporter ZIP4.", "Crystal structures of a ZIP zinc transporter reveal a binuclear metal center in the transp...
[ 1998, 2020, 2017, 2002, 2014 ]
5
[]
[ "IPR004698", "IPR023498", "IPR045891" ]
0
3
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 976, 15252, 47405, 324 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 81, 18, 56, 75, 1, 65, 26, 8, 36, 57, 5, 3, 69 ]
13
true
Family
Zinc/iron permease
Zinc/iron permease
ZIP
1
IPR003690
3,690
Transcription termination factor, mitochondrial/chloroplastic
MTERF
Family
27,276
false
false
This entry represents the mitochondrial/chloroplastic transcription termination factors (MTERFs). In humans, four MTERFs have been identified (MTERF1-4). MTERF1 was first identified as a factor responsible for terminating heavy strand transcription at a specific site at the leu-tRNA, thereby modulating the ratio of mit...
[ "GO:0003676", "GO:0043231" ]
[ "nucleic acid binding", "intracellular membrane-bounded organelle" ]
[ "molecular_function", "cellular_component" ]
2
[ "PFAM", "PANTHER", "PANTHER", "SMART" ]
[ "PF02536", "PTHR13068", "PTHR15437", "SM00733" ]
[ "mTERF", "", "", "Mterf" ]
[ 26400, 22625, 2033, 24744 ]
4
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-DME-163316", "R-DME-5205685", "R-HSA-163316", "R-HSA-2151201", "R-HSA-5205685", "R-HSA-6793080", "R-HSA-9937008", "R-MMU-163316", "R-MMU-5205685", "R-RNO-163316", "R-RNO-5205685" ]
[ "REACTOME:R-DME-163316", "REACTOME:R-DME-5205685", "REACTOME:R-HSA-163316", "REACTOME:R-HSA-2151201", "REACTOME:R-HSA-5205685", "REACTOME:R-HSA-6793080", "REACTOME:R-HSA-9937008", "REACTOME:R-MMU-163316", "REACTOME:R-MMU-5205685", "REACTOME:R-RNO-163316", "REACTOME:R-RNO-5205685" ]
11
[ "3m66", "3mva", "3mvb", "3n6s", "3n7q", "4fp9", "4fzv", "5cky", "5co0", "5crj", "5crk", "6z1p", "7o9k", "7o9m", "7odr", "7ods", "7odt", "7of0", "7of3", "7of5", "7of7", "7oic", "7pd3", "8pk0", "8qsj", "9e9c", "9hcf", "9hcg", "9hch" ]
29
[ "PUB00071547", "PUB00071548", "PUB00071549", "PUB00071550" ]
[ "20550934", "19366610", "2752429", "17884915" ]
[ "Helix unwinding and base flipping enable human MTERF1 to terminate mitochondrial transcription.", "The MTERF family proteins: mitochondrial transcription regulators and beyond.", "Termination of transcription in human mitochondria: identification and purification of a DNA binding protein factor that promotes t...
[ 2010, 2009, 1989, 2007 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "marine sediment metagenome" ]
[ 2, 16, 27246, 12 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 169, 2, 7, 4, 17, 10, 95, 13, 117 ]
9
true
Family
Transcription termination factor, mitochondrial/chloroplastic
Transcription termination factor, mitochondrial/chloroplastic
MTERF
8
IPR003691
3,691
Fluoride-specific ion channel FluC
FluC
Family
33,875
false
false
FluC, also known as CrcB, is an integral membrane protein that acts as an efflux transporter which confers resistance to fluoride ion, thus reducing its toxicity [ , , ]. It is highly specific for fluoride ions and cannot transport chloride ions [ ]. Over expression in E. coli leads to camphor resistance [ ].
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "HAMAP", "PFAM", "PANTHER", "NCBIFAM" ]
[ "MF_00454", "PF02537", "PTHR28259", "TIGR00494" ]
[ "FluC", "CRCB", "", "crcB" ]
[ 29805, 33813, 31228, 17882 ]
4
[]
[]
[]
0
[ "5a40", "5a43", "5kbn", "5kom", "5nkq", "6b24", "6b2a", "6b2b", "6b2d", "6bqo", "6bx4", "6bx5", "6x58", "7kk8", "7kk9", "7kka", "7kkb", "7kkr" ]
18
[ "PUB00008171", "PUB00068778", "PUB00106866", "PUB00153320", "PUB00153321" ]
[ "8844142", "22194412", "26344196", "23991286", "34250906" ]
[ "Overproduction of three genes leads to camphor resistance and chromosome condensation in Escherichia coli.", "Widespread genetic switches and toxicity resistance proteins for fluoride.", "Crystal structures of a double-barrelled fluoride ion channel.", "A family of fluoride-specific ion channels with dual-to...
[ 1996, 2012, 2015, 2013, 2021 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences", "uncultured Caudovirales phage" ]
[ 977, 29178, 3251, 468, 1 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 4, 1, 1, 2, 2, 2, 3 ]
7
true
Family
Fluoride-specific ion channel FluC
Fluoride-specific ion channel FluC
FluC
4
IPR003692
3,692
Hydantoinase B/oxoprolinase
Hydantoinase_B
Domain
22,326
false
false
An appreciable fraction of the sulphur present in mammals occurs in the form of glutathione. The synthesis of glutathione and its utilization take place by the reactions of the gamma-glutamyl cycle, which include those catalysed by gamma-glutamylcysteine and glutathione synthetases, gamma-glutamyl transpeptidase, cyste...
[ "GO:0003824" ]
[ "catalytic activity" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF02538" ]
[ "Hydantoinase_B" ]
[ 22326 ]
1
[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GenProp1664", "R-DDI-174403", "R-HSA-174403", "R-HSA-5578998", "R-MMU-174403", "R-RNO-174403", "R-SCE-174403", "R-SPO-174403" ]
[ "GP:GenProp1664", "REACTOME:R-DDI-174403", "REACTOME:R-HSA-174403", "REACTOME:R-HSA-5578998", "REACTOME:R-MMU-174403", "REACTOME:R-RNO-174403", "REACTOME:R-SCE-174403", "REACTOME:R-SPO-174403" ]
8
[ "5l9w", "5m45", "5svb", "5svc", "6yra", "9h03" ]
6
[ "PUB00008174" ]
[ "45011" ]
[ "New aspects of glutathione metabolism and translocation in mammals." ]
[ 1979 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 732, 13945, 7153, 496 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 5, 3, 1, 2, 3, 4, 1, 6, 6, 1, 2, 2 ]
12
true
Domain
Hydantoinase B/oxoprolinase
Hydantoinase B/oxoprolinase
Hydantoinase_B
5
IPR003694
3,694
NAD(+) synthetase
NAD_synthase
Family
36,209
false
false
This entry represents NAD(+) synthetases, including glutamine-dependent NAD(+) synthetases and NH(3)-dependent NAD(+) synthetases. NAD+ is involved electron transport and redox reactions and in DNA ligation and protein ADP-ribosylation. In yeast and most other organisms, NAD is generated through the de novo pathway and...
[ "GO:0003952", "GO:0004359", "GO:0009435", "GO:0005737" ]
[ "NAD+ synthase (glutamine-hydrolyzing) activity", "glutaminase activity", "NAD+ biosynthetic process", "cytoplasm" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PANTHER", "NCBIFAM", "CDD" ]
[ "PTHR23090", "TIGR00552", "cd00553" ]
[ "", "nadE", "NAD_synthase" ]
[ 36094, 32042, 35034 ]
3
[ "EC", "GP", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "6.3.1.5", "GenProp0057", "PWY-7761", "PWY-8277", "PWY-8352", "R-BTA-196807", "R-DDI-196807", "R-DME-196807", "R-HSA-196807", "R-MMU-196807", "R-RNO-196807", "R-SCE-196807", "R-SPO-196807" ]
[ "EC:6.3.1.5", "GP:GenProp0057", "METACYC:PWY-7761", "METACYC:PWY-8277", "METACYC:PWY-8352", "REACTOME:R-BTA-196807", "REACTOME:R-DDI-196807", "REACTOME:R-DME-196807", "REACTOME:R-HSA-196807", "REACTOME:R-MMU-196807", "REACTOME:R-RNO-196807", "REACTOME:R-SCE-196807", "REACTOME:R-SPO-196807" ]
13
[ "1ee1", "1fyd", "1ifx", "1ih8", "1kqp", "1nsy", "1wxe", "1wxf", "1wxg", "1wxh", "1wxi", "1xng", "1xnh", "2e18", "2nsy", "2pz8", "2pza", "2pzb", "3dla", "3dpi", "3fiu", "3hmq", "3ilv", "3n05", "3p52", "3q4g", "3sdb", "3seq", "3sez", "3syt", "3szg", "4f4h"...
43
[ "PUB00070122", "PUB00070123", "PUB00070124" ]
[ "12898714", "7890752", "12771147" ]
[ "Saccharomyces cerevisiae QNS1 codes for NAD(+) synthetase that is functionally conserved in mammals.", "The outB gene of Bacillus subtilis codes for NAD synthetase.", "Eukaryotic NAD+ synthetase Qns1 contains an essential, obligate intramolecular thiol glutamine amidotransferase domain related to nitrilase." ]
[ 2003, 1995, 2003 ]
3
[]
[ "IPR014445", "IPR022926" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1259, 28122, 6047, 19, 762 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 2, 3, 1, 2, 1, 9, 4, 1, 3, 9, 1, 1, 20 ]
13
true
Family
NAD(+) synthetase
NAD(+) synthetase
NAD_synthase
5
IPR003695
3,695
Ppx/GppA phosphatase, N-terminal
Ppx_GppA_N
Domain
36,131
false
false
This entry represents the N-terminal domain of Exopolyphosphate phosphatase (Ppx) and guanosine pentaphosphate phosphatase (GppA) , which belong to the sugar kinase/actin/hsp70 superfamily [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF02541" ]
[ "Ppx-GppA" ]
[ 36131 ]
1
[ "EC", "GP", "GP" ]
[ "3.6.1.40", "GenProp0840", "GenProp1755" ]
[ "EC:3.6.1.40", "GP:GenProp0840", "GP:GenProp1755" ]
3
[ "1t6c", "1t6d", "1u6z", "2flo", "2j4r", "3cer", "3hi0", "3mdq", "6pbz", "6pc0", "6pc1", "6pc2", "6pc3", "7epq", "8gty", "8gtz", "8jgo", "8jgp", "8jgq", "8jgr", "8jgt", "8jgu", "8jgw", "8jgx" ]
24
[ "PUB00008176" ]
[ "8212131" ]
[ "Exopolyphosphate phosphatase and guanosine pentaphosphate phosphatase belong to the sugar kinase/actin/hsp 70 superfamily." ]
[ 1993 ]
1
[]
[ "IPR022371" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 168, 33205, 2203, 555 ]
4
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)" ]
[ 12, 2, 1, 1 ]
4
true
Domain
Ppx/GppA phosphatase, N-terminal
Ppx/GppA phosphatase, N-terminal
Ppx_GppA_N
4
IPR003696
3,696
Carbamoyltransferase
Carbtransf_dom
Domain
8,259
false
false
This domain is found in NodU from Rhizobium, CmcH from Nocardia lactamdurans and the bifunctional carbamoyltransferase TobZ from Streptoalloteichus tenebrarius. NodU a Rhizobium nodulation protein involved in the synthesis of nodulation factors has 6-O-carbamoyltransferase-like activity [ ]. CmcH is involved in cephamy...
[ "GO:0003824", "GO:0009058" ]
[ "catalytic activity", "biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF02543" ]
[ "Carbam_trans_N" ]
[ 8259 ]
1
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "2.1.3.-", "PWY-5", "PWY-7693", "PWY-7694", "PWY-8039", "PWY-8344" ]
[ "EC:2.1.3.-", "METACYC:PWY-5", "METACYC:PWY-7693", "METACYC:PWY-7694", "METACYC:PWY-8039", "METACYC:PWY-8344" ]
6
[ "3ven", "3veo", "3ver", "3ves", "3vet", "3vew", "3vex", "3vez", "3vf2", "3vf4", "7vx0", "7vyj", "7vyo", "7vyp", "7vzn", "7vzq", "7vzu", "7vzy", "7vzz", "7xb6", "8hiu", "9s2t" ]
22
[ "PUB00008177", "PUB00008178", "PUB00058263" ]
[ "7559434", "7557411", "22383337" ]
[ "Involvement of nodS in N-methylation and nodU in 6-O-carbamoylation of Rhizobium sp. NGR234 nod factors.", "Characterization of the cmcH genes of Nocardia lactamdurans and Streptomyces clavuligerus encoding a functional 3'-hydroxymethylcephem O-carbamoyltransferase for cephamycin biosynthesis.", "The O-Carbamo...
[ 1995, 1995, 2012 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]
[ 223, 7521, 39, 216, 260 ]
5
[]
[]
0
true
Domain
Carbamoyltransferase
Carbamoyltransferase
Carbtransf_dom
1
IPR003697
3,697
Nucleoside triphosphate pyrophosphatase Maf-like protein
Maf-like
Family
38,606
false
false
The Maf protein of Bacillus subtilis shares substantial amino acid sequence identity with Escherichia coli YhdE (previously known as OrfE) [ ]. Maf-like proteins are conserved in bacteria, archaea, and eukaryotes. Maf proteins have been implicated in cell division arrest [ ]. It has also been proposed that they belong ...
[ "GO:0047429" ]
[ "nucleoside triphosphate diphosphatase activity" ]
[ "molecular_function" ]
1
[ "HAMAP", "PFAM", "PIRSF", "PANTHER", "NCBIFAM", "CDD" ]
[ "MF_00528", "PF02545", "PIRSF006305", "PTHR43213", "TIGR00172", "cd00555" ]
[ "Maf", "Maf", "Maf", "", "maf", "Maf" ]
[ 36689, 38583, 34035, 38203, 32469, 34190 ]
6
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "3.6.1.9", "PWY-6545", "PWY-7184", "PWY-7187", "PWY-7206", "PWY-7821" ]
[ "EC:3.6.1.9", "METACYC:PWY-6545", "METACYC:PWY-7184", "METACYC:PWY-7187", "METACYC:PWY-7206", "METACYC:PWY-7821" ]
6
[ "1ex2", "1exc", "2amh", "2p5x", "4heb", "4jhc", "4lu1", "4oo0", "4p0e", "4p0u", "6xi4", "6xi5" ]
12
[ "PUB00008179", "PUB00079689", "PUB00083350", "PUB00083351", "PUB00092592", "PUB00092593", "PUB00092594" ]
[ "8387996", "16359314", "24210219", "21564336", "25658941", "28811554", "4210219" ]
[ "Amplification of the Bacillus subtilis maf gene results in arrested septum formation.", "House cleaning, a part of good housekeeping.", "Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides.", "Maf acts downstream of ComG...
[ 1993, 2006, 2013, 2011, 2015, 2017, 1973 ]
7
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 115, 31591, 6228, 672 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 25, 1, 2, 1, 2, 4, 1, 1, 18, 4, 1, 1, 27 ]
13
true
Family
Nucleoside triphosphate pyrophosphatase Maf-like protein
Nucleoside triphosphate pyrophosphatase Maf-like protein
Maf-like
6
IPR003698
3,698
Lipoyl synthase
Lipoyl_synth
Family
28,141
false
false
Lipoyl synthase is an iron-sulphur protein [ ]. It is localised to mitochondria in yeast and Arabidopsis [ , ]. It generates lipoic acid, a thiol antioxidant that is linked to a specific Lys as prosthetic group for the pyruvate and alpha-ketoglutarate dehydrogenase complexes and the glycine-cleavage system.
[ "GO:0016992", "GO:0051539", "GO:0009107" ]
[ "lipoate synthase activity", "4 iron, 4 sulfur cluster binding", "lipoate biosynthetic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "HAMAP", "PIRSF", "PANTHER", "SFLD", "NCBIFAM" ]
[ "MF_00206", "PIRSF005963", "PTHR10949", "SFLDF00271", "TIGR00510" ]
[ "Lipoyl_synth", "Lipoyl_synth", "", "lipoyl_synthase", "lipA" ]
[ 26974, 23483, 28112, 25937, 26165 ]
5
[ "EC", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.8.1.8", "GenProp0745", "GenProp1237", "GenProp1298", "GenProp1625", "PWY-6987", "PWY-7382", "R-BTA-9857492", "R-DME-9857492", "R-DRE-9857492", "R-HSA-9857492", "R-MMU-9857492", "R-RNO-9857492" ]
[ "EC:2.8.1.8", "GP:GenProp0745", "GP:GenProp1237", "GP:GenProp1298", "GP:GenProp1625", "METACYC:PWY-6987", "METACYC:PWY-7382", "REACTOME:R-BTA-9857492", "REACTOME:R-DME-9857492", "REACTOME:R-DRE-9857492", "REACTOME:R-HSA-9857492", "REACTOME:R-MMU-9857492", "REACTOME:R-RNO-9857492" ]
13
[ "4u0o", "4u0p", "5exi", "5exj", "5exk", "8trw", "8tsk", "8ugo", "8v0j", "9c19" ]
10
[ "PUB00016125", "PUB00017446", "PUB00057854" ]
[ "10403368", "8349643", "12062419" ]
[ "The lipoate synthase from Escherichia coli is an iron-sulfur protein.", "Isolation and characterization of LIP5. A lipoate biosynthetic locus of Saccharomyces cerevisiae.", "The biosynthetic pathway for lipoic acid is present in plastids and mitochondria in Arabidopsis thaliana." ]
[ 1999, 1993, 2002 ]
3
[]
[ "IPR027526", "IPR027527" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences" ]
[ 434, 21000, 6120, 1, 586 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 7, 1, 2, 1, 1, 10, 4, 1, 3, 3, 1, 1, 21 ]
13
true
Family
Lipoyl synthase
Lipoyl synthase
Lipoyl_synth
7
IPR003699
3,699
S-adenosylmethionine:tRNA ribosyltransferase-isomerase, QueA
QueA
Family
24,595
false
false
This entry represents the S-adenosylmethionine:tRNA ribosyltransferase-isomerase, QueA. Queuosine is a hypermodified nucleoside that usually occurs in the first position of the anticodon of tRNAs specifying the amino acids asparagine, aspartate, histidine, and tyrosine. The hypermodified nucleoside is found in bacteria...
[ "GO:0016740", "GO:0016853" ]
[ "transferase activity", "isomerase activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "HAMAP", "PFAM", "PANTHER", "NCBIFAM" ]
[ "MF_00113", "PF02547", "PTHR30307", "TIGR00113" ]
[ "QueA", "Queuosine_synth", "", "queA" ]
[ 20290, 24587, 24490, 19818 ]
4
[ "EC", "GP", "GP", "METACYC", "METACYC" ]
[ "2.4.99.17", "GenProp0677", "GenProp1400", "PWY-6700", "PWY-8106" ]
[ "EC:2.4.99.17", "GP:GenProp0677", "GP:GenProp1400", "METACYC:PWY-6700", "METACYC:PWY-8106" ]
5
[ "1vky", "1wdi", "1yy3" ]
3
[ "PUB00008181", "PUB00032106" ]
[ "8347586", "15822125" ]
[ "A new function of S-adenosylmethionine: the ribosyl moiety of AdoMet is the precursor of the cyclopentenediol moiety of the tRNA wobble base queuine.", "Crystal structure of S-adenosylmethionine:tRNA ribosyltransferase-isomerase (QueA) from Thermotoga maritima at 2.0 A resolution reveals a new fold." ]
[ 1993, 2005 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified Caudoviricetes", "unclassified sequences" ]
[ 17, 23782, 245, 2, 549 ]
5
[ "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica" ]
[ 1, 1 ]
2
true
Family
S-adenosylmethionine:tRNA ribosyltransferase-isomerase, QueA
S-adenosylmethionine:tRNA ribosyltransferase-isomerase, QueA
QueA
6
IPR003700
3,700
Ketopantoate hydroxymethyltransferase
Pantoate_hydroxy_MeTrfase
Family
25,884
false
false
The panB gene from Escherichia coli encodes the first enzyme of the pantothenate biosynthesis pathway, ketopantoate hydroxymethyltransferase (KPHMT) . Fungal ketopantoate hydroxymethyltransferase is essential for the biosynthesis of coenzyme A, while the pathway intermediate 4'-phosphopantetheine is required for penici...
[ "GO:0003864", "GO:0015940" ]
[ "3-methyl-2-oxobutanoate hydroxymethyltransferase activity", "pantothenate biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "PFAM", "PIRSF", "PANTHER", "NCBIFAM", "CDD" ]
[ "MF_00156", "PF02548", "PIRSF000388", "PTHR20881", "TIGR00222", "cd06557" ]
[ "PanB", "Pantoate_transf", "Pantoate_hydroxy_MeTrfase", "", "panB", "KPHMT-like" ]
[ 23805, 25875, 22323, 25761, 24075, 24135 ]
6
[ "EC", "GP", "GP", "METACYC" ]
[ "2.1.2.11", "GenProp0124", "GenProp1748", "PWY-6654" ]
[ "EC:2.1.2.11", "GP:GenProp0124", "GP:GenProp1748", "METACYC:PWY-6654" ]
4
[ "1m3u", "1o66", "1o68", "1oy0", "3ez4", "3vav" ]
6
[ "PUB00008182" ]
[ "10503542" ]
[ "The Aspergillus nidulans panB gene encodes ketopantoate hydroxymethyltransferase, required for biosynthesis of pantothenate and Coenzyme A." ]
[ 1999 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 587, 21422, 3259, 616 ]
4
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 9, 1, 1, 6, 1, 1, 8 ]
7
true
Family
Ketopantoate hydroxymethyltransferase
Ketopantoate hydroxymethyltransferase
Pantoate_hydroxy_MeTrfase
3
IPR003701
3,701
DNA double-strand break repair protein Mre11
Mre11
Family
4,351
false
false
Mre11 and Rad50 are two proteins required for DNA repair and meiosis-specific double-strand break formation in Saccharomyces cerevisiae. Mre11 by itself has 3' to 5' exonuclease activity that is increased when Mre11 is in a complex with Rad50 [ ].
[ "GO:0004520", "GO:0008296", "GO:0006302", "GO:0030870" ]
[ "DNA endonuclease activity", "3'-5'-DNA exonuclease activity", "double-strand break repair", "Mre11 complex" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PIRSF", "NCBIFAM" ]
[ "PIRSF000882", "TIGR00583" ]
[ "DSB_repair_MRE11", "mre11" ]
[ 3936, 3727 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-CEL-1834949", "R-CEL-5685939", "R-CEL-5693548", "R-CEL-5693607", "R-GGA-217106", "R-GGA-351442", "R-GGA-351444", "R-HSA-1834949", "R-HSA-2559586", "R-HSA-3270619", "R-HSA-5685938", "R-HSA-5685939", "R-HSA-5685942", "R-HSA-5693548", "R-HSA-5693554", "R-HSA-5693565", "R-HSA-5693568"...
[ "REACTOME:R-CEL-1834949", "REACTOME:R-CEL-5685939", "REACTOME:R-CEL-5693548", "REACTOME:R-CEL-5693607", "REACTOME:R-GGA-217106", "REACTOME:R-GGA-351442", "REACTOME:R-GGA-351444", "REACTOME:R-HSA-1834949", "REACTOME:R-HSA-2559586", "REACTOME:R-HSA-3270619", "REACTOME:R-HSA-5685938", "REACTOME:R...
67
[ "3t1i", "4fbk", "4fbq", "4fbw", "4fcx", "4yke", "7zr1", "8bah", "9bi4", "9bi5", "9q9h", "9q9i", "9q9j", "9q9k", "9q9m" ]
15
[ "PUB00008183", "PUB00014360", "PUB00014366", "PUB00014392" ]
[ "9651580", "7789757", "7885834", "9799249" ]
[ "The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks.", "Interaction of Mre11 and Rad50: two proteins required for DNA repair and meiosis-specific double-strand break formation in Saccharomyces cerevisiae.", "Cloning and characterisation of the Schizosaccharomyces pombe ra...
[ 1998, 1995, 1995, 1998 ]
4
[]
[]
0
0
null
[ "Eukaryota" ]
[ 4351 ]
1
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 7, 1, 1, 13, 3, 4, 1, 4, 7, 1, 1, 13 ]
12
true
Family
DNA double-strand break repair protein Mre11
DNA double-strand break repair protein Mre11
Mre11
9
IPR003702
3,702
Acetyl-CoA hydrolase/transferase, N-terminal
ActCoA_hydro_N
Domain
14,290
false
false
This entry represents an acetyl-CoA hydrolase/transferase N-terminal domain. This domain is found in several enzymes which take part in pathways involving acetyl-CoA, including acetyl-CoA hydrolase , propionyl-CoA:succinate CoA transferase, succinyl-CoA:coenzyme A transferase (CAT1) and 4-hydroxybutyrate coenzyme A tra...
[ "GO:0008410" ]
[ "CoA-transferase activity" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF02550" ]
[ "AcetylCoA_hydro" ]
[ 14290 ]
1
[ "GP" ]
[ "GenProp1723" ]
[ "GP:GenProp1723" ]
1
[ "2g39", "2nvv", "2oas", "3d3u", "3eh7", "3gk7", "3qdq", "3qli", "3qlk", "3s8d", "4eu3", "4eu4", "4eu5", "4eu6", "4eu7", "4eu8", "4eu9", "4eua", "4eub", "4euc", "4eud", "4n8h", "4n8i", "4n8j", "4n8k", "4n8l", "5ddk", "5dw4", "5dw5", "5dw6", "5e5h", "8dh7"...
32
[ "PUB00042977", "PUB00042978", "PUB00061981" ]
[ "10769117", "12606555", "1357077" ]
[ "Discovering new enzymes and metabolic pathways: conversion of succinate to propionate by Escherichia coli.", "Functional characterization and localization of acetyl-CoA hydrolase, Ach1p, in Saccharomyces cerevisiae.", "An acetate-sensitive mutant of Neurospora crassa deficient in acetyl-CoA hydrolase." ]
[ 2000, 2003, 1992 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 160, 11474, 2504, 152 ]
4
[ "Caenorhabditis elegans", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]
[ 2, 1, 1, 1, 1, 1 ]
6
true
Domain
Acetyl-CoA hydrolase/transferase, N-terminal
Acetyl-CoA hydrolase/transferase, N-terminal
ActCoA_hydro_N
9
IPR003703
3,703
Acyl-CoA thioesterase
Acyl_CoA_thio
Family
22,344
false
false
Acyl-CoA thioesterases are a group of enzymes that catalyse the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH). They consequently have the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. They may also be involved in the metabolic regulation of peroxisome proli...
[ "GO:0047617", "GO:0006637" ]
[ "fatty acyl-CoA hydrolase activity", "acyl-CoA metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PANTHER", "NCBIFAM" ]
[ "PTHR11066", "TIGR00189" ]
[ "", "tesB" ]
[ 22339, 6602 ]
2
[ "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.1.2", "GenProp1488", "R-HSA-193368", "R-HSA-2046106", "R-HSA-389887", "R-HSA-390247", "R-HSA-9033241", "R-MMU-193368", "R-MMU-2046106", "R-MMU-389887", "R-MMU-390247", "R-MMU-9033241", "R-RNO-193368", "R-RNO-2046106", "R-RNO-389887", "R-RNO-390247", "R-RNO-9033241", "R-SCE-19336...
[ "EC:3.1.2", "GP:GenProp1488", "REACTOME:R-HSA-193368", "REACTOME:R-HSA-2046106", "REACTOME:R-HSA-389887", "REACTOME:R-HSA-390247", "REACTOME:R-HSA-9033241", "REACTOME:R-MMU-193368", "REACTOME:R-MMU-2046106", "REACTOME:R-MMU-389887", "REACTOME:R-MMU-390247", "REACTOME:R-MMU-9033241", "REACTOM...
22
[ "1c8u", "1tbu", "3rd7", "3u0a", "4qfw", "4r4u", "4r9z" ]
7
[ "PUB00008184", "PUB00016113", "PUB00057420", "PUB00100263", "PUB00100264" ]
[ "1645722", "10092594", "15194431", "14660652", "11171266" ]
[ "Cloning, sequencing, and characterization of Escherichia coli thioesterase II.", "Identification of peroxisomal acyl-CoA thioesterases in yeast and humans.", "Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis.", "Biochemical and molecular characterization of ACH2, an acyl-CoA th...
[ 1991, 1999, 2004, 2004, 2000 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 15513, 6630, 201 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae ...
[ 11, 9, 2, 1, 12, 3, 1, 4, 6, 1, 13 ]
11
true
Family
Acyl-CoA thioesterase
Acyl-CoA thioesterase
Acyl_CoA_thio
9
IPR003704
3,704
Acetyl-CoA decarbonylase/synthase complex subunit epsilon
CdhB
Family
433
false
false
The ACDS complex contains five subunits, among which beta possesses an Ni-Fe-S active-site metal cluster, the A-cluster, at which reaction with acetyl-CoA takes place, generating an acetyl-enzyme species poised for C-C bond cleavage [ ]. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a...
[ "GO:0019385" ]
[ "methanogenesis, from acetate" ]
[ "biological_process" ]
1
[ "HAMAP", "PFAM", "PIRSF", "NCBIFAM" ]
[ "MF_01134", "PF02552", "PIRSF006035", "TIGR00315" ]
[ "CdhB", "CO_dh", "CO_dh_b_ACDS_e", "cdhB" ]
[ 168, 433, 190, 221 ]
4
[]
[]
[]
0
[ "1ytl", "3cf4", "8riu", "9c0q", "9c0r", "9c0s", "9c0t" ]
7
[ "PUB00008185", "PUB00008186", "PUB00043435", "PUB00082744", "PUB00082745" ]
[ "8662887", "8550451", "14664578", "12464601", "20202935" ]
[ "Carbon monoxide dehydrogenase from Methanosarcina frisia Go1. Characterization of the enzyme and the regulated expression of two operon-like cdh gene clusters.", "Characterization of the cdhD and cdhE genes encoding subunits of the corrinoid/iron-sulfur enzyme of the CO dehydrogenase complex from Methanosarcina ...
[ 1996, 1996, 2003, 2003, 2010 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "ecological metagenomes" ]
[ 246, 151, 3, 33 ]
4
[]
[]
0
true
Family
Acetyl-CoA decarbonylase/synthase complex subunit epsilon
Acetyl-CoA decarbonylase/synthase complex subunit epsilon
CdhB
1
IPR003705
3,705
Cobalt transport protein CbiN
CbiN
Family
2,787
false
false
The cobalt transport protein CbiN is part of the active cobalt transport system involved in uptake of cobalt in to the cell involved with cobalamin biosynthesis (vitamin B12). It has been suggested that CbiN may function as the periplasmic binding protein component of the active cobalt transport system [ ].
[ "GO:0015087", "GO:0006824", "GO:0009236", "GO:0016020" ]
[ "cobalt ion transmembrane transporter activity", "cobalt ion transport", "cobalamin biosynthetic process", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "cellular_component" ]
4
[ "HAMAP", "NCBIFAM", "PFAM", "PANTHER", "NCBIFAM" ]
[ "MF_00330", "NF002780", "PF02553", "PTHR38662", "TIGR01165" ]
[ "CbiN", "PRK02898.1", "CbiN", "", "cbiN" ]
[ 2720, 2475, 2787, 2770, 1639 ]
5
[ "GP" ]
[ "GenProp0277" ]
[ "GP:GenProp0277" ]
1
[]
0
[ "PUB00015329" ]
[ "8501034" ]
[ "Characterization of the cobalamin (vitamin B12) biosynthetic genes of Salmonella typhimurium." ]
[ 1993 ]
1
[]
[]
0
0
null
[ "Bacteria", "Methanobacteriati", "metagenomes" ]
[ 2525, 242, 20 ]
3
[]
[]
0
true
Family
Cobalt transport protein CbiN
Cobalt transport protein CbiN
CbiN
5
IPR003706
3,706
CstA, N-terminal domain
CstA_N
Domain
16,492
false
false
Escherichia coli induces the synthesis of at least 30 proteins at the onset of carbon starvation, two-thirds of which are positively regulated by the cyclic AMP (cAMP) and cAMP receptor protein (CRP) complex. Proteins in this entry include carbon starvation protein CstA, which is a predicted membrane protein that may b...
[ "GO:0009267", "GO:0016020" ]
[ "cellular response to starvation", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM" ]
[ "PF02554" ]
[ "CstA" ]
[ 16492 ]
1
[]
[]
[]
0
[]
0
[ "PUB00008188" ]
[ "1848300" ]
[ "Molecular and functional characterization of a carbon starvation gene of Escherichia coli." ]
[ 1991 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctzWr28", "unclassified sequences" ]
[ 413, 15820, 40, 1, 218 ]
5
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Domain
CstA, N-terminal domain
CstA, N-terminal domain
CstA_N
1
IPR003708
3,708
Bacterial protein export chaperone SecB
SecB
Family
9,678
false
false
Secretion across the inner membrane in some Gram-negative bacteria occurs via the preprotein translocase pathway. Proteins are produced in the cytoplasm as precursors, and require a chaperone subunit to direct them to the translocase component [ ]. From there, the mature proteins are either targeted to the outer membra...
[ "GO:0051082", "GO:0015031", "GO:0051262" ]
[ "unfolded protein binding", "protein transport", "protein tetramerization" ]
[ "molecular_function", "biological_process", "biological_process" ]
3
[ "HAMAP", "PFAM", "PRINTS", "PANTHER", "NCBIFAM" ]
[ "MF_00821", "PF02556", "PR01594", "PTHR36918", "TIGR00809" ]
[ "SecB", "SecB", "SECBCHAPRONE", "", "secB" ]
[ 8844, 9676, 8890, 9259, 8819 ]
5
[ "GP" ]
[ "GenProp0209" ]
[ "GP:GenProp0209" ]
1
[ "1fx3", "1ozb", "1qyn", "5jtl", "5jtm", "5jtn", "5jto", "5jtp", "5jtq", "5jtr" ]
10
[ "PUB00007064", "PUB00007065", "PUB00007066", "PUB00007563" ]
[ "2202721", "11336818", "10418149", "11101901" ]
[ "The sec and prl genes of Escherichia coli.", "SecB, a molecular chaperone with two faces.", "Effects of pre-protein overexpression on SecB synthesis in Escherichia coli.", "Crystal structure of the bacterial protein export chaperone secB." ]
[ 1990, 2001, 1999, 2000 ]
4
[]
[]
0
0
null
[ "Bacteria", "Caudoviricetes", "Eukaryota", "Methanobacteriota", "unclassified sequences" ]
[ 9512, 5, 33, 5, 123 ]
5
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Bacterial protein export chaperone SecB
Bacterial protein export chaperone SecB
SecB
6
IPR003709
3,709
D-alanyl-D-alanine carboxypeptidase-like, core domain
VanY-like_core_dom
Domain
15,422
false
false
This entry represents the common core domain found in D-alanyl-D-alanine carboxypeptidases (DD-CPases) and related proteins from the MEROPS peptidase M15 family mostly found in bacteria. This domain features a central twisted antiparallel β-sheet (β1-β6) flanked by two pairs of three α-helices (α2, α3, α6, and α1, α5, ...
[ "GO:0008233", "GO:0006508" ]
[ "peptidase activity", "proteolysis" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF02557" ]
[ "VanY" ]
[ 15422 ]
1
[]
[]
[]
0
[ "4d0y", "4f78", "4jid", "4mph", "4muq", "4mur", "4mus", "4mut", "4nt9", "4oak", "4ox3", "4ox5", "4oxd", "5hnm", "5zhf", "5zhw", "6a6a" ]
17
[ "PUB00008189", "PUB00008190", "PUB00106228", "PUB00140679", "PUB00140738", "PUB00140739", "PUB00160313", "PUB00160314", "PUB00161022" ]
[ "8631706", "1398115", "24909784", "10500118", "1510448", "24711382", "26867711", "27270282", "9257766" ]
[ "Regulation of VanB-type vancomycin resistance gene expression by the VanS(B)-VanR (B) two-component regulatory system in Enterococcus faecalis V583.", "Sequence of the vanY gene required for production of a vancomycin-inducible D,D-carboxypeptidase in Enterococcus faecium BM4147.", "Structure of the LdcB LD-ca...
[ 1996, 1992, 2014, 1999, 1992, 2014, 2016, 2016, 1997 ]
9
[]
[ "IPR058193" ]
0
1
0
[ "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 15006, 147, 99, 170 ]
4
[ "Arabidopsis thaliana" ]
[ 1 ]
1
true
Domain
D-alanyl-D-alanine carboxypeptidase-like, core domain
D-alanyl-D-alanine carboxypeptidase-like, core domain
VanY-like_core_dom
1
IPR003710
3,710
Ketopantoate reductase ApbA/PanE
ApbA
Family
26,807
false
false
ApbA, the ketopantoate reductase enzyme of Salmonella typhimurium is required for the synthesis of thiamine via the alternative pyrimidine biosynthetic pathway [ ]. Precursors to the pyrimidine moiety of thiamine are synthesised de novo by the purine biosynthetic pathway or the alternative pyrimidine biosynthetic (APB)...
[ "GO:0008677", "GO:0015940" ]
[ "2-dehydropantoate 2-reductase activity", "pantothenate biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "NCBIFAM" ]
[ "TIGR00745" ]
[ "apbA_panE" ]
[ 26807 ]
1
[ "EC", "GP", "GP", "METACYC" ]
[ "1.1.1.169", "GenProp0124", "GenProp1748", "PWY-6654" ]
[ "EC:1.1.1.169", "GP:GenProp0124", "GP:GenProp1748", "METACYC:PWY-6654" ]
4
[ "1ks9", "1yjq", "1yon", "2ew2", "2ofp", "2qyt", "3ego", "3g17", "3hn2", "3hwr", "3i83", "3wfi", "3wfj", "4ol9", "4s3m", "4yca", "5ayv", "5hws", "5x20", "5zik", "5zix", "6k1r", "8iwg", "8iwq", "8ix9", "8ixh", "8ixm", "8wl1", "8wl3", "8wl4" ]
30
[ "PUB00020970", "PUB00020974", "PUB00086634" ]
[ "9488683", "9721324", "11154694" ]
[ "ApbA, the ketopantoate reductase enzyme of Salmonella typhimurium is required for the synthesis of thiamine via the alternative pyrimidine biosynthetic pathway.", "The panE gene, encoding ketopantoate reductase, maps at 10 minutes and is allelic to apbA in Salmonella typhimurium.", "Saccharomyces cerevisiae is...
[ 1998, 1998, 2001 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 657, 21448, 4472, 230 ]
4
[ "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]
[ 1, 1, 1, 1 ]
4
true
Family
Ketopantoate reductase ApbA/PanE
Ketopantoate reductase ApbA/PanE
ApbA
1
IPR003711
3,711
CarD-like/TRCF, RNAP-interacting domain
CarD-like/TRCF_RID
Domain
38,426
false
false
This is the RNA polymerase-interacting domain (RID) superfamily of transcription-repair-coupling factor (TRCF), CarD and CarD homologue in Myxococcus xanthus, called CdnL [ , , , ]. CarD is a Myxococcus xanthus protein required for the activation of light- and starvation-inducible genes [ ]. Furthermore, CarD is widely...
[]
[]
[]
0
[ "PFAM", "SMART" ]
[ "PF02559", "SM01058" ]
[ "CarD_TRCF_RID", "CarD_TRCF" ]
[ 38226, 38096 ]
2
[ "EC", "METACYC" ]
[ "3.6.4.-", "PWY-7250" ]
[ "EC:3.6.4.-", "METACYC:PWY-7250" ]
2
[ "2eyq", "2lqk", "2lt1", "2lt4", "2lwj", "3mlq", "4ilu", "4kbm", "4l5g", "4mfr", "4xax", "4xlr", "4xls", "6ac6", "6ac8", "6aca", "6acx", "6edt", "6ee8", "6eec", "6m6a", "6m6b", "6vvx", "6vvy", "6vvz", "6vw0", "6x26", "6x2f", "6x2n", "6x43", "6x4w", "6x4y"...
50
[ "PUB00008194", "PUB00040473", "PUB00065411", "PUB00101051", "PUB00101052" ]
[ "8692912", "16469698", "20702425", "24115125", "23858468" ]
[ "High mobility group I(Y)-like DNA-binding domains on a bacterial transcription factor.", "Structural basis for bacterial transcription-coupled DNA repair.", "Structural basis for the bacterial transcription-repair coupling factor/RNA polymerase interaction.", "Crystal structure of Mycobacterium tuberculosis ...
[ 1996, 2006, 2010, 2014, 2013 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 36907, 737, 782 ]
3
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 4, 1, 4, 3 ]
4
true
Domain
CarD-like/TRCF, RNAP-interacting domain
CarD-like/TRCF, RNAP-interacting domain
CarD-like/TRCF_RID
6
IPR003712
3,712
Cyanate lyase, C-terminal
Cyanate_lyase_C
Domain
6,298
false
false
Some bacteria can overcome the toxicity of environmental cyanate by hydrolysis of cyanate. This reaction is catalyzed by cyanate lyase (also known as cyanase) [ ]. Cyanate lyase is found in bacteria and plants and catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. The cyanate lyas...
[ "GO:0009440" ]
[ "cyanate catabolic process" ]
[ "biological_process" ]
1
[ "PFAM", "SMART", "CDD" ]
[ "PF02560", "SM01116", "cd00559" ]
[ "Cyanate_lyase", "Cyanate_lyase", "Cyanase_C" ]
[ 6297, 6236, 5660 ]
3
[ "EC" ]
[ "4.2.1.104" ]
[ "EC:4.2.1.104" ]
1
[ "1dw9", "1dwk", "2iu7", "2iuo", "2iv1", "2ivb", "2ivg", "2ivq", "4y42", "5uk3", "6b6m", "6tv0", "6xgt", "7o74", "8c7e", "8k6g", "8k6h", "8k6s", "8k6u", "8k6x" ]
20
[ "PUB00008197", "PUB00008198" ]
[ "3049588", "10801492" ]
[ "Characterization of the cyn operon in Escherichia coli K12.", "Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site." ]
[ 1988, 2000 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes", "uncultured Caudovirales phage" ]
[ 24, 3971, 2280, 22, 1 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 4, 1, 2, 1, 4 ]
5
true
Domain
Cyanate lyase, C-terminal
Cyanate lyase, C-terminal
Cyanate_lyase_C
2
IPR003713
3,713
Flagellar protein FliS
FliS
Family
11,275
false
false
The fliD operon of several bacteria consists of three flagellar genes, fliD, fliS, and fliT, and is transcribed in this order [ ]. In Bacillus subtilis the operon encoding the flagellar proteins FliD, FliS, and FliT is sigma D-dependent [ ]. FliS is a flagellin-specific T3S chaperone that binds in 1:1 stoichiometry to ...
[ "GO:0044780" ]
[ "bacterial-type flagellum assembly" ]
[ "biological_process" ]
1
[ "PFAM", "PIRSF", "PANTHER", "NCBIFAM", "CDD" ]
[ "PF02561", "PIRSF039090", "PTHR34773", "TIGR00208", "cd16098" ]
[ "FliS", "Flis", "", "fliS", "FliS" ]
[ 11273, 8931, 10910, 9938, 10501 ]
5
[ "GP" ]
[ "GenProp0881" ]
[ "GP:GenProp0881" ]
1
[ "1orj", "1ory", "1vh6", "3iqc", "3k1i", "4iwb", "5maw", "5xef", "6ch3", "6gow", "6lea" ]
11
[ "PUB00008199", "PUB00008200", "PUB00078325", "PUB00078326", "PUB00078327", "PUB00078328" ]
[ "8550529", "8195064", "11327763", "12620624", "16806204", "11401962" ]
[ "Negative regulation by fliD, fliS, and fliT of the export of the flagellum-specific anti-sigma factor, FlgM, in Salmonella typhimurium.", "The Bacillus subtilis sigma D-dependent operon encoding the flagellar proteins FliD, FliS, and FliT.", "Flagellin polymerisation control by a cytosolic export chaperone.", ...
[ 1996, 1994, 2001, 2003, 2006, 2001 ]
6
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 11095, 19, 161 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Flagellar protein FliS
Flagellar protein FliS
FliS
7
IPR003714
3,714
PhoH-like protein
PhoH
Domain
38,831
false
false
PhoH is a cytoplasmic protein and predicted ATPase that is induced by phosphate starvation and belongings to the phosphate regulon (pho) in Escherichia coli [ ].
[ "GO:0005524" ]
[ "ATP binding" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF02562" ]
[ "PhoH" ]
[ 38831 ]
1
[]
[]
[]
0
[ "3b85" ]
1
[ "PUB00008201" ]
[ "8444794" ]
[ "Molecular analysis of the phoH gene, belonging to the phosphate regulon in Escherichia coli." ]
[ 1993 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 84, 35505, 80, 2112, 1050 ]
5
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Domain
PhoH-like protein
PhoH-like protein
PhoH
6
IPR003715
3,715
Polysaccharide export protein, N-terminal domain
Poly_export_N
Domain
29,494
false
false
This entry represents a domain found N-terminal in a group of bacterial polysaccharide export proteins, including Wza from Escherichia coli, which is likely to be involved in the export of the extracellular polysaccharide colanic acid (CA) from the cell to medium [ , ] and Capsule polysaccharide export outer membrane p...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02563" ]
[ "Poly_export" ]
[ 29494 ]
1
[]
[]
[]
0
[ "2j58", "2w8h", "2w8i", "7xfd", "7xff" ]
5
[ "PUB00008202", "PUB00153092" ]
[ "8759852", "16030241" ]
[ "Organization of the Escherichia coli K-12 gene cluster responsible for production of the extracellular polysaccharide colanic acid.", "functional analysis of conserved gene products involved in assembly of Escherichia coli capsules and exopolysaccharides: evidence for molecular recognition between Wza and Wzc fo...
[ 1996, 2005 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 29113, 27, 354 ]
3
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Domain
Polysaccharide export protein, N-terminal domain
Polysaccharide export protein, N-terminal domain
Poly_export_N
4
IPR003716
3,716
DNA-directed RNA polymerase, omega subunit
DNA-dir_RNA_pol_omega
Family
19,398
false
false
Bacterial DNA-dependent RNA polymerase (RNAP) has the core composition of α(2)-β-β'-omega, where omega is the smallest of the subunits. The omega subunit is required to promote RNAP assembly by acting like a chaperone to maintain beta' in the correct conformation and to recruit it to the α(2)β subassembly to form a fun...
[ "GO:0003899", "GO:0006351" ]
[ "DNA-directed RNA polymerase activity", "DNA-templated transcription" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "PANTHER", "NCBIFAM" ]
[ "MF_00366", "PTHR34476", "TIGR00690" ]
[ "RNApol_bact_RpoZ", "", "rpoZ" ]
[ 19050, 17468, 18352 ]
3
[ "EC", "GP", "REACTOME" ]
[ "2.7.7.6", "GenProp0262", "R-HSA-9639775" ]
[ "EC:2.7.7.6", "GP:GenProp0262", "REACTOME:R-HSA-9639775" ]
3
[ "1hqm", "1i6v", "1iw7", "1l9u", "1l9z", "1smy", "1ynj", "1ynn", "1zyr", "2a68", "2a69", "2a6e", "2a6h", "2be5", "2cw0", "2o5i", "2o5j", "2ppb", "3aoh", "3aoi", "3dxj", "3eql", "3iyd", "3lu0", "3wod", "4g7h", "4g7o", "4g7z", "4gzy", "4gzz", "4jk1", "4jk2"...
616
[ "PUB00016269" ]
[ "12727285" ]
[ "Inter-subunit recognition and manifestation of segmental mobility in Escherichia coli RNA polymerase: a case study with omega-beta' interaction." ]
[ 2003 ]
1
[ "IPR006110" ]
[]
1
0
1
[ "Bacteria", "Eukaryota", "unclassified sequences", "uncultured Caudovirales phage" ]
[ 18759, 265, 369, 5 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
DNA-directed RNA polymerase, omega subunit
DNA-directed RNA polymerase, omega subunit
DNA-dir_RNA_pol_omega
1
IPR003717
3,717
Recombination protein O, RecO
RecO
Family
25,393
false
false
The damage avoidance-tolerance pathway(s) requires functional recA, recF, recO, and recR genes, suggesting the mechanism to be daughter strand gap repair. The ruvABC genes or the recG gene is also required. The RecG pathway appears to be more active than the RuvABC pathway [ ]. RecO may contain a mononucleotide-binding...
[ "GO:0006281", "GO:0006310" ]
[ "DNA repair", "DNA recombination" ]
[ "biological_process", "biological_process" ]
2
[ "HAMAP", "PFAM", "PANTHER", "NCBIFAM" ]
[ "MF_00201", "PF02565", "PTHR33991", "TIGR00613" ]
[ "RecO", "RecO_C", "", "reco" ]
[ 22862, 24395, 25163, 24117 ]
4
[ "GP" ]
[ "GenProp0491" ]
[ "GP:GenProp0491" ]
1
[ "1u5k", "1w3s", "2v1c", "3q8d", "4jcv", "8ab0", "8bpr" ]
7
[ "PUB00008204", "PUB00008205" ]
[ "11073901", "2544549" ]
[ "Escherichia coli responses to a single DNA adduct.", "Molecular analysis of the Escherichia coli recO gene." ]
[ 2000, 1989 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified Caudoviricetes", "unclassified sequences" ]
[ 24774, 41, 2, 576 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Recombination protein O, RecO
Recombination protein O, RecO
RecO
8
IPR003718
3,718
OsmC/Ohr conserved domain
OsmC/Ohr_dom
Domain
66,025
false
false
This is a conserved domain of peroxiredoxins that includes osmotically inducible protein C (OsmC), a stress-induced protein found in Escherichia coli. This entry also contains organic hydroperoxide resistance protein (Ohr), that has a novel pattern of oxidative stress regulation. The transcription of the osmC gene of E...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02566" ]
[ "OsmC" ]
[ 66025 ]
1
[]
[]
[]
0
[ "1lql", "1ml8", "1n2f", "1nye", "1qwi", "1ukk", "1usp", "1vla", "1zb8", "1zb9", "2bjo", "2d7v", "2e8c", "2e8e", "2e8f", "2egt", "2onf", "2opl", "2pn2", "2ql8", "3cje", "3eer", "3i07", "3lus", "4mh4", "4noz", "4xx2", "6d9n", "6eb4", "6ebc", "6ebd", "6ebg"...
39
[ "PUB00008206", "PUB00008207", "PUB00045449" ]
[ "8820643", "9573147", "18084893" ]
[ "Growth-phase-dependent expression of the osmotically inducible gene osmC of Escherichia coli K-12.", "Identification and characterization of a new organic hydroperoxide resistance (ohr) gene with a novel pattern of oxidative stress regulation from Xanthomonas campestris pv. phaseoli.", "Peroxiredoxins in bacte...
[ 1996, 1998, 2007 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Synechococcus phage S-N03", "unclassified sequences" ]
[ 1100, 62997, 1398, 1, 529 ]
5
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Domain
OsmC/Ohr conserved domain
OsmC/Ohr conserved domain
OsmC/Ohr_dom
2
IPR003719
3,719
Phenazine biosynthesis PhzF-like
Phenazine_PhzF-like
Family
31,711
false
false
This entry represents the PhzF family, which includes PhzF and uncharacterised isomerases. PhzF is part of the seven-gene operon phzABCDEFG, responsible for the synthesis of phenazine-1-carboxylic acid (PCA) in Pseudomonas species [ ]. PhzF is a trans-2,3-dihydro-3-hydroxyanthranilate isomerase that catalyses the conde...
[ "GO:0003824", "GO:0009058" ]
[ "catalytic activity", "biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PIRSF", "PANTHER", "NCBIFAM" ]
[ "PF02567", "PIRSF016184", "PTHR13774", "TIGR00654" ]
[ "PhzC-PhzF", "PhzC_PhzF", "", "PhzF_family" ]
[ 31623, 27969, 29918, 27130 ]
4
[]
[]
[]
0
[ "1qy9", "1qya", "1s7j", "1sdj", "1t6k", "1u0k", "1u1v", "1u1w", "1u1x", "1xua", "1xub", "1ym5", "3edn", "4dun", "5iwe", "9f92", "9f93", "9f94", "9f95", "9f96" ]
20
[ "PUB00031002", "PUB00031360", "PUB00106522" ]
[ "15545603", "15449932", "28740244" ]
[ "Structure and function of the phenazine biosynthetic protein PhzF from Pseudomonas fluorescens.", "Structure and function of the phenazine biosynthesis protein PhzF from Pseudomonas fluorescens 2-79.", "Mechanisms and Specificity of Phenazine Biosynthesis Protein PhzF." ]
[ 2004, 2004, 2017 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctcfw7", "unclassified sequences" ]
[ 495, 24720, 6264, 1, 231 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae ...
[ 20, 3, 6, 1, 6, 5, 1, 9, 7, 1, 2, 5 ]
12
true
Family
Phenazine biosynthesis PhzF-like
Phenazine biosynthesis PhzF-like
Phenazine_PhzF-like
6
IPR003721
3,721
Pantoate-beta-alanine ligase
Pantoate_ligase
Family
24,565
false
false
D-Pantothenate is synthesized via four enzymes from ketoisovalerate, which is an intermediate of branched-chain amino acid synthesis [ ]. Pantoate-beta-alanine ligase, also know as pantothenate synthase, (PanC; ) catalyzes the formation of pantothenate from pantoate and alanine in the pantothenate biosynthesis pathway ...
[ "GO:0004592", "GO:0015940" ]
[ "pantoate-beta-alanine ligase activity", "pantothenate biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "PFAM", "NCBIFAM", "CDD" ]
[ "MF_00158", "PF02569", "TIGR00018", "cd00560" ]
[ "PanC", "Pantoate_ligase", "panC", "PanC" ]
[ 23342, 24565, 23176, 21525 ]
4
[ "EC", "GP", "GP", "GP" ]
[ "6.3.2.1", "GenProp0124", "GenProp1601", "GenProp1748" ]
[ "EC:6.3.2.1", "GP:GenProp0124", "GP:GenProp1601", "GP:GenProp1748" ]
4
[ "1iho", "1mop", "1n2b", "1n2e", "1n2g", "1n2h", "1n2i", "1n2j", "1n2o", "1ufv", "1v8f", "2a7x", "2a84", "2a86", "2a88", "2ejc", "2x3f", "3ag5", "3ag6", "3cov", "3cow", "3coy", "3coz", "3guz", "3imc", "3ime", "3img", "3inn", "3iob", "3ioc", "3iod", "3ioe"...
71
[ "PUB00008210", "PUB00008211", "PUB00019988", "PUB00079800", "PUB00079882", "PUB00079883", "PUB00079884" ]
[ "10223988", "8760912", "374975", "7479698", "15565250", "7037743", "10417331" ]
[ "D-Pantothenate synthesis in Corynebacterium glutamicum and use of panBC and genes encoding L-valine synthesis for D-pantothenate overproduction.", "Sequence analysis of the Bacillus subtilis chromosome region between the serA and kdg loci cloned in a yeast artificial chromosome.", "Pantothenate synthetase from...
[ 1999, 1996, 1979, 1995, 2004, 1982, 1999 ]
7
[]
[ "IPR024894" ]
0
1
0
[ "Bacteria", "Candidatus Iainarchaeum sp.", "Eukaryota", "unclassified sequences" ]
[ 21153, 1, 2837, 574 ]
4
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 3, 1, 1, 4, 1, 1, 3 ]
7
true
Family
Pantoate-beta-alanine ligase
Pantoate-beta-alanine ligase
Pantoate_ligase
9
IPR003722
3,722
Cobalamin biosynthesis precorrin-8X methylmutase CobH/CbiC
Cbl_synth_CobH/CbiC
Domain
11,402
false
false
This entry represents CbiC and CobH precorrin-8X methylmutase ( ), both as stand-alone enzymes and when CobJ forms part of a bifunctional enzyme. CobH and CbiC from the aerobic and anaerobic pathways, respectively, catalyse a methyl rearrangement in precorrin-8 that moves the methyl group from C-11 to C-12 to produce h...
[ "GO:0016993", "GO:0009236" ]
[ "precorrin-8X methylmutase activity", "cobalamin biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF02570" ]
[ "CbiC" ]
[ 11402 ]
1
[ "EC", "GP" ]
[ "5.4.99", "GenProp0275" ]
[ "EC:5.4.99", "GP:GenProp0275" ]
2
[ "1f2v", "1i1h", "1ou0", "1v9c", "2afr", "2afv", "3e7d", "4au1", "4fdv", "5n0g", "8x33", "9ika", "9ikt", "9ipl" ]
14
[ "PUB00009744", "PUB00014669", "PUB00014672", "PUB00015657", "PUB00035308", "PUB00035309", "PUB00035310", "PUB00070131" ]
[ "11215515", "11470433", "11153269", "12869542", "17163662", "16042605", "12055304", "23922391" ]
[ "Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.", "Crystal structure of precorrin-8x methyl mutase.", "Multiple biosynthetic pathways for vitamin B12: variations on a central theme.", "Comparative genomics of the vitamin B12 metabolism and regulation in prokaryotes.", "B12 trafficking in ma...
[ 2000, 2001, 2001, 2003, 2006, 2005, 2002, 2013 ]
8
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 611, 10670, 14, 107 ]
4
[]
[]
0
true
Domain
Cobalamin biosynthesis precorrin-8X methylmutase CobH/CbiC
Cobalamin biosynthesis precorrin-8X methylmutase CobH/CbiC
Cbl_synth_CobH/CbiC
3
IPR003723
3,723
Precorrin-6x reductase
Precorrin-6x_reduct
Family
10,109
false
false
Cobalamins (vitamin B12), both as deoxyadenosylcobalamin and methylcobalamin, are involved as cofactors in a variety of enzymatic reactions and are synthesized by some bacteria and archaea. About thirty enzymes are required to manufacture cobalamins, some of the most complex nonpolymeric molecules biosynthesized in the...
[ "GO:0016994", "GO:0009236" ]
[ "precorrin-6A reductase activity", "cobalamin biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PROFILE", "PANTHER", "NCBIFAM" ]
[ "PF02571", "PS51014", "PTHR36925", "TIGR00715" ]
[ "CbiJ", "COBK_CBIJ", "", "precor6x_red" ]
[ 10078, 10088, 9290, 7580 ]
4
[ "EC", "GP", "PROSITEDOC" ]
[ "1.3.1", "GenProp0275", "PDOC51014" ]
[ "EC:1.3.1", "GP:GenProp0275", "PROSITEDOC:PDOC51014" ]
3
[ "4x7g", "5c4n", "5c4r" ]
3
[ "PUB00009744", "PUB00017560", "PUB00018459" ]
[ "11215515", "1732193", "10559155" ]
[ "Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.", "Precorrin-6x reductase from Pseudomonas denitrificans: purification and characterization of the enzyme and identification of the structural gene.", "Anaerobic growth of Paracoccus denitrificans requires cobalamin: characterization of cobK and c...
[ 2000, 1992, 1999 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriati", "metagenomes" ]
[ 9933, 11, 101, 64 ]
4
[]
[]
0
true
Family
Precorrin-6x reductase
Precorrin-6x reductase
Precorrin-6x_reduct
4
IPR003724
3,724
ATP:cob(I)alamin adenosyltransferase CobA/CobO/BtuR
CblAdoTrfase_CobA
Family
15,111
false
false
ATP:cob(I)alamin (or ATP:corrinoid) adenosyltransferases ( ), catalyse the conversion of cobalamin (vitamin B12) into its coenzyme form, adenosylcobalamin (AdoCbl)or coenzyme B12 [ ]. AdoCbl contains an adenosyl moiety liganded to the cobalt ion of cobalamin via a covalent Co-C bond. AdoCbl is required as a cofactor fo...
[ "GO:0005524", "GO:0008817", "GO:0009236" ]
[ "ATP binding", "corrinoid adenosyltransferase activity", "cobalamin biosynthetic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM", "PIRSF", "PANTHER", "NCBIFAM", "CDD" ]
[ "PF02572", "PIRSF015617", "PTHR46638", "TIGR00708", "cd00561" ]
[ "CobA_CobO_BtuR", "Adensltrnsf_CobA", "", "cobA", "CobA_ACA" ]
[ 15111, 14290, 15035, 11578, 12215 ]
5
[ "EC", "GP" ]
[ "2.5.1.17", "GenProp0269" ]
[ "EC:2.5.1.17", "GP:GenProp0269" ]
2
[ "1g5r", "1g5t", "1g64", "4hut" ]
4
[ "PUB00013593", "PUB00014667", "PUB00015064", "PUB00035323", "PUB00035324", "PUB00035326", "PUB00079512" ]
[ "11160088", "12196148", "15317775", "16672609", "15516577", "7916712", "12195810" ]
[ "Functional genomic, biochemical, and genetic characterization of the Salmonella pduO gene, an ATP:cob(I)alamin adenosyltransferase gene.", "Biosynthesis of cobalamin (vitamin B(12)).", "The eutT gene of Salmonella enterica Encodes an oxygen-labile, metal-containing ATP:corrinoid adenosyltransferase enzyme.", ...
[ 2001, 2002, 2004, 2006, 2004, 1993, 2002 ]
7
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 572, 14223, 37, 279 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
ATP:cob(I)alamin adenosyltransferase CobA/CobO/BtuR
ATP:cob(I)alamin adenosyltransferase CobA/CobO/BtuR
CblAdoTrfase_CobA
9
IPR003725
3,725
Molybdenum-binding protein ModE, N-terminal
ModE-bd_N
Domain
3,071
false
false
This entry represents the N-terminal domain of the ModE protein. ModE is a molybdate-activated repressor of the molybdate transport operon in E. coli. It consists of the N-terminal domain represented by this entry and two tandem copies of mop-like domain, where Mop proteins are a family of 68-residue molybdenum-pterin ...
[]
[]
[]
0
[ "NCBIFAM" ]
[ "TIGR00637" ]
[ "ModE_repress" ]
[ 3071 ]
1
[ "GP" ]
[ "GenProp0192" ]
[ "GP:GenProp0192" ]
1
[ "1b9m", "1b9n", "1o7l" ]
3
[ "PUB00008215", "PUB00008216", "PUB00017513" ]
[ "9210473", "9044285", "8550508" ]
[ "Characterisation of the molybdenum-responsive ModE regulatory protein and its binding to the promoter region of the modABCD (molybdenum transport) operon of Escherichia coli.", "Characterization of the ModE DNA-binding sites in the control regions of modABCD and moaABCDE of Escherichia coli.", "Repression of t...
[ 1997, 1997, 1996 ]
3
[ "IPR000847" ]
[]
1
0
1
[ "Bacteria", "Beauveria bassiana D1-5", "Methanobacteriota", "ecological metagenomes" ]
[ 3049, 1, 12, 9 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
Molybdenum-binding protein ModE, N-terminal
Molybdenum-binding protein ModE, N-terminal
ModE-bd_N
6
IPR003726
3,726
Homocysteine-binding domain
HCY_dom
Domain
42,071
false
false
The homocysteine (Hcy) binding domain is an ~300-residue module which is found in a set of enzymes involved in alkyl transfer to thiols: Prokaryotic and eukaryotic B12-dependent methionine synthase (MetH) ( ), a large, modular protein that catalyses the transfer of a methyl group from methyltetrahydrofolate (CH3-H4fola...
[]
[]
[]
0
[ "PFAM", "PROFILE" ]
[ "PF02574", "PS50970" ]
[ "S-methyl_trans", "HCY" ]
[ 42065, 41340 ]
2
[ "EC", "GP", "GP", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME"...
[ "2.1.1", "GenProp1414", "GenProp1719", "PDOC50970", "R-CEL-156581", "R-CEL-1614635", "R-CEL-9013407", "R-CEL-9759218", "R-DDI-156581", "R-DDI-1614635", "R-DDI-9013407", "R-DDI-9759218", "R-DRE-1614635", "R-DRE-6798163", "R-HSA-156581", "R-HSA-1614635", "R-HSA-3359467", "R-HSA-33594...
[ "EC:2.1.1", "GP:GenProp1414", "GP:GenProp1719", "PROSITEDOC:PDOC50970", "REACTOME:R-CEL-156581", "REACTOME:R-CEL-1614635", "REACTOME:R-CEL-9013407", "REACTOME:R-CEL-9759218", "REACTOME:R-DDI-156581", "REACTOME:R-DDI-1614635", "REACTOME:R-DDI-9013407", "REACTOME:R-DDI-9759218", "REACTOME:R-DR...
33
[ "1lt7", "1lt8", "1q7m", "1q7q", "1q7z", "1q85", "1q8a", "1q8j", "1umy", "3bof", "3bol", "4ccz", "4m3p", "5dml", "5dmm", "5dmn", "8d45", "8g3h", "8ssc", "9cbp", "9cbr", "9ssp", "9ssq", "9ssr", "9sss", "9sst", "9ssu", "9ssv" ]
28
[ "PUB00018442", "PUB00018443" ]
[ "12220488", "14752199" ]
[ "Betaine-homocysteine methyltransferase: zinc in a distorted barrel.", "Structures of the N-terminal modules imply large domain motions during catalysis by methionine synthase." ]
[ 2002, 2004 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 39, 30711, 10482, 2, 837 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 16, 2, 4, 13, 2, 20, 5, 1, 12, 16, 3, 1, 32 ]
13
true
Domain
Homocysteine-binding domain
Homocysteine-binding domain
HCY_dom
9
IPR003728
3,728
Ribosome maturation factor RimP
Ribosome_maturation_RimP
Family
23,230
false
false
The RimP protein (also known as YlxS in Bacillus subtilis) facilitates maturation of the 30S ribosomal subunit, and is required for the efficient production of translationally competent ribosomes [ ].
[ "GO:0042274" ]
[ "ribosomal small subunit biogenesis" ]
[ "biological_process" ]
1
[ "HAMAP", "PANTHER" ]
[ "MF_01077", "PTHR33867" ]
[ "RimP", "" ]
[ 23042, 22605 ]
2
[ "GP" ]
[ "GenProp0802" ]
[ "GP:GenProp0802" ]
1
[ "1ib8", "5gl6", "7afi", "7afl", "7afo", "7afr", "7nas", "7nat", "7nau", "7nav", "7naw", "8bdv", "8bh7" ]
13
[ "PUB00053910" ]
[ "19150615" ]
[ "The RimP protein is important for maturation of the 30S ribosomal subunit." ]
[ 2009 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 22104, 656, 470 ]
3
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 4, 1, 2, 5 ]
4
true
Family
Ribosome maturation factor RimP
Ribosome maturation factor RimP
Ribosome_maturation_RimP
4
IPR003729
3,729
Bifunctional nuclease domain
Bi_nuclease_dom
Domain
11,083
false
false
The bifunctional nuclease (BFN) domain is specific to bacteria and plant organisms. It has both RNase and DNase activities [ ]. The dimer of the BFN domain forms a wedge, each monomer being a basic triangular shape. The BFN domain is composed of an eight-stranded, distorted β-sheet consisting of a four-stranded, antipa...
[ "GO:0004518" ]
[ "nuclease activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PROFILE" ]
[ "PF02577", "PS51658" ]
[ "BFN_dom", "BFN" ]
[ 10939, 11019 ]
2
[]
[]
[]
0
[ "1sj5", "1vjl" ]
2
[ "PUB00029328", "PUB00057454" ]
[ "15557262", "20018603" ]
[ "On the use of DXMS to produce more crystallizable proteins: structures of the T. maritima proteins TM0160 and TM1171.", "Novel bifunctional nucleases, OmBBD and AtBBD1, are involved in abscisic acid-mediated callose deposition in Arabidopsis." ]
[ 2004, 2010 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes", "uncultured marine phage" ]
[ 670, 8265, 1789, 358, 1 ]
5
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 15, 4, 21 ]
3
true
Domain
Bifunctional nuclease domain
Bifunctional nuclease domain
Bi_nuclease_dom
1
IPR003730
3,730
Multi-copper polyphenol oxidoreductase
Cu_polyphenol_OxRdtase
Family
22,229
false
false
Laccases are multi-copper oxidoreductases able to oxidise a wide variety of phenolic and non-phenolic compounds and are widely distributed among both prokaryotes and eukaryotes. There are two main active catalytic sites with conserved histidines that are capable of binding four copper atoms [ ]. This family consists of...
[]
[]
[]
0
[ "PFAM", "PANTHER", "NCBIFAM", "CDD" ]
[ "PF02578", "PTHR30616", "TIGR00726", "cd16833" ]
[ "Cu-oxidase_4", "", "", "YfiH" ]
[ 22224, 22059, 18141, 21874 ]
4
[ "EC", "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "2.4.2.1", "2.4.2.28", "3.5.4.4", "PWY-4202", "PWY-5532", "PWY-5695", "PWY-6608", "PWY-6609", "PWY-6611", "PWY-6620", "PWY-6627", "PWY-6644", "PWY-6756", "PWY-7179", "PWY-8130", "PWY-8440" ]
[ "EC:2.4.2.1", "EC:2.4.2.28", "EC:3.5.4.4", "METACYC:PWY-4202", "METACYC:PWY-5532", "METACYC:PWY-5695", "METACYC:PWY-6608", "METACYC:PWY-6609", "METACYC:PWY-6611", "METACYC:PWY-6620", "METACYC:PWY-6627", "METACYC:PWY-6644", "METACYC:PWY-6756", "METACYC:PWY-7179", "METACYC:PWY-8130", "ME...
16
[ "1rv9", "1rw0", "1t8h", "1u05", "1xaf", "1xfj", "1z9t", "6dzd", "6t0y", "6t1b", "7f3v", "7fbg", "7w1g" ]
13
[ "PUB00044734", "PUB00086031", "PUB00086032" ]
[ "16740638", "27478939", "28593945" ]
[ "Novel polyphenol oxidase mined from a metagenome expression library of bovine rumen: biochemical properties, structural analysis, and phylogenetic relationships.", "C13orf31 (FAMIN) is a central regulator of immunometabolic function.", "Human LACC1 increases innate receptor-induced responses and a LACC1 diseas...
[ 2006, 2016, 2017 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Siphoviridae sp. ctFn287", "unclassified sequences" ]
[ 20776, 996, 1, 456 ]
4
[ "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 1, 3, 2, 3 ]
5
true
Family
Multi-copper polyphenol oxidoreductase
Multi-copper polyphenol oxidoreductase
Cu_polyphenol_OxRdtase
9
IPR003731
3,731
Dinitrogenase iron-molybdenum cofactor biosynthesis
Di-Nase_FeMo-co_biosynth
Domain
10,755
false
false
This entry represents several Nif (B, X and Y) proteins, which are involved in the biosynthesis of the iron-molybdenum cofactor (FeMo-co) found in the dinitrogenase enzyme of the nitrogenase complex in nitrogen-fixing bacteria. The nitrogenase complex catalyses the reduction of atmospheric dinitrogen to ammonia, and is...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02579" ]
[ "Nitro_FeMo-Co" ]
[ 10755 ]
1
[]
[]
[]
0
[ "1eo1", "1o13", "1p90", "1rdu", "1t3v", "2kla", "2qtd", "2re2", "2wfb", "2yx6" ]
10
[ "PUB00015608", "PUB00016259", "PUB00016260" ]
[ "12836677", "11279153", "12892890" ]
[ "NMR structure determination and structure-based functional characterization of conserved hypothetical protein MTH1175 from Methanobacterium thermoautotrophicum.", "Accumulation of 55Fe-labeled precursors of the iron-molybdenum cofactor of nitrogenase on NifH and NifX of Azotobacter vinelandii.", "Nitrogenase a...
[ 2000, 2001, 2003 ]
3
[]
[ "IPR033913", "IPR034165", "IPR034169" ]
0
3
0
[ "Archaea", "Bacteria", "unclassified sequences" ]
[ 1026, 9376, 353 ]
3
[]
[]
0
true
Domain
Dinitrogenase iron-molybdenum cofactor biosynthesis
Dinitrogenase iron-molybdenum cofactor biosynthesis
Di-Nase_FeMo-co_biosynth
7
IPR003732
3,732
D-aminoacyl-tRNA deacylase DTD
Daa-tRNA_deacyls_DTD
Family
25,716
false
false
This family consists of D-aminoacyl-tRNA deacylase DTD, also known as D-Tyr-tRNA(Tyr) deacylase. It is an enzyme that cleaves misacetylated D-aminoacyl-tRNA molecules into free tRNAs and D-amino acids [ , ]. Cell growth inhibition by several D-amino acids can be explained by an in vivo production of D-aminoacyl-tRNA mo...
[ "GO:0002161", "GO:0051499", "GO:0005737" ]
[ "aminoacyl-tRNA deacylase activity", "D-aminoacyl-tRNA deacylase activity", "cytoplasm" ]
[ "molecular_function", "molecular_function", "cellular_component" ]
3
[ "HAMAP", "PFAM", "PANTHER", "NCBIFAM", "CDD" ]
[ "MF_00518", "PF02580", "PTHR10472", "TIGR00256", "cd00563" ]
[ "Deacylase_Dtd", "Tyr_Deacylase", "", "", "Dtyr_deacylase" ]
[ 21289, 25696, 25212, 23548, 14470 ]
5
[ "EC" ]
[ "3.1.1.96" ]
[ "EC:3.1.1.96" ]
1
[ "1j7g", "1jke", "1tc5", "2dbo", "2okv", "3knf", "3knp", "3ko3", "3ko4", "3ko5", "3ko7", "3ko9", "3kob", "3koc", "3kod", "3lmt", "3lmu", "3lmv", "4nbi", "4nbj", "5j61", "5xaq" ]
22
[ "PUB00017393", "PUB00074108", "PUB00080046", "PUB00080047", "PUB00080048" ]
[ "11568181", "25441601", "10918062", "10766779", "10383414" ]
[ "Structure of crystalline D-Tyr-tRNA(Tyr) deacylase. A representative of a new class of tRNA-dependent hydrolases.", "The dtd gene from Bacillus amyloliquefaciens encodes a putative d-tyrosyl-tRNA(Tyr) deacylase and is a selectable marker for Bacillus subtilis.", "Metabolism of D-aminoacyl-tRNAs in Escherichia ...
[ 2001, 2015, 2000, 2000, 1999 ]
5
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriota", "Siphoviridae sp. ctBLh2", "unclassified sequences" ]
[ 19525, 5816, 15, 1, 359 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 6, 1, 3, 3, 1, 6, 2, 1, 2, 7, 1, 1, 8 ]
13
true
Family
D-aminoacyl-tRNA deacylase DTD
D-aminoacyl-tRNA deacylase DTD
Daa-tRNA_deacyls_DTD
4
IPR003734
3,734
Domain of unknown function DUF155
DUF155
Domain
10,621
false
false
This entry represents a domain found in RMND1 from mammals, Sif2/Sif3 from fission yeasts and Rmd1/Rmd8/YDR282C (Mrx10) from budding yeasts. RMND1 and its yeast homologue, Mrx10, are mitochondrial proteins required for mitochondrial translation [ , ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF02582" ]
[ "DUF155" ]
[ 10621 ]
1
[]
[]
[]
0
[]
0
[ "PUB00075393", "PUB00076329", "PUB00076330" ]
[ "12586695", "23022098", "23022099" ]
[ "Large-scale functional genomic analysis of sporulation and meiosis in Saccharomyces cerevisiae.", "An RMND1 Mutation causes encephalopathy associated with multiple oxidative phosphorylation complex deficiencies and a mitochondrial translation defect.", "Infantile encephaloneuromyopathy and defective mitochondr...
[ 2003, 2012, 2012 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 1216, 9392, 13 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 5, 1, 9, 1, 9, 2, 3, 5, 4, 3, 2, 15 ]
12
true
Domain
Domain of unknown function DUF155
Domain of unknown function DUF155
DUF155
5
IPR003735
3,735
Metal-sensitive transcriptional repressor
Metal_Tscrpt_repr
Family
26,552
false
false
This is a family of metal-sensitive repressors, involved in resistance to metal ions. Members of this family bind copper, nickel or cobalt ions via conserved cysteine and histidine residues. In the absence of metal ions, these proteins bind to promoter regions and repress transcription. When bound to metal ions they ar...
[ "GO:0003677", "GO:0046872", "GO:0006355" ]
[ "DNA binding", "metal ion binding", "regulation of DNA-templated transcription" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM", "PANTHER" ]
[ "PF02583", "PTHR33677" ]
[ "Trns_repr_metal", "" ]
[ 26552, 26095 ]
2
[]
[]
[]
0
[ "2hh7", "3aai", "4adz", "4m1p", "4uig", "5fmn", "5lbm", "5lcy", "6ahx", "7mq1", "7mq2", "7mq3" ]
12
[ "PUB00035608", "PUB00041403", "PUB00057455", "PUB00057456", "PUB00057457" ]
[ "16956381", "17143269", "20395270", "17186148", "17293508" ]
[ "Nickel homeostasis in Escherichia coli - the rcnR-rcnA efflux pathway and its linkage to NikR function.", "CsoR is a novel Mycobacterium tuberculosis copper-sensing transcriptional regulator.", "Structural and functional characterization of the transcriptional repressor CsoR from Thermus thermophilus HB8.", ...
[ 2006, 2007, 2010, 2007, 2007 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 38, 26177, 30, 307 ]
4
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)" ]
[ 1, 2 ]
2
true
Family
Metal-sensitive transcriptional repressor
Metal-sensitive transcriptional repressor
Metal_Tscrpt_repr
5
IPR003736
3,736
Phenylacetic acid degradation-related domain
PAAI_dom
Domain
56,578
false
false
This domain is found in the PAAI protein from Escherichia coli that may be involved in phenylacetic acid degradation and in a few others that may be transcription regulators [ ]. Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from Caenorhabditis elegans consists ...
[]
[]
[]
0
[ "NCBIFAM" ]
[ "TIGR00369" ]
[ "unchar_dom_1" ]
[ 56578 ]
1
[ "EC", "EC", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC...
[ "3.1.2", "3.1.2.-", "GenProp1291", "GenProp1498", "GenProp1560", "GenProp1694", "PWY-3602", "PWY-5109", "PWY-6322", "PWY-6585", "PWY-6917", "PWY-6948", "PWY-6995", "PWY-6997", "PWY-7007", "PWY-7216", "PWY-7292", "PWY-7401", "PWY-7402", "PWY-7471", "PWY-7690", "PWY-7706", ...
[ "EC:3.1.2", "EC:3.1.2.-", "GP:GenProp1291", "GP:GenProp1498", "GP:GenProp1560", "GP:GenProp1694", "METACYC:PWY-3602", "METACYC:PWY-5109", "METACYC:PWY-6322", "METACYC:PWY-6585", "METACYC:PWY-6917", "METACYC:PWY-6948", "METACYC:PWY-6995", "METACYC:PWY-6997", "METACYC:PWY-7007", "METACYC...
41
[ "1j1y", "1psu", "1q4s", "1q4t", "1q4u", "1sbk", "1sc0", "1vh5", "1vh9", "1vi8", "1wlu", "1wlv", "1wm6", "1wn3", "1zki", "2b6e", "2cy9", "2dsl", "2f0x", "2fs2", "2h4u", "2pim", "2qwz", "3dkz", "3e1e", "3e29", "3e8p", "3f1t", "3f5o", "3gek", "3lbb", "3lbe"...
69
[ "PUB00008223" ]
[ "2507523" ]
[ "Sequence and transcription mapping of Bacillus subtilis competence genes comB and comA, one of which is related to a family of bacterial regulatory determinants." ]
[ 1989 ]
1
[ "IPR006683" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 1112, 48595, 6265, 606 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 15, 3, 3, 3, 4, 1, 2, 1, 10, 2, 21 ]
11
true
Domain
Phenylacetic acid degradation-related domain
Phenylacetic acid degradation-related domain
PAAI_dom
6
IPR003738
3,738
SOS response associated peptidase (SRAP)
SRAP
Family
26,893
false
false
The SRAP (SOS-response associated peptidase) family is characterised by the SRAP domain with a novel thiol autopeptidase activity, whose active site in human HMCES is comprised of the catalytic triad residues C2, E127, and H210 [ ]. SRAP proteins are evolutionarily conserved in all domains of life. For instance, human ...
[ "GO:0003697", "GO:0006974", "GO:0106300" ]
[ "single-stranded DNA binding", "DNA damage response", "protein-DNA covalent cross-linking repair" ]
[ "molecular_function", "biological_process", "biological_process" ]
3
[ "PFAM", "PANTHER" ]
[ "PF02586", "PTHR13604" ]
[ "SRAP", "" ]
[ 26862, 25333 ]
2
[]
[]
[]
0
[ "1zn6", "2aeg", "2bdv", "2f20", "2icu", "5ko9", "6kbs", "6kbu", "6kbx", "6kbz", "6kcq", "6kij", "6nua", "6nuh", "6oe7", "6oea", "6oeb", "6oov", "8d2m" ]
19
[ "PUB00075418", "PUB00093989", "PUB00093990", "PUB00093991", "PUB00093992" ]
[ "23945014", "31235915", "31806351", "30554877", "23434322" ]
[ "Novel autoproteolytic and DNA-damage sensing components in the bacterial SOS response and oxidized methylcytosine-induced eukaryotic DNA demethylation systems.", "Protection of abasic sites during DNA replication by a stable thiazolidine protein-DNA cross-link.", "HMCES Functions in the Alternative End-Joining...
[ 2013, 2019, 2020, 2019, 2013 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 416, 21853, 4200, 19, 405 ]
5
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae...
[ 9, 1, 1, 1, 8, 1, 1, 2, 2, 1, 13 ]
11
true
Family
SOS response associated peptidase (SRAP)
SOS response associated peptidase (SRAP)
SRAP
2
IPR003739
3,739
Lysine-2,3-aminomutase/glutamate 2,3-aminomutase
Lys_aminomutase/Glu_NH3_mut
Family
13,232
false
false
This entry represents the lysine-2,3-aminomutase (LAM) family of proteins. LAM catalyses the interconversion of L-alpha-lysine and L-beta-lysine, which proceeds by migration of the amino group from C2 to C3 concomitant with cross-migration of the 3-pro-R hydrogen of L-alpha-lysine to the 2-pro-R position of L-beta-lysi...
[]
[]
[]
0
[ "PIRSF", "PANTHER", "SFLD", "NCBIFAM" ]
[ "PIRSF004911", "PTHR30538", "SFLDG01070", "TIGR00238" ]
[ "DUF160", "", "PLP-dependent", "" ]
[ 8345, 13232, 11189, 9678 ]
4
[ "EC" ]
[ "5.4.3" ]
[ "EC:5.4.3" ]
1
[ "2a5h" ]
1
[ "PUB00074042" ]
[ "17222594" ]
[ "Glutamate 2,3-aminomutase: a new member of the radical SAM superfamily of enzymes." ]
[ 2007 ]
1
[]
[ "IPR022447", "IPR022459", "IPR022462", "IPR030801", "IPR031015" ]
0
5
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 318, 12011, 655, 248 ]
4
[ "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 1, 1 ]
2
true
Family
Lysine-2,3-aminomutase/glutamate 2,3-aminomutase
Lysine-2,3-aminomutase/glutamate 2,3-aminomutase
Lys_aminomutase/Glu_NH3_mut
2
IPR003740
3,740
Uncharacterised membrane protein YitT
YitT
Family
27,622
false
false
This entry includes proteins with transmembrane domains, such as YitT from Bacillus subtilis. The function of YitT is not clear.
[]
[]
[]
0
[ "PFAM", "PIRSF" ]
[ "PF02588", "PIRSF006483" ]
[ "YitT_membrane", "Membrane_protein_YitT" ]
[ 27622, 20168 ]
2
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriota", "unclassified Caudoviricetes", "unclassified sequences" ]
[ 27431, 17, 2, 2, 170 ]
5
[]
[]
0
true
Family
Uncharacterised membrane protein YitT
Uncharacterised membrane protein YitT
YitT
4
IPR003741
3,741
LUD domain
LUD_dom
Domain
26,754
false
false
This entry represents a domain found in lactate utilization proteins B (LutB) and C (LutC), as well as several uncharacterised proteins. LutB and LutC are encoded by the conserved LutABC operon in bacteria. They are involved in lactate utilization and is implicated in the oxidative conversion of L-lactate into pyruvate...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02589" ]
[ "LUD_dom" ]
[ 26754 ]
1
[]
[]
[]
0
[ "2g40" ]
1
[ "PUB00053899", "PUB00076952", "PUB00083829" ]
[ "19201793", "24274019", "26167158" ]
[ "A widely conserved gene cluster required for lactate utilization in Bacillus subtilis and its involvement in biofilm formation.", "LUD, a new protein domain associated with lactate utilization.", "The primary pathway for lactate oxidation in Desulfovibrio vulgaris." ]
[ 2009, 2013, 2015 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Inoviridae sp. ct1ro12", "unclassified sequences" ]
[ 1165, 25150, 167, 1, 271 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)" ]
[ 1, 2 ]
2
true
Domain
LUD domain
LUD domain
LUD_dom
6
IPR003742
3,742
RNA methyltransferase RlmH
RlmH-like
Family
18,966
false
false
Methyltransferases (Mtases) are responsible for the transfer of methyl groups between two molecules. The transfer of the methyl group from the ubiquitous S-adenosyl-L-methionine (AdoMet) to nitrogen, oxygen or carbon atoms is frequently employed in diverse organisms. The reactions are catalysed by Mtases and modify DNA...
[ "GO:0008168", "GO:0006364" ]
[ "methyltransferase activity", "rRNA processing" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "PFAM", "PIRSF", "PANTHER", "NCBIFAM", "CDD" ]
[ "MF_00658", "PF02590", "PIRSF004505", "PTHR33603", "TIGR00246", "cd18081" ]
[ "23SrRNA_methyltr_H", "SPOUT_MTase", "MT_bac", "", "tRNA_RlmH_YbeA", "RlmH-like" ]
[ 18252, 18947, 17967, 18830, 9402, 18629 ]
6
[ "EC" ]
[ "2.1.1.177" ]
[ "EC:2.1.1.177" ]
1
[ "1ns5", "1o6d", "1to0", "1vh0", "4fak", "5twj", "5twk", "5zyo", "7cem", "7cf7", "7cfy" ]
11
[ "PUB00016836" ]
[ "12077432" ]
[ "An enzyme with a deep trefoil knot for the active-site architecture." ]
[ 2002 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriati", "unclassified sequences" ]
[ 17877, 799, 56, 234 ]
4
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 6, 1, 3, 10 ]
4
true
Family
RNA methyltransferase RlmH
RNA methyltransferase RlmH
RlmH-like
8
IPR003743
3,743
C4-type zinc ribbon domain
Zf-RING_7
Domain
7,646
false
false
This entry represents a Zn-ribbon domain rich in aromatic and positively charged amino acid residues. This C-terminal Zn-ribbon domain consists of two β-strands acting as a scaffold for the two Zn knuckles. Both pairs of cysteines making up the two Zn knuckles are situated at highly conserved sharp β-turns, an arrangem...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02591" ]
[ "Zn_ribbon_9" ]
[ 7646 ]
1
[]
[]
[]
0
[ "3na7", "4ilo", "5y05", "5y06" ]
4
[ "PUB00070793", "PUB00075417" ]
[ "21348639", "20826163" ]
[ "Ab initio modeling led annotation suggests nucleic acid binding function for many DUFs.", "The 2.2-A structure of the HP0958 protein from Helicobacter pylori reveals a kinked anti-parallel coiled-coil hairpin domain and a highly conserved ZN-ribbon domain." ]
[ 2011, 2010 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 7384, 4, 258 ]
3
[]
[]
0
true
Domain
C4-type zinc ribbon domain
C4-type zinc ribbon domain
Zf-RING_7
5
IPR003744
3,744
Queuosine precursor transporter
YhhQ
Family
13,887
false
false
This entry includes queuosine (Q) precursor transporter from Escherichia coli , which is required for the import and rescue of the queuosine precursors 7-cyano-7-deazaguanine (preQ0) and 7-aminomethyl-7-deazaguanine (preQ1) [ ]. Membranes are impermeable to purines; therefore, transporters are required for the salvage ...
[]
[]
[]
0
[ "HAMAP", "PFAM", "PANTHER", "NCBIFAM" ]
[ "MF_02088", "PF02592", "PTHR34300", "TIGR00697" ]
[ "Q_prec_transport", "Vut_1", "", "" ]
[ 12099, 13877, 13153, 12192 ]
4
[]
[]
[]
0
[]
0
[ "PUB00085169" ]
[ "28208705" ]
[ "The Escherichia coli COG1738 Member YhhQ Is Involved in 7-Cyanodeazaguanine (preQ₀) Transport." ]
[ 2017 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]
[ 526, 13077, 31, 34, 219 ]
5
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Queuosine precursor transporter
Queuosine precursor transporter
YhhQ
9
IPR003745
3,745
Thymidylate synthase MJ0757-like
MJ0757-like
Family
498
false
false
This entry represents Thymidylate synthase (MJ0757) from Methanocaldococcus jannaschii. This protein is able to catalyse the biosynthesis of dTMP using dUMP, tetrahydrofolate and formaldehyde in vitro, i.e. a reaction equivalent to that catalysed by bacterial thymidylate synthases . However, M.jannaschii like most meth...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02593" ]
[ "DUF166" ]
[ 498 ]
1
[ "GP" ]
[ "GenProp1264" ]
[ "GP:GenProp1264" ]
1
[]
0
[ "PUB00057368", "PUB00072924", "PUB00158992" ]
[ "10426953", "11790254", "39120137" ]
[ "Identifying two ancient enzymes in Archaea using predicted secondary structure alignment.", "Quod erat demonstrandum? The mystery of experimental validation of apparently erroneous computational analyses of protein sequences.", "High-throughput genetics enables identification of nutrient utilization and access...
[ 1999, 2001, 2024 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "ecological metagenomes" ]
[ 376, 89, 33 ]
3
[]
[]
0
true
Family
Thymidylate synthase MJ0757-like
Thymidylate synthase MJ0757-like
MJ0757-like
9
IPR003748
3,748
Protein of unknown function DUF169
DUF169
Family
2,255
false
false
This entry includes Uncharacterized protein MJ0308 and related uncharacterised proteins from prokaryotes.
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF02596", "PTHR37954" ]
[ "DUF169", "" ]
[ 2255, 1511 ]
2
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 626, 1506, 2, 121 ]
4
[]
[]
0
true
Family
Protein of unknown function DUF169
Protein of unknown function DUF169
DUF169
1
IPR003749
3,749
Sulfur carrier ThiS/MoaD-like
ThiS/MoaD-like
Family
48,376
false
false
ThiS (thiaminS) is a 66 aa protein involved in sulphur transfer. ThiS is coded in the thiCEFSGH operon in Escherichia coli. This family of proteins have two conserved Glycines at the COOH terminus. Thiocarboxylate is formed at the last G in the activation process. Sulphur is transferred from ThiI to ThiS in a reaction ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02597" ]
[ "ThiS" ]
[ 48376 ]
1
[ "GP", "REACTOME", "REACTOME" ]
[ "GenProp1711", "R-HSA-947581", "R-MTU-936654" ]
[ "GP:GenProp1711", "REACTOME:R-HSA-947581", "REACTOME:R-MTU-936654" ]
3
[ "1f0z", "1fm0", "1fma", "1jw9", "1jwa", "1jwb", "1nvi", "1rws", "1ryj", "1sf0", "1tyg", "1v8c", "1vjk", "1zud", "2cu3", "2g1e", "2htm", "2k22", "2k5p", "2l52", "2l83", "2lek", "2m19", "2q5w", "2qie", "3bii", "3cwi", "3dwg", "3dwm", "3po0", "3rpf", "4hro"...
39
[ "PUB00007564", "PUB00035630", "PUB00088041", "PUB00088042" ]
[ "10781607", "17223713", "28439027", "16547008" ]
[ "The iscS gene in Escherichia coli is required for the biosynthesis of 4-thiouridine, thiamin, and NAD.", "Role of the C-terminal Gly-Gly motif of Escherichia coli MoaD, a molybdenum cofactor biosynthesis protein with a ubiquitin fold.", "Biochemical and structural characterization of oxygen-sensitive 2-thiouri...
[ 2000, 2007, 2017, 2006 ]
4
[]
[ "IPR010035", "IPR010038", "IPR044672" ]
0
3
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 2118, 42165, 3111, 982 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 4, 1, 1, 1, 2, 2, 1, 1, 2, 5 ]
10
true
Family
Sulfur carrier ThiS/MoaD-like
Sulfur carrier ThiS/MoaD-like
ThiS/MoaD-like
4
IPR003750
3,750
Putative RNA methyltransferase C9orf114-like
Put_MeTrfase-C9orf114-like
Family
4,737
false
false
This entry includes the putative methyltransferase C9orf114 from human, also known as SPOUT1, and its homologues [ , ]. It is required for association of the centrosomes with the poles of the bipolar mitotic spindle during metaphase [ , ]. It is also involved in chromosome alignment [ ]. SPOUT1 binds specifically to mi...
[]
[]
[]
0
[ "PFAM", "PANTHER", "CDD" ]
[ "PF02598", "PTHR12150", "cd18086" ]
[ "Methyltrn_RNA_3", "", "HsC9orf114-like" ]
[ 4728, 4601, 4413 ]
3
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC"...
[ "2.1.1.-", "PWY-1061", "PWY-2083", "PWY-3542", "PWY-4021", "PWY-4161", "PWY-4202", "PWY-5059", "PWY-5105", "PWY-5301", "PWY-5305", "PWY-5479", "PWY-5665", "PWY-5729", "PWY-5748", "PWY-5765", "PWY-5773", "PWY-5846", "PWY-5883", "PWY-5975", "PWY-5987", "PWY-601", "PWY-6045"...
[ "EC:2.1.1.-", "METACYC:PWY-1061", "METACYC:PWY-2083", "METACYC:PWY-3542", "METACYC:PWY-4021", "METACYC:PWY-4161", "METACYC:PWY-4202", "METACYC:PWY-5059", "METACYC:PWY-5105", "METACYC:PWY-5301", "METACYC:PWY-5305", "METACYC:PWY-5479", "METACYC:PWY-5665", "METACYC:PWY-5729", "METACYC:PWY-5...
146
[ "1k3r", "4rg1", "8qsu", "8qsv", "8qsw" ]
5
[ "PUB00044735", "PUB00057459", "PUB00089985", "PUB00143243", "PUB00158921" ]
[ "17338813", "18844986", "28431233", "25657325", "20813266" ]
[ "Structural and evolutionary bioinformatics of the SPOUT superfamily of methyltransferases.", "RNomics and Modomics in the halophilic archaea Haloferax volcanii: identification of RNA modification genes.", "A Compendium of RNA-Binding Proteins that Regulate MicroRNA Biogenesis.", "CENP-32 is required to maint...
[ 2007, 2008, 2017, 2015, 2010 ]
5
[]
[]
0
0
null
[ "Archaea", "Eukaryota", "ecological metagenomes" ]
[ 674, 4052, 11 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 5, 1, 1, 5, 4, 2, 1, 5, 5, 2, 1, 8 ]
12
true
Family
Putative RNA methyltransferase C9orf114-like
Putative RNA methyltransferase C9orf114-like
Put_MeTrfase-C9orf114-like
5
IPR003751
3,751
Translational regulator CsrA
CsrA
Family
11,470
false
false
The RNA-binding protein CsrA (carbon storage regulator) is a new kind of global regulator, which facilitates specific mRNA decay [ ]. CsrA is entirely contained within a globular complex of approximately 18 CsrA-H6 subunits and a single RNA, CsrB. CsrA binds to the CsrB RNA molecule to form the Csr regulatory system wh...
[ "GO:0003723", "GO:0006109", "GO:0006402" ]
[ "RNA binding", "regulation of carbohydrate metabolic process", "mRNA catabolic process" ]
[ "molecular_function", "biological_process", "biological_process" ]
3
[ "HAMAP", "PFAM", "PANTHER", "NCBIFAM" ]
[ "MF_00167", "PF02599", "PTHR34984", "TIGR00202" ]
[ "CsrA", "CsrA", "", "csrA" ]
[ 10439, 11470, 10704, 9231 ]
4
[]
[]
[]
0
[ "1t3o", "1vpz", "1y00", "2bti", "2jpp", "2mf0", "2mf1", "2mfc", "2mfe", "2mff", "2mfg", "2mfh", "4k59", "4kji", "4krw", "5dmb", "5z38", "7yr6", "7yr7" ]
19
[ "PUB00008225" ]
[ "9211896" ]
[ "The RNA molecule CsrB binds to the global regulatory protein CsrA and antagonizes its activity in Escherichia coli." ]
[ 1997 ]
1
[]
[]
0
0
null
[ "Bacteria", "Candidatus Methanofastidiosum methylothiophilum", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 11195, 1, 15, 34, 225 ]
5
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Translational regulator CsrA
Translational regulator CsrA
CsrA
4
IPR003752
3,752
Disulphide bond formation protein DsbB/BdbC
DiS_bond_form_DsbB/BdbC
Family
15,765
false
false
Disulphide bonds contribute to folding, maturation, stability, and regulation of proteins, in particular those localized out of the cytosol. Oxidation of selected pairs of cysteines to disulphide in vivo requires cellular factors present in the bacterial periplasmic space or in the endoplasmic reticulum of eukaryotic c...
[ "GO:0015035", "GO:0006457", "GO:0016020" ]
[ "protein-disulfide reductase activity", "protein folding", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM" ]
[ "PF02600" ]
[ "DsbB" ]
[ 15765 ]
1
[]
[]
[]
0
[ "2hi7", "2k73", "2k74", "2leg", "2ltq", "2zup", "2zuq", "3e9j", "6wvf" ]
9
[ "PUB00008228", "PUB00008229", "PUB00014003", "PUB00053944", "PUB00054232" ]
[ "8430071", "7957076", "12524212", "11844773", "12415301" ]
[ "A pathway for disulfide bond formation in vivo.", "Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation.", "Protein disulfide bond formation in prokaryotes.", "Mutations in the thiol-disulfide oxidoreductases BdbC and BdbD can...
[ 1993, 1994, 2003, 2002, 2002 ]
5
[]
[ "IPR012187", "IPR022920", "IPR023792" ]
0
3
0
[ "Archaea", "Bacillus phage SPbeta", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 185, 1, 15386, 14, 179 ]
5
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Disulphide bond formation protein DsbB/BdbC
Disulphide bond formation protein DsbB/BdbC
DiS_bond_form_DsbB/BdbC
3
IPR003753
3,753
Exonuclease VII, large subunit
Exonuc_VII_L
Family
25,188
false
false
Exonuclease VII ( ) is composed of two nonidentical subunits; one large subunit and 4 small ones [ ]. Exonuclease VII catalyses exonucleolytic cleavage in either 5'-3' or 3'-5' direction to yield 5'-phosphomononucleotides. The large subunit also contains the OB-fold domains that bind to nucleic acids at the N terminus.
[ "GO:0008855", "GO:0006308", "GO:0009318" ]
[ "exodeoxyribonuclease VII activity", "DNA catabolic process", "exodeoxyribonuclease VII complex" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "HAMAP", "PANTHER", "NCBIFAM" ]
[ "MF_00378", "PTHR30008", "TIGR00237" ]
[ "Exonuc_7_L", "", "xseA" ]
[ 22422, 25185, 24345 ]
3
[ "EC", "GP" ]
[ "3.1.11.6", "GenProp1095" ]
[ "EC:3.1.11.6", "GP:GenProp1095" ]
2
[ "8txr" ]
1
[ "PUB00008230" ]
[ "6284744" ]
[ "Subunit structure of Escherichia coli exonuclease VII." ]
[ 1982 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriati", "Viruses", "unclassified sequences" ]
[ 24197, 52, 277, 39, 623 ]
5
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Exonuclease VII, large subunit
Exonuclease VII, large subunit
Exonuc_VII_L
3
IPR003754
3,754
Tetrapyrrole biosynthesis, uroporphyrinogen III synthase
4pyrrol_synth_uPrphyn_synth
Domain
35,122
false
false
This entry represents uroporphyrinogen III synthase ( ) which functions during the second stage of tetrapyrrole biosynthesis. This enzyme catalyses the inversion of the final pyrrole unit (ring D) of the linear tetrapyrrole molecule, linking it to the first pyrrole unit (ring A), thereby generating a large macrocyclic ...
[ "GO:0004852", "GO:0033014" ]
[ "uroporphyrinogen-III synthase activity", "tetrapyrrole biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "CDD" ]
[ "PF02602", "cd06578" ]
[ "HEM4", "HemD" ]
[ 35117, 33644 ]
2
[ "EC", "GP", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "4.2.1.75", "GenProp0220", "GenProp1525", "GenProp1701", "GenProp1716", "GenProp1720", "PWY-5188", "PWY-5189", "R-HSA-189451", "R-MMU-189451", "R-SCE-189451", "R-SPO-189451" ]
[ "EC:4.2.1.75", "GP:GenProp0220", "GP:GenProp1525", "GP:GenProp1701", "GP:GenProp1716", "GP:GenProp1720", "METACYC:PWY-5188", "METACYC:PWY-5189", "REACTOME:R-HSA-189451", "REACTOME:R-MMU-189451", "REACTOME:R-SCE-189451", "REACTOME:R-SPO-189451" ]
12
[ "1jr2", "1wcw", "1wcx", "1wd7", "3d8n", "3d8r", "3d8s", "3d8t", "3mw8", "3p9z", "3re1", "4es6", "6th8" ]
13
[ "PUB00009744", "PUB00014673", "PUB00035496", "PUB00035498", "PUB00035503" ]
[ "11215515", "11689424", "17227226", "16564539", "17270473" ]
[ "Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.", "Crystal structure of human uroporphyrinogen III synthase.", "Tetrapyrrole biosynthesis in higher plants.", "Evolutionary relationship between initial enzymes of tetrapyrrole biosynthesis.", "Study of the genotype-phenotype relationship in f...
[ 2000, 2001, 2007, 2006, 2007 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 814, 28815, 5056, 437 ]
4
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae...
[ 7, 1, 5, 1, 15, 4, 1, 2, 4, 1, 1, 10 ]
12
true
Domain
Tetrapyrrole biosynthesis, uroporphyrinogen III synthase
Tetrapyrrole biosynthesis, uroporphyrinogen III synthase
4pyrrol_synth_uPrphyn_synth
4
IPR003755
3,755
HPr(Ser) kinase/phosphorylase
HPr(Ser)_kin/Pase
Family
7,595
false
false
This entry represents the bifunctional HPr serine kinase/phosphorylase (HprK/P). It catalyses the phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). It also catalyses thedephosphorylation of seryl-phosphorylated HPr (...
[ "GO:0000155", "GO:0005524", "GO:0000160", "GO:0006109" ]
[ "phosphorelay sensor kinase activity", "ATP binding", "phosphorelay signal transduction system", "regulation of carbohydrate metabolic process" ]
[ "molecular_function", "molecular_function", "biological_process", "biological_process" ]
4
[ "HAMAP", "NCBIFAM" ]
[ "MF_01249", "TIGR00679" ]
[ "HPr_kinase", "hpr-ser" ]
[ 7200, 7594 ]
2
[ "EC", "EC", "GP", "METACYC", "METACYC" ]
[ "2.7.11.-", "2.7.4.-", "GenProp0119", "PWY-5107", "PWY-7039" ]
[ "EC:2.7.11.-", "EC:2.7.4.-", "GP:GenProp0119", "METACYC:PWY-5107", "METACYC:PWY-7039" ]
5
[ "1jb1", "1kkl", "1kkm", "1knx", "1ko7", "2qmh" ]
6
[ "PUB00017535", "PUB00068780" ]
[ "9987110", "15023355" ]
[ "The hprK gene of Enterococcus faecalis encodes a novel bifunctional enzyme: the HPr kinase/phosphatase.", "HPr kinase/phosphorylase, a Walker motif A-containing bifunctional sensor enzyme controlling catabolite repression in Gram-positive bacteria." ]
[ 1999, 2004 ]
2
[]
[]
0
0
null
[ "Bacteria", "Opisthokonta", "metagenomes" ]
[ 7519, 13, 63 ]
3
[]
[]
0
true
Family
HPr(Ser) kinase/phosphorylase
HPr(Ser) kinase/phosphorylase
HPr(Ser)_kin/Pase
8
IPR003757
3,757
Photosystem I PsaL, reaction centre subunit XI
PSI_PsaL
Domain
1,757
false
false
The trimeric photosystem I of the cyanobacterium Synechococcus elongatus recomprises 11 protein subunits. Subunit XI, PsaL, from plants and bacteria is one of the smaller subunits with only two transmembrane α helices. PsaL interacts closely with PsaI [ ].
[ "GO:0015979", "GO:0009522", "GO:0009538" ]
[ "photosynthesis", "photosystem I", "photosystem I reaction center" ]
[ "biological_process", "cellular_component", "cellular_component" ]
3
[ "PFAM" ]
[ "PF02605" ]
[ "PsaL" ]
[ 1757 ]
1
[ "GP" ]
[ "GenProp0660" ]
[ "GP:GenProp0660" ]
1
[ "1jb0", "2o01", "2wsc", "2wse", "2wsf", "3lw5", "3pcq", "4fe1", "4l6v", "4rku", "4xk8", "4y28", "5l8r", "5oy0", "5zf0", "5zgb", "5zgh", "5zji", "6fos", "6hqb", "6igz", "6ijj", "6ijo", "6jeo", "6jo5", "6jo6", "6k33", "6k61", "6kif", "6kig", "6kmw", "6kmx"...
137
[ "PUB00008234" ]
[ "8901876" ]
[ "Photosystem I at 4 A resolution represents the first structural model of a joint photosynthetic reaction centre and core antenna system." ]
[ 1996 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 536, 1221 ]
2
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 4, 3, 10 ]
3
true
Domain
Photosystem I PsaL, reaction centre subunit XI
Photosystem I PsaL, reaction centre subunit XI
PSI_PsaL
2
IPR003758
3,758
Tetraacyldisaccharide 4'-kinase
LpxK
Family
15,076
false
false
Tetraacyldisaccharide 4'-kinase (LpxK) phosphorylates the 4'-position of a tetraacyldisaccharide 1-phosphate precursor (DS-1-P) of lipid [ ]. This enzyme is involved in the synthesis of lipid A portion of the bacterial lipopolysaccharide layer (LPS). It is organised into two α/β/α sandwich domains linked by a two-stran...
[ "GO:0005524", "GO:0009029", "GO:0009245" ]
[ "ATP binding", "lipid-A 4'-kinase activity", "lipid A biosynthetic process" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "HAMAP", "PFAM", "PANTHER", "NCBIFAM" ]
[ "MF_00409", "PF02606", "PTHR42724", "TIGR00682" ]
[ "LpxK", "LpxK", "", "lpxK" ]
[ 14197, 15059, 14868, 14050 ]
4
[ "EC", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC" ]
[ "2.7.1.130", "GenProp0204", "GenProp1290", "GenProp1325", "GenProp1647", "PWY-8073", "PWY-8245", "PWY-8283" ]
[ "EC:2.7.1.130", "GP:GenProp0204", "GP:GenProp1290", "GP:GenProp1325", "GP:GenProp1647", "METACYC:PWY-8073", "METACYC:PWY-8245", "METACYC:PWY-8283" ]
8
[ "4ehw", "4ehx", "4ehy", "4itl", "4itm", "4itn", "4lkv" ]
7
[ "PUB00008235", "PUB00062712" ]
[ "9575203", "22826246" ]
[ "Accumulation of a lipid A precursor lacking the 4'-phosphate following inactivation of the Escherichia coli lpxK gene.", "Crystal structure of LpxK, the 4'-kinase of lipid A biosynthesis and atypical P-loop kinase functioning at the membrane interface." ]
[ 1998, 2012 ]
2
[]
[]
0
0
null
[ "Bacteria", "Candidatus Methanophaga sp. ANME-1 ERB7", "Eukaryota", "unclassified sequences" ]
[ 13914, 1, 833, 328 ]
4
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 8, 1, 3, 8 ]
4
true
Family
Tetraacyldisaccharide 4'-kinase
Tetraacyldisaccharide 4'-kinase
LpxK
1
IPR003759
3,759
Cobalamin (vitamin B12)-binding module, cap domain
Cbl-bd_cap
Domain
34,327
false
false
Cobalamin-dependent methionine synthase ( ) is a large modular protein that catalyses methyl transfer from methyltetrahydrofolate (CH3-H4folate) to homocysteine. During the catalytic cycle, it supports three distinct methyl transfer reactions, each involving the cobalamin (vitamin B12) cofactor and a substrate bound to...
[]
[]
[]
0
[ "PFAM", "PROFILE", "SMART" ]
[ "PF02607", "PS51337", "SM01018" ]
[ "B12-binding_2", "B12_BINDING_NTER", "B12-binding_2" ]
[ 34218, 26754, 26800 ]
3
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CEL-156581", "R-CEL-1614635", "R-CEL-9013407", "R-CEL-9759218", "R-DDI-156581", "R-DDI-1614635", "R-DDI-9013407", "R-DDI-9759218", "R-HSA-156581", "R-HSA-1614635", "R-HSA-3359467", "R-HSA-3359469", "R-HSA-9013407", "R-HSA-9759218", "R-MMU-156581", "R-MMU-1614635", "R-MMU-9013407",...
[ "REACTOME:R-CEL-156581", "REACTOME:R-CEL-1614635", "REACTOME:R-CEL-9013407", "REACTOME:R-CEL-9759218", "REACTOME:R-DDI-156581", "REACTOME:R-DDI-1614635", "REACTOME:R-DDI-9013407", "REACTOME:R-DDI-9759218", "REACTOME:R-HSA-156581", "REACTOME:R-HSA-1614635", "REACTOME:R-HSA-3359467", "REACTOME:R...
22
[ "1bmt", "1k7y", "1k98", "1y80", "2i2x", "3bul", "3ezx", "3iv9", "3iva", "3whp", "4jgi", "5c8a", "5c8d", "5c8e", "5c8f", "7xcn", "8c31", "8c32", "8c33", "8c34", "8c35", "8c36", "8c37", "8c73", "8c76", "8g3h", "8j2w", "8j2x", "8j2y", "8jbs", "8jbt", "8ssc"...
45
[ "PUB00014004", "PUB00016227" ]
[ "11731805", "8939751" ]
[ "Domain alternation switches B(12)-dependent methionine synthase to the activation conformation.", "The structure of the C-terminal domain of methionine synthase: presenting S-adenosylmethionine for reductive methylation of B12." ]
[ 2002, 1996 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 1105, 30079, 2265, 878 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 1, 1, 9, 1, 6 ]
6
true
Domain
Cobalamin (vitamin B12)-binding module, cap domain
Cobalamin (vitamin B12)-binding module, cap domain
Cbl-bd_cap
3
IPR003760
3,760
ABC transporter substrate-binding protein PnrA-like
PnrA-like
Domain
25,012
false
false
Proteins containing this domain were originally annotated as basic membrane lipoproteins [ ]. However, several proteins containing this domain were later predicted as ABC transporter substrate-binding proteins, such as PnrA (also known as TmpC or TP0319) and RfuA (also known as Tpn38 or TP0298) from Treponema pallidum....
[ "GO:0005886" ]
[ "plasma membrane" ]
[ "cellular_component" ]
1
[ "PFAM" ]
[ "PF02608" ]
[ "Bmp" ]
[ 25012 ]
1
[]
[]
[]
0
[ "2fqw", "2fqx", "2fqy", "2hqb", "3s99", "4iil", "4p98", "4pev", "4ycs", "6pi5", "6pi6", "6pii", "6shu", "6y9u", "6ya3", "6ya4", "6yab", "6yag", "7x0r" ]
19
[ "PUB00008238", "PUB00008239", "PUB00040783", "PUB00065217", "PUB00070398" ]
[ "9350727", "9335269", "16418175", "23404400", "17501984" ]
[ "Heterogeneity of BmpA (P39) among European isolates of Borrelia burgdorferi sensu lato and influence of interspecies variability on serodiagnosis.", "A new Bacillus subtilis gene, med, encodes a positive regulator of comK.", "The PnrA (Tp0319; TmpC) lipoprotein represents a new family of bacterial purine nucle...
[ 1997, 1997, 2006, 2013, 2007 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]
[ 669, 23602, 4, 174, 563 ]
5
[]
[]
0
true
Domain
ABC transporter substrate-binding protein PnrA-like
ABC transporter substrate-binding protein PnrA-like
PnrA-like
6
IPR003763
3,763
CDP-diacylglycerol pyrophosphatase
CDP-diacylglyc_Pase
Family
2,630
false
false
The CDP-diacylglycerol pyrophosphatases play a role in the regulation of phospholipid metabolism by inositol, as well as regulating the cellular levels of phosphatidylinositol [ ].
[ "GO:0008715", "GO:0008654", "GO:0016020" ]
[ "CDP-diacylglycerol diphosphatase activity", "phospholipid biosynthetic process", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "HAMAP", "NCBIFAM", "PFAM", "PIRSF" ]
[ "MF_00319", "NF003986", "PF02611", "PIRSF001273" ]
[ "Cdh", "PRK05471.1-5", "CDH", "CDH" ]
[ 1113, 1624, 2630, 1866 ]
4
[ "EC" ]
[ "3.6.1.26" ]
[ "EC:3.6.1.26" ]
1
[ "2pof" ]
1
[ "PUB00008242" ]
[ "11016943" ]
[ "Regulation of the DPP1-encoded diacylglycerol pyrophosphate (DGPP) phosphatase by inositol and growth phase. Inhibition of DGPP phosphatase activity by CDP-diacylglyceron and activation of phosphatidylserine synthase activity by DGPP." ]
[ 2000 ]
1
[]
[ "IPR015993" ]
0
1
0
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 2604, 22, 4 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
CDP-diacylglycerol pyrophosphatase
CDP-diacylglycerol pyrophosphatase
CDP-diacylglyc_Pase
4
IPR003764
3,764
N-acetylglucosamine-6-phosphate deacetylase
GlcNAc_6-P_deAcase
Family
23,195
false
false
Three enzymes are required for N-acetylglucosamine (NAG) utilization in Escherichia coli: enzyme IInag (gene nagE), N-acetylglucosamine-6-phosphate deacetylase (gene nagA), and glucosamine-6-phosphate isomerase (gene nagB) [ ]. This entry represents the N-acetylglucosamine-6-phosphate deacetylases (NagA), [ ]. NagA cat...
[ "GO:0008448", "GO:0006044" ]
[ "N-acetylglucosamine-6-phosphate deacetylase activity", "N-acetylglucosamine metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PIRSF", "NCBIFAM", "CDD" ]
[ "PIRSF038994", "TIGR00221", "cd00854" ]
[ "NagA", "nagA", "NagA" ]
[ 22458, 19855, 18561 ]
3
[ "EC", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.5.1.25", "GenProp1303", "GenProp1565", "GenProp1623", "PWY-6906", "PWY-7077", "PWY-7395", "R-BTA-446210", "R-CEL-446210", "R-DME-446210", "R-DRE-446210", "R-HSA-446210", "R-MMU-446210", "R-RNO-446210" ]
[ "EC:3.5.1.25", "GP:GenProp1303", "GP:GenProp1565", "GP:GenProp1623", "METACYC:PWY-6906", "METACYC:PWY-7077", "METACYC:PWY-7395", "REACTOME:R-BTA-446210", "REACTOME:R-CEL-446210", "REACTOME:R-DME-446210", "REACTOME:R-DRE-446210", "REACTOME:R-HSA-446210", "REACTOME:R-MMU-446210", "REACTOME:R...
14
[ "1o12", "1ymy", "1yrr", "2p50", "2p53", "2vhl", "3egj", "3iv8", "6fv3", "6fv4", "6jku", "7nut", "7nuu" ]
13
[ "PUB00008243", "PUB00008244", "PUB00080582" ]
[ "2190615", "9301118", "11395446" ]
[ "Cloning and characterization of the N-acetylglucosamine operon of Escherichia coli.", "Cloning and sequencing of the genes for N-acetylglucosamine use that construct divergent operons (nagE-nagAC) from Vibrio cholerae non-O1.", "Identification of a dedicated recycling pathway for anhydro-N-acetylmuramic acid a...
[ 1990, 1997, 2001 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 80, 19711, 3248, 156 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 8, 3, 1, 2, 3, 4 ]
7
true
Family
N-acetylglucosamine-6-phosphate deacetylase
N-acetylglucosamine-6-phosphate deacetylase
GlcNAc_6-P_deAcase
7
IPR003765
3,765
Nitrate reductase chaperone, NarJ
NO3_reductase_chaperone_NarJ
Family
7,905
false
false
The nitrate-reducing system, nitrate reductase ( ), is stimulated by anaerobiosis, nitrate, and nitrite. The NarJ/delta subunit is not part of the nitrate reductase enzyme but is needed for assembly of the multisubunit enzyme complex. In the absence of the delta subunit the core alpha beta enzyme complex is unstable [ ...
[ "GO:0051082", "GO:0051131" ]
[ "unfolded protein binding", "chaperone-mediated protein complex assembly" ]
[ "molecular_function", "biological_process" ]
2
[ "PANTHER", "NCBIFAM" ]
[ "PTHR43680", "TIGR00684" ]
[ "", "narJ" ]
[ 7868, 7707 ]
2
[ "GP" ]
[ "GenProp0636" ]
[ "GP:GenProp0636" ]
1
[ "8jzc", "8jzd" ]
2
[ "PUB00008245", "PUB00017539", "PUB00053977", "PUB00053978" ]
[ "9738886", "9632249", "1732220", "9305880" ]
[ "Identification and characterization of the Staphylococcus carnosus nitrate reductase operon.", "NarJ is a specific chaperone required for molybdenum cofactor assembly in nitrate reductase A of Escherichia coli.", "The narJ gene product is required for biogenesis of respiratory nitrate reductase in Escherichia ...
[ 1998, 1998, 1992, 1997 ]
4
[ "IPR020945" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Opisthokonta", "unclassified sequences" ]
[ 26, 7792, 5, 82 ]
4
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Family
Nitrate reductase chaperone, NarJ
Nitrate reductase chaperone, NarJ
NO3_reductase_chaperone_NarJ
5
IPR003766
3,766
Uronate isomerase
Uronate_isomerase
Family
9,565
false
false
Uronate isomerase (also known as glucuronate isomerase) catalyses the reaction D-glucuronate to D-fructuronate and also converts D-galacturonate to D-tagaturonate [ ].
[ "GO:0008880", "GO:0006064" ]
[ "glucuronate isomerase activity", "glucuronate catabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "PFAM" ]
[ "MF_00675", "PF02614" ]
[ "UxaC", "UxaC" ]
[ 7623, 9565 ]
2
[ "EC", "GP", "GP", "METACYC", "METACYC" ]
[ "5.3.1.12", "GenProp1387", "GenProp1636", "PWY-7247", "PWY-7248" ]
[ "EC:5.3.1.12", "GP:GenProp1387", "GP:GenProp1636", "METACYC:PWY-7247", "METACYC:PWY-7248" ]
5
[ "1j5s", "2q01", "3iac", "4i6v" ]
4
[ "PUB00009406" ]
[ "9882655" ]
[ "Regulation of hexuronate utilization in Bacillus subtilis." ]
[ 1999 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctCCX1", "unclassified sequences" ]
[ 54, 9349, 25, 2, 135 ]
5
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Uronate isomerase
Uronate isomerase
Uronate_isomerase
5
IPR003767
3,767
Malate/L-lactate dehydrogenase-like
Malate/L-lactate_DH-like
Family
18,968
false
false
The malate dehydrogenase (MDH) of some extremophilies is more similar to the L-lactate dehydrogenases (L-LDH) from various sources than to other MDHs [ ]. This family consists of bacterial and archaeal malate/L-lactate dehydrogenases and related proteins. The archaebacterial malate dehydrogenase , deviates from the eub...
[ "GO:0016491" ]
[ "oxidoreductase activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PANTHER" ]
[ "PF02615", "PTHR11091" ]
[ "Ldh_2", "" ]
[ 18941, 18758 ]
2
[ "EC", "METACYC" ]
[ "1.1.1.130", "PWY-6961" ]
[ "EC:1.1.1.130", "METACYC:PWY-6961" ]
2
[ "1nxu", "1s20", "1v9n", "1vbi", "1wtj", "1x0a", "1xrh", "1z2i", "2cwf", "2cwh", "2g8y", "2x06", "3i0p", "3uoe", "4fjs", "4fju", "4h8a" ]
17
[ "PUB00000381", "PUB00008807" ]
[ "8476859", "2110059" ]
[ "Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui.", "Properties and primary structure of the L-malate dehydrogenase from the extremely thermophilic archaebacterium Methanothermus fervidus." ]
[ 1993, 1990 ]
2
[]
[ "IPR017590", "IPR023689" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 225, 15068, 3231, 444 ]
4
[ "Caenorhabditis elegans", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 2, 10, 3, 2 ]
4
true
Family
Malate/L-lactate dehydrogenase-like
Malate/L-lactate dehydrogenase-like
Malate/L-lactate_DH-like
2
IPR003768
3,768
Segregation and condensation protein A
ScpA
Family
20,815
false
false
This family represents ScpA, which along with ScpB ( ) interacts with SMC in vivo forming a complex that is required for chromosome condensation and segregation [ , ]. The SMC-Scp complex appears to be similar to the MukB-MukE-Muk-F complex in Escherichia coli [ ], where MukB ( ) is the homologue of SMC. ScpA and ScpB ...
[]
[]
[]
0
[ "HAMAP", "PFAM", "PANTHER" ]
[ "MF_01805", "PF02616", "PTHR33969" ]
[ "ScpA", "SMC_ScpA", "" ]
[ 9882, 20563, 20756 ]
3
[ "GP" ]
[ "GenProp0201" ]
[ "GP:GenProp0201" ]
1
[ "3w6j", "3zgx", "4i98", "5h66", "5h67", "5xg3", "6ivh" ]
7
[ "PUB00015249", "PUB00015250", "PUB00015251", "PUB00015252" ]
[ "12065423", "12897137", "10545099", "12100548" ]
[ "Cell cycle-dependent localization of two novel prokaryotic chromosome segregation and condensation proteins in Bacillus subtilis that interact with SMC protein.", "A prokaryotic condensin/cohesin-like complex can actively compact chromosomes from a single position on the nucleoid and binds to DNA as a ring-like ...
[ 2002, 2003, 1999, 2002 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 717, 19567, 25, 506 ]
4
[]
[]
0
true
Family
Segregation and condensation protein A
Segregation and condensation protein A
ScpA
7
IPR003769
3,769
Adaptor protein ClpS, core
ClpS_core
Domain
23,925
false
false
In the bacterial cytosol, ATP-dependent protein degradation is performed by several different chaperone-protease pairs, including ClpAP. ClpS directly influences the ClpAP machine by binding to the N-terminal domain of the chaperone ClpA. The degradation of ClpAP substrates, both SsrA-tagged proteins and ClpA itself, i...
[ "GO:0030163" ]
[ "protein catabolic process" ]
[ "biological_process" ]
1
[ "PFAM" ]
[ "PF02617" ]
[ "ClpS" ]
[ 23925 ]
1
[ "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GenProp0251", "GenProp1754", "R-CEL-983168", "R-DME-983168", "R-HSA-983168", "R-MMU-983168", "R-SPO-983168" ]
[ "GP:GenProp0251", "GP:GenProp1754", "REACTOME:R-CEL-983168", "REACTOME:R-DME-983168", "REACTOME:R-HSA-983168", "REACTOME:R-MMU-983168", "REACTOME:R-SPO-983168" ]
7
[ "1lzw", "1mbu", "1mbv", "1mbx", "1mg9", "1r6o", "1r6q", "2w9r", "2wa8", "2wa9", "3dnj", "3g19", "3g1b", "3g3p", "3gq0", "3gq1", "3gw1", "3o1f", "3o2b", "3o2h", "3o2o", "4o2x", "4yjm", "4yjx", "4yka", "7d34", "7uiv", "7uiw", "7uix", "7uiy", "7uiz", "7uj0"...
39
[ "PUB00013965", "PUB00013966" ]
[ "11931773", "12426582" ]
[ "ClpS, a substrate modulator of the ClpAP machine.", "Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA." ]
[ 2002, 2002 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Marine Group I thaumarchaeote", "Viruses", "unclassified sequences" ]
[ 17478, 6056, 1, 33, 357 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 3, 1, 10, 2, 1, 5, 8, 4, 10, 1, 8 ]
11
true
Domain
Adaptor protein ClpS, core
Adaptor protein ClpS, core
ClpS_core
8
IPR003770
3,770
Endolytic murein transglycosylase
MLTG-like
Family
26,998
false
false
Endolytic murein transglycosylase (also known as MltG, YrrL and YceG) functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation. The structure of E. coli MltG has been solved by X-ray crystallography (PDB: 2r1f). It has an extended N terminus topped by...
[]
[]
[]
0
[ "HAMAP", "PFAM", "PANTHER", "NCBIFAM", "CDD" ]
[ "MF_02065", "PF02618", "PTHR30518", "TIGR00247", "cd08010" ]
[ "MltG", "YceG", "", "", "MltG_like" ]
[ 25544, 26942, 26627, 25388, 20462 ]
5
[ "EC" ]
[ "4.2.2.29" ]
[ "EC:4.2.2.29" ]
1
[ "2r1f", "4iiw", "8yoa", "8yq7" ]
4
[ "PUB00080717" ]
[ "26507882" ]
[ "Identification of MltG as a potential terminase for peptidoglycan polymerization in bacteria." ]
[ 2016 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "candidate division MSBL1 archaeon SCGC-AAA382N08", "unclassified Caudoviricetes", "unclassified sequences" ]
[ 26363, 37, 1, 3, 594 ]
5
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Endolytic murein transglycosylase
Endolytic murein transglycosylase
MLTG-like
7
IPR003772
3,772
Large ribosomal RNA subunit accumulation protein YceD
YceD
Family
23,148
false
false
This family includes the large ribosomal RNA subunit accumulation protein YceD. Gene knockout in Escherichia coli leads to significant reduction of 23S rRNA. These proteins are nearly universally conserved in bacteria and plants. In Nicotiana benthamiana leaves the protein is localized in chloroplasts [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF02620" ]
[ "YceD" ]
[ 23148 ]
1
[]
[]
[]
0
[]
0
[ "PUB00083910" ]
[ "27574185" ]
[ "Essential role of conserved DUF177A protein in plastid 23S rRNA accumulation and plant embryogenesis." ]
[ 2016 ]
1
[]
[ "IPR039255", "IPR044985" ]
0
2
0
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 21750, 932, 466 ]
3
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 8, 1, 8, 5 ]
4
true
Family
Large ribosomal RNA subunit accumulation protein YceD
Large ribosomal RNA subunit accumulation protein YceD
YceD
8
IPR003773
3,773
Menaquinone biosynthesis enzyme
Menaquinone_biosynth
Family
7,823
false
false
This family includes two enzymes which are involved in menaquinone (vitamin K2) biosynthesis. One which catalyses the conversion of cyclic de-hypoxanthine futalosine to 1,4-dihydroxy-6-naphthoate, and one which may be involved in the conversion of chorismate to futalosine [ ]. These enzymes comprise two domains with α/...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02621" ]
[ "VitK2_biosynth" ]
[ 7823 ]
1
[ "EC", "GP", "METACYC", "METACYC" ]
[ "4.2.1.151", "GenProp0829", "PWY-7371", "PWY-7374" ]
[ "EC:4.2.1.151", "GP:GenProp0829", "METACYC:PWY-7371", "METACYC:PWY-7374" ]
4
[ "1zbm", "2czl", "2i6e", "2nxo", "3a3u", "6o9a", "7ahr", "7an5", "7an6", "7an7", "7an8", "7an9", "7ywc" ]
13
[ "PUB00045374", "PUB00057460" ]
[ "18801996", "19602440" ]
[ "An alternative menaquinone biosynthetic pathway operating in microorganisms.", "Crystal structure of MqnD (TTHA1568), a menaquinone biosynthetic enzyme from Thermus thermophilus HB8." ]
[ 2008, 2009 ]
2
[]
[ "IPR030868", "IPR030869" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 280, 7357, 11, 175 ]
4
[]
[]
0
true
Family
Menaquinone biosynthesis enzyme
Menaquinone biosynthesis enzyme
Menaquinone_biosynth
6
IPR003774
3,774
AlgH-like
AlgH-like
Family
19,053
false
false
This entry represents a group of bacterial proteins, including AlgH from Pseudomonas aeruginosa, VC_0467 from Vibrio cholerae and YqgE from Escherichia coli. AlgH is involved in the transcriptional regulation of alginate biosynthesis [ , ]. VC_0467 has been described as a putative translation repressor ( ). This family...
[]
[]
[]
0
[ "HAMAP", "PFAM", "PANTHER", "PANTHER" ]
[ "MF_00758", "PF02622", "PTHR30327", "PTHR31984" ]
[ "UPF0301", "DUF179", "", "" ]
[ 12431, 18770, 15277, 3479 ]
4
[]
[]
[]
0
[ "2aj2", "2do8", "2ew0", "2gs5", "2gzo", "2haf", "2hrx", "2mui" ]
8
[ "PUB00071244", "PUB00104069" ]
[ "7730279", "25857636" ]
[ "Regulation of nucleoside diphosphate kinase and secretable virulence factors in Pseudomonas aeruginosa: roles of algR2 and algH.", "Solution structure and properties of AlgH from Pseudomonas aeruginosa." ]
[ 1995, 2015 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "unclassified sequences", "uncultured Caudovirales phage" ]
[ 15409, 3367, 276, 1 ]
4
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 21, 1, 11, 26 ]
4
true
Family
AlgH-like
AlgH-like
AlgH-like
6
IPR003775
3,775
Flagellar assembly factor FliW
Flagellar_assembly_factor_FliW
Family
4,313
false
false
FliW binds to the C-terminal region of flagellin, which is implicated in polymerisation, and participates in the assembly of the flagellum [ , ]. FliW is part of a three-part feedback loop: in Bacillus subtilis FliW inhibits CsrA (an RNA-binding protein) which inhibits FliC translation; hence FliW is required for FliC ...
[ "GO:0044780" ]
[ "bacterial-type flagellum assembly" ]
[ "biological_process" ]
1
[ "HAMAP", "PFAM", "PANTHER" ]
[ "MF_01185", "PF02623", "PTHR39190" ]
[ "FliW", "FliW", "" ]
[ 3740, 4313, 4216 ]
3
[ "GP" ]
[ "GenProp0881" ]
[ "GP:GenProp0881" ]
1
[ "2aj7", "5dmb", "5dmd", "5jak" ]
4
[ "PUB00043393", "PUB00067598", "PUB00067599" ]
[ "16936039", "17555441", "21895793" ]
[ "Novel conserved assembly factor of the bacterial flagellum.", "CsrA of Bacillus subtilis regulates translation initiation of the gene encoding the flagellin protein (hag) by blocking ribosome binding.", "CsrA-FliW interaction governs flagellin homeostasis and a checkpoint on flagellar morphogenesis in Bacillus...
[ 2006, 2007, 2011 ]
3
[]
[]
0
0
null
[ "Bacteria", "Symbiodiniaceae", "metagenomes" ]
[ 4231, 2, 80 ]
3
[]
[]
0
true
Family
Flagellar assembly factor FliW
Flagellar assembly factor FliW
Flagellar_assembly_factor_FliW
8
IPR003776
3,776
YcaO-like domain
YcaO-like_dom
Domain
12,822
false
false
This domain comprises the whole of a protein in Methanocaldococcus jannaschii and Methanobacterium thermoautotrophicum, all but the N-terminal 60 residues from a protein of Mycobacterium tuberculosis, and all but the C-terminal 180 residues from a protein in Haemophilus influenzae and Escherichia coli, among proteins f...
[]
[]
[]
0
[ "PFAM", "PROFILE", "NCBIFAM" ]
[ "PF02624", "PS51664", "TIGR00702" ]
[ "YcaO", "YCAO", "" ]
[ 12652, 12670, 7495 ]
3
[]
[]
[]
0
[ "4bs9", "4q84", "4q85", "4q86", "4v1t", "4v1u", "4v1v", "6ci7", "6cib", "6gos", "6grg", "6grh", "6gri", "6pe3", "6peu", "7u58" ]
16
[ "PUB00064880", "PUB00067937", "PUB00078765", "PUB00093672" ]
[ "22522320", "21169565", "25129028", "29507203" ]
[ "YcaO domains use ATP to activate amide backbones during peptide cyclodehydrations.", "A proteomic and transcriptomic approach reveals new insight into beta-methylthiolation of Escherichia coli ribosomal protein S12.", "Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis.", "Enzymat...
[ 2012, 2011, 2014, 2018 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes", "uncultured Caudovirales phage" ]
[ 663, 12075, 9, 74, 1 ]
5
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
YcaO-like domain
YcaO-like domain
YcaO-like_dom
9
IPR003777
3,777
XdhC- CoxI
XdhC_CoxI
Domain
22,933
false
false
This domain is often found in association with an NAD-binding region, related to TrkA-N ( ). XdhC is believed to be involved in the attachment of molybdenum to Xanthine Dehydrogenase [ ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF02625" ]
[ "XdhC_CoxI" ]
[ 22933 ]
1
[ "GP" ]
[ "GenProp0705" ]
[ "GP:GenProp0705" ]
1
[ "2we7", "2we8", "3on5" ]
3
[ "PUB00016133" ]
[ "10217763" ]
[ "Role of XDHC in Molybdenum cofactor insertion into xanthine dehydrogenase of Rhodobacter capsulatus." ]
[ 1999 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 280, 22237, 27, 389 ]
4
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Domain
XdhC- CoxI
XdhC- CoxI
XdhC_CoxI
9
IPR003778
3,778
Carboxyltransferase domain, subdomain A and B
CT_A_B
Domain
22,705
false
false
Urea carboxylase (UC) catalyses a two-step, ATP- and biotin-dependent carboxylation reaction of urea. It is composed of biotin carboxylase (BC), carboxyltransferase (CT), and biotin carboxyl carrier protein (BCCP) domains. The CT domain of UC consists of four subdomains, named A, B, C and D. This domain covers the A an...
[]
[]
[]
0
[ "PFAM", "SMART", "NCBIFAM" ]
[ "PF02626", "SM00797", "TIGR00724" ]
[ "CT_A_B", "AHS2", "urea_amlyse_rel" ]
[ 22704, 22505, 18270 ]
3
[]
[]
[]
0
[ "3mml", "3oep", "3opf", "3ore", "3va7", "5dud", "5i8i" ]
7
[ "PUB00064884", "PUB00076467", "PUB00076468", "PUB00076469" ]
[ "9334321", "20884691", "22869039", "22277658" ]
[ "A novel histidine kinase inhibitor regulating development in Bacillus subtilis.", "Dur3 is the major urea transporter in Candida albicans and is co-regulated with the urea amidolyase Dur1,2.", "Structure and function of biotin-dependent carboxylases.", "Crystal structure of urea carboxylase provides insights...
[ 1997, 2011, 2013, 2012 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 93, 20784, 1597, 231 ]
4
[ "Escherichia coli (strain K12)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)" ]
[ 1, 1 ]
2
true
Domain
Carboxyltransferase domain, subdomain A and B
Carboxyltransferase domain, subdomain A and B
CT_A_B
2
IPR003779
3,779
Alkyl hydroperoxide reductase AhpD/CMD-like
AhpD/CMD-like
Domain
90,439
false
false
This entry includes a group of alkyl hydroperoxide reductases, carboxymuconolactone decarboxylase and other decarboxylases, such as Nitrosuccinic acid decarboxylase npaB [ ]. Alkyl hydroperoxide reductases are involved in protection against oxidative stresses [ , , ]. The catechol and protocatechuate branches of the 3-...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02627" ]
[ "CMD" ]
[ 90439 ]
1
[ "EC", "REACTOME" ]
[ "1.11.1.28", "R-HSA-1222541" ]
[ "EC:1.11.1.28", "REACTOME:R-HSA-1222541" ]
2
[ "1gu9", "1knc", "1lw1", "1me5", "1p8c", "1vke", "2af7", "2cwq", "2gmy", "2ijc", "2o4d", "2ouw", "2oyo", "2pfx", "2prr", "2q0t", "2qeu", "3bey", "3c1l", "3d7i", "3lvy", "4g9q", "5dik", "5dip", "6e8l", "6k40", "7xw1", "7y4r" ]
28
[ "PUB00008247", "PUB00022129", "PUB00163378", "PUB00163379", "PUB00163380" ]
[ "9495744", "12761216", "27818650", "35745538", "38588324" ]
[ "Characterization of a protocatechuate catabolic gene cluster from Rhodococcus opacus 1CP: evidence for a merged enzyme with 4-carboxymuconolactone-decarboxylating and 3-oxoadipate enol-lactone-hydrolyzing activity.", "The mechanism of Mycobacterium tuberculosis alkylhydroperoxidase AhpD as defined by mutagenesis...
[ 1998, 2003, 2016, 2022, 2024 ]
5
[]
[ "IPR004675", "IPR012788" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences", "uncultured Caudovirales phage" ]
[ 1644, 83902, 4060, 832, 1 ]
5
[ "Danio rerio", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]
[ 1, 1, 1, 1, 1 ]
5
true
Domain
Alkyl hydroperoxide reductase AhpD/CMD-like
Alkyl hydroperoxide reductase AhpD/CMD-like
AhpD/CMD-like
3
IPR003780
3,780
COX15/CtaA family
COX15/CtaA_fam
Family
21,990
false
false
This is a family of integral membrane proteins. CtaA (also known as heme A synthase) is required for cytochrome aa3 oxidase assembly in Bacillus subtilis [ ]. COX15 is required for cytochrome c oxidase assembly [ ], and is involved in the synthesis of heme A [ , , ]. COX15 forms highly stable complexes through hydropho...
[ "GO:0006784", "GO:0016020" ]
[ "heme A biosynthetic process", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM" ]
[ "PF02628" ]
[ "COX15-CtaA" ]
[ 21990 ]
1
[ "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.17.99.9", "GenProp0614", "R-BTA-189451", "R-BTA-9864848", "R-HSA-189451", "R-HSA-9864848", "R-MMU-189451", "R-MMU-9864848", "R-SCE-189451", "R-SPO-189451" ]
[ "EC:1.17.99.9", "GP:GenProp0614", "REACTOME:R-BTA-189451", "REACTOME:R-BTA-9864848", "REACTOME:R-HSA-189451", "REACTOME:R-HSA-9864848", "REACTOME:R-MMU-189451", "REACTOME:R-MMU-9864848", "REACTOME:R-SCE-189451", "REACTOME:R-SPO-189451" ]
10
[ "6a2j", "6ied", "8aw5" ]
3
[ "PUB00008248", "PUB00070778", "PUB00070779", "PUB00097267", "PUB00097268", "PUB00153672" ]
[ "2549006", "12474143", "9228094", "11248251", "26940873", "11841224" ]
[ "Isolation and sequence of ctaA, a gene required for cytochrome aa3 biosynthesis and sporulation in Bacillus subtilis.", "Mutations in COX15 produce a defect in the mitochondrial heme biosynthetic pathway, causing early-onset fatal hypertrophic cardiomyopathy.", "COX15 codes for a mitochondrial protein essentia...
[ 1989, 2003, 1997, 2001, 2016, 2002 ]
6
[]
[ "IPR023754", "IPR050450" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 522, 16072, 4961, 435 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 4, 1, 1, 1, 3, 1, 1, 3, 4, 1, 1, 6 ]
12
true
Family
COX15/CtaA family
COX15/CtaA family
COX15/CtaA_fam
5
IPR003781
3,781
CoA-binding
CoA-bd
Domain
80,846
false
false
This domain has a Rossmann fold and is found in a number of proteins including bacterial Redox-sensing transcriptional repressor Rex [ ], succinyl CoA synthetases [ ], malate and ATP-citrate ligases [ ].
[]
[]
[]
0
[ "PFAM", "PFAM", "SMART" ]
[ "PF02629", "PF13380", "SM00881" ]
[ "CoA_binding", "CoA_binding_2", "CoA_binding" ]
[ 43769, 36803, 73423 ]
3
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-6798695", "R-BTA-75105", "R-CEL-6798695", "R-CEL-71403", "R-CEL-75105", "R-DDI-71403", "R-DME-71403", "R-HSA-163765", "R-HSA-6798695", "R-HSA-71403", "R-HSA-75105", "R-MMU-6798695", "R-MMU-71403", "R-MMU-75105", "R-RNO-6798695", "R-RNO-71403", "R-RNO-75105", "R-SCE-71403", ...
[ "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-75105", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-71403", "REACTOME:R-CEL-75105", "REACTOME:R-DDI-71403", "REACTOME:R-DME-71403", "REACTOME:R-HSA-163765", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-71403", "REACTOME:R-HSA-75105", "REACTOME:R-MMU-6798695...
22
[ "1cqi", "1cqj", "1euc", "1eud", "1iuk", "1iul", "1jkj", "1jll", "1oi7", "1scu", "1xcb", "1y81", "2csu", "2d59", "2d5a", "2dt5", "2duw", "2e6u", "2fp4", "2fpg", "2fpi", "2fpp", "2nu6", "2nu7", "2nu8", "2nu9", "2nua", "2scu", "2vt2", "2vt3", "2yv1", "2yv2"...
117
[ "PUB00021911", "PUB00032388", "PUB00075004" ]
[ "11781092", "15642260", "23932781" ]
[ "Two glutamate residues, Glu 208 alpha and Glu 197 beta, are crucial for phosphorylation and dephosphorylation of the active-site histidine residue in succinyl-CoA synthetase.", "X-ray structure of a Rex-family repressor/NADH complex insights into the mechanism of redox sensing.", "Acetylation stabilizes ATP-ci...
[ 2002, 2005, 2013 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Sym plasmid", "unclassified sequences" ]
[ 2916, 63932, 12428, 1, 1569 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 7, 4, 11, 7, 5, 9, 5, 4, 1, 13, 1, 2, 13 ]
13
true
Domain
CoA-binding
CoA-binding
CoA-bd
9
IPR003782
3,782
Copper chaperone SCO1/SenC
SCO1/SenC
Family
31,334
false
false
The SCO (an acronym for Synthesis of Cytochrome c Oxidase) family is involved in biogenesis of respiratory and photosynthetic systems. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop.
[]
[]
[]
0
[ "PFAM", "PANTHER", "CDD" ]
[ "PF02630", "PTHR12151", "cd02968" ]
[ "SCO1-SenC", "", "SCO" ]
[ 31224, 29870, 30568 ]
3
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-9864848", "R-DRE-9864848", "R-HSA-5628897", "R-HSA-9864848", "R-MMU-9864848" ]
[ "REACTOME:R-BTA-9864848", "REACTOME:R-DRE-9864848", "REACTOME:R-HSA-5628897", "REACTOME:R-HSA-9864848", "REACTOME:R-MMU-9864848" ]
5
[ "1on4", "1wp0", "1xzo", "2b7j", "2b7k", "2ggt", "2gqk", "2gql", "2gqm", "2gt5", "2gt6", "2gvp", "2hrf", "2hrn", "2k6v", "2rli", "3me7", "3me8", "4bpy", "4hde", "4txo", "4wbj", "4wbr", "6n5u" ]
24
[ "PUB00008249", "PUB00008250", "PUB00032292", "PUB00057824", "PUB00080795", "PUB00080796", "PUB00080797" ]
[ "1944230", "7592491", "15659396", "10837475", "15119951", "15229189", "11546815" ]
[ "Immunological identification of yeast SCO1 protein as a component of the inner mitochondrial membrane.", "Cloning and characterization of senC, a gene involved in both aerobic respiration and photosynthesis gene expression in Rhodobacter capsulatus.", "Crystal structure of human SCO1: implications for redox si...
[ 1991, 1995, 2005, 2000, 2004, 2004, 2001 ]
7
[]
[ "IPR017276" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 458, 24469, 6013, 394 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 6, 1, 2, 1, 5, 5, 1, 4, 5, 2, 1, 9 ]
12
true
Family
Copper chaperone SCO1/SenC
Copper chaperone SCO1/SenC
SCO1/SenC
5
IPR003783
3,783
Regulatory protein RecX
Regulatory_RecX
Family
21,727
false
false
RecX is a putative bacterial regulatory protein [ ]. The gene encoding RecX is found downstream of recA, and it is suggested that the RecX protein might be regulator of RecA activity by interaction with the RecA protein or filament [ ].
[ "GO:0006282" ]
[ "regulation of DNA repair" ]
[ "biological_process" ]
1
[ "HAMAP", "PANTHER" ]
[ "MF_01114", "PTHR33602" ]
[ "RecX", "" ]
[ 18869, 21522 ]
2
[]
[]
[]
0
[ "3c1d", "3d5l", "3dfg", "3e3v" ]
4
[ "PUB00008251" ]
[ "10869079" ]
[ "Transcriptional and mutational analyses of the Streptomyces lividans recX gene and its interference with RecA activity." ]
[ 2000 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Siphoviridae sp. ctj8j9", "unclassified sequences" ]
[ 20717, 644, 1, 365 ]
4
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 4, 1, 4, 7 ]
4
true
Family
Regulatory protein RecX
Regulatory protein RecX
Regulatory_RecX
6
IPR003784
3,784
BioY protein
BioY
Family
14,983
false
false
BioMNY, a high-affinity biotin transporter, is a member of the ECF (energy-coupling factor) transporters. ECF transporters share a common architecture consisting of pairs of ABC (ATP-binding cassette)-containing ATPases, a conserved transmembrane protein and a transmembrane substrate-capture protein. In the case of the...
[ "GO:0015225", "GO:0015878", "GO:0005886" ]
[ "biotin transmembrane transporter activity", "biotin transport", "plasma membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PIRSF", "PANTHER" ]
[ "PF02632", "PIRSF016661", "PTHR34295" ]
[ "BioY", "BioY", "" ]
[ 14982, 14358, 14931 ]
3
[ "GP", "GP" ]
[ "GenProp0036", "GenProp1094" ]
[ "GP:GenProp0036", "GP:GenProp1094" ]
2
[ "4dve" ]
1
[ "PUB00043617", "PUB00061677" ]
[ "17301237", "20738254" ]
[ "Biotin uptake in prokaryotes by solute transporters with an optional ATP-binding cassette-containing module.", "Subunit composition of an energy-coupling-factor-type biotin transporter analysed in living bacteria." ]
[ 2007, 2010 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 586, 14040, 61, 296 ]
4
[]
[]
0
true
Family
BioY protein
BioY protein
BioY
2
IPR003785
3,785
Creatininase/formamide hydrolase
Creatininase/forma_Hydrolase
Family
14,527
false
false
This family includes the enzymes creatininase and 2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase, also known as formamide hydrolase. Creatinase or creatinine amidohydrolase ( ) catalyses the hydrolysis of creatinine to creatine, which can then be metabolised to urea and sarcosine b...
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF02633", "PTHR35005" ]
[ "Creatininase", "" ]
[ 14526, 14366 ]
2
[ "EC", "GP", "METACYC" ]
[ "3.5.1.102", "GenProp1527", "PWY-6167" ]
[ "EC:3.5.1.102", "GP:GenProp1527", "METACYC:PWY-6167" ]
3
[ "1j2t", "1j2u", "1q3k", "1v7z", "3a6d", "3a6e", "3a6f", "3a6g", "3a6h", "3a6j", "3a6k", "3a6l", "3lub", "3no4" ]
14
[ "PUB00021871", "PUB00056772", "PUB00086033" ]
[ "15003455", "19309161", "23441918" ]
[ "Crystal structures of creatininase reveal the substrate binding site and provide an insight into the catalytic mechanism.", "An iron(II) dependent formamide hydrolase catalyzes the second step in the archaeal biosynthetic pathway to riboflavin and 7,8-didemethyl-8-hydroxy-5-deazariboflavin.", "Novel inositol c...
[ 2004, 2009, 2013 ]
3
[]
[ "IPR023871", "IPR024901", "IPR031034", "IPR049842" ]
0
4
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 1420, 12671, 61, 375 ]
4
[]
[]
0
true
Family
Creatininase/formamide hydrolase
Creatininase/formamide hydrolase
Creatininase/forma_Hydrolase
6
IPR003786
3,786
Sulfur carrier protein FdhD
FdhD
Family
17,851
false
false
FdhD is a protein essential for the activity of formate dehydrogenases (FDHs) [ ], but it is not a component of membrane-bound formate dehydrogenase [ ]. In Escherichia coli, it has been shown to function as a sulfurtransferase between IscS to the molybdenum cofactor prior to its insertion into formate dehydrogenase [ ...
[ "GO:0016783" ]
[ "sulfurtransferase activity" ]
[ "molecular_function" ]
1
[ "HAMAP", "PFAM", "PIRSF", "PANTHER", "NCBIFAM" ]
[ "MF_00187", "PF02634", "PIRSF015626", "PTHR30592", "TIGR00129" ]
[ "FdhD", "FdhD-NarQ", "FdhD", "", "fdhD_narQ" ]
[ 16456, 17851, 16903, 17779, 15049 ]
5
[]
[]
[]
0
[ "2pw9", "4pde" ]
2
[ "PUB00009643", "PUB00070731", "PUB00070732", "PUB00084375" ]
[ "2170340", "22194618", "8034623", "25649206" ]
[ "Identification and expression of the Escherichia coli fdhD and fdhE genes, which are involved in the formation of respiratory formate dehydrogenase.", "A sulfurtransferase is essential for activity of formate dehydrogenases in Escherichia coli.", "Catalytic formation of a nitrogenase iron-sulfur cluster.", "...
[ 1990, 2012, 1994, 2015 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 482, 17007, 18, 344 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Sulfur carrier protein FdhD
Sulfur carrier protein FdhD
FdhD
6
IPR003787
3,787
Sulphur relay, DsrE/F-like
Sulphur_relay_DsrE/F-like
Family
22,225
false
false
Four small, soluble proteins (DsrE, DsrF, DsrH and DsrC) are encoded in the dsr gene region of the phototrophic sulphur bacterium Chromatium vinosum D. The dsrAB genes encoding dissimilatory sulphite reductase are part of the gene cluster, dsrABEFHCMK. The remaining proteins that are encoded are a transmembrane protein...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02635" ]
[ "DsrE" ]
[ 22225 ]
1
[]
[]
[]
0
[ "1jx7", "1l1s", "2d1p", "2hy5", "2hyb", "2pd2", "3mc3" ]
7
[ "PUB00008255", "PUB00043028" ]
[ "9695921", "16387657" ]
[ "Sirohaem sulfite reductase and other proteins encoded by genes at the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur.", "Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions." ]
[ 1998, 2006 ]
2
[]
[ "IPR017462", "IPR017463" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1272, 20408, 36, 4, 505 ]
5
[ "Escherichia coli (strain K12)" ]
[ 3 ]
1
true
Family
Sulphur relay, DsrE/F-like
Sulphur relay, DsrE/F-like
Sulphur_relay_DsrE/F-like
1
IPR003788
3,788
Protein arginine methyltransferase NDUFAF7
NDUFAF7
Family
17,101
false
false
NDUFAF7 (NADH:ubiquinone oxidoreductase complex assembly factor 7), also known as MidA or mitochondrial protein midA homologue, plays a role in mitochondrial complex I activity [ ].
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF02636", "PTHR12049" ]
[ "Methyltransf_28", "" ]
[ 16964, 16451 ]
2
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.1.1.320", "R-CEL-6799198", "R-DDI-6799198", "R-DME-6799198", "R-HSA-6799198", "R-MMU-6799198", "R-RNO-6799198", "R-XTR-6799198" ]
[ "EC:2.1.1.320", "REACTOME:R-CEL-6799198", "REACTOME:R-DDI-6799198", "REACTOME:R-DME-6799198", "REACTOME:R-HSA-6799198", "REACTOME:R-MMU-6799198", "REACTOME:R-RNO-6799198", "REACTOME:R-XTR-6799198" ]
8
[ "1zkd", "4f3n", "4g67", "5ztz", "5zu0", "5zzw" ]
6
[ "PUB00057462" ]
[ "20406883" ]
[ "MidA is a putative methyltransferase that is required for mitochondrial complex I function." ]
[ 2010 ]
1
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriota", "unclassified sequences" ]
[ 9146, 7692, 16, 247 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 12, 1, 1, 2, 10, 5, 2, 5, 8, 1, 1, 27 ]
12
true
Family
Protein arginine methyltransferase NDUFAF7
Protein arginine methyltransferase NDUFAF7
NDUFAF7
5
IPR003789
3,789
Aspartyl/glutamyl-tRNA amidotransferase subunit B-like
Asn/Gln_tRNA_amidoTrase-B-like
Homologous_superfamily
47,776
false
false
This domain superfamily is found in GatB and proteins related to bacterial Yqey. The domain is about 140 amino acid residues long. This domain is found at the C terminus of GatB which transamidates Glu-tRNA to Gln-tRNA. The function of this domain is uncertain. It does however suggest that Yqey and its relatives have a...
[ "GO:0016884" ]
[ "carbon-nitrogen ligase activity, with glutamine as amido-N-donor" ]
[ "molecular_function" ]
1
[ "SSF" ]
[ "SSF89095" ]
[ "" ]
[ 47776 ]
1
[ "EC", "METACYC", "METACYC", "METACYC" ]
[ "6.3.5.-", "PWY-5297", "PWY-7811", "PWY-8229" ]
[ "EC:6.3.5.-", "METACYC:PWY-5297", "METACYC:PWY-7811", "METACYC:PWY-8229" ]
4
[ "1ng6", "1zq1", "2d6f", "2df4", "2dqn", "2f2a", "2g5h", "2g5i", "2hz7", "3al0", "3h0l", "3h0m", "3h0r", "3ip4", "3kfu", "4wj3", "8xje", "8xjg", "9ihq", "9ihr" ]
20
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1710, 38588, 6127, 294, 1057 ]
5
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "...
[ 3, 1, 2, 3, 3, 2, 2, 5, 2, 2, 5 ]
11
true
Homologous_superfamily
Aspartyl/glutamyl-tRNA amidotransferase subunit B-like
Aspartyl/glutamyl-tRNA amidotransferase subunit B-like
Asn/Gln_tRNA_amidoTrase-B-like
9
IPR003790
3,790
Glycosyl hydrolase-like 10
GHL10
Domain
11,304
false
false
This TIM barrel domain is found in a group of bacterial glycosyl-hydrolase-like proteins falling into the family GHL10 [ , ].
[]
[]
[]
0
[ "PFAM" ]
[ "PF02638" ]
[ "GHL10" ]
[ 11304 ]
1
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC"...
[ "3.2.1.-", "PWY-1921", "PWY-5821", "PWY-5976", "PWY-6527", "PWY-6717", "PWY-6735", "PWY-6737", "PWY-6749", "PWY-6784", "PWY-6821", "PWY-6848", "PWY-6855", "PWY-6906", "PWY-6972", "PWY-7056", "PWY-7057", "PWY-7074", "PWY-7091", "PWY-7133", "PWY-7134", "PWY-7256", "PWY-7445...
[ "EC:3.2.1.-", "METACYC:PWY-1921", "METACYC:PWY-5821", "METACYC:PWY-5976", "METACYC:PWY-6527", "METACYC:PWY-6717", "METACYC:PWY-6735", "METACYC:PWY-6737", "METACYC:PWY-6749", "METACYC:PWY-6784", "METACYC:PWY-6821", "METACYC:PWY-6848", "METACYC:PWY-6855", "METACYC:PWY-6906", "METACYC:PWY-6...
31
[ "5oq2", "5oq3" ]
2
[ "PUB00057447", "PUB00066710" ]
[ "20556855", "22295578" ]
[ "GH101 family of glycoside hydrolases: subfamily structure and evolutionary connections with other families.", "[GHL1-GHL15: new families of hypothetical glycoside hydrolases]." ]
[ 2010, 2011 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 4, 10929, 224, 147 ]
4
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)" ]
[ 1, 1 ]
2
true
Domain
Glycosyl hydrolase-like 10
Glycosyl hydrolase-like 10
GHL10
4
IPR003791
3,791
Protein of unknown function UPF0178
UPF0178
Family
11,109
false
false
This is a protein of unknown function.
[]
[]
[]
0
[ "HAMAP", "PFAM", "PANTHER" ]
[ "MF_00489", "PF02639", "PTHR35146" ]
[ "UPF0178", "DUF188", "" ]
[ 10580, 11099, 11061 ]
3
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Methanobacteriati", "unclassified sequences" ]
[ 10963, 12, 3, 131 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Protein of unknown function UPF0178
Protein of unknown function UPF0178
UPF0178
6
IPR003793
3,793
UPF0166
UPF0166
Family
4,342
false
false
UPF0166 protein family includes TM_0021 from Thermotoga maritima ( ) and other proteins predominantly found in bacteria but also in some archaea. TM_0021 is a putative PII-like signaling protein thought to be involved in the regulation of the nitrogen status in this organism. The protein adopts a trimeric assembly. Eac...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02641" ]
[ "DUF190" ]
[ 4342 ]
1
[]
[]
[]
0
[ "1o51", "2dcl" ]
2
[ "PUB00029323" ]
[ "14997579" ]
[ "Crystal structure of a putative PII-like signaling protein (TM0021) from Thermotoga maritima at 2.5 A resolution." ]
[ 2004 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Tanacetum cinerariifolium", "unclassified sequences", "uncultured Caudovirales phage" ]
[ 173, 4093, 1, 74, 1 ]
5
[]
[]
0
true
Family
UPF0166
UPF0166
UPF0166
7
IPR003795
3,795
Protein of unknown function DUF192
DUF192
Family
11,272
false
false
This is a protein of unknown function.
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF02643", "PTHR37953" ]
[ "DUF192", "" ]
[ 11272, 9509 ]
2
[]
[]
[]
0
[ "3m7a", "3pjy" ]
2
[]
[]
[]
[]
0
[]
[ "IPR022906" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1094, 9874, 24, 14, 266 ]
5
[]
[]
0
true
Family
Protein of unknown function DUF192
Protein of unknown function DUF192
DUF192
7
IPR003796
3,796
Ribonucleotide reductase regulator NrdR-like
RNR_NrdR-like
Family
19,732
false
false
Ribonucleotide reductases (RNRs) are essential enzymes which catalyse the reduction of ribonucleotides to their respective deoxyribonucleotides, thus providing the precursors necessary for DNA synthesis [ ]. Proteins in this entry are orthologues of the novel transcriptional regulator NrdR ( ) from Streptomyces coelico...
[ "GO:0008270", "GO:0045892" ]
[ "zinc ion binding", "negative regulation of DNA-templated transcription" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "PANTHER", "NCBIFAM" ]
[ "MF_00440", "PTHR30455", "TIGR00244" ]
[ "NrdR", "", "" ]
[ 19583, 19724, 19148 ]
3
[ "GP" ]
[ "GenProp0287" ]
[ "GP:GenProp0287" ]
1
[ "7p37", "7p3f", "7p3q", "9fvr", "9fxk", "9fzf" ]
6
[ "PUB00005164", "PUB00020981", "PUB00020982" ]
[ "8511586", "15522084", "15949864" ]
[ "From RNA to DNA, why so many ribonucleotide reductases?", "Alternative oxygen-dependent and oxygen-independent ribonucleotide reductases in Streptomyces: cross-regulation and physiological role in response to oxygen limitation.", "Identification of a bacterial regulatory system for ribonucleotide reductases by...
[ 1993, 2004, 2005 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 129, 19177, 23, 403 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Ribonucleotide reductase regulator NrdR-like
Ribonucleotide reductase regulator NrdR-like
RNR_NrdR-like
9
IPR003797
3,797
DegV
DegV
Family
25,289
false
false
This family of proteins is related to DegV of Bacillus subtilis and includes paralogous sets in several species (B. subtilis, Deinococcus radiodurans, Mycoplasma pneumoniae) that are closer in percent identity to each other than to most homologues from other species. This suggests both recent paralogy and diversity of ...
[]
[]
[]
0
[ "PFAM", "PROFILE", "NCBIFAM" ]
[ "PF02645", "PS51482", "TIGR00762" ]
[ "DegV", "DEGV", "DegV" ]
[ 25223, 25251, 24549 ]
3
[]
[]
[]
0
[ "1mgp", "1pzx", "1vpv", "2dt8", "2g7z", "3egl", "3fdj", "3fys", "3jr7", "3lup", "3nyi", "3pl5", "4x9x", "5uto", "5uxy", "5v85", "5woo", "6alw", "6b9i", "6cng", "6dj6", "6dke", "6mh9", "6nm1", "6nok", "6nr1", "6nyu", "7scl", "7sg3", "7w7h" ]
30
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 21, 24732, 23, 513 ]
4
[]
[]
0
true
Family
DegV
DegV
DegV
9
IPR003798
3,798
DNA recombination RmuC
DNA_recombination_RmuC
Family
18,618
false
false
This protein contains several bacterial RmuC DNA recombination proteins. The function of the RMUC protein is unknown but it is suspected that it is either a structural protein that protects DNA against nuclease action, or is itself involved in DNA cleavage at the regions of DNA secondary structures [ ]. Proteins in thi...
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF02646", "PTHR30563" ]
[ "RmuC", "" ]
[ 18585, 18514 ]
2
[]
[]
[]
0
[]
0
[ "PUB00020261", "PUB00020736", "PUB00054003" ]
[ "10886369", "15972856", "16011798" ]
[ "Genes involved in the determination of the rate of inversions at short inverted repeats.", "Identification of novel restriction endonuclease-like fold families among hypothetical proteins.", "The PD-(D/E)XK superfamily revisited: identification of new members among proteins involved in DNA metabolism and funct...
[ 2000, 2005, 2005 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 58, 17941, 61, 558 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
DNA recombination RmuC
DNA recombination RmuC
DNA_recombination_RmuC
4
IPR003801
3,801
GTP cyclohydrolase FolE2/MptA
GTP_cyclohydrolase_FolE2/MptA
Family
6,339
false
false
This is a family of prokaryotic/archaeal proteins with type I GTP cyclohydrolase activity. GTP cyclohydrolase I is the first enzyme of the de novo tetrahydrofolate biosynthetic pathway present in bacteria, fungi, and plants, and encoded in Escherichia coli by the folE gene [ ]. FolE is Zinc 2+ dependent [ ]. In bacteri...
[ "GO:0003934" ]
[ "GTP cyclohydrolase I activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PANTHER" ]
[ "PF02649", "PTHR36445" ]
[ "GCHY-1", "" ]
[ 6339, 6313 ]
2
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "3.5.4.16", "PWY-5663", "PWY-6147", "PWY-6703", "PWY-6983", "PWY-7442", "PWY-7852" ]
[ "EC:3.5.4.16", "METACYC:PWY-5663", "METACYC:PWY-6147", "METACYC:PWY-6703", "METACYC:PWY-6983", "METACYC:PWY-7442", "METACYC:PWY-7852" ]
7
[ "2r5r", "3d2o", "5k95", "5k9g", "8g6c", "8g8v", "8tcc" ]
7
[ "PUB00051207", "PUB00057463", "PUB00057465" ]
[ "17032654", "17497938", "19767425" ]
[ "Discovery of a new prokaryotic type I GTP cyclohydrolase family.", "Characterization of an Fe(2+)-dependent archaeal-specific GTP cyclohydrolase, MptA, from Methanocaldococcus jannaschii.", "Zinc-independent folate biosynthesis: genetic, biochemical, and structural investigations reveal new metal dependence fo...
[ 2006, 2007, 2009 ]
3
[]
[ "IPR022838", "IPR022840" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 705, 5454, 11, 2, 167 ]
5
[]
[]
0
true
Family
GTP cyclohydrolase FolE2/MptA
GTP cyclohydrolase FolE2/MptA
GTP_cyclohydrolase_FolE2/MptA
1
IPR003804
3,804
L-lactate permease
Lactate_perm
Family
13,746
false
false
This entry represents a family of L-lactate permeases [ , ]. This family also includes GlcA, a permease for glycolate which is structurally and functionally similar to L-lactate permease and can also transport L-lactate and D-lactate [ , ].
[ "GO:0015129", "GO:0015727", "GO:0005886" ]
[ "lactate transmembrane transporter activity", "lactate transport", "plasma membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PANTHER", "NCBIFAM" ]
[ "PF02652", "PTHR30003", "TIGR00795" ]
[ "Lactate_perm", "", "lctP" ]
[ 13685, 13659, 9921 ]
3
[]
[]
[]
0
[]
0
[ "PUB00019771", "PUB00053899", "PUB00060982", "PUB00060983" ]
[ "8407843", "19201793", "11283302", "11785976" ]
[ "Three overlapping lct genes involved in L-lactate utilization by Escherichia coli.", "A widely conserved gene cluster required for lactate utilization in Bacillus subtilis and its involvement in biofilm formation.", "The gene yghK linked to the glc operon of Escherichia coli encodes a permease for glycolate th...
[ 1993, 2009, 2001, 2002 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctwzt2", "metagenomes" ]
[ 337, 13141, 167, 1, 100 ]
5
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Family
L-lactate permease
L-lactate permease
Lactate_perm
1
IPR003805
3,805
Adenosylcobinamide-GDP ribazoletransferase
CobS
Family
15,827
false
false
Cobalamin (vitamin B12) is a structurally complex cofactor, consisting of a modified tetrapyrrole with a centrally chelated cobalt. Cobalamin is usually found in one of two biologically active forms: methylcobalamin and adocobalamin. Most prokaryotes, as well as animals, have cobalamin-dependent enzymes, whereas plants...
[ "GO:0008818", "GO:0051073" ]
[ "cobalamin 5'-phosphate synthase activity", "adenosylcobinamide-GDP ribazoletransferase activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "HAMAP", "PFAM", "PANTHER", "NCBIFAM" ]
[ "MF_00719", "PF02654", "PTHR34148", "TIGR00317" ]
[ "CobS", "CobS", "", "cobS" ]
[ 15544, 15822, 15606, 9223 ]
4
[ "EC", "GP", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "2.7.8.26", "GenProp0269", "GenProp1349", "GenProp1366", "GenProp1378", "GenProp1454", "PWY-5509", "PWY-6269", "PWY-7961", "PWY-7963", "PWY-7964", "PWY-7965", "PWY-7966", "PWY-7967", "PWY-7968", "PWY-7969", "PWY-7970", "PWY-7975" ]
[ "EC:2.7.8.26", "GP:GenProp0269", "GP:GenProp1349", "GP:GenProp1366", "GP:GenProp1378", "GP:GenProp1454", "METACYC:PWY-5509", "METACYC:PWY-6269", "METACYC:PWY-7961", "METACYC:PWY-7963", "METACYC:PWY-7964", "METACYC:PWY-7965", "METACYC:PWY-7966", "METACYC:PWY-7967", "METACYC:PWY-7968", "...
18
[]
0
[ "PUB00008256", "PUB00009744", "PUB00014672", "PUB00015657", "PUB00035308", "PUB00035309", "PUB00035310", "PUB00035334", "PUB00070131", "PUB00074102" ]
[ "10518530", "11215515", "11153269", "12869542", "17163662", "16042605", "12055304", "15133100", "23922391", "17209023" ]
[ "In vitro synthesis of the nucleotide loop of cobalamin by Salmonella typhimurium enzymes.", "Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.", "Multiple biosynthetic pathways for vitamin B12: variations on a central theme.", "Comparative genomics of the vitamin B12 metabolism and regulation i...
[ 1999, 2000, 2001, 2003, 2006, 2005, 2002, 2004, 2013, 2007 ]
10
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 803, 14724, 81, 219 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Adenosylcobinamide-GDP ribazoletransferase
Adenosylcobinamide-GDP ribazoletransferase
CobS
5
IPR003806
3,806
ATP-grasp fold, PylC-type
ATP-grasp_PylC-type
Domain
6,383
false
false
The ATP-grasp fold is one of several distinct ATP-binding folds, and is found in enzymes that catalyze the formation of amide bonds, catalyzing the ATP-dependent ligation of a carboxylate-containing molecule to an amino or thiol group-containing molecule [ ]. This fold is found in many different enzyme families, includ...
[ "GO:0005524", "GO:0046872" ]
[ "ATP binding", "metal ion binding" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM" ]
[ "PF02655" ]
[ "ATP-grasp_3" ]
[ 6383 ]
1
[]
[]
[]
0
[ "2pn1", "3df7", "4ffl", "4ffm", "4ffn", "4ffo", "4ffp", "4ffr", "8yi6" ]
9
[ "PUB00015342", "PUB00020972", "PUB00028114", "PUB00065010" ]
[ "7862655", "9416615", "12392708", "22985965" ]
[ "A common fold for peptide synthetases cleaving ATP to ADP: glutathione synthetase and D-alanine:d-alanine ligase of Escherichia coli.", "A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity.", "Mutational analysis of ATP-grasp residues in the two ATP sites of Saccharomyce...
[ 1995, 1997, 2002, 2012 ]
4
[ "IPR011761" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 708, 5093, 456, 5, 121 ]
5
[]
[]
0
true
Domain
ATP-grasp fold, PylC-type
ATP-grasp fold, PylC-type
ATP-grasp_PylC-type
6