LiteFold/InterPro · Datasets at Hugging Face

IPR011737

11,737

Uncharacterized protein TP_0381/YwaF

TP_0381/YwaF

Family

3,003

false

This entry represents a family of hydrophobic proteins with seven predicted transmembrane α helices. Members are found in Bacillus subtilis (ywaF), TP0381 from Treponema pallidum (TP0381), Streptococcus pyogenes, Rhodococcus erythropolis, etc.

[]

0

[ "NCBIFAM" ]

[ "TIGR02206" ]

[ "intg_mem_TP0381" ]

[ 3003 ]

1

[]

0

[]

0

[]

0

[ "IPR059250" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "Nitrososphaerota", "metagenomes" ]

[ 2936, 2, 2, 63 ]

4

[]

0

true

Family

Uncharacterized protein TP_0381/YwaF

TP_0381/YwaF

8

IPR011738

11,738

Phage conserved hypothetical protein

Phage_CHP

Family

2,531

false

This entry describes a putative DNA packaging protein from bacteriophage 16-3, related proteins in other bacteriophage and prophage regions of bacterial genomes. Homologues are also found in Gene Transfer Agents (GTA) [ ], including ORFg6 (RCAP_rcc01688) of the GTA of Rhodobacter capsulatus (Rhodopseudomonas capsulata)...

[]

0

[ "NCBIFAM" ]

[ "TIGR02215" ]

[ "phage_chp_gp8" ]

[ 2531 ]

1

[ "GP" ]

[ "GenProp0208" ]

[ "GP:GenProp0208" ]

1

[ "6tba", "6te8", "6te9", "6to8", "6toa", "6tui" ]

6

[ "PUB00055430", "PUB00055431" ]

[ "11382219", "12399927" ]

[ "The gene transfer agent of Rhodobacter capsulatus and \"constitutive transduction\" in prokaryotes.", "Evolutionary implications of phylogenetic analyses of the gene transfer agent (GTA) of Rhodobacter capsulatus." ]

[ 2001, 2002 ]

2

[ "IPR021146" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]

[ 2393, 6, 43, 89 ]

4

[]

0

true

Family

Phage conserved hypothetical protein

Phage_CHP

6

IPR011739

11,739

Gene transfer agent, rcc01693

GTA_rcc01693

Family

826

false

This entry represents gene transfer agents (GTAs), which are involved in a novel mechanism for bacterial gene transfer. They resemble small, tailed bacteriophages in ultrastructure and act like generalized transducing prophages. In contrast to functional prophages, GTAs package random fragments of bacterial genomes and...

[]

0

[ "NCBIFAM" ]

[ "TIGR02216" ]

[ "phage_TIGR02216" ]

[ 826 ]

1

[ "GP" ]

[ "GenProp0208" ]

[ "GP:GenProp0208" ]

1

[]

0

[ "PUB00055423", "PUB00055424", "PUB00055431" ]

[ "20532745", "17513139", "12399927" ]

[ "The gene transfer agent of Rhodobacter capsulatus.", "Prophage-like gene transfer agents-novel mechanisms of gene exchange for Methanococcus, Desulfovibrio, Brachyspira, and Rhodobacter species.", "Evolutionary implications of phylogenetic analyses of the gene transfer agent (GTA) of Rhodobacter capsulatus." ]

[ 2010, 2007, 2002 ]

3

[ "IPR019056" ]

[]

1

0

1

[ "Alphaproteobacteria", "Rhodogtaviriformidae", "ecological metagenomes" ]

[ 815, 4, 7 ]

3

[]

0

true

Family

Gene transfer agent, rcc01693

GTA_rcc01693

8

IPR011740

11,740

Domain of unknown function DUF2460

DUF2460

Domain

2,466

false

The entry represents a domain found in a number of conserved hypothetical proteins. Their genes are often, though not always, encoded in apparent phage-derived regions of bacterial chromosomes. The Rhodobacter capsulatus sequence is apparently part of the gene transfer agent [see Fig.1, in ].

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF09343", "TIGR02217" ]

[ "DUF2460", "chp_TIGR02217" ]

[ 2466, 2145 ]

2

[]

0

[ "6tba", "6teb", "6teh", "8gtc" ]

4

[ "PUB00055431" ]

[ "12399927" ]

[ "Evolutionary implications of phylogenetic analyses of the gene transfer agent (GTA) of Rhodobacter capsulatus." ]

[ 2002 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]

[ 2371, 9, 56, 30 ]

4

[]

0

true

Domain

Domain of unknown function DUF2460

DUF2460

9

IPR011741

11,741

Phage conserved hypothetical protein, C-terminal

Phg_2220_C

Domain

1,704

false

This entry represents the conserved C-terminal domain of a family of proteins found exclusively in bacteriophage and in bacterial prophage regions. The functions of this domain and the proteins containing it are unknown.

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF09524", "TIGR02220" ]

[ "Phg_2220_C", "phg_TIGR02220" ]

[ 1704, 1229 ]

2

[ "GP" ]

[ "GenProp0208" ]

[ "GP:GenProp0208" ]

1

[]

0

[]

0

[]

0

null

[ "Bacteria", "Opisthokonta", "Viruses", "metagenomes" ]

[ 1522, 4, 143, 35 ]

4

[]

0

true

Domain

Phage conserved hypothetical protein, C-terminal

Phg_2220_C

2

IPR011743

11,743

Caa(3)-type oxidase, subunit IV

Caa3_sub_IV

Family

1,046

false

This entry represents a small set of proteins with weak similarity to the sequences , which describes the cytochrome C oxidase subunit IV [ ].

[]

0

[ "NCBIFAM" ]

[ "TIGR02229" ]

[ "caa3_sub_IV" ]

[ 1046 ]

1

[ "GP" ]

[ "GenProp0614" ]

[ "GP:GenProp0614" ]

1

[]

0

[ "PUB00015306" ]

[ "11133964" ]

[ "Gene cluster of Rhodothermus marinus high-potential iron-sulfur Protein: oxygen oxidoreductase, a caa(3)-type oxidase belonging to the superfamily of heme-copper oxidases." ]

[ 2001 ]

1

[ "IPR005171" ]

[]

1

0

1

[ "Bacteria", "Methanobacteriati", "ecological metagenomes" ]

[ 975, 6, 65 ]

3

[]

0

true

Family

Caa(3)-type oxidase, subunit IV

Caa3_sub_IV

9

IPR011744

11,744

F0F1-ATPase subunit, putative

ATPase_gene1

Family

847

false

This entry represents a protein found encoded in F1F0-ATPase operons in several genomes, including Methanosarcina barkeri (archaeal) and Chlorobium tepidum (bacterial). It is a small protein (about 100 amino acids) with long hydrophic stretches and is presumed to be a subunit of the enzyme [ ].

[]

0

[ "NCBIFAM" ]

[ "TIGR02230" ]

[ "ATPase_gene1" ]

[ 847 ]

1

[]

0

[]

0

[ "PUB00015307" ]

[ "9425287" ]

[ "F0F1-ATPase genes from an archaebacterium, Methanosarcina barkeri." ]

[ 1997 ]

1

[ "IPR032820" ]

[]

1

0

1

[ "Bacteria", "Methanomicrobia", "Symbiodinium necroappetens", "ecological metagenomes" ]

[ 793, 27, 1, 26 ]

4

[]

0

true

Family

F0F1-ATPase subunit, putative

ATPase_gene1

6

IPR011745

11,745

RNA polymerase sigma-70, Myxococcus xanthus

RNA_pol_sigma70_MYXXA

Family

374

false

The bacterial core RNA polymerase complex, which consists of five subunits, is sufficient for transcription elongation and termination but is unable to initiate transcription. Transcription initiation from promoter elements requires a sixth, dissociable subunit called a sigma factor, which reversibly associates with th...

[]

0

[ "NCBIFAM" ]

[ "TIGR03001" ]

[ "Sig-70_gmx1" ]

[ 374 ]

1

[]

0

[]

0

[ "PUB00000061", "PUB00002181", "PUB00004340", "PUB00088319" ]

[ "3052291", "1597408", "3092189", "25596450" ]

[ "Structure and function of bacterial sigma factors.", "The sigma 70 family: sequence conservation and evolutionary relationships.", "Sigma factors from E. coli, B. subtilis, phage SP01, and phage T4 are homologous proteins.", "Plastid sigma factors: Their individual functions and regulation in transcription."...

[ 1988, 1992, 1986, 2015 ]

4

[]

0

null

[ "Pseudomonadati" ]

[ 374 ]

1

[]

0

true

Family

RNA polymerase sigma-70, Myxococcus xanthus

RNA_pol_sigma70_MYXXA

1

IPR011747

11,747

Conserved hypothetical protein CHP02241

CHP02241

Family

7,505

false

This entry consists of uncharacterised proteins. All members so far represent bacterial genes found in apparent phage or otherwise laterally transferred regions of the chromosome. Tentatively identified neighbouring proteins tend to be phage tail region proteins. In some species, including Photorhabdus luminescens subs...

[]

0

[ "PANTHER", "NCBIFAM" ]

[ "PTHR38009", "TIGR02241" ]

[ "", "" ]

[ 7489, 7164 ]

2

[]

0

[ "6j0b", "6j0f", "6j0n", "6rao", "6rap", "6rbn", "7adz", "7ae0", "7aeb", "7aef", "7b5h", "7b5i", "8bl4", "9gtp", "9gts", "9qgl", "9qgn" ]

17

[]

0

[ "IPR010667" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "metagenomes" ]

[ 162, 7263, 30, 10, 40 ]

5

[]

0

true

Family

Conserved hypothetical protein CHP02241

CHP02241

1

IPR011748

11,748

Uncharacterised protein family, phage tail-like

Unchr_phage_tail-like

Domain

1,748

false

This entry describes a region of sequence similarity shared by a number of uncharacterised proteins in bacterial genomes, including Geobacter sulfurreducens PCA, Rhizobium loti (Mesorhizobium loti), Streptomyces coelicolor (strain A3(2)), Gloeobacter violaceus PCC 7421, and Myxococcus xanthus. In all cases, the genomic...

[]

0

[ "NCBIFAM" ]

[ "TIGR02242" ]

[ "tail_TIGR02242" ]

[ 1748 ]

1

[ "GP" ]

[ "GenProp0208" ]

[ "GP:GenProp0208" ]

1

[ "9gtp" ]

1

[]

0

[]

0

null

[ "Bacteria", "Myoviridae sp. ctB7y8", "Stenosarchaea group", "metagenomes" ]

[ 1681, 1, 53, 13 ]

4

[]

0

true

Domain

Uncharacterised protein family, phage tail-like

Unchr_phage_tail-like

8

IPR011749

11,749

Conserved hypothetical protein CHP02243

CHP02243

Family

2,928

false

This family consists of a large, conserved hypothetical protein in phage tail-like regions of at least six bacterial genomes: Gloeobacter violaceus PCC 7421, Geobacter sulfurreducens PCA, Streptomyces coelicolor (strain A3(2)), Streptomyces avermitilis MA-4680, Rhizobium loti (Mesorhizobium loti), and Myxococcus xanthu...

[]

0

[ "NCBIFAM" ]

[ "TIGR02243" ]

[ "" ]

[ 2928 ]

1

[]

0

[ "9gtp" ]

1

[]

0

[]

0

null

[ "Archaea", "Bacteria", "ecological metagenomes" ]

[ 85, 2833, 10 ]

3

[]

0

true

Family

Conserved hypothetical protein CHP02243

CHP02243

1

IPR011750

11,750

Myxococcus xanthus double-CXXCG motif

Gmx_para_CXXCG

Family

359

false

This entry consists of at least 10 paralogous proteins from Myxococcus xanthus that lack detectable sequence similarity to any other protein family. An imperfectly conserved CXXCG motif, a probable binding site, appears twice in the multiple sequence alignment.

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF09535", "TIGR02264" ]

[ "Gmx_para_CXXCG", "gmx_para_CXXCG" ]

[ 359, 325 ]

2

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria" ]

[ 359 ]

1

[]

0

true

Family

Myxococcus xanthus double-CXXCG motif

Gmx_para_CXXCG

4

IPR011751

11,751

Myxococcus xanthus paralogous protein 2265

Mxa_paralog_2265

Family

1,012

false

This family consists of a set of at least 17 paralogous proteins in Myxococcus xanthus (strain DK 1622). Members are about 200 amino acids in length. No other homologuess are known; the function is unknown.

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF09536", "TIGR02265" ]

[ "DUF2378", "Mxa_TIGR02265" ]

[ 992, 1001 ]

2

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria" ]

[ 1012 ]

1

[]

0

true

Family

Myxococcus xanthus paralogous protein 2265

Mxa_paralog_2265

2

IPR011752

11,752

PilZ domain, Myxococcales-type

PilV_Myxo-type

Domain

597

false

This entry represents predicted PilZ domain found mainly in Myxococcales. The ubiquitous bacterial second messenger cyclic-di-GMP (c-di-GMP) is associated with the regulation of biofilm formation, the control of exopolysaccharide synthesis, flagellar- and pili-based motility, gene expression, interactions of bacteria w...

[]

0

[ "NCBIFAM" ]

[ "TIGR02266" ]

[ "gmx_TIGR02266" ]

[ 597 ]

1

[]

0

[]

0

[ "PUB00049330", "PUB00054999", "PUB00055000", "PUB00098203" ]

[ "18034161", "16249258", "16920715", "31740493" ]

[ "The structural basis of cyclic diguanylate signal transduction by PilZ domains.", "PilZ domain is part of the bacterial c-di-GMP binding protein.", "The PilZ domain is a receptor for the second messenger c-di-GMP: the PilZ domain protein YcgR controls motility in enterobacteria.", "Structural Conservation an...

[ 2007, 2006, 2006, 2020 ]

4

[ "IPR009875" ]

[]

1

0

1

[ "Bacteria", "marine sediment metagenome" ]

[ 595, 2 ]

2

[]

0

true

Domain

PilZ domain, Myxococcales-type

PilV_Myxo-type

7

IPR011753

11,753

DUSAM domain

DUSAM_dom

Domain

241

false

This domain is found in at least eight paraloguous proteins in Myxococcus xanthus and six in Stigmatella aurantiaca DW4/3-1, both members of Myxococcales order within the Deltaproteobacteria. The function is unknown. Some proteins consist of two copies of the domain. This domain is hereby named DUSAM, DUplication in St...

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF09543", "TIGR02267" ]

[ "DUF2379", "" ]

[ 241, 229 ]

2

[]

0

[]

0

[]

0

[]

0

null

[ "Pseudomonadati" ]

[ 241 ]

1

[]

0

true

Domain

DUSAM domain

DUSAM_dom

1

IPR011754

11,754

Myxococcus xanthus paralogous protein 2268

Mxa_paralog_2268

Family

776

false

This family consists of at least 8 paralogs in Myxococcus xanthus, a member of the Deltaproteobacteria. The function is unknown.

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF09544", "TIGR02268" ]

[ "DUF2381", "" ]

[ 776, 566 ]

2

[]

0

[]

0

[]

0

[]

0

null

[ "Myxococcota" ]

[ 776 ]

1

[]

0

true

Family

Myxococcus xanthus paralogous protein 2268

Mxa_paralog_2268

9

IPR011755

11,755

Conserved hypothetical protein CHP02269, MYXXA

CHP02269_MYXXA

Family

427

false

This family represents a group of uncharacterised proteins from Myxococcales, including CHP02269, MYXXA from Stigmatella aurantiaca and at least 9 paralogues in Myxococcus xanthus. One appears truncated toward the N-terminal; the others are predicted lipoproteins. The function is unknown.

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF09533", "TIGR02269" ]

[ "DUF2380", "" ]

[ 427, 231 ]

2

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria", "Eukaryota" ]

[ 414, 13 ]

2

[]

0

true

Family

Conserved hypothetical protein CHP02269, MYXXA

CHP02269_MYXXA

5

IPR011757

11,757

Lytic transglycosylase MltB

Lytic_transglycosylase_MltB

Family

5,733

false

This family consists of lytic murein transglycosylases (murein hydrolases) related to MltB ( ), which is a 38kDa membrane-bound lipoprotein in Escherichia coli. The N-terminal region of this protein contains a lipoprotein-processing site which is conserved in about half the members of this family. Proteolytic cleavage ...

[]

0

[ "NCBIFAM" ]

[ "TIGR02282" ]

[ "MltB" ]

[ 5733 ]

1

[]

0

[ "1d0k", "1d0l", "1d0m", "1ltm", "1qdr", "1qdt", "1qus", "1qut", "4anr", "5o8x" ]

10

[ "PUB00024079", "PUB00027135", "PUB00028076", "PUB00028077", "PUB00028078" ]

[ "10684641", "9761817", "7476170", "10545329", "10570954" ]

[ "Crystallographic studies of the interactions of Escherichia coli lytic transglycosylase Slt35 with peptidoglycan.", "Accelerated X-ray structure elucidation of a 36 kDa muramidase/transglycosylase using wARP.", "Cloning and expression of a murein hydrolase lipoprotein from Escherichia coli.", "Crystal struct...

[ 2000, 1998, 1995, 1999, 1999 ]

5

[ "IPR043426" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 5642, 12, 79 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Lytic transglycosylase MltB

Lytic_transglycosylase_MltB

6

IPR011758

11,758

Alpha-L-glutamate ligase-related protein

RimK-rel_E_lig

Family

2,052

false

Members of this protein family contain a region of homology to the RimK family of alpha-L-glutamate ligases ( ), various members of which modify the Glu-Glu C terminus of ribosomal protein S6, or tetrahydromethanopterin, or a form of coenzyme F420 derivative. Members of this family are found so far in various Vibrio an...

[]

0

[ "NCBIFAM" ]

[ "TIGR02291" ]

[ "rimK_rel_E_lig" ]

[ 2052 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria", "Eukaryota", "metagenomes", "unclassified Candidatus Methanogaster" ]

[ 2039, 2, 9, 2 ]

4

[]

0

true

Family

Alpha-L-glutamate ligase-related protein

RimK-rel_E_lig

8

IPR011759

11,759

Cytochrome C oxidase subunit II, transmembrane domain

Cyt_c_oxidase_su2_TM_dom

Domain

92,548

false

Cytochrome c oxidase ( ) [ , ] is an oligomeric enzymatic complex which is a component of the respiratory chain and is involved in the transfer of electrons from cytochrome c to oxygen. In eukaryotes this enzyme complex is located in the mitochondrial inner membrane; in aerobic prokaryotes it is found in the plasma mem...

[ "GO:0022900", "GO:0016020" ]

[ "electron transport chain", "membrane" ]

[ "biological_process", "cellular_component" ]

2

[ "PFAM", "PROFILE" ]

[ "PF02790", "PS50999" ]

[ "COX2_TM", "COX2_TM" ]

[ 82821, 91632 ]

2

[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REA...

[ "7.1.1.9", "PWY-3781", "PWY-4521", "PWY-6692", "PWY-7279", "PWY-7429", "PWY-8271", "PDOC00075", "R-BTA-5419276", "R-BTA-5628897", "R-BTA-611105", "R-BTA-9707564", "R-BTA-9864848", "R-CEL-5419276", "R-DDI-9837999", "R-DME-5419276", "R-DME-5628897", "R-DME-611105", "R-DME-9707564",...

[ "EC:7.1.1.9", "METACYC:PWY-3781", "METACYC:PWY-4521", "METACYC:PWY-6692", "METACYC:PWY-7279", "METACYC:PWY-7429", "METACYC:PWY-8271", "PROSITEDOC:PDOC00075", "REACTOME:R-BTA-5419276", "REACTOME:R-BTA-5628897", "REACTOME:R-BTA-611105", "REACTOME:R-BTA-9707564", "REACTOME:R-BTA-9864848", "RE...

45

[ "1ar1", "1fft", "1m56", "1m57", "1occ", "1oco", "1ocr", "1ocz", "1qle", "1v54", "1v55", "2dyr", "2dys", "2eij", "2eik", "2eil", "2eim", "2ein", "2gsm", "2occ", "2y69", "2ybb", "2yev", "2zxw", "3abk", "3abl", "3abm", "3ag1", "3ag2", "3ag3", "3ag4", "3asn"...

179

[ "PUB00000581", "PUB00002253", "PUB00005218" ]

[ "6307356", "8083153", "8638158" ]

[ "Structure of cytochrome c oxidase.", "The superfamily of heme-copper respiratory oxidases.", "The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A." ]

[ 1983, 1994, 1996 ]

3

[]

0

null

[ "Archaea", "Bacteria", "Caulobacter phage CcrPW", "Eukaryota", "unclassified sequences" ]

[ 307, 20802, 1, 71173, 265 ]

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, 2, 2, 9, 1, 505, 3, 1, 4, 6, 1, 1, 6 ]

13

true

Domain

Cytochrome C oxidase subunit II, transmembrane domain

Cyt_c_oxidase_su2_TM_dom

5

IPR011760

11,760

Pseudouridine synthase, TruD, insertion domain

PsdUridine_synth_TruD_insert

Domain

13,860

false

Pseudouridine synthases catalyse the isomerisation of uridine to pseudouridine (Psi) in a variety of RNA molecules, and may function as RNA chaperones. Pseudouridine is the most abundant modified nucleotide found in all cellular RNAs. There are four distinct families of pseudouridine synthases that share no global sequ...

[ "GO:0003723", "GO:0009982", "GO:0001522", "GO:0009451" ]

[ "RNA binding", "pseudouridine synthase activity", "pseudouridine synthesis", "RNA modification" ]

[ "molecular_function", "molecular_function", "biological_process", "biological_process" ]

4

[ "PROFILE" ]

[ "PS50984" ]

[ "TRUD" ]

[ 13860 ]

1

[ "EC", "PROSITEDOC", "REACTOME" ]

[ "5.4.99.27", "PDOC50984", "R-HSA-6782315" ]

[ "EC:5.4.99.27", "PROSITEDOC:PDOC50984", "REACTOME:R-HSA-6782315" ]

3

[ "1sb7", "1si7", "1szw", "1z2z", "5kkp", "7am2", "7mzv" ]

7

[ "PUB00014308", "PUB00015731", "PUB00015813", "PUB00045922", "PUB00092579" ]

[ "12756329", "15135053", "15208439", "10529181", "19664587" ]

[ "A novel unanticipated type of pseudouridine synthase with homologs in bacteria, archaea, and eukarya.", "X-ray structure of tRNA pseudouridine synthase TruD reveals an inserted domain with a novel fold.", "Crystal structure of the highly divergent pseudouridine synthase TruD reveals a circular permutation of a...

[ 2003, 2004, 2004, 1999, 2009 ]

5

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 959, 6043, 6742, 116 ]

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",...

[ 5, 1, 14, 1, 1, 7, 4, 1, 7, 8, 1, 1, 28 ]

13

true

Domain

Pseudouridine synthase, TruD, insertion domain

PsdUridine_synth_TruD_insert

2

IPR011761

11,761

ATP-grasp fold

ATP-grasp

Domain

369,673

false

The ATP-grasp superfamily currently includes 17 groups of enzymes, catalysing ATP-dependent ligation of a carboxylate containing molecule to an amino or thiol group-containing molecule [ ]. They contribute predominantly to macromolecular synthesis. ATP-hydrolysis is used to activate a substrate. For example, DD-ligase ...

[ "GO:0005524", "GO:0046872" ]

[ "ATP binding", "metal ion binding" ]

[ "molecular_function", "molecular_function" ]

2

[ "PROFILE" ]

[ "PS50975" ]

[ "ATP_GRASP" ]

[ 369673 ]

1

[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...

[ "PDOC50975", "R-BTA-1855167", "R-BTA-1855204", "R-BTA-196780", "R-BTA-70263", "R-BTA-70268", "R-BTA-73817", "R-BTA-8964539", "R-BTA-983231", "R-CEL-196780", "R-CEL-500753", "R-CEL-70263", "R-CEL-70268", "R-CEL-71032", "R-CEL-71403", "R-DDI-196780", "R-DDI-200425", "R-DDI-500753", ...

[ "PROSITEDOC:PDOC50975", "REACTOME:R-BTA-1855167", "REACTOME:R-BTA-1855204", "REACTOME:R-BTA-196780", "REACTOME:R-BTA-70263", "REACTOME:R-BTA-70268", "REACTOME:R-BTA-73817", "REACTOME:R-BTA-8964539", "REACTOME:R-BTA-983231", "REACTOME:R-CEL-196780", "REACTOME:R-CEL-500753", "REACTOME:R-CEL-7026...

92

[ "1a9x", "1b6r", "1b6s", "1bnc", "1bxr", "1c30", "1c3o", "1ce8", "1cqi", "1cqj", "1cs0", "1dv1", "1dv2", "1e4e", "1ehi", "1eyz", "1ez1", "1glv", "1gsa", "1gsh", "1gso", "1iov", "1iow", "1jdb", "1jkj", "1jll", "1kee", "1kj8", "1kj9", "1kji", "1kjj", "1kjq"...

384

[ "PUB00015340", "PUB00015341", "PUB00015342", "PUB00020972" ]

[ "7939684", "8804825", "7862655", "9416615" ]

[ "Vancomycin resistance: structure of D-alanine:D-alanine ligase at 2.3 A resolution.", "Structural classification of proteins: new superfamilies.", "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...

[ 1994, 1996, 1995, 1997 ]

4

[]

[ "IPR003806", "IPR004218", "IPR005479", "IPR009720", "IPR011095", "IPR013650", "IPR013651", "IPR020561", "IPR039523" ]

0

9

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 8809, 285487, 70313, 58, 5006 ]

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",...

[ 66, 16, 69, 19, 11, 60, 39, 9, 21, 80, 9, 6, 140 ]

13

true

Domain

ATP-grasp fold

ATP-grasp

1

IPR011762

11,762

Acetyl-coenzyme A carboxyltransferase, N-terminal

COA_CT_N

Domain

99,976

false

Acetyl-coenzyme A carboxylase ( ) (ACC), a member of the biotin-dependent enzyme family, catalyses the formation of malonyl-coenzyme A (CoA) and regulates fatty acid biosynthesis and oxidation. Biotin-dependent carboxylase enzymes perform a two step reaction: enzyme-bound biotin is first carboxylated by bicarbonate and...

[]

0

[ "PROFILE" ]

[ "PS50980" ]

[ "COA_CT_NTER" ]

[ 99976 ]

1

[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "RE...

[ "2.1.3.15", "PWY-4381", "PWY-5743", "PWY-5744", "PWY-5789", "PWY-6722", "PDOC50980", "R-CEL-196780", "R-CEL-70895", "R-DDI-196780", "R-DDI-200425", "R-DDI-70895", "R-DDI-75105", "R-DME-196780", "R-DME-70895", "R-HSA-163765", "R-HSA-196780", "R-HSA-200425", "R-HSA-2426168", "R-H...

[ "EC:2.1.3.15", "METACYC:PWY-4381", "METACYC:PWY-5743", "METACYC:PWY-5744", "METACYC:PWY-5789", "METACYC:PWY-6722", "PROSITEDOC:PDOC50980", "REACTOME:R-CEL-196780", "REACTOME:R-CEL-70895", "REACTOME:R-DDI-196780", "REACTOME:R-DDI-200425", "REACTOME:R-DDI-70895", "REACTOME:R-DDI-75105", "REA...

46

[ "1od2", "1od4", "1on3", "1on9", "1pix", "1uyr", "1uys", "1uyt", "1uyv", "1vrg", "1w2x", "1x0u", "1xnv", "1xnw", "1xny", "1xo6", "2a7s", "2bzr", "2f9i", "2f9y", "2x24", "3ff6", "3gf3", "3gf7", "3glm", "3gma", "3h0j", "3h0q", "3h0s", "3iav", "3ib9", "3ibb"...

115

[ "PUB00000064", "PUB00015343", "PUB00015346" ]

[ "2673009", "11851389", "12663926" ]

[ "The mechanism of biotin-dependent enzymes.", "Chemical and catalytic mechanisms of carboxyl transfer reactions in biotin-dependent enzymes.", "Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase." ]

[ 1989, 2002, 2003 ]

3

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 2261, 62831, 33691, 1193 ]

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",...

[ 22, 7, 54, 5, 1, 53, 17, 2, 7, 28, 2, 1, 154 ]

13

true

Domain

Acetyl-coenzyme A carboxyltransferase, N-terminal

COA_CT_N

9

IPR011763

11,763

Acetyl-coenzyme A carboxyltransferase, C-terminal

COA_CT_C

Domain

85,460

false

Acetyl-coenzyme A carboxylase ( ) (ACC), a member of the biotin-dependent enzyme family, catalyses the formation of malonyl-coenzyme A (CoA) and regulates fatty acid biosynthesis and oxidation. Biotin-dependent carboxylase enzymes perform a two step reaction: enzyme-bound biotin is first carboxylated by bicarbonate and...

[ "GO:0016874" ]

[ "ligase activity" ]

[ "molecular_function" ]

1

[ "PROFILE" ]

[ "PS50989" ]

[ "COA_CT_CTER" ]

[ 85460 ]

1

[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "RE...

[ "2.1.3.15", "PWY-4381", "PWY-5743", "PWY-5744", "PWY-5789", "PWY-6722", "PDOC50980", "R-CEL-196780", "R-CEL-70895", "R-DDI-196780", "R-DDI-200425", "R-DDI-70895", "R-DDI-75105", "R-DME-196780", "R-DME-70895", "R-HSA-163765", "R-HSA-196780", "R-HSA-200425", "R-HSA-2426168", "R-H...

[ "EC:2.1.3.15", "METACYC:PWY-4381", "METACYC:PWY-5743", "METACYC:PWY-5744", "METACYC:PWY-5789", "METACYC:PWY-6722", "PROSITEDOC:PDOC50980", "REACTOME:R-CEL-196780", "REACTOME:R-CEL-70895", "REACTOME:R-DDI-196780", "REACTOME:R-DDI-200425", "REACTOME:R-DDI-70895", "REACTOME:R-DDI-75105", "REA...

46

[ "1od2", "1od4", "1on3", "1on9", "1pix", "1uyr", "1uys", "1uyt", "1uyv", "1vrg", "1w2x", "1x0u", "1xnv", "1xnw", "1xny", "1xo6", "2a7s", "2bzr", "2f9i", "2f9y", "2x24", "3ff6", "3gf3", "3gf7", "3glm", "3gma", "3h0j", "3h0q", "3h0s", "3iav", "3ib9", "3ibb"...

113

[ "PUB00000064", "PUB00015343", "PUB00015346" ]

[ "2673009", "11851389", "12663926" ]

[ "The mechanism of biotin-dependent enzymes.", "Chemical and catalytic mechanisms of carboxyl transfer reactions in biotin-dependent enzymes.", "Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase." ]

[ 1989, 2002, 2003 ]

3

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 2213, 63015, 18959, 1273 ]

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",...

[ 18, 7, 52, 5, 1, 48, 16, 2, 8, 29, 2, 1, 149 ]

13

true

Domain

Acetyl-coenzyme A carboxyltransferase, C-terminal

COA_CT_C

9

IPR011764

11,764

Biotin carboxylation domain

Biotin_carboxylation_dom

Domain

93,171

false

Biotin-dependent carboxylase enzymes perform a two step reaction. Enzyme-bound biotin is first carboxylated by bicarbonated and ATP and the carboxyl group temporarily bound to biotin is subsequently transferred to an acceptor substrate such as pyruvate or acetyl-CoA. The first step is mediated by the BC domain common t...

[]

0

[ "PROFILE" ]

[ "PS50979" ]

[ "BC" ]

[ 93171 ]

1

[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...

[ "6.4.1", "PDOC50979", "R-BTA-196780", "R-BTA-70263", "R-BTA-70268", "R-CEL-196780", "R-CEL-70263", "R-CEL-70268", "R-CEL-71032", "R-DDI-196780", "R-DDI-200425", "R-DDI-70895", "R-DDI-75105", "R-HSA-163765", "R-HSA-196780", "R-HSA-200425", "R-HSA-2426168", "R-HSA-3371599", "R-HSA-...

[ "EC:6.4.1", "PROSITEDOC:PDOC50979", "REACTOME:R-BTA-196780", "REACTOME:R-BTA-70263", "REACTOME:R-BTA-70268", "REACTOME:R-CEL-196780", "REACTOME:R-CEL-70263", "REACTOME:R-CEL-70268", "REACTOME:R-CEL-71032", "REACTOME:R-DDI-196780", "REACTOME:R-DDI-200425", "REACTOME:R-DDI-70895", "REACTOME:R-...

50

[ "1bnc", "1dv1", "1dv2", "1ulz", "1w93", "1w96", "2c00", "2dzd", "2gps", "2gpw", "2hjw", "2j9g", "2qf7", "2v58", "2v59", "2v5a", "2vpq", "2vqd", "2vr1", "2w6m", "2w6n", "2w6o", "2w6p", "2w6q", "2w6z", "2w70", "2w71", "2yl2", "3bg5", "3g8c", "3g8d", "3gid"...

145

[ "PUB00014226", "PUB00015348", "PUB00015349", "PUB00015350" ]

[ "10821865", "8564538", "14993673", "12769720" ]

[ "Movement of the biotin carboxylase B-domain as a result of ATP binding.", "Biotin carboxylase comes into the fold.", "Structure of the biotin carboxylase subunit of pyruvate carboxylase from Aquifex aeolicus at 2.2 A resolution.", "The biotin enzyme family: conserved structural motifs and domain rearrangemen...

[ 2000, 1996, 2004, 2003 ]

4

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 881, 65469, 25731, 1090 ]

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",...

[ 23, 8, 54, 8, 1, 29, 25, 3, 5, 40, 5, 2, 90 ]

13

true

Domain

Biotin carboxylation domain

Biotin_carboxylation_dom

5

IPR011765

11,765

Peptidase M16, N-terminal

Pept_M16_N

Domain

101,123

false

This entry represents an N-terminal domain found in metallopeptidases and non-peptidase homologues belonging to MEROPS peptidase family M16 (clan ME), subfamilies M16A, M16B and M16C. Members of this group of proteins include: Insulinase, insulin-degrading enzyme ( ) Mitochondrial processing peptidase alpha subunit, (A...

[]

0

[ "PFAM" ]

[ "PF00675" ]

[ "Peptidase_M16" ]

[ 101123 ]

1

[ "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...

[ "3.4.24", "GenProp1637", "R-BTA-5689880", "R-BTA-611105", "R-BTA-77387", "R-BTA-8949664", "R-BTA-9033241", "R-BTA-9837999", "R-BTA-9865881", "R-CEL-611105", "R-CEL-8949664", "R-CEL-9837999", "R-CEL-9865881", "R-DDI-611105", "R-DDI-9033241", "R-DDI-9837999", "R-DME-5689880", "R-DME-...

[ "EC:3.4.24", "GP:GenProp1637", "REACTOME:R-BTA-5689880", "REACTOME:R-BTA-611105", "REACTOME:R-BTA-77387", "REACTOME:R-BTA-8949664", "REACTOME:R-BTA-9033241", "REACTOME:R-BTA-9837999", "REACTOME:R-BTA-9865881", "REACTOME:R-CEL-611105", "REACTOME:R-CEL-8949664", "REACTOME:R-CEL-9837999", "REAC...

53

[ "1bcc", "1be3", "1bgy", "1ezv", "1hr6", "1hr7", "1hr8", "1hr9", "1kb9", "1kyo", "1l0l", "1l0n", "1ntk", "1ntm", "1ntz", "1nu1", "1p84", "1pp9", "1ppj", "1q2l", "1qcr", "1sqb", "1sqp", "1sqq", "1sqv", "1sqx", "2a06", "2bcc", "2fge", "2fyu", "2g47", "2g48"...

299

[ "PUB00004194" ]

[ "7990931" ]

[ "A yeast gene necessary for bud-site selection encodes a protein similar to insulin-degrading enzymes." ]

[ 1994 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 37, 61698, 38284, 54, 1050 ]

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",...

[ 49, 16, 15, 8, 3, 74, 24, 6, 41, 44, 8, 6, 115 ]

13

true

Domain

Peptidase M16, N-terminal

Pept_M16_N

1

IPR011766

11,766

Thiamine pyrophosphate enzyme, TPP-binding

TPP_enzyme_TPP-bd

Domain

159,329

false

A number of enzymes require thiamine pyrophosphate (TPP) (vitamin B1) as a cofactor. It has been shown [ ] that some of these enzymes are structurally related. The thiamin diphosphate-binding fold comprises two different functional modules, the pyridine-binding (Pyr) and pyrophosphate-binding (PP) modules. This represe...

[ "GO:0003824", "GO:0030976" ]

[ "catalytic activity", "thiamine pyrophosphate binding" ]

[ "molecular_function", "molecular_function" ]

2

[ "PFAM" ]

[ "PF02775" ]

[ "TPP_enzyme_C" ]

[ 159329 ]

1

[ "EC", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "2.2.1", "GenProp0839", "GenProp0842", "GenProp1226", "GenProp1245", "GenProp1256", "GenProp1269", "GenProp1292", "GenProp1328", "GenProp1334", "GenProp1342", "GenProp1467", "GenProp1485", "GenProp1620", "GenProp1655", "GenProp1698", "GenProp1722", "R-DDI-389599", "R-DDI-9033241"...

[ "EC:2.2.1", "GP:GenProp0839", "GP:GenProp0842", "GP:GenProp1226", "GP:GenProp1245", "GP:GenProp1256", "GP:GenProp1269", "GP:GenProp1292", "GP:GenProp1328", "GP:GenProp1334", "GP:GenProp1342", "GP:GenProp1467", "GP:GenProp1485", "GP:GenProp1620", "GP:GenProp1655", "GP:GenProp1698", "G...

29

[ "1b0p", "1bfd", "1jsc", "1kek", "1mcz", "1n0h", "1ovm", "1ozf", "1ozg", "1ozh", "1pi3", "1po7", "1pow", "1pox", "1pvd", "1pyd", "1q6z", "1qpb", "1t9a", "1t9b", "1t9c", "1t9d", "1upa", "1upb", "1upc", "1v5e", "1v5f", "1v5g", "1y9d", "1ybh", "1yhy", "1yhz"...

283

[ "PUB00015103" ]

[ "8604141" ]

[ "Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 A resolution." ]

[ 1996 ]

1

[]

[ "IPR022494", "IPR039368", "IPR047034", "IPR047212", "IPR047214" ]

0

5

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 5804, 130345, 20227, 9, 2944 ]

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",...

[ 31, 3, 4, 1, 7, 7, 7, 5, 25, 14, 7, 6, 43 ]

13

true

Domain

Thiamine pyrophosphate enzyme, TPP-binding

TPP_enzyme_TPP-bd

9

IPR011768

11,768

Translation elongation factor P

Transl_elongation_fac_P

Family

25,295

false

Members of this family possess translation elongation factor activity. They have been shown to stimulate efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro, possibly indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity a...

[ "GO:0003746", "GO:0006414", "GO:0005737" ]

[ "translation elongation factor activity", "translational elongation", "cytoplasm" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_00141", "TIGR00038" ]

[ "EF_P", "efp" ]

[ 25241, 24433 ]

2

[ "GP" ]

[ "GenProp0741" ]

[ "GP:GenProp0741" ]

1

[ "1ueb", "1yby", "3a5z", "3oyy", "3tre", "4v6a", "5j3b", "6enj", "6enu", "6j7m", "6rji", "6rk3", "6s8z", "8vwq", "8w2n" ]

15

[ "PUB00000702" ]

[ "9195040" ]

[ "Molecular characterization of the prokaryotic efp gene product involved in a peptidyltransferase reaction." ]

[ 1997 ]

1

[ "IPR020599" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences", "uncultured crenarchaeote MCG" ]

[ 23985, 819, 1, 489, 1 ]

5

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 5, 1, 7, 6 ]

4

true

Family

Translation elongation factor P

Transl_elongation_fac_P

5

IPR011771

11,771

Magnesium-chelatase, subunit H

BchH

Family

2,144

false

This entry represents the H subunit of the magnesium chelatase complex responsible for magnesium insertion into the protoporphyrin IX ring in the biosynthesis of both chlorophyll and bacteriochlorophyll. In chlorophyll-utilizing species, this gene is known as ChlH, while in bacteriochlorophyll-utilizing spoecies it is ...

[ "GO:0016851", "GO:0015995" ]

[ "magnesium chelatase activity", "chlorophyll biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR02025" ]

[ "BchH" ]

[ 2144 ]

1

[ "EC", "GP", "METACYC", "METACYC" ]

[ "6.6.1.1", "GenProp0144", "PWY-5531", "PWY-7159" ]

[ "EC:6.6.1.1", "GP:GenProp0144", "METACYC:PWY-5531", "METACYC:PWY-7159" ]

4

[ "4zhj", "6ysg", "6yt0", "6ytj", "6ytn" ]

5

[ "PUB00015452" ]

[ "12828371" ]

[ "Biosynthesis of chlorophylls from protoporphyrin IX." ]

[ 2003 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "ecological metagenomes" ]

[ 81, 1229, 829, 5 ]

4

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 3, 7, 4 ]

3

true

Family

Magnesium-chelatase, subunit H

BchH

1

IPR011773

11,773

DNA-directed RNA polymerase, alpha subunit

DNA-dir_RpoA

Family

39,341

false

DNA-directed RNA polymerases (also known as DNA-dependent RNA polymerases) are responsible for the polymerisation of ribonucleotides into a sequence complementary to the template DNA. In eukaryotes, there are three different forms of DNA-directed RNA polymerases transcribing different sets of genes. Most RNA polymerase...

[ "GO:0003677", "GO:0003899", "GO:0006351" ]

[ "DNA binding", "DNA-directed RNA polymerase activity", "DNA-templated transcription" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_00059", "TIGR02027" ]

[ "RNApol_bact_RpoA", "rpoA" ]

[ 37497, 39232 ]

2

[ "EC", "GP", "REACTOME" ]

[ "2.7.7.6", "GenProp0262", "R-HSA-9639775" ]

[ "EC:2.7.7.6", "GP:GenProp0262", "REACTOME:R-HSA-9639775" ]

3

[ "1bdf", "1hqm", "1i6v", "1iw7", "1l9u", "1l9z", "1smy", "1ynj", "1ynn", "1zyr", "2a68", "2a69", "2a6e", "2a6h", "2be5", "2cw0", "2gho", "2o5i", "2o5j", "2ppb", "3aoh", "3aoi", "3dxj", "3eql", "3iyd", "3lu0", "3wod", "4g7h", "4g7o", "4g7z", "4gzy", "4gzz"...

651

[ "PUB00000061", "PUB00001064", "PUB00005231", "PUB00033173" ]

[ "3052291", "7613089", "9657722", "10499798" ]

[ "Structure and function of bacterial sigma factors.", "The Escherichia coli RNA polymerase alpha subunit: structure and function.", "Structure of the Escherichia coli RNA polymerase alpha subunit amino-terminal domain.", "Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution." ]

[ 1988, 1995, 1998, 1999 ]

4

[]

0

null

[ "Bacteria", "Eukaryota", "candidate division MSBL1 archaeon SCGC-AAA382N08", "unclassified sequences" ]

[ 25458, 13477, 1, 405 ]

4

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 4, 1, 6, 2 ]

4

true

Family

DNA-directed RNA polymerase, alpha subunit

DNA-dir_RpoA

3

IPR011774

11,774

Geranylgeranyl reductase, plant/cyanobacteria

Geranylgeranyl_Rdtase_pln/cyn

Family

1,502

false

This entry represents the reductase which acts reduces the geranylgeranyl group to the phytyl group in the side chain of chlorophyll. It is unclear whether the enzyme has a preference for acting before or after the attachment of the side chain to chlorophyllide a by chlorophyll synthase. This clade is restricted to pla...

[ "GO:0045550" ]

[ "geranylgeranyl reductase activity" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR02028" ]

[ "ChlP" ]

[ 1502 ]

1

[ "EC", "GP", "GP", "GP" ]

[ "1.3.1.83", "GenProp0150", "GenProp1355", "GenProp1382" ]

[ "EC:1.3.1.83", "GP:GenProp0150", "GP:GenProp1355", "GP:GenProp1382" ]

4

[]

0

[]

0

[ "IPR010253" ]

[]

1

0

1

[ "Cyanobacteriota", "Eukaryota" ]

[ 356, 1146 ]

2

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 2, 5, 5 ]

3

true

Family

Geranylgeranyl reductase, plant/cyanobacteria

Geranylgeranyl_Rdtase_pln/cyn

5

IPR011776

11,776

Magnesium chelatase, ATPase subunit D

Mg_chelatase_ATPase-dsu

Family

1,211

false

This entry represents one of two ATPase subunits of the trimeric magnesium chelatase responsible for insertion of magnesium ion into protoporphyrin IX. This is an essential step in the biosynthesis of both chlorophyll and bacteriochlorophyll. This subunit is found in green plants, photosynthetic algae, cyanobacteria an...

[ "GO:0005524", "GO:0016851", "GO:0015995" ]

[ "ATP binding", "magnesium chelatase activity", "chlorophyll biosynthetic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR02031" ]

[ "BchD-ChlD" ]

[ 1211 ]

1

[ "EC", "GP", "METACYC", "METACYC" ]

[ "6.6.1.1", "GenProp0144", "PWY-5531", "PWY-7159" ]

[ "EC:6.6.1.1", "GP:GenProp0144", "METACYC:PWY-5531", "METACYC:PWY-7159" ]

4

[]

0

[]

0

[]

0

null

[ "Bacteria", "Eukaryota", "Methanobacteriota" ]

[ 522, 681, 8 ]

3

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 4, 2, 6 ]

3

true

Family

Magnesium chelatase, ATPase subunit D

Mg_chelatase_ATPase-dsu

1

IPR011777

11,777

Geranylgeranyl reductase family

Geranylgeranyl_Rdtase_fam

Family

11,918

false

This entry includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates.

[ "GO:0016628" ]

[ "oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR02032" ]

[ "GG-red-SF" ]

[ 11918 ]

1

[ "GP", "GP" ]

[ "GenProp1355", "GenProp1382" ]

[ "GP:GenProp1355", "GP:GenProp1382" ]

2

[ "3atq", "3atr", "3oz2", "4opc", "4opd", "4opg", "4opi", "4opl", "4opt", "4opu" ]

10

[]

0

[]

[ "IPR010253", "IPR023590" ]

0

2

0

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 2078, 8487, 1109, 244 ]

4

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 2, 5, 4 ]

3

true

Family

Geranylgeranyl reductase family

Geranylgeranyl_Rdtase_fam

3

IPR011778

11,778

Hydantoinase/dihydropyrimidinase

Hydantoinase/dihydroPyrase

Family

19,776

false

Dihydropyrimidinase (DHPase) catalyses the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines [ ]. Primarily converts 5,6-dihydrouracil to N-carbamyl-beta-alanine (also called 3-ureidopropanoate) but also acts on dihydrothymine and hydantoin. The enzyme is ...

[ "GO:0005737" ]

[ "cytoplasm" ]

[ "cellular_component" ]

1

[ "NCBIFAM", "CDD" ]

[ "TIGR02033", "cd01314" ]

[ "D-hydantoinase", "D-HYD" ]

[ 19239, 19180 ]

2

[ "EC", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "3.5.2", "GenProp1273", "GenProp1371", "R-BTA-399956", "R-CEL-399956", "R-CEL-73621", "R-DDI-73621", "R-DRE-399956", "R-GGA-399956", "R-HSA-399956", "R-HSA-437239", "R-HSA-73621", "R-MMU-399956", "R-MMU-437239", "R-MMU-73621", "R-RNO-399956", "R-RNO-437239", "R-RNO-73621", "R-XTR...

[ "EC:3.5.2", "GP:GenProp1273", "GP:GenProp1371", "REACTOME:R-BTA-399956", "REACTOME:R-CEL-399956", "REACTOME:R-CEL-73621", "REACTOME:R-DDI-73621", "REACTOME:R-DRE-399956", "REACTOME:R-GGA-399956", "REACTOME:R-HSA-399956", "REACTOME:R-HSA-437239", "REACTOME:R-HSA-73621", "REACTOME:R-MMU-399956...

19

[ "1gkp", "1gkq", "1k1d", "1kcx", "1nfg", "1yny", "2ftw", "2fty", "2fvk", "2fvm", "2gse", "2vm8", "2vr2", "3dc8", "3sfw", "4b3z", "4b90", "4b91", "4b92", "4bkn", "4cns", "4cnt", "4cnu", "4gz7", "4h00", "4h01", "4kir", "4kqn", "4lcq", "4lcr", "4lcs", "4tqt"...

56

[ "PUB00015455", "PUB00054984", "PUB00054985", "PUB00073343", "PUB00073380" ]

[ "7765480", "11092864", "12626710", "23443259", "9375656" ]

[ "A thermostable hydantoinase of Bacillus stearothermophilus NS1122A: cloning, sequencing, and high expression of the enzyme gene, and some properties of the expressed enzyme.", "Functional expression and characterization of the two cyclic amidohydrolase enzymes, allantoinase and a novel phenylhydantoinase, from E...

[ 1994, 2000, 2003, 2013, 1997 ]

5

[]

[ "IPR023766" ]

0

1

0

[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]

[ 29, 8816, 10833, 98 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]

[ 3, 2, 15, 4, 1, 20, 13, 3, 23, 9 ]

10

true

Family

Hydantoinase/dihydropyrimidinase

Hydantoinase/dihydroPyrase

1

IPR011779

11,779

Sulphate adenylyltransferase, large subunit

SO4_adenylTrfase_lsu

Family

17,161

false

Metabolic assimilation of sulphur from inorganic sulphate, requires sulphate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulphates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulphation of sulphate with ATP by sul...

[ "GO:0006790" ]

[ "sulfur compound metabolic process" ]

[ "biological_process" ]

1

[ "HAMAP", "NCBIFAM" ]

[ "MF_00062", "TIGR02034" ]

[ "Sulf_adenylyltr_sub1", "CysN" ]

[ 8470, 17157 ]

2

[ "EC", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME" ]

[ "2.7.7.4", "GenProp1573", "PWY-5278", "PWY-5340", "PWY-6683", "PWY-6932", "R-MTU-936635" ]

[ "EC:2.7.7.4", "GP:GenProp1573", "METACYC:PWY-5278", "METACYC:PWY-5340", "METACYC:PWY-6683", "METACYC:PWY-6932", "REACTOME:R-MTU-936635" ]

7

[ "1zun" ]

1

[ "PUB00015456", "PUB00015457", "PUB00015558" ]

[ "2828368", "12676676", "7961471" ]

[ "The sulfate activation locus of Escherichia coli K12: cloning, genetic, and enzymatic characterization.", "Identification of a third sulfate activation system in Sinorhizobium sp. strain BR816: the CysDN sulfate activation complex.", "Rhizobium meliloti NodP and NodQ form a multifunctional sulfate-activating c...

[ 1988, 2003, 1994 ]

3

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]

[ 28, 16923, 12, 198 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Sulphate adenylyltransferase, large subunit

SO4_adenylTrfase_lsu

8

IPR011780

11,780

D-serine ammonia-lyase

D_Ser_am_lyase

Family

3,990

false

This family consists of D-serine ammonia-lyases, pyridoxal-phosphate enzymes that convert D-serine to pyruvate and NH3. These enzyme are also called D-serine dehydratase and D-serine deaminase and was previously designated . It is homologous to an enzyme that acts on threonine and may itself act weakly on threonine.

[ "GO:0008721", "GO:0030170", "GO:0046416" ]

[ "D-serine ammonia-lyase activity", "pyridoxal phosphate binding", "D-amino acid metabolic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_01030", "TIGR02035" ]

[ "D_Ser_dehydrat", "D_Ser_am_lyase" ]

[ 3990, 3941 ]

2

[ "EC" ]

[ "4.3.1.18" ]

[ "EC:4.3.1.18" ]

1

[ "3r0x", "3r0z", "3ss7", "3ss9", "6aa9" ]

5

[]

0

[]

0

null

[ "Bacteria", "Eukaryota", "Haloferax volcanii", "unclassified sequences" ]

[ 3965, 7, 1, 17 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

D-serine ammonia-lyase

D_Ser_am_lyase

3

IPR011781

11,781

D-serine deaminase transcriptional activator

DsdC

Family

1,032

false

This family, part of the LysR family of transcriptional regulators, activates transcription of the gene for D-serine deaminase, dsdA. Trusted members of this family so far are found adjacent to dsdA and only in Gammaproteobacteria, including Escherichia coli, Vibrio cholerae, and Colwellia psychrerythraea (Vibrio psych...

[]

0

[ "NCBIFAM" ]

[ "TIGR02036" ]

[ "dsdC" ]

[ 1032 ]

1

[]

0

[]

0

[]

0

[ "IPR058163" ]

[]

1

0

1

[ "Bacteria", "Opisthokonta", "bioreactor metagenome" ]

[ 1028, 3, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

D-serine deaminase transcriptional activator

DsdC

9

IPR011782

11,782

Peptidase S1C, Do

Pept_S1C_Do

Family

20,362

false

Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes [ ]. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identif...

[ "GO:0004252", "GO:0006508" ]

[ "serine-type endopeptidase activity", "proteolysis" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR02037" ]

[ "degP_htrA_DO" ]

[ 20362 ]

1

[ "EC", "GP", "REACTOME" ]

[ "3.4.21.107", "GenProp0928", "R-HSA-9760173" ]

[ "EC:3.4.21.107", "GP:GenProp0928", "REACTOME:R-HSA-9760173" ]

3

[ "1ky9", "2zle", "3cs0", "3mh4", "3mh5", "3mh6", "3mh7", "3otp", "3ou0", "3pv2", "3pv3", "3pv5", "3stj", "4a8a", "4a8b", "4a8c", "4a8d", "4a9g", "4ynn", "5y2d", "6jjk", "6jjl", "6jjo", "6z05", "7xs0", "7xs2", "8f0a", "8f0u", "8f1t", "8f1u", "8f21", "8f26"...

35

[ "PUB00000522", "PUB00003576", "PUB00015458", "PUB00015459" ]

[ "8439290", "7845208", "11919638", "12458220" ]

[ "Evolutionary families of peptidases.", "Families of serine peptidases.", "Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine.", "Crystal structure of the protease domain of a heat-shock protein HtrA from Thermotoga maritima." ]

[ 1993, 1994, 2002, 2003 ]

4

[ "IPR001940" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 20100, 30, 232 ]

3

[ "Escherichia coli (strain K12)" ]

[ 2 ]

1

true

Family

Peptidase S1C, Do

Pept_S1C_Do

1

IPR011783

11,783

Peptidase S1C, DegS

Pept_S1C_DegS

Family

1,889

false

Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes [ ]. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identif...

[ "GO:0004252", "GO:0006508" ]

[ "serine-type endopeptidase activity", "proteolysis" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR02038" ]

[ "protease_degS" ]

[ 1889 ]

1

[ "EC" ]

[ "3.4.21.107" ]

[ "EC:3.4.21.107" ]

1

[ "1sot", "1soz", "1te0", "1vcw", "2qf0", "2qf3", "2r3y", "2rce", "3gcn", "3gco", "3gds", "3gdu", "3gdv", "3lgi", "3lh3", "4rqy", "4rqz", "4rr0", "4rr1", "5jd8", "6ew9" ]

21

[ "PUB00000522", "PUB00003576", "PUB00015531", "PUB00015532", "PUB00036042" ]

[ "8439290", "7845208", "11442831", "12679025", "17360428" ]

[ "Evolutionary families of peptidases.", "Families of serine peptidases.", "degS (hhoB) is an essential Escherichia coli gene whose indispensable function is to provide sigma (E) activity.", "A stress sensor for the bacterial periplasm.", "Inhibition of regulated proteolysis by RseB." ]

[ 1993, 1994, 2001, 2003, 2007 ]

5

[ "IPR001940" ]

[]

1

0

1

[ "Bacteria", "Rhodnius prolixus" ]

[ 1888, 1 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Peptidase S1C, DegS

Pept_S1C_DegS

8

IPR011786

11,786

Sulphite reductase (NADPH) hemoprotein, beta subunit

CysI

Family

5,405

false

Sulphite reductase (NADPH) ( ) catalyses a six electron reduction of sulfite to sulfide in prokaryotic organisms and is required for the biosynthesis of L-cysteine from sulfate. It is a complex oligomeric enzyme composed of two different peptides with a subunit composition of α(8)-β(4). The alpha component, encoded by ...

[ "GO:0004783", "GO:0050661", "GO:0051539", "GO:0008652", "GO:0009337" ]

[ "sulfite reductase (NADPH) activity", "NADP binding", "4 iron, 4 sulfur cluster binding", "amino acid biosynthetic process", "sulfite reductase complex (NADPH)" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

5

[ "HAMAP", "NCBIFAM" ]

[ "MF_01540", "TIGR02041" ]

[ "CysI", "CysI" ]

[ 5286, 4908 ]

2

[ "EC", "GP", "GP", "METACYC" ]

[ "1.8.1.2", "GenProp1283", "GenProp1301", "PWY-6683" ]

[ "EC:1.8.1.2", "GP:GenProp1283", "GP:GenProp1301", "METACYC:PWY-6683" ]

4

[ "1aop", "2aop", "2gep", "3aop", "3geo", "4aop", "4g38", "4g39", "4gep", "4htr", "5aop", "5gep", "6c3m", "6c3x", "6c3y", "6c3z", "6gep", "7gep", "8gep", "9c91" ]

20

[ "PUB00014496" ]

[ "7569952" ]

[ "Sulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions." ]

[ 1995 ]

1

[ "IPR045169" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 4493, 907, 5 ]

3

[ "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]

[ 1, 1 ]

2

true

Family

Sulphite reductase (NADPH) hemoprotein, beta subunit

CysI

2

IPR011787

11,787

Sulphite reductase, ferredoxin dependent

SiR_ferredoxin-dep

Family

1,185

false

Sulphite reductase (ferredoxin) is a cyanobacterial and plant monomeric enzyme distantly related to the iron-sulphur hemoprotein of sulphite reductase (NADPH) found in Proteobacteria and Eubacteria that also catalyses the reduction of sulphite to sulphide [ , ]. Optimal activity of sulfite reductase (SiR) is essential ...

[ "GO:0020037", "GO:0050311", "GO:0051539" ]

[ "heme binding", "sulfite reductase (ferredoxin) activity", "4 iron, 4 sulfur cluster binding" ]

[ "molecular_function", "molecular_function", "molecular_function" ]

3

[ "NCBIFAM" ]

[ "TIGR02042" ]

[ "sir" ]

[ 1185 ]

1

[ "EC", "GP" ]

[ "1.8.7.1", "GenProp1392" ]

[ "EC:1.8.7.1", "GP:GenProp1392" ]

2

[ "5h8v", "5h8y", "5h92" ]

3

[ "PUB00016903", "PUB00076661", "PUB00076662" ]

[ "11132635", "10712553", "20424176" ]

[ "Plant sulfite reductase: molecular structure, catalytic function and interaction with ferredoxin.", "Analysis of reductant supply systems for ferredoxin-dependent sulfite reductase in photosynthetic and nonphotosynthetic organs of maize.", "Sulfite reductase defines a newly discovered bottleneck for assimilato...

[ 2000, 2000, 2010 ]

3

[ "IPR045169" ]

[]

1

0

1

[ "Cyanobacteriota", "Eukaryota" ]

[ 345, 840 ]

2

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 3, 4, 6 ]

3

true

Family

Sulphite reductase, ferredoxin dependent

SiR_ferredoxin-dep

6

IPR011788

11,788

Zn(II)-responsive transcriptional regulator

ZntR

Family

1,595

false

This entry represents the zinc and cadmium (II) responsive transcriptional activator of the gammaproteobacterial zinc efflux system [ ]. This protein is a member of the MerR family of transcriptional activators and contains a distinctive pattern of cysteine residues in its metal binding loop, Cys-Cys-X(8-9)-Cys, as wel...

[ "GO:0003677", "GO:0008270", "GO:0006351" ]

[ "DNA binding", "zinc ion binding", "DNA-templated transcription" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR02043" ]

[ "ZntR" ]

[ 1595 ]

1

[]

0

[]

0

[ "PUB00015461" ]

[ "10048032" ]

[ "ZntR is a Zn(II)-responsive MerR-like transcriptional regulator of zntA in Escherichia coli." ]

[ 1999 ]

1

[ "IPR047057" ]

[]

1

0

1

[ "Bacteria", "Timema douglasi", "metagenomes" ]

[ 1591, 1, 3 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Zn(II)-responsive transcriptional regulator

ZntR

1

IPR011789

11,789

Cu(I)-responsive transcriptional regulator

CueR

Family

7,052

false

This entry represents the copper-, silver-and gold-(I) responsive transcriptional activator of the gammaproteobacterial copper efflux system [ ]. This protein is a member of the MerR family of transcriptional activators and contains a distinctive pattern of cysteine residues in its metal binding loop, Cys-X7-Cys. This ...

[ "GO:0003677", "GO:0003700", "GO:0005507", "GO:0045893" ]

[ "DNA binding", "DNA-binding transcription factor activity", "copper ion binding", "positive regulation of DNA-templated transcription" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "NCBIFAM", "CDD" ]

[ "TIGR02044", "cd01108" ]

[ "CueR", "HTH_CueR" ]

[ 6968, 6450 ]

2

[]

0

[ "1q05", "1q06", "1q07", "4wls", "4wlw", "6ldi", "6xh7", "6xh8", "7c17" ]

9

[ "PUB00015462", "PUB00015536" ]

[ "11136469", "12958362" ]

[ "CueR (YbbI) of Escherichia coli is a MerR family regulator controlling expression of the copper exporter CopA.", "Molecular basis of metal-ion selectivity and zeptomolar sensitivity by CueR." ]

[ 2001, 2003 ]

2

[ "IPR047057" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 7024, 8, 20 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Cu(I)-responsive transcriptional regulator

CueR

3

IPR011790

11,790

ADP-specific phosphofructokinase, archaeal

ADP_PFK_arc

Family

139

false

Phosphofructokinase is a key enzyme of glycolysis. The phosphate group donor for different subtypes of phosphofructokinase can be ATP, ADP, or pyrophosphate. This family consists of ADP-dependent phosphofructokinases found in archaea. Members are more similar to ADP-dependent glucokinases (excluded from this family) th...

[ "GO:0008443", "GO:0006000", "GO:0006096", "GO:0005737" ]

[ "phosphofructokinase activity", "fructose metabolic process", "glycolytic process", "cytoplasm" ]

[ "molecular_function", "biological_process", "biological_process", "cellular_component" ]

4

[ "HAMAP", "NCBIFAM" ]

[ "MF_00561", "TIGR02045" ]

[ "ADP_PFKinase", "P_fruct_ADP" ]

[ 134, 139 ]

2

[ "EC", "METACYC" ]

[ "2.7.1.146", "PWY-6142" ]

[ "EC:2.7.1.146", "METACYC:PWY-6142" ]

2

[ "1u2x", "3drw", "5k27", "5kkg", "5od2", "6c8z", "6xio" ]

7

[ "PUB00015463" ]

[ "11342216" ]

[ "Sequencing, expression, characterisation and phylogeny of the ADP-dependent phosphofructokinase from the hyperthermophilic, euryarchaeal Thermococcus zilligii." ]

[ 2001 ]

1

[ "IPR015990" ]

[]

1

0

1

[ "Methanobacteriota" ]

[ 139 ]

1

[]

0

true

Family

ADP-specific phosphofructokinase, archaeal

ADP_PFK_arc

5

IPR011791

11,791

Cd(II)/Pb(II)-responsive transcriptional regulator

CadR-PbrR

Family

3,408

false

This entry represents the cadmium(II) and/or lead(II) responsive transcriptional activator of the proteobacterial metal efflux system [ , ]. This protein contains a distinctive pattern of cysteine residues in its metal binding loop, Cys-X(6-9)-Cys, as well as a conserved and critical cysteine at the N-terminal end of t...

[ "GO:0003677", "GO:0003700", "GO:0046872", "GO:0045893" ]

[ "DNA binding", "DNA-binding transcription factor activity", "metal ion binding", "positive regulation of DNA-templated transcription" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "NCBIFAM", "CDD" ]

[ "TIGR02047", "cd04784" ]

[ "CadR-PbrR", "HTH_CadR-PbrR" ]

[ 2893, 3384 ]

2

[]

0

[ "5gpe", "6jgf", "6jgv", "6jgw", "6jgx", "6jni", "6jyw" ]

7

[ "PUB00015536", "PUB00015559", "PUB00015560", "PUB00017958", "PUB00081086" ]

[ "12958362", "11282588", "11544228", "12829265", "12901859" ]

[ "Molecular basis of metal-ion selectivity and zeptomolar sensitivity by CueR.", "Chromosomal locus for cadmium resistance in Pseudomonas putida consisting of a cadmium-transporting ATPase and a MerR family response regulator.", "Cloning and functional analysis of the pbr lead resistance determinant of Ralstonia...

[ 2003, 2001, 2001, 2003, 2003 ]

5

[ "IPR047057" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 3380, 3, 25 ]

3

[]

0

true

Family

Cd(II)/Pb(II)-responsive transcriptional regulator

CadR-PbrR

9

IPR011792

11,792

Glutamate--cysteine ligase, putative

GshA_cyano

Family

376

false

This family consists of proteins believed to be the glutamate--cysteine ligases of several cyanobacteria, which are known to make glutathione [ , ].

[]

0

[ "NCBIFAM" ]

[ "TIGR02048" ]

[ "gshA_cyano" ]

[ 376 ]

1

[ "GP" ]

[ "GenProp0030" ]

[ "GP:GenProp0030" ]

1

[]

0

[ "PUB00015464", "PUB00104796" ]

[ "12049666", "23170977" ]

[ "Lateral gene transfer and parallel evolution in the history of glutathione biosynthesis genes.", "Probing the origins of glutathione biosynthesis through biochemical analysis of glutamate-cysteine ligase and glutathione synthetase from a model photosynthetic prokaryote." ]

[ 2002, 2013 ]

2

[ "IPR006336" ]

[]

1

0

1

[ "Bacteria", "Paulinella" ]

[ 370, 6 ]

2

[]

0

true

Family

Glutamate--cysteine ligase, putative

GshA_cyano

9

IPR011793

11,793

Putative glutamate--cysteine ligase YbdK

YbdK

Family

12,244

false

This entry represents a family of proteins that are thought to function as carboxylate-amine ligases. One protein ( ) shows weak glutamate--cysteine ligase activity, but the low catalytic rate casts doubt on whether L-cysteine is the actual biological substrate [ ]. Glutamate--cysteine ligase is the first of two enzyme...

[ "GO:0016879" ]

[ "ligase activity, forming carbon-nitrogen bonds" ]

[ "molecular_function" ]

1

[ "HAMAP", "NCBIFAM" ]

[ "MF_01609", "TIGR02050" ]

[ "Glu_cys_ligase_2", "gshA_cyan_rel" ]

[ 12225, 12211 ]

2

[ "EC", "METACYC", "METACYC", "METACYC" ]

[ "6.3.2.2", "PWY-6840", "PWY-7255", "PWY-8043" ]

[ "EC:6.3.2.2", "METACYC:PWY-6840", "METACYC:PWY-7255", "METACYC:PWY-8043" ]

4

[ "1r8g", "1tt4" ]

2

[ "PUB00030571" ]

[ "15211520" ]

[ "YbdK is a carboxylate-amine ligase with a gamma-glutamyl:Cysteine ligase activity: crystal structure and enzymatic assays." ]

[ 2004 ]

1

[ "IPR006336" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]

[ 337, 11832, 6, 69 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Putative glutamate--cysteine ligase YbdK

YbdK

8

IPR011794

11,794

Hg(II)-responsive transcriptional regulator

MerR

Family

2,411

false

This entry represents the mercury (II) responsive transcriptional activator of the mer organomercurial resistance operon [ ]. This protein is a member of the MerR family of transcriptional activators and contains a distinctive pattern of cysteine residues in its metal binding loop, Cys-X(8)-Cys-Pro, as well as a conser...

[ "GO:0003677", "GO:0045340", "GO:0006355", "GO:0046689" ]

[ "DNA binding", "mercury ion binding", "regulation of DNA-templated transcription", "response to mercury ion" ]

[ "molecular_function", "molecular_function", "biological_process", "biological_process" ]

4

[ "NCBIFAM", "CDD" ]

[ "TIGR02051", "cd04783" ]

[ "MerR", "HTH_MerR1" ]

[ 1808, 2334 ]

2

[ "GP" ]

[ "GenProp0151" ]

[ "GP:GenProp0151" ]

1

[ "4ua1", "4ua2", "5crl" ]

3

[ "PUB00002075", "PUB00005125", "PUB00015536", "PUB00017958", "PUB00081082", "PUB00081083", "PUB00081085" ]

[ "2492496", "2305262", "12958362", "12829265", "10079080", "9843394", "16514151" ]

[ "Homologous metalloregulatory proteins from both gram-positive and gram-negative bacteria control transcription of mercury resistance operons.", "The MerR metalloregulatory protein binds mercuric ion as a tricoordinate, metal-bridged dimer.", "Molecular basis of metal-ion selectivity and zeptomolar sensitivity ...

[ 1989, 1990, 2003, 2003, 1999, 1998, 2006 ]

7

[ "IPR047057" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "ecological metagenomes", "plasmids" ]

[ 2355, 6, 48, 2 ]

4

[]

0

true

Family

Hg(II)-responsive transcriptional regulator

MerR

4

IPR011795

11,795

Mercuric transport protein periplasmic component

MerP

Family

1,478

false

This entry represents the periplasmic mercury (II) binding protein of the bacterial mercury detoxification system which passes mercuric ion to the MerT transporter for subsequent reduction to Hg(0) by the mercuric reductase MerA [ , ]. MerP contains a distinctive GMTCXXC motif associated with metal binding [ ]. MerP is...

[ "GO:0015097", "GO:0045340", "GO:0015694", "GO:0046689", "GO:0042597" ]

[ "mercury ion transmembrane transporter activity", "mercury ion binding", "mercury ion transport", "response to mercury ion", "periplasmic space" ]

[ "molecular_function", "molecular_function", "biological_process", "biological_process", "cellular_component" ]

5

[ "NCBIFAM" ]

[ "TIGR02052" ]

[ "MerP" ]

[ 1478 ]

1

[ "GP" ]

[ "GenProp0151" ]

[ "GP:GenProp0151" ]

1

[ "1afi", "1afj", "1osd", "2hqi" ]

4

[ "PUB00000447", "PUB00078052", "PUB00078053" ]

[ "9188683", "1328156", "3038684" ]

[ "Structures of the reduced and mercury-bound forms of MerP, the periplasmic protein from the bacterial mercury detoxification system.", "Roles of the Tn21 merT, merP, and merC gene products in mercury resistance and mercury binding.", "Role of the merT and merP gene products of transposon Tn501 in the induction...

[ 1997, 1992, 1987 ]

3

[ "IPR001802" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "ecological metagenomes", "plasmids" ]

[ 1447, 3, 26, 2 ]

4

[]

0

true

Family

Mercuric transport protein periplasmic component

MerP

2

IPR011797

11,797

Mercuric resistence transcriptional repressor protein MerD

MerD

Family

740

false

This entry represents a transcriptional repressor protein of the MerR family whose expression is regulated by the mercury-sensitive transcriptional activator, MerR. MerD has been shown to repress the transcription of the mer operon [ ].

[ "GO:0003677", "GO:0045892", "GO:0046689" ]

[ "DNA binding", "negative regulation of DNA-templated transcription", "response to mercury ion" ]

[ "molecular_function", "biological_process", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR02054" ]

[ "MerD" ]

[ 740 ]

1

[ "GP" ]

[ "GenProp0151" ]

[ "GP:GenProp0151" ]

1

[]

0

[ "PUB00015466" ]

[ "1917975" ]

[ "Purification and functional characterization of MerD. A coregulator of the mercury resistance operon in gram-negative bacteria." ]

[ 1991 ]

1

[ "IPR047057" ]

[]

1

0

1

[ "Bacteria", "ecological metagenomes", "plasmids" ]

[ 732, 6, 2 ]

3

[]

0

true

Family

Mercuric resistence transcriptional repressor protein MerD

MerD

3

IPR011799

11,799

Chlorophyll synthase, ChlG

ChlG

Family

1,108

false

This entry represents the strictly cyanobacterial and plant-specific chlorophyll synthase ChlG. ChlG is the enzyme (esterase) which attaches the side chain moiety onto chlorophyllide a. Both geranylgeranyl and phytyl pyrophosphates are substrates to varying degrees in enzymes from different sources [ ]. Thus, ChlG may ...

[ "GO:0046408", "GO:0015995", "GO:0016020" ]

[ "chlorophyll synthetase activity", "chlorophyll biosynthetic process", "membrane" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "NCBIFAM" ]

[ "TIGR02056" ]

[ "ChlG" ]

[ 1108 ]

1

[ "EC", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]

[ "2.5.1.62", "GenProp0150", "GenProp1355", "GenProp1724", "PWY-5064", "PWY-5068", "PWY-5086", "PWY-7764", "PWY-8126", "PWY-8127" ]

[ "EC:2.5.1.62", "GP:GenProp0150", "GP:GenProp1355", "GP:GenProp1724", "METACYC:PWY-5064", "METACYC:PWY-5068", "METACYC:PWY-5086", "METACYC:PWY-7764", "METACYC:PWY-8126", "METACYC:PWY-8127" ]

10

[]

0

[ "PUB00015452" ]

[ "12828371" ]

[ "Biosynthesis of chlorophylls from protoporphyrin IX." ]

[ 2003 ]

1

[ "IPR006372" ]

[]

1

0

1

[ "Cyanobacteriota", "Eukaryota" ]

[ 356, 752 ]

2

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 5, 1, 3 ]

3

true

Family

Chlorophyll synthase, ChlG

ChlG

5

IPR011800

11,800

Phosphoadenosine phosphosulphate reductase CysH

PAPS_reductase_CysH

Family

4,381

false

Requiring thioredoxin as an electron donor, phosphoadenosine phosphosulphate reductase catalyzes the reduction of phosphoadenosine phosphosulphate (PAPS) to sulphite and phosphoadenosine phosphate (PAP) [ ]. Found in enterobacteria, cyanobacteria, and yeast, PAPS reductase is related to a group of plant ( ) and bacteri...

[ "GO:0004604", "GO:0019379" ]

[ "phosphoadenylyl-sulfate reductase (thioredoxin) activity", "sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR02057" ]

[ "PAPS_reductase" ]

[ 4381 ]

1

[ "EC", "GP" ]

[ "1.8.4.8", "GenProp1283" ]

[ "EC:1.8.4.8", "GP:GenProp1283" ]

2

[ "1sur", "2o8v", "2oq2", "6vpu", "7rge" ]

5

[ "PUB00005294", "PUB00017738" ]

[ "9261082", "10613872" ]

[ "Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases.", "Identification of a new class of 5'-adenylylsulfate (APS) reductases from sulfate-assimilating bacteria." ]

[ 1997, 2000 ]

2

[ "IPR004511" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 2888, 1488, 5 ]

3

[ "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

Phosphoadenosine phosphosulphate reductase CysH

PAPS_reductase_CysH

1

IPR011801

11,801

Cyanobacterial long protein repeat

Swm_rep_I_cyn

Repeat

463

false

This motif appears in 29 copies in a large (greater than 10000 amino protein in Synechococcus sp. (strain WH8102) associated with a novel flagellar system, as one of three different repeats. Similar domains are found in two different large (less than 3500 amino acid) proteins of Synechocystis sp. (strain PCC 6803).

[]

0

[ "NCBIFAM" ]

[ "TIGR02059" ]

[ "swm_rep_I" ]

[ 463 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria", "Bilateria", "ecological metagenomes" ]

[ 459, 2, 2 ]

3

[]

0

true

Repeat

Cyanobacterial long protein repeat

Swm_rep_I_cyn

8

IPR011802

11,802

Adenylylsulphate reductase, beta subunit

AprB

Family

682

false

During dissimilatory sulphate reduction and sulphur oxidation, adenylylsulphate (APS) reductase catalyzes reversibly the two-electron reduction of APS to sulphite and AMP. Found in several bacterial lineages and in Archaeoglobales, APS reductase is a heterodimer composed of an alpha subunit containing a noncovalently b...

[]

0

[ "NCBIFAM" ]

[ "TIGR02060" ]

[ "aprB" ]

[ 682 ]

1

[ "GP" ]

[ "GenProp0155" ]

[ "GP:GenProp0155" ]

1

[ "1jnr", "1jnz", "2fja", "2fjb", "2fjd", "2fje", "3gyx" ]

7

[]

0

[]

0

null

[ "Archaea", "Bacteria", "Metazoa", "unclassified sequences" ]

[ 40, 568, 9, 65 ]

4

[]

0

true

Family

Adenylylsulphate reductase, beta subunit

AprB

7

IPR011804

11,804

Ribonuclease II

RNase_II

Family

2,538

false

This family consists of exoribonuclease II (RNase II), the product of the rnb gene, as found in a number of gamma proteobacteria. In Escherichia coli, it is one of eight different exoribonucleases. It is involved in mRNA degradation [ ] and tRNA precursor end processing [ ].

[ "GO:0003723", "GO:0008859", "GO:0006401" ]

[ "RNA binding", "exoribonuclease II activity", "RNA catabolic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_01036", "TIGR02062" ]

[ "RNase_II", "RNase_B" ]

[ 2317, 2538 ]

2

[ "EC", "GP" ]

[ "3.1.13.1", "GenProp1360" ]

[ "EC:3.1.13.1", "GP:GenProp1360" ]

2

[ "2id0", "2ix0", "2ix1" ]

3

[ "PUB00015537", "PUB00056786" ]

[ "11948193", "320007" ]

[ "Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II.", "Processing by ribonuclease II of the tRNATyr precursor of Escherichia coli synthesized in vitro." ]

[ 2002, 1977 ]

2

[ "IPR004476" ]

[]

1

0

1

[ "Bacteria", "Beauveria bassiana D1-5", "marine sediment metagenome" ]

[ 2536, 1, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Ribonuclease II

RNase_II

4

IPR011805

11,805

Ribonuclease R

RNase_R

Family

19,108

false

Ribonuclease R (RNaseR) is a 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs [ , ]. It is one of the eight exoribonucleases reported in Escherichia coli and is broadly distributed throughout the bacteria. In E. coli, double mutants of this protein and po...

[ "GO:0003723", "GO:0004518" ]

[ "RNA binding", "nuclease activity" ]

[ "molecular_function", "molecular_function" ]

2

[ "HAMAP", "NCBIFAM" ]

[ "MF_01895", "TIGR02063" ]

[ "RNase_R", "RNase_R" ]

[ 19078, 18312 ]

2

[ "EC" ]

[ "3.1.13.1" ]

[ "EC:3.1.13.1" ]

1

[ "5xgu", "7dcy", "7dic", "7did", "7dol", "8cdu", "8cdv", "8cec", "8ced", "8cee" ]

10

[ "PUB00015537", "PUB00056800", "PUB00056801" ]

[ "11948193", "14622421", "20023028" ]

[ "Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II.", "Cold shock induction of RNase R and its role in the maturation of the quality control mediator SsrA/tmRNA.", "Escherichia coli RNase R has dual activities, helicase and RNase." ]

[ 2002, 2003, 2010 ]

3

[ "IPR004476" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "unclassified sequences", "uncultured marine phage" ]

[ 18928, 15, 164, 1 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Ribonuclease R

RNase_R

4

IPR011806

11,806

Sulphite reductase, dissimilatory-type alpha subunit

DsrA

Family

2,571

false

Dissimilatory sulphite reductase catalyses the six-electron reduction of sulphite to sulphide as the terminal reaction in dissimilatory sulphate reduction. It remains unclear, however, whether trithionate and thiosulphate serve as intermediate compounds to sulphide or as end products of sulphite reduction [ ]. Sulphite...

[ "GO:0018551", "GO:0020037", "GO:0051539" ]

[ "dissimilatory sulfite reductase (NADH) activity", "heme binding", "4 iron, 4 sulfur cluster binding" ]

[ "molecular_function", "molecular_function", "molecular_function" ]

3

[ "NCBIFAM" ]

[ "TIGR02064" ]

[ "dsrA" ]

[ 2571 ]

1

[ "GP" ]

[ "GenProp0155" ]

[ "GP:GenProp0155" ]

1

[ "2v4j", "2xsj", "3mm5", "3mm6", "3mm7", "3mm8", "3mm9", "3mma", "3mmb", "3mmc", "3or1", "3or2" ]

12

[ "PUB00009960", "PUB00015467", "PUB00015468" ]

[ "1555572", "7747930", "11557144" ]

[ "The third subunit of desulfoviridin-type dissimilatory sulfite reductases.", "Metabolism of sulfate-reducing prokaryotes.", "A novel organization of the dissimilatory sulfite reductase operon of Thermodesulforhabdus norvegica verified by RT-PCR." ]

[ 1992, 1994, 2001 ]

3

[ "IPR045169" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Lauvirus lau218", "unclassified sequences" ]

[ 28, 2310, 2, 231 ]

4

[]

0

true

Family

Sulphite reductase, dissimilatory-type alpha subunit

DsrA

8

IPR011807

11,807

Exosome complex component Rrp41

Rrp41

Family

520

false

Rrp41 is a major subunit of the exosome, helping form the catalytic core [ ]. Rrp41 is a member of the RNase PH family, named after the bacterial ribonuclease PH, a 3'-5' exoribonuclease. Structurally all members of this family form hexameric rings (trimers of dimers). In archaea, the ring is formed by three Rrp41:Rrp4...

[ "GO:0016896", "GO:0006401", "GO:0000178" ]

[ "RNA exonuclease activity, producing 5'-phosphomonoesters", "RNA catabolic process", "exosome (RNase complex)" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP", "NCBIFAM", "CDD" ]

[ "MF_00591", "TIGR02065", "cd11366" ]

[ "Exosome_Rrp41", "ECX1", "RNase_PH_archRRP41" ]

[ 455, 482, 519 ]

3

[ "EC" ]

[ "3.1.13.-" ]

[ "EC:3.1.13.-" ]

1

[ "2ba0", "2ba1", "2br2", "2c37", "2c38", "2c39", "2je6", "2jea", "2jeb", "2pnz", "2po0", "2po1", "2po2", "2wnr", "3l7z", "3m7n", "3m85", "4ba1", "4ba2", "8xfx", "8xie" ]

21

[ "PUB00074087", "PUB00074089", "PUB00074104" ]

[ "22503705", "24789718", "21713675" ]

[ "Heterogeneous complexes of the RNA exosome in Sulfolobus solfataricus.", "Structure and function of the archaeal exosome.", "The archaeal exosome." ]

[ 2012, 2014, 2011 ]

3

[]

0

null

[ "Archaea", "Geodia barretti", "unclassified sequences" ]

[ 493, 3, 24 ]

3

[]

0

true

Family

Exosome complex component Rrp41

Rrp41

3

IPR011808

11,808

Sulphite reductase, dissimilatory-type beta subunit

DsrB

Family

953

false

Dissimilatory sulphite reductase catalyses the six-electron reduction of sulphite to sulphide as the terminal reaction in dissimilatory sulphate reduction. It remains unclear, however, whether trithionate and thiosulphate serve as intermediate compounds to sulphide or as end products of sulphite reduction [ ]. Sulphite...

[ "GO:0009055", "GO:0018551", "GO:0051539", "GO:0006790" ]

[ "electron transfer activity", "dissimilatory sulfite reductase (NADH) activity", "4 iron, 4 sulfur cluster binding", "sulfur compound metabolic process" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "NCBIFAM" ]

[ "TIGR02066" ]

[ "dsrB" ]

[ 953 ]

1

[ "GP" ]

[ "GenProp0155" ]

[ "GP:GenProp0155" ]

1

[ "2v4j", "2xsj", "3mm5", "3mm6", "3mm7", "3mm8", "3mm9", "3mma", "3mmb", "3mmc", "3or1", "3or2" ]

12

[ "PUB00009960", "PUB00015467", "PUB00015468" ]

[ "1555572", "7747930", "11557144" ]

[ "The third subunit of desulfoviridin-type dissimilatory sulfite reductases.", "Metabolism of sulfate-reducing prokaryotes.", "A novel organization of the dissimilatory sulfite reductase operon of Thermodesulforhabdus norvegica verified by RT-PCR." ]

[ 1992, 1994, 2001 ]

3

[ "IPR045169" ]

[]

1

0

1

[ "Archaea", "Bacteria", "unclassified sequences" ]

[ 46, 809, 98 ]

3

[]

0

true

Family

Sulphite reductase, dissimilatory-type beta subunit

DsrB

1

IPR011809

11,809

Histidinol-phosphate phosphatase, putative, inositol monophosphatase

His_9_proposed

Family

6,804

false

This entry contains proteins that belong to the inositol monophosphatase family. The members of this family consist of no more than one per species and are found only in species in which histidine is synthesized de novo but no histidinol phosphatase can be found in either of the two described families ( , ). In at leas...

[ "GO:0004401" ]

[ "histidinol-phosphatase activity" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR02067" ]

[ "his_9_HisN" ]

[ 6804 ]

1

[ "EC", "GP", "GP", "REACTOME" ]

[ "3.1.3.15", "GenProp0109", "GenProp1244", "R-MTU-879299" ]

[ "EC:3.1.3.15", "GP:GenProp0109", "GP:GenProp1244", "REACTOME:R-MTU-879299" ]

4

[ "5eq7", "5eq8", "5eq9", "5eqa", "5t3j", "5yht", "5zon" ]

7

[]

0

[ "IPR000760" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "metagenomes" ]

[ 6213, 544, 47 ]

3

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 4, 3, 3 ]

3

true

Family

Histidinol-phosphate phosphatase, putative, inositol monophosphatase

His_9_proposed

7

IPR011810

11,810

Cyanophycin synthetase

Cya_phycin_syn

Family

4,059

false

Cyanophycin is an insoluble storage polymer for carbon, nitrogen, and energy, found in most Cyanobacteria. The polymer has a backbone of L-aspartic acid, with most Asp side chain carboxyl groups attached to L-arginine. The polymer is made by this enzyme, cyanophycin synthetase, and degraded by cyanophycinase. Heterolog...

[ "GO:0005524", "GO:0016874", "GO:0009059" ]

[ "ATP binding", "ligase activity", "macromolecule biosynthetic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR02068" ]

[ "cya_phycin_syn" ]

[ 4059 ]

1

[ "EC", "EC", "GP", "METACYC" ]

[ "6.3.2.29", "6.3.2.30", "GenProp0156", "PWY-7052" ]

[ "EC:6.3.2.29", "EC:6.3.2.30", "GP:GenProp0156", "METACYC:PWY-7052" ]

4

[ "7lg5", "7lgj", "7lgm", "7lgn", "7lgq", "7txu", "7txv", "7wac", "7wad", "7wae", "7waf" ]

11

[ "PUB00015470" ]

[ "11976746" ]

[ "Evaluation of non-cyanobacterial genome sequences for occurrence of genes encoding proteins homologous to cyanophycin synthetase and cloning of an active cyanophycin synthetase from Acinetobacter sp. strain DSM 587." ]

[ 2002 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "Marine Group III euryarchaeote", "metagenomes" ]

[ 4019, 2, 2, 36 ]

4

[]

0

true

Family

Cyanophycin synthetase

Cya_phycin_syn

1

IPR011812

11,812

Biosynthetic peptidoglycan transglycosylase

Pep_trsgly

Family

11,376

false

This family is one of the transglycosylases involved in the late stages of peptidoglycan biosynthesis. Members tend to be small, about 240 amino acids in length, and consist almost entirely of a domain, which describes transglycosylases. Species with this protein will have several other transglycosylases as well. All s...

[ "GO:0016763", "GO:0009252", "GO:0009274", "GO:0016020" ]

[ "pentosyltransferase activity", "peptidoglycan biosynthetic process", "peptidoglycan-based cell wall", "membrane" ]

[ "molecular_function", "biological_process", "cellular_component", "cellular_component" ]

4

[ "HAMAP", "PANTHER", "NCBIFAM" ]

[ "MF_00766", "PTHR30400", "TIGR02070" ]

[ "PGT_MtgA", "", "mono_pep_trsgly" ]

[ 9961, 11315, 9815 ]

3

[ "EC" ]

[ "2.4.99.28" ]

[ "EC:2.4.99.28" ]

1

[]

0

[]

0

[]

0

null

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 11288, 11, 77 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Biosynthetic peptidoglycan transglycosylase

Pep_trsgly

8

IPR011813

11,813

Penicillin-binding protein 1B

PBP_1b

Family

4,936

false

Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of a particular bifunctional transglycosylase/transpeptidase in Escherichia coli and other Proteobacteria, designated penicillin-binding protein 1B. It's struct...

[ "GO:0008233", "GO:0008955", "GO:0009252", "GO:0046677", "GO:0009274" ]

[ "peptidase activity", "peptidoglycan glycosyltransferase activity", "peptidoglycan biosynthetic process", "response to antibiotic", "peptidoglycan-based cell wall" ]

[ "molecular_function", "molecular_function", "biological_process", "biological_process", "cellular_component" ]

5

[ "PIRSF", "NCBIFAM" ]

[ "PIRSF002799", "TIGR02071" ]

[ "PBP_1b", "PBP_1b" ]

[ 4872, 4892 ]

2

[ "EC", "EC", "METACYC", "METACYC", "REACTOME" ]

[ "2.4.99.28", "3.4.16.4", "PWY-5265", "PWY-6471", "R-HSA-9638771" ]

[ "EC:2.4.99.28", "EC:3.4.16.4", "METACYC:PWY-5265", "METACYC:PWY-6471", "REACTOME:R-HSA-9638771" ]

5

[ "3fwl", "3vma", "5fgz", "5hl9", "5hla", "5hlb", "5hld", "6yn0", "7lq6" ]

9

[ "PUB00052062" ]

[ "19458048" ]

[ "Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli." ]

[ 2009 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 4894, 7, 35 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Penicillin-binding protein 1B

PBP_1b

9

IPR011814

11,814

Malonyl-[acyl-carrier protein] O-methyltransferase BioC

BioC

Family

6,806

false

Malonyl-[acyl-carrier protein] O-methyltransferase BioC is a biotin synthesis protein that converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via by a modified fatty acid synthetic pathway [ ]...

[ "GO:0010340", "GO:0009102" ]

[ "carboxyl-O-methyltransferase activity", "biotin biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP", "NCBIFAM" ]

[ "MF_00835", "TIGR02072" ]

[ "BioC", "BioC" ]

[ 6639, 5719 ]

2

[ "EC", "GP", "METACYC" ]

[ "2.1.1.197", "GenProp0036", "PWY-6519" ]

[ "EC:2.1.1.197", "GP:GenProp0036", "METACYC:PWY-6519" ]

3

[ "8x8i", "8x8j" ]

2

[ "PUB00060658" ]

[ "20693992" ]

[ "Biotin synthesis begins by hijacking the fatty acid synthetic pathway." ]

[ 2010 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 6731, 5, 70 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Malonyl-[acyl-carrier protein] O-methyltransferase BioC

BioC

6

IPR011815

11,815

Penicillin-binding protein 1C

PBP_1c

Family

8,308

false

This entry contains penicillin binding proteins includes the member from Escherichia coli designated penicillin-binding protein 1C. Members have both transglycosylase and transpeptidase domains and are involved in forming cross-links in the late stages of peptidoglycan biosynthesis. All members of this entry are presum...

[ "GO:0008955", "GO:0009252" ]

[ "peptidoglycan glycosyltransferase activity", "peptidoglycan biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR02073" ]

[ "PBP_1c" ]

[ 8308 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria", "Eukaryota", "metagenomes" ]

[ 8263, 7, 38 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Penicillin-binding protein 1C

PBP_1c

9

IPR011819

11,819

Pyrococcus aspartate kinase subunit, putative

AspKin_pair

Family

31

false

This family consists of proteins restricted to and found as paralogous pairs (typically close together) in species of Pyrococcus, a hyperthermophilic archaeal genus. Members are always found close to other genes of threonine biosynthesis and appear to represent the Pyrococcal form of aspartate kinase. Alignment to aspa...

[]

0

[ "NCBIFAM" ]

[ "TIGR02078" ]

[ "AspKin_pair" ]

[ 31 ]

1

[ "GP" ]

[ "GenProp0160" ]

[ "GP:GenProp0160" ]

1

[]

0

[]

0

[]

0

null

[ "Thermococcaceae" ]

[ 31 ]

1

[]

0

true

Family

Pyrococcus aspartate kinase subunit, putative

AspKin_pair

7

IPR011821

11,821

O-succinylhomoserine (thiol)-lyase

O_succ_thio_ly

Family

2,812

false

This family consists of O-succinylhomoserine (thiol)-lyase, one of three different enzymes designated cystathionine gamma-synthase and involved in methionine biosynthesis. In all three cases, sulphur is added by transsulphuration from Cys to yield cystathionine rather than by a sulphhydrylation step that uses H2S direc...

[]

0

[ "NCBIFAM" ]

[ "TIGR02080" ]

[ "O_succ_thio_ly" ]

[ 2812 ]

1

[]

0

[ "1cs1", "6ld7", "6ld8", "6ld9", "6lgo" ]

5

[ "PUB00001321" ]

[ "9843488" ]

[ "Crystal structure of Escherichia coli cystathionine gamma-synthase at 1.5 A resolution." ]

[ 1998 ]

1

[ "IPR000277" ]

[]

1

0

1

[ "Bacteria", "Opisthokonta", "ecological metagenomes" ]

[ 2801, 4, 7 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

O-succinylhomoserine (thiol)-lyase

O_succ_thio_ly

3

IPR011823

11,823

3-isopropylmalate dehydratase, large subunit, bacteria

IsopropMal_deHydtase_lsu_bac

Family

1,807

false

This entry represents the large subunit of 3-isopropylmalate dehydratase (LeuC) from prokaryotes. Homoaconitase, aconitase and 3-isopropylmalate dehydratase have similar overall structures and domain organisation [ ]. All are dehydratases that bind a [4Fe-4S]-cluster. 3-isopropylmalate dehydratase (or isopropylmalate i...

[ "GO:0003861", "GO:0051539", "GO:0009098" ]

[ "3-isopropylmalate dehydratase activity", "4 iron, 4 sulfur cluster binding", "L-leucine biosynthetic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR02083" ]

[ "LEU2" ]

[ 1807 ]

1

[ "EC", "GP", "GP" ]

[ "4.2.1.33", "GenProp0164", "GenProp0193" ]

[ "EC:4.2.1.33", "GP:GenProp0164", "GP:GenProp0193" ]

3

[]

0

[ "PUB00005471", "PUB00016210", "PUB00032014", "PUB00033924", "PUB00036023", "PUB00082326" ]

[ "9020582", "9813279", "15522288", "1400210", "16524361", "20663849" ]

[ "The aconitase family: three structural variations on a common theme.", "The organization of the leuC, leuD and leuB genes of the extreme thermophile Thermus thermophilus.", "Crystal structure of the Pyrococcus horikoshii isopropylmalate isomerase small subunit provides insight into the dual substrate specifici...

[ 1997, 1998, 2004, 1992, 2006, 2010 ]

6

[ "IPR011826" ]

[]

1

0

1

[ "Archaea", "Bacteria", "unclassified sequences" ]

[ 10, 1768, 29 ]

3

[]

0

true

Family

3-isopropylmalate dehydratase, large subunit, bacteria

IsopropMal_deHydtase_lsu_bac

6

IPR011824

11,824

Hydrolyase LeuD/DmdB, bacterial

LeuD/DmdB_bac

Family

1,151

false

This entry includes 3-isopropylmalate dehydratase small subunit LeuD from Heliobacterium modesticaldum and 2,3-dimethylmalate dehydratase small subunit DmdB from Eubacterium barkeri [ ]. The structure of the Pyrococcus horikoshii small subunit ( ) has recently been determined [ ]. As expected the structure of this poly...

[ "GO:0016836" ]

[ "hydro-lyase activity" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR02084" ]

[ "leud" ]

[ 1151 ]

1

[ "EC", "GP" ]

[ "4.2.1.33", "GenProp0164" ]

[ "EC:4.2.1.33", "GP:GenProp0164" ]

2

[]

0

[ "PUB00032014", "PUB00074095" ]

[ "15522288", "6489933" ]

[ "Crystal structure of the Pyrococcus horikoshii isopropylmalate isomerase small subunit provides insight into the dual substrate specificity of the enzyme.", "Nicotinic acid metabolism. Dimethylmaleate hydratase." ]

[ 2004, 1984 ]

2

[ "IPR011827" ]

[]

1

0

1

[ "Archaea", "Bacteria", "metagenomes" ]

[ 6, 1114, 31 ]

3

[]

0

true

Family

Hydrolyase LeuD/DmdB, bacterial

LeuD/DmdB_bac

5

IPR011825

11,825

23S rRNA (uracil(747)-C(5))-methyltransferase RlmC

23SrRNA_MeTrfase_RlmC

Family

2,342

false

This family consists of RNA methyltransferases designated RlmC or RumB, formerly YbjF. Members act on 23S rRNA U747 in Escherichia coli and the equivalent position in other proteobacterial species [ ].

[ "GO:0016436", "GO:0016070" ]

[ "rRNA (uridine) methyltransferase activity", "RNA metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP", "NCBIFAM" ]

[ "MF_01012", "TIGR02085" ]

[ "23SrRNA_methyltr_RlmC", "meth_trns_rumB" ]

[ 1955, 2337 ]

2

[ "EC" ]

[ "2.1.1.189" ]

[ "EC:2.1.1.189" ]

1

[]

0

[ "PUB00015471" ]

[ "12907714" ]

[ "Identifying the methyltransferases for m(5)U747 and m(5)U1939 in 23S rRNA using MALDI mass spectrometry." ]

[ 2003 ]

1

[ "IPR010280" ]

[]

1

0

1

[ "Bacteria", "Opisthokonta", "mine drainage metagenome" ]

[ 2339, 2, 1 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

23S rRNA (uracil(747)-C(5))-methyltransferase RlmC

23SrRNA_MeTrfase_RlmC

2

IPR011826

11,826

Homoaconitase/3-isopropylmalate dehydratase, large subunit, prokaryotic

HAcnase/IPMdehydase_lsu_prok

Family

4,510

false

This entry represents the large subunit of 3-isopropylmalate dehydratase (LeuC), as well as homoaconitase enzymes, from prokaryotes. Homoaconitase, aconitase and 3-isopropylmalate dehydratase have similar overall structures and domain organisation [ ]. All are dehydratases that bind a [4Fe-4S]-cluster. 3-isopropylmalat...

[ "GO:0003861", "GO:0051539", "GO:0009098" ]

[ "3-isopropylmalate dehydratase activity", "4 iron, 4 sulfur cluster binding", "L-leucine biosynthetic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_01027", "TIGR02086" ]

[ "LeuC_type2", "IPMI_arch" ]

[ 3892, 4487 ]

2

[ "EC", "GP" ]

[ "4.2.1.33", "GenProp0164" ]

[ "EC:4.2.1.33", "GP:GenProp0164" ]

2

[ "4kp1", "4kp2", "4nqy" ]

3

[ "PUB00005471", "PUB00016210", "PUB00032014", "PUB00033924", "PUB00036023", "PUB00082326" ]

[ "9020582", "9813279", "15522288", "1400210", "16524361", "20663849" ]

[ "The aconitase family: three structural variations on a common theme.", "The organization of the leuC, leuD and leuB genes of the extreme thermophile Thermus thermophilus.", "Crystal structure of the Pyrococcus horikoshii isopropylmalate isomerase small subunit provides insight into the dual substrate specifici...

[ 1997, 1998, 2004, 1992, 2006, 2010 ]

6

[ "IPR006251" ]

[ "IPR011823" ]

1

0

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 826, 3572, 11, 101 ]

4

[]

0

true

Family

Homoaconitase/3-isopropylmalate dehydratase, large subunit, prokaryotic

HAcnase/IPMdehydase_lsu_prok

9

IPR011827

11,827

Hydrolyase LeuD/HacB/DmdB

LeuD_type2/HacB/DmdB

Family

5,723

false

This entry is most closely related to the 3-isopropylmalate dehydratase . It includes methanogen homoaconitase small subunit HacB from Methanocaldococcus jannaschii [ , ], 3-isopropylmalate dehydratase small subunit LeuD from Salmonella typhimurium [ ], 2,3-dimethylmalate dehydratase small subunit DmdB from Eubacterium...

[ "GO:0016836" ]

[ "hydro-lyase activity" ]

[ "molecular_function" ]

1

[ "HAMAP", "NCBIFAM" ]

[ "MF_01032", "TIGR02087" ]

[ "LeuD_type2", "LEUD_arch" ]

[ 3576, 5723 ]

2

[ "EC", "EC", "GP", "GP" ]

[ "4.2.1", "4.2.1.33", "GenProp0164", "GenProp0193" ]

[ "EC:4.2.1", "EC:4.2.1.33", "GP:GenProp0164", "GP:GenProp0193" ]

4

[ "1v7l", "2pkp", "3vba" ]

3

[ "PUB00032014", "PUB00054348", "PUB00074093", "PUB00074094", "PUB00074095", "PUB00089812" ]

[ "15522288", "20170198", "18765671", "2993799", "6489933", "10875335" ]

[ "Crystal structure of the Pyrococcus horikoshii isopropylmalate isomerase small subunit provides insight into the dual substrate specificity of the enzyme.", "Substrate specificity determinants of the methanogen homoaconitase enzyme: structure and function of the small subunit.", "Methanogen homoaconitase catal...

[ 2004, 2010, 2008, 1985, 1984, 2000 ]

6

[]

[ "IPR011824" ]

0

1

0

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 838, 3748, 955, 182 ]

4

[]

0

true

Family

Hydrolyase LeuD/HacB/DmdB

LeuD_type2/HacB/DmdB

4

IPR011828

11,828

Isopropylmalate/isohomocitrate dehydrogenase

LEU3_arc

Family

365

false

This entry represents a group of archaeal decarboxylating dehydrogenases which include the leucine biosynthesis enzyme 3-isopropylmalate dehydrogenase (LeuB, LEU3) and the methanogenic cofactor CoB biosynthesis enzyme isohomocitrate dehydrogenase (AksF). Both of these have been characterised in Methanococcus janaschii ...

[ "GO:0003862", "GO:0051287", "GO:0009098" ]

[ "3-isopropylmalate dehydrogenase activity", "NAD binding", "L-leucine biosynthetic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR02088" ]

[ "LEU3_arch" ]

[ 365 ]

1

[ "EC", "GP", "METACYC" ]

[ "1.1.1.85", "GenProp0164", "PWY-7396" ]

[ "EC:1.1.1.85", "GP:GenProp0164", "METACYC:PWY-7396" ]

3

[ "1wpw", "4y1p", "5hn3", "5hn4", "5hn5", "5hn6" ]

6

[ "PUB00015472" ]

[ "10940051" ]

[ "Identification of enzymes homologous to isocitrate dehydrogenase that are involved in coenzyme B and leucine biosynthesis in methanoarchaea." ]

[ 2000 ]

1

[]

0

null

[ "Archaea", "Bacteria", "bioreactor metagenome" ]

[ 346, 18, 1 ]

3

[]

0

true

Family

Isopropylmalate/isohomocitrate dehydrogenase

LEU3_arc

6

IPR011829

11,829

Tartrate dehydrogenase

TTC_DH

Family

8,559

false

Tartrate dehydrogenase catalyzes the oxidation of both meso-and (+)-tartrate as well as a D-malate [ ]. These enzymes are closely related to the 3-isopropylmalate and isohomocitrate dehydrogenases found in and , respectively.

[ "GO:0016616", "GO:0051287" ]

[ "oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor", "NAD binding" ]

[ "molecular_function", "molecular_function" ]

2

[ "NCBIFAM" ]

[ "TIGR02089" ]

[ "TTC" ]

[ 8559 ]

1

[ "EC", "EC", "EC", "METACYC" ]

[ "1.1.1.83", "1.1.1.93", "4.1.1.73", "PWY-7469" ]

[ "EC:1.1.1.83", "EC:1.1.1.93", "EC:4.1.1.73", "METACYC:PWY-7469" ]

4

[ "3flk", "3fmx" ]

2

[ "PUB00015473" ]

[ "2184888" ]

[ "Characterization of the multiple catalytic activities of tartrate dehydrogenase." ]

[ 1990 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "Halobacteriales", "metagenomes" ]

[ 6968, 1533, 4, 54 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Tartrate dehydrogenase

TTC_DH

6

IPR011830

11,830

Isopropylmalate/citramalate/homocitrate synthase

LEU1_arch

Domain

687

false

Methanogenic archaea contain three closely related homologues of the 2-isopropylmalate synthases (LeuA) represented by . Two of these in Methanococcus janaschii (MJ1392 - CimA [ ]; MJ0503 - AksA [ ]) have been characterised as catalyzing alternative reactions leaving the third (MJ1195) as the presumptive LeuA enzyme. C...

[ "GO:0046912", "GO:0019752" ]

[ "acyltransferase activity, acyl groups converted into alkyl on transfer", "carboxylic acid metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR02090" ]

[ "LEU1_arch" ]

[ 687 ]

1

[ "EC", "GP", "GP" ]

[ "2.3.3", "GenProp0164", "GenProp0193" ]

[ "EC:2.3.3", "GP:GenProp0164", "GP:GenProp0193" ]

3

[]

0

[ "PUB00015474", "PUB00015475" ]

[ "9864346", "9665716" ]

[ "(R)-citramalate synthase in methanogenic archaea.", "Alpha-keto acid chain elongation reactions involved in the biosynthesis of coenzyme B (7-mercaptoheptanoyl threonine phosphate) in methanogenic Archaea." ]

[ 1999, 1998 ]

2

[ "IPR000891" ]

[]

1

0

1

[ "Archaea", "Pseudothermotoga thermarum DSM 5069", "ecological metagenomes" ]

[ 677, 1, 9 ]

3

[]

0

true

Domain

Isopropylmalate/citramalate/homocitrate synthase

LEU1_arch

7

IPR011831

11,831

Glucose-1-phosphate adenylyltransferase

ADP-Glc_PPase

Family

24,925

false

This entry represents the GLGC in plants and bacteria. Glucose-1-phosphate adenylyltransferase (GLGC) catalyses the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for the regulation of storage polysaccharide accumulation in plants ...

[ "GO:0008878", "GO:0005978" ]

[ "glucose-1-phosphate adenylyltransferase activity", "glycogen biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PANTHER", "NCBIFAM" ]

[ "PTHR43523", "TIGR02091" ]

[ "", "glgC" ]

[ 24920, 16913 ]

2

[ "EC", "GP", "GP", "GP", "METACYC", "METACYC" ]

[ "2.7.7.27", "GenProp0168", "GenProp0264", "GenProp1247", "PWY-622", "PWY-7902" ]

[ "EC:2.7.7.27", "GP:GenProp0168", "GP:GenProp0264", "GP:GenProp1247", "METACYC:PWY-622", "METACYC:PWY-7902" ]

6

[ "1yp2", "1yp3", "1yp4", "3brk", "5l6s", "5l6v", "5mni", "5w5r", "5w5t", "5w6j", "6r8b", "6r8u", "6shj", "6shn", "6shq", "6si8", "6v96", "6v99", "6v9a", "6vr0" ]

20

[ "PUB00032683", "PUB00086423" ]

[ "15692569", "24112771" ]

[ "Crystal structure of potato tuber ADP-glucose pyrophosphorylase.", "The ADP-glucose pyrophosphorylase from Streptococcus mutans provides evidence for the regulation of polysaccharide biosynthesis in Firmicutes." ]

[ 2005, 2013 ]

2

[]

[ "IPR011832", "IPR023049" ]

0

2

0

[ "Bacteria", "Bathycoccus sp. RCC716 virus 1", "Eukaryota", "unclassified sequences" ]

[ 19816, 1, 4870, 238 ]

4

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 29, 1, 16, 91 ]

4

true

Family

Glucose-1-phosphate adenylyltransferase

ADP-Glc_PPase

3

IPR011832

11,832

Glucose-1-phosphate adenylyltransferase, GlgD subunit

GlgDAde_trans

Family

3,525

false

This family is GlgD, an apparent regulatory protein that appears in an alpha2/beta2 heterotetramer with GlgC (glucose-1-phosphate adenylyltransferase, ) in a subset of bacteria that use GlgC for glycogen biosynthesis.

[ "GO:0005978" ]

[ "glycogen biosynthetic process" ]

[ "biological_process" ]

1

[ "NCBIFAM" ]

[ "TIGR02092" ]

[ "glgD" ]

[ 3525 ]

1

[ "GP" ]

[ "GenProp0168" ]

[ "GP:GenProp0168" ]

1

[]

0

[]

0

[ "IPR011831" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "bioreactor metagenome" ]

[ 3512, 2, 11 ]

3

[]

0

true

Family

Glucose-1-phosphate adenylyltransferase, GlgD subunit

GlgDAde_trans

5

IPR011833

11,833

Glycogen/starch/alpha-glucan phosphorylase

Glycg_phsphrylas

Family

23,780

false

The biosynthesis of disaccharides, oligosaccharides and polysaccharides involves the action of hundreds of different glycosyltransferases. These enzymes catalyse the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. A classification of glycosyltransferas...

[ "GO:0004645", "GO:0030170", "GO:0005975" ]

[ "1,4-alpha-oligoglucan phosphorylase activity", "pyridoxal phosphate binding", "carbohydrate metabolic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR02093" ]

[ "P_ylase" ]

[ 23780 ]

1

[ "EC", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "2.4.1.1", "GenProp0168", "GenProp1259", "GenProp1412", "GenProp2089", "PWY-5941", "PWY-6731", "PWY-6737", "PWY-7238", "R-BTA-6798695", "R-BTA-70221", "R-DDI-6798695", "R-DDI-70221", "R-DME-70221", "R-HSA-6798695", "R-HSA-70221", "R-MMU-6798695", "R-MMU-70221", "R-RNO-6798695", ...

[ "EC:2.4.1.1", "GP:GenProp0168", "GP:GenProp1259", "GP:GenProp1412", "GP:GenProp2089", "METACYC:PWY-5941", "METACYC:PWY-6731", "METACYC:PWY-6737", "METACYC:PWY-7238", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-70221", "REACTOME:R-DDI-6798695", "REACTOME:R-DDI-70221", "REACTOME:R-DME-70221", ...

22

[ "1a8i", "1abb", "1ahp", "1axr", "1b4d", "1bx3", "1c50", "1c8k", "1c8l", "1e1y", "1e4o", "1em6", "1exv", "1fa9", "1fc0", "1fs4", "1ftq", "1ftw", "1fty", "1fu4", "1fu7", "1fu8", "1gfz", "1gg8", "1ggn", "1gpa", "1gpb", "1gpy", "1h5u", "1hlf", "1k06", "1k08"...

279

[ "PUB00006243", "PUB00006246", "PUB00006354", "PUB00006436", "PUB00009409" ]

[ "2667896", "2182117", "8798388", "10077830", "9334165" ]

[ "The family of glycogen phosphorylases: structure and function.", "The role of pyridoxal 5'-phosphate in glycogen phosphorylase catalysis.", "Role of the active site gate of glycogen phosphorylase in allosteric inhibition and substrate binding.", "Bacterial alpha-glucan phosphorylases.", "A classification o...

[ 1989, 1990, 1996, 1999, 1997 ]

5

[ "IPR000811" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "Siphoviridae sp. ctPyh10", "unclassified sequences" ]

[ 14221, 9496, 1, 62 ]

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",...

[ 10, 3, 9, 2, 2, 11, 12, 1, 7, 21, 1, 15 ]

12

true

Family

Glycogen/starch/alpha-glucan phosphorylase

Glycg_phsphrylas

6

IPR011834

11,834

Alpha-glucan phosphorylase

Agluc_phsphrylas

Family

7,471

false

This family consists of known phosphorylases, and homologues believed to share the function of using inorganic phosphate to cleave an alpha 1,4 linkage between the terminal glucose residue and the rest of the polymer (maltodextrin, glycogen, etc.). The name of the glucose storage polymer substrate, and therefore the na...

[ "GO:0004645", "GO:0030170", "GO:0005975" ]

[ "1,4-alpha-oligoglucan phosphorylase activity", "pyridoxal phosphate binding", "carbohydrate metabolic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR02094" ]

[ "more_P_ylases" ]

[ 7471 ]

1

[ "EC", "METACYC", "METACYC", "METACYC", "METACYC" ]

[ "2.4.1.1", "PWY-5941", "PWY-6731", "PWY-6737", "PWY-7238" ]

[ "EC:2.4.1.1", "METACYC:PWY-5941", "METACYC:PWY-6731", "METACYC:PWY-6737", "METACYC:PWY-7238" ]

5

[]

0

[]

0

[ "IPR000811" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]

[ 240, 7015, 11, 205 ]

4

[]

0

true

Family

Alpha-glucan phosphorylase

Agluc_phsphrylas

6

IPR011835

11,835

Bacterial/plant glycogen synthase

GS/SS

Family

18,610

false

This entry represents glycogen (GS) and starch synthases (SS) from bacteria and plants. GS and SS are involved in the elongation of the linear chains of glycogen and starch, respectively, by catalysing the transfer of the glucosyl moiety of the activated glucosyl donor (UDP-glucose or ADP-glucose, depending on the orga...

[ "GO:0004373" ]

[ "alpha-1,4-glucan glucosyltransferase (UDP-glucose donor) activity" ]

[ "molecular_function" ]

1

[ "HAMAP", "NCBIFAM" ]

[ "MF_00484", "TIGR02095" ]

[ "Glycogen_synth", "glgA" ]

[ 17842, 17680 ]

2

[ "EC", "GP", "GP", "METACYC" ]

[ "2.4.1.21", "GenProp0168", "GenProp1247", "PWY-622" ]

[ "EC:2.4.1.21", "GP:GenProp0168", "GP:GenProp1247", "METACYC:PWY-622" ]

4

[ "1rzu", "1rzv", "2bis", "2qzs", "2r4t", "2r4u", "3cop", "3cx4", "3d1j", "3fro", "3guh", "3l01", "3vue", "3vuf", "4hln", "6gne", "6gnf", "6gng" ]

18

[ "PUB00074531" ]

[ "19666739" ]

[ "Starch granule initiation in Arabidopsis requires the presence of either class IV or class III starch synthases." ]

[ 2009 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "Methanobacteriati", "Siphoviridae sp. cttuu15", "metagenomes" ]

[ 13229, 5274, 4, 1, 102 ]

5

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 26, 1, 73, 70 ]

4

true

Family

Bacterial/plant glycogen synthase

GS/SS

4

IPR011836

11,836

YhdP

Family

7,190

false

This entry describes YhdP and related proteins present in the Proteobacteria. Intermembrane phospholipid transporter YhdP is involved in maintaining lipid homeostasis in the outer membrane of Gram-negative bacteria. It likely transports phospholipids between the inner and outer membranes, providing a bridge-like struct...

[]

0

[ "PANTHER", "NCBIFAM" ]

[ "PTHR38690", "TIGR02099" ]

[ "", "" ]

[ 7190, 5787 ]

2

[]

0

[]

0

[ "PUB00104645", "PUB00104679", "PUB00106658", "PUB00160777", "PUB00160778", "PUB00160779" ]

[ "34781743", "30087168", "35226662", "33046656", "39638236", "37873249" ]

[ "YhdP, TamB, and YdbH Are Redundant but Essential for Growth and Lipid Homeostasis of the Gram-Negative Outer Membrane.", "Cyclic Enterobacterial Common Antigen Maintains the Outer Membrane Permeability Barrier of Escherichia coli in a Manner Controlled by YhdP.", "Absence of YhdP, TamB, and YdbH leads to defec...

[ 2021, 2018, 2022, 2020, 2025, 2023 ]

6

[]

0

null

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 7043, 14, 133 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

YhdP

2

IPR011837

11,837

Glycogen debranching enzyme, GlgX type

Glycogen_debranch_GlgX

Family

18,421

false

This entry represents the glycogen debranching enzyme GlgX found in Escherichia coli, as well as its equivalogs in other prokaryotic species. This enzyme encodes an isoamylase-type debranching enzyme with high specificity for hydrolysis of chains consisting of three or four glucose residues, and is classed as family 13...

[ "GO:0004135", "GO:0004553", "GO:0005980" ]

[ "amylo-alpha-1,6-glucosidase activity", "hydrolase activity, hydrolyzing O-glycosyl compounds", "glycogen catabolic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR02100" ]

[ "glgX_debranch" ]

[ 18421 ]

1

[ "EC", "GP", "GP" ]

[ "3.2.1.196", "GenProp0168", "GenProp1412" ]

[ "EC:3.2.1.196", "GP:GenProp0168", "GP:GenProp1412" ]

3

[ "2vnc", "2vr5", "2vuy", "2wsk", "7eav", "7u39", "7u3a", "7u3b", "7u3d" ]

9

[ "PUB00004870", "PUB00005266", "PUB00015476", "PUB00016734" ]

[ "7624375", "8535779", "8576033", "15687211" ]

[ "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.", "Structures and mechanisms of glycosyl hydrolases.", "Coordinate genetic regulation of glycogen catabolism and biosynthesis in Escherichia coli via the CsrA gene product.", "Role of the Escherichi...

[ 1995, 1995, 1996, 2005 ]

4

[]

[ "IPR022844" ]

0

1

0

[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]

[ 64, 18173, 73, 111 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Glycogen debranching enzyme, GlgX type

Glycogen_debranch_GlgX

9

IPR011838

11,838

Pullulanase, extracellular

Pullulan_Gpos

Domain

735

false

Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. In contrast, a gl...

[]

0

[ "NCBIFAM" ]

[ "TIGR02102" ]

[ "pullulan_Gpos" ]

[ 735 ]

1

[ "EC" ]

[ "3.2.1.41" ]

[ "EC:3.2.1.41" ]

1

[ "2ya0", "2ya1", "2ya2", "3faw", "3fax" ]

5

[ "PUB00015477", "PUB00015478" ]

[ "11083842", "8798645" ]

[ "Antigenicity, expression, and molecular characterization of surface-located pullulanase of Streptococcus pneumoniae.", "Amino acid sequence and molecular structure of an alkaline amylopullulanase from Bacillus that hydrolyzes alpha-1,4 and alpha-1,6 linkages in polysaccharides at different active sites." ]

[ 2000, 1996 ]

2

[]

0

null

[ "Bacteria" ]

[ 735 ]

1

[]

0

true

Domain

Pullulanase, extracellular

Pullulan_Gpos

7

IPR011839

11,839

Alpha-1,6-glucosidases, pullulanase-type

Pullul_strch

Domain

3,316

false

Members of this protein family include secreted (or membrane-anchored) pullulanases of Gram-negative bacteria and pullulanase-type starch debranching enzymes of plants. Both enzymes hydrolyze alpha-1,6 glycosidic linkages. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (ma...

[ "GO:0051060", "GO:0005975" ]

[ "pullulanase activity", "carbohydrate metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR02103" ]

[ "pullul_strch" ]

[ 3316 ]

1

[]

0

[ "2fgz", "2fh6", "2fh8", "2fhb", "2fhc", "2fhf", "2y4s", "2y5e", "2yoc", "4aio", "4cvw", "4j3s", "4j3t", "4j3u", "4j3v", "4j3w", "4j3x", "5yn2", "5yn7", "5yna", "5ync", "5ynd", "5yne", "5ynh", "6j33", "6j34", "6j35", "6j4h" ]

28

[]

0

[]

0

null

[ "Bacteria", "Eukaryota", "metagenomes" ]

[ 2733, 579, 4 ]

3

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 4, 5, 7 ]

3

true

Domain

Alpha-1,6-glucosidases, pullulanase-type

Pullul_strch

2

IPR011840

11,840

Pullulanase, type I

PulA_typeI

Domain

4,045

false

Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family consi...

[]

0

[ "NCBIFAM" ]

[ "TIGR02104" ]

[ "pulA_typeI" ]

[ 4045 ]

1

[]

0

[ "2e8y", "2e8z", "2e9b", "2wan", "3wdh", "3wdi", "3wdj", "6jeq", "6jfj", "6jfx", "6jhf", "6jhg", "6jhh", "6jhi", "7lsa", "7lsr", "7lst", "7lsu", "9qf8", "9qfa" ]

20

[ "PUB00015479" ]

[ "9375788" ]

[ "Cloning and sequence of a type I pullulanase from an extremely thermophilic anaerobic bacterium, Caldicellulosiruptor saccharolyticus." ]

[ 1997 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 4006, 6, 33 ]

3

[]

0

true

Domain

Pullulanase, type I

PulA_typeI

7

IPR011841

11,841

Type III secretion system, needle protein

T3SS_needle_YscF

Family

1,302

false

Type III secretion systems translocate proteins, usually virulence factors, out across both inner and outer membranes of certain Gram-negative bacteria and further across the plasma membrane and into the cytoplasm of the host cell. This protein, termed YscF in Yersinia, and EscF, PscF, EprI, etc. in other systems, form...

[ "GO:0030254", "GO:0030257" ]

[ "protein secretion by the type III secretion system", "type III protein secretion system complex" ]

[ "biological_process", "cellular_component" ]

2

[ "NCBIFAM" ]

[ "TIGR02105" ]

[ "III_needle" ]

[ 1302 ]

1

[ "GP" ]

[ "GenProp0052" ]

[ "GP:GenProp0052" ]

1

[ "2ca5", "2g0u", "2jow", "2kv7", "2lpz", "2mex", "2mme", "2p58", "2v6l", "2x9c", "3j0r", "3zqb", "3zqe", "6dwb", "6ofe", "6off", "6ofg", "6ofh", "6pep", "6q15", "6q16", "6rwy", "6znh", "6zni", "7agx", "7ah9", "7ahi", "7rye", "7y6c", "8axk", "8fvu" ]

31

[ "PUB00015480", "PUB00095091", "PUB00095092" ]

[ "14580388", "32601072", "31001211" ]

[ "Genetic analysis of the formation of the Ysc-Yop translocation pore in macrophages by Yersinia enterocolitica: role of LcrV, YscF and YopN.", "A Structure-Function-Inhibition Analysis of the P. aeruginosa Type III Secretion Needle Protein PscF.", "Structural and Functional Characterization of the Type Three Se...

[ 2003, 2020, 2019 ]

3

[ "IPR021123" ]

[]

1

0

1

[ "Bacteria", "Bracon brevicornis", "human gut metagenome" ]

[ 1300, 1, 1 ]

3

[]

0

true

Family

Type III secretion system, needle protein

T3SS_needle_YscF

3

IPR011842

11,842

Coenzyme PQQ biosynthesis protein B

PQQ_synth_PqqB

Family

4,215

false

This entry describes coenzyme PQQ biosynthesis protein B, a gene required for the biosynthesis of pyrrolo-quinoline-quinone (coenzyme PQQ). PQQ is required for some glucose dehydrogenases and alcohol dehydrogenases. Note that this gene appears to be required for PQQ in biosynthesis in Methylobacterium extorquens (under...

[]

0

[ "HAMAP", "NCBIFAM", "CDD" ]

[ "MF_00653", "TIGR02108", "cd16274" ]

[ "PQQ_syn_PqqB", "PQQ_syn_pqqB", "PQQB-like_MBL-fold" ]

[ 4206, 4157, 2872 ]

3

[ "GP" ]

[ "GenProp0170" ]

[ "GP:GenProp0170" ]

1

[ "1xto", "3jxp", "4z5y", "4z5z", "4z60", "4z67", "4z6x", "4z7r", "6e13" ]

9

[ "PUB00015481", "PUB00035752" ]

[ "2536663", "2549866" ]

[ "Acinetobacter calcoaceticus genes involved in biosynthesis of the coenzyme pyrrolo-quinoline-quinone: nucleotide sequence and expression in Escherichia coli K-12.", "Genes involved in the biosynthesis of PQQ from Acinetobacter calcoaceticus." ]

[ 1989, 1989 ]

2

[]

0

null

[ "Bacteria", "Metazoa", "metagenomes" ]

[ 4193, 4, 18 ]

3

[]

0

true

Family

Coenzyme PQQ biosynthesis protein B

PQQ_synth_PqqB

7

IPR011843

11,843

Coenzyme PQQ biosynthesis protein E, bacteria

PQQ_synth_PqqE_bac

Family

4,237

false

Coenzyme PQQ biosynthesis protein E is required for the biosynthesis of pyrrolo-quinoline-quinone (coenzyme PQQ). PqqE is also known as PqqA peptide cyclase, as it carries out, in conjunction with PqqD, the radical-mediated formation of a new carbon-carbon bond between two amino acid side chains on PqqA [ ].

[ "GO:0051539", "GO:0018189" ]

[ "4 iron, 4 sulfur cluster binding", "pyrroloquinoline quinone biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP", "SFLD", "NCBIFAM" ]

[ "MF_00660", "SFLDF00280", "TIGR02109" ]

[ "PqqE", "coenzyme_PQQ_synthesis_protein", "PQQ_syn_pqqE" ]

[ 4235, 4189, 4234 ]

3

[ "EC", "GP", "METACYC" ]

[ "1.21.98.4", "GenProp0170", "PWY-6420" ]

[ "EC:1.21.98.4", "GP:GenProp0170", "METACYC:PWY-6420" ]

3

[ "6c8v" ]

1

[ "PUB00091347" ]

[ "26961875" ]

[ "Demonstration That the Radical S-Adenosylmethionine (SAM) Enzyme PqqE Catalyzes de Novo Carbon-Carbon Cross-linking within a Peptide Substrate PqqA in the Presence of the Peptide Chaperone PqqD." ]

[ 2016 ]

1

[ "IPR017200" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "metagenomes" ]

[ 4216, 4, 17 ]

3

[]

0

true

Family

Coenzyme PQQ biosynthesis protein E, bacteria

PQQ_synth_PqqE_bac

3

IPR011844

11,844

Coenzyme PQQ biosynthesis protein PqqF

PQQ_synth_PqqF

Family

1,126

false

In the subset of species that make coenzyme PQQ (pyrrolo-quinoline-quinone), this peptidase is found in the PQQ biosynthesis region and is thought to act as a protease on PqqA ( ), a probable peptide precursor of the coenzyme. PQQ is required for some glucose dehydrogenases and alcohol dehydrogenases [ ].

[ "GO:0004222", "GO:0008270", "GO:0006508", "GO:0018189" ]

[ "metalloendopeptidase activity", "zinc ion binding", "proteolysis", "pyrroloquinoline quinone biosynthetic process" ]

[ "molecular_function", "molecular_function", "biological_process", "biological_process" ]

4

[ "NCBIFAM" ]

[ "TIGR02110" ]

[ "PQQ_syn_pqqF" ]

[ 1126 ]

1

[ "EC", "GP", "METACYC" ]

[ "3.4.24.-", "GenProp0170", "PWY-8119" ]

[ "EC:3.4.24.-", "GP:GenProp0170", "METACYC:PWY-8119" ]

3

[ "5cio" ]

1

[ "PUB00015482" ]

[ "8526497" ]

[ "Tn5-directed cloning of pqq genes from Pseudomonas fluorescens CHA0: mutational inactivation of the genes results in overproduction of the antibiotic pyoluteorin." ]

[ 1995 ]

1

[]

0

null

[ "Bacteria" ]

[ 1126 ]

1

[]

0

true

Family

Coenzyme PQQ biosynthesis protein PqqF

PQQ_synth_PqqF

1

IPR011845

11,845

Coenzyme PQQ biosynthesis protein C

PqqC

Family

4,234

false

This entry describes the coenzyme PQQ (pyrrolo-quinoline-quinone) biosynthesis protein PqqC. Pyrroloquinoline quinone (PQQ) is the prosthetic group of several bacterial enzymes, including methanol dehydrogenase of methylotrophs and the glucose dehydrogenase of a number of bacteria [ ]. PQQC is an oxidase whose reaction...

[ "GO:0018189" ]

[ "pyrroloquinoline quinone biosynthetic process" ]

[ "biological_process" ]

1

[ "HAMAP", "NCBIFAM" ]

[ "MF_00654", "TIGR02111" ]

[ "PQQ_syn_PqqC", "PQQ_syn_pqqC" ]

[ 4234, 4206 ]

2

[ "EC", "GP", "METACYC" ]

[ "1.3.3.11", "GenProp0170", "PWY-6420" ]

[ "EC:1.3.3.11", "GP:GenProp0170", "METACYC:PWY-6420" ]

3

[ "1otv", "1otw", "3hlx", "3hml", "3hnh", "4ny7", "5vrc", "5vrd" ]

8

[ "PUB00010477", "PUB00088860" ]

[ "12437981", "23718207" ]

[ "PqqC/D, which converts a biosynthetic intermediate to pyrroloquinoline quinone.", "Multistep, eight-electron oxidation catalyzed by the cofactorless oxidase, PqqC: identification of chemical intermediates and their dependence on molecular oxygen." ]

[ 2002, 2013 ]

2

[ "IPR039068" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Metazoa", "metagenomes" ]

[ 2, 4213, 3, 16 ]

4

[]

0

true

Family

Coenzyme PQQ biosynthesis protein C

PqqC

2

IPR011846

11,846

Cyd operon protein YbgE

Cyd_oper_YbgE

Family

2,138

false

This entry describes a small protein of unknown function, about 100 amino acids in length, essentially always found in an operon with CydAB, subunits of the cytochrome d terminal oxidase. It appears to be an integral membrane protein. It is found so far only in the Proteobacteria [ ].

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF09600", "TIGR02112" ]

[ "Cyd_oper_YbgE", "cyd_oper_ybgE" ]

[ 2138, 1454 ]

2

[]

0

[]

0

[ "PUB00015302" ]

[ "9068659" ]

[ "Characterization of the tol-pal and cyd region of Escherichia coli K-12: transcript analysis and identification of two new proteins encoded by the cyd operon." ]

[ 1997 ]

1

[]

0

null

[ "Bacteria", "metagenomes" ]

[ 2133, 5 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Cyd operon protein YbgE

Cyd_oper_YbgE

6

IPR011847

11,847

Phosphopantothenoylcysteine decarboxylase

CoaC_strep

Family

673

false

In most bacteria, a single bifunctional protein catalyses phosphopantothenoylcysteine decarboxylase and phosphopantothenate--cysteine ligase activities, sequential steps in coenzyme A biosynthesis. These activities reside in separate proteins encoded by tandem genes in some bacterial lineages. This entry describes prot...

[]

0

[ "NCBIFAM" ]

[ "TIGR02113" ]

[ "coaC_strep" ]

[ 673 ]

1

[ "GP" ]

[ "GenProp0171" ]

[ "GP:GenProp0171" ]

1

[]

0

[ "PUB00015483" ]

[ "11278255" ]

[ "Phosphopantothenoylcysteine synthetase from Escherichia coli. Identification and characterization of the last unidentified coenzyme A biosynthetic enzyme in bacteria." ]

[ 2001 ]

1

[]

0

null

[ "Bacteria" ]

[ 673 ]

1

[]

0

true

Family

Phosphopantothenoylcysteine decarboxylase

CoaC_strep

3

IPR011848

11,848

Phosphopantothenate--cysteine ligase

CoaB_strep

Family

733

false

In most bacteria, a single bifunctional protein catalyses phosphopantothenoylcysteine decarboxylase and phosphopantothenate--cysteine ligase activities, sequential steps in coenzyme A biosynthesis. These activities reside in separate proteins encoded by tandem genes in some bacterial lineages. This entry describes prot...

[]

0

[ "NCBIFAM" ]

[ "TIGR02114" ]

[ "coaB_strep" ]

[ 733 ]

1

[ "GP" ]

[ "GenProp0171" ]

[ "GP:GenProp0171" ]

1

[ "2gk4" ]

1

[ "PUB00015483" ]

[ "11278255" ]

[ "Phosphopantothenoylcysteine synthetase from Escherichia coli. Identification and characterization of the last unidentified coenzyme A biosynthetic enzyme in bacteria." ]

[ 2001 ]

1

[]

0

null

[ "Bacteria" ]

[ 733 ]

1

[]

0

true

Family

Phosphopantothenate--cysteine ligase

CoaB_strep

1

IPR011849

11,849

Sodium/pantothenate symporter

Na/pantothenate_symporter

Family

2,964

false

Pantothenate (vitamin B5) is a precursor of coenzyme A and is made from aspartate and 2-oxoisovalerate in most bacteria. However, some pathogens must import pantothenate. This entry describes PanF, a sodium/pantothenate symporter. Several species that have this transporter appear to lack all enzymes of pantothenate bio...

[ "GO:0015081", "GO:0015233", "GO:0015887", "GO:0036376", "GO:0016020" ]

[ "sodium ion transmembrane transporter activity", "pantothenate transmembrane transporter activity", "pantothenate transmembrane transport", "sodium ion export across plasma membrane", "membrane" ]

[ "molecular_function", "molecular_function", "biological_process", "biological_process", "cellular_component" ]

5

[ "NCBIFAM", "CDD" ]

[ "TIGR02119", "cd10327" ]

[ "panF", "SLC5sbd_PanF" ]

[ 2963, 2808 ]

2

[ "GP" ]

[ "GenProp0171" ]

[ "GP:GenProp0171" ]

1

[]

0

[ "PUB00015484" ]

[ "2193919" ]

[ "Cloning, sequence, and expression of the pantothenate permease (panF) gene of Escherichia coli." ]

[ 1990 ]

1

[ "IPR001734" ]

[]

1

0

1

[ "Bacteria", "Trichuris trichiura", "metagenomes" ]

[ 2961, 1, 2 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Sodium/pantothenate symporter

Na/pantothenate_symporter

7

IPR011850

11,850

Type II secretion system protein GspF

T2SS_GspF

Family

5,140

false

GspF is the inner membrane component of the type II secretion system (T2SS). It interacts with GspE, a cytoplasmic hexameric ATPase of the T2SS [ ]. The type II secretion system (T2SS) is one of several extracellular secretion systems in gram-negative bacteria. It delivers toxins and a range of hydrolytic enzymes inclu...

[ "GO:0015628", "GO:0015627" ]

[ "protein secretion by the type II secretion system", "type II protein secretion system complex" ]

[ "biological_process", "cellular_component" ]

2

[ "NCBIFAM" ]

[ "TIGR02120" ]

[ "GspF" ]

[ 5140 ]

1

[ "GP" ]

[ "GenProp0053" ]

[ "GP:GenProp0053" ]

1

[]

0

[ "PUB00051842", "PUB00093998", "PUB00094002", "PUB00094004" ]

[ "19217396", "30767847", "28258547", "22523076" ]

[ "Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody.", "Architecture, Function, and Substrates of the Type II Secretion System.", "1H, 15N and 13C resonance assignments and secondary structure of PulG, the major pseudopilin from Klebsiella oxyt...

[ 2009, 2019, 2017, 2012 ]

4

[ "IPR003004" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 5064, 5, 71 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Type II secretion system protein GspF

T2SS_GspF

2

IPR011851

11,851

Sodium/proline symporter

Na/Pro_symporter

Family

10,335

false

This family consists of the sodium/proline symporter (proline permease) from a number of Gram-negative and Gram-positive bacteria and from the archaeal genus Methanosarcina. The Na+/proline transporter contributes to the use of L-proline as a nutrient and may supply cells with compatible solute during adaptation to osm...

[ "GO:0005298", "GO:0031402", "GO:0006814", "GO:0015824", "GO:0016020" ]

[ "proline:sodium symporter activity", "sodium ion binding", "sodium ion transport", "proline transport", "membrane" ]

[ "molecular_function", "molecular_function", "biological_process", "biological_process", "cellular_component" ]

5

[ "NCBIFAM", "CDD" ]

[ "TIGR02121", "cd11475" ]

[ "Na_Pro_sym", "SLC5sbd_PutP" ]

[ 8706, 10335 ]

2

[]

0

[]

0

[ "PUB00070816" ]

[ "22201772" ]

[ "The Na⁺/L-proline transporter PutP." ]

[ 2012 ]

1

[ "IPR001734" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 253, 10005, 8, 69 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Sodium/proline symporter

Na/Pro_symporter

3

IPR011853

11,853

TRAP C4-dicarboxylate transport system permease, fused DctM-DctQ

TRAP_DctM-Dct_fused

Family

12,114

false

In some species, the 12-transmembrane spanning (DctM) and 4-transmembrane spanning (DctQ) components of tripartite ATP-independent periplasmic (TRAP)-type transporters are fused. This entry describes such transporters, found in the archaea and in bacteria.

[]

0

[ "PANTHER", "NCBIFAM" ]

[ "PTHR43849", "TIGR02123" ]

[ "", "TRAP_fused" ]

[ 12114, 11679 ]

2

[ "GP" ]

[ "GenProp0176" ]

[ "GP:GenProp0176" ]

1

[]

0

[]

0

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 537, 11252, 16, 309 ]

4

[]

0

true

Family

TRAP C4-dicarboxylate transport system permease, fused DctM-DctQ

TRAP_DctM-Dct_fused

4

IPR011854

11,854

Carbamoyl dehydratase HypE

HypE

Family

9,608

false

This family includes carbamoyl dehydratase HypE (sometimes known as hydrogenase maturation protein HypE or HupE) which is involved in the maturation of [NiFe] hydrogenases. Along with HypF, it catalyzes the synthesis of the CN ligands of the active site iron of [NiFe]-hydrogenases [ , ]. HypE dehydrates its own carbamo...

[]

0

[ "PIRSF", "PANTHER", "NCBIFAM", "CDD" ]

[ "PIRSF005644", "PTHR30303", "TIGR02124", "cd02197" ]

[ "Hdrgns_mtr_HypE", "", "hypE", "HypE" ]

[ 8622, 9604, 7149, 7025 ]

4

[ "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"...

[ "4.2.1.-", "PWY-2229", "PWY-2467", "PWY-5061", "PWY-5367", "PWY-5408", "PWY-5409", "PWY-5410", "PWY-5644", "PWY-5780", "PWY-5793", "PWY-5979", "PWY-6322", "PWY-6602", "PWY-6627", "PWY-6672", "PWY-6679", "PWY-6721", "PWY-6749", "PWY-6944", "PWY-6945", "PWY-6946", "PWY-6948...

[ "EC:4.2.1.-", "METACYC:PWY-2229", "METACYC:PWY-2467", "METACYC:PWY-5061", "METACYC:PWY-5367", "METACYC:PWY-5408", "METACYC:PWY-5409", "METACYC:PWY-5410", "METACYC:PWY-5644", "METACYC:PWY-5780", "METACYC:PWY-5793", "METACYC:PWY-5979", "METACYC:PWY-6322", "METACYC:PWY-6602", "METACYC:PWY-6...

53

[ "2i6r", "2rb9", "2z1e", "2z1f", "2z1t", "2z1u", "3vti", "3vys", "3vyt", "3vyu", "3wjp", "3wjq", "3wjr" ]

13

[ "PUB00013569", "PUB00013571", "PUB00080732", "PUB00080733", "PUB00080736", "PUB00088186" ]

[ "12196162", "1482271", "14726233", "14612240", "12586941", "15291820" ]

[ "Metal insertion into NiFe-hydrogenases.", "The hyp operon gene products are required for the maturation of catalytically active hydrogenase isoenzymes in Escherichia coli.", "Requirement of hydD, hydE, hypC and hypE genes for hydrogenase activity in Helicobacter pylori.", "FNR-mediated regulation of hyp expr...

[ 2002, 1992, 2004, 2003, 2003, 2004 ]

6

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 1225, 8104, 18, 261 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Carbamoyl dehydratase HypE

HypE

3

IPR011855

11,855

Phage major tail protein TP901-1

Phgtail_TP901_1

Family

3,774

false

This entry describes the major tail protein (MTP) of the Siphoviridae and MTP genes in prophage regions of bacterial genomes. Homologues are also found in Gene Transfer Agents (GTA) [ ], including ORFg9 (RCAP_rcc01691) of the GTA of Rhodobacter capsulatus (Rhodopseudomonas capsulata) [see Fig.1, in ]. The tail tube pro...

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF06199", "TIGR02126" ]

[ "Phage_tail_2", "phgtail_TP901_1" ]

[ 3710, 2446 ]

2

[ "GP" ]

[ "GenProp0208" ]

[ "GP:GenProp0208" ]

1

[ "5a20", "5a21", "6tba", "6te9", "6tea", "6teb", "6toa", "6tsv", "6tui", "6v8i", "6yeg", "6yq5", "8qhs", "9j1j", "9j1k", "9mu2", "9mu3" ]

17

[ "PUB00055430", "PUB00055431", "PUB00082622" ]

[ "11382219", "12399927", "17611601" ]

[ "The gene transfer agent of Rhodobacter capsulatus and \"constitutive transduction\" in prokaryotes.", "Evolutionary implications of phylogenetic analyses of the gene transfer agent (GTA) of Rhodobacter capsulatus.", "Structure of bacteriophage SPP1 tail reveals trigger for DNA ejection." ]

[ 2001, 2002, 2007 ]

3

[]

[ "IPR022344", "IPR022345" ]

0

2

0

[ "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]

[ 3423, 11, 293, 47 ]

4

[]

0

true

Family

Phage major tail protein TP901-1

Phgtail_TP901_1

7

IPR011856

11,856

tRNA endonuclease-like domain superfamily

tRNA_endonuc-like_dom_sf

Homologous_superfamily

99,718

false

This superfamily represents a structural domain found in three types of endonucleases: TsnA endonuclease (N-terminal) [ ], Hjc-type resolvase [ ], and tRNA-intron endonuclease (C-terminal) ( ) [ ]. These domains have a 3-layer α/β/α topology, which is similar in structure to a motif found in several restriction endonuc...

[ "GO:0003676" ]

[ "nucleic acid binding" ]

[ "molecular_function" ]

1

[ "CATHGENE3D" ]

[ "G3DSA:3.40.1350.10" ]

[ "" ]

[ 99718 ]

1

[ "REACTOME", "REACTOME", "REACTOME" ]

[ "R-HSA-6783310", "R-HSA-6784531", "R-MMU-6783310" ]

[ "REACTOME:R-HSA-6783310", "REACTOME:R-HSA-6784531", "REACTOME:R-MMU-6783310" ]

3

[ "1a79", "1f1z", "1gef", "1hh1", "1ipi", "1ob8", "1ob9", "1p9q", "1r0v", "1r11", "1rlv", "1rzn", "1t0f", "1xmx", "1y1o", "1y88", "1zp7", "2cv8", "2eo0", "2f4z", "2fco", "2gjw", "2guh", "2gw6", "2hmc", "2i6h", "2inb", "2ohc", "2ohe", "2okf", "2ost", "2r6u"...

118

[ "PUB00020493", "PUB00021680", "PUB00022719" ]

[ "9535656", "11286886", "15257292" ]

[ "Crystal structure and evolution of a transfer RNA splicing enzyme.", "Crystal structure of the archaeal holliday junction resolvase Hjc and implications for DNA recognition.", "The carboxy-terminal portion of TnsC activates the Tn7 transposase through a specific interaction with TnsA." ]

[ 1998, 2001, 2004 ]

3

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "IncN plasmid pKM101", "Viruses", "unclassified sequences" ]

[ 4369, 75652, 15587, 1, 2364, 1745 ]

6

[ "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",...

[ 17, 4, 21, 6, 3, 39, 9, 5, 5, 12, 3, 5, 20 ]

13

true

Homologous_superfamily

tRNA endonuclease-like domain superfamily

tRNA_endonuc-like_dom_sf

6