interpro_id string | interpro_numeric_id int64 | name string | short_name string | entry_type string | protein_count int64 | is_llm bool | is_llm_reviewed bool | abstract string | go_ids list | go_terms list | go_categories list | go_count int64 | member_databases list | member_accessions list | member_names list | member_protein_counts list | member_count int64 | external_databases list | external_accessions list | external_xrefs list | external_xref_count int64 | pdb_ids list | structure_count int64 | publication_ids list | pubmed_ids list | publication_titles list | publication_years list | publication_count int64 | parent_ids list | child_ids list | parent_count int64 | child_count int64 | tree_depth float64 | taxonomy_names list | taxonomy_protein_counts list | taxonomy_count int64 | key_species_names list | key_species_protein_counts list | key_species_count int64 | in_entry_list bool | entry_list_type string | entry_list_name string | names_dat_name string | short_names_dat_name string | split_bucket int64 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
IPR017603 | 17,603 | Benzoyl-CoA reductase, bzd-type, N subunit | Benzoyl-CoA_Rdtase_bzd_nsu | Family | 47 | false | false | Members of this family are the N subunit of one of two related types of four-subunit ATP-dependent benzoyl-CoA reductase. This enzyme system catalyses the dearomatization of benzoyl-CoA, a common intermediate in pathways for the degradation for a number of different aromatic compounds, such as phenol and toluene. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03190"
] | [
"benz_CoA_bzdN"
] | [
47
] | 1 | [] | [] | [] | 0 | [
"8s02",
"8s1t",
"8s2r"
] | 3 | [] | [] | [] | [] | 0 | [
"IPR010327"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"marine sediment metagenome"
] | [
45,
2
] | 2 | [] | [] | 0 | true | Family | Benzoyl-CoA reductase, bzd-type, N subunit | Benzoyl-CoA reductase, bzd-type, N subunit | Benzoyl-CoA_Rdtase_bzd_nsu | 6 |
IPR017604 | 17,604 | Benzoyl-CoA reductase, bzd-type, O subunit | Benzoyl-CoA_Rdtase_bzd_osu | Family | 52 | false | false | Members of this family are the O subunit of one of two related types of four-subunit ATP-dependent benzoyl-CoA reductase. This enzyme system catalyses the dearomatization of benzoyl-CoA, a common intermediate in pathways for the degradation for a number of different aromatic compounds, such as phenol and toluene. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03191"
] | [
"benz_CoA_bzdO"
] | [
52
] | 1 | [] | [] | [] | 0 | [
"8s02",
"8s1t",
"8s2r"
] | 3 | [] | [] | [] | [] | 0 | [
"IPR010327"
] | [] | 1 | 0 | 1 | [
"Archaeoglobaceae",
"Bacteria",
"ecological metagenomes"
] | [
3,
44,
5
] | 3 | [] | [] | 0 | true | Family | Benzoyl-CoA reductase, bzd-type, O subunit | Benzoyl-CoA reductase, bzd-type, O subunit | Benzoyl-CoA_Rdtase_bzd_osu | 4 |
IPR017605 | 17,605 | Benzoyl-CoA reductase, bzd-type, Q subunit | Benzoyl-CoA_Rdtase_bzd_qsu | Family | 58 | false | false | Members of this family are the Q subunit of one of two related types of four-subunit ATP-dependent benzoyl-CoA reductase. This enzyme system catalyses the dearomatization of benzoyl-CoA, a common intermediate in pathways for the degradation for a number of different aromatic compounds, such as phenol and toluene. | [
"GO:0018522"
] | [
"benzoyl-CoA reductase activity"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM",
"CDD"
] | [
"TIGR03192",
"cd24106"
] | [
"benz_CoA_bzdQ",
"ASKHA_NBD_benz_CoA_BzdQ"
] | [
52,
58
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00119922"
] | [
"15317781"
] | [
"The bzd gene cluster, coding for anaerobic benzoate catabolism, in Azoarcus sp. strain CIB."
] | [
2004
] | 1 | [] | [] | 0 | 0 | null | [
"Archaeoglobaceae",
"Bacteria",
"ecological metagenomes"
] | [
3,
50,
5
] | 3 | [] | [] | 0 | true | Family | Benzoyl-CoA reductase, bzd-type, Q subunit | Benzoyl-CoA reductase, bzd-type, Q subunit | Benzoyl-CoA_Rdtase_bzd_qsu | 5 |
IPR017606 | 17,606 | 4-hydroxybenzoyl-CoA reductase, gamma subunit | 4hydrxbenzoyl-CoA_Rdtase_gsu | Family | 44 | false | false | This entry represents the gamma subunit (HcrC) of the three-subunit enzyme 4-HBCR. It is 17 kDa in size and has two [2Fe-2S] clusters [ ]. 4-Hydroxybenzoyl-CoA reductase (4-HBCR) is a member of the xanthine oxidase (XO) family of molybdenum cofactor containing enzymes. It catalyses the irreversible removal of a phenoli... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03193"
] | [
"4hydroxCoAred"
] | [
44
] | 1 | [
"GP"
] | [
"GenProp0703"
] | [
"GP:GenProp0703"
] | 1 | [
"1rm6",
"1sb3"
] | 2 | [
"PUB00030666",
"PUB00043316",
"PUB00043317"
] | [
"14747735",
"18393440",
"9490068"
] | [
"Crystallization of 4-hydroxybenzoyl-CoA reductase and the structure of its electron donor ferredoxin.",
"Inhibitors of the molybdenum cofactor containing 4-hydroxybenzoyl-CoA reductase.",
"4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from the denitrifying bacterium Thauera aromatica--prosthetic groups, ele... | [
2004,
2008,
1998
] | 3 | [] | [] | 0 | 0 | null | [
"Pseudomonadota",
"ecological metagenomes"
] | [
42,
2
] | 2 | [] | [] | 0 | true | Family | 4-hydroxybenzoyl-CoA reductase, gamma subunit | 4-hydroxybenzoyl-CoA reductase, gamma subunit | 4hydrxbenzoyl-CoA_Rdtase_gsu | 9 |
IPR017607 | 17,607 | 4-hydroxybenzoyl-CoA reductase, alpha subunit | 4hydrxbenzoyl-CoA_Rdtase_asu | Family | 70 | false | false | This entry represents the largest chain of 4-HBCR, alpha (HcrA) of 4-hydroxybenzoyl-CoA reductase. It is 82 kDa in size and contains a Mo-cofactor-binding site [ ]. 4-Hydroxybenzoyl-CoA reductase (4-HBCR) is a member of the xanthine oxidase (XO) family of molybdenum cofactor containing enzymes. It catalyses the irrever... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03194"
] | [
"4hydrxCoA_A"
] | [
70
] | 1 | [
"GP"
] | [
"GenProp0703"
] | [
"GP:GenProp0703"
] | 1 | [
"1rm6",
"1sb3"
] | 2 | [
"PUB00030666",
"PUB00043316",
"PUB00043317"
] | [
"14747735",
"18393440",
"9490068"
] | [
"Crystallization of 4-hydroxybenzoyl-CoA reductase and the structure of its electron donor ferredoxin.",
"Inhibitors of the molybdenum cofactor containing 4-hydroxybenzoyl-CoA reductase.",
"4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from the denitrifying bacterium Thauera aromatica--prosthetic groups, ele... | [
2004,
2008,
1998
] | 3 | [
"IPR016208"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"ecological metagenomes"
] | [
67,
3
] | 2 | [] | [] | 0 | true | Family | 4-hydroxybenzoyl-CoA reductase, alpha subunit | 4-hydroxybenzoyl-CoA reductase, alpha subunit | 4hydrxbenzoyl-CoA_Rdtase_asu | 2 |
IPR017608 | 17,608 | 4-hydroxybenzoyl-CoA reductase, beta subunit | 4hydrxbenzoyl-CoA_Rdtase_bsu | Family | 48 | false | false | This entry represents the second largest chain, beta (HcrB, 35 kDa), of the enzyme 4-hydroxybenzoyl-CoA reductase. In Thauera aromatica, there is an additional domain in the beta-subunit, which probably has an extra iron-sulphur cluster [ ]. 4-Hydroxybenzoyl-CoA reductase (4-HBCR) is a member of the xanthine oxidase (X... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03195"
] | [
"4hydrxCoA_B"
] | [
48
] | 1 | [
"GP"
] | [
"GenProp0703"
] | [
"GP:GenProp0703"
] | 1 | [
"1rm6",
"1sb3"
] | 2 | [
"PUB00030666",
"PUB00043316",
"PUB00043317"
] | [
"14747735",
"18393440",
"9490068"
] | [
"Crystallization of 4-hydroxybenzoyl-CoA reductase and the structure of its electron donor ferredoxin.",
"Inhibitors of the molybdenum cofactor containing 4-hydroxybenzoyl-CoA reductase.",
"4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from the denitrifying bacterium Thauera aromatica--prosthetic groups, ele... | [
2004,
2008,
1998
] | 3 | [] | [] | 0 | 0 | null | [
"Pseudomonadota",
"mine drainage metagenome"
] | [
47,
1
] | 2 | [] | [] | 0 | true | Family | 4-hydroxybenzoyl-CoA reductase, beta subunit | 4-hydroxybenzoyl-CoA reductase, beta subunit | 4hydrxbenzoyl-CoA_Rdtase_bsu | 3 |
IPR017609 | 17,609 | Xanthine dehydrogenase D subunit | Xanthine_dehydrogenase_dsu | Family | 1,116 | false | false | This gene has been characterised in Bacillus subtilis [ ] as the molybdopterin binding-subunit of xanthine dehydrogenase (pucD), acting in conjunction with pucC, the FAD-binding subunit and pucE, the FeS-binding subunit. The more common XDH complex ( ) includes the xdhB gene which is related to pucD. It appears that mo... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03196"
] | [
"pucD"
] | [
1116
] | 1 | [
"GP"
] | [
"GenProp0705"
] | [
"GP:GenProp0705"
] | 1 | [] | 0 | [
"PUB00016396"
] | [
"11344136"
] | [
"Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator."
] | [
2001
] | 1 | [
"IPR016208"
] | [] | 1 | 0 | 1 | [
"Bacillati",
"ecological metagenomes"
] | [
1080,
36
] | 2 | [] | [] | 0 | true | Family | Xanthine dehydrogenase D subunit | Xanthine dehydrogenase D subunit | Xanthine_dehydrogenase_dsu | 4 |
IPR017610 | 17,610 | tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC, C-terminal | tRNA_S-uridine_synth_MnmC_C | Domain | 7,084 | false | false | In Escherichia coli, the protein previously designated YfcK is now identified as the bifunctional enzyme MnmC. It acts, following the action of the heterotetramer of GidA and MnmE, in the modification of U-34 of certain tRNA to 5-methylaminomethyl-2-thiouridine (mnm5s2U). In other bacteria, the corresponding proteins a... | [
"GO:0008168",
"GO:0016645"
] | [
"methyltransferase activity",
"oxidoreductase activity, acting on the CH-NH group of donors"
] | [
"molecular_function",
"molecular_function"
] | 2 | [
"NCBIFAM"
] | [
"TIGR03197"
] | [
"MnmC_Cterm"
] | [
7084
] | 1 | [
"EC",
"GP",
"GP",
"METACYC"
] | [
"2.1.1.61",
"GenProp0704",
"GenProp1555",
"PWY-7892"
] | [
"EC:2.1.1.61",
"GP:GenProp0704",
"GP:GenProp1555",
"METACYC:PWY-7892"
] | 4 | [
"3awi",
"3ps9",
"3pvc",
"3sgl"
] | 4 | [
"PUB00043072",
"PUB00106732"
] | [
"15247431",
"23617613"
] | [
"Identification of a bifunctional enzyme MnmC involved in the biosynthesis of a hypermodified uridine in the wobble position of tRNA.",
"Structural basis for hypermodification of the wobble uridine in tRNA by bifunctional enzyme MnmC."
] | [
2004,
2013
] | 2 | [
"IPR006076"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
7033,
5,
46
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC, C-terminal | tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC, C-terminal | tRNA_S-uridine_synth_MnmC_C | 2 |
IPR017611 | 17,611 | Xanthine dehydrogenase E subunit | Xanthine_dehydrogenase_esu | Family | 34 | false | false | This protein has been characterised in Bacillus subtilis [ ] as the iron-sulphur cluster binding-subunit of xanthine dehydrogenase (pucE), acting in conjunction with pucC, the FAD-binding subunit and pucD, the molybdopterin binding subunit. The more common XDH complex ( ) includes the xdhA gene as the Fe-S cluster bind... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03198"
] | [
"pucE"
] | [
34
] | 1 | [
"GP"
] | [
"GenProp0705"
] | [
"GP:GenProp0705"
] | 1 | [] | 0 | [
"PUB00016396"
] | [
"11344136"
] | [
"Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Bacillaceae"
] | [
34
] | 1 | [] | [] | 0 | true | Family | Xanthine dehydrogenase E subunit | Xanthine dehydrogenase E subunit | Xanthine_dehydrogenase_esu | 3 |
IPR017612 | 17,612 | Xanthine dehydrogenase C subunit | Xanthine_dehydrogenase_csu | Family | 30 | false | false | This protein has been characterised in Bacillus subtilis [ ] as the FAD binding-subunit of xanthine dehydrogenase (pucC), acting in conjunction with pucD, the molybdopterin-binding subunit and pucE, the FeS-binding subunit. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03199"
] | [
"pucC"
] | [
30
] | 1 | [
"GP"
] | [
"GenProp0705"
] | [
"GP:GenProp0705"
] | 1 | [] | 0 | [
"PUB00016396"
] | [
"11344136"
] | [
"Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Bacillaceae"
] | [
30
] | 1 | [] | [] | 0 | true | Family | Xanthine dehydrogenase C subunit | Xanthine dehydrogenase C subunit | Xanthine_dehydrogenase_csu | 4 |
IPR017613 | 17,613 | 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase | Dearomat_hydrolase | Family | 137 | false | false | 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase is a ring-hydrolysing enzyme involved in the anaerobic metabolism of aromatic enzymes by way of benzoyl-CoA, as seen in Thauera aromatica [ ], Geobacter metallireducens, and Azoarcus sp. (strain EbN1). Note that Rhodopseudomonas palustris uses a different pathway to perform ... | [
"GO:0016823"
] | [
"hydrolase activity, acting on carbon-carbon bonds, in ketonic substances"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR03200"
] | [
"dearomat_oah"
] | [
137
] | 1 | [
"EC",
"GP"
] | [
"3.7.1.21",
"GenProp0706"
] | [
"EC:3.7.1.21",
"GP:GenProp0706"
] | 2 | [] | 0 | [
"PUB00042973"
] | [
"10406950"
] | [
"6-Hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase and 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase, enzymes of the benzoyl-CoA pathway of anaerobic aromatic metabolism in the denitrifying bacterium Thauera aromatica."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"ecological metagenomes"
] | [
127,
10
] | 2 | [] | [] | 0 | true | Family | 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase | 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase | Dearomat_hydrolase | 3 |
IPR017614 | 17,614 | 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase | Dearomat_deydrogenase | Family | 130 | false | false | 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase is an enzyme found in the anaerobic metabolism of aromatic enzymes by way of benzoyl-CoA, as seen in Thauera aromatica [ ], Geobacter metallireducens, and Azoarcus sp. (strain EbN1). The experimentally characterised form from T. aromatica uses only NAD+, not NADP+. N... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03201"
] | [
"dearomat_had"
] | [
130
] | 1 | [
"GP"
] | [
"GenProp0706"
] | [
"GP:GenProp0706"
] | 1 | [
"7qul",
"7quy"
] | 2 | [
"PUB00042973"
] | [
"10406950"
] | [
"6-Hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase and 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase, enzymes of the benzoyl-CoA pathway of anaerobic aromatic metabolism in the denitrifying bacterium Thauera aromatica."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"ecological metagenomes"
] | [
122,
8
] | 2 | [] | [] | 0 | true | Family | 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase | 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase | Dearomat_deydrogenase | 3 |
IPR017615 | 17,615 | Xanthine dehydrogenase, accessory protein PucB | Xanthine_dehydrogenase_PucB | Family | 57 | false | false | Members of this protein family are PucB proteins found in Bacillus subtilis [ ]. The expression of this protein is located in an operon with the structural subunits of xanthine dehydrogenase, and has been found to be essential for XDH activity. Some members of this family appear to have a distant relationship to the Mo... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03202"
] | [
"pucB"
] | [
57
] | 1 | [
"GP"
] | [
"GenProp0705"
] | [
"GP:GenProp0705"
] | 1 | [] | 0 | [
"PUB00016396"
] | [
"11344136"
] | [
"Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator."
] | [
2001
] | 1 | [] | [] | 0 | 0 | null | [
"Bacillales"
] | [
57
] | 1 | [] | [] | 0 | true | Family | Xanthine dehydrogenase, accessory protein PucB | Xanthine dehydrogenase, accessory protein PucB | Xanthine_dehydrogenase_PucB | 6 |
IPR017616 | 17,616 | Pimeloyl-CoA dehydrogenase, small subunit | Pimeloyl_CoA_dehydrogenase_ssu | Family | 128 | false | false | Members of this protein family are PimD proteins, and can be found in Rhodopseudomonas palustris and Bradyrhizobium japonicum. The pimFABCDE operon encodes proteins for the metabolism of straight chain dicarboxylates of seven to fourteen carbons. Pimeloyl-CoA is a catabolite of benzoyl-CoA degradation, which occurs in ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03203"
] | [
"pimD_small"
] | [
128
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Nitrobacteraceae"
] | [
128
] | 1 | [] | [] | 0 | true | Family | Pimeloyl-CoA dehydrogenase, small subunit | Pimeloyl-CoA dehydrogenase, small subunit | Pimeloyl_CoA_dehydrogenase_ssu | 3 |
IPR017617 | 17,617 | Pimeloyl-CoA dehydrogenase, large subunit | Pimeloyl_CoA_dehydrogenase_lsu | Family | 222 | false | false | Members of this protein family are PimC proteins that can be found in Rhodopseudomonas palustris and Bradyrhizobium japonicum. The pimFABCDE operon encodes proteins for the metabolism of straight chain dicarboxylates of seven to fourteen carbons. Pimeloyl-CoA, is a catabolite of benzoyl-CoA degradation, which occurs in... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03204"
] | [
"pimC_large"
] | [
222
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Alphaproteobacteria",
"marine sediment metagenome"
] | [
221,
1
] | 2 | [] | [] | 0 | true | Family | Pimeloyl-CoA dehydrogenase, large subunit | Pimeloyl-CoA dehydrogenase, large subunit | Pimeloyl_CoA_dehydrogenase_lsu | 5 |
IPR017618 | 17,618 | Dicarboxylate-CoA ligase PimA | Dicarboxylate-CoA_ligase_PimA | Family | 149 | false | false | PimA, a member of a large family of acyl-CoA ligases, is found in a characteristic operon pimFABCDE for the metabolism of pimelate and related compounds. It is found, so far, in Bradyrhizobium japonicum and several strains of Rhodopseudomonas palustris. PimA from R. palustris was shown to be active as a CoA ligase for ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03205"
] | [
"pimA"
] | [
149
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00042974"
] | [
"15758219"
] | [
"The pimFABCDE operon from Rhodopseudomonas palustris mediates dicarboxylic acid degradation and participates in anaerobic benzoate degradation."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Alphaproteobacteria"
] | [
149
] | 1 | [] | [] | 0 | true | Family | Dicarboxylate-CoA ligase PimA | Dicarboxylate-CoA ligase PimA | Dicarboxylate-CoA_ligase_PimA | 6 |
IPR017619 | 17,619 | 2-hydroxycyclohexanecarboxyl-CoA dehydrogenase | OH-benzo_CoA_DH_BadH | Family | 183 | false | false | This entry represents the enzyme 2-hydroxycyclohexanecarboxyl-CoA dehydrogenase. The enzymatic properties the enzyme is homotetrameric, and not sensitive to oxygen. 2-hydroxycyclohexanecarboxyl-CoA dehydrogenaseis part of proposed pathway for degradation of benzoyl-CoA to 3-hydroxypimeloyl-CoA that differs from the ana... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03206"
] | [
"benzo_BadH"
] | [
183
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00042975"
] | [
"10781543"
] | [
"2-Hydroxycyclohexanecarboxyl coenzyme A dehydrogenase, an enzyme characteristic of the anaerobic benzoate degradation pathway used by Rhodopseudomonas palustris."
] | [
2000
] | 1 | [
"IPR002347"
] | [] | 1 | 0 | 1 | [
"Pseudomonadota",
"bioreactor metagenome"
] | [
182,
1
] | 2 | [] | [] | 0 | true | Family | 2-hydroxycyclohexanecarboxyl-CoA dehydrogenase | 2-hydroxycyclohexanecarboxyl-CoA dehydrogenase | OH-benzo_CoA_DH_BadH | 6 |
IPR017621 | 17,621 | Cyclohexanecarboxylate-CoA ligase | Cyclohxane-COOH-CoA_Ligase | Family | 227 | false | false | Cyclohexanecarboxylate-CoA ligase prepares the aliphatic ring compound, cyclohexanecarboxylate, for dehydrogenation and then degradation by a pathway also used in benzoyl-CoA degradation in Rhodopseudomonas palustris. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03208"
] | [
"cyc_hxne_CoA_lg"
] | [
227
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Pseudomonadota",
"bioreactor metagenome"
] | [
226,
1
] | 2 | [] | [] | 0 | true | Family | Cyclohexanecarboxylate-CoA ligase | Cyclohexanecarboxylate-CoA ligase | Cyclohxane-COOH-CoA_Ligase | 6 |
IPR017622 | 17,622 | Botulinum neurotoxin transcription-activating sigma factor BotR | Tscrpt_reg_BotR | Family | 60 | false | false | Regulatory sigma-70 protein, BotR transcription regulator regulates neurotoxin production in Clostridium botulinum. Similarly, tetanus toxin production of Clostridium tetani is regulated by TetR which is a very close relative of BotR. Functional complementation experiments have been done for botR and tetR in highly tra... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03209"
] | [
"P21_Cbot"
] | [
60
] | 1 | [
"GP"
] | [
"GenProp0707"
] | [
"GP:GenProp0707"
] | 1 | [] | 0 | [
"PUB00042842",
"PUB00043073",
"PUB00043074"
] | [
"16677313",
"15158256",
"16701505"
] | [
"Regulation of toxin and bacteriocin gene expression in Clostridium by interchangeable RNA polymerase sigma factors.",
"Nucleotide sequence and transcriptional analysis of the type A2 neurotoxin gene cluster in Clostridium botulinum.",
"Organization and regulation of the neurotoxin genes in Clostridium botulinu... | [
2006,
2004,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Clostridium",
"unclassified Caudoviricetes"
] | [
58,
2
] | 2 | [] | [] | 0 | true | Family | Botulinum neurotoxin transcription-activating sigma factor BotR | Botulinum neurotoxin transcription-activating sigma factor BotR | Tscrpt_reg_BotR | 8 |
IPR017623 | 17,623 | 2-ketocyclohexanecarboxyl-CoA hydrolase | Keto-benzo_CoA_Hydrolase | Family | 300 | false | false | 2-ketocyclohexanecarboxyl-CoA hydrolase is a ring-opening enzyme that acts in catabolism of molecules such as benzoyl-CoA and cyclohexane carboxylate. It converts -ketocyclohexanecarboxyl-CoA to pimelyl-CoA. It is not sensitive to oxygen [ ]. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03210"
] | [
"badI"
] | [
300
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00042976"
] | [
"9573182"
] | [
"2-Ketocyclohexanecarboxyl coenzyme A hydrolase, the ring cleavage enzyme required for anaerobic benzoate degradation by Rhodopseudomonas palustris."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Pseudomonadota",
"ecological metagenomes"
] | [
298,
2
] | 2 | [] | [] | 0 | true | Family | 2-ketocyclohexanecarboxyl-CoA hydrolase | 2-ketocyclohexanecarboxyl-CoA hydrolase | Keto-benzo_CoA_Hydrolase | 5 |
IPR017624 | 17,624 | Catechol 2,3 dioxygenase | Catechol_2-3_dOase | Family | 1,712 | false | false | This entry represents catechol 2,3 dioxygenase ( ), although some members have highly significant activity on catechol derivatives such as 3-methylcatechol, 3-chlorocatechol, and 4-chlorocatechol [ ]. Catechol 2,3 dioxygenase is also called metapyrocatechase, as it performs a meta-cleavage (an extradiol ring cleavage) ... | [
"GO:0008198",
"GO:0018577",
"GO:0009056"
] | [
"ferrous iron binding",
"catechol 2,3-dioxygenase activity",
"catabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR03211"
] | [
"catechol_2_3"
] | [
1712
] | 1 | [
"EC",
"GP",
"METACYC",
"METACYC"
] | [
"1.13.11.2",
"GenProp0708",
"PWY-5419",
"PWY-5641"
] | [
"EC:1.13.11.2",
"GP:GenProp0708",
"METACYC:PWY-5419",
"METACYC:PWY-5641"
] | 4 | [
"1mpy",
"3hpv",
"3hpy",
"3hq0",
"5znh",
"5zsx",
"5zsz"
] | 7 | [
"PUB00042843"
] | [
"9973359"
] | [
"Conversion of 3-chlorocatechol by various catechol 2,3-dioxygenases and sequence analysis of the chlorocatechol dioxygenase region of Pseudomonas putida GJ31."
] | [
1999
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Potamilus streckersoni",
"Saccharolobus solfataricus",
"Sym plasmid",
"unclassified sequences"
] | [
1689,
1,
3,
1,
18
] | 5 | [] | [] | 0 | true | Family | Catechol 2,3 dioxygenase | Catechol 2,3 dioxygenase | Catechol_2-3_dOase | 3 |
IPR017625 | 17,625 | Allantoinase PuuE | PuuE | Domain | 6,254 | false | false | Allantoinase ([ec:]3.5.2.5) can hydrolyze allantoin((2,5-dioxoimidazolidin-4-yl)urea), one of the most important nitrogen carrier for some plants, soil animals, and microorganisms, to allantoate. DAL1 gene from Saccharomyces cerevisiae encodes an allantoinase. However, some organisms possess allantoinase activity but l... | [] | [] | [] | 0 | [
"NCBIFAM",
"CDD"
] | [
"TIGR03212",
"cd10977"
] | [
"uraD_N-term-dom",
"CE4_PuuE_SpCDA1"
] | [
5881,
6175
] | 2 | [
"GP"
] | [
"GenProp0688"
] | [
"GP:GenProp0688"
] | 1 | [
"1z7a",
"3cl6",
"3cl7",
"3cl8",
"3s6o"
] | 5 | [
"PUB00051042"
] | [
"18550550"
] | [
"Logical identification of an allantoinase analog (puuE) recruited from polysaccharide deacetylases."
] | [
2008
] | 1 | [
"IPR002509"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
6061,
140,
53
] | 3 | [] | [] | 0 | true | Domain | Allantoinase PuuE | Allantoinase PuuE | PuuE | 2 |
IPR017626 | 17,626 | Biphenyl-2,3-diol 1,2-dioxygenase | DiOHbiphenyl_dOase | Family | 541 | false | false | Biphenyl-2,3-diol 1,2-dioxygenase (also called 2,3-dihydroxybiphenyl 1,2-dioxygenase) is the third enzyme of a pathway for biphenyl degradation. Many of the extradiol ring-cleaving dioxygenases, to which these proteins belong, act on a range of related substrates. Some members of this family may be found operons for to... | [
"GO:0005506",
"GO:0051213",
"GO:0042178"
] | [
"iron ion binding",
"dioxygenase activity",
"xenobiotic catabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR03213"
] | [
"23dbph12diox"
] | [
541
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC"
] | [
"1.13.11.39",
"PWY-6550",
"PWY-7008",
"PWY-7747"
] | [
"EC:1.13.11.39",
"METACYC:PWY-6550",
"METACYC:PWY-7008",
"METACYC:PWY-7747"
] | 4 | [
"1dhy",
"1eil",
"1eiq",
"1eir",
"1han",
"1kmy",
"1knd",
"1knf",
"1kw3",
"1kw6",
"1kw8",
"1kw9",
"1lgt",
"1lkd",
"2wl3",
"2wl9"
] | 16 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Geodia barretti"
] | [
540,
1
] | 2 | [] | [] | 0 | true | Family | Biphenyl-2,3-diol 1,2-dioxygenase | Biphenyl-2,3-diol 1,2-dioxygenase | DiOHbiphenyl_dOase | 4 |
IPR017627 | 17,627 | (S)-ureidoglycine aminohydrolase | UGHY | Family | 4,758 | false | false | This entry represents the (S)-ureidoglycine aminohydrolase UGlyAH from bacteria and fungi, including UGlyAH from Escherichia coli and some plant homologues. (S)-ureidoglycine aminohydrolase (UGHY or UGlyAH) is involved in the ureide pathway, a metabolic route of purine catabolism in plants, some bacteria and probably i... | [
"GO:0071522"
] | [
"ureidoglycine aminohydrolase activity"
] | [
"molecular_function"
] | 1 | [
"PANTHER",
"NCBIFAM"
] | [
"PTHR34571",
"TIGR03214"
] | [
"",
"ura-cupin"
] | [
4754,
4453
] | 2 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC"
] | [
"3.5.3.26",
"GenProp0686",
"GenProp0687",
"GenProp1326",
"GenProp1416",
"PWY-5692",
"PWY-5698"
] | [
"EC:3.5.3.26",
"GP:GenProp0686",
"GP:GenProp0687",
"GP:GenProp1326",
"GP:GenProp1416",
"METACYC:PWY-5692",
"METACYC:PWY-5698"
] | 7 | [
"1rc6",
"1sef",
"1sfn",
"1sq4",
"4e2q",
"4e2s"
] | 6 | [
"PUB00078751",
"PUB00096858",
"PUB00096859"
] | [
"19935661",
"20038185",
"22493446"
] | [
"Ureide catabolism in Arabidopsis thaliana and Escherichia coli.",
"Chemical basis of nitrogen recovery through the ureide pathway: formation and hydrolysis of S-ureidoglycine in plants and bacteria.",
"Structural and functional insights into (S)-ureidoglycine aminohydrolase, key enzyme of purine catabolism in ... | [
2010,
2010,
2012
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
3828,
912,
18
] | 3 | [
"Arabidopsis thaliana",
"Escherichia coli (strain K12)",
"Oryza sativa subsp. japonica",
"Zea mays"
] | [
6,
1,
1,
6
] | 4 | true | Family | (S)-ureidoglycine aminohydrolase | (S)-ureidoglycine aminohydrolase | UGHY | 7 |
IPR017628 | 17,628 | 2-hydroxymuconic semialdehyde dehydrogenase | OHmuconic_semiald_DH | Family | 1,644 | false | false | Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. 2-hydroxymuconic semialdehyde dehydrogenase performs the second of seven steps in that pathway for catechol degradation. | [
"GO:0016620"
] | [
"oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR03216"
] | [
"OH_muco_semi_DH"
] | [
1644
] | 1 | [
"GP"
] | [
"GenProp0708"
] | [
"GP:GenProp0708"
] | 1 | [
"4i1w",
"4i25",
"4i26",
"4i2r",
"4npi",
"4oe2",
"4ou2",
"4oub",
"4u3w",
"5kj5",
"5klk",
"5kll",
"5klm",
"5kln",
"5klo",
"7bzv"
] | 16 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Sym plasmid",
"unclassified sequences"
] | [
1630,
1,
13
] | 3 | [] | [] | 0 | true | Family | 2-hydroxymuconic semialdehyde dehydrogenase | 2-hydroxymuconic semialdehyde dehydrogenase | OHmuconic_semiald_DH | 5 |
IPR017629 | 17,629 | 4-hydroxy-2-oxovalerate aldolase | 4OH_2_O-val_aldolase | Family | 5,931 | false | false | 4-hydroxy 2-ketovalerate aldolase (also known as 4-hydroxy-2-ketovalerate aldolase and 4-hydroxy-2-oxopentanoate aldolase (HOA)) converts 4-hydroxy-2-oxopentanoate to acetaldehyde and pyruvate, the penultimate step in the meta-cleavage pathway for the degradation of phenols, cresols and catechol. Acetaldehyde is then c... | [
"GO:0008701",
"GO:0009056"
] | [
"4-hydroxy-2-oxovalerate aldolase activity",
"catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01656",
"TIGR03217"
] | [
"HOA",
"4OH_2_O_val_ald"
] | [
5865,
5930
] | 2 | [
"EC",
"GP",
"GP",
"METACYC"
] | [
"4.1.3.39",
"GenProp0708",
"GenProp1231",
"PWY-5162"
] | [
"EC:4.1.3.39",
"GP:GenProp0708",
"GP:GenProp1231",
"METACYC:PWY-5162"
] | 4 | [
"1nvm",
"4jn6",
"4lrs",
"4lrt",
"8ih7"
] | 5 | [
"PUB00016385",
"PUB00038481",
"PUB00085887",
"PUB00085888",
"PUB00085889"
] | [
"12764229",
"16330546",
"16782065",
"19476337",
"11264589"
] | [
"Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate.",
"Crystal structures of two bacterial 3-hydroxy-3-methylglutaryl-CoA lyases suggest a common catalytic mechanism among a family of TIM barrel metalloenzymes cleaving carbon-carbon bonds.",
"Coupled e... | [
2003,
2006,
2006,
2009,
2001
] | 5 | [
"IPR050073"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"Halobacteriales",
"Sym plasmid",
"unclassified sequences"
] | [
5873,
11,
13,
1,
33
] | 5 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | 4-hydroxy-2-oxovalerate aldolase | 4-hydroxy-2-oxovalerate aldolase | 4OH_2_O-val_aldolase | 3 |
IPR017630 | 17,630 | 4-oxalocrotonate decarboxylase | 4-oxalocrotonate_decarboxylase | Family | 608 | false | false | This entry represents 4-oxalocrotonate decarboxylase. This protein is characterised (indirectly) in Pseudomonas sp. (strain CF600) and was inactive except when co-expressed with DmpE, 2-oxopent-4-enoate hydratase, a homologous protein from the same operon [ ]. Both of these enzymes are active in the degradation of cate... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03218"
] | [
"catechol_dmpH"
] | [
608
] | 1 | [
"GP"
] | [
"GenProp0708"
] | [
"GP:GenProp0708"
] | 1 | [
"5d2f",
"5d2g",
"5d2h",
"5d2i",
"5d2j",
"5d2k"
] | 6 | [
"PUB00042979",
"PUB00150964",
"PUB00150965"
] | [
"1732207",
"27082660",
"29487229"
] | [
"Nucleotide sequence and functional analysis of the complete phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600.",
"Crystal Structures of Apo and Liganded 4-Oxalocrotonate Decarboxylase Uncover a Structural Basis for the Metal-Assisted Decarboxylation of a Vinylogous β-Keto Acid.",
"The... | [
1992,
2016,
2018
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Sym plasmid",
"unclassified sequences"
] | [
601,
1,
6
] | 3 | [] | [] | 0 | true | Family | 4-oxalocrotonate decarboxylase | 4-oxalocrotonate decarboxylase | 4-oxalocrotonate_decarboxylase | 8 |
IPR017632 | 17,632 | 2-oxopent-4-enoate hydratase | 2-oxopent-4-enoate_hydratase | Family | 737 | false | false | 2-oxopent-4-enoate hydratase, which is also called 2-hydroxypent-2,4-dienoate hydratase is closely related to another gene found in the same operon, 4-oxalocrotonate decarboxylase, with which it interacts closely [ ]. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03220"
] | [
"catechol_dmpE"
] | [
737
] | 1 | [
"GP"
] | [
"GenProp0708"
] | [
"GP:GenProp0708"
] | 1 | [] | 0 | [
"PUB00042979"
] | [
"1732207"
] | [
"Nucleotide sequence and functional analysis of the complete phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600."
] | [
1992
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Sym plasmid",
"ecological metagenomes"
] | [
733,
1,
3
] | 3 | [] | [] | 0 | true | Family | 2-oxopent-4-enoate hydratase | 2-oxopent-4-enoate hydratase | 2-oxopent-4-enoate_hydratase | 3 |
IPR017633 | 17,633 | Benzoyl-CoA-dihydrodiol lyase | Benz-CoA_dihydrodiol_lyase | Family | 1,178 | false | false | In the presence of O2, the benzoyl-CoA oxygenase/reductase BoxBA BoxAB converts benzoyl-CoA to 2,3-dihydro-2,3-dihydroxybenzoyl-CoA [ ]. Members of this family, BoxC, homologous to enoyl-CoA hydratases/isomerases, hydrolyse this compound to 3,4-dehydroadipyl-CoA semialdehyde + HCOOH. | [
"GO:0016829"
] | [
"lyase activity"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR03222"
] | [
"benzo_boxC"
] | [
1178
] | 1 | [
"GP"
] | [
"GenProp0709"
] | [
"GP:GenProp0709"
] | 1 | [
"2w3p"
] | 1 | [
"PUB00042986"
] | [
"15916608"
] | [
"Aerobic benzoyl-CoA catabolic pathway in Azoarcus evansii: studies on the non-oxygenolytic ring cleavage enzyme."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Effrenium voratum",
"unclassified sequences"
] | [
1162,
1,
15
] | 3 | [] | [] | 0 | true | Family | Benzoyl-CoA-dihydrodiol lyase | Benzoyl-CoA-dihydrodiol lyase | Benz-CoA_dihydrodiol_lyase | 9 |
IPR017634 | 17,634 | Benzoyl-CoA oxygenase/reductase BoxA | Benzoyl_CoA_Oase_BoxA | Family | 660 | false | false | Members of this protein family are BoxA, the A component of the BoxAB benzoyl-CoA oxygenase/reductase. This oxygen-requiring enzyme acts in an aerobic pathway of benzoate catabolism via coenzyme A ligation. BoxA is a homodimeric iron-sulphur-flavoprotein and acts as an NADPH-dependent reductase for BoxB [ , ]. | [] | [] | [] | 0 | [
"PIRSF",
"NCBIFAM"
] | [
"PIRSF501177",
"TIGR03224"
] | [
"BoxA",
"benzo_boxA"
] | [
660,
652
] | 2 | [
"GP"
] | [
"GenProp0709"
] | [
"GP:GenProp0709"
] | 1 | [] | 0 | [
"PUB00042986",
"PUB00043075"
] | [
"15916608",
"15458418"
] | [
"Aerobic benzoyl-CoA catabolic pathway in Azoarcus evansii: studies on the non-oxygenolytic ring cleavage enzyme.",
"New enzymes involved in aerobic benzoate metabolism in Azoarcus evansii."
] | [
2005,
2004
] | 2 | [
"IPR015701"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
656,
2,
2
] | 3 | [] | [] | 0 | true | Family | Benzoyl-CoA oxygenase/reductase BoxA | Benzoyl-CoA oxygenase/reductase BoxA | Benzoyl_CoA_Oase_BoxA | 4 |
IPR017635 | 17,635 | Benzoyl-CoA oxygenase BoxB | Benzoyl_CoA_Oase_BoxB | Family | 1,204 | false | false | Members of this protein family are BoxB, the B subunit of benzoyl-CoA oxygenase. This oxygen-requiring enzyme acts in an aerobic pathway of benzoate catabolism via coenzyme A ligation [ ]. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03225"
] | [
"benzo_boxB"
] | [
1204
] | 1 | [
"GP"
] | [
"GenProp0709"
] | [
"GP:GenProp0709"
] | 1 | [
"3per",
"3pf7",
"3pm5",
"3q1g"
] | 4 | [
"PUB00042986"
] | [
"15916608"
] | [
"Aerobic benzoyl-CoA catabolic pathway in Azoarcus evansii: studies on the non-oxygenolytic ring cleavage enzyme."
] | [
2005
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
1178,
4,
22
] | 3 | [] | [] | 0 | true | Family | Benzoyl-CoA oxygenase BoxB | Benzoyl-CoA oxygenase BoxB | Benzoyl_CoA_Oase_BoxB | 2 |
IPR017636 | 17,636 | 2-aminoethylphosphonate ABC transporter system, permease protein PhnU | AminoethylPonate_ABC_perm-PhnU | Family | 1,386 | false | false | The enzyme phosphonatase catalyses the degradation of 2-aminoethylphosphonate (AEP) in bacteria. This allows them to metabolise a range of organophosphonate compounds, including 2-aminoethylphosphonate, as a sole source of carbon, energy and phosphorus for growth [ ]. The C-P bond in phosphonoacetaldehyde (Pald) is hyd... | [
"GO:0033223",
"GO:0016020"
] | [
"2-aminoethylphosphonate transport",
"membrane"
] | [
"biological_process",
"cellular_component"
] | 2 | [
"NCBIFAM"
] | [
"TIGR03226"
] | [
"PhnU"
] | [
1386
] | 1 | [
"GP"
] | [
"GenProp0712"
] | [
"GP:GenProp0712"
] | 1 | [] | 0 | [
"PUB00042844",
"PUB00042854",
"PUB00043416",
"PUB00093741"
] | [
"7592415",
"17070898",
"16842370",
"29137138"
] | [
"Molecular cloning, mapping, and regulation of Pho regulon genes for phosphonate breakdown by the phosphonatase pathway of Salmonella typhimurium LT2.",
"Diversification of function in the haloacid dehalogenase enzyme superfamily: The role of the cap domain in hydrolytic phosphoruscarbon bond cleavage.",
"A rol... | [
1995,
2006,
2006,
2017
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"mine drainage metagenome"
] | [
1385,
1
] | 2 | [] | [] | 0 | true | Family | 2-aminoethylphosphonate ABC transporter system, permease protein PhnU | 2-aminoethylphosphonate ABC transporter system, permease protein PhnU | AminoethylPonate_ABC_perm-PhnU | 1 |
IPR017637 | 17,637 | Putative 2-aminoethylphosphonate binding protein, ABC transporter | AminoethylPonate_ABC-bd | Family | 844 | false | false | Bacterial high affinity transport systems are involved in active transport of solutes across the cytoplasmic membrane. Most of the bacterial ABC (ATP-binding cassette) importers are composed of one or two transmembrane permease proteins, one or two nucleotide-binding proteins and a highly specific periplasmic solute-bi... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03227"
] | [
"PhnS"
] | [
844
] | 1 | [
"GP"
] | [
"GenProp0712"
] | [
"GP:GenProp0712"
] | 1 | [
"4r6y"
] | 1 | [
"PUB00042844",
"PUB00071925",
"PUB00071938"
] | [
"7592415",
"18310026",
"8003968"
] | [
"Molecular cloning, mapping, and regulation of Pho regulon genes for phosphonate breakdown by the phosphonatase pathway of Salmonella typhimurium LT2.",
"Characterization of a Pseudomonas putida ABC transporter (AatJMQP) required for acidic amino acid uptake: biochemical properties and regulation by the Aau two-c... | [
1995,
2008,
1994
] | 3 | [] | [] | 0 | 0 | null | [
"Bacteria",
"mine drainage metagenome"
] | [
843,
1
] | 2 | [] | [] | 0 | true | Family | Putative 2-aminoethylphosphonate binding protein, ABC transporter | Putative 2-aminoethylphosphonate binding protein, ABC transporter | AminoethylPonate_ABC-bd | 2 |
IPR017638 | 17,638 | Anthranilate 1,2-dioxygenase, large subunit | Anthranilate_1-2-diOase_lsu | Family | 701 | false | false | This entry represents a group of anthranilate 1,2-dioxygenase large subunit proteins from proteobacteria, including AndAc from Burkholderia cepacia and AntA from Acinetobacter baylyi. They are part of the multicomponent anthranilate dioxygenase, that converts anthranilate to catechol. Anthranilate (2-aminobenzoate) is ... | [] | [] | [] | 0 | [
"NCBIFAM",
"NCBIFAM"
] | [
"NF041684",
"TIGR03228"
] | [
"ant_diox_AndAc",
"anthran_1_2_A"
] | [
218,
483
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00042987",
"PUB00093822",
"PUB00152881"
] | [
"11114907",
"13129960",
"22360670"
] | [
"Characterization and evolution of anthranilate 1,2-dioxygenase from Acinetobacter sp. strain ADP1.",
"Characterization and regulation of the genes for a novel anthranilate 1,2-dioxygenase from Burkholderia cepacia DBO1.",
"Pivotal role of anthranilate dioxygenase genes in the adaptation of Burkholderia multivo... | [
2001,
2003,
2012
] | 3 | [
"IPR001663"
] | [] | 1 | 0 | 1 | [
"Anopheles maculatus",
"Bacteria"
] | [
1,
700
] | 2 | [] | [] | 0 | true | Family | Anthranilate 1,2-dioxygenase, large subunit | Anthranilate 1,2-dioxygenase, large subunit | Anthranilate_1-2-diOase_lsu | 8 |
IPR017639 | 17,639 | Benzoate 1,2-dioxygenase, large subunit | Benzo_1-2-diOase_lsu | Family | 1,305 | false | false | Benzoate 1,2-dioxygenase ( ) belongs to the larger family of aromatic ring-hydroxylating dioxygenases. Members of this family all act on benzoate, but may have additional activities on various benozate analogs. This entry describes the large subunit. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03229"
] | [
"benzo_1_2_benA"
] | [
1305
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR001663"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Oppiella nova",
"bioreactor metagenome"
] | [
1303,
1,
1
] | 3 | [] | [] | 0 | true | Family | Benzoate 1,2-dioxygenase, large subunit | Benzoate 1,2-dioxygenase, large subunit | Benzo_1-2-diOase_lsu | 3 |
IPR017640 | 17,640 | Anthranilate 1,2-dioxygenase, small subunit | Anthranilate_1-2-diOase_ssu | Family | 677 | false | false | This entry represents a group of anthranilate 1,2-dioxygenase small subunit proteins from proteobacteria, including AndAd from Burkholderia cepacia and AntB from Acinetobacter baylyi. They are part of the multicomponent anthranilate dioxygenase, that converts anthranilate to catechol. Anthranilate (2-aminobenzoate) is ... | [
"GO:0009056"
] | [
"catabolic process"
] | [
"biological_process"
] | 1 | [
"NCBIFAM",
"NCBIFAM"
] | [
"NF041685",
"TIGR03231"
] | [
"ant_diox_AndAd",
"anthran_1_2_B"
] | [
203,
474
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00042987",
"PUB00093822",
"PUB00152881"
] | [
"11114907",
"13129960",
"22360670"
] | [
"Characterization and evolution of anthranilate 1,2-dioxygenase from Acinetobacter sp. strain ADP1.",
"Characterization and regulation of the genes for a novel anthranilate 1,2-dioxygenase from Burkholderia cepacia DBO1.",
"Pivotal role of anthranilate dioxygenase genes in the adaptation of Burkholderia multivo... | [
2001,
2003,
2012
] | 3 | [
"IPR000391"
] | [] | 1 | 0 | 1 | [
"Anopheles maculatus",
"Bacteria"
] | [
1,
676
] | 2 | [] | [] | 0 | true | Family | Anthranilate 1,2-dioxygenase, small subunit | Anthranilate 1,2-dioxygenase, small subunit | Anthranilate_1-2-diOase_ssu | 3 |
IPR017641 | 17,641 | Benzoate 1,2-dioxygenase, small subunit | Benzo_1-2-diOase_ssu | Family | 1,976 | false | false | Benzoate 1,2-dioxygenase ( ) belongs to the larger family of aromatic ring-hydroxylating dioxygenases. Members of this family should all act on benzoate, but several have additional known activities on various benozate analogs. Some members actually may be named more suitably according to such alternate an activity, su... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03232"
] | [
"benzo_1_2_benB"
] | [
1976
] | 1 | [] | [] | [] | 0 | [
"3e99"
] | 1 | [] | [] | [] | [] | 0 | [
"IPR000391"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Oppiella nova",
"ecological metagenomes"
] | [
1973,
1,
2
] | 3 | [] | [] | 0 | true | Family | Benzoate 1,2-dioxygenase, small subunit | Benzoate 1,2-dioxygenase, small subunit | Benzo_1-2-diOase_ssu | 2 |
IPR017642 | 17,642 | DNA sulphur modification protein DndB | DNA_S_mod_DndB | Family | 3,631 | false | false | This is family of bacterial proteins likely to be necessary for binding to DNA and recognising the modification sites. Members are found in bacteria, archaea and on viral plasmids, and are typically between 354 and 474 amino acids in length. There is a conserved DGQHR sequence motif. Included in this family is the DndB... | [] | [] | [] | 0 | [
"PFAM",
"NCBIFAM",
"CDD"
] | [
"PF14072",
"TIGR03233",
"cd16412"
] | [
"DndB",
"DNA_S_dndB",
"dndB"
] | [
3631,
651,
1008
] | 3 | [
"GP"
] | [
"GenProp0701"
] | [
"GP:GenProp0701"
] | 1 | [] | 0 | [
"PUB00042946"
] | [
"16102010"
] | [
"A novel DNA modification by sulphur."
] | [
2005
] | 1 | [] | [
"IPR026440"
] | 0 | 1 | 0 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Viruses",
"metagenomes"
] | [
15,
3539,
5,
19,
53
] | 5 | [] | [] | 0 | true | Family | DNA sulphur modification protein DndB | DNA sulphur modification protein DndB | DNA_S_mod_DndB | 4 |
IPR017645 | 17,645 | DNA phosphorothioation-dependent restriction protein DptG | Dnd_assoc_1 | Family | 448 | false | false | A DNA sulfur modification (phosphorothioation) system, dnd (degradation during electrophoresis), is sparsely and sporadically distributed among the bacteria. This protein is one member of a three-gene restriction enzyme cassette that depends on DNA phosphorothioation [ ]. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03236"
] | [
"dnd_assoc_1"
] | [
448
] | 1 | [
"GP"
] | [
"GenProp0701"
] | [
"GP:GenProp0701"
] | 1 | [
"7exx"
] | 1 | [
"PUB00060412"
] | [
"20627870"
] | [
"A novel host-specific restriction system associated with DNA backbone S-modification in Salmonella."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"Methanobacteriota",
"ecological metagenomes"
] | [
428,
10,
8,
2
] | 4 | [] | [] | 0 | true | Family | DNA phosphorothioation-dependent restriction protein DptG | DNA phosphorothioation-dependent restriction protein DptG | Dnd_assoc_1 | 9 |
IPR017646 | 17,646 | DNA phosphorothioation-dependent restriction protein DptH | Dnd_assoc_2 | Family | 363 | false | false | A DNA sulfur modification (phosphorothioation) system, dnd (degradation during electrophoresis), is sparsely and sporadically distributed among the bacteria. This protein is one member of a three-gene restriction enzyme cassette that depends on DNA phosphorothioation [ ]. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03237"
] | [
"dnd_assoc_2"
] | [
363
] | 1 | [
"GP"
] | [
"GenProp0701"
] | [
"GP:GenProp0701"
] | 1 | [] | 0 | [
"PUB00060412"
] | [
"20627870"
] | [
"A novel host-specific restriction system associated with DNA backbone S-modification in Salmonella."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanomada group",
"Plasmopara halstedii",
"marine sediment metagenome"
] | [
358,
3,
1,
1
] | 4 | [] | [] | 0 | true | Family | DNA phosphorothioation-dependent restriction protein DptH | DNA phosphorothioation-dependent restriction protein DptH | Dnd_assoc_2 | 3 |
IPR017647 | 17,647 | DNA phosphorothioation-dependent restriction protein DptF | Dnd_assoc_3 | Family | 462 | false | false | A DNA sulfur modification (phosphorothioation) system, dnd (degradation during electrophoresis), is sparsely and sporadically distributed among the bacteria. This protein is one member of a three-gene restriction enzyme cassette that depends on DNA phosphorothioation [ ]. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03238"
] | [
"dnd_assoc_3"
] | [
462
] | 1 | [
"GP"
] | [
"GenProp0701"
] | [
"GP:GenProp0701"
] | 1 | [] | 0 | [
"PUB00060412"
] | [
"20627870"
] | [
"A novel host-specific restriction system associated with DNA backbone S-modification in Salmonella."
] | [
2010
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanobacteriota",
"Plasmopara halstedii",
"marine sediment metagenome"
] | [
453,
7,
1,
1
] | 4 | [] | [] | 0 | true | Family | DNA phosphorothioation-dependent restriction protein DptF | DNA phosphorothioation-dependent restriction protein DptF | Dnd_assoc_3 | 4 |
IPR017648 | 17,648 | 5-keto-4-deoxy-D-glucarate aldolase | GarL | Family | 1,209 | false | false | 5-keto-4-deoxy-D-glucarate aldolase GarL is involved in step 2 of the subpathway that synthesizes D-glycerate from galactarate. It catalyses the reversible retro-aldol cleavage of both 5-keto-4-deoxy-D-glucarate and 2-keto-3-deoxy-D-glucarate to pyruvate and tartronic semialdehyde [ ]. | [
"GO:0008672",
"GO:0019394"
] | [
"2-dehydro-3-deoxyglucarate aldolase activity",
"glucarate catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01291",
"TIGR03239"
] | [
"KDGluc_aldolase",
"GarL"
] | [
951,
1209
] | 2 | [
"EC",
"GP",
"GP",
"GP",
"GP"
] | [
"4.1.2.20",
"GenProp0714",
"GenProp0716",
"GenProp1225",
"GenProp1514"
] | [
"EC:4.1.2.20",
"GP:GenProp0714",
"GP:GenProp0716",
"GP:GenProp1225",
"GP:GenProp1514"
] | 5 | [
"1dxe",
"1dxf"
] | 2 | [
"PUB00009936"
] | [
"9772162"
] | [
"Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli."
] | [
1998
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Peronospora farinosa",
"mine drainage metagenome"
] | [
1207,
1,
1
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | 5-keto-4-deoxy-D-glucarate aldolase | 5-keto-4-deoxy-D-glucarate aldolase | GarL | 2 |
IPR017649 | 17,649 | Succinylglutamate-semialdehyde dehydrogenase | SuccinylGlu_semiald_DH_AstD | Family | 5,340 | false | false | Succinylglutamic-semialdehyde dehydrogenase (or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71)) is the fourth enzyme in the arginine succinyltransferase (AST) pathway for arginine catabolism [ ], and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglu... | [
"GO:0043824",
"GO:0006527"
] | [
"succinylglutamate-semialdehyde dehydrogenase activity",
"L-arginine catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM",
"CDD"
] | [
"MF_01174",
"TIGR03240",
"cd07095"
] | [
"Aldedh_AstD",
"arg_catab_astD",
"ALDH_SGSD_AstD"
] | [
4552,
5268,
5318
] | 3 | [
"EC",
"GP",
"GP"
] | [
"1.2.1.71",
"GenProp0309",
"GenProp1280"
] | [
"EC:1.2.1.71",
"GP:GenProp0309",
"GP:GenProp1280"
] | 3 | [
"3ju8",
"4kna",
"5u0l",
"5u0m"
] | 4 | [
"PUB00043365",
"PUB00081173"
] | [
"3144259",
"10200310"
] | [
"N2-succinylornithine in ornithine catabolism of Pseudomonas aeruginosa.",
"Escherichia coli genes regulated by cell-to-cell signaling."
] | [
1988,
1999
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
5324,
2,
14
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Succinylglutamate-semialdehyde dehydrogenase | Succinylglutamate-semialdehyde dehydrogenase | SuccinylGlu_semiald_DH_AstD | 2 |
IPR017650 | 17,650 | Arginine N-succinyltransferase | Arginine_N-succinylTrfase | Family | 4,428 | false | false | Arginine N-succinyltransferase catalyses the transfer of succinyl-CoA to arginine to produce succinylarginine. This is the first step in arginine catabolism via the arginine succinyltransferase pathway. Six major L-arginine-degrading pathways have been described for prokaryotes [ ]. Arginine succinyltransferase AstA ( ... | [
"GO:0008791",
"GO:0006527"
] | [
"arginine N-succinyltransferase activity",
"L-arginine catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR03244"
] | [
"arg_catab_AstA"
] | [
4428
] | 1 | [
"EC",
"GP",
"GP"
] | [
"2.3.1.109",
"GenProp0309",
"GenProp1280"
] | [
"EC:2.3.1.109",
"GP:GenProp0309",
"GP:GenProp1280"
] | 3 | [] | 0 | [
"PUB00008006",
"PUB00043076",
"PUB00043524"
] | [
"9696779",
"9393691",
"18045455"
] | [
"Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli.",
"Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa.",
"Bioinformatic evaluation of L-arginine catabolic pathways in 24 cyanobacter... | [
1998,
1997,
2007
] | 3 | [
"IPR007041"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Beauveria bassiana D1-5",
"unclassified sequences"
] | [
4417,
1,
10
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Arginine N-succinyltransferase | Arginine N-succinyltransferase | Arginine_N-succinylTrfase | 8 |
IPR017651 | 17,651 | Arginine/ornithine succinyltransferase, alpha subunit | Arg/Orn_succinylTfrase_asu | Family | 1,024 | false | false | Arginine N-succinyltransferase catalyses the transfer of succinyl-CoA to arginine to produce succinylarginine. This is the first step in arginine catabolism via the arginine succinyltransferase pathway. Six major L-arginine-degrading pathways have been described for prokaryotes [ ]. Arginine succinyltransferase AstA ( ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03245"
] | [
"arg_AOST_alph"
] | [
1024
] | 1 | [
"GP"
] | [
"GenProp1280"
] | [
"GP:GenProp1280"
] | 1 | [
"1yle"
] | 1 | [
"PUB00008006",
"PUB00043076",
"PUB00043524"
] | [
"9696779",
"9393691",
"18045455"
] | [
"Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli.",
"Cloning and characterization of the aru genes encoding enzymes of the catabolic arginine succinyltransferase pathway in Pseudomonas aeruginosa.",
"Bioinformatic evaluation of L-arginine catabolic pathways in 24 cyanobacter... | [
1998,
1997,
2007
] | 3 | [
"IPR007041"
] | [] | 1 | 0 | 1 | [
"Pseudomonadota"
] | [
1024
] | 1 | [] | [] | 0 | true | Family | Arginine/ornithine succinyltransferase, alpha subunit | Arginine/ornithine succinyltransferase, alpha subunit | Arg/Orn_succinylTfrase_asu | 8 |
IPR017652 | 17,652 | Acetyl/Succinylornithine transaminase family, bacteria | Ac/SucOrn_transaminase_bac | Family | 5,991 | false | false | This family consists of bacteria acetyl/succinylornithine transaminases. Succinylornithine transaminase ( ), catalyses the third of five steps in arginine succinyltransferase (AST) pathway, an ammonia-releasing pathway of arginine degradation. A number of sequences extremely closely related in sequence, found in differ... | [
"GO:0008483",
"GO:0030170",
"GO:0006520"
] | [
"transaminase activity",
"pyridoxal phosphate binding",
"amino acid metabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR03246"
] | [
"arg_catab_astC"
] | [
5991
] | 1 | [
"EC",
"EC",
"GP",
"GP",
"GP"
] | [
"2.6.1",
"2.6.1.81",
"GenProp0309",
"GenProp1280",
"GenProp1466"
] | [
"EC:2.6.1",
"EC:2.6.1.81",
"GP:GenProp0309",
"GP:GenProp1280",
"GP:GenProp1466"
] | 5 | [
"2pb0",
"2pb2",
"4adb",
"4adc",
"4add",
"4ade",
"4jev",
"4jew",
"4jex",
"4jey",
"4jez",
"4jf0",
"4jf1"
] | 13 | [] | [] | [] | [] | 0 | [
"IPR004636"
] | [
"IPR026330"
] | 1 | 1 | 0 | [
"Bacteria",
"Opisthokonta",
"unclassified sequences"
] | [
5977,
2,
12
] | 3 | [
"Escherichia coli (strain K12)"
] | [
2
] | 1 | true | Family | Acetyl/Succinylornithine transaminase family, bacteria | Acetyl/Succinylornithine transaminase family, bacteria | Ac/SucOrn_transaminase_bac | 6 |
IPR017653 | 17,653 | Glucarate dehydratase | Glucarate_dehydratase | Family | 2,869 | false | false | This entry represents glucarate dehydratase ( ), which is involved in the first step of the degradation of D-glucaric acid. This enzyme converts D-glucarate (and L-idarate, a stereoisomer) to 5-dehydro-4-deoxyglucarate, which is subsequently acted on by GarL, tartronate semialdehyde reductase and glycerate kinase ([ ],... | [
"GO:0000287",
"GO:0008872",
"GO:0019394"
] | [
"magnesium ion binding",
"glucarate dehydratase activity",
"glucarate catabolic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR03247"
] | [
"glucar-dehydr"
] | [
2869
] | 1 | [
"EC",
"GP",
"GP",
"GP",
"METACYC"
] | [
"4.2.1.40",
"GenProp0716",
"GenProp0717",
"GenProp1514",
"PWY-6499"
] | [
"EC:4.2.1.40",
"GP:GenProp0716",
"GP:GenProp0717",
"GP:GenProp1514",
"METACYC:PWY-6499"
] | 5 | [
"1bqg",
"1ec7",
"1ec8",
"1ec9",
"1ecq",
"1jct",
"1jdf",
"3pwg",
"3pwi",
"4g8t",
"4gyp"
] | 11 | [
"PUB00009936"
] | [
"9772162"
] | [
"Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli."
] | [
1998
] | 1 | [
"IPR034598"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Peronospora farinosa",
"organismal metagenomes"
] | [
2864,
1,
4
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Glucarate dehydratase | Glucarate dehydratase | Glucarate_dehydratase | 8 |
IPR017654 | 17,654 | Galactarate dehydratase GarD-like | GarD-like | Family | 3,264 | false | false | This entry includes GarD from Enterobacteriaceae and its homologues from other bacterial species. | [
"GO:0008867",
"GO:0046392"
] | [
"galactarate dehydratase activity",
"galactarate catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR03248"
] | [
"galactar-dH20"
] | [
3264
] | 1 | [
"GP"
] | [
"GenProp1225"
] | [
"GP:GenProp1225"
] | 1 | [
"6u7l"
] | 1 | [
"PUB00009936"
] | [
"9772162"
] | [
"Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli."
] | [
1998
] | 1 | [] | [
"IPR032893"
] | 0 | 1 | 0 | [
"Bacteria",
"Peronospora farinosa",
"metagenomes"
] | [
3253,
1,
10
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Galactarate dehydratase GarD-like | Galactarate dehydratase GarD-like | GarD-like | 8 |
IPR017655 | 17,655 | 5-dehydro-4-deoxyglucarate dehydratase | Dehydro-deoxyglucarate_dehyd | Family | 5,326 | false | false | 5-dehydro-4-deoxyglucarate dehydratase (also called 5-keto-4-deoxy-glucarate dehydratase or KDGDH), is a member of the same family as dihydrodipicolinate synthase (DHDPS) [ ]. 5-dehydro-4-deoxyglucarate dehydratase is involved in glucarate metabolism, where it catalyses the dehydration and decarboxylation of 5-dehydro-... | [
"GO:0047448",
"GO:0016052"
] | [
"5-dehydro-4-deoxyglucarate dehydratase activity",
"carbohydrate catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM",
"NCBIFAM",
"CDD"
] | [
"MF_00694",
"NF002958",
"TIGR03249",
"cd00951"
] | [
"KDGDH",
"PRK03620.1",
"KdgD",
"KDGDH"
] | [
5232,
5326,
3237,
3312
] | 4 | [
"EC",
"GP",
"GP",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"4.2.1.41",
"GenProp0715",
"GenProp0717",
"PWY-6486",
"PWY-6497",
"PWY-6499",
"PWY-6501"
] | [
"EC:4.2.1.41",
"GP:GenProp0715",
"GP:GenProp0717",
"METACYC:PWY-6486",
"METACYC:PWY-6497",
"METACYC:PWY-6499",
"METACYC:PWY-6501"
] | 7 | [
"4ur7",
"4ur8",
"5hwj",
"5hwm",
"5hwn"
] | 5 | [
"PUB00021570",
"PUB00080596",
"PUB00080598"
] | [
"11031117",
"4311826",
"4982840"
] | [
"Active site modulation in the N-acetylneuraminate lyase sub-family as revealed by the structure of the inhibitor-complexed Haemophilus influenzae enzyme.",
"The metabolism of D-glucarate by Pseudomonas acidovorans.",
"Purification and properties of D-4-deoxy-5-oxoglucarate hydro-lyase (decarboxylating)."
] | [
2000,
1969,
1969
] | 3 | [
"IPR002220"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"metagenomes"
] | [
5320,
6
] | 2 | [] | [] | 0 | true | Family | 5-dehydro-4-deoxyglucarate dehydratase | 5-dehydro-4-deoxyglucarate dehydratase | Dehydro-deoxyglucarate_dehyd | 1 |
IPR017656 | 17,656 | Putative phosphonoacetaldehyde dehydrogenase | Put_phosphonoacetaldehyde_DH | Family | 931 | false | false | This family of genes are members of the NAD-dependent aldehyde dehydrogenase family. These genes are observed in Ralstonia eutropha (strain JMP134) (Alcaligenes eutrophus), Sinorhizobium meliloti 1021, Burkholderia mallei ATCC 23344, Burkholderia thailandensis (strain E264/ATCC 700388/DSM 13276/CIP 106301), Burkholderi... | [] | [] | [] | 0 | [
"NCBIFAM",
"CDD"
] | [
"TIGR03250",
"cd07146"
] | [
"PhnAcAld_DH",
"ALDH_PhpJ"
] | [
910,
918
] | 2 | [
"GP",
"GP"
] | [
"GenProp0713",
"GenProp0724"
] | [
"GP:GenProp0713",
"GP:GenProp0724"
] | 2 | [
"4i3t",
"4i3u",
"4i3v",
"4i3w",
"4i3x"
] | 5 | [
"PUB00081180",
"PUB00091684"
] | [
"15616300",
"24361046"
] | [
"Molecular cloning, sequence analysis, and heterologous expression of the phosphinothricin tripeptide biosynthetic gene cluster from Streptomyces viridochromogenes DSM 40736.",
"Structure and function of phosphonoacetaldehyde dehydrogenase: the missing link in phosphonoacetate formation."
] | [
2005,
2014
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Magallana gigas",
"ecological metagenomes"
] | [
926,
1,
4
] | 3 | [] | [] | 0 | true | Family | Putative phosphonoacetaldehyde dehydrogenase | Putative phosphonoacetaldehyde dehydrogenase | Put_phosphonoacetaldehyde_DH | 6 |
IPR017657 | 17,657 | L-lysine 6-transaminase | L-lysine_6-transaminase | Family | 1,370 | false | false | The immediate product of the reaction of L-lysine 6-transaminase, also called lysine epsilon-aminotransferase (LAT) on lysine, 2-aminoadipate 6-semialdehyde, becomes 1-piperideine 6-carboxylate, or P6C. This product may be converted subsequently to pipecolate or alpha-aminoadipate, lysine catabolites that may be precur... | [
"GO:0030170",
"GO:0045484",
"GO:0017000"
] | [
"pyridoxal phosphate binding",
"L-lysine 6-transaminase activity",
"antibiotic biosynthetic process"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR03251"
] | [
"LAT_fam"
] | [
1370
] | 1 | [
"EC",
"METACYC"
] | [
"2.6.1.36",
"PWY-5298"
] | [
"EC:2.6.1.36",
"METACYC:PWY-5298"
] | 2 | [
"2cin",
"2cjd",
"2cjg",
"2cjh",
"2jje",
"2jjf",
"2jjg",
"2jjh"
] | 8 | [
"PUB00043001",
"PUB00043002"
] | [
"12005058",
"9355735"
] | [
"Biotransformation of L-lysine to L-pipecolic acid catalyzed by L-lysine 6-aminotransferase and pyrroline-5-carboxylate reductase.",
"Delta-1-piperideine-6-carboxylate dehydrogenase, a new enzyme that forms alpha-aminoadipate in Streptomyces clavuligerus and other cephamycin C-producing actinomycetes."
] | [
2002,
1997
] | 2 | [
"IPR005814"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"Eukaryota",
"Klosneuvirinae",
"ecological metagenomes"
] | [
9,
1331,
12,
2,
16
] | 5 | [] | [] | 0 | true | Family | L-lysine 6-transaminase | L-lysine 6-transaminase | L-lysine_6-transaminase | 2 |
IPR017658 | 17,658 | HhH-GPD-type base excision DNA repair protein | HhH-GPD_base_excis | Family | 3,214 | false | false | This entry describes a small, well-conserved bacterial protein family. Its sequence largely consists of a domain, HhH-GPD, found in a variety of related base excision DNA repair enzymes. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03252"
] | [
""
] | [
3214
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Mesorhabditis spiculigera",
"metagenomes"
] | [
3174,
1,
39
] | 3 | [] | [] | 0 | true | Family | HhH-GPD-type base excision DNA repair protein | HhH-GPD-type base excision DNA repair protein | HhH-GPD_base_excis | 7 |
IPR017660 | 17,660 | Oxalyl-CoA decarboxylase | Oxalyl-CoA_decarboxylase | Family | 1,243 | false | false | Oxalate accumulation from amino-acid catabolism is toxic and leads to acute disorders in mammals. Gut microflora are therefore pivotal in maintaining a safe intestinal oxalate balance through oxalate degradation. A number of bacteria, including Oxalobacter formigenes from the human gut, can carry out oxalate degradatio... | [
"GO:0008949",
"GO:0030976",
"GO:0046872",
"GO:0033611"
] | [
"oxalyl-CoA decarboxylase activity",
"thiamine pyrophosphate binding",
"metal ion binding",
"oxalate catabolic process"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"biological_process"
] | 4 | [
"NCBIFAM"
] | [
"TIGR03254"
] | [
"oxalate_oxc"
] | [
1243
] | 1 | [
"EC",
"GP",
"METACYC",
"METACYC",
"METACYC"
] | [
"4.1.1.8",
"GenProp0718",
"PWY-6695",
"PWY-6696",
"PWY-7985"
] | [
"EC:4.1.1.8",
"GP:GenProp0718",
"METACYC:PWY-6695",
"METACYC:PWY-6696",
"METACYC:PWY-7985"
] | 5 | [
"2c31",
"2ji6",
"2ji7",
"2ji8",
"2ji9",
"2jib",
"2q27",
"2q28",
"2q29",
"7ayg",
"7b2e"
] | 11 | [
"PUB00042988",
"PUB00042989"
] | [
"16517636",
"15345383"
] | [
"Transcriptional and functional analysis of oxalyl-coenzyme A (CoA) decarboxylase and formyl-CoA transferase genes from Lactobacillus acidophilus.",
"Characterization and heterologous expression of the oxalyl coenzyme A decarboxylase gene from Bifidobacterium lactis."
] | [
2006,
2004
] | 2 | [
"IPR045025"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Polarella glacialis",
"ecological metagenomes"
] | [
1236,
2,
5
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Oxalyl-CoA decarboxylase | Oxalyl-CoA decarboxylase | Oxalyl-CoA_decarboxylase | 6 |
IPR017661 | 17,661 | 2-aminoethylphosphonate ABC transport system, membrane component PhnV | AminoethylPonate_ABC_PhnV | Family | 718 | false | false | This entry represents PhnV, the membrane component of an ABC transport system that is mainly found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate. The enzyme phosphonatase catalyses the degradation of 2-aminoethylphosphonate (AEP) in bacteria. This allows... | [
"GO:0016020"
] | [
"membrane"
] | [
"cellular_component"
] | 1 | [
"NCBIFAM"
] | [
"TIGR03255"
] | [
"PhnV"
] | [
718
] | 1 | [
"GP"
] | [
"GenProp0712"
] | [
"GP:GenProp0712"
] | 1 | [] | 0 | [
"PUB00004290",
"PUB00014769",
"PUB00017894",
"PUB00017895",
"PUB00017896",
"PUB00017897",
"PUB00017898",
"PUB00017899",
"PUB00025109",
"PUB00026406",
"PUB00042844",
"PUB00042854",
"PUB00043416",
"PUB00043654",
"PUB00093741"
] | [
"9872322",
"9873074",
"11421269",
"1282354",
"9640644",
"11988180",
"11470432",
"11402022",
"11080142",
"11532960",
"7592415",
"17070898",
"16842370",
"11421270",
"29137138"
] | [
"Crystal structure of the ATP-binding subunit of an ABC transporter.",
"Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters.",
"ABC transporters: physiology, structure and mechanism--an overview.",
"ABC transporters: from microorgani... | [
1998,
1999,
2001,
1992,
1998,
2002,
2001,
2001,
2000,
2001,
1995,
2006,
2006,
2001,
2017
] | 15 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
718
] | 1 | [] | [] | 0 | true | Family | 2-aminoethylphosphonate ABC transport system, membrane component PhnV | 2-aminoethylphosphonate ABC transport system, membrane component PhnV | AminoethylPonate_ABC_PhnV | 8 |
IPR017662 | 17,662 | 2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT | AminoethylPonate_ABC_PhnT | Family | 875 | false | false | ABC transporters belong to the ATP-Binding Cassette (ABC) superfamily, which uses the hydrolysis of ATP to energise diverse biological systems. ABC transporters minimally consist of two conserved regions: a highly conserved ATP binding cassette (ABC) and a less conserved transmembrane domain (TMD). These can be found o... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03258"
] | [
"PhnT"
] | [
875
] | 1 | [
"GP"
] | [
"GenProp0712"
] | [
"GP:GenProp0712"
] | 1 | [] | 0 | [
"PUB00004290",
"PUB00014769",
"PUB00017894",
"PUB00017895",
"PUB00017896",
"PUB00017897",
"PUB00017898",
"PUB00017899",
"PUB00025109",
"PUB00026406",
"PUB00042844",
"PUB00042854",
"PUB00043416",
"PUB00043654",
"PUB00093741"
] | [
"9872322",
"9873074",
"11421269",
"1282354",
"9640644",
"11988180",
"11470432",
"11402022",
"11080142",
"11532960",
"7592415",
"17070898",
"16842370",
"11421270",
"29137138"
] | [
"Crystal structure of the ATP-binding subunit of an ABC transporter.",
"Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters.",
"ABC transporters: physiology, structure and mechanism--an overview.",
"ABC transporters: from microorgani... | [
1998,
1999,
2001,
1992,
1998,
2002,
2001,
2001,
2000,
2001,
1995,
2006,
2006,
2001,
2017
] | 15 | [] | [] | 0 | 0 | null | [
"Pseudomonadota"
] | [
875
] | 1 | [] | [] | 0 | true | Family | 2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT | 2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT | AminoethylPonate_ABC_PhnT | 6 |
IPR017663 | 17,663 | ABC transport system, 1-aminoethylphosphonate-binding protein | ABC_2-AEP-bd | Family | 2,044 | false | false | This ABC transporter extracellular solute-binding protein is found in a number of bacterial genomes in operon-like contexts with substrate specificity for 2-aminoethylphosphonate (2-AEP) [ ], though some proteins in this group are described as ferric ion transporters. ABC transporters belong to the ATP-Binding Cassette... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03261"
] | [
"phnS2"
] | [
2044
] | 1 | [
"GP"
] | [
"GenProp0721"
] | [
"GP:GenProp0721"
] | 1 | [] | 0 | [
"PUB00004290",
"PUB00014769",
"PUB00017894",
"PUB00017895",
"PUB00017896",
"PUB00017897",
"PUB00017898",
"PUB00017899",
"PUB00025109",
"PUB00026406",
"PUB00043654",
"PUB00153316"
] | [
"9872322",
"9873074",
"11421269",
"1282354",
"9640644",
"11988180",
"11470432",
"11402022",
"11080142",
"11532960",
"11421270",
"34315891"
] | [
"Crystal structure of the ATP-binding subunit of an ABC transporter.",
"Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters.",
"ABC transporters: physiology, structure and mechanism--an overview.",
"ABC transporters: from microorgani... | [
1998,
1999,
2001,
1992,
1998,
2002,
2001,
2001,
2000,
2001,
2001,
2021
] | 12 | [
"IPR026045"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"metagenomes"
] | [
2024,
20
] | 2 | [] | [] | 0 | true | Family | ABC transport system, 1-aminoethylphosphonate-binding protein | ABC transport system, 1-aminoethylphosphonate-binding protein | ABC_2-AEP-bd | 8 |
IPR017664 | 17,664 | 2-aminoethylphosphonate ABC transport system, permease protein, putative | AminoethylPonate_ABC_perm-1 | Family | 2,110 | false | false | ABC transporters belong to the ATP-Binding Cassette (ABC) superfamily, which uses the hydrolysis of ATP to energise diverse biological systems. ABC transporters minimally consist of two conserved regions: a highly conserved ATP binding cassette (ABC) and a less conserved transmembrane domain (TMD). These can be found o... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03262"
] | [
"PhnU2"
] | [
2110
] | 1 | [
"GP"
] | [
"GenProp0721"
] | [
"GP:GenProp0721"
] | 1 | [] | 0 | [
"PUB00004290",
"PUB00014769",
"PUB00017894",
"PUB00017895",
"PUB00017896",
"PUB00017897",
"PUB00017898",
"PUB00017899",
"PUB00025109",
"PUB00026406",
"PUB00042844",
"PUB00042854",
"PUB00043416",
"PUB00043654",
"PUB00093741",
"PUB00093742"
] | [
"9872322",
"9873074",
"11421269",
"1282354",
"9640644",
"11988180",
"11470432",
"11402022",
"11080142",
"11532960",
"7592415",
"17070898",
"16842370",
"11421270",
"29137138",
"27375568"
] | [
"Crystal structure of the ATP-binding subunit of an ABC transporter.",
"Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters.",
"ABC transporters: physiology, structure and mechanism--an overview.",
"ABC transporters: from microorgani... | [
1998,
1999,
2001,
1992,
1998,
2002,
2001,
2001,
2000,
2001,
1995,
2006,
2006,
2001,
2017,
2016
] | 16 | [] | [] | 0 | 0 | null | [
"Bacteria",
"metagenomes"
] | [
2098,
12
] | 2 | [] | [] | 0 | true | Family | 2-aminoethylphosphonate ABC transport system, permease protein, putative | 2-aminoethylphosphonate ABC transport system, permease protein, putative | AminoethylPonate_ABC_perm-1 | 9 |
IPR017665 | 17,665 | Guanylate kinase | Guanylate_kinase | Family | 30,019 | false | false | Guanylate kinase, also called GMP kinase, is essential for recycling GMP and indirectly, cGMP. This enzyme transfers a phosphate from ATP to GMP, yielding ADP and GDP [ ]. Guanylate kinase is a highly conserved monomer and is important for the activation of various antiviral drugs. | [
"GO:0004385",
"GO:0006163"
] | [
"GMP kinase activity",
"purine nucleotide metabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00328",
"TIGR03263"
] | [
"Guanylate_kinase",
"guanyl_kin"
] | [
24842,
30016
] | 2 | [
"EC",
"GP",
"GP",
"GP",
"GP",
"GP",
"METACYC",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"2.7.4.8",
"GenProp1389",
"GenProp1406",
"GenProp1484",
"GenProp1607",
"GenProp1650",
"PWY-7221",
"PWY-8289",
"R-BTA-499943",
"R-BTA-9748787",
"R-DDI-499943",
"R-DDI-9748787",
"R-HSA-499943",
"R-HSA-9748787",
"R-MMU-499943",
"R-MMU-9748787",
"R-SCE-499943",
"R-SCE-9748787",
"R-SP... | [
"EC:2.7.4.8",
"GP:GenProp1389",
"GP:GenProp1406",
"GP:GenProp1484",
"GP:GenProp1607",
"GP:GenProp1650",
"METACYC:PWY-7221",
"METACYC:PWY-8289",
"REACTOME:R-BTA-499943",
"REACTOME:R-BTA-9748787",
"REACTOME:R-DDI-499943",
"REACTOME:R-DDI-9748787",
"REACTOME:R-HSA-499943",
"REACTOME:R-HSA-974... | 20 | [
"1ex6",
"1ex7",
"1gky",
"1lvg",
"1s4q",
"1s96",
"1z6g",
"1z8f",
"1znw",
"1znx",
"1zny",
"1znz",
"2an9",
"2anb",
"2anc",
"2f3r",
"2f3t",
"2j41",
"2qor",
"3lnc",
"3tau",
"3tr0",
"4f4j",
"4qrh",
"6mfu",
"6nui",
"6wct",
"7luy",
"7s5e",
"7u5f",
"8egl",
"8pts"... | 44 | [
"PUB00022121"
] | [
"12036965"
] | [
"Structural characterization of the closed conformation of mouse guanylate kinase."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Iainarchaeum sp.",
"Eukaryota",
"Viruses",
"unclassified sequences"
] | [
23326,
1,
6190,
27,
475
] | 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",... | [
19,
2,
4,
1,
1,
6,
2,
1,
5,
4,
1,
1,
12
] | 13 | true | Family | Guanylate kinase | Guanylate kinase | Guanylate_kinase | 3 |
IPR017667 | 17,667 | MTH_987/MJ1094 | MTH_987/MJ1094 | Family | 270 | false | false | Members of this protein family were previously designated 'methanogenesis marker protein 1', now named YcaO-related McrA-glycine thioamidation protein, which is universal in and restricted to methanogenic archaea. It shares homology with YcaO (ribosomal protein S12 methylthiotransferase) and its homologues involved in ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03266"
] | [
"methan_mark_1"
] | [
270
] | 1 | [
"GP"
] | [
"GenProp0722"
] | [
"GP:GenProp0722"
] | 1 | [
"6ci7",
"6cib",
"6pe3",
"6peu"
] | 4 | [
"PUB00034422",
"PUB00060475",
"PUB00093716"
] | [
"16930487",
"22070167",
"28880150"
] | [
"Exopolysaccharide-associated protein sorting in environmental organisms: the PEP-CTERM/EpsH system. Application of a novel phylogenetic profiling heuristic.",
"ProPhylo: partial phylogenetic profiling to guide protein family construction and assignment of biological process.",
"Post-translational thioamidation... | [
2006,
2011,
2017
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"ecological metagenomes"
] | [
264,
6
] | 2 | [] | [] | 0 | true | Family | MTH_987/MJ1094 | MTH_987/MJ1094 | MTH_987/MJ1094 | 4 |
IPR017668 | 17,668 | Methanogenesis marker protein 2 | Methan_mark_2 | Family | 241 | false | false | Members of this protein family are only found archaeal methanogens. They show sequence similarity AIR synthase related protein N-and C-terminal domains ( and ). The functions of proteins in this family are unknown, but their role is likely one essential to methanogenesis [ ]. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03267"
] | [
"methan_mark_2"
] | [
241
] | 1 | [
"GP"
] | [
"GenProp0722"
] | [
"GP:GenProp0722"
] | 1 | [] | 0 | [
"PUB00060475"
] | [
"22070167"
] | [
"ProPhylo: partial phylogenetic profiling to guide protein family construction and assignment of biological process."
] | [
2011
] | 1 | [
"IPR011413"
] | [] | 1 | 0 | 1 | [
"Methanobacteriati",
"ecological metagenomes"
] | [
235,
6
] | 2 | [] | [] | 0 | true | Family | Methanogenesis marker protein 2 | Methanogenesis marker protein 2 | Methan_mark_2 | 2 |
IPR017669 | 17,669 | Methyl coenzyme M reductase system, component A2 | Me_Coenz_M_Rdtase_A2 | Family | 290 | false | false | The enzyme that catalyses the final step in methanogenesis, methyl coenzyme M reductase (MCR), contains alpha, beta, and gamma chains [ ]. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed component A2 of the methyl coenzyme M reductase ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03269"
] | [
"met_CoM_red_A2"
] | [
290
] | 1 | [
"GP",
"GP"
] | [
"GenProp0719",
"GenProp0722"
] | [
"GP:GenProp0719",
"GP:GenProp0722"
] | 2 | [
"8s7v",
"9h1l"
] | 2 | [
"PUB00006391",
"PUB00042996",
"PUB00093738",
"PUB00161766"
] | [
"9367957",
"8491734",
"24769699",
"40240609"
] | [
"Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.",
"Component A2 of methylcoenzyme M reductase system from Methanobacterium thermoautotrophicum delta H: nucleotide sequence and functional expression by Escherichia coli.",
"Elucidating the process of activation o... | [
1997,
1993,
2014,
2025
] | 4 | [] | [] | 0 | 0 | null | [
"Archaea",
"ecological metagenomes"
] | [
284,
6
] | 2 | [] | [] | 0 | true | Family | Methyl coenzyme M reductase system, component A2 | Methyl coenzyme M reductase system, component A2 | Me_Coenz_M_Rdtase_A2 | 3 |
IPR017671 | 17,671 | Methanogenesis marker domain 9 | Methan_mark_9 | Domain | 223 | false | false | The exact function of this protein is unknown, but likely is linked to methanogenesis or a process closely connected to it. A 69-amino acid core region of this 110-amino acid domain contains eight invariant Cys residues, including two copies of a motif [WFY]CCxxKPC. These motifs may be metal-binding transcription facto... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03277"
] | [
"methan_mark_9"
] | [
223
] | 1 | [
"GP"
] | [
"GenProp0722"
] | [
"GP:GenProp0722"
] | 1 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Methanobacteriota",
"ecological metagenomes"
] | [
218,
5
] | 2 | [] | [] | 0 | true | Domain | Methanogenesis marker domain 9 | Methanogenesis marker domain 9 | Methan_mark_9 | 6 |
IPR017672 | 17,672 | Radical SAM methyltransferase MA_4551-like | MA_4551-like | Family | 226 | false | false | Members of this protein family, to date, are found in a completed prokaryotic genome if and only if the species is one of the archaeal methanogens, including Methyl coenzyme M reductase-arginine methyltransferase Mmp10. Mmp10 is encoded near the gene for methyl coenzyme M reductase, whose product it modifies. The C-ter... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03278"
] | [
"methan_mark_10"
] | [
226
] | 1 | [
"GP"
] | [
"GenProp0722"
] | [
"GP:GenProp0722"
] | 1 | [
"7qbs",
"7qbt",
"7qbu",
"7qbv"
] | 4 | [
"PUB00092772",
"PUB00106734",
"PUB00158978"
] | [
"29743535",
"31113866",
"31740491"
] | [
"Identification of a unique Radical SAM methyltransferase required for the sp3-C-methylation of an arginine residue of methyl-coenzyme M reductase.",
"Methanogenesis marker protein 10 (Mmp10) from <i>Methanosarcina acetivorans</i> is a radical <i>S</i>-adenosylmethionine methylase that unexpectedly requires cobal... | [
2018,
2019,
2020
] | 3 | [] | [] | 0 | 0 | null | [
"Methanobacteriota",
"ecological metagenomes"
] | [
220,
6
] | 2 | [] | [] | 0 | true | Family | Radical SAM methyltransferase MA_4551-like | Radical SAM methyltransferase MA_4551-like | MA_4551-like | 1 |
IPR017673 | 17,673 | Putative radical SAM enzyme, CHP03279 family | CHP03279_fam | Family | 349 | false | false | Members of this protein family are predicted FeS-containing oxidoreductases of unknown function, apparently restricted to and universal across the Cyanobacteria. The high trusted cut-off score for this model, 700 bits, excludes homologues from other lineages. This exclusion seems justified because a significant number ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03279"
] | [
"cyano_FeS_chp"
] | [
349
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Cyanobacteriota",
"Paulinella"
] | [
344,
5
] | 2 | [] | [] | 0 | true | Family | Putative radical SAM enzyme, CHP03279 family | Putative radical SAM enzyme, CHP03279 family | CHP03279_fam | 6 |
IPR017674 | 17,674 | Methanogenesis marker 11 protein | Methan_mark_11 | Family | 255 | false | false | Members of this protein family, to date, are found in a completed prokaryotic genome if and only if the species is one of the archaeal methanogens. The exact function is unknown, but likely is linked to methanogenesis or a process closely connected to it [ ]. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03280"
] | [
"methan_mark_11"
] | [
255
] | 1 | [
"GP"
] | [
"GenProp0722"
] | [
"GP:GenProp0722"
] | 1 | [] | 0 | [
"PUB00060475"
] | [
"22070167"
] | [
"ProPhylo: partial phylogenetic profiling to guide protein family construction and assignment of biological process."
] | [
2011
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"Microgenomates group",
"ecological metagenomes"
] | [
244,
6,
5
] | 3 | [] | [] | 0 | true | Family | Methanogenesis marker 11 protein | Methanogenesis marker 11 protein | Methan_mark_11 | 3 |
IPR017676 | 17,676 | Methanogenesis marker protein 15 | Methan_mark_15 | Family | 249 | false | false | Members of this protein family, to date, are found in a completed prokaryotic genome if and only if the species is one of the archaeal methanogens. The exact function is unknown, but likely is linked to methanogenesis or a process closely connected to it [ ]. Related proteins include the BadF/BadG/BcrA/BcrD ATPase fami... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03286"
] | [
"methan_mark_15"
] | [
249
] | 1 | [
"GP"
] | [
"GenProp0722"
] | [
"GP:GenProp0722"
] | 1 | [] | 0 | [
"PUB00060475"
] | [
"22070167"
] | [
"ProPhylo: partial phylogenetic profiling to guide protein family construction and assignment of biological process."
] | [
2011
] | 1 | [] | [] | 0 | 0 | null | [
"Archaea",
"ecological metagenomes"
] | [
244,
5
] | 2 | [] | [] | 0 | true | Family | Methanogenesis marker protein 15 | Methanogenesis marker protein 15 | Methan_mark_15 | 2 |
IPR017678 | 17,678 | CoB--CoM heterodisulphide reductase, subunit B | CoB/CoM_hetero-S_Rdtase_bsu | Family | 370 | false | false | This entry represents subunit B (HdrB) from CoB--CoM heterodisulphide reductase (or heterodisulphide reductase; Hdr; ), an iron-sulphur protein found in methanogenic archaea [ , ]. Hdr catalyses the reversible reduction of the heterodisulphide (CoM-S-S-CoB) to the thiol-coenzymes: coenzyme M (H-S-CoM) and coenzyme B (H... | [
"GO:0051912",
"GO:0015948"
] | [
"CoB--CoM heterodisulfide reductase activity",
"methanogenesis"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM",
"NCBIFAM"
] | [
"NF041780",
"TIGR03288"
] | [
"hetero_SS_HdrB",
"CoB_CoM_SS_B"
] | [
96,
274
] | 2 | [
"EC",
"GP",
"GP"
] | [
"1.8.98",
"GenProp0722",
"GenProp1477"
] | [
"EC:1.8.98",
"GP:GenProp0722",
"GP:GenProp1477"
] | 3 | [
"5odc",
"5odh",
"5odi",
"5odq",
"5odr",
"7bkb",
"7bkc",
"7bkd",
"7bke",
"8rvu",
"8rvv",
"8rvy",
"8rwn"
] | 13 | [
"PUB00042894",
"PUB00044672",
"PUB00044673",
"PUB00088716"
] | [
"12102556",
"11322875",
"15168610",
"19968794"
] | [
"The unique biochemistry of methanogenesis.",
"A paramagnetic species with unique EPR characteristics in the active site of heterodisulfide reductase from methanogenic archaea.",
"The membrane-bound electron transport system of Methanosarcina species.",
"Methanogenesis by Methanosarcina acetivorans involves t... | [
2002,
2001,
2004,
2010
] | 4 | [
"IPR051278"
] | [] | 1 | 0 | 1 | [
"Archaea",
"ecological metagenomes"
] | [
357,
13
] | 2 | [] | [] | 0 | true | Family | CoB--CoM heterodisulphide reductase, subunit B | CoB--CoM heterodisulphide reductase, subunit B | CoB/CoM_hetero-S_Rdtase_bsu | 6 |
IPR017679 | 17,679 | Coenzyme F420 hydrogenase subunit beta, archaea | FrhB_archaea | Family | 200 | false | false | This entry represents the beta subunit of coenzyme F420 hydrogenase (FRH) ( ) found exclusively and universally in methanogenic archaea [ ]. Active coenzyme F420 hydrogenase forms a heterocomplex of three subunits: alpha ( ), beta and gamma ( ). This enzyme reduces the physiological low-potential two-electron acceptor ... | [
"GO:0016151",
"GO:0050454",
"GO:0050660",
"GO:0051536"
] | [
"nickel cation binding",
"coenzyme F420 hydrogenase activity",
"flavin adenine dinucleotide binding",
"iron-sulfur cluster binding"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"molecular_function"
] | 4 | [
"NCBIFAM"
] | [
"TIGR03289"
] | [
"frhB"
] | [
200
] | 1 | [
"EC",
"GP",
"METACYC"
] | [
"1.12.98.1",
"GenProp0723",
"PWY-5207"
] | [
"EC:1.12.98.1",
"GP:GenProp0723",
"METACYC:PWY-5207"
] | 3 | [
"3zfs",
"4ci0",
"4omf",
"6qgr",
"6qgt",
"6qii",
"9r51",
"9r52",
"9r5i",
"9r6z"
] | 10 | [
"PUB00009571",
"PUB00044647"
] | [
"2207102",
"3663585"
] | [
"Cloning, sequence determination, and expression of the genes encoding the subunits of the nickel-containing 8-hydroxy-5-deazaflavin reducing hydrogenase from Methanobacterium thermoautotrophicum delta H.",
"8-Hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum: 1. Purification an... | [
1990,
1987
] | 2 | [
"IPR045220"
] | [] | 1 | 0 | 1 | [
"Methanobacteriota",
"ecological metagenomes"
] | [
196,
4
] | 2 | [] | [] | 0 | true | Family | Coenzyme F420 hydrogenase subunit beta, archaea | Coenzyme F420 hydrogenase subunit beta, archaea | FrhB_archaea | 5 |
IPR017680 | 17,680 | CoB--CoM heterodisulphide reductase, subunit C | CoB/CoM_hetero-S_Rdtase_csu | Family | 274 | false | false | This entry represents subunit C (HdrC) from CoB--CoM heterodisulphide reductase (or heterodisulphide reductase; Hdr; ), an iron-sulphur protein found in methanogenic archaea [ ]. Hdr catalyses the reversible reduction of the heterodisulphide (CoM-S-S-CoB) to the thiol-coenzymes: coenzyme M (H-S-CoM) and coenzyme B (H-S... | [
"GO:0051539",
"GO:0051912",
"GO:0015948"
] | [
"4 iron, 4 sulfur cluster binding",
"CoB--CoM heterodisulfide reductase activity",
"methanogenesis"
] | [
"molecular_function",
"molecular_function",
"biological_process"
] | 3 | [
"NCBIFAM"
] | [
"TIGR03290"
] | [
"CoB_CoM_SS_C"
] | [
274
] | 1 | [
"EC",
"GP",
"GP"
] | [
"1.8.98",
"GenProp0722",
"GenProp1477"
] | [
"EC:1.8.98",
"GP:GenProp0722",
"GP:GenProp1477"
] | 3 | [
"5odc",
"5odh",
"5odi",
"5odq",
"5odr",
"7bkb",
"7bkc",
"7bkd",
"7bke",
"8rvu",
"8rvv",
"8rvy",
"8rwn"
] | 13 | [
"PUB00042894",
"PUB00044672",
"PUB00044673"
] | [
"12102556",
"11322875",
"15168610"
] | [
"The unique biochemistry of methanogenesis.",
"A paramagnetic species with unique EPR characteristics in the active site of heterodisulfide reductase from methanogenic archaea.",
"The membrane-bound electron transport system of Methanosarcina species."
] | [
2002,
2001,
2004
] | 3 | [] | [] | 0 | 0 | null | [
"Archaea",
"ecological metagenomes"
] | [
262,
12
] | 2 | [] | [] | 0 | true | Family | CoB--CoM heterodisulphide reductase, subunit C | CoB--CoM heterodisulphide reductase, subunit C | CoB/CoM_hetero-S_Rdtase_csu | 9 |
IPR017681 | 17,681 | Coenzyme F420 hydrogenase, subunit gamma | Coenz_F420_hydrogenase_gsu | Family | 200 | false | false | This entry represents the gamma subunit of coenzyme F420 hydrogenase (FRH) ( ) found exclusively and universally in methanogenic archaea [ ]. Active coenzyme F420 hydrogenase forms a heterocomplex of three subunits: alpha ( ), beta ( ) and gamma. This enzyme reduces the physiological low-potential two-electron acceptor... | [
"GO:0016151",
"GO:0050454",
"GO:0050660",
"GO:0051536"
] | [
"nickel cation binding",
"coenzyme F420 hydrogenase activity",
"flavin adenine dinucleotide binding",
"iron-sulfur cluster binding"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"molecular_function"
] | 4 | [
"NCBIFAM"
] | [
"TIGR03294"
] | [
"FrhG"
] | [
200
] | 1 | [
"EC",
"GP",
"METACYC"
] | [
"1.12.98.1",
"GenProp0723",
"PWY-5207"
] | [
"EC:1.12.98.1",
"GP:GenProp0723",
"METACYC:PWY-5207"
] | 3 | [
"3zfs",
"4ci0",
"4omf",
"6qgr",
"6qgt",
"6qii",
"9r51",
"9r52",
"9r5i",
"9r6z"
] | 10 | [
"PUB00009571",
"PUB00044647"
] | [
"2207102",
"3663585"
] | [
"Cloning, sequence determination, and expression of the genes encoding the subunits of the nickel-containing 8-hydroxy-5-deazaflavin reducing hydrogenase from Methanobacterium thermoautotrophicum delta H.",
"8-Hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum: 1. Purification an... | [
1990,
1987
] | 2 | [] | [] | 0 | 0 | null | [
"Methanobacteriota",
"Thermovibrio ammonificans (strain DSM 15698 / JCM 12110 / HB-1)",
"ecological metagenomes"
] | [
194,
1,
5
] | 3 | [] | [] | 0 | true | Family | Coenzyme F420 hydrogenase, subunit gamma | Coenzyme F420 hydrogenase, subunit gamma | Coenz_F420_hydrogenase_gsu | 5 |
IPR017682 | 17,682 | Coenzyme F420 hydrogenase, subunit alpha | Coenz_F420_hydrogenase_asu | Family | 209 | false | false | This entry represents the beta subunit of coenzyme F420 hydrogenase (FRH) ( ) found exclusively and universally in methanogenic archaea [ ]. Active coenzyme F420 hydrogenase forms a heterocomplex of three subunits: alpha, beta ( ) and gamma ( ). This enzyme reduces the physiological low-potential two-electron acceptor ... | [
"GO:0016151",
"GO:0050454",
"GO:0050660",
"GO:0051536"
] | [
"nickel cation binding",
"coenzyme F420 hydrogenase activity",
"flavin adenine dinucleotide binding",
"iron-sulfur cluster binding"
] | [
"molecular_function",
"molecular_function",
"molecular_function",
"molecular_function"
] | 4 | [
"NCBIFAM"
] | [
"TIGR03295"
] | [
"frhA"
] | [
209
] | 1 | [
"EC",
"GP",
"METACYC"
] | [
"1.12.98.1",
"GenProp0723",
"PWY-5207"
] | [
"EC:1.12.98.1",
"GP:GenProp0723",
"METACYC:PWY-5207"
] | 3 | [
"3zfs",
"4ci0",
"4omf",
"6qgr",
"6qgt",
"6qii",
"9r51",
"9r52",
"9r5i",
"9r6z"
] | 10 | [
"PUB00009571",
"PUB00044647"
] | [
"2207102",
"3663585"
] | [
"Cloning, sequence determination, and expression of the genes encoding the subunits of the nickel-containing 8-hydroxy-5-deazaflavin reducing hydrogenase from Methanobacterium thermoautotrophicum delta H.",
"8-Hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum: 1. Purification an... | [
1990,
1987
] | 2 | [
"IPR001501"
] | [] | 1 | 0 | 1 | [
"Methanobacteriota",
"ecological metagenomes"
] | [
205,
4
] | 2 | [] | [] | 0 | true | Family | Coenzyme F420 hydrogenase, subunit alpha | Coenzyme F420 hydrogenase, subunit alpha | Coenz_F420_hydrogenase_asu | 4 |
IPR017684 | 17,684 | Phosphonopyruvate decarboxylase | Phosphono-pyrv_decarboxylase | Family | 1,401 | false | false | This entry represents phosphonopyruvate, a decarboxylase enzyme that produces phosphonoacetaldehyde (Pald), which is the second step in the biosynthesis phosphonate-containing compounds. Since the preceding enzymatic step, PEP phosphomutase (AepX, ) favours the substrate PEP energetically, the decarboxylase is required... | [
"GO:0033980",
"GO:0032923"
] | [
"phosphonopyruvate decarboxylase activity",
"organic phosphonate biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR03297"
] | [
"Ppyr-DeCO2ase"
] | [
1401
] | 1 | [
"GP"
] | [
"GenProp0724"
] | [
"GP:GenProp0724"
] | 1 | [] | 0 | [
"PUB00042846",
"PUB00042847",
"PUB00042848",
"PUB00042849",
"PUB00042850"
] | [
"1337066",
"9673017",
"11035722",
"1547241",
"12672809"
] | [
"Studies on the biosynthesis of bialaphos (SF-1293). 14. Nucleotide sequence of phosphoenolpyruvate phosphomutase gene isolated from a bialaphos producing organism, Streptomyces hygroscopicus, and its expression in Streptomyces lividans.",
"Isolation and characterization of the PEP-phosphomutase and the phosphono... | [
1992,
1998,
2000,
1992,
2003
] | 5 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
13,
1188,
183,
17
] | 4 | [] | [] | 0 | true | Family | Phosphonopyruvate decarboxylase | Phosphonopyruvate decarboxylase | Phosphono-pyrv_decarboxylase | 4 |
IPR017685 | 17,685 | HTH-type transcriptional regulator ArgP | ArgP | Family | 8,128 | false | false | ArgP (formally known as IciA) is a positive regulator of argK. It is a negative autoregulator in presence of arginine. It competes with DnaA for oriC iteron (13-mer) binding. It activates dnaA and nrd transcription. It has been demonstrated to be part of the pho regulon [ ]. ArgP mutants convey canavanine (an L-arginin... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03298"
] | [
"argP"
] | [
8128
] | 1 | [] | [] | [] | 0 | [
"3isp",
"6xtu",
"6xtv"
] | 3 | [
"PUB00042857",
"PUB00042858",
"PUB00067927"
] | [
"10589831",
"15150242",
"18502871"
] | [
"PhoB-dependent transcriptional activation of the iciA gene during starvation for phosphate in Escherichia coli.",
"Evidence for an arginine exporter encoded by yggA (argO) that is regulated by the LysR-type transcriptional regulator ArgP in Escherichia coli.",
"Lysine represses transcription of the Escherichia... | [
1999,
2004,
2008
] | 3 | [] | [
"IPR023490"
] | 0 | 1 | 0 | [
"Bacteria",
"Opisthokonta",
"metagenomes"
] | [
8104,
4,
20
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | HTH-type transcriptional regulator ArgP | HTH-type transcriptional regulator ArgP | ArgP | 9 |
IPR017686 | 17,686 | Phage/plasmid-like protein | Phg/plasmid-like_prot | Family | 2,981 | false | false | Members of this uncharacterised protein family are found in various Mycobacterium phage genomes, in Streptomyces coelicolor plasmid SCP1, and in bacterial genomes near various markers that suggest lateral gene transfer. Their function is unknown. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03299"
] | [
"LGT_TIGR03299"
] | [
2981
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [
"IPR026325"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Opisthokonta",
"Viruses",
"unclassified sequences"
] | [
2593,
2,
345,
41
] | 4 | [] | [] | 0 | true | Family | Phage/plasmid-like protein | Phage/plasmid-like protein | Phg/plasmid-like_prot | 6 |
IPR017689 | 17,689 | Outer membrane protein assembly factor BamD | BamD | Family | 12,785 | false | false | Outer membrane protein assembly factor BamD, also known as YfiO in Escherichia coli, is part of the outer membrane protein assembly Bam complex (composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE), which is involved in assembly and insertion of β-barrel proteins into the outer ... | [] | [] | [] | 0 | [
"HAMAP",
"NCBIFAM",
"CDD"
] | [
"MF_00922",
"TIGR03302",
"cd15830"
] | [
"OM_assembly_BamD",
"OM_YfiO",
"BamD"
] | [
9729,
12767,
9300
] | 3 | [
"GP",
"GP",
"REACTOME"
] | [
"GenProp0725",
"GenProp1116",
"R-HSA-9760173"
] | [
"GP:GenProp0725",
"GP:GenProp1116",
"REACTOME:R-HSA-9760173"
] | 3 | [
"2yhc",
"3q5m",
"3qky",
"3tgo",
"5ayw",
"5d0o",
"5d0q",
"5efr",
"5ekq",
"5ljo",
"5waq",
"6lyq",
"6lyr",
"6lys",
"6lyu",
"6smx",
"6sn0",
"6sn2",
"6sn3",
"6sn4",
"6sn5",
"6sn7",
"6sn8",
"6sn9",
"6so7",
"6so8",
"6soa",
"6sob",
"6soc",
"6sog",
"6soh",
"6soj"... | 99 | [
"PUB00043080",
"PUB00059811",
"PUB00060769",
"PUB00060770",
"PUB00060771",
"PUB00106876"
] | [
"16824102",
"21586578",
"20378773",
"21823654",
"22281737",
"27686148"
] | [
"YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli.",
"Structural basis of outer membrane protein biogenesis in bacteria.",
"Reconstitution of outer membrane protein assembly from purified components.",
"The reconstituted Escherichia coli Bam complex cat... | [
2006,
2011,
2010,
2011,
2012,
2016
] | 6 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
12510,
32,
243
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Outer membrane protein assembly factor BamD | Outer membrane protein assembly factor BamD | BamD | 1 |
IPR017691 | 17,691 | ATP synthase subunit beta, bacterial and archaeal | Alt_ATPase_F1_bsu | Family | 386 | false | false | Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel ... | [
"GO:0046933",
"GO:0046961",
"GO:0015986",
"GO:0045259"
] | [
"proton-transporting ATP synthase activity, rotational mechanism",
"proton-transporting ATPase activity, rotational mechanism",
"proton motive force-driven ATP synthesis",
"proton-transporting ATP synthase complex"
] | [
"molecular_function",
"molecular_function",
"biological_process",
"cellular_component"
] | 4 | [
"NCBIFAM"
] | [
"TIGR03305"
] | [
"alt_F1F0_F1_bet"
] | [
386
] | 1 | [
"EC",
"METACYC"
] | [
"7.1.2.2",
"PWY-7980"
] | [
"EC:7.1.2.2",
"METACYC:PWY-7980"
] | 2 | [] | 0 | [
"PUB00015307",
"PUB00020603",
"PUB00020604",
"PUB00068786",
"PUB00068787",
"PUB00068788",
"PUB00068789"
] | [
"9425287",
"15473999",
"15078220",
"20450191",
"18937357",
"1385979",
"9741106"
] | [
"F0F1-ATPase genes from an archaebacterium, Methanosarcina barkeri.",
"The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.",
"Mechanisms of ATPases--a multi-disciplinary approach.",
"Regulation and isoform function of the V-ATPases.",
... | [
1997,
2004,
2004,
2010,
2008,
1992,
1998
] | 7 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Methanomicrobia",
"Symbiodinium necroappetens",
"ecological metagenomes"
] | [
348,
24,
1,
13
] | 4 | [] | [] | 0 | true | Family | ATP synthase subunit beta, bacterial and archaeal | ATP synthase subunit beta, bacterial and archaeal | Alt_ATPase_F1_bsu | 4 |
IPR017692 | 17,692 | Alternate ATP synthase, F0complex, subunit A | Alt_ATP_synth_F0_Asu | Family | 448 | false | false | Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03306"
] | [
"altF1_A"
] | [
448
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00015307",
"PUB00020603",
"PUB00020604",
"PUB00068786",
"PUB00068787",
"PUB00068788",
"PUB00068789"
] | [
"9425287",
"15473999",
"15078220",
"20450191",
"18937357",
"1385979",
"9741106"
] | [
"F0F1-ATPase genes from an archaebacterium, Methanosarcina barkeri.",
"The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.",
"Mechanisms of ATPases--a multi-disciplinary approach.",
"Regulation and isoform function of the V-ATPases.",
... | [
1997,
2004,
2004,
2010,
2008,
1992,
1998
] | 7 | [
"IPR045082"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Methanosarcinales",
"Symbiodinium necroappetens",
"ecological metagenomes"
] | [
406,
25,
1,
16
] | 4 | [] | [] | 0 | true | Family | Alternate ATP synthase, F0complex, subunit A | Alternate ATP synthase, F0complex, subunit A | Alt_ATP_synth_F0_Asu | 4 |
IPR017693 | 17,693 | Phosphonate metabolism protein PhnP | Phosphonate_metab_PhnP | Family | 1,262 | false | false | This family of proteins found in operons encoding phosphonate C-P lyase systems as is observed in Escherichia coli [ ] and is a member of the metallo-beta-lactamase superfamily ( ). Instances of this protein are associated with the C-P lyase, but not all genomes containing the C-P lyase system contain phnP. | [
"GO:0008081",
"GO:0019700"
] | [
"phosphoric diester hydrolase activity",
"organic phosphonate catabolic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"NCBIFAM"
] | [
"TIGR03307"
] | [
"PhnP"
] | [
1262
] | 1 | [
"GP",
"GP",
"GP"
] | [
"GenProp0232",
"GenProp1381",
"GenProp1630"
] | [
"GP:GenProp0232",
"GP:GenProp1381",
"GP:GenProp1630"
] | 3 | [
"3g1p",
"3p2u"
] | 2 | [
"PUB00011671"
] | [
"2155230"
] | [
"Molecular biology of carbon-phosphorus bond cleavage. Cloning and sequencing of the phn (psiD) genes involved in alkylphosphonate uptake and C-P lyase activity in Escherichia coli B."
] | [
1990
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"unclassified sequences"
] | [
1259,
3
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Phosphonate metabolism protein PhnP | Phosphonate metabolism protein PhnP | Phosphonate_metab_PhnP | 3 |
IPR017694 | 17,694 | Phosphonate metabolism protein, transferase hexapeptide repeat family | Phosphonate_tfrase_rpt | Family | 2,255 | false | false | This family of proteins contains copies of the Bacterial transferase hexapeptide repeat family ( ) and is only found in operons encoding the phosphonate C-P lyase system ( ). Many C-P lyase operons, however, lack a homologue of this protein. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03308"
] | [
"phn_thr-fam"
] | [
2255
] | 1 | [
"GP"
] | [
"GenProp0232"
] | [
"GP:GenProp0232"
] | 1 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Halobacteriales",
"Opisthokonta",
"ecological metagenomes"
] | [
2221,
29,
2,
3
] | 4 | [] | [] | 0 | true | Family | Phosphonate metabolism protein, transferase hexapeptide repeat family | Phosphonate metabolism protein, transferase hexapeptide repeat family | Phosphonate_tfrase_rpt | 3 |
IPR017695 | 17,695 | Selenium-dependent molybdenum hydroxylase system protein, YqeB family | Se-dep_Mo_hydrolase_YqeB | Domain | 1,522 | false | false | Members of this protein family are probable accessory proteins for the biosynthesis of enzymes with labile selenium-containing centres, different from selenocysteine-containing proteins [ ]. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03309"
] | [
"matur_yqeB"
] | [
1522
] | 1 | [
"GP"
] | [
"GenProp0726"
] | [
"GP:GenProp0726"
] | 1 | [] | 0 | [
"PUB00045880"
] | [
"18289380"
] | [
"Orphan SelD proteins and selenium-dependent molybdenum hydroxylases."
] | [
2008
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Metamonada",
"Methanobacteriota",
"metagenomes"
] | [
1460,
5,
33,
24
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Domain | Selenium-dependent molybdenum hydroxylase system protein, YqeB family | Selenium-dependent molybdenum hydroxylase system protein, YqeB family | Se-dep_Mo_hydrolase_YqeB | 3 |
IPR017696 | 17,696 | Molybdenum cofactor cytidylyltransferase | Mo_hydrolase_YgfJ | Family | 344 | false | false | Members of this protein include MocA, which transfers cytosine from CTP to molybdopterin during molybdopterin cytosine dinucleotide (MCD) cofactor biosynthesis. It is distantly related to MobA (Molybdopterin-guanine dinucleotide biosynthesis protein A) [ , ]. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03310"
] | [
"matur_MocA_YgfJ"
] | [
344
] | 1 | [
"GP"
] | [
"GenProp0726"
] | [
"GP:GenProp0726"
] | 1 | [] | 0 | [
"PUB00045880",
"PUB00074056"
] | [
"18289380",
"19542235"
] | [
"Orphan SelD proteins and selenium-dependent molybdenum hydroxylases.",
"MocA is a specific cytidylyltransferase involved in molybdopterin cytosine dinucleotide biosynthesis in Escherichia coli."
] | [
2008,
2009
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Candidatus Marsarchaeota G2 archaeon BE_D",
"marine sediment metagenome"
] | [
341,
1,
2
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Molybdenum cofactor cytidylyltransferase | Molybdenum cofactor cytidylyltransferase | Mo_hydrolase_YgfJ | 7 |
IPR017697 | 17,697 | Selenium-dependent xanthine dehydrogenase | Xdh | Family | 709 | false | false | Members of this protein resemble conventional xanthine dehydrogenase enzymes, which depend on molybdenum cofactor - molybdopterin bound to molybdate with two sulfur atoms as ligands. But all members of this family occur in species that contain markers for the biosynthesis of enzymes with a selenium-containing form of m... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03311"
] | [
"Se_dep_XDH"
] | [
709
] | 1 | [
"GP"
] | [
"GenProp0726"
] | [
"GP:GenProp0726"
] | 1 | [] | 0 | [
"PUB00045880",
"PUB00074055"
] | [
"18289380",
"21257770"
] | [
"Orphan SelD proteins and selenium-dependent molybdenum hydroxylases.",
"A selenium-dependent xanthine dehydrogenase triggers biofilm proliferation in Enterococcus faecalis through oxidant production."
] | [
2008,
2011
] | 2 | [
"IPR016208"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Candidatus Heimdallarchaeum",
"ecological metagenomes"
] | [
690,
2,
17
] | 3 | [] | [] | 0 | true | Family | Selenium-dependent xanthine dehydrogenase | Selenium-dependent xanthine dehydrogenase | Xdh | 6 |
IPR017698 | 17,698 | Probable molybdopterin-containing oxidoreductase, FAD-binding subunit | Molybdo-cont_Rdtase_FAD-bd_su | Family | 265 | false | false | This entry represents a group of proteins from gammaproteobacteria, including Uncharacterized protein YgfM from Escherichia coli, which has been suggested to be the FAD-binding subunit of a molydbopterin-containing selenate reductase [ ]. This family seems to be related to the FAD-binding subunit of a molybdopterin-con... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03312"
] | [
"Se_sel_red_FAD"
] | [
265
] | 1 | [
"GP"
] | [
"GenProp0726"
] | [
"GP:GenProp0726"
] | 1 | [] | 0 | [
"PUB00042852",
"PUB00042853"
] | [
"11571140",
"12480890"
] | [
"Effect of selenite on growth and protein synthesis in the phototrophic bacterium Rhodobacter sphaeroides.",
"Involvement of a putative molybdenum enzyme in the reduction of selenate by Escherichia coli."
] | [
2001,
2002
] | 2 | [] | [] | 0 | 0 | null | [
"Bacteria"
] | [
265
] | 1 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Probable molybdopterin-containing oxidoreductase, FAD-binding subunit | Probable molybdopterin-containing oxidoreductase, FAD-binding subunit | Molybdo-cont_Rdtase_FAD-bd_su | 8 |
IPR017699 | 17,699 | Molybdenum-binding protein YgfN/XdhD | Mo-bd_YgfN/XdhD | Family | 336 | false | false | This family consists of YgfN, whose function is not clear. YgfN was identified as a molybdenum-binding subunit of a putative molydbopterin-containing selenate reductase complex consisting of proteins YgfK, YgfM and YgfN [ , ]. However, another study showed that a mutation in the gene (b2881) encoding this protein confe... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03313"
] | [
"Se_sel_red_Mo"
] | [
336
] | 1 | [
"GP"
] | [
"GenProp0726"
] | [
"GP:GenProp0726"
] | 1 | [] | 0 | [
"PUB00033239",
"PUB00042852",
"PUB00042853"
] | [
"10986234",
"11571140",
"12480890"
] | [
"Purine catabolism in Escherichia coli and function of xanthine dehydrogenase in purine salvage.",
"Effect of selenite on growth and protein synthesis in the phototrophic bacterium Rhodobacter sphaeroides.",
"Involvement of a putative molybdenum enzyme in the reduction of selenate by Escherichia coli."
] | [
2000,
2001,
2002
] | 3 | [
"IPR016208"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"metagenomes"
] | [
334,
2
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Molybdenum-binding protein YgfN/XdhD | Molybdenum-binding protein YgfN/XdhD | Mo-bd_YgfN/XdhD | 7 |
IPR017700 | 17,700 | Putative aminohydrolase SsnA | Aminohydrolase_SsnA | Family | 1,138 | false | false | Members of this protein family are found exclusively in genomes that contain putative set of labile selenium-dependent enzyme accessory proteins as well as homologues of a labile selenium-dependent purine hydroxylase. A mutant in this gene in Escherichia coli had improved stationary phase viability. The function of thi... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03314"
] | [
"Se_ssnA"
] | [
1138
] | 1 | [] | [] | [] | 0 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
4,
1109,
16,
9
] | 4 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Putative aminohydrolase SsnA | Putative aminohydrolase SsnA | Aminohydrolase_SsnA | 6 |
IPR017701 | 17,701 | Putative selenate reductase YgfK | Se_rdtase_YgfK | Family | 957 | false | false | Members of this protein family are found in genomic regions associated with selenium and/or purine metabolism [ ]. | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03315"
] | [
"Se_ygfK"
] | [
957
] | 1 | [
"GP"
] | [
"GenProp0726"
] | [
"GP:GenProp0726"
] | 1 | [] | 0 | [
"PUB00042853"
] | [
"12480890"
] | [
"Involvement of a putative molybdenum enzyme in the reduction of selenate by Escherichia coli."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"metagenomes"
] | [
952,
5
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Putative selenate reductase YgfK | Putative selenate reductase YgfK | Se_rdtase_YgfK | 4 |
IPR017702 | 17,702 | Putative carbamoyltransferase YgeW | Carbamoyltransferase_YgeW | Family | 835 | false | false | Members of this protein family include the ygeW gene product of Escherichia coli. The function of this protein is unknown. Members show some homology to ornithine carbamoyltransferase and aspartate carbamoyltransferase (carbamoyltransferase), and may belong to the carbamoyltransferases in function. Members often are fo... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03316"
] | [
"ygeW"
] | [
835
] | 1 | [
"EC",
"METACYC",
"METACYC",
"METACYC",
"METACYC",
"METACYC"
] | [
"2.1.3.-",
"PWY-5",
"PWY-7693",
"PWY-7694",
"PWY-8039",
"PWY-8344"
] | [
"EC:2.1.3.-",
"METACYC:PWY-5",
"METACYC:PWY-7693",
"METACYC:PWY-7694",
"METACYC:PWY-8039",
"METACYC:PWY-8344"
] | 6 | [
"2yfk",
"3q98"
] | 2 | [
"PUB00086881"
] | [
"21557323"
] | [
"The ygeW encoded protein from Escherichia coli is a knotted ancestral catabolic transcarbamylase."
] | [
2011
] | 1 | [
"IPR006130"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Eukaryota",
"metagenomes"
] | [
816,
12,
7
] | 3 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Putative carbamoyltransferase YgeW | Putative carbamoyltransferase YgeW | Carbamoyltransferase_YgeW | 6 |
IPR017703 | 17,703 | YgfZ/CAF17, C-terminal | YgfZ/CAF17_C | Domain | 20,267 | false | false | This entry represents the C-terminal region of YgfZ from Escherichia coli, which includes includes the conserved motif KGCYxGQE. This domain is also found in the eukaryotic homologue - CAF17 (Iron-sulfur cluster assembly factor IBA57 homolog, IBA57), which apparently has a critical role in the proper formation of eithe... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03317"
] | [
"CAF17_like_YgfZ"
] | [
20267
] | 1 | [] | [] | [] | 0 | [
"1nrk",
"1vly",
"3ttg",
"6geu",
"6qe3",
"6qe4",
"7z3h"
] | 7 | [
"PUB00001870",
"PUB00038140",
"PUB00069711",
"PUB00162751",
"PUB00163184",
"PUB00163185"
] | [
"9047339",
"16051266",
"20375021",
"36902159",
"22323289",
"23462291"
] | [
"Cloning, and molecular characterization of the GCV1 gene encoding the glycine cleavage T-protein from Saccharomyces cerevisiae.",
"Crystal structure of human T-protein of glycine cleavage system at 2.0 A resolution and its implication for understanding non-ketotic hyperglycinemia.",
"Crystal structure of amino... | [
1997,
2005,
2010,
2023,
2012,
2013
] | 6 | [] | [] | 0 | 0 | null | [
"Archaea",
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
312,
15194,
4401,
360
] | 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",... | [
7,
1,
1,
1,
1,
2,
1,
1,
3,
2,
1,
1,
3
] | 13 | true | Domain | YgfZ/CAF17, C-terminal | YgfZ/CAF17, C-terminal | YgfZ/CAF17_C | 7 |
IPR017704 | 17,704 | Putative selenium-binding protein YdfZ | Se-bd_putative_YdfZ | Family | 788 | false | false | This small protein has a very limited distribution, being found so far only among some gamma-Proteobacteria. The member from Escherichia coli was shown to bind selenium in the absence of a working SelD-dependent selenium incorporation system [ ]. Note that while the E. coli member contains a single Cys residue, a likel... | [] | [] | [] | 0 | [
"PFAM",
"NCBIFAM"
] | [
"PF14001",
"TIGR03318"
] | [
"YdfZ",
"YdfZ_fam"
] | [
788,
782
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00057301"
] | [
"12084818"
] | [
"Direct detection of potential selenium delivery proteins by using an Escherichia coli strain unable to incorporate selenium from selenite into proteins."
] | [
2002
] | 1 | [] | [] | 0 | 0 | null | [
"Bacteria",
"human gut metagenome"
] | [
787,
1
] | 2 | [
"Escherichia coli (strain K12)"
] | [
1
] | 1 | true | Family | Putative selenium-binding protein YdfZ | Putative selenium-binding protein YdfZ | Se-bd_putative_YdfZ | 6 |
IPR017705 | 17,705 | Ribonuclease Y | Ribonuclease_Y | Family | 11,293 | false | false | Ribonuclease Y is an endoribonuclease that initiates mRNA decay [ ]. The member from Bacillus subtilis, YmdA, has been shown to be involved in turnover of yitJ riboswitch [ ]. It also has been shown in Staphylococcus aureus that it catalyses the hydrolysis of both 2',3'-cyclic AMP and 2',3'-cyclic GMP into 3'-AMP and 3... | [
"GO:0003723",
"GO:0006402",
"GO:0016020"
] | [
"RNA binding",
"mRNA catabolic process",
"membrane"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00335",
"TIGR03319"
] | [
"RNase_Y",
"RNase_Y"
] | [
11290,
11136
] | 2 | [] | [] | [] | 0 | [] | 0 | [
"PUB00044724",
"PUB00054925",
"PUB00064872",
"PUB00064873"
] | [
"10817902",
"17951247",
"19779461",
"20418391"
] | [
"2',3'-cyclic nucleotide 2'-phosphodiesterase from Fusarium culmorum.",
"Phosphodiesterase activity of CvfA is required for virulence in Staphylococcus aureus.",
"RNase Y, a novel endoribonuclease, initiates riboswitch turnover in Bacillus subtilis.",
"Initiation of decay of Bacillus subtilis rpsO mRNA by end... | [
2000,
2008,
2009,
2010
] | 4 | [] | [] | 0 | 0 | null | [
"Bacteria",
"Eukaryota",
"unclassified sequences"
] | [
11089,
56,
148
] | 3 | [] | [] | 0 | true | Family | Ribonuclease Y | Ribonuclease Y | Ribonuclease_Y | 7 |
IPR017707 | 17,707 | Alternate ATP synthase, F0 complex, subunit b | Alt_ATP_synth_F0_bsu | Family | 353 | false | false | Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03321"
] | [
"alt_F1F0_F0_B"
] | [
353
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00015307",
"PUB00020603",
"PUB00020604",
"PUB00068786",
"PUB00068787",
"PUB00068788",
"PUB00068789"
] | [
"9425287",
"15473999",
"15078220",
"20450191",
"18937357",
"1385979",
"9741106"
] | [
"F0F1-ATPase genes from an archaebacterium, Methanosarcina barkeri.",
"The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.",
"Mechanisms of ATPases--a multi-disciplinary approach.",
"Regulation and isoform function of the V-ATPases.",
... | [
1997,
2004,
2004,
2010,
2008,
1992,
1998
] | 7 | [
"IPR002146"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Methanomicrobia",
"Symbiodinium necroappetens",
"ecological metagenomes"
] | [
310,
25,
1,
17
] | 4 | [] | [] | 0 | true | Family | Alternate ATP synthase, F0 complex, subunit b | Alternate ATP synthase, F0 complex, subunit b | Alt_ATP_synth_F0_bsu | 6 |
IPR017708 | 17,708 | Alternate ATP synthase, F0 complex, subunit C, bacterial/archaeal | Alt_ATP_synth_F0_Csu | Family | 506 | false | false | Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03322"
] | [
"alt_F1F0_F0_C"
] | [
506
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00015307",
"PUB00020603",
"PUB00020604",
"PUB00068786",
"PUB00068787",
"PUB00068788",
"PUB00068789"
] | [
"9425287",
"15473999",
"15078220",
"20450191",
"18937357",
"1385979",
"9741106"
] | [
"F0F1-ATPase genes from an archaebacterium, Methanosarcina barkeri.",
"The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.",
"Mechanisms of ATPases--a multi-disciplinary approach.",
"Regulation and isoform function of the V-ATPases.",
... | [
1997,
2004,
2004,
2010,
2008,
1992,
1998
] | 7 | [
"IPR005953"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Methanomicrobia",
"ecological metagenomes"
] | [
459,
26,
21
] | 3 | [] | [] | 0 | true | Family | Alternate ATP synthase, F0 complex, subunit C, bacterial/archaeal | Alternate ATP synthase, F0 complex, subunit C, bacterial/archaeal | Alt_ATP_synth_F0_Csu | 5 |
IPR017709 | 17,709 | Alternate ATP synthase, F1 complex, subunit gamma | Alt_ATP_synth_F1_gsu | Family | 371 | false | false | Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03323"
] | [
"alt_F1F0_F1_gam"
] | [
371
] | 1 | [] | [] | [] | 0 | [] | 0 | [
"PUB00015307",
"PUB00020603",
"PUB00020604",
"PUB00068786",
"PUB00068787",
"PUB00068788",
"PUB00068789"
] | [
"9425287",
"15473999",
"15078220",
"20450191",
"18937357",
"1385979",
"9741106"
] | [
"F0F1-ATPase genes from an archaebacterium, Methanosarcina barkeri.",
"The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.",
"Mechanisms of ATPases--a multi-disciplinary approach.",
"Regulation and isoform function of the V-ATPases.",
... | [
1997,
2004,
2004,
2010,
2008,
1992,
1998
] | 7 | [
"IPR000131"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Methanomicrobia",
"ecological metagenomes"
] | [
332,
25,
14
] | 3 | [] | [] | 0 | true | Family | Alternate ATP synthase, F1 complex, subunit gamma | Alternate ATP synthase, F1 complex, subunit gamma | Alt_ATP_synth_F1_gsu | 6 |
IPR017710 | 17,710 | Alternate ATP synthase, F1 complex, subunit alpha | Alt_ATP_synth_F1_asu | Family | 405 | false | false | A small number of taxonomically diverse prokaryotic species, including Methanosarcina barkeri, have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea [ ]. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction.... | [
"GO:0046933",
"GO:0015986",
"GO:0045259"
] | [
"proton-transporting ATP synthase activity, rotational mechanism",
"proton motive force-driven ATP synthesis",
"proton-transporting ATP synthase complex"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"NCBIFAM"
] | [
"TIGR03324"
] | [
"alt_F1F0_F1_al"
] | [
405
] | 1 | [
"EC",
"METACYC"
] | [
"7.1.2.2",
"PWY-7980"
] | [
"EC:7.1.2.2",
"METACYC:PWY-7980"
] | 2 | [] | 0 | [
"PUB00015307",
"PUB00020603",
"PUB00020604",
"PUB00068786",
"PUB00068787",
"PUB00068788",
"PUB00068789"
] | [
"9425287",
"15473999",
"15078220",
"20450191",
"18937357",
"1385979",
"9741106"
] | [
"F0F1-ATPase genes from an archaebacterium, Methanosarcina barkeri.",
"The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio.",
"Mechanisms of ATPases--a multi-disciplinary approach.",
"Regulation and isoform function of the V-ATPases.",
... | [
1997,
2004,
2004,
2010,
2008,
1992,
1998
] | 7 | [
"IPR005294"
] | [] | 1 | 0 | 1 | [
"Bacteria",
"Methanomicrobia",
"ecological metagenomes"
] | [
366,
27,
12
] | 3 | [] | [] | 0 | true | Family | Alternate ATP synthase, F1 complex, subunit alpha | Alternate ATP synthase, F1 complex, subunit alpha | Alt_ATP_synth_F1_asu | 8 |
IPR017711 | 17,711 | Cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase | BphB_TodD | Family | 69 | false | false | Members of this family occur as the BphD protein of biphenyl catabolism and as the TodD protein of toluene catabolism. Members catalyse the second step in each pathway and proved interchangeable when tested; the first and fourth enzymes in each pathway confer metabolic specificity. In the context of biphenyl degradatio... | [
"GO:0016628"
] | [
"oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor"
] | [
"molecular_function"
] | 1 | [
"NCBIFAM"
] | [
"TIGR03325"
] | [
"BphB_TodD"
] | [
69
] | 1 | [
"EC",
"METACYC"
] | [
"1.3.1.56",
"PWY-7747"
] | [
"EC:1.3.1.56",
"METACYC:PWY-7747"
] | 2 | [
"1bdb",
"2y93",
"2y99",
"3zv3",
"3zv4",
"3zv5",
"3zv6"
] | 7 | [] | [] | [] | [] | 0 | [
"IPR047950"
] | [] | 1 | 0 | 1 | [
"Bacteria"
] | [
69
] | 1 | [] | [] | 0 | true | Family | Cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase | Cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase | BphB_TodD | 9 |
IPR017712 | 17,712 | Ribulose bisphosphate carboxylase, type III | RuBisCO_III | Family | 366 | false | false | Type III ribulose bisphosphate carboxylase (RuBisCO) is composed of a large chain homodimer in a "head-to-tail" conformation. In contrast to type I RuBisCO, type III RuBisCO is composed solely of large subunits [ ], or RuBisCO. These proteins act in a three-step pathway for conversion of the sugar moiety of AMP to two ... | [
"GO:0016984",
"GO:0015977"
] | [
"ribulose-bisphosphate carboxylase activity",
"carbon fixation"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM",
"CDD"
] | [
"MF_01133",
"TIGR03326",
"cd08213"
] | [
"RuBisCO_L_type3",
"rubisco_III",
"RuBisCO_large_III"
] | [
359,
355,
124
] | 3 | [
"EC",
"GP",
"METACYC",
"METACYC"
] | [
"4.1.1.39",
"GenProp0728",
"PWY-5532",
"PWY-5723"
] | [
"EC:4.1.1.39",
"GP:GenProp0728",
"METACYC:PWY-5532",
"METACYC:PWY-5723"
] | 4 | [
"1geh",
"2cwx",
"2cxe",
"2d69",
"3a12",
"3a13",
"3kdn",
"3kdo",
"3wqp",
"6hun",
"7qsv",
"7qsx",
"7qsy",
"7qvi",
"8dht"
] | 15 | [
"PUB00042998",
"PUB00042999"
] | [
"12730164",
"17303759"
] | [
"Synthesis of catalytically active form III ribulose 1,5-bisphosphate carboxylase/oxygenase in archaea.",
"Archaeal type III RuBisCOs function in a pathway for AMP metabolism."
] | [
2003,
2007
] | 2 | [
"IPR033966"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Bacteria",
"ecological metagenomes"
] | [
342,
18,
6
] | 3 | [] | [] | 0 | true | Family | Ribulose bisphosphate carboxylase, type III | Ribulose bisphosphate carboxylase, type III | RuBisCO_III | 6 |
IPR017713 | 17,713 | AMP phosphorylase | AMP_phosphorylase | Family | 410 | false | false | AMP phosphorylase is found in archaea, and only in those with a type III Rubisco enzyme. Most of the members previously were annotated as thymidine phosphorylase, or DeoA. The AMP metabolised by this enzyme may be produced by ADP-dependent sugar kinases [ ]. | [
"GO:0046125"
] | [
"pyrimidine deoxyribonucleoside metabolic process"
] | [
"biological_process"
] | 1 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_02132",
"TIGR03327"
] | [
"AMP_phosphorylase",
"AMP_phos"
] | [
237,
410
] | 2 | [
"EC",
"GP",
"METACYC"
] | [
"2.4.2.57",
"GenProp0728",
"PWY-5532"
] | [
"EC:2.4.2.57",
"GP:GenProp0728",
"METACYC:PWY-5532"
] | 3 | [
"4ga4",
"4ga5",
"4ga6"
] | 3 | [
"PUB00042999"
] | [
"17303759"
] | [
"Archaeal type III RuBisCOs function in a pathway for AMP metabolism."
] | [
2007
] | 1 | [
"IPR013466"
] | [] | 1 | 0 | 1 | [
"Archaea",
"Parcubacteria group",
"ecological metagenomes"
] | [
389,
15,
6
] | 3 | [] | [] | 0 | true | Family | AMP phosphorylase | AMP phosphorylase | AMP_phosphorylase | 3 |
IPR017714 | 17,714 | Methylthioribulose-1-phosphate dehydratase | MethylthioRu-1-P_deHdtase_MtnB | Family | 8,235 | false | false | Members of this family are the methylthioribulose-1-phosphate dehydratase of the methionine salvage pathway. This pathway allows methylthioadenosine, left over from polyamine biosynthesis, to be recycled to methionine. Proteins in this entry also include the bifunctional enzyme MtnB/MtnX from bacteria and the probable ... | [
"GO:0046872",
"GO:0019509",
"GO:0005737"
] | [
"metal ion binding",
"L-methionine salvage from methylthioadenosine",
"cytoplasm"
] | [
"molecular_function",
"biological_process",
"cellular_component"
] | 3 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_01677",
"TIGR03328"
] | [
"Salvage_MtnB",
"salvage_mtnB"
] | [
4043,
8078
] | 2 | [
"EC",
"GP",
"METACYC",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME",
"REACTOME"
] | [
"4.2.1.109",
"GenProp0729",
"PWY-4361",
"R-BTA-111458",
"R-BTA-9627069",
"R-DME-111458",
"R-DME-9627069",
"R-DRE-111458",
"R-DRE-9627069",
"R-HSA-111458",
"R-HSA-1237112",
"R-HSA-9627069",
"R-MMU-111458",
"R-MMU-9627069",
"R-XTR-111458",
"R-XTR-9627069"
] | [
"EC:4.2.1.109",
"GP:GenProp0729",
"METACYC:PWY-4361",
"REACTOME:R-BTA-111458",
"REACTOME:R-BTA-9627069",
"REACTOME:R-DME-111458",
"REACTOME:R-DME-9627069",
"REACTOME:R-DRE-111458",
"REACTOME:R-DRE-9627069",
"REACTOME:R-HSA-111458",
"REACTOME:R-HSA-1237112",
"REACTOME:R-HSA-9627069",
"REACTOM... | 16 | [
"2irp",
"4m6r"
] | 2 | [] | [] | [] | [] | 0 | [] | [
"IPR027514"
] | 0 | 1 | 0 | [
"Bacteria",
"Eukaryota",
"Thermoplasmatales",
"ecological metagenomes"
] | [
4131,
4093,
2,
9
] | 4 | [
"Arabidopsis thaliana",
"Caenorhabditis elegans",
"Danio rerio",
"Drosophila melanogaster",
"Homo sapiens",
"Mus musculus",
"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)",
"Oryza sativa subsp. japonica",
"Rattus norvegicus",
"Saccharomyces cerevisiae (strai... | [
11,
1,
5,
2,
3,
1,
1,
1,
3,
1,
1,
5
] | 12 | true | Family | Methylthioribulose-1-phosphate dehydratase | Methylthioribulose-1-phosphate dehydratase | MethylthioRu-1-P_deHdtase_MtnB | 4 |
IPR017715 | 17,715 | Putative aminophosphonate oxidoreductase | NH2-phosphonate_OxRdtase | Family | 646 | false | false | This entry represents FAD-dependent oxidoreductases. Characterised proteins within this family include glycerol-3-phosphate dehydrogenase ( ), sarcosine oxidase beta subunit ( ) and a number of deaminating amino acid oxidases ( ). These genes have been consistently observed in a genomic context including genes for the ... | [] | [] | [] | 0 | [
"NCBIFAM"
] | [
"TIGR03329"
] | [
"Phn_aa_oxid"
] | [
646
] | 1 | [
"GP"
] | [
"GenProp0720"
] | [
"GP:GenProp0720"
] | 1 | [] | 0 | [] | [] | [] | [] | 0 | [] | [] | 0 | 0 | null | [
"Pseudomonadota",
"Stylophora pistillata"
] | [
645,
1
] | 2 | [] | [] | 0 | true | Family | Putative aminophosphonate oxidoreductase | Putative aminophosphonate oxidoreductase | NH2-phosphonate_OxRdtase | 5 |
IPR017716 | 17,716 | S-adenosylmethionine decarboxylase proenzyme | S-AdoMet_deCOase_pro-enz | Family | 5,452 | false | false | Members of this protein family are the single chain precursor of the two chains of the mature S-adenosylmethionine decarboxylase as found in Methanocaldococcus jannaschii (Methanococcus jannaschii), Bacillus subtilis and a wide range of other species [ ]. S-adenosylmethionine decarboxylase catalyses the decarboxylation... | [
"GO:0004014",
"GO:0008295"
] | [
"adenosylmethionine decarboxylase activity",
"spermidine biosynthetic process"
] | [
"molecular_function",
"biological_process"
] | 2 | [
"HAMAP",
"NCBIFAM"
] | [
"MF_00464",
"TIGR03330"
] | [
"AdoMetDC_1",
"SAM_DCase_Bsu"
] | [
4305,
5450
] | 2 | [
"EC",
"GP",
"METACYC"
] | [
"4.1.1.50",
"GenProp1571",
"PWY-6834"
] | [
"EC:4.1.1.50",
"GP:GenProp1571",
"METACYC:PWY-6834"
] | 3 | [
"1tlu",
"1tmi",
"1vr7",
"2iii",
"3iwb",
"3iwc",
"3iwd"
] | 7 | [
"PUB00044723"
] | [
"1084469"
] | [
"Reflections on the definition and biologic behavior of some dermatologic diseases."
] | [
1976
] | 1 | [
"IPR003826"
] | [
"IPR027549"
] | 1 | 1 | 0 | [
"Archaea",
"Bacteria",
"Caudoviricetes",
"Eukaryota",
"unclassified sequences"
] | [
399,
4807,
43,
102,
101
] | 5 | [] | [] | 0 | true | Family | S-adenosylmethionine decarboxylase proenzyme | S-adenosylmethionine decarboxylase proenzyme | S-AdoMet_deCOase_pro-enz | 8 |
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